INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(282, 'Q9CXH7', 'Shugoshin-like 1', 'GO:0000776===GO:0000777===GO:0008608===GO:0000779===GO:0000780===SCL', 58966, 'Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase; when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the STAG2 subunit of cohesin complex at the centromere; ensuring cohesin persistence at centromere until cohesin cleavage by ESPL1/separase at anaphase. Essential for proper chromosome segregation during mitosis and this function requires interaction with PPP2R1A. Its phosphorylated form is necessary for chromosome congression and for the proper attachment of spindle microtubule to the kinetochore. Necessary for kinetochore localization of PLK1 and CENPF. May play a role in the tension sensing mechanism of the spindle-assembly checkpoint by regulating PLK1 kinetochore affinity. {ECO:0000269|PubMed:18084284; ECO:0000269|PubMed:18331714}.', 'MAKERCQKRSFQDTLEDIKNRMKEKRNKNLAGIGKRKSFIVAPGQVPTNTATLLRYYQDNNRLLVLALENEKSKVREAQDVILQLRKECYYLTCQLYALKEKLTSRQSEETTQNWKGRPSDVVSSIDNTTRDLSGKSLQQIAVEETDCPYQTTEPSPAVTPETQGCDFDSGKVESTDEVLPRTISIRRHLRKDFSNISHSTTLEDCKASPRVAQSLEVKGSRCREVTVTLHRLENVCLWNKDQISLCSRLINPAKITETEVILSSKPEQIESKHKRARKRRAEQRRTKQRCKSKSSLRSKGNKNKDKQGLPPTTLDGGIGSCDAYDFNLKGTVHPTPFRQKMNNGCNKETDSSNSEVSDLECSTSEDESDDLYLPPSKRLRDYRESERAVTRPRSKRGLQYPDGKERKEVLPSTAPTGIPPETQESPRCSLKDVTNILQCPRVKIRKPSLPPKRREDSPAVALTKRRCSTIKSYKEPTLASKLRRGDPFTDLCFLNSPIFKQKRGMRCPKRRTKQTQ', 517, 'Q9CXH7; Q3U4K4; Q588H1; Q8BKW2;', 'KD00282', 'Mus musculus (Mouse)', 'Sgol1', '#Shugoshin-like 1', '-', '-', '72415'),
(283, 'Q9UR39', 'NAD-dependent protein deacetylase hst4', 'k', 46590, 'NAD-dependent histone deacetylase; which contributes to both telomeric and centromeric silencing; proper cell cycle progression; DNA damage control; recombination; and genomic maintenance. {ECO:0000269|PubMed:10512858}.', 'MKVEEHVPLIQESRKRKCQSSENASKRQQLLSKLPLRLHTGNENVDLSPLVSAIRKAKRIVVVTGAGISCDAGIPDFRSSEGLFSSLRAEYKLNCSGKELFDGSVYRDLKSVNIFHAMIRKLHMLSNNARPTDFHLFLSQLAQESKLLRLYTQNIDFLETRLEGLQTCIPLPQSAPWPTTIPLHGTLEVVSCTRCSFLKKFNPDIFDRNGVTVCPDCKTENEVRRIAGKRSVIEGCLRPRIVLYNEIHPDSESIGSVCSQDLKSRPDCLIVAGTSCKIPGVKRIIKEMSNCVHKQKGNVIWLNYDEPTKDFLNLCDLVVQGDLQIAIRRLKPLLDAPSWKLKSHSAKRTSKQKSSEQTKITSSTKITKAIGLNTKSNDSSKKDNTSFQLHQVLNSIEIPKVEIKQEVEYATPSPL', 415, 'Q9UR39;', 'KD00283', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hst4', '#NAD-dependent protein deacetylase hst4#3.5.1.-#Homologous to SIR2 protein 4#Regulatory protein SIR2 homolog 4', '-', '-', '2542366'),
(284, 'Q5FBB7', 'Shugoshin-like 1', 'GO:0000776===GO:0000777===GO:0008608===GO:0000779===GO:0000780===c;k', 64190, 'Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase; when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the STAG2 subunit of cohesin complex at the centromere; ensuring cohesin persistence at centromere until cohesin cleavage by ESPL1/separase at anaphase. Essential for proper chromosome segregation during mitosis and this function requires interaction with PPP2R1A. Its phosphorylated form is necessary for chromosome congression and for the proper attachment of spindle microtubule to the kinetochore. Necessary for kinetochore localization of PLK1 and CENPF. May play a role in the tension sensing mechanism of the spindle-assembly checkpoint by regulating PLK1 kinetochore affinity. Isoform 3 plays a role in maintaining centriole cohesion involved in controlling spindle pole integrity. {ECO:0000269|PubMed:15604152; ECO:0000269|PubMed:15723797; ECO:0000269|PubMed:15737064; ECO:0000269|PubMed:16580887; ECO:0000269|PubMed:17617734; ECO:0000269|PubMed:17621308; ECO:0000269|PubMed:18331714}.', 'MAKERCLKKSFQDSLEDIKKRMKEKRNKNLAEIGKRRSFIAAPCQIITNTSTLLKNYQDNNKMLVLALENEKSKVKEAQDIILQLRKECYYLTCQLYALKGKLTSQQTVEPAQNQEICSSGMDPNSDDSSRNLFVKDLPQIPLEETELPGQGESFQIEDQIPTIPQDTLGVDFDSGEAKSTDNVLPRTVSVRSSLKKHCNSICQFDSLDDFETSHLAGKSFEFERVGFLDPLVNMHIPENVQHNACQWSKDQVNLSPKLIQPGTFTKTKEDILESKSEQTKSKQRDTQERKREEKRKANRRKSKRMSKYKENKSENKKTVPQKKMHKSVSSNDAYNFNLEEGVHLTPFRQKVSNDSNREENNESEVSLCESSGSGDDSDDLYLPTCKYIQNPTSNSDRPVTRPLAKRALKYTDEKETEGSKPTKTPTTTPPETQQSPHLSLKDITNVSLYPVVKIRRLSLSPKKNKASPAVALPKRRCTASVNYKEPTLASKLRRGDPFTDLCFLNSPIFKQKKDLRRSKKRALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR', 561, 'Q5FBB7; Q588H5; Q5FBB4; Q5FBB5; Q5FBB6; Q5FBB8; Q8N579; Q8WVL0;Q9BVA8; Q9H275;', 'KD00284', 'Homo sapiens (Human)', 'SGOL1', '#Shugoshin-like 1#hSgo1#Serologically defined breast cancer antigen NY-BR-85', '-', 'ENSG00000237485', '-'),
(285, 'Q9CPV5', 'Polyamine-modulated factor 1', 'GO:0000444', 23121, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis (By similarity). May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. {ECO:0000250; ECO:0000269|PubMed:11583586}.', 'MAEVSRDSEAAERGPEGSSPEAVPGDATIPRVKLLDAIVDTFLQKLVADRSYERFTTCYKHFHQLNPEVTQRIYDKFVAQLQTSIREEISEIKEEGNLEAVLNSLDKIIEEGRERGEPAWRPSGIPEKDLCSVMAPYFLKQQDTLCHQVRKQEAKNQELADAVLAGRRQVEELQQQVRALQQTWQALHREQRELLSVLRAPE', 202, 'Q9CPV5; Q3UCB8; Q8K237; Q924B3; Q9D6E2;', 'KD00285', 'Mus musculus (Mouse)', 'Pmf1', '#Polyamine-modulated factor 1#PMF-1', '-', '-', '67037'),
(286, 'Q4P3S3', 'Histone acetyltransferase ESA1', 'GO:0034508', 63408, 'Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4; H3; H2B; H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac; H4K8ac; H4K12ac and H4K16ac; histone H3 to form H3K14ac; and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me. {ECO:0000250|UniProtKB:Q08649}.', 'MAPRTQKSTSGTPGGSGTPGPDEGPQISPGGTYGLEDVVVGCKAFVQKPDVVTGEMEERKAEILSIREKPKPRLTKKQQAELADKPAPTLEETLEYYVHYCEFNKRLDEWVSGTRLITSRELEWPKKEVTSDKTKRKVIRAGSGATTPSTPLTPTGKGYRGAGASNLLKKAAAQAAKNVQGESGLETPQKRKADSGDTSTAQSIRADSIDADADGEDDENGAVVAMEMLGGNDQQEKDDVATESNGGLTASLNANQGQETFSKKQEIEKLRTSGSMTQSVSEVARVKNLNKIQMGKSEVETWYFSPYPLEYAHIDTLYICEMCLSYFPSPFTLKRHRSKCTLLHPPGNEIYRHEDISFFEIDGRLQRTWCRNLCLLSKCFLDHKTLYYDVDPFLYYCMVKRDDLGCHLLGYFSKEKDSAENYNVACILTLPQHQRAGYGKLLIEFSYELTKIEGKLGSPEKPLSDLGLLSYRAYWAEIIVELLLKTEDEISIEEIAQKTAFTHADILHTCMALNMLKQYQGKHMIVLSDLIISKYTAKRPRKRINPQKLHWTAKNWHRSQLNFGW', 565, 'Q4P3S3;', 'KD00286', 'Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)', 'ESA1', '#Histone acetyltransferase ESA1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}', '-', '-', '3633352'),
(287, 'Q9CPV1', 'Spindle and kinetochore-associated protein 1', 'GO:0000940', 29445, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis; when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it mediates the interaction with microtubules (By similarity). {ECO:0000250}.', 'MDSELEDLCSYVNEKIGNIKKILSIRNLGQDPALKTTLSKIGDEIIAVNELLNKFELEIQYQEQTNSSLKELCESLREECEDVEHLKEHVPPHLPQVTATQSLVHKPEPDPKESDKAEEPGLPKKPPREQRVIKEMQFITMDEFSDVPAYMKSRLTYCQINDIIKEINKAVVSKYKIMHQPKASMSSVKRNLYQRFINEETKDTKGHHFIVEADIKEFTALKVDKRFYVIMHILRHCHRLSEVRGGGLTRYVIT', 254, 'Q9CPV1; Q005W7; Q8VE34; Q9CYW9;', 'KD00287', 'Mus musculus (Mouse)', 'Ska1', '#Spindle and kinetochore-associated protein 1', '-', '-', '66468'),
(288, 'P23624', 'Meiosis-specific protein SPO13', 'GO:0000780===c;k', 33295, 'Required for meiosis I segmentation (PubMed:2123556). Probably acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (PubMed:25533956). {ECO:0000269|PubMed:2123556; ECO:0000305|PubMed:25533956}.', 'MAPRKRFRLLELGSPTHSKRKVQKPLQEKTPNLRVSPLAFKIGKEIKNKEIRKTKKTESENIFNSKHVDLRLESPHPGLNFVSDAQQYSKAGDVRYLKNKSSNTLKNERQTIERPSFDNSLRFEDIEQPPKSTSTPVLSQSSQINVEREAPMFPVPYYIAPSPMYNFSPYQNFVGNPTFLTPSHNPNLNYAIPIQRPELLYPNVNVYDSPLFKKTRLPHQTKSLDKEKNYQYLPIYPVSISNNGDFVGQETPRAAPKLSKKRLSNTLDVNCSDYESSGQNATYNDSESSLN', 291, 'P23624; D3DKV9;', 'KD00288', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SPO13', '#Meiosis-specific protein SPO13#Sporulation-specific protein 13', '-', '-', '856405'),
(289, 'Q561R1', 'Centromere protein T', 'GO:0000777===GO:0051382', 56861, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome- associated complex that binds specifically to histone H3- containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis (By similarity). {ECO:0000250}.', 'MADLSSPDGDPTIRTLLRHVLDTADSHTPRRRQSTQTNPQRRRSQTPYSKRQGSQRKTSTRKHSHGTGSVGRLARVQGHGHLEEQTPRTLLQNILLTAPESSTVMPNPVVKPAQVPEVARPSRRGSSRGSLELQLPELDPPSTLAPGLKAPGKRKQKLRLSVFQQEVNQQLPLPQEQRGAADGSSLASSFNLSFVPSVQPQTVDRPGLARRRPVRRPVNIGAFLQNLENKSLTSALPGDSHRTPVAALPTDVVFEDTQPFSQPLAGCSLSVHHSLPNPSQTEVEDAERVVGPRTPSTGTRPQSQMSRAGFGASPLPFSEPQPQSPELREAVGSKEAEEPKDLEGSSGDEETSGMPASRELSSSAQDLLLAEEPHQLFEPPPSPGVAAVSSESVPAKLPSRTRTAQPRHHQDPYKAGLSHYVKLFSFHTKMPVEKAALEMVEKCLDEYFQRLCNDLEVFAAHAGRKTVKPKDLELLMRRQGLVTDQVSLHVLVERYLPLEYRQQLIPCAFRGNSVFPAQ', 518, 'Q561R1;', 'KD00289', 'Rattus norvegicus (Rat)', 'Cenpt', '#Centromere protein T#CENP-T', '-', '-', '307805'),
(290, 'Q08E31', 'Calcium-responsive transactivator', 'GO:0000777===GO:0000780', 43329, 'Transcriptional activator which is required for calcium- dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex; a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons; transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx; RB1 is dephosphorylated by calcineurin; which leads to release of the repressor complex. At the same time; there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism; which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter; and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP (By similarity). {ECO:0000250}.', 'MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILDYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQSMTLGPGGLSQSGSAQGLHSQGSLSDAIGAGLPPSSLMQAQIGNGPNHVSLQQTAQSTLPTTSMSMSGSGHGSGPGYSHSGPASQSVPLQSQGAISNYVSRANINMQSNPVSMMHQQAASSHYSAAQGGSQHYQGQSMAMMGQSGQGGGVMGQRPMAPYRPSQQGSSQQYLGQEEYYGGEQYGHGQAASEPMSQQYYPDGHGDYAYQPASYTDQSYDRSFEDSTQHYYEGGNSQYSQQQTGYQQGTAQQQTYSQQQYPNQQSYPGQQQGYGPAQGAPSQYSSYQQGQGQQYGSYRASQTGPSTQQQRPYGYEQGQYGNYQQ', 402, 'Q08E31;', 'KD00290', 'Bos taurus (Bovine)', 'SS18L1', '#Calcium-responsive transactivator#SS18-like protein 1', '-', '-', '768207'),
(291, 'Q08DR0', 'PHD finger protein 6', 'GO:0000777', 41289, 'Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000250}.', 'MSSSVEQKKGPTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMVYCRKHKKTAHNSEADLEESFNEHELEPSSPKSKKKSRKGRPRKTNFKGLSEDTRSTSSHGTDEMESSSYRDRSPHRSSPSDTRPKCGFCHVGEEENQARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMKCTLCSQPGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNHSGNDERDEEDEERESKSRGKVEIDQQQLTQQQLNGN', 365, 'Q08DR0;', 'KD00291', 'Bos taurus (Bovine)', 'PHF6', '#PHD finger protein 6', '-', '-', '100847396'),
(292, 'Q9HAF1', 'Chromatin modification-related protein MEAF6', 'k', 21635, 'Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity; a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. {ECO:0000269|PubMed:14966270; ECO:0000269|PubMed:16387653; ECO:0000269|PubMed:18794358}.', 'MAMHNKAAPPQIPDTRRELAELVKRKQELAETLANLERQIYAFEGSYLEDTQMYGNIIRGWDRYLTNQKNSNSKNDRRNRKFKEAERLFSKSSVTSAAAVSALAGVQDQLIEKREPGSGTESDTSPDFHNQENEPSQEDPEDLDGSVQGVKPQKAASSTSSGSHHSSHKKRKNKNRHRIDLKLNKKPRADY', 191, 'Q9HAF1; B1AK64; Q4F967; Q7Z311; Q86WE3;', 'KD00292', 'Homo sapiens (Human)', 'MEAF6', '#Chromatin modification-related protein MEAF6#MYST/Esa1-associated factor 6#Esa1-associated factor 6 homolog#Protein EAF6 homolog#hEAF6#Sarcoma antigen NY-SAR-91', '-', 'ENSG00000163875', '-'),
(293, 'Q28H51', 'Baculoviral IAP repeat-containing protein 5.1', 'GO:0000777===GO:0032133', 18756, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Stimulates the mitotic kinase activity of aurkb/aurora-B in the CPC. Does not appear to exhibit anti-apoptotic activity (By similarity). {ECO:0000250|UniProtKB:Q8JGN5}.', 'MHSAKNRFVQAVQRLQDFRNMYDYEARLATFADWPFTENCKCTPENMAKAGFVHCPTENEPDVACCFFCLKELEGWEPDDDPWTEHSKRSASCGFLSLTKCVNDLTMEGFLRLEADRIKSFYRKFSTVVLQYVEEEMTATTKRLLEYFSNQHQCSIDLDR', 160, 'Q28H51;', 'KD00293', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'birc5.1', '#Baculoviral IAP repeat-containing protein 5.1#Survivin1 {ECO:0000250|UniProtKB:Q8JGN5}', '-', '-', '733532'),
(294, 'Q08DR9', 'Protein Spindly', 'GO:0043515===GO:0034501===GO:0000940', 69621, 'Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. {ECO:0000255|HAMAP-Rule:MF_03041}.', 'MESDVIADLRCKLKETEEERRKAAQYGLQLVESQNELQNQLDKCRNEMMTLTESYEQEKYTLQREVELKSRMLESLSSECETIKQQQKMHLEQLEETLSRSHGQEVNELKKKLETLKAELDEARLSEKQLKHKVDHQEKLLSSKSKEMQMSERVHESVSSETLTLQIELTEMENVKTTLQEEVNELQYRQEQLELLNANLMRQVDRLKGEKEEREKEAVSYYDALEKARVVNQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNAFNREQMQRMKVQIATLLQMKGSQAEFEQQERLLAMLEQKNGEIKHLLGEIRNLEKFKSLYESMESKPSANSVALEDDTYYTDLLQIKLDNLNKESESIKGELSIQRMKALLESQRALDIERKLFLNERHLQLSQSENMKLRAKLDELKLKYEPEEKIEVPVLKKRREVLPVDISTPNGVCAPSAVGEEDYRLSPQKEEAQSCSDGSEDNNLQLEKTVSVSTSGVILSPYKSLTLDIQPRKEKKCVKLTGVPADLEALSERSRNTPNSPRLAAESRLQREVKQGKETASKLEKAACKKSYPTVYVSSKSTPETQCPQQ', 603, 'Q08DR9;', 'KD00294', 'Bos taurus (Bovine)', 'SPDL1', '#Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041}#Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041}#Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041}', '-', '-', '515158'),
(295, 'Q96IF1', 'LIM domain-containing protein ajuba', 'c;k', 56934, 'Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination; cytoskeletal organization; repression of gene transcription; mitosis; cell-cell adhesion; cell differentiation; proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell- cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1- induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. {ECO:0000269|PubMed:12417594; ECO:0000269|PubMed:13678582; ECO:0000269|PubMed:15870274; ECO:0000269|PubMed:16413547; ECO:0000269|PubMed:17909014; ECO:0000269|PubMed:18805794; ECO:0000269|PubMed:20303269; ECO:0000269|PubMed:20616046; ECO:0000269|PubMed:22286099}.', 'MERLGEKASRLLEKFGRRKGESSRSGSDGTPGPGKGRLSGLGGPRKSGPRGATGGPGDEPLEPAREQGSLDAERNQRGSFEAPRYEGSFPAGPPPTRALPLPQSLPPDFRLEPTAPALSPRSSFASSSASDASKPSSPRGSLLLDGAGAGGAGGSRPCSNRTSGISMGYDQRHGSPLPAGPCLFGPPLAGAPAGYSPGGVPSAYPELHAALDRLYAQRPAGFGCQESRHSYPPALGSPGALAGAGVGAAGPLERRGAQPGRHSVTGYGDCAVGARYQDELTALLRLTVGTGGREAGARGEPSGIEPSGLEEPPGPFVPEAARARMREPEAREDYFGTCIKCNKGIYGQSNACQALDSLYHTQCFVCCSCGRTLRCKAFYSVNGSVYCEEDYLFSGFQEAAEKCCVCGHLILEKILQAMGKSYHPGCFRCIVCNKCLDGIPFTVDFSNQVYCVTDYHKNYAPKCAACGQPILPSEGCEDIVRVISMDRDYHFECYHCEDCRMQLSDEEGCCCFPLDGHLLCHGCHMQRLNARQPPANYI', 538, 'Q96IF1; A8MX18; D3DS37;', 'KD00295', 'Homo sapiens (Human)', 'AJUBA', '#LIM domain-containing protein ajuba', '-', 'ENSG00000129474', '-'),
(296, 'Q12334', 'Protein SCM3', 'GO:0051382===GO:0000780===k', 25754, '', 'MKTNKKISKRRSLKNLHGALKGLLKESGKKSESKIRKHSDCNPVHRVYPPNIEKRKTKKDDGISRPIAERNGHVYIMSKENHIIPKLTDDEVMERHKLADENMRKVWSNIISKYESIEEQGDLVDLKTGEIVEDNGHIKTLTANNSTKDKRTKYTSVLRDIIDISDEEDGDKNDEYTLWANDSEASDSEVDADNDTEEEKDEKLIDADFKKYEAKLSKRILRD', 223, 'Q12334; D6VRK9;', 'KD00296', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SCM3', '#Protein SCM3#Suppressor of chromosome missegregation protein 3', '-', '-', '851416'),
(297, 'Q8JGN5', 'Baculoviral IAP repeat-containing protein 5.1-A', 'GO:0000777===GO:0032133', 18686, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Stimulates the mitotic kinase activity of aurkb/aurora-B in the CPC. Does not appear to exhibit anti-apoptotic activity. {ECO:0000269|PubMed:12221116; ECO:0000269|PubMed:15853809; ECO:0000269|PubMed:16888809}.', 'MYSAKNRFVQAVQRLQDFKNMYDYDARLATFADWPFTENCKCTPESMAKAGFVHCPTENEPDVACCFFCLKELEGWEPDDDPWTEHSKRSANCGFLSLTKCVNDLTMEGFLRLEGDRIKSFYRKFSTVVLQYVEEEMTAATKRLLEYFSNQHHCSIDLDH', 160, 'Q8JGN5; Q4V7U0; Q50L40; Q8JG75;', 'KD00297', 'Xenopus laevis (African clawed frog)', 'birc5.1-a', '#Baculoviral IAP repeat-containing protein 5.1-A#Bir1-A protein {ECO:0000312|EMBL:AAH73047.1}#Survivin/XBIR1 {ECO:0000303|PubMed:12464631}#XBIR1 {ECO:0000303|PubMed:12464631}#Survivin1-a#XSurvivin1 {ECO:0000303|PubMed:15853809}#XSurvivin1A {ECO:0000312|EMBL:BAD98265.1}#Xsvv1 {ECO:0000303|PubMed:15853809}#xSurvivin {ECO:0000303|PubMed:12221116}', '-', '-', '394382'),
(298, 'Q148G7', 'Dynactin subunit 6', 'GO:0000777', 20675, '', 'MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQALIINAHPDNITPDAEDPEPKPMIIGTNNVFEVGCYCQAMKIGDNNVIESKAYVGRNVILTSGCIIGACCNLNTFEVIPENTVIYGGDCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKTMKGSSTPVKN', 190, 'Q148G7;', 'KD00298', 'Bos taurus (Bovine)', 'DCTN6', '#Dynactin subunit 6', '-', '-', '513751'),
(299, 'Q9YGY3', 'Mitotic checkpoint protein BUB3', 'GO:0000777===k', 37253, 'Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Plays a role in the kinetochore-mediated mitotic checkpoint; which delays anaphase onset until all chromosomes have attached properly to the mitotic spindle. Required to establish and maintain spindle checkpoint arrest in eggs. {ECO:0000269|PubMed:12538762}.', 'MNTQTDMTGSNEFKLNQAPEDGISAVKFSPNTSQFLLVSSWDSSVRLYDVPANTMRLKYQHAGPVLDCAFYDPTHAWSGGLDHQLKMHDLNTDGDTVVGSHDAPIRCVEYCPEVNVIVTGSWDQTVKLWDPRTPCNAGTFSQPDKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSLEVQKKKYAFKCHRLKENNIEQIYPVNAVSFHNLHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGSTLAIAASYMYEMDDIDHPEDAIYIRQVTDAETKPK', 330, 'Q9YGY3; Q98UH2;', 'KD00299', 'Xenopus laevis (African clawed frog)', 'bub3', '#Mitotic checkpoint protein BUB3#xbub3#WD repeat protein Bub3', '-', '-', '399106'),
(300, 'Q6IRM9', 'Protein zwilch homolog', 'GO:0000777', 67380, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and mad1-mad2 complexes onto kinetochores (By similarity). {ECO:0000250}.', 'MWAERHRAAVELQQFLSSVYEQVKKEESLGPFQFKDDIQVHVVCDGHCKPLESFCSGSEVLYILEKKPLTLEDNVLDETENNEGISFYTSLQEIPQPQAIPTMRARQFLTSYTLTHNPNMVQLNSGAPVKVLPPLWVRCDCSDAEGTCWLGAEPIKSSRNEITGMSFRTVTCAGPTADKSTFPSLDSLRQAHKERHYSSVMQTRGFAQYDLFGCNTVENSVIESQSSVTVDFVWNGVERILQLPPLASAATLNIKVESGDLRSPVYSVYKELDFLLVLAEGLKTGVTEWPETGETKSAVDLVQLLLNDLKNKVDGLTSSVSKKDNEKIKSDTAAVDCSIQSFITERGDLDFAEMLWCRMRKSVSSYQDVVNCFSLVIQSLKNGEVHPWIHRGSSSALSKLIQQSYHGKMQSVSLTGLTPMRMLLEIGLDKMKKDYISCFIGQDLATFNYLDYFISSSVDIQEQVQRVKKLHHMLEVVVVCNAFLSLGHENLFPLTQSCLKYYKENPWNEQHVFQLPIRPSVISTFYQNSHPQTWRVEIISGHGQKEVKTTWQLTSRRPVDHVSFAVPDVPIDMTISGENEEIVYYPTQVSCSQVNFC', 597, 'Q6IRM9;', 'KD00300', 'Xenopus laevis (African clawed frog)', 'zwilch', '#Protein zwilch homolog', '-', '-', '432018'),
(301, 'Q9UQE7', 'Structural maintenance of chromosomes protein 3', 'GO:0003777===c;k', 141542, 'Central component of cohesin; a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase; the complex is cleaved and dissociates from chromatin; allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement. {ECO:0000269|PubMed:11076961; ECO:0000269|PubMed:19907496}.', 'MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDVEGSQSQDEGEGSGESERGSGSQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG', 1217, 'Q9UQE7; A8K156; O60464; Q5T482;', 'KD00301', 'Homo sapiens (Human)', 'SMC3', '#Structural maintenance of chromosomes protein 3#SMC protein 3#SMC-3#Basement membrane-associated chondroitin proteoglycan#Bamacan#Chondroitin sulfate proteoglycan 6#Chromosome-associated polypeptide#hCAP', '-', 'ENSG00000108055', '-'),
(302, 'Q9Y496', 'Kinesin-like protein KIF3A', 'GO:0003777', 80041, 'Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation (By similarity). {ECO:0000250}.', 'MPINKSEKPESCDNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQMLIIDNFIPRDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKEKDPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKTGRRKRSAKPETVIDSLLQ', 699, 'Q9Y496; A8MSW9; Q59EN1; Q86XE9; Q9Y6V4;', 'KD00302', 'Homo sapiens (Human)', 'KIF3A', '#Kinesin-like protein KIF3A#Microtubule plus end-directed kinesin motor 3A', '-', 'ENSG00000131437', '-'),
(303, 'Q75E95', 'DASH complex subunit DAD1', 'GO:0008608===GO:0051987===GO:0042729', 12043, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MIMSKDIATTPELSEPDKYFVEQRDLLLQEITSTLDSILNNLNGLNISLENSIAVGKEFESVSELWKVFYDGLANGAAPGVAAANPSSQDLPTEPVAAHQNAAAGNSDAPAPSQ', 114, 'Q75E95;', 'KD00303', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DAD1', '#DASH complex subunit DAD1#Outer kinetochore protein DAD1', '-', '-', '4618765'),
(304, 'Q9VYB1', 'LD33040pNdc80', 'k', 77888, '', 'MSHLMPRRTSEFRGDVLEERGTADKRQTRATKRSAATHTPSSSQAAPRRPSASRLPQPLNLERDRASQMGVTPKRGHRFVPSTAERAIAPHSDKKWVAERAQQILEYLHGIQNSEAPTGLIADLFSRPGGLRHMTIKQFVSILNFMFHHIWRNRVTVGQNHVEDITSAMQKLQYPYQVNKSWLVSPTTQHSFGHVIVLLDFLMDFLPPLPSSDVVEEEFPFMETMEQPSSYLNSMHCESTTIMSTTQAHAIQLDEDVNGLLFEEASKCIALWDQELTNEEAKLQAETRDQVISKKCDLPDRKALDQLIGDLKTKLQQLENKLHDPSEDNKLNKLERLTKEHDQLAQQLAASEEELIKKLKLYEQLSAQVEEKQSNLRQQMKYEKRLEQAVNRQKFSAQQLKELQMKCDDMENYSKAYERQVKEVSELELHQQVMLSRAKQKQLDSVEVFNSHVRHLSMDPVICGLIKSGIGQQSDLTLPLNPNQEDISERVQCLELLGKLLQQHRQQNIDRRQMLDKQVAKVKSDSIELDTEIATMDSQLRAQKQRLTKMEASYRTKRDMQAQHRQQLLEDQYDQTARLDELEKREKQALEKLEASKQRNEDLLTAAEQFQEQDLKARQDRLEKCEQKLAKAEDQLLAVESKVNATQAKLNEVEQKVYSAKLPSFQPVLDAIKNH', 675, 'Q9VYB1;', 'KD00304', 'Drosophila melanogaster (Fruit fly)', 'Ndc80', '#LD33040p {ECO:0000313|EMBL:AAL28950.1}#Ndc80 {ECO:0000313|EMBL:AAF48292.1}', '-', '-', '32316'),
(305, 'Q9CQ82', 'Centromere protein R', 'GO:0000777', 20026, 'Transcription coregulator that can have both coactivator and corepressor functions. Involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast; it does not coactivate nuclear receptors for retinoic acid; vitamin D; progesterone receptor; nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit; possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells; but not in other cancer cells; via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A-associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex (By similarity). {ECO:0000250}.', 'MPVKRSLKLDDQFEKNSFSPSKIVRKKSITAYSPTTGTYQLSPFSSPATPKEQEHRNGPSNETRKRSNLSSPVRQESTVKDRDGFMVLLSKIEISSEKTMEIMKNLSSIQALEGNRQLEDLIGVSLVPCSLKSEARKTKELMTKVIKQKLFEKKKSRITPKDHHLDSFEFLKAILN', 176, 'Q9CQ82; Q3TLR0; Q3TNR4;', 'KD00305', 'Mus musculus (Mouse)', 'Itgb3bp', '#Centromere protein R#CENP-R#Nuclear receptor-interacting factor 3', '-', '-', '67733'),
(306, 'P23635', 'Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit', 'k', 35291, 'Essential role in cell cycle control. PP2A may be involved in controlling the entry into mitosis; possibly acting as an inhibitor.', 'MSVSGKIGEVDRWIEQLSRCEPLSEEDVIQMCDLAKEVLSVESNVQSVRCPVTVCGDIHGQFHDLMELFNIGGPSPDTNYLFMGDYVDRGYHSVETVSLLIAFKIRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWQYFTDLFDYLPLTALIEDRIFCLHGGLSPSIDTLDHVRILDRVQEVPHEGPICDLLWSDPDDRPGWGISPRGAGYTFGPDIAEAFNHNNGLDLIARAHQLVMEGYNWTTNHNVVTIFSAPNYCYRCGNQAAIMGIDDHINYAFIQYDTAPRKEELHVTRRTPDYFL', 309, 'P23635;', 'KD00306', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ppa1', '#Minor serine/threonine-protein phosphatase PP2A-1 catalytic subunit#3.1.3.16', '-', '-', '2542052'),
(307, 'P23636', 'Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit', 'k', 36489, 'Essential role in cell cycle control. PP2A may be involved in controlling the entry into mitosis; possibly acting as an inhibitor.', 'MSIDPANDSKLAPEANDATLGDVDRWIEQLKKCEPLSEADVEMLCDKAREVLCQENNVQPVRNPVTVCGDIHGQFHDLMELFKIGGDVPDMNYLFMGDYVDRGYHSVETVSLLVAMKLRYPNRITILRGNHESRQITQVYGFYDECLRKYGSANVWKHFTNLFDYFPLTALIEDRIFCLHGGLSPSIDSLDHVRTLDRVQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISETFNHANGLSLTARAHQLVMEGFNWAHDGDVVTIFSAPNYCYRCGNQAAILEVDDTMNQVFLQFDPAPREGEPVIARRTPDYFL', 322, 'P23636;', 'KD00307', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ppa2', '#Major serine/threonine-protein phosphatase PP2A-2 catalytic subunit#3.1.3.16', '-', '-', '2540072'),
(308, 'P38265', 'Central kinetochore subunit IML3', 'GO:0000942===k', 28066, 'Component of the central kinetochore; which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle- microtubule attachments and proper chromosome segregation. {ECO:0000269|PubMed:11361335; ECO:0000269|PubMed:15241623}.', 'MPYTWKFLGISKQLSLENGIAKLNQLLNLEVDLDIQTIRVPSDPDGGTAADEYIRYEMRLDISNLDEGTYSKFIFLGNSKMEVPMFLCYCGTDNRNEVVLQWLKAEYGVIMWPIKFEQKTMIKLADASIVHVTKENIEQITWFSSKLYFEPETQDKNLRQFSIEIPRESCEGLALGYGNTMHPYNDAIVPYIYNETGMAVERLPLTSVILAGHTKIMRESIVTSTRSLRNRVLAVVLQSIQFTSE', 245, 'P38265; D6VQA6;', 'KD00308', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'IML3', '#Central kinetochore subunit IML3#Increased minichromosome loss protein 3#Minichromosome maintenance protein 19', '-', '-', '852404'),
(309, 'O94751', 'Checkpoint serine/threonine-protein kinase bub1', 'GO:0034501===GO:0000778===GO:0051315===GO:1990298===k', 118353, 'Involved in cell cycle checkpoint enforcement. Acts to stabilize the spindle during mitosis. Required for the correct localization of bub3 and mad3 to the kinetochore. Appears to have a role in chromosome segregation. Catalyzes the phosphorylation of bub3. {ECO:0000269|PubMed:15509783; ECO:0000269|PubMed:15525673; ECO:0000269|PubMed:9864354}.', 'MSDWRLTENVLDQNIPETKPRESKTRLEEIQRLALFQEELDIIEELDDPVDVWYRCIEWLLETRFLGMETVNKMLDDAIQYLERCRFALNDVRHLLIQLAKIKQSYETPDELQQAAKQFYQLASKGIGLELALFYEEYGSLLIRMQRWKEASEVFHAAVSREARPLVRLLRNAAEFSRAYDLHNAHPSIHDAPYSSPFPPPRIVLGSKPVSSSTLPSKPKSFQVFSDASSSRDSQNASDLPQAKSLESEANTPNLPLLYDKSSGKRVEYSAFNFLALYENGEERSMEECRAQRYLSSIQPNTAASFPKVVPKNEISVHHDSSSSNVSPIYKNPVAEQSDTPTRSLPKNYAYVAKSTSPELKVFDTVMPVALSPKPAQKPPSPTIHTKAALADILDIFNQPLRSESLEKSSKSPISAQSSYLGTPLKNDENSSNSGATSLTGRSQEEHLDFIPSLTPSKNYPSKIYSPNKNLDFSHTASKAETYKNSNELENVKREQPFSELLPSTLQEETATGTTSTTFANAKRRPEDSNISPTNPKKLHTLPRSPQYSTVDSNSVLSPAMPKGYMFVNENQSMKHESSVSNPVATIPHENGKHDFGQLSPIEHKPFFPKNDDELPGPSGYLTMPYEEAMASLSNLPTLINPLDQSLRDLLFQVLRPSLLRDKDYHEHETSFALVEHIESFVSKIKPKAGGPGRRRSSNRHSLDGPEFHLFYPPNTNLSVISKLGQGAFAPVYLVKSKIETENGDVSQGGAENNESKLFALKIETPPSCFEFYLTRQAMTRLKGLRETNSILPVHQLHMFHDTSHLLMDYRPQGSILDLVNSMHNSTFSSSGMDEILVVFFSIEFLRIIEALHTHKIIHGDLKADNALLRLETVADSEWSPIYSPEGLYGWSFKGIYLIDFGRGIDLSLFEEKVKFIADWDTDLQDCIEMREGRPWTYQIDYHGLAAIIYTMLFGQYIETRIEVINGQRRQVLTQRMKRYWNQDLWHRLFDLLLNPTLHVSEENLPMTEELSKIRIEMEEWLVNHSTGGSGLKGLLKSIEKRKI', 1044, 'O94751;', 'KD00309', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'bub1', '#Checkpoint serine/threonine-protein kinase bub1#2.7.11.1', '-', '-', '2538736'),
(310, 'Q6BWK6', 'DASH complex subunit DAM1', 'GO:0008608===GO:0042729', 33059, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MASSPRPTTPNSQKKRSGRRQSHRSSGAYNILPQSPKIHYPVDPDNLPLEAPGNTEKFESLSDALEELDVNMTNLQSIHEAISDGFNESFASFLYGLSITMWCVDFPGCPSRNQWEKLKLVEGLDDRISELAEKIRSHREENERLKNRLASNVVESTEEVENHSDSHENRKPQHSHRVGKGPTRQVDEGDDTYMTNEGSFVVNPSAPSATRIPQPVKTAPRRFTKHTPPPPPPPPPADTSMHSSYRGPNLNQPPRYMRGLFDSTNRPTTPSNNRSKRVANPNRIQKATGRPPFR', 294, 'Q6BWK6;', 'KD00310', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'DAM1', '#DASH complex subunit DAM1#Outer kinetochore protein DAM1', '-', '-', '2913340'),
(311, 'Q6FRP0', 'DASH complex subunit DAD4', 'GO:0008608===GO:0042729', 8467, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MVENPYEEVQVNVLSRIIANVEKLNQSVRTLNQELENVNKRNKNLEVMGQICENYHRSVQFNLEATGNKKPPL', 73, 'Q6FRP0;', 'KD00311', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'DAD4', '#DASH complex subunit DAD4#Outer kinetochore protein DAD4', '-', '-', '2888581'),
(312, 'Q9LDN0', 'Kinesin-like protein KIN12A', 'GO:0003777', 144632, 'Plus-end directed kinesin-like motor enzyme that plays a critical role in the organization of phragmoplast microtubules during cytokinesis. Constitutes a signaling module in association with serine/threonine-protein kinase TIO that is required to support phragmoplast expansion and cell-plate growth in plant cells. Binds microtubules in an ATP-sensitive manner. {ECO:0000269|PubMed:10898978; ECO:0000269|PubMed:17720869}.', 'MKKHFTLPRNAILRDGGEPHSPNPSISKSKPPRKLRSAKENAPPLDRNTSTPDHRSMRMKNPLPPRPPPSNPLKRKLSAETATESGFSDSGVKVIVRMKPLNKGEEGDMIVEKMSKDSLTVSGQTFTFDSIANPESTQEQMFQLVGAPLVENCLSGFNSSVFAYGQTGSGKTYTMWGPANGLLEEHLCGDQRGLTPRVFERLFARIKEEQVKHAERQLNYQCRCSLLEIYNEQITDLLDPSQKNLMIREDVKSGVYVENLTEEYVKNLTDVSQLLIKGLGNRRTGATSVNTESSRSHCVFTCVVESRCKNVADGLSSFKTSRINLVDLAGSERQKSTGAAGERLKEAGNINRSLSQLGNLINILAEISQTGKPRHIPYRDSRLTFLLQESLGGNAKLAMVCAVSPSQSCRSETFSTLRFAQRAKAIQNKAVVNEVMQDDVNFLRGVIHQLRDELQRMKNDGNNPTNPNVAYSTAWNARRSLNLLRSFGLGHPRSLPHEDNDGDIEMEIDEAAVERLCVQVGLQSSLASEGINHDMNRVKSIHSSDGQSIEKRLPEDSDVAMEDACCHTENHEPETVDNMRTETETGIRENQIKTHSQTLDHESSFQPLSVKDALCSSLNKSEDVSSCPDLVPQDVTSANVLIADGVDDPEHLVNSASPSLCIDPVGATPVLKSPTLSVSPTIRNSRKSLKTSELSTASQKDSEGENLVTEAADPSPATSKKMNNCSSALSTQKSKVFPVRTERLASSLHKGIKLLESYCQSTAQRRSTYRFSFKAPDSEPSTSISKADAGVQTIPGADAISEENTKEFLCCKCKCREQFDAQQMGDMPNLQLVPVDNSEVAEKSKNQVPKAVEKVLAGSIRREMALEEFCTKQASEITQLNRLVQQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFLDEEFASLLHEHKLLKDMYQNHPEVLKTKIELERTQEEVENFKNFYGDMGEREVLLEEIQDLKLQLQCYIDPSLKSALKTCTLLKLSYQAPPVNAIPESQDESLEKTLEQERLCWTEAETKWISLSEELRTELEASKALINKQKHELEIEKRCGEELKEAMQMAMEGHARMLEQYADLEEKHMQLLARHRRIQDGIDDVKKAAARAGVRGAESRFINALAAEISALKVEKEKERQYLRDENKSLQTQLRDTAEAIQAAGELLVRLKEAEEGLTVAQKRAMDAEYEAAEAYRQIDKLKKKHENEINTLNQLVPQSHIHNECSTKCDQAVEPSVNASSEQQWRDEFEPLYKKETEFSNLAEPSWFSGYDRCNI', 1292, 'Q9LDN0; O23274;', 'KD00312', 'Arabidopsis thaliana (Mouse-ear cress)', 'KIN12A', '#Kinesin-like protein KIN12A#Phragmoplast-associated kinesin-related protein 1#AtPAKRP1', '-', '-', '827054'),
(313, 'Q0MTC0', 'Histone H3-like centromeric protein CSE4', 'GO:0000777', 22435, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). {ECO:0000250}.', 'MEQSVRSIDGARSVAGAGRTIIDRESINQRALQLLQRNRQRRLLLKRSEDRARYIPERREQKRELDETLETRNVPQHHISAHERITKAKSHGSKYKPSDLALAEIRKYQRSTDLLISRMPFARLVKEVTDQFASDEEPLRWQSMAIMALQEASEAYLVGLLEHTNLLALHAKRITIMRKDMQLARRIRGQFI', 192, 'Q0MTC0;', 'KD00313', 'Kluyveromyces marxianus (Yeast) (Candida kefyr)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog', '-', '-', '-'),
(314, 'Q22257', 'HCP-2', 'k', 147395, '', 'MEESTNDGDENKPATGKKRQQLESPFSAATPKSRLGKESKRFFGRSAMNLADGNLEETRIEPDSRHSSTSTSDSILDDSSISNFSTLAPPNTSVDDNSVCEPPRASSAHDVDPNLEQTKVYSEDSISKDCSIADESFATDGDVTLANDFFQQATIQDLENTPSTPLRSQTQVGDESTPTAPSPLRSKIPIESEVVQSTSVESVQSTSQHEKSRIEYSLYEFEMLEKNIEHDEVVKDLQLKIELLGEKHRQTLVEIKEAREVEEKMLMQQVEEAVKKTKSEREAAKTLEQLLEKRIEELEMKLTEPNGEKLQFEHQLEELKSRCEELTDKALKVDVMQHSIEDYEKKFVELQEMKEEADEQLQKAKEDIETLQMKYVELETTINKEVFSNSEIETLKSEHEIVRKLMLDEIHRLENEMSALQPKNDTTELEELQKTLDDLKIDCCNLTSKMLELQSELVEVKEKATSEIGEAVQKNGELLEQINSLRVENAKLVDMEGQLNDAHRKAEDKDVRISELLTTIESLRQDSEASDKLLMDSESTQNEYSLALENTVSELETMRREYKASVDKVCSLQLELEEIQHETSVELEEAEIRIKELELAQEEAVKTGSSQLKKLEIVQEDCQKLRDQLKEEQIQQLVSLRETSEVMHQESARHQEEKYQIQSKLMSTEAEVIELRSSIDSLQAEVRVQSDSAADQKHILEDYLRKIRQAEETNEKLRSDLASSEEQILDLKNQQESLIDDLKEKLHSAESTNQELQVSLEMLKIEVSNARQKVMESEVLKESFEALQLELSASQEVSRSVVDAAVQEKDGLLRLVDTLKLKIEDTEKSAQDLQQSSVEEIKQLQLDLQNFKQNAEVLESLNEKLNSSHKRDMVALASQLEELQHKLVVGESQVENVKEELIGAKIMNKEMVDELNAKLGDALEGMEELKKSLEVSEAKVQRREEELIAQVSKHRDQQEQLQLTLDELKSAQHSTETSRSQSNELAARIEELEASISFAQKALQDVEDVKHQQDIQISEANEAMVKLKQDFETERTSLQNEFNQTVSADKEQLGHAEQMIAQKEKEIITLQARIEAMSQQFEERLEASNVWKTQAMNVGTLTESLSQLQVQLQQMNEKLVASDKYAVEVEQQAQHDITVIQEEKNEQSAALEEALSKIAELEEQLGRAQKEIVRLEKVCDDFDDVERELKDAISKLQSEIKQLKGIKKPPKVMGLLQQARLGVKPLSREHSHAEPPEPVVEDKFEDAQDSFQEEFSHSPDAITSSTVLHPDDHLQETTAVETPSKKANRSNCNQQ', 1295, 'Q22257;', 'KD00314', 'Caenorhabditis elegans', 'hcp-2', '#HCP-2 {ECO:0000313|EMBL:CAA94789.1}', '-', '-', '179353'),
(315, 'P84243', 'Histone H3.3', 'c;k;m', 15328, 'Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes; suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin; limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation; DNA repair; DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones; also called histone code; and nucleosome remodeling. {ECO:0000269|PubMed:14718166; ECO:0000269|PubMed:15776021; ECO:0000269|PubMed:16258499}.', 'MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA', 136, 'P84243; P06351; P33155; Q5VV55; Q5VV56; Q66I33; Q9V3W4;', 'KD00315', 'Homo sapiens (Human)', 'H3F3A', '#Histone H3.3', '-', 'ENSG00000163041', '-'),
(316, 'P56523', 'Histone deacetylase clr3', 'k', 76792, 'Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A; H2B; H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation; cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac- containing repressor complex (SHREC). {ECO:0000269|PubMed:17289569}.', 'MLASNSDGASTSVKPSDDAVNTVTPWSILLTNNKPMSGSENTLNNESHEMSQILKKSGLCYDPRMRFHATLSEVDDHPEDPRRVLRVFEAIKKAGYVSNVPSPSDVFLRIPAREATLEELLQVHSQEMYDRVTNTEKMSHEDLANLEKISDSLYYNNESAFCARLACGSAIETCTAVVTGQVKNAFAVVRPPGHHAEPHKPGGFCLFNNVSVTARSMLQRFPDKIKRVLIVDWDIHHGNGTQMAFYDDPNVLYVSLHRYENGRFYPGTNYGCAENCGEGPGLGRTVNIPWSCAGMGDGDYIYAFQRVVMPVAYEFDPDLVIVSCGFDAAAGDHIGQFLLTPAAYAHMTQMLMGLADGKVFISLEGGYNLDSISTSALAVAQSLLGIPPGRLHTTYACPQAVATINHVTKIQSQYWRCMRPKHFDANPKDAHVDRLHDVIRTYQAKKLFEDWKITNMPILRDSVSNVFNNQVLCSSNFFQKDNLLVIVHESPRVLGNGTSETNVLNLNDSLLVDPVSLYVEWAMQQDWGLIDINIPEVVTDGENAPVDILSEVKELCLYVWDNYVELSISKNIFFIGGGKAVHGLVNLASSRNVSDRVKCMVNFLGTEPLVGLKTASEEDLPTWYYRHSLVFVSSSNECWKKAKRAKRRYGRLMQSEHTETSDMMEQHYRAVTQYLLHLLQKARPTSQ', 687, 'P56523;', 'KD00316', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'clr3', '#Histone deacetylase clr3#3.5.1.98#Cryptic loci regulator 3', '-', '-', '2540821'),
(317, 'O75122', 'CLIP-associating protein 2', 'GO:0000777===GO:0005828===k', 141133, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269|PubMed:11290329; ECO:0000269|PubMed:15631994; ECO:0000269|PubMed:16824950; ECO:0000269|PubMed:16866869; ECO:0000269|PubMed:16914514; ECO:0000269|PubMed:17543864; ECO:0000269|PubMed:20937854}.', 'MAMGDDKSFDDEESVDGNRPSSAASAFKVPAPKTSGNPANSARKPGSAGGPKVGGASKEGGAGAVDEDDFIKAFTDVPSIQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSTVAGRVSAGSSKASSLPGSLQRSRSDIDVNAAAGAKAHHAAGQSVRRGRLGAGALNAGSYASLEDTSDKLDGTASEDGRVRAKLSAPLAGMGNAKADSRGRSRTKMVSQSQPGSRSGSPGRVLTTTALSTVSSGVQRVLVNSASAQKRSKIPRSQGCSREASPSRLSVARSSRIPRPSVSQGCSREASRESSRDTSPVRSFQPLASRHHSRSTGALYAPEVYGASGPGYGISQSSRLSSSVSAMRVLNTGSDVEEAVADALKKPARRRYESYGMHSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASSNWSERKEGLLGLQNLLKNQRTLSRVELKRLCEIFTRMFADPHGKRVFSMFLETLVDFIQVHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRESFPNDLQFNILMRFTVDQTQTPSLKVKVAILKYIETLAKQMDPGDFINSSETRLAVSRVITWTTEPKSSDVRKAAQSVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLRNTGNGTQSSMGSPLTRPTPRSPANWSSPLTSPTNTSQNTLSPSAFDYDTENMNSEDIYSSLRGVTEAIQNFSFRSQEDMNEPLKRDSKKDDGDSMCGGPGMSDPRAGGDATDSSQTALDNKASLLHSMPTHSSPRSRDYNPYNYSDSISPFNKSALKEAMFDDDADQFPDDLSLDHSDLVAELLKELSNHNERVEERKIALYELMKLTQEESFSVWDEHFKTILLLLLETLGDKEPTIRALALKVLREILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEAASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLIQGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGSGGADPTTDVSGQS', 1294, 'O75122; B2RTR1; F5H604; Q7L8F6; Q8N6R6; Q9BQT3; Q9BQT4; Q9H7A3;Q9NSZ2;', 'KD00317', 'Homo sapiens (Human)', 'CLASP2', '#CLIP-associating protein 2#Cytoplasmic linker-associated protein 2#Protein Orbit homolog 2#hOrbit2', '-', 'ENSG00000163539', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(318, 'Q80TF6', 'StAR-related lipid transfer protein 9', 'GO:0003777', 500243, 'Microtubule-dependent motor protein required for spindle pole assembly during mitosis. Required to stabilize the pericentriolar material (PCM) (By similarity). {ECO:0000250}.', 'MANVQVAVRVRPLSKRETKEGGRIIVEVDDKVAKIRNVKVDSRPESFGDTREKVVAFGFDYCYWSVNPEDPHYASQEVVFRDLGTEVLSGAAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFIREDDCASQPCSRSIKVSFLEIYNERVRDLLKQSNQNKSYTLRVREHPEMGPYVQGLSQHVVTNYQQVIQLLEAGIANRITAATHVHEASSRSHAIFTIHCTQAILQNNLPSETASKINLVDLAGSERADPSYCKDRITEGANINKSLVTLGIVISTLAQNSQVFSSCQSLSSAASSGGDSGVPSTTSGASSGGGPARRQSYIPYRDSVLTWLLKESLGGNSKTIMVATVSPAHTSYSETMSTMRYASNAKNIINKPRVNEDANVKLIRELREEIERLKAVLLNFELIDTLTQHWTEKRNDRQALMEHYGVDINRKRARVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSTCGVVILRPTQGARCTVNGREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRHQRLKVGEALGSSGSLEWLDLDGDVSASRLGLCPVLRKERRVLEEQCDRDQQPSRHSEIPYRAQPEQQQCHVEALKQQAKEGQSRVQKELELDHTHISQQIKDNQQWLLTEETWLASLRETQQEGNCGEEKELEASVAPDAWLPTVPQTPPSPLVQSQKRVVQPQCSPRHTTRATVWNIRQKKVSFQLERIIKKRRLLEAQRRLEQLSTFFWIQDDGASRAPSWASSSNTSGPGSQRRSRWTTCSSLSLQRLGCRRLPQLHSDFMNWDPSAMSPPVPELTHQMPEKTLSTDCIPPKAGRLGRNSFHSSRWRKFSPARRASTQGTHLTVSHKSVSSQEIESLGKQPCQMSSQGQSTKKQKARDGSRTFIPAAQTRWASVNTKTGWQKEGTCGTYKDPKETTSQSTDLSGLEPAAGHRKVVKTFQAESKPSPSSRASKKHQRVLAARARDIVKTFSRLPHGGPLKNQPRAGDPGTPASFTDSRPIKDPVREEDRDLSDTESSYSVDSLSYIYAKVPKKLLKPEDLQGKWNLPDSENSESDNSQISEDSLAGKGHKSLPENSRGEYSMKDHGHSRARTSASVRGLPMPSDSSLCTQKYRSFSLDSLIDPENRQGEPFLGSADEMPTETFWHLQNATPSSVDQEAMDRPSPTNHRMGVGVNVLLPKSNSFYLDPQFQPPCEQLESEMEASYSEHTNPLRGLQLARESPLLSVDSWFSCDSKVSPSSPSGDIHSLCPSPDIHEIQPHDEKPKHWLSIEEPKPPGTCKLPQSSTEPPCSSDLYATSASDTSKPSVCESQGLLQPGDGGFFQGREMPDMTNQGISEESHNSDMSSVLAPSATSFTQVCSVNKDWAALHQEYLLELSDSGFEAVGEPRPAFPFLEEDSSSLAEASDKVDTQLPTGPGLPRNLDFSSFPVHISKIGHLRAEKDHDSLSAKVESASDLLSTVERMSSNGTYPADIESLTSGSINAQPYTAGNVIPSSMTEAWEVHRASLEGCLQGDRHSVLITSSGQKRAYHNDDTLATEGDCLPQDGALLGKNTKVQPGLLSHNSYQQPLLEEKAASQQCTDGEVAGTRIDACCAFPSGPELFLHSTPWSSSPSSLQPPPLETFYVTKSRDALTETALEIPACREAWVPSPPPREAWGFDHSHQVSQKAHWKNNLPKLSQSQNSKIDSPQQTTTKRPTDLDTGEGTEELGKHSRNMREEENHDSAYSFVAQNRQHLPSTRLKVCECGNQLGILNKEYSLSVHQDEEGASAWHHGSVAFNGSEPKTLLFICDSKASGEEQSLLLPQIQSCGMHSQSPGARSDFIGKIANLDPEKVIPEEAAVSLKSRSLHCLSSPVIVAGGRSPTRRREGRNETGLLREVISKDIQEEFSLPGTQYICERCHLLLCSRERKPTECKAHGQSQEVQSKEEPLEEKQNKRVNNIDEMARLMRSVMQLETGILEIESKHNKHLHASHMPSTELMLQDLEDQEKADHVPTPESSGEHLCFEDQPSFPIQIKDDIFEDSKAREIEVTNATSNNNTQIQKLTGSPFRSREYVQTRESESEHSYPPPGADRLARDTCDSLGKGTALRKPSNISLHSRTMRGLARALPLQPSIERPKKDNELLKASAKFQGQTWALESLEELESMERFQESQIVVVPSGSELEDAKTQGGVEEMTVDRRGSLQEKEDMVSSTQKVPTPSQHWKGTFFSQEAVSPFYYQTGFSAALPHGELSGTQPVHSLSFPRSGLHGSDTKGVSSFEYILEPVMLKTNRNSLATGVGDQDHSGETRSSSPQERASGDVSTTHTPLGGSVMPVVVRASGQAVTSDSTLLNTEDWITVSTSSQEDQEGDFRDTSTGSTTQEALGSEAEATVQKERKNSSLDRISRQAEKRVSFLLQEDSNQGEEERQKAEETSEDQQLPNSAYLTPISELKGPDAEPLLLPDSSINASICLGILAEIRQAKTQRKQLTDLVAEGTVLPYETLQEAEWFSEAAGKPQTQKVKLGWGSTRNDAKAQRLHEASPSAVSADLLADERKAQVSAGSFHHLPNPETDRGPQHHLLASPHIVSELEKRYCTGKPRQFCGASGRSDSSEVIEKRKEASRTKSSVDPLPSDRLLSIPAVEQDGGLGSEKVSVLPSQTSYAPGRILHGQGQLTARETVKGLSFGGKDSILGHQEPRSLDSTHGGGSEKISVTTQKENAVFSECPSVICTVDNAVDLSQSKQDHVQGLDASTGLEETKASPKSGAVHPEAPGNVGAEANIRHPVKWKNVDSGLACGGDSKNPWSTPFLDQRPSLHPSGVREEAPGPCPKECLVFERNTGGSRPLGSSYEEAENRTIPCPHLSGSQPTTAVHACCSHSSTLLCCRDGVLRKGTPWAAAPPDHSLCIVPSTVCEVDGTGECLSRVSLAHDLKHKCGPVDNSIPNPPTTTPVSSPAQNCSCLSTSEMRARCLTHTFARGRSVEGSGEETTGKKVTTAPEDTFPSSPAGMSSEPLRTLKNNSVDENGQASQTMPEPPAVTQGPGTLNSNECVDSKLVIAAQFGHLENTKCCSEKMQPSTKVRGHSCLAPQARFVDMLKPTCHPKIETSWEEEEQQRDQVSGDGKDHAQVRNLVPSNVGGFDGYQTRDGETKSSVPQTFFSDFEAQTEPSQPAAQTHSQHCSDREQLPRSHRHLLPVIAIFSGPKHARYSPRPQFTVVSSSRSLQELNLSVEPPSPTDEDAQRPDSSWRPHLRGYSSEKPISTSLKTQDCSQKALCNLNNSSSNHRPLNPVIPPYPTSSTVSCMPTPEFMTTWMPGALEQAHQGKTDKLSVQGMPENWHSQTDEEMLHFGSSELSPSVLSSCPQGLVHIGWKQYVFGSAVDVSCSQKPQCLIQSNMAQCSSIDNVLEDKKSPFHSHPKTDAQTQDLPNIHSDVENDQSSNELPLVGGSATAQVDEILLLCPPEMGCAGGEASVNTFEQGTQALGSRRHWCCTDVSLQPEARTMSDSELASWTSMHNLSVHLSQLLHSTSELLGSLSHPGVVIKEQNVKRDSLDEAQQALRMDGSASTTVDEGIQTDLALPPLAFQGPEVKSEEVSVILDMMDSGITTVAQEKGDVPVVFQKREAEGAAETPGLHEESTHNKLQSPPLPSPHLRVQKADLGQNFTFMSPPASPDGSPPPSLRPEESCMVVNMPRFSPHSGLSLGAFESTQEPRTQKRLCGSRAVLVDRASSPILTFSASIQELSNPLACVTLSAPSVHPLEDFQKLDDINSDLAVGDPRPPVDNSQATDESGDSQRAESLDREGKSPLGKSSERLLLDNSSSCSPQQSSSLQVSFLGIAPQQLQPKTTTGDQSKLPSPPPRHKNPKLDDSCVSEKVTSVEHGPLRPSQWQGRTTNKDWGSEFMVEPQPNLDQPSSRRGLQPLSPCQISDTTGLQSPAVDPPQACHPVGLLCSGSHMHVAPGPQHYNLRDLPVHNNFNNLYGVQGGPGRGLHEGESLGVRCDSSSVGTHRPPQLSDKYSQNLEWLRLEHIPLQAGVQKLALSVELTEAKLHHGFGETDALLKVLQSGTGEVLAPQEPAVPSSEEFYTRQKKTIETLRRQRAERLHNFRRTRSLSPQKQLGLLPSKDLPTWELDLPSRRQEYLQQLRKHIVDTTRIPEPAPGLARPPSDIELMLQEYRRAREEAKVEIAQARDRLKERTEQEKMRIRQQIISQLLKEEEKLQTLANFSSLYTSSNGSISSGVTSGYNSSPAFSGHLQSLEVSGDSQVPDSQDTWIGDWQDQSTVRNSYLYLTGSSWKSLAHSRRASMGSGCCSASSLSSLGACFSFPYQDLAKHIVSTSMADVMAACSDNLHNLFIRQATDGWNYQGEEQEVQLYYKEFSSTRHGFLGASVVSQPLSQVWAAVSDPTLWPLYHKPIQTARLHQRVTNSISLVYLVCNTTLCELKQLRDFCCVCVEAKEGCLSIMAAQSVYDASMPRPSRKMVRGEILPSAWVLQPVIIEGKEITRVISLVQVELGAPGFPPHLLNSCIKQQPLVVAKLASFLRS', 4561, 'Q80TF6; O35058; Q8C121; Q8CFL0;', 'KD00318', 'Mus musculus (Mouse)', 'Stard9', '#StAR-related lipid transfer protein 9#Kinesin-like protein Kif16a#START domain-containing protein 9#StARD9', '-', '-', '-'),
(319, 'Q5SW96', 'Low density lipoprotein receptor adapter protein 1', 'c;k;m', 33885, 'Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes; but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides; which regulate clathrin bud assembly at the cell surface. {ECO:0000269|PubMed:15728179}.', 'MDALKSAGRALIRSPSLAKQSWGGGGRHRKLPENWTDTRETLLEGMLFSLKYLGMTLVEQPKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCTADKMHDKVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFKVAFEFWQVSKEEKEKRDKASQEGGDVLGARQDCTPSLKSLVATGNLLDLEETAKAPLSTVSANTTNMDEVPRPQALSGSSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDMHYAQCLSPVDWDKPDSSGTEQDDLFSF', 308, 'Q5SW96; A2BHI5; Q6TQS9; Q8N2Y0; Q9UFI9;', 'KD00319', 'Homo sapiens (Human)', 'LDLRAP1', '#Low density lipoprotein receptor adapter protein 1#Autosomal recessive hypercholesterolemia protein', '-', 'ENSG00000157978', '-'),
(320, 'P97477', 'Aurora kinase A', 'GO:0032133===GO:0000780', 44772, 'Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle; centrosome duplication; centrosome separation as well as maturation; chromosomal alignment; spindle assembly checkpoint; and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins; including ARHGEF2; BORA; BRCA1; CDC25B; DLGP5; HDAC6; KIF2A; LATS2; NDEL1; PARD3; PPP1R2; PLK1; RASSF1; TACC3; p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway; and particularly the checkpoint-response pathways critical for oncogenic transformation of cells; by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors; the protein phosphatase type 1 (PP1) isoforms; to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. {ECO:0000269|PubMed:19075002; ECO:0000269|PubMed:19668197; ECO:0000269|PubMed:20643351; ECO:0000269|PubMed:9245792}.', 'MDRCKENCVSRPVKTTVPFGPKRVLVTEQIPSQNLGSASSGQAQRVLCPSNSQRVPSQAQKLGAGQKPAPKQLPAASVPRPVSRLNNPQKNEQPAASGNDSEKEQASLQKTEDTKKRQWTLEDFDIGRPLGKGKFGNVYLARERQSKFILALKVLFKTQLEKANVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSNGELKIADFGWSVHAPSSRRTTMCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGMPPFEAHTYQETYRRISRVEFTFPDFVTEGARDLISRLLKHNASQRLTLAEVLEHPWIKANSSKPPTGHTSKEPTSKSS', 395, 'P97477; O35624; Q8C3H8; Q91YU4;', 'KD00320', 'Mus musculus (Mouse)', 'Aurka', '#Aurora kinase A#2.7.11.1#Aurora 2#Aurora family kinase 1#Aurora/IPL1-related kinase 1#ARK-1#Aurora-related kinase 1#Ipl1- and aurora-related kinase 1#Serine/threonine-protein kinase 6#Serine/threonine-protein kinase Ayk1#Serine/threonine-protein kinase aurora-A', '-', '-', '20878'),
(321, 'O14423', 'CENP-B homolog protein 1', 'GO:0000780', 59865, 'Binds to centromeric K-type repeat DNA and ARS3002 DNA. The CBH-binding consensus sequence is Py-Pu-A-T-A-T-Py-Pu-T-A. {ECO:0000269|PubMed:9237993}.', 'MPPIRQAVSLAEKKAIRDYYNQSAHRIPQKEVTEWFRKTYNKDLSQSTISEILSPKYSYLDDGSVRLGDIKKIRAPKFPLLDNAVYEWLQQREVEGLPISGDMIKQAATRFWSKIPAYASLPLPDFSNGWLDKFRRRHYIQQSAVNQALESIKFEVFREYPVHIQEFIRPYAQKDIFCVGGTSLFWKLTPNKQNLDYQEIQGMKRGKAKVSLIMCCNADGSERLPLWIVGYAQNPRSFEQCGIFPKSMNFEWKWNGRASISPIIMEEWLRWFDTRMQGRKVLLMLESNDTYQFGVESVRRFKGGFQNTSVFRIPEKTLDIKSPFEQGIVDTFKANYRRYWLQYSLNQINILRDPLKAVNVLKAIRWMLWSWNFGVSEKTIQASFLRSGLLGPHSEAEGQGMESYQKAIMEIGNLISSKGSEAVKQINEYIRPSEEDETKLHQDAVDTVAAEFLEERRFESDEEEDVEPQISNVEAAMAFEVLIKYFEQHENGDPSFVLDLYRRQRVIAPNNLIA', 514, 'O14423; O14294;', 'KD00321', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cbh1', '#CENP-B homolog protein 1#CBHP-1', '-', '-', '2543290'),
(322, 'P38283', 'Inner centromere protein-related protein SLI15', 'GO:0000777===GO:0005828===GO:0032133===k', 79186, 'Required for high-fidelity chromosome segregation during the later part of each cell cycle in association with the protein kinase IPL1. Stimulates IPL1 kinase activity and facilitates its association with the mitotic spindle. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. {ECO:0000269|PubMed:10385519; ECO:0000269|PubMed:11724818; ECO:0000269|PubMed:11853667}.', 'MDWAIKAARKKTQRKPGSTRSIIETLDDLNNLTTDAHSEINQRLYESSEWLRNNVYMNTLKYEDKKMEESLISPENTHNKMDVEFPKMKGEYELSNSQNDAAKDVTKTPRNGLHNDKSITPKSLRRKEVTEGMNRFSIHDTNKSPVEPLNSVKVDANESEKSSPWSPYKVEKVLRESSKTSESPINTKRFDNQTWAAKEEMENEPILQALKKAESVKVKPPPNSGIARSQRRSNMFVPLPNKDPLIIQHIPPTKSSGSIPKVRTVKESPIAFKKKSTINSPAIRAVENSDTAGSTKASSVFDRLSSIPTKSFENKISRGNVGHKYSSSSIDLTGSPMKKVSQKFKSINSTDTDMQEALRDIFSVKNKITKNNSPKGKNSRKSSIPRFDKTSLKLTTHKKLAIIAEQKKKSKHSSDVHKTGSRPHSISPTKISVDSSSPSKEVKNYYQSPVRGYLRPTKASISPNKNKNLTTSQTPHRLKIKEKTLRKLSPNIADISKPESRKSKNYRLTNLQLLPPAEAERDDLKKKFDKRLSGIMRSQQEHHRRKQEKQKRMSHLEQDLKKQTSFSNDYKDIRLKESLAPFDNHVRDTINKNTAFSTDNILATINTVDHREIIGNVTPKIASVNDSLPEINTDSEDEASVTLAAWAKSPYLQEQLIRQQDINPQTIFGPIPPLHTDEIFPNPRLNRLKPRQIVPKRS', 698, 'P38283; D6VQF1;', 'KD00322', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SLI15', '#Inner centromere protein-related protein SLI15#INCENP-related protein SLI15', '-', '-', '852453'),
(323, 'Q7TNC6', 'Kinesin-like protein KIF26B', 'GO:0003777', 225511, 'Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds; possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8; which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules. {ECO:0000269|PubMed:20439720; ECO:0000269|PubMed:22768111}.', 'MNSVAGNKERLAVSTRGKKYGVNEMCSPTKPSAPCSPESWYRKAYEESRAGSRPTPEGAGSALGSSGTPSPGSGTSSPSSFTGSPGPASPGIGTSSPGSLGGSPGFGTGSPGSGSGGGSSPGSDRGVWCENCNARLVELKRQALKLLLPGPLPGKDPAFSAVIHDKLQVPNTIRKSWNDRDNRCDICATHLNQLKQEAIQMVLTLEQAAGSEHYDTSLGSPPPISSIPTLVGSRHMGGLQQPREWAFVPAPYATSTYTGLVNKHSGKPNSLGVSNGAEKKSGSPTHQAKVSLQMATSPSNGNILNSVAIQAHQYLDGTWSLSRTNGVTLYPYQISQLMTETGREGLTESALNRYNADKPAASSVPAPQGSCVASETSTGTSVAASFFARAAQKLNLSSKKKKHRPSTPSVAEAPLFATSFSGILQTSPPPAPPCLLRAVNKVKDTPGMGKVKVMLRICSTSARDTSESSSFLKVDPRKKQITLYDPLTCGGQNAFQKRSSQVPPKMFAFDAVFPQDASQAEVCAGTVAEVIQSVVNGADGCVFCFGHAKLGKSYTMIGRDDSMQNLGIIPCAISWLFKLINERKEKTGARFSVRISAVEVWGKEENLRDLLSEVATGSLQDGQSPGVYLCEDPICGTQLQNQSELRAPTAEKAAFFLDAAIASRRSNQQDCDEDDHRNSHMLFTLHIYQYRMEKSGKGGMSGGRSRLHLIDLGSCVKALSKNREGGSGLCLSLSALGNVILALVNGSKHIPYKESKLTMLLRESLGNVNCRTTMIAHISAAASSYAETLSTIQIASRVLRMKKKKTKYTSSSSGGESSCEEGRMRRPTQLRPFHARAPVDPEFPLAPLSSDPDYSSSSEQSCDTVIYIGPNGTALSDKELTDNEGPPDFVPIVPALQKTRGDSRPGEAAEAAASKSERDCLKCNTFAELQERLDCIDGSEEPSKFPFEELPIQFGPEQAGRCAPLSQAVGPDTPSESEKEDNGSDNGQLTEREGTELPASKAQRNRSPAPTVTRSSSPSPASPRSIPGSSSQHSTSQLTQSPSLQSSRESLNSCGFVEGKPRPMGSPRLGIASLSKTSEYKPPSSPSQRCKVYTQKGVLPSSAPPPSLSKDSGMVSSESLLQPDVRTPPVGMSPQVLKKSMSAGSEGFPGTLVDGEDQEGPPADSKKEILSTTMVTVQQPLELNGEDELVFTLVEELTISGVLDSGRPTSIISFNSDCSVQALASGSRPVSIISSISEDLECYSSMAPVSEVSITQFLPLPKLGLDEKARDAGSRRSSISSWLSEMSAGSDGEQSCHSFIAQTCFGHGEAMAEPPASEFVSSIQNTAVVCREKPEVGPDNLLILSEMGEESGNKAAPIKGCKISTVGKAMVTISNTASLSSCEGYIPMKTNITVYPCIAMSPRNVQEPESSTATPKVSPKASQAQESKEPSTRREMKFEDPWLKREEEVKRENAYSSEEGVKCEPLPSSLKTEGKSEQELDGRPSSGNRLSSSSSEAAAFQGTDNVRRVVDGCEMALPGLVAQSPLHVNRNLKSSSLPRAFQKADRHEELDSFYHCLADSNGFSAASGIPSSKTTLERKVASPKHCVLARPKGTPPLPPVRKSSLDQKNRASPQHGGGSSNTSSPLNQPATFLACFPDESNGKTKDVSSSSKLFSAKLEQLASRSNSLGRTTVSHYECLSLERAESLSSVSSRMHAGKDSTMPRTGRSLGRSTGASPPSCGITQSTGASPKASQSKISAVSKLLLASPKSRSSLSTSTTKTLSFSTKSLPQSVGQSSNLPPSGKHMSWSTQSLSRNRGSGLASKLPLRAVNGRISELLQGSAGPRSAQLRAEAEERSGAPSEDKPAAAHLLPSPYSKITPPRKPHRCSSGHGSDNSSVLSGELPPAMGKTALFYHSGGSSGYESMMRDSEATGSASSAQDSMSENSSSVGGRCRSLKNQKKRSNSGSQRRRLIPALSLDTPSPVRKTASSTGVRWVDGPLRSTQRSLGEPFEIKVYEIDDVERLQRRRGATSKEVMCFNAKLKILEHRQQRIAEVRAKYEWLMKELEATKQYLMLDPNKWLREFDLEQVLQLDSLEYLEALEGVTERLESRVNFCKAHLMMITCFDITSRRR', 2112, 'Q7TNC6; D5MP63; E9PXV6; Q0VB48; Q8BHX2; Q8BKH6;', 'KD00323', 'Mus musculus (Mouse)', 'Kif26b', '#Kinesin-like protein KIF26B', '-', '-', '269152'),
(324, 'Q80TG1', 'KAT8 regulatory NSL complex subunit 1', 'GO:0000777', 113179, 'As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. {ECO:0000250}.', 'MAAMAPALTDAAAEAHHIRFKLAPPSSTLSPGSAENNGNANILISANGTKRKAIAAEDPSLDFRNNPTKEDLGKLQPLVASYLCSDVTSVPAKESLKLQGVFSKQTVLKSHPLLSQSYELRAELLGRQPVLEFSLENLRTMNTSGQTALPQAPVNGLAKKLTKSSTHSDHDNSSSLNGGKRSLTSSSLQGGEVGGPDSGNLKGGMTNCTLPHRSLDIQHTTLYSNNSTANKSSVNSMDQPALQGSSRLSPSTDSSSNLTNVKLEVKKSPLSSILFSALDSDTRITALLRRQADIEIRARRLQKRLQVVQAKQVERHLQHQLGGFLETTLSKLPNLESLRSRSQLMLTRKAEAALRKAASESATSEGLSNFLKSDSISEELERFTASGIANLRCSEQAFDSDVTDSSSGGESDIEEEELTRADPEQCHVPLKRRSEWRWAADRAAIVSRWNWLQAHVSDLEYRIRQQTDIYKQIRANKGLIVLGEAPFPDHTTDLLSLSSEVKTDHGRDKLIESVSQPSENHGILVSNITESLSTKSCGAPRPVNGVVNSLQPVLADQVPGDSSDAEEQLHKKQRLNLVSSSDGTCVAARTRPVLTCKKRRLVRPSSIVPLSKKVHRNVRSGCDVNPSCALCGSGSVNTMPPEIHYEAPLLERLSQLDSCVHPVLAFPDDVPTSLHFQSMLKSQWQNKPFDKIKPTKKFSLKHRATMPCSLSDPVRKDRHKLVNSFLTTAMLKHHTDMSSPSYLTATHHPPHSPLVRQLSTSSDTSTPTSSGSQVAASTSQPVRRRRGESSFDINNIVIPMSVAATTRVEKLQYKEILTPSWREVDVQSLKGSPDEENEEIEDLSDAAFAALHAKCEEMERARWLWTTSVPPQRRGSRSYRSSDGRTTPQLGSANPSTPQPASPDVSSSHSLSEFSHGQSPRSPISPELHSAPLTPVARDSLRHLASEDTRCSTPELGLDEQSVQPWERRTFPLAYSPQAECEEQLDAQDTAARCTRRTSGSKTGREAEVAPTSPPVVPLKSRHLAATVTAQRPAHR', 1036, 'Q80TG1; A2A5Y5; Q3TT88; Q3U5D8; Q3V3N3; Q7TMU3; Q80XP7; Q8R3L6;Q9D9G0;', 'KD00324', 'Mus musculus (Mouse)', 'Kansl1', '#KAT8 regulatory NSL complex subunit 1#NSL complex protein NSL1#Non-specific lethal 1 homolog', '-', '-', '76719'),
(325, 'P78972', 'WD repeat-containing protein slp1', 'GO:0000778===k', 53418, 'Required for mad2-dependent spindle checkpoint activation. Promotes ubiquitin-dependent degradation of cdc13 by the anaphase promoting complex/cyclosome (APC/C). {ECO:0000269|PubMed:15791259; ECO:0000269|PubMed:9001228; ECO:0000269|PubMed:9461438}.', 'MEIAGNSSTISPTFSTPTKKRNLVFPNSPITPLHQQALLGRNGRSSKRCSPKSSFIRNSPKIDVVNTDWSIPLCGSPRNKSRPASRSDRFIPSRPNTANAFVNSISSDVPFDYSESVAEACGFDLNTRVLAFKLDAPEAKKPVDLRTQHNRPQRPVVTPAKRRFNTTPERVLDAPGIIDDYYLNLLDWSNLNVVAVALERNVYVWNADSGSVSALAETDESTYVASVKWSHDGSFLSVGLGNGLVDIYDVESQTKLRTMAGHQARVGCLSWNRHVLSSGSRSGAIHHHDVRIANHQIGTLQGHSSEVCGLAWRSDGLQLASGGNDNVVQIWDARSSIPKFTKTNHNAAVKAVAWCPWQSNLLATGGGTMDKQIHFWNAATGARVNTVDAGSQVTSLIWSPHSKEIMSTHGFPDNNLSIWSYSSSGLTKQVDIPAHDTRVLYSALSPDGRILSTAASDENLKFWRVYDGDHVKRPIPITKTPSSSITIR', 488, 'P78972;', 'KD00325', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'slp1', '#WD repeat-containing protein slp1', 'BIOMD0000000111,Novak2001_FissionYeast_CellCycle;BIOMD0000000406,Moriya2011_CellCycle_FissionYeast;', '-', '2543222'),
(326, 'O14417', 'Mitotic spindle checkpoint component mad2', 'GO:0000778===k', 23583, 'Feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. It interacts with the anaphase promoting complex/cyclosome (APC/C) thereby inhibiting APC/C-dependent proteolysis; a step required for exit from mitosis. {ECO:0000269|PubMed:9461438}.', 'MSSVPIRTNFSLKGSSKLVSEFFEYAVNSILFQRGIYPAEDFKVVRKYGLNMLVSVDEEVKTYIRKIVSQLHKWMFAKKIQKLILVITSKCSGEDLERWQFNVEMVDTADQFQNIGNKEDELRVQKEIQALIRQITATVTFLPQLEEQCTFNVLVYADKDSEVPTDWVDSDPRILRDAEQVQLRSFSTSMHKIDCQVAYRVNP', 203, 'O14417;', 'KD00326', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mad2', '#Mitotic spindle checkpoint component mad2', '-', '-', '2540589'),
(327, 'Q4R4S6', 'Nuclear distribution protein nudE-like 1', 'GO:0000777', 38587, 'Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity; the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors; which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL (By similarity). {ECO:0000250}.', 'MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPDPGLGSSRPSSAPGMLPLSV', 347, 'Q4R4S6;', 'KD00327', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'NDEL1', '#Nuclear distribution protein nudE-like 1#Protein Nudel', '-', '-', '-'),
(328, 'Q19555', 'SCC-3', 'k', 124775, '', 'MSETPTDQSPQRMSTRNQARVNYTDMAAGNNSVEKEPVFRSPTASTRGRKKRAANVDVADLSASFGNLNNFSTPPKRGRPRGGGLGSARGGRAPMVRRTTTEESAEVDDRELVAAVKSGKKITEAVDRWIGRYNEKFLVAIAEMHQFFFAICGCKGIVTPQMSATLTYKDIICRMTEDFEEDSADYPLVHGGSLKKVRANLHNFIHTLIIRTKASMLFDSNLMDGFVQLLTGMADSQVRAFRHTATFCAMKITSALVDVTIELTQSKEKTSKQIEAEKAKLKNNSAGNEKYEALVAQRTQTEERAEEIRQIIGYLFRSVFVHRYRDVVPDIRCICIQELGHWMDVYPEHFVEDSYLKYIGWSMFDKVGDVRQRCIRALIPLFEKTLILDKLELFVNKFKDRLVSMLLDKDLETSIETVHLMRVLYTVFPTLLTIKDVVPIYELIYASNRPLAVAAGMFLNTKVFRSAEKPGKAPTAANIPLVKDLTTFFIEGDLHQHATYLVDALFESNPIVKDWATMGELLINDQYQLDSNFETKLIEILTCSVVQSATGEPPVGRHIVKKGAPSAKESRDLVEDRQRLTETLIPLIPRLITKFSSDNEKIINLVNIPLHFQLETYLSARMQTHLMELMEGLDSLIEKHLDEELLKAVAELYYHLTTNSSISALVEGHKMKLLDGVAAFIRKSMQQFDDDQMGEEEEALFVSYIKRMAAFAGFMDLRHWDLWDILLKVVSNYTREDTQRDVRERSMQMLFMQLCFDSMNIKKEGETPKADQVRKLKKRRDQLIRIVTETLNEEACGVEQAYLVICDLMILFGSQLAEESKALEPLIWRPDAMVLGNLKIFLDVNVFDVSNLDDMDQQEKIEVMHKMRQHVAQYAKLIIHGAMPVAEASHLIKRYQSHFQDFGDIFKNLLSKCREISFVETGVMICETLKTLYSQLDEDQGTDPLSESFNSIRDLAKRLGPAFGVDYAKNRFAISSLHKKAIDFAFEEYDKENHQMPKNIFFLEIAIEFSGKLLAQDKMAVVRYLNKIYTNRVGTSTVVWEPYRLYLGSLSDRNDDDNMSVRSGMTVTSNATMRSTASSTRGRGRGRGRSRIADDF', 1096, 'Q19555;', 'KD00328', 'Caenorhabditis elegans', 'scc-3', '#SCC-3 {ECO:0000313|EMBL:CAA99836.1}', '-', '-', '179749'),
(329, 'Q9CY25', 'Protein MIS12 homolog', 'GO:0051382===GO:0000444', 24131, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis. {ECO:0000250}.', 'MSVDPMAYEAQFFGFTPQTCLLRIYVAFQDHLFEVMQAVEQVILKKLEDIPNCEITPVQTRKCTEKFLCFMKGRFDNLFGKMEQLILQSILCIPPNILLPEDKCQETNPFSEEKLELLQQEIKELQEKYKVELCTEQALLAELEEQKTVKAKLRETLTFFDELENIGRYQGTSNFRESLASLVQSCRKLQSIRDNVEKESRRLETQ', 206, 'Q9CY25; Q3V261; Q5QNU7; Q5QNU8; Q5QNU9;', 'KD00329', 'Mus musculus (Mouse)', 'Mis12', '#Protein MIS12 homolog', '-', '-', '67139'),
(330, 'P35978', 'Kinesin heavy chain', 'GO:0003777', 117523, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.', 'MADPAECNIKVVCRVRPMNATEQNTSHICTKFISEEQVQIGGKLNMFDRIFKPNTTQEEVYNKAARQIVKDVLDGYNGTIFAYGQTSSGKTFTMEGVMGNPQYMGIIPRIVQDIFNHIYQMDESLEFHIKVSYFEIYMDRIRDLLDVSKTNLSVHEDKNRVPFVKGATERFASSPEEVMDVIEEGKSNRHIAVTNMNEHSSRSHSIFLIQVKQENMETKKKLSGKLYLVDLAGSEKVSKTGAEGTVLDEAKNINKSLSALGNVISALADGKKSHIPYRDSKMTRILQESLGGNARTTIVICCSPSSFNESESKSTLMFGQRAKTIKNTVTVNMELTAEEWRNRYEKEKEKNGRLKAQLLILENELQRWRAGESVPVKEQGNKNDEILKEMMKPKQMTVHVSEEEKNKWEEEKVKLYEQLDEKDSEIDNQSRLTEKLKQQMLEQEELLSSMQRDYELLQSQMGRLEAENAAAKEEAKEVLQALEEMAVNYDEKSKEVEDKNRMNETLSEEVNEKMTALHTTSTELQKLQELEQHQRRRITEMMASLLKDLGEIGTALGGNAADMKPNVENIEKVDEEFTMARLFVSKMKTEVKTMSQRCKILEASNAENETKIRTSEDELDSCRMTIQQHEAKMKSLSENIRETEGKKRHLEDSLDMLNEEIVKLRAAEEIRLTDQEDKKREEEDKMQSATEMQASMSEQMESHRDAHQKQLANLRTEINEKEHQMEELKDVNQRMTLQHEKLQLDYEKLKIEEAEKAAKLRELSQQFDRREQAKQDLKGLEETVAKELQTLHNLRKLFVSDLQNRVKKALEGGDRDDDSGGSQAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLERRLRATSERVKALEMSLKETKEGAMRDRKRYQQEVDRIREAVRQRNFAKRGSSAQIAKAIRAGHPPPSPGGSTGIRGGGYSGIRGGGSPVIRPPSHGSPEPISHNNSFEKSLNPNDAENMEKKANKRLPKLPPGGNKLTESDIAAMKARSKARNNTPGKAPLTTSGEQGS', 1031, 'P35978;', 'KD00330', 'Strongylocentrotus purpuratus (Purple sea urchin)', '', '#Kinesin heavy chain', '-', '-', '373178'),
(331, 'Q8MNT1', 'KBP-2', 'k', 14285, '', 'MDKAAVDAVMARMAKSTQQKVLEKTDQMIKENSVYELFDDMEQLTRESEELNKQLGREMGYNPVNAKRDVALHLSETAEKMLTEADAEIEKIEKELKAEEDEIARRKQVLKELATIVESQQQKL', 124, 'Q8MNT1;', 'KD00331', 'Caenorhabditis elegans', 'kbp-2', '#KBP-2 {ECO:0000313|EMBL:CCD65761.1}', '-', '-', '266885'),
(332, 'Q6CNJ1', 'Probable kinetochore protein SPC24', 'GO:0000777', 22048, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSRLNDPVELLQQTRSNFIIESDVSNIKEIKSNMRQLTKLMAEKQTHHNELMKQLQSQLQRQQTKVQALKKNFQEQTSQVKRVEDELNIPKLQQDIDKLVQEINQLRDTIQEGIQKVVETQKQLLNDDTDAAHTIDEEPIGKDDKIRVLKLKLFHSLDVALYNDQLLDLRNEARPLSSSSSSHNIWDEL', 189, 'Q6CNJ1;', 'KD00332', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'SPC24', '#Probable kinetochore protein SPC24', '-', '-', '2894210'),
(333, 'A0JN40', 'Kinesin-like protein KIF3C', 'GO:0003777', 89487, 'Microtubule-based anterograde translocator for membranous organelles. {ECO:0000250}.', 'MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAALGELPKTFTFDAVYDASSKQADLYDETVRPLVDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPEQRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLVSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQTRAVGSTHMNEVSSRSHAIFVITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNTTGGTATQPTGGGGGGGGGGGGGERPKEASKINLSLSALGNVIAALSGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKKGMLGKRLRRKSSRRKKAVSAPAGYPEGPVIEAWVAEEEDDNNNNHRPPQPILETALDKNMENYLQEQKERLEEEKAAIQDDRSLVSEEKKKLLEEKEKMLEDLRREQEATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMMLRDEETMELRGTYTSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHDEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWKFQPLVPSGANSSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAVFEMEFSHDQDQDPRALHMERLMRLDSFLERPSTSKVRKSRSWCQSPQRPPPPTAHASLAASAALRPTTVLDHE', 792, 'A0JN40;', 'KD00333', 'Bos taurus (Bovine)', 'KIF3C', '#Kinesin-like protein KIF3C', '-', '-', '777770'),
(334, 'Q9NVF7', 'F-box only protein 28', 'k', 41149, 'Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000250}.', 'MAAAAEERMAEEGGGGQGDGGSSLASGSTQRQPPPPAPQHPQPGSQALPAPALAPDQLPQNNTLVALPIVAIENILSFMSYDEISQLRLVCKRMDLVCQRMLNQGFLKVERYHNLCQKQVKAQLPRRESERRNHSLARHADILAAVETRLSLLNMTFMKYVDSNLCCFIPGKVIDEIYRVLRYVNSTRAPQRAHEVLQELRDISSMAMEYFDEKIVPILKRKLPGSDVSGRLMGSPPVPGPSAALTTMQLFSKQNPSRQEVTKLQQQVKTNGAGVTVLRREISELRTKVQEQQKQLQDQDQKLLEQTQIIGEQNARLAELERKLREVMESAVGNSSGSGQNEESPRKRKKATEAIDSLRKSKRLRNRK', 368, 'Q9NVF7; E9PEM8; O75070;', 'KD00334', 'Homo sapiens (Human)', 'FBXO28', '#F-box only protein 28', '-', 'ENSG00000143756', '-'),
(335, 'Q6FW62', 'Probable kinetochore protein NDC80', 'GO:0000777', 81821, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MPNEQSEASVLSRLNPHRFTTQIPQHPLSQNMQRRRNSVSSAASDSINSLKQSSARAVSNSNGIQKNNKKYMRSTVAGASGILPTYNKSMSFSQNKNLDDNNMRASLPVLERDLNANNFKSANNNPIGFSSFSQPYSGSRDPRPLRDKNFQSAIQQEIFDYLIQNTFEIDTNYPISLKTLKQPTQKSFVTIFKWLYLRLDPGYTFTKSIEYEVYQLLKILQYPYLESINKSQISAVGGSGWPKFLGMLHWLVTINLRLDKCLNTLDQNLLNQQTQDLTTLSKPVENIEDQEVRQEKYELMAERLFIDYITDSYKTFLNLKDDYSDHMNELKAGFERYLHIIKLDVNNIQSKNENMFEKFEISRNRVEKLKVARGKSTALNGDLVKFQKYVDSMKAKSEEWPIKLSKIEDELNEKKENIKLITEEISQIQDSLQRKGLSVEQIENKNEQKLQLEKEIDQIAEKADEFVSLIKSTKVDNEKVFVTFQDSIRQYNDLLLEFLTSRRKLGHDIEIEPLKITLPNEVVVPNSENALTMDKLFPTDHPMPEYYQNMLLSINSDIMKRIETLKTDNQELEREIGMLTEEINSRGSTNESLELKLSDLNLNLKNVRQENRAEILAQSLEIEKLERQITEGNKNIEQKIANAERIVTELLNEKEVLYNEHSKFKSDLNLKIQKLIKEAHSLRFAVKDSTNRLNELIFTESSETDD', 706, 'Q6FW62;', 'KD00335', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '2887182'),
(336, 'B0LSW3', 'Platelet-activating factor acetylhydrolase IB subunit alpha', 'GO:0000776', 46670, 'Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein- mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity; the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis; whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position. {ECO:0000255|HAMAP-Rule:MF_03141}.', 'MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR', 410, 'B0LSW3;', 'KD00336', 'Felis catus (Cat) (Felis silvestris catus)', 'PAFAH1B1', '#Platelet-activating factor acetylhydrolase IB subunit alpha {ECO:0000255|HAMAP-Rule:MF_03141}#Lissencephaly-1 protein {ECO:0000255|HAMAP-Rule:MF_03141}#LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141}#PAF acetylhydrolase 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141}#PAF-AH 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141}#PAF-AH alpha {ECO:0000255|HAMAP-Rule:MF_03141}#PAFAH alpha {ECO:0000255|HAMAP-Rule:MF_03141}', '-', '-', '100135766'),
(337, 'Q758R8', 'DASH complex subunit SPC34', 'GO:0008608===GO:0051987===GO:0042729', 33394, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MSESLSYCLDQIKESADSIATLYFKPPGIFQNALVHNSKTSYAEIITRLIRDADPVDEMSLYMTDKGGKLRRKDGKQGVYDHLTERAATLKRARLLGAPEETPIVHVPKEFYLKQHDIITKKKQRQNRDFLFDEFSKESGGMFEVLIKKFAGDQQVRNLLLALQNGSVITGEDASSRRKTMFVEDFSVELILRLLREIVTQWPLNEHRTKYEHLLQTYHDISDATNKLRAQIADQEHRLQSQDALSEEPDADDDDVAHPTSGVSYLIQQELDEIDALERELEQLRRDSRT', 290, 'Q758R8;', 'KD00337', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'SPC34', '#DASH complex subunit SPC34#Outer kinetochore protein SPC34', '-', '-', '4620717'),
(338, 'Q6CWQ4', 'Spindle assembly checkpoint kinase', 'GO:0000777', 41892, 'Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by selectively detaching kinetochore-microtubule attachments that are not under tension. Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis (By similarity). {ECO:0000250}.', 'MRPSLSRDASDTGRRHSLLQQSKLLSIRLSNAGKRPSLSRGHAHEKDSITSSHHRLSTGPVNNNPRRSLMVKKPNTAHGTRVPILNDHNDKFENMTLQDFEIGKILGKGKFGKVYCVKHRETGLICALKAMEKKEIVQYTIQKQFRREVEIQGSFKHKNLTQLYGFFYDEKRVYLLMEYVYYGELYKFLKNNGPLNETLASYFVYQMANALDYMHSKNILHRDIKPENILIGFNNTIKLTDFGWSVYNEDGQKRKTLCGTIDYLSPELIKSREYNNKVDVWALGVLTYELLVGSPPFEEDTKEMTYRRILRCDLKFPLNVSPQARDLIVRLLQFEPSKRIPLSEVKSHAWIANNRGSWTDL', 361, 'Q6CWQ4;', 'KD00338', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'IPL1', '#Spindle assembly checkpoint kinase#2.7.11.1#Aurora kinase', '-', '-', '2897422'),
(339, 'Q8C1Z7', 'Bardet-Biedl syndrome 4 protein homolog', 'GO:0003777', 58255, 'The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor; which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8; the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex; together with the LTZL1; controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome (By similarity). {ECO:0000250}.', 'MAEVKLGMKTQVPASVESQKPRSKKAPDFPIVEKQNWLIHLHYIRKDYEACKAVIKEQLQETQGLCEYAIYVQALIFRLEGNIQESLELFQTCAVLSPQCADNLKQVARSLFLLGKHKAATEVYNEAAKLNQKDWEICHNLGVCYTYLKQFNKAQDQLHSALQLNKHDLTYIMLGKIHLLQGDLDKAIEIYKKAVEFSPENTELLTTLGLLYLQLGVYQKAFEHLGNALTYDPANYKAILAAGSMMQTHGDFDVALTKYRVVACAIPESPPLWNNIGMCFFGKKKYVAAISCLKRANYLAPFDWKILYNLGLVHLTMQQYASAFHFLSAAINFQPKMGELYMLLAVALTNLEDIENARRAYVEAVRLDKCNPLVNLNYAVLLYNQGEKKSALAQYQEMEKKVNFLKDNSPLEFDSEMVEMAQKLGAALQVGEALVWTKPVKDPKTKHRTNSGSKSATLQQPLGSIQALGQAMSSAAAYRKILSGAVGAQLPKPPSLPLEPEPEPTVEASPTEASEQKKEK', 520, 'Q8C1Z7; Q3UYF0; Q562E1; Q5EBJ7; Q8CA57;', 'KD00339', 'Mus musculus (Mouse)', 'Bbs4', '#Bardet-Biedl syndrome 4 protein homolog', '-', '-', '102774'),
(340, 'Q4R4R6', 'Cell division control protein 42 homolog', 'GO:0051988', 21258, 'Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin; actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration (By similarity). {ECO:0000250}.', 'MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFNNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL', 191, 'Q4R4R6;', 'KD00340', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'CDC42', '#Cell division control protein 42 homolog', '-', '-', '101925934'),
(341, 'Q4FZW5', 'Nucleoporin seh1-A', 'GO:0000777===GO:0051315', 39726, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (By similarity). {ECO:0000250}.', 'MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSENGNWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGVVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNIMGKVQIYEYNENTRKYAKAETLMSVSDPVHDIAFAPNLGRSFHILAVATKDVRIFTMKPLRKELSSSGGVTKFEIHTVAQFDNHNSQVWRVSWNITGTVLASSGDDGTVRLWKANYMDNWKCIGVLKGDGNPVGNSYQGFFGSSVGSAGQSLQNSVNGTPSSGRKHS', 360, 'Q4FZW5;', 'KD00341', 'Xenopus laevis (African clawed frog)', 'seh1l-a', '#Nucleoporin seh1-A#Nup107-160 subcomplex subunit seh1-A', '-', '-', '734650'),
(342, 'Q61771', 'Kinesin-like protein KIF3B', 'GO:0003777', 85288, 'Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro (By similarity). {ECO:0000250}.', 'MSKLKSSESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTSHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGVRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKDALLREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEDGDDKDDYWREQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYTSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKNKIMNRSFFDDEEDHWKLHPITRLENQQMMKRPVSAVGYKRPLSQHARMSMMIRPEPRYRAENIMLLELDMPSRTTRDYEGPAISPKVQAALDAALQDEDEIQVDASSFESTASRKPKARPKSGRKSGSSSSSSGNPASQFYPQSRGLVPK', 747, 'Q61771;', 'KD00342', 'Mus musculus (Mouse)', 'Kif3b', '#Kinesin-like protein KIF3B#Microtubule plus end-directed kinesin motor 3B#Kinesin-like protein KIF3B; N-terminally processed', '-', '-', '16569'),
(343, 'Q9CQ48', 'NudC domain-containing protein 2', 'GO:0000777', 17660, 'May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. {ECO:0000250}.', 'MSAPFEERSGVVPCGTPWGQWYQTLEEVFIEVQVPPGTRAQDIQCGLQSRHVALAVGGREILKGKLFDSTIADEGTWTLEDRKMVRIVLTKTKRDAANCWTSLLESEYAADPWVQDQMQRKLTLERFQKENPGFDFSGAEISGNYTKGGPDFSNLEK', 157, 'Q9CQ48; Q8CD03; Q9CY63; Q9D0V4;', 'KD00343', 'Mus musculus (Mouse)', 'Nudcd2', '#NudC domain-containing protein 2', '-', '-', '52653'),
(344, 'Q8BH74', 'Nuclear pore complex protein Nup107', 'GO:0000777', 106717, 'Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC (By similarity). {ECO:0000250}.', 'MDRSGFGGMSSPVIRDAEVTRTARKHSAHKRVLIQANQEDNFGTATPRSQIIPRTPSSFRQPFVTPSSRSLLRHPDISYILGTEGRSPRHTQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGLYTNTEHHSMTEDVNLSTVMLREDDPGEAASMSMFSDFLHSFLKHSSTTVFDLVEEYENICGSQVNILSKIVSRATPGLQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSSLEEENMFAIAGINASEKMVVETLFQRDSLVRQSQLVVDWLESIAKDEIGEFSDNIEFYAKSVYWENTLHSLKQRQLLSHMGSTRPLVTELDPDAPIRQKLPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLYHDPNVNGGTELEPVEGNPYRRIWKISCWRMAEDELFNKYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIRTSVMTQDDSEELPREYMEANWTLEKVFEELQATDKKRVLEENQEHYHIVQKFLILGDVDGLMDEFSKWLSKSGSSLPGHLLRFMTHLILFLRTLGLQTKEEVSIEVLKTYIQLLISEKHTSLIAFYTCHLPQDLAVAQYALFLEGVTEFEQRHQCLELAKEADLDVATITKTVVENICKKDNGEFSHHDLAPSLDTGTTEEDRLKIDVIDWLVFDPAQRAEALRQGNAIMRKFLALKKHEAAKEVFVKIPQDSIAEIYNQWEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNEWFKHMNSAPQKPTLLSQATFTEKVAYEHREKKYEMDHNIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAEDDPERTHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQS', 926, 'Q8BH74; Q99KH5;', 'KD00344', 'Mus musculus (Mouse)', 'Nup107', '#Nuclear pore complex protein Nup107#107 kDa nucleoporin#Nucleoporin Nup107', '-', '-', '103468'),
(345, 'Q19542', 'Cytoplasmic dynein 2 heavy chain 1', 'GO:0003777', 473818, 'Function as a motor for intraflagellar retrograde transport in chemosensory neurons. Functions in cilia biogenesis. {ECO:0000269|PubMed:10545497}.', 'MSSDSKDQRKTYFLRVASYLLGLNIVEEKLKSTEPLEIFLDSNTNLLVFSRSEQKLELSNKMKSSAPSANVFRVVFYKTQSVPLNNDNFKSVVNVISANGTLNHVFLKSVQNVFGKELTEGNNMQLIAAVNELEESLLATVEMSGGGSLHDEIRSWKGQTGKPANDYNEAFKQLQLLVETMEERSIDELSELVECFEDTCDELWNCGTPYPQNRMKMLIEYGASYLCETITFKIDDSAIWRNDKVADQLRSAIDVCDQMLIIVRLLTAQTWKRNVEHTWEGDAMEMKFLNGFKDRLDEILSLKSLGGQLEELLEERGVREETEKTIETAMRGMAPLAYNPFTEPNWKSRLLVSERSIEGTIDRTLPILKQRLAPANGDSQSIVLSLEKLKSFLCRSNIKEKLQHEREMFLNRLVSMLSQKNQEFNEKSLQVDAKNFQFLTEVAARIVWIRQQTSQMESIRSLSKMMLNNISNYSAFASKLDEFIEKLQYAEKECFDDWCRETVGLIDNKNETINLETTGKIMYLEASNRELNVNYSDRLLRLLKEVRQLISLGFNIPSKIMSCANNGEKYYRFGVILKQIAHFYNTIDQQMIPSQQSLMLEEAIAFEKLVIPRKDASNSASKVTWNDPKQLEEFIVQLQSAEQKLSNRNRRLRNVHMELIEMVEKLMDLNIVKQNNEWKEIILKIRSKMKEEEIVHGAVKNNMKPWLIHWDFQLYKALLIQYEWGIESIQSQLSTISVSLVFADQKIQLRPTIEEIRSKYYKELCRFLRIPDKFRGVQEDENSTKFYAQMIERSMHLLPTVYEKAEQLMMKVETCDAIFVDWLVISQVDLEELIEENLKTAADWESQFKILKGKAREAERLPHELKFECILVSTAGVKSAIEDAIQRLYDALSWTLRHSISTTSQSISTFLSQAIEVLNTVPQSIDEIAEANAKHVIFAENNRRLKEEWKVMEEQLTLLRSVAGTGMEQIDNLEQTWDRFELMLDGHQSMIKDQVEVLKSNVETSVKGMKDEAEKLKARWEQFKPRNDALQGDREEMLKAIQFIKEKRVQWQQLSDGREKIEKECGQFGLEPPKMDIIDEIDEDIKQFEDNWLIYEMFNNELDTMSQEEWIVFRSKTYLFDEFLQKWMEKLKGTGSQTHMSVRLMKDVEHFKEVSSALKFCRGDVLSADHWHEMFRFLGLPRGTTIEKLKFADLLSVSKNIIENTDQLKQLNSRAQGEVAIRDAIQELTLWAAQTEFTLADYKHSNGQNLKIIKEWKESINSLKDSQALLQSLKSSPYYSQFTDKTAVWETRLADLDVFLAQMNEIQRKWIYLEPIFGRGALPSEASRFSRVDSEYRAILNDVSKDARLVSLCSRQSLKKSLEQIVDQLNRCQKALNQFLEQKRTAFPRFYFIGDDDLLEILGQSTNPQVIQTHMKKLFQGINRVQFSSTGETIISMVSSEGETVPLSKAVRIVPQVESWLQELSDEMRRTLKDLTAQAVADAQPSLAKYPSQVLCLAEEVKFSASIENNLNGSSDLNSFKSQLLEKLKAYTNMKVDDKVSDLKLKSLILDLIHHIDVVDQLLTNQAKSINSWTWQRQLRFYLVNGGIVLRQVSSEFEYTYEYQGNYAKLVHTPLTDKCYLTLTQAMYMGLGGNPYGPAGTGKTESVKALAALMGRQVLVFNCDEGIDVTSMGRIFTGIVECGAWGCFDEFNRLDSTVLSAVSMQIQTIQGAIKSRAGSCTFGGKNVQVNPNSAIFVTLNPAGKGYGGRQKMPDNLKQLFRAVVMGKPDNELISSTILYSEGFVDATALARKIVSVFQLSRQMLSKQQHYDWGLRALKVVLGGCGALRRTQTNKNETDLVVQALLLNTLSKLTFSDSERFNSLIDDIFSNVTKEMTKFEELVEPLGVAAQEMGIKLGDKQMEKVFQLYEQMRQRIGVVVVGAAGSGKSTIWKILQRSLILTKKPLKVTQFNPKAVNRSKLLGNMDMDTREWSDGIITMAAREVTKDTSVHHWIVCDGDIDPEWVEALNSVLDDNRLLTMPSGERIQFGSNVNFLFETDSLQFASPATVSRMGMIYISEEDVTPKDIVASWLVKTTEDLHADMPSWIEEHFWRCLKWVRSHKISGITSFAILKNGLTHLKASKTKTQFLVLLFNGFLPTVTPENRQEFAKGVVFQGMSVPDPKNICYDERIDGIMSYTDDVSQNVTKEEVEREDLRPFVQTADTQRYSDIIGSWLQSGNRESFLITGTTGCGKQQLLKHCFQNDPESQLASLYCSAQSSSSHLLQLIQQNCVQASNPTGRVWRPKDRPNMILFLKGINLPAPDKYGTNELLALLQQLLTYQGFFDHNLEWVSIENIQFVGSMNPIGDGAAVSISNRLFSLLRCVSLNTTDSSQLTSIYRTYLTPILEEVGERNSEIIANRMVDIYNKVQSNFRPTDSVVFLFSPRDLTNWVVSLLRHELDQGKLEAVICFEARRIFADRLPTENDKLKFEEILRNVIPISQANETVIFKEKVYVTTGTVVPGESNTGLPLTPINMSDFNQLLAKSINRFAFEIANFNCPLTSQLAFFCACIDRVLTGPGGHLFLPGRPGFGRRDSVRLVAHMHNIQVFSPPVTANFSAKQFDNELKNAITQAVTNNEHVVLILEDHQLRKNIFLQAINSLLASGNVPGLFTQQELDGLVALVSEAANQASFTGALQQFLAHRIRSLVHVVLILEVEANDFKINITENPAILKHCNVIFADRFDRNSLVEIPKIQMESQGITTTDAILTGFNDVLVNLPEHLSIQPIKYRQFVENFFQLLGYKRLTLSVRLERLKGGVSKLNEARDEVAKMQKKAGKKSKLLAEKQAEADEALKAITESMSGAEDQKLSMEQLKAATEKENVRIEEQKAKIDEQLKEVQPLIDEARRAVGSIKSESLSEIRSLRAPPEAVRDILQAVLLFMGILDTSWEAMRKFLSKSGVKDDIMNFDANRITNEIHKKVTALVKQKSNSFEEANAKRASAAAAPLAAWVKANLEYSKILEKIAPLEGEKNKLVKNLKKAEKQMENLSKGLQSVDEVVGELKRKFEVLMKEATQIKVDLDREQDTIRIAGTLVESLSGEFERWKIQIETFGEEQSKMELCSLITSAFITYLGGCSEKDRKSLLKSMCKMFNMPPTFKPLSFASLETEQLNWKTKGLPADQLSLENGSILFTSCHAPLIIDRSGQVSLFLSKFLEKSETFKAAQPDLMTQIELAIRFGKTIIIDDIVEFDSALIPILRKDLSSQGPRQVISFGGKSIDFNPDFKIYFCTRDEKVDIRPNSYVQLNIVNFTTTISALSAQLLDVAIHLEKPELEERSSSLLRDAELKKLELEGLEQLLLQQLASSQGNLLENTALLDSLNKSKESAEIITKSIVESEQLHKELTTQKDIYVPLSLFTSSLFFSFSNLQFHNPMYNYSVNTIMHLFGKTIKSCEDKSSTRVETLARQMQLTVFYHISRGIFRQDRLMFAVAFINATMPKMFQPKEWELFTGVLVDESTDLSALRVQWISPDRLQSLARIRTHLPSLFNNFQIQDDATWNEFSKTLQCENAFPKNVELKMTHFQKVLFIQAVKPERLYNCLMDFVLKTLNIPSINPPAFELKHIFQESESTEPILFILADGADPSQELSEFASSMNVPYHSISMGQGQEIAAYEAIRESASKGEWLCLNNLHLMLQAVPSIFKHLSLTTPHENFRLWLTTEGDARFPSMMLQQSLKITFEPPPGVRNNLLRTYTQIDRSTKNVITCQSIFVLAWLHALLQERRTFIPQGWTKFYEFGASDVRVAKSFVEQLTANKADWEFVRGILKFVIYGGRIENDFDFKVLDSYLNVLFCDEKINGRAGSQLVKGIDLLATTNVQEYIGHISKSVPSVDEPYLFGLPENIKYSWQIVEADRTISSIRTLALGDTKNALSDQSDKISQIVSLWKKLCQSDDLPKRELPTAIRSADPISEVLCLETINALSLIKQLHRSIGHVAKSMKTPSLASPAVQKTIQSLVFQQTPDEWDSMWAGPSDPADYLNVVVKKTRGTLQLFESSKSSSLLSSPIDFSDLFYPNIFLNALRQTTSRQIKIPLDQLILSSAWTPSQLPAKQCVQVQGLLLQGATFDSFLRETTVSSAAYSQAPIVFLAWTSESSSTITGEQIQVPVYSSSERSDLICSVNMPCRGADQWNIAAVALFLR', 4171, 'Q19542;', 'KD00345', 'Caenorhabditis elegans', 'che-3', '#Cytoplasmic dynein 2 heavy chain 1#Abnormal chemotaxis protein 3', '-', '-', '172593'),
(346, 'Q5REP4', 'Kinesin-like protein KIF22', 'GO:0003777', 73365, 'Kinesin family that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA (By similarity). {ECO:0000250}.', 'MAAEGSTQQRRRVMAAASAASTSGAGRCRLSKIGASRRPPPARVRVAVRLRPFVDGTAGASDPPCVRGMDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGAEGRPWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERCFYLDTVSALNFAARSKEVINRPFTNESLQPHVLGPVKLSQKELLGPPEAKRARGPEEEEIGSPEPMAAPASASQKLSPLQKLSSMDPAMLERLLSLDRLLASQGSQGAPLLSTPKRERMVLMKTVEEKDLEIERLKTKQKELEAKMLAQKAEEKENHCPTMLRPLSHRTVTVAKPLKKAVVMPLQLIQEQAASPNAEIHILKNKGRKRKLESLDALEPEEKAEDCWELQISPELLAHGRQKILDLLNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQMESFLKANILGLAAGQRCGPS', 665, 'Q5REP4;', 'KD00346', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'KIF22', '#Kinesin-like protein KIF22', '-', '-', '100189644'),
(347, 'Q9CXS4', 'Centromere protein V', 'GO:0000776===GO:0000777===GO:0034508', 27541, 'Required for distribution of pericentromeric heterochromatin in interphase nuclei and for centromere formation and organization; chromosome alignment and cytokinesis. {ECO:0000250}.', 'MRRTRSAVATGPREQRRSGATGGLSGGESRAQRSRSRTRAGAGGGGGAVGPQPSAKPRPKPPPRAQEAAAEEPPPAVTPAASVSALDLGEQRERWETFQKRQRLSFEGAAKLLLDTFEYQGLVKHTGGCHCGAVRFEVWASADLHIFDCNCSICKKKQNRHFIVPASRFKLLKGAESITTYTFNTHKAQHTFCKRCGVQSFYTPRSNPGGFGIAPHCLDEGTVRSVVTEEFNGSDWERAMKEHKTIKNMSKE', 252, 'Q9CXS4; B2RWK8; B9EK22; Q5SX21; Q6PIA5;', 'KD00347', 'Mus musculus (Mouse)', 'Cenpv', '#Centromere protein V#CENP-V#Proline-rich protein 6', '-', '-', '73139'),
(348, 'Q5BDI8', 'Probable kinetochore protein spc25', 'GO:0000777', 30152, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSSFDPSLSTSGMRPPLASATAPSMADSLPSINFGFEELRSRMAQFTAQFDAFIERGRKQVLEERNQFKIGLAELQEDERMRQRDIEILNLKSQTHEQTLQKEAAEAAEMHAAVSSVTLERDSRLTKRDRLKQQIEETQKAINQKLEAQRSHSRYLDAQARLNVPELEFWQDYLCLRIEGAGREDRLKFVYSHLLEKDWEAEAWFELGTSSRDYEVFHSRPKLDREYLDRELDILNEDRDFGAFLKRMRRLFIEALK', 257, 'Q5BDI8; C8VRN0;', 'KD00348', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'spc25', '#Probable kinetochore protein spc25', '-', '-', '2877167'),
(349, 'Q86VH2', 'Kinesin-like protein KIF27', 'GO:0003777', 160283, 'Plays an essential role in motile ciliogenesis. {ECO:0000250}.', 'MEEIPVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHIASVVEGQKGIIPRAIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLLELETSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEDGSWYSPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDRIDEMEFEIKLLREALQSQQAGVSQTTQINREGSPDTNRIHSLEEQVAQLQGECLGYQCCVEEAFTFLVDLKDTVRLNEKQQHKLQEWFNMIQEVRKAVLTSFRGIGGTASLEEGPQHVTVLQLKRELKKCQCVLAADEVVFNQKELEVKELKNQVQMMVQENKGHAVSLKEAQKVNRLQNEKIIEQQLLVDQLSEELTKLNLSVTSSAKENCGDGPDARIPERRPYTVPFDTHLGHYIYIPSRQDSRKVHTSPPMYSLDRIFAGFRTRSQMLLGHIEEQDKVLHCQFSDNSDDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELVGEAIRRQLAPSEYQEAGDGVLKPEGGGMLSEELKWASRPESMKLSGREREMDSSASSLRTQPNPQKLWEDIPELPPIHSSLAPPSGHMLGNENKTETDDNQFTKSHSRLSSQIQVVGNVGRLHGVTPVKLCRKELRQISALELSLRRSSLGVGIGSMAADSIEVSRKPRDLKT', 1401, 'Q86VH2; B2RTR8; Q5T6W0; Q86VH0; Q86VH1; Q9UF54;', 'KD00349', 'Homo sapiens (Human)', 'KIF27', '#Kinesin-like protein KIF27', '-', 'ENSG00000165115', '-'),
(350, 'Q8BGW5', 'SOSS complex subunit B2', 'k;t', 21749, 'Component of the SOSS complex; a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex; acts as a sensor of single-stranded DNA that binds to single-stranded DNA; in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation; recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways (By similarity). {ECO:0000250}.', 'MHGVNDPPLFIKDIKAGLKNLNVVFIVLEIGRVTKTKDGHEVRSCKVADRTGSITISVWDEIGGLIQTGDIIRLTRGYASMWKGCLTLYTGRGGELQKIGEFCMVYSEVPNFSEPNPDYRGQQNRGVQNEQKDKLSTNTFGPVGNGDQTGPESRGYHLPYGRSNGPGPISPQLPGTPSSQTVRTTISNARDPRRAFKR', 198, 'Q8BGW5; Q8C154; Q8C164;', 'KD00350', 'Mus musculus (Mouse)', 'Nabp1', '#SOSS complex subunit B2#Nucleic acid-binding protein 1#Oligonucleotide/oligosaccharide-binding fold-containing protein 2A#Sensor of single-strand DNA complex subunit B2#Sensor of ssDNA subunit B2#SOSS-B2#Single-stranded DNA-binding protein 2', '-', '-', '109019'),
(351, 'Q5XGL1', 'Centromere protein K', 'GO:0000777', 31888, 'Probable component of a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. {ECO:0000250}.', 'MSGYQHELPPNISKTSPAPEEAREELLQQCEAIWKQMEECQSKLTMSGPETLPETDVQLYLLMMQVKALTAEYEQWQKRTPEIISDNQDVLLAVGKEELEKIAQELEMVLSSVQAKNKKLKKDLEKEQNWLDGQQKIVDALTSRQDELKNQLTAFSEKRVYQDIAGKLYKVRAHKEELLSALGDFLEEHFPLPQEQENQSKKKKGQSGKKSVQLMTLHEILEILINKLMTTPHDPYLVLEPHHWPPYIEMLLRYGIALRHPEDPKRIRLEAFHQ', 274, 'Q5XGL1;', 'KD00351', 'Xenopus laevis (African clawed frog)', 'cenpk', '#Centromere protein K#CENP-K', '-', '-', '495196');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(352, 'P06493', 'Cyclin-dependent kinase 1', 'GO:0034501', 34095, 'Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition; and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin; APC; AMPH; APC; BARD1; Bcl- xL/BCL2L1; BRCA2; CALD1; CASP8; CDC7; CDC20; CDC25A; CDC25C; CC2D1A; CSNK2 proteins/CKII; FZR1/CDH1; CDK7; CEBPB; CHAMP1; DMD/dystrophin; EEF1 proteins/EF-1; EZH2; KIF11/EG5; EGFR; FANCG; FOS; GFAP; GOLGA2/GM130; GRASP1; UBE2A/hHR6A; HIST1H1 proteins/histone H1; HMGA1; HIVEP3/KRC; LMNA; LMNB; LMNC; LBR; LATS1; MAP1B; MAP4; MARCKS; MCM2; MCM4; MKLP1; MYB; NEFH; NFIC; NPC/nuclear pore complex; PITPNM1/NIR2; NPM1; NCL; NUCKS1; NPM1/numatrin; ORC1; PRKAR2A; EEF1E1/p18; EIF3F/p47; p53/TP53; NONO/p54NRB; PAPOLA; PLEC/plectin; RB1; UL40/R2; RAB4A; RAP1GAP; RCC1; RPS6KB1/S6K1; KHDRBS1/SAM68; ESPL1; SKI; BIRC5/survivin; STIP1; TEX14; beta-tubulins; MAPT/TAU; NEDD1; VIM/vimentin; TK1; FOXO1; RUNX1/AML1; SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis; CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation; Golgi dynamics; nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate; CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation; chromosome decondensation; reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C- mediated dephosphorylation and restoring cell cycle progression. In proliferating cells; CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity; leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome; an important step for spindle formation. In addition; CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl- xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast; CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines; as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. {ECO:0000269|PubMed:16371510; ECO:0000269|PubMed:16407259; ECO:0000269|PubMed:16933150; ECO:0000269|PubMed:17459720; ECO:0000269|PubMed:18356527; ECO:0000269|PubMed:18480403; ECO:0000269|PubMed:19509060; ECO:0000269|PubMed:19917720; ECO:0000269|PubMed:20171170; ECO:0000269|PubMed:20360007; ECO:0000269|PubMed:20395957; ECO:0000269|PubMed:20935635; ECO:0000269|PubMed:20937773; ECO:0000269|PubMed:21063390}.', 'MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM', 297, 'P06493; A8K7C4; C9J497; O60764;', 'KD00352', 'Homo sapiens (Human)', 'CDK1', '#Cyclin-dependent kinase 1#CDK1#2.7.11.22#2.7.11.23#Cell division control protein 2 homolog#Cell division protein kinase 1#p34 protein kinase', 'BIOMD0000000109,Haberichter2007_cellcycle;BIOMD0000000196,Srividhya2006_CellCycle;BIOMD0000000207,Romond1999_CellCycle;', 'ENSG00000170312', '-'),
(353, 'Q9D1P2', 'Histone acetyltransferase KAT8', 'GO:0000776', 52574, 'Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at ''Lys-120''. {ECO:0000250|UniProtKB:Q9H7Z6}.', 'MAAQGATAAVAATTSGTVGEGEPGPGENAAVEGPARSPGRVSPPTPARGEPEVTVEIGETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKFEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPKHKQVKLSKK', 458, 'Q9D1P2; Q3UIY0; Q8BJ69; Q8BJ76; Q8CI73;', 'KD00353', 'Mus musculus (Mouse)', 'Kat8', '#Histone acetyltransferase KAT8#2.3.1.48 {ECO:0000250|UniProtKB:Q9H7Z6}#Lysine acetyltransferase 8#MOZ; YBF2/SAS3; SAS2 and TIP60 protein 1#MYST-1', '-', '-', '67773'),
(354, 'G5EDD8', 'SKR-2', 'k', 19595, '', 'MADQKEASEAAKNREIKISSSDDEIFLVPRNVIRLSNTLNTLLVDLGLDDDEGTNAEPIPVQNVTASILKKVINWCTKHQSDPIPTEDSEKKTDGSIQDWDKKFLDIDQGTLFELILAANYLDIKGLLDVACQSVANMIKGKSPDEIRRAFNIKDDFTAEEREQIRKENAWCDD', 174, 'G5EDD8;', 'KD00354', 'Caenorhabditis elegans', 'skr-2', '#SKR-2 {ECO:0000313|EMBL:CAB03108.1}', '-', '-', '172773'),
(355, 'P36131', 'DASH complex subunit SPC34', 'GO:0008608===GO:0051987===GO:0042729===SCL===c;k', 34078, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A; and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally; thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids. {ECO:0000269|PubMed:15664196; ECO:0000269|PubMed:16415853; ECO:0000269|PubMed:16777964}.', 'MGESLDRCIDDINRAVDSMSTLYFKPPGIFHNAILQGASNKASIRKDITRLIKDCNHDEAYLLFKVNPEKQSVSRRDGKEGVFDYVIKRDTDMKRNRRLGRPGEKPIIHVPKEVYLNKDRLDLNNKRRRTATTSGGGLNGFIFDTDLIGSSVISNSSSGTFKALSAVFKDDPQIQRLLYALENGSVLMEEESNNQRRKTIFVEDFPTDLILKVMAEVTDLWPLTEFKQDYDQLYHNYEQLSSKLRFIKKEVLLQDDRLKTMSQYHPSSSHDVAKIIRKEKDEIRRLEMEIANLQE', 295, 'P36131; D6VXA0;', 'KD00355', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SPC34', '#DASH complex subunit SPC34#34 kDa spindle pole component protein#Outer kinetochore protein SPC34', '-', '-', '853909'),
(356, 'Q7L2Z9', 'Centromere protein Q', 'k', 30595, 'Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:16622420}.', 'MSGKANASKKNAQQLKRNPKRKKDNEEVVLSENKVRNTVKKNKNHLKDLSSEGQTKHTNLKHGKTAASKRKTWQPLSKSTRDHLQTMMESVIMTILSNSIKEKEEIQYHLNFLKKRLLQQCETLKVPPKKMEDLTNVSSLLNMERARDKANEEGLALLQEEIDKMVETTELMTGNIQSLKNKIQILASEVEEEEERVKQMHQINSSGVLSLPELSQKTLKAPTLQKEILALIPNQNALLKDLDILHNSSQMKSMSTFIEEAYKKLDAS', 268, 'Q7L2Z9; A8KAF1; Q6IN61; Q9NVS5;', 'KD00356', 'Homo sapiens (Human)', 'CENPQ', '#Centromere protein Q#CENP-Q', '-', 'ENSG00000031691', '-'),
(357, 'Q8JGT8', 'Spindle checkpoint protein BubR1', 'k', 117622, '', 'MAQAGDEWELSKENVQPLRQGRVMSTLQEVLSQQESASHTAVQQQKQAFELELRFYAGDDPLDVWDRYIKWAEQAFPQGGKESNLCPLLERGVKIFHEEQRYYDDLRYLNICLKFANFCSEPLDLYSYLHSQGIGVSHSLLYITWAEQFEARGNFKKADSMFQQGMQCKAEPLEKLEIHHRQFQARVSRQVLQGISEGPDVEEPELSEPQRSSLADLKSRGKTKAKVPVNRVGDSIKSRPQGLGLQAAPPQQIPNRSRFSVFDENAAMSAAQELPSLTPQQWTAPPPARSKENEQRARPWNSGRPSRNGHQAPVSELPQSLPSFTPYVDEGAQHQTVTPCKINPAVTSVLSSRKPGKDEDPLQRVQNNSQGKEETVMYCKDKVYAGVEEFSLEEIRAEIYMAKVRRKREDDLQASALRRQDMERQIEEMERQLKGSCIGSKETVIEQPAHNVEPIITPCNSKTSESICAPQQEPGMEFPLCFEMADAAPTLPRMGILPVSDVLGNNHNSSGLSPALSCDMPFTIFDESSEALPSMSVPKTIAAPVRRPLAVVSKTKSESQLTDTLDGIEHLNEEAIVCGSGKNKSLFPDPEDTCDFVRAAHLASTPFHRARDESEESLQRNSAERLPLQEKTPVCEESYRQELCIKKLSPILEASQEDTRTSVSSVSSISSTTSMFTSKTLPLSEKLELATQITGVYESEPTTEELPQAEEIAELHRQLLELLPELLVSPEIQHEVGTMPDLKEQEELVLGCETYSLKNEVILHPNSKLFMGAPVDWDMEEMKAFALKVDYQPVPWDLYVTLQLKERLGDLFETFFMEQTNCFLYQNGCISLYKDINRFSIQEILLDSEELIKEVIVLVTYNLLSLVEKLHSVEIVHGDLRPETLLLDDKIFDLSSSLELEGLFKMVDFSHSMDLKLCPTMSSLRGFPIAQSESGQQFLNPQSSPYQVDILGIADLVHLMIFRKPLQLNQENSVWTICKEVPRLRGGNLWNQFFTKILNAEGPSTCVLRELKGEMMELFDSGFQDKLCNYFIQLEMRLNPL', 1041, 'Q8JGT8;', 'KD00357', 'Xenopus laevis (African clawed frog)', 'bub1b', '#Spindle checkpoint protein BubR1 {ECO:0000313|EMBL:AAM23315.1}', '-', '-', '378923'),
(358, 'Q96AC6', 'Kinesin-like protein KIFC2', 'GO:0003777', 90147, 'May play a role in microtubule-dependent retrograde axonal transport. May function as the motor for the transport of multivesicular body (MVB)-like organelles in dendrites (By similarity). {ECO:0000250}.', 'MYAFYSLLIYIFYSLFRRDGGAAAAAEPGDPAQRARKPRGRRRPDLPAPELWTELTGLAASSEPEDGSEGAAEGRAAAVSLEEALLRLAEFLSVQLGAEESCGGPADLGQSGEVPSLLTVTSQLLALLAWLRSPRGRQALLQGTQPAPRVRPPSPDGSTSQEESPSHFTAVPGEPLGDETQGQQPLQLEEDQRAWQRLEQLILGQLEELKQQLEQQEEELGRLRLGVGATDSEKRVQHLTLENEALKQSLSLMRDLLLHWGPGPPIRAPQEEAEALLELQGRLQEAQDTTEALRAQLGVQEVQLQGLQGALQQLQQETEQNCRRELQQMHGQLAGLRARMASLRQGCGDLRGLVSTFTQSCQGSLSEARGQVSWALGALSSGGPGTQLPEGQQGPPAGCPGRLPELKGNIRVLCRLRPGTSSSLVSVEPGPGGTVTTCYRGRHRRFRLDWVFPPDASQEEVFRELEPAVLSCLRGYSVCIFTYGQTGTGKTYSMEGPPEDPGIVPRALQSLFREMGAGRQHRVTLSMVEIYNEAVRDLLAPGPPERLAVRQGPEGQGGIQVAGLTHWDVPNLETLHQMLKLGRSNRATAATAMNQRSSRSHALVTLTLRAASPPRAPGTAGTLHLVDLAGSERARKAGAAGPPRGDPDGARRLREAQTINRSLLALGGVMAALRAHRPHVPFRDSQLTRLLQPALGPGTTAVLLLQVGAGAGQVCACRSPPTRARPPAPLARRSPRGRRISGRQSAPSSSPTEWVKWSWGQPGAAGSRAPPGRLLPSAPTLRSPGPPAPLRRPLAVLHAPVPTTARARLSRPQRACPSSPGSRPCPWGLRPGLCWQRR', 838, 'Q96AC6; E9PHB2; Q96NN6;', 'KD00358', 'Homo sapiens (Human)', 'KIFC2', '#Kinesin-like protein KIFC2', '-', 'ENSG00000167702', '-'),
(359, 'Q6PCJ1', 'Dynactin subunit 1', 'k', 137285, 'Required for the cytoplasmic dynein-driven retrograde movement of vesicles and organelles along microtubules. Dynein- dynactin interaction is a key component of the mechanism of axonal transport of vesicles and organelles (By similarity). {ECO:0000250}.', 'MSVEATGKPLKVGSRVEVIGKGYRGTVAYVGATLFATGKWVGVILDDSKGKNDGTVQGRRYFTCEENHGIFVRQSQIQVIEDGADTTSPETPEPTASKGLKKDVMETPKSSKLPTRPSSSAASSGTASASCGEISSSEPSTPAQTPLAAPIIPSPSSAITSPVAPLPGPGPSKEEENLRAQVKDLEEKLETLKMKRAEDKAKLKEMEKSKLQLEQVQEWKSKMQEQQADIQRQLKEAKKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVDTLKDKVEEHKIDLEILKHEIEEKGSDGAASSYQVKQLEEQNARLKEALVRMRDLSASEKQEHIKVQKQMEKKNTELDTLRQQKEKLQEEASHMEKTIDELKEQVDAALGAEEMVETLAERNLDLEEKVRELRETVSDLEAINEMNDELQENARETELELREQLDMAGARVREAEKRVEAAQETVADYQQTIKKYRDLTAHLQEVNSELRNQQEASVEKEQQPSPEMFDFKIKFAETKAHAKAIEMELRKMEVTQANRHVSLLTSFMPDSFLRHGGDHDCILVLLLIPRLICKAELISKQAQEKFELSEVGEQKSGMRGAVGEQMSFAAGLVYSLTLLQATLHKYEQALDKCSVEVYKKVGMLYPEMSVHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLADQAEECTMQLSDHIKFTQSALDCMGVEVSRLRAFLHAGQESSDFAILLKDLETSCSDIRQFCKKIRRRMPGTEAAGIPAALGFGQQVCETLLDCRKYLKCVVAVFQEVAAAGAQMIAPMGENEGLQALKLEDVAFKATEQIYGTKGSNPYECLRQSCSVVIATMNKMATAMQEGEYDAEKPQSKSPPPVEQRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSASKEADDRVEKIQTKLEETQTVLKKKEKEFEETMDALQADIDQLESEKAELRQRLNNQSKRTIEGLRGVPASGVASIVSGLAGGVSSGQSLINGSGPVQVKDSPLLLQQIDALRLSMKHLKHENNKLKAHQIKTDLSSLPALHVPKLTLPKDRQKEEAMSGTLYRKTSQLLDALQQMSANAKVVDITHKKAGNPAAQLLEQTARLKSLSDTIDKLKNEVMKETVSQCPGANVPTDFATFPSTDFIKAKEEKKEDTVYIGKVTLSCQPGQGQIHKLVLTPEQLHELHERLIC', 1232, 'Q6PCJ1;', 'KD00359', 'Xenopus laevis (African clawed frog)', 'dctn1', '#Dynactin subunit 1', '-', '-', '379696'),
(360, 'Q3URR0', 'Centromere protein W', 'GO:0000776===GO:0000777===GO:0051382', 9734, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPW has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis (By similarity). {ECO:0000250}.', 'MAPSTTVTRRVKRKAPRAFLKRTLKQKKPHLGLGRCCDLLIHLNCLLFIQRLAEESRTNACESKSRVIKKDHVLAAGKVILKKSRG', 86, 'Q3URR0;', 'KD00360', 'Mus musculus (Mouse)', 'Cenpw', '#Centromere protein W#CENP-W#Cancer-up-regulated gene 2 protein', '-', '-', '66311'),
(361, 'G2TRL2', 'Histone-fold domain-containing protein new1', 'GO:0000776', 8640, '', 'MSYPKARIRRFFRQHCQRSLESSALDLVYLDYCLFLQSLLKEANIEAAKTGERRVQPEHVRSIQRKILAQFKG', 73, 'G2TRL2;', 'KD00361', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'new1', '#Histone-fold domain-containing protein new1', '-', '-', '14218186'),
(362, 'Q06675', 'Central kinetochore subunit MCM21', 'GO:0000778===GO:0000817===GO:0034508===k', 42971, 'Component of the central kinetochore; which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle- microtubule attachments and proper chromosome segregation. {ECO:0000269|PubMed:9987135}.', 'MSRIDDLQQDIESLLSEINSLEESREKLKAKIKDKRKNEESANPIVQEFEDLFDQFPQLNNFLFNEHPELEETDDKDISRAQADIPATPIPYEPKKRAKLENEEILPEQEWVLKTQPMVQHQMFDPGVADLLDTDILTSPSKRKRKLKIDDISTSDRSELEDYIVLENVYRMFGITFFPLVDPIDLKIKDASGEIFVDREMLGIRLEVFSERTSQFEKPHYVLLKKRIKSNSWFLFKHTIPSFIDVQGIFDDTNGGLVISHDDAYLFAKRVFLQLVEVQKRRQIFKDLEAKKIIHDLDLDLESSMVSFFVKDIKVELFVKQNEIVSCSILDDIHDFSQNNKSKWEIALLGSLDDLELKLNHSFATIFK', 368, 'Q06675; D6VSU9;', 'KD00362', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MCM21', '#Central kinetochore subunit MCM21#Chromosome transmission fidelity protein 5#Minichromosome maintenance protein 21', '-', '-', '851916'),
(363, 'Q91XQ0', 'Dynein heavy chain 8; axonemal', 'GO:0003777', 541238, 'Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly. {ECO:0000269|PubMed:10602986; ECO:0000269|PubMed:12297094}.', 'MESEEGNAEPPPPSEEAPPPVVEEAPPPLPPEDTAPPPPEEQAPPPEGDAAPPPTGDAFQLTVEGEAPHPEDPKLLSEQGPATSVTDYRSLIPSDEEVTLPEDEESGQARVRARHTPRPAQSVLSDGISQSSRRPSKFRRSMTGIPNLQETLKEKQARFREARENRKMKIGPSHKYIFEVLGEKLGLDLVTVEELILDCPSLDPFTSFFEKGGCKTLKFLYQEGEVPGFECGRTITGVPKGGKMMRIYVDNAAPDKLKGLCLFFVRCRNDVAINSKTIHEDVLFSFLDASKGLLEGIKHMLKSIFLPAILATSNWGALNQSKQGESEKHIFIETIHRYLASLDDATISIEGTVMLKKVDNIDFSKLHTFEEVTAAASSSEMVHQLEEVLMVWYKQIEQVLIESEQMRKEADDSGPLTELEHWKRMSAKFNFIIEQIKGSNCKAVINVLNVAHSKLLKNWRDLDARITDSANESKDNVRYLYTLEKVCQPLYNYDLVSMAHGIQNLINAIRMIHSVSRYYNTSERMTSLFIKVTNQMVTACKAYITDGGTNHVWDQETPAVLKKIQDCIFLFKEYQASFHKTRKQILESSGEKSFEVSEMYIFGKFEAFCKRLEKITEMITIVQTYSALSNSTIEGIDILGIKFKNIYQGIKKNQYDILDPRRTEFDTDFTEFMGKINILEIQIQAFMNSTFGKILSSQQALQLLQRFQKLNIPCLHLEINHTIERILQCYVAELEFTKKLYLSQKDDPPLARNMPPIAGKILWVRQLFRRINEPINYFFKNSDILSSTEGKAVIRQYNRIAYVLVEFEVAYHTAWFKEVSQLQYALQATLFVRHPETGKLLVNFDPKILEVVRETKCMIKMKLDVPEQAKNLLKLESKLKADKLYLQGLLQYYDDLCQEVPSVFVNLMTPKMKKVESVLRQGLTVLTWSSLMLESFFKEVESVLDMFNQLLKKVNDLCEMHIDTVLKEIAKTLLISLSDSGTTKVEDMLTLNETYTKECADILNHKSRHVEEAVKELILIFEQIYEVKYTGKAAKSVKEQRKRVVFGSEAEETEGLDFESTTMEVDTNDKEDEFKKECKEVYAFFSHQLLDSLQKATRLSLDTMKRRIFVGSQGRRRSEDIVSFIKTEVHLAIPNVVMVPSLDDIQQAINRMIQLTLEVSRGVAHWGQQQVRQIKSFQNNSRGSDQPPASGKPLKKEERSFEETIPARKLKNFYPGVAEHKDISKLVLLLSSSVNSLRKAATEALQDFQKYKTLWIEDRHVKVKEFLANNPSLTEIRSEILHYATLEQEIKELKPIIVVGSLELHTEPMKLALSIEAKAWKMLLCRYLNEEYKKKMSDMITFINEYLKKLSRPIRDLDDVRFAMEALSCIRDNEIQMDMTLGPIEEAYGILNRFEVKVTKEESEGVDTLRYSFNKLQSKAVSVQGELVKVQPKFKSNLLESVKVFCEDVINFTEAYETEGPMVPNIPPQEASNRLQIFQANFDDLWRKFVTYSSGEQLFGLPVTDYEVLHKTRKELNLLQKLYGLYDTVMGSISGYYEILWGDVDIEKINAELQEFQNRCRKLPRALKDWQAFLDLKKRIDDFSESCPLLEMMTNKAMKQRHWDRISELTGTPFDVESDTFCLRNIMEAPLLKNKDDIEDICISAIKEKDIEAKLTQVIENWTYQNLSFAAFKGKGELLLKGTESGEIITLMEDSLMVLGSLLSNRYNTPFKKNIQNWVFKLSTSSDIIEEWLIVQNLWVYLEAVFVGGDIAKQLPQEAKRFQNIDKSWIKIMQRAHENPNVISCCVGDETMGQLLPHLHEQLEVCQKSLTGYLEKKRLLFPRFFFVSDPVLLEILGQASDSHTIQPHLPAVSDNINEVTFHAKDYDRMTAVISREGEKIMLDTPVMAKGPVEIWLLDLLKVQMSSLHNIIRSAFYQISDSGFLLLPFLNHFPAQVGLLGIQMLWTHDSEEALNNAKDDRKIMQITNQKFLDILNTLISQTTHDLTKFDRVKFETLITIHVHQRDIFDDLVKMHIKSVTDFEWLKQSRFYFKEDLDQTVVSITDVDFIYQNEFLGCTDRLVITPLTDRCYITLAQALGMNMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDEFNRIELPVLSVAAQQIYIVLTARKERKKQFIFSDGDCVDLNPEFGIFLTMNPGYAGRQELPENLKIQFRTVAMMVPDRQIIMRVKLASCGFLENVILAQKFYVLYKLCEEQLTKQVHYDFGLRNILSVLRTLGSQKRARPEDSELSTVMRGLRDMNLSKLVDEDEPLFLSLINDLFPGLQLDSSTYAELQSAVDNQVNLEGLINHPPWNLKLVQLYETSLVRHGLMTLGPSGSGKTTVITILMKSLTECGRPHREMRMNPKAITAPQMFGRLDTATNDWTDGIFSTLWRKTLKAKKGENIFLILDGPVDAIWIENLNSVLDDNKTLTLANGDRIPMAPTCKLLFEVHNIENASPATVSRMGMVYISSSALSWRPILQAWLKKRSQQEASVFLSLYDKVFEDAYTYMKLSLNPKMQLLECNYIMQSLNLLEGLIPSKEEGGVSSGDHLHKLFVFGLMWSLGALLELDSREKLEVFLRGHGSKLNLPEIPKGSQQTMYEFYVTDYGDWEHWNKRIQPYFYPTDSIPEYSSILVPNVDNIRTNFLIDTIAKQHKAVLLTGEQGTAKTVMVKAYLKKYDPEVQLSKSLNFSSATEPMMFQRTIESYVDKRMGSTYGPPGGRKMTVFIDDINMPVINEWGDQITNEIVRQMMEMEGMYSLDKPGDFTTIVDVQLIAAMIHPGGGRNDIPQRLKRQFTVFNCTLPSNTSIDKIFGIIGCGYFDPCRKFRPEICDMVGNLVSVSRVLWQWTKVKMLPTPSKFHYIFNLRDLSRIWQGMLTVKAEECSSIPILLSLFKHECNRVIADRFITPDDEQWFNSQLIRAVEENISPEVAANILPEPYFVDFLRDMPEPTGDEPEDTMFEVPKIYELVPSFEFLSEKLQFYQRQFNEIIRGTSLDLVFFKDAMTHLVKISRIIRTSCGNALLVGVGGSGKQSLSKLASFIAGYQIFQITLTRSYNVSNLIEDLKNLYKVAGAEGKGITFIFTDNEIKDEAFLEYLNNLLSSGEISNLFARDEMDEITQGLISVMKRELPRHPPTFDNLYEYFITRSRKNLHVVLCFSPVGEKFRARSLKFPGLISGCTMDWFSRWPKEALIAVASYFLLDYNIVCSIETKRHVVETMGLFHDMVSESCENYFQRYRRRAHVTPKSYLSFINGYKSIYTDKVKYINEQAERMNIGLDKLMEASESVAKLSQDLAVKEKELAVASIKADEVLAEVTVSAQASAKVKNEVQEVKDKAQKIVDEIDSEKVKAETKLEAAKPALEEAEAALNTIKPNDIATVRKLAKPPHLIMRIMDCVLLLFQKKIDPVTMDPEKPCCKPSWGESLKLMSATGFLFSLQQFPKDTINEETVELLQPYFNMDDYTFESAKKVCGNVAGLLSWTLAMVIFYGINREVLPLKANLAKQEGRLAVANVELGKAQALLDEKQAELDKVQAKFDAAMKEKMDLLNDADMCRKKMQAASTLIDGLSGEKVRWTQQSKEFKTQINRLVGDVLLCTGFLSYLGPFNQIFRNYLLKDQWELELKARKIPFTENLNLIAMLVDPPTIGEWGLQGLPGDDLSIQNGIIVTKATRYPLLIDPQTQGKTWIKSKEKENDLQVTSLNHKYFRTHLEDSLSLGRPLLIEDIREELDPALDNVLEKNFIKSGTAFKVKVGDKECDIMDTFKLYITTKLPNPAFTPEINAKTSVIDFTVTMKGLENQLLRRVILTEKQELESERVKLLEDVTFNKRKMKELEDNLLYKLSATKGSLVDDESLIGVLRITKQTAAEVSEKLHVAAETEIKINTAQEEFRPAATRGSILYFLITEMSMVNIMYQTSLAQFLKLFDQSMARSEKSPLPQKRITNIIEYLTYEVFTYSVRGLYENHKFLFVLLMTLKIDLQRGTVKHKEFQALIKGGAALDLKACPPKPFRWILDMTWLNLVELSKLPQFAEIMNQISRNEKGWKNWFDKDAPEEEIIPDGYNDSLDTCRKLLLIRSWCPDRTVFQARKYIADSLEEKYTEPVILNLEKTWEESDTHTPLICFLSMGSDPTIQIDALAKKLKLECRTISMGQGQEVHARKLIQLSMQQGGWVLLQNCHLGLEFMEELLEMLMVTETTEDSFRVWITTEPHDRFPITLLQTSIKFTNEPPQGVRAGLKRTFAGINQDLLDISNLPMWKPMLYTVAFLHSTVQERRKFGPLGWNIPYEFNSADFSASVQFIQNHLDECDIKKGVSWSTVRYMIGEVQYGGRVTDDFDKRLLNCFARVWFSEKMFEPSFCFYTGYKIPICKTLDQYFEFIQSLPSLDNPEVFGLHPNADITYQSNTASDVLETITNIQPKESGGGVGETREAIVYRLSEDMLSKLPPNYVPHEVKARLMKMGHLNSMNIFLRQEIDRMQKVISILRSSLSDLKLAIEGTIIMSENLRDALDNMYDARIPQLWKRVSWDSSTLGFWFTELLERNAQFSTWIFEGRPNVFWMTGFFNPQGFLTAMRQEVTRAHKGWALDTVTIHNEVLRQTKEEIITPPAEGVYIYGLYMDGASWDRRNGKLTESTPKVLFTQLPVLHIFAINSTAPKDPKLYVCPIYKKPRRTDLTFITVVYLRTVLSPDHWILRGVALLCDIK', 4731, 'Q91XQ0; E9Q010; O08830; Q3V0D2; Q91V63; Q91XP8; Q91XP9; Q99MH8;Q9QY72;', 'KD00363', 'Mus musculus (Mouse)', 'Dnah8', '#Dynein heavy chain 8; axonemal#Axonemal beta dynein heavy chain 8#Ciliary dynein heavy chain 8', '-', '-', '13417'),
(364, 'Q9GSX9', 'Synembryn', 'GO:0005828===GO:0005818', 63447, 'Guanine nucleotide exchange factor (GEF); which can activate some; but not all; G-alpha proteins independently of G- protein coupled receptors. Acts by exchanging bound GDP for free GTP. Able to facilitate synaptic transmission in the nervous system probably by activating G(q)-alpha (egl-30). Also able to activate the G(s)-alpha in synaptic signaling network. Plays a key role in asymmetric spindle positioning; a step for asymmetric cell division that generates cell diversity during development by activating G(i)-alpha protein goa-1 and gpa-16 independently of G- protein coupled receptors. While it acts as a GEF for goa-1; it has no GEF activity toward gpa-16. In addition to its GEF activity; it is required for cortical subcellular localization of G-alpha proteins such as gpa-16. Also required for the interaction of goa-1 and gpr-1/2; suggesting that it may act by generating G- alpha proteins free from G-beta-gamma subunits; enabling gpr-1/2 to mediate asymmetric cell division. {ECO:0000269|PubMed:11102364; ECO:0000269|PubMed:15479638; ECO:0000269|PubMed:15479639; ECO:0000269|PubMed:15489510; ECO:0000269|PubMed:15489511; ECO:0000269|PubMed:15498497; ECO:0000269|PubMed:16162648; ECO:0000269|PubMed:9851916}.', 'MSEELHSDLIASIFGGKPAKIEEFFSKWNFANAAVSKFDMANSAKNELGDRICEVIENGELTHVLLETIKILSREKDGLEGLLNDPLCDKILAFAELSSNENNSKTVHTLMEAQKCLINTLFHSQRMRDRFYANPKTGENLQFFLGEFEENRRKTSSIDWIRLLNPVQAAEIWYFYHRIAFIATALGREFQKNWANDPKTIDSLLLAVEICTNRSENSTQDINRATEALKTFFNVFCHFHGDVKAIDHKNAAKTCQILRDAICSDVLTDDVVQSAIHCLSVPPLPMVLSVLCGKNSKNNGGENEEEKFFVEELSNMQLTEAILMHLDKQLTKVVALLLNDAPNQQQNPMLSAEASTLTDLVGPYFQVLARLCTDSKYVRRYCRIRVIPPLVSEEVQKRPEENNTLRGRIARIMMLPSSTKDVAAEFLFIICKRSVNRMIKYLGFGHSAGHLANLGLLGQINQPKHASDSEDSETEDYNQIKDSVNPVTGAIYPSDHGSALAGMSEEQKEYEAMKLVDAMNQMMETGIVKPGTIGDDGKIREVSHVLELLKNAPEPAPAENSDSDEE', 566, 'Q9GSX9; Q86DD4;', 'KD00364', 'Caenorhabditis elegans', 'ric-8', '#Synembryn#Resistance to inhibitors of cholinesterase protein 8', '-', '-', '177048'),
(365, 'P46060', 'Ran GTPase-activating protein 1', 'GO:0000777===k;s', 63542, 'GTPase activator for the nuclear Ras-related regulatory protein Ran; converting it to the putatively inactive GDP-bound state.', 'MASEDIAKLAETLAKTQVAGGQLSFKGKSLKLNTAEDAKDVIKEIEDFDSLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRTEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVQGFEALLKSSACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFRVIGTLEEVHMPQNGINHPGITALAQAFAVNPLLRVINLNDNTFTEKGAVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAIRGGLPKLKELNLSFCEIKRDAALAVAEAMADKAELEKLDLNGNTLGEEGCEQLQEVLEGFNMAKVLASLSDDEDEEEEEEGEEEEEEAEEEEEEDEEEEEEEEEEEEEEPQQRGQGEKSATPSRKILDPNTGEPAPVLSSPPPADVSTFLAFPSPEKLLRLGPKSSVLIAQQTDTSDPEKVVSAFLKVSSVFKDEATVRMAVQDAVDALMQKAFNSSSFNSNTFLTRLLVHMGLLKSEDKVKAIANLYGPLMALNHMVQQDYFPKALAPLLLAFVTKPNSALESCSFARHSLLQTLYKV', 587, 'P46060; Q96JJ2;', 'KD00365', 'Homo sapiens (Human)', 'RANGAP1', '#Ran GTPase-activating protein 1#RanGAP1', 'BIOMD0000000192,Gorlich2003_RanGTP_gradient;', 'ENSG00000100401', '-'),
(366, 'P46061', 'Ran GTPase-activating protein 1', 'GO:0000777', 63531, 'GTPase activator for the nuclear Ras-related regulatory protein Ran; converting it to the putatively inactive GDP-bound state. Required for postimplantation development. {ECO:0000269|PubMed:16469311; ECO:0000269|PubMed:9442102; ECO:0000269|PubMed:9456312}.', 'MASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRVINLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADKAELEKLDLNGNALGEEGCEQLQEVMDSFNMAKVLASLSDDEGEDEDEEEEGEEDDEEEEDEEDEEDDDEEEEEQEEEEEPPQRGSGEEPATPSRKILDPNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVASVFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVRQDYFPKALAPLLLAFVTKPNGALETCSFARHNLLQTLYNI', 589, 'P46061; Q60801; Q6NZB5;', 'KD00366', 'Mus musculus (Mouse)', 'Rangap1', '#Ran GTPase-activating protein 1#RanGAP1', '-', '-', '19387'),
(367, 'Q8N3U4', 'Cohesin subunit SA-2', 'k', 141326, 'Component of cohesin complex; a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase; the complex is cleaved and dissociates from chromatin; allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000269|PubMed:12034751}.', 'MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKGGNGGGKPPSGPNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSRRDPEEDGMMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDDRTKITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCTHYVILWQLAKITESSSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDNNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGISSRGSTVRSKKSKPSTGKRKVVEGMQLSLTEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMSVYPMQTEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPPSKNRRERTELKPDFFDPASIMDESVLGVSMF', 1231, 'Q8N3U4; B1AMT5; D3DTF5; O00540; Q5JTI6; Q68DE9; Q9H1N8;', 'KD00367', 'Homo sapiens (Human)', 'STAG2', '#Cohesin subunit SA-2#SCC3 homolog 2#Stromal antigen 2', '-', 'ENSG00000101972', '-'),
(368, 'F1MJR8', 'Inactive serine/threonine-protein kinase TEX14', 'GO:0000776===GO:0000777===GO:0008608', 165254, 'Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101; blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro (By similarity). {ECO:0000250}.', 'MSRAVHLPVPCPVQLGSLRNDSLEAQLHEYVKQGNYVKVKRILKKGIYVDAVNSLGQTALFIAALLGLTKLVDVLVDYGADPNHRCFDGSTPVHAAAFSGNQWILSKLLDAGGDLRLHDEKGRNPQTWALAAGKERSTVMVEFMQRCAAHMQAIIQGFSDLLKKIDSPQRLISGVPRFGGLMQGNPNGSPNRPPKAGVISAQNIYSFGFGKFYLTGGTQLAYLGSLPVIGEKEVIQADDEPTFSFFSGPYMVMTNLVWNGSRVTVKELHLSTHPHCSRLRMADLLIAEQEHSSKLRHPHVLQLMAVCLSPDLEKTRLVYERVTVGTLFSVLHERRAQFPVLHMEVIVHLLLQISDALRYLHSRGFIHRSLSSYAIHIVSTGEARLTNLEYMMESQDGGAHRGLTRVPLPTQLYNWAAPEVIIQKAATVKSDIYSFSVIVQEILTDNIPWDGLDGSVIKETIVLGNYLEADVRLPKPYYDIVKSGLQVKQKDRTMNLQDIRYIMKNDLKDFIGAQRTQPTESPRVQRYEFHPDVNVCLGLTSEHPKETPNLEIKELKETGSQFHSPRGHSSPTGKATPEPPVPDVSPVAQQTHRQDAASPACSVAEEARNPSPDQTSLCSFEINEIYSGCLDTADDPEEECPGTGSSLEGAIPNQTDELKSMEEELEKMEREVCCSCDEDESSSDADTELSCEDWEWQNDALCSPSRPEPARGAKGATNNRSMTEEYISKCVLNLKISQTLIHQNADLLRNVQQKIEKLEMIQKEQAERRSLWASSREFAGIHDSPSALGPPASSYLPPVVQRPGDQQLDPGGSGLTLARSPRTLPTLCGPGKQSRGEQFQPTHGAKASLERDRNQNTSSQGRPRESSPQSKTTQLSSALLTVPSHPQGSPTSSKPGQDSTRISMQSVSSEIYNAKSRNNKDDGEIHLKWKTEVKEMAAKAATGQLTVPPWHPRSGVALDSEAENEPDPLPQLPIRVSEHMDWQQAADYLKKSDEPGGNDKCGQTDSSDQRGRQSGPQRFTSIRHLPPREDEQPEHSEVFQANSDASVAVEKSYSGQSAQSTCSPESSEDTEDMTDEFLTPDHEYFYSSIAQENLALETSSPIDEDFEGIQHACARPQASGEEKFQMRKNLGKNSEILTKSQFQPIRSPEGEQDETLKEPPKEVKEKDISLTDIQDLSSISCEHDGSFKEVSCKTPKINHAPTSVSTPLSPGSLSSVASQYKDCLESIPFQDTKTGSTSCGTSQESTQTLSDKFTSVREKAKSLDSLLTSSEVLPARLTNLKRLPAFTGAGSSSIAKAPDTSRCATQRRSLPKELVEAISQHHIDELPPPSQELLDEIEHLKGQQVSSTALDENTASRPGSTENDQRHLEEQETHSNKEDSSMLWTKETQDLEEDTERAHSTLDEDLERWLQPPEDSTQLPDLPKGPAREASSKDQEVGEKKRKGEESTKPEKRKPESFLGTSEEEELKPCFWKRLGWSEPSRIIVLDQSDLSD', 1493, 'F1MJR8;', 'KD00368', 'Bos taurus (Bovine)', 'TEX14', '#Inactive serine/threonine-protein kinase TEX14#Testis-expressed sequence 14#Testis-expressed sequence 14 protein', '-', '-', '522810'),
(369, 'P54703', 'Cytoplasmic dynein 1 intermediate chain', 'GO:0005868', 72328, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chain mediates the binding of dynein to dynactin.', 'MDRDQKKKELEQTKNEMRRKLEEYKERNRIMASKTTPTATTTSTLNTASTPSPPVAQEDFNSIMNSIDSMVPTQATPSSSSTISTSTHAESQKSNYIRPTLTIQSLVIEHDFPPKEIPMYSKGTQTMTDADTSNTNNTPELEAPNKNKTKYQLLQQQQQQQQQQQSSLNQDMQNLSIGTDSINGDGSSTSVANSANIDDDDKDEIEIPELDENEKKDILESDSFKSFFGRSSRVIERALCLDDSIDILVDYTISDENSKGTSKELKLLATLSDERWTKHRSITDISWSTKHPELVVSSYSANEAGSHDPDGVALVWSVNNYFQKPEYVFTCQSPVMTTFFSKFHSTLIVGGTYSGQIVIWDTRAEAKPVQKTPLSSVGHTHPVYSMAVVGSANANSLVSISTDAKLCSWNLENLSQPIETIELNSSNTNSANKAGGGGSGGGAPNMSIAVTSLVFPENELNHFYIGTEEGVICQAGRHGNRIVMNERYKGHFGPITSVDLHPSKGGADFSQYFLSSSTDWTCKLWSSKKETPLYSFEDYVDYVYDARWSPVHPSIFSTGDGSGTLSLWDLNQDLEAPIFRHKISNRSVNRLAWSHDGKRILVGDSGGSLSLFDSSEFSSPTSEEYSQFEDVMTKMVNKSRTSDSPLLGEGENQE', 654, 'P54703; Q54UP8;', 'KD00369', 'Dictyostelium discoideum (Slime mold)', 'dicA', '#Cytoplasmic dynein 1 intermediate chain#DH IC#Dynein intermediate chain; cytosolic', '-', '-', '8622777'),
(370, 'Q8I009', 'Baculoviral IAP repeat-containing protein 5', 'GO:0000777===GO:0032133', 16271, 'Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokenesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). {ECO:0000250}.', 'MGASSLPPAWQLYLKDHRVSTFKNWPFLEGCACTPDRMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLSEFLKLDKERAKNKIAKETNNKQKEFEETAKKVRCAIEQLAAAE', 142, 'Q8I009; Q5XPZ7; Q6L673;', 'KD00370', 'Canis familiaris (Dog) (Canis lupus familiaris)', 'BIRC5', '#Baculoviral IAP repeat-containing protein 5#Apoptosis inhibitor survivin', '-', '-', '442936'),
(371, 'P25992', 'Yemanuclein-alpha', 'GO:0000776===GO:0000777', 109311, 'May play a key role in egg organization. May be a transcriptional regulator having a role in chromatin remodeling in concert with Hira; a histone chaperone. Involved in chromosome segregation by affecting kinetochores function in the first meiotic division. {ECO:0000269|PubMed:1606021; ECO:0000269|PubMed:21080953}.', 'MSKGGEHKRVTLTSIIQGDAGFSRFGSNILEPDAASAAPDNSSKPTTKTAKCIRIKLDLFETDSNKYPEFNYSRLLYLEKKKTKKLKQVSTTNGSASTDPFADNDDDVARIVKELEAKYGNSYATGRGKSKKDDYRDIGMGYDESDSFIDNTEAYDEIIPEEAETLEGGFYINCGALEFKNLTKKSYTTRTDAIIKMPERSRKRMVSSSSESSSSSSGDDDENDDGNNEEDDESDSEDDSEENDESDSEDDSESESLEDEDSAATAKSSSKYKDNHQAKRAKVIVTGKSKPSSSSLTSGKKPPTKPITTSSSSNSPRPSTVEISDTEDGQDPIQTQPSSQLQSLPQSQAQAQALKKVVKTTTVKDMLKAKRDSFLKSQSGTAAVKGVGNGELKCVSTDVSSSDSSDMESEHGRADRQAGQHGKDGQENLRTADTLLPTTLDADIVTAVNSFKEAVKSRDMCGKKFNLDVKLSPLLLRVYEAVLCTDRNERNMVFSHIEYQLQLPKYYMLRKGKQVRAKEEKRKSTIMLEKLRRAVAVVMPKAVANYETELRTFAEQAAADVNSELPPKMPRKKFQWTSELRHLLYDVYQARWTSYAFLAKRKESLEEFINWYLKEKVVELWPPGWMRLDELQREITRYKNAKLKAKEKPKAPPASASPKPVGVVSAPEQMPPASSYLKAVEDPRSRGNSDTDSATSASSNSLKRKLKEMPKQTSKPPKKKVAKQVPLQPQLTPHPQFQLAPAATAAVSIPAISNNNNHLPHLDTLLSMPSTSAQAAALNAAAVAAASTVLDLASPSRKIDLNTSNNFYNLITAASLAASGNPSPHSGDGQAKVIVGARPSPHVINLDDYQCTSDILQTSKQLAATTTVITAISKAAQTTSVARESSSESDGVEIVGVFPASKPQKKVQSKPKNKTQNRGRSSLGAVGQVNGSLGYSANNMYIYNSPRTLGPVYDLTDPHIMKTMSNLKEMEKQFIQAAFSPNSVKGASGGMGSSAPSTPTRQ', 1002, 'P25992; Q6AWM5; Q9VAP4;', 'KD00371', 'Drosophila melanogaster (Fruit fly)', 'yemalpha', '#Yemanuclein-alpha', '-', '-', '43439'),
(372, 'Q6CDG5', 'DASH complex subunit DAD4', 'GO:0008608===GO:0051987===GO:0042729', 8667, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MENPHEKDQSDALARIISGVSKLNSSIARVNEIQEEVYSRNLNLSVVSEIMQNYQASVDYYLRESGAMKEPFKNDD', 76, 'Q6CDG5;', 'KD00372', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'DAD4', '#DASH complex subunit DAD4#Outer kinetochore protein DAD4', '-', '-', '2909185'),
(373, 'Q8TE73', 'Dynein heavy chain 5; axonemal', 'GO:0003777', 529021, 'Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles.', 'MFRIGRRQLWKHSVTRVLTQRLKGEKEAKRALLDARHNYLFAIVASCLDLNKTEVEDAILEGNQIERIDQLFAVGGLRHLMFYYQDVEEAETGQLGSLGGVNLVSGKIKKPKVFVTEGNDVALTGVCVFFIRTDPSKAITPDNIHQEVSFNMLDAADGGLLNSVRRLLSDIFIPALRATSHGWGELEGLQDAANIRQEFLSSLEGFVNVLSGAQESLKEKVNLRKCDILELKTLKEPTDYLTLANNPETLGKIEDCMKVWIKQTEQVLAENNQLLKEADDVGPRAELEHWKKRLSKFNYLLEQLKSPDVKAVLAVLAAAKSKLLKTWREMDIRITDATNEAKDNVKYLYTLEKCCDPLYSSDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISACKAYITNNGTASIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFTTLKTYSVLQDSTIEGLEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAKIQNTNQALRMLKKFERLNIPNLGIDDKYQLILENYGADIDMISKLYTKQKYDPPLARNQPPIAGKILWARQLFHRIQQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVGLEASLLVKAPGTGELFVNFDPQILILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWTSLNIEAYLENTFAKIKDLELLLDRVNDLIEFRIDAILEEMSSTPLCQLPQEEPLTCEEFLQMTKDLCVNGAQILHFKSSLVEEAVNELVNMLLDVEVLSEEESEKISNENSVNYKNESSAKREEGNFDTLTSSINARANALLLTTVTRKKKETEMLGEEARELLSHFNHQNMDALLKVTRNTLEAIRKRIHSSHTINFRDSNSASNMKQNSLPIFRASVTLAIPNIVMAPALEDVQQTLNKAVECIISVPKGVRQWSSELLSKKKIQERKMAALQSNEDSDSDVEMGENELQDTLEIASVNLPIPVQTKNYYKNVSENKEIVKLVSVLSTIINSTKKEVITSMDCFKRYNHIWQKGKEEAIKTFITQSPLLSEFESQILYFQNLEQEINAEPEYVCVGSIALYTADLKFALTAETKAWMVVIGRHCNKKYRSEMENIFMLIEEFNKKLNRPIKDLDDIRIAMAALKEIREEQISIDFQVGPIEESYALLNRYGLLIAREEIDKVDTLHYAWEKLLARAGEVQNKLVSLQPSFKKELISAVEVFLQDCHQFYLDYDLNGPMASGLKPQEASDRLIMFQNQFDNIYRKYITYTGGEELFGLPATQYPQLLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCPLLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFTFGSFKTRGELLLRGDSTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVGGDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCVGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVSDPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEKIYDRILSISSQEGETIELDKPVMAEGNVEVWLNSLLEESQSSLHLVIRQAAANIQETGFQLTEFLSSFPAQVGLLGIQMIWTRDSEEALRNAKFDKKIMQKTNQAFLELLNTLIDVTTRDLSSTERVKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDSDKMMIHITDVAFIYQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFTDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINFRSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIVMRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTLGPSGAGKTTCIHTLMRAMTDCGKPHREMRMNPKAITAPQMFGRLDVATNDWTDGIFSTLWRKTLRAKKGEHIWIILDGPVDAIWIENLNSVLDDNKTLTLANGDRIPMAPNCKIIFEPHNIDNASPATVSRNGMVFMSSSILDWSPILEGFLKKRSPQEAEILRQLYTESFPDLYRFCIQNLEYKMEVLEAFVITQSINMLQGLIPLKEQGGEVSQAHLGRLFVFALLWSAGAALELDGRRRLELWLRSRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPSDTTPEYGSILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKGFMSKYDPECHMIKSLNFSSATTPLMFQRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYNLEKPGEFTSIVDIQFLAAMIHPGGGRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKIKMLPTPAKFHYVFNLRDLSRVWQGMLNTTSEVIKEPNDLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGEEKKLLVDCGIDTYFVDFLRDAPEAAGETSEEADAETPKIYEPIESFSHLKERLNMFLQLYNESIRGAGMDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEFPRCLPTNENLHDYFMSRVRQNLHIVLCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLTSYDIDCSLEIKKEVVQCMGSFQDGVAEKCVDYFQRFRRSTHVTPKSYLSFIQGYKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMDCVLLLFQRKVSAVKIDLEKSCTMPSWQESLKLMTAGNFLQNLQQFPKDTINEEVIEFLSPYFEMPDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDWRKEMKARKIPFGKNLNLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEISAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDLSLARSVKSPITSKRIANIIEHMTYEVYKYAARGLYEEHKFLFTLLLTLKIDIQRNRVKHEEFLTLIKGGASLDLKACPPKPSKWILDITWLNLVELSKLRQFSDVLDQISRNEKMWKIWFDKENPEEEPLPNAYDKSLDCFRRLLLIRSWCPDRTIAQARKYIVDSMGEKYAEGVILDLEKTWEESDPRTPLICLLSMGSDPTDSIIALGKRLKIETRYVSMGQGQEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIETELVHDAFRLWMTTEAHKQFPITLLQMSIKFANDPPQGLRAGLKRTYSGVSQDLLDVSSGSQWKPMLYAVAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLDDMDVKKGVSWTTIRYMIGEIQYGGRVTDDYDKRLLNTFAKVWFSENMFGPDFSFYQGYNIPKCSTVDNYLQYIQSLPAYDSPEVFGLHPNADITYQSKLAKDVLDTILGIQPKDTSGGGDETREAVVARLADDMLEKLPPDYVPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSLVRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISSTLGFWFTELIERNSQFTSWVFNGRPHCFWMTGFFNPQGFLTAMRQEITRANKGWALDNMVLCNEVTKWMKDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFELMPVIRIYAENNTLRDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLCDVK', 4624, 'Q8TE73; Q92860; Q96L74; Q9H5S7; Q9HCG9;', 'KD00373', 'Homo sapiens (Human)', 'DNAH5', '#Dynein heavy chain 5; axonemal#Axonemal beta dynein heavy chain 5#Ciliary dynein heavy chain 5', '-', 'ENSG00000039139', '-'),
(374, 'P47134', 'Protein BIR1', 'GO:0000778===GO:0031134===GO:0032133===k', 108667, 'Seems to act in the pleiotropic control of cell division. May participate in chromosome segregation events.', 'MDGQIDKMEKRYSMTKLENRLRTFQDGVALEKKKLKWSFKVIPYQAMAKLGFYFDPVIDPKTSKLKKDSVRCCYCHRQTYNVRDCRSKRKDVLETLSNIMRQHLTVTDNKQVCLLIYLRNKLLTDYSFHMGVSDWKNDKYFSNPDDENVINLRKFTFQDNWPHSGSQNEHPLGIEKMVNAGLMRYDSSIEGLGDPSMDKTLMNDTCYCIYCKQLLQGWSINDDPMSRHYKVSQNGNCYFFQTRNRFERIKNDNDSITKNCEVSPTLGENGKREVINTKTASQRQCPLFESPPSSTGPQLDDYNEKTDISVIQHNISVLDGAQGENVKRNSVEEKEQINMENGSTTLEEGNINRDVLADKKEVISTPTAKEIKRPNVQLTQSSSPIKKKRKFKRISPRKIFDEEDSEHSLNNNSANGDNKDKDLVIDFTSHIIKNRDVGRKNAILDDSTDEFSFSNQGHNTFDIPIPTSSHLLKGIDSDNDNVIREDDTGINTDTKGASSKHEKFSVNSEEDLNFSEVKLTGRDSSTNILIRTQIVDQNLGDIDRDKVPNGGSPEVPKTHELIRDNSEKREAQNGEFRHQKDSTVRQSPDILHSNKSGDNSSNITAIPKEEQRRGNSKTSSIPADIHPKPRKNLQEPRSLSISGKVVPTERKLDNINIDLNFSASDFSPSSQSEQSSKSSSVISTPVASPKINLTRSLHAVKELSGLKKETDDGKYFTNKQETIKILEDVSVKNETPNNEMLLFETGTPIASQENKSRKLFDEEFSGKELDIPIDSSTVEIKKVIKPEFEPVPSVARNLVSGTSSYPRNSRLEEQRKETSTSLADNSKKGSSFNEGNNEKEPNAAEWFKIDENRHLVKNYFHDLLKYINNNDATLANDKDGDLAFLIKQMPAEELDMTFNNWVNLKVQSIKREFIDDCDKKLDILRRDYYTATNFIETLEDDNQLIDIAKKMGIL', 954, 'P47134; D6VWQ7;', 'KD00374', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'BIR1', '#Protein BIR1', '-', '-', '853551'),
(375, 'Q9N583', 'HCP-6; isoform a', 'k', 195174, '', 'MSNINEKDLSEFLESNLRSLNDIDDAVATSSAECNYEDYEEFTNSVDLTFFEQDLSGVLKELKKLAESVVISGKKCDIRNIFEESDVATMKFNLFVWYFLENGQRSDSSEEDVDKGVSAASSYIAMCSLPGAISDLYQIGLYNQCLKIIRNCCHTVRIGETVVTKKSSGAKKKKAGGKSDETNVDGEMTVTTGAADPIIGPPRIAVDSAERYLHHLTTQLFAFLHSNTFSIDTPTLMSTLEVVEDIGRLDLDNRTAGRAIRANSVHEFRSLERFTDRYCAFVHSLVESKYKTRAEVAYGRLIRPRLALMPYPDESNKSSKISTERKRSGELHVNLILSRISRNPEARELKYIQTVTVMVYSQCPDLAEFRTNIATFIHKILEALPYTYTYDFVQFMNVLFKGRGAGVKSLSTELSSILISSFDFTAPDPGAIPNLDAEQNEEEDEEEEGEDEEEEEENEQDDVAVKEEEQSDKSDEENDGDNEENVSKKKEEKKKEKKAKEVKEVGRMDAMSVLYNIVYMACLDKAAAMRLHGANSLTKILQSQSHREAFQLFCATINAEMDEKFGAVGDNLSESLEDLNVSGKAPSSKTKKPTDLLLDEQQIIQKFNKLKLMNKGETRVEKDIVYMIVRRLSTDDKAPVKKAACSLLKSYLSYCDEASKFEVVLSILQMLCRDRMVSVRKTGADAFTELMLRDAILFKESLSSKWLHTLISMLNDTDNDVTEHARKLIMKVLTPLLENSSDLTWTLLDTIESVTNHRQYLMSTLKDAVREKLVKRTVMDSMKQHIISGSEKLDGAWMVFSQLCVQFEQNVDFAIETFSRVDLSRESNLVQYMIHVIENNIKKIDDDTKSDLVNTLQGTFRDYCLHPSHSRSIYHCLGKLMDGIGDRSLHGKEFSDFGETLLIKCFDTIVQSFEMFKDKDEWKRNSESQERLLCTALNVASEVFSYSPQLVPRHERLGKTLSLIVNSTENGSSDASTVNPDMPSVHHTRPPTQLSEVPSSQKSSKGGMMSHEGAMFSDKVRAVGVVTLANMILAHDRLLKLMPMLVKQLQYNTAHQIRSNIVLAIGDICSSYKTDRYAPMLAASLCDPSVIVRRHAINQIARLISFGIFRFNGEIMIRMMLASLDANEDVRNDAKLYISEVLQSEEPNFFPLNFVQYMIALTQARRLVGVGHDEDDRGQVDVAIGGGDPLARPSRIAIYTFMIDSLDDRSRFDVKMSICQRIFTPIVNGEYDFSDYNVQCLLDDALLIMASNEMQVKMDVGKNPNENAMDDPSPEVLEAATGFMQKVYLDHYMKTIVPSILSLREFLNQHRSPLQRKCLLAIRMICIEHKNDIDEILQDNRQLKDEMMFELQRVKQRTEEANRILDEYLKRVAEFKKQQKRLSKSPAPMELDAEPVQESAEAVEMGSPARRIEEDQENVEEEVEMRTPQKKNPDADVPRTPLNALRSTTEEKSTPNARLLSPKTIKKIRRSLGALIHTEMRLNPPNLEETKIDDTTINRSKQADKTEEKTIVEEEPMEEAAAEKTVTAENDHVDAEKTVIAVEIPPATEAEEDEVVDVQSESRRSRRRKTPNYDDEESVDADGKIWKKPKIVNKSPEKEVNISANVTLRRSRRGQSTEPPVVKENSNRKRKSVDEEEENVPTSSSGNTENDPLSRGVTPLIFDESKLGAGRHCSTPIRSREDADPSDVTFSLNLSAITEKEDLKNRKSQAYHLHNIFEEDEEES', 1724, 'Q9N583;', 'KD00375', 'Caenorhabditis elegans', 'hcp-6', '#HCP-6; isoform a {ECO:0000313|EMBL:CCD66189.1}', '-', '-', '266830'),
(376, 'Q9WTX8', 'Mitotic spindle assembly checkpoint protein MAD1', 'GO:0000776===GO:0000777===k', 83541, 'Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression; possibly by interfering with MYC binding (By similarity). {ECO:0000250}.', 'MEDLGENTTVLSSLRSLNNFISQRMEGTSGLDVSTSASGSLQKQYEYHMQLEERAEQIRSKSYLIQVEREKMQMELSHKRARVELERAASTNARNYEREVDRNQELLARIRQLQECEATAEEKMREQLERHRLCKQNLDAVSQQLREQEDSLASAREMISSLKGRVSELQLSAMDQKVQVKRLESEKQELKEQLELQQRKWQEANQKIQELQASQDERAEHEQKIKDLEQKLCLQEQDAAVVKSMKSELMRMPRMERELKRLHEENTHLREMKETNGLLTEELEGLQRKLSRQEKMQEALVDLELEKEKLLAKLQSWENLDQTMGLNLRTPEDLSRFVVELQQRELTLKEKNNSITSSARGLEKVQQQLQDEVRQANAQLLEERKKRETHEALARRLQKRNALLTKERDGMRAILGSYDSELTQTEYSTQLTQRLWEAEDMVQKVHAHSSEMEAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGGPIPADLEAASSLPSSKEVAELRKQVESAELKNQRLKEVFQTKIQEFRKVCYTLTGYQIDVTTESQYRLTSRYAEHQTDCLIFKATGPSGSKMQLLETEFSRSVPELIELHLLQQDSIPAFLSALTIELFSRQTSI', 717, 'Q9WTX8; Q9WTX9;', 'KD00376', 'Mus musculus (Mouse)', 'Mad1l1', '#Mitotic spindle assembly checkpoint protein MAD1#Mitotic arrest deficient 1-like protein 1#MAD1-like protein 1', '-', '-', '17120'),
(377, 'Q39575', 'Dynein gamma chain; flagellar outer arm', 'GO:0003777', 512846, 'Force generating protein of eukaryotic cilia and flagella. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.', 'MALDNRHRLIVGKLAEAFGLPENVIEKTLTQDKQAVNSFFTPAGPPSLVFVYQVKEDKLKDGSVGPVDNKPTLHRIGPHERIHNSVYFTRLNPKGINEKTLEADMGSGELSVLWALENFKAIVSDLYLPIMQEQQQWGKMSTEYLEDFLSSTAKFGSMLTEAVATVSGGVEPMPDPRYIDQYGDLRPAGITQAAGDDDTLQEMEECLTEWCREAELLLNQTNKIKDGEERGPDTELEYWRTRMSNFNSITEHLKTKECKLVLGICSHAKTKAYLRWRGLDVQITDAANESKDNVKYLATLEKSMEPMYQGRVTDITESLPALMTNVRMMYTIARFYSTAEHMTRLFTKITNQLVRRCKEQIMENGKIWDQDKVTLIGNMKVSVELANVYRQQYRLAKETLAAQPKSKQFDFDEQAIFLKFDLSSKALHKLIDMFTTIHQFSSLEQHTHIEGLDTMLKSLNNIIDDVKRKPYDLLDYSRNAFDTDFLEFNVQINDLELQLQGFVNASFEHITSTEHALSLLAQFQAIMQRETLQQDLENKYMVIFQNYAKDLDAVQKLYEKNKYEPPVPRNAPPVAGNIMWARQLLRRIEAPMQLAQNKNLLAAKESKKNIKTYNKVAKALIEFETLWHQAWIKSIEQCKAGLAAPLLVQHPDTGKILVNFDKEIMQLVREAKYMQRFNIRCSSPSQMVLLQEEKFKFYHNQLTHLVREYEHVLGRGATIKPLLRPHLDDMERKIAPGFAVLTWTSLNIDGYLHRFKQGLARLEELVRKVVDLTENRVDSNLGAISSTLLVELPTDRSFTYEGFVEQNRFQKKQAELLAIRNEEVRRAIEDLYTLVRNYPRENTEDVLDEKEVSLLVRHYSKNMYNAIMQCTLNSLQAMKRRLGSKTTTGIFFMERPFFDVDVELKVPSVCMNPTLEEIQAAINQCAKKVLTISKQLPAWGMDNVATYHEMMRGDRRWVKAVLRLTGSVEGIKTQVGEYIRTFDKYDFLWKEDLQAAYDHFMRSNPTLEAFEAELKKYMAIETEVTMINGVNNIGALSLETHPLKNSLKAEAVSWKTQFAQNLHKQCSDDLKLDNYIRDTNSKFHRKIEDLEDVRNVMAVLKEVREKESEIDNLIGPIEEMYGLLMRYEVRVPKEETTMVSDLRYGWKKLKKVATEVSDNLTRLQVGFKRELIKEVKTFVVDAQMFRKDWEANAMVPGLDPQEAVDRLRKFQQMFEVRKRKWENYSSGEELFGLPVTQYPELEQTEKEIQMLDRLYSLYVAVITTIKGYGDYFWVDVVEKIDEMGEQVQQYQNQSKKLPKLRDWPAYNACRKTIDDFLEMLPLFQALTHKSMRERHWKEVMRVTGHELNLAEDHFKLQHLLDCNVLRYREDIEDLTGAAVKEEIIEVKLNQLKADWATANLALAEYKNRGPVILKPSDTSELMEKLEESQMTLGSMATNRYSAPFRDEVQAWSIKLSTVSEIIEQWLMVQSMWQYMEAVFSGGDIVKQLPQEAKRFLNIDKNFMKIVSNALETQNVINTCFGNELMKNMLPHLHEQLEMCQKSLSAYLEQKRAEFPRFTCVGPHLLEICRWAHDPPSVVPHFQSGLFDSLSNVTFDRIDKTRMTEMFSQQNEKVEFERPVDAKGNIEVWLQRLVDGMEDTVKQIIKRAVRNVAEMPLEDFVFGHPAQVSLLGIQFQWTAETQMALSSAKVDKTIMNKNMKKVDALLRDMVNITVRLDLTKNQRTNLETCITVHMHQKESTEDLVKKKIKDPTDFEWLKQVRFYWRDDKDTVIISICDVDFEYSFEYLGVKERLVITPLTDICYITLSQALGMFLGGAPAGPAGTGKTETTKDLGNTLGKYVVVFNCSDQFDYTYMGKIYKGLAQSGLWGCFDEFNRINLDVLSVCAQQVYCICRTRERKKSFQFTDGTTVSLDPRVGFFITMNPGYAGAQELPENLKALFRGVTMMVPNRQIIMKVKLAAAGYQENDILSKKFFVLYGLCEQQLSKQAHYDFGLRNILSVLRTAGASKRQSPDKSEVFLMMRTVRDMNMSKFVAEDVPLFLSLIDDLFPGLKADATRPDVNKDAEKVVLERGLQVHPTWMNKCIQLYETYLVRHGIMLVGPSGSGKSAICECLAAALTELGTKHVIWRMNPKAITAPQMFGRRDDTTGDWTDGIFAVLWRRAAKNKNQNTWIVLDGPVDAIWIENLNTVLDDNKVLTLANGDRILMSAAMKAMFEPENLNNASPATVSRAGIIYVSDVELGWEPPVKSWLQKRDPTEACWARLFSKYIDRMLEFVRISLKPVMYNEQVSIVGTVMTLLNGYLKSMKEAGTAMNDAKYERVFLYCMTWSLGGLLEMKERPLFDQELRTFAHNMPPKEEDSDTIFEFLVNTTDAEWLHWRHCVPVWTYPKNEEKPQYAQLVIPTLDSVRYGALLNLSYNVDKATLLVGGPGTAKTNTINQFISKFNAETTANKTITFSSLTTPGIFQMSIEGAVEKRQGRTFGPPGGKQMCIFVDDISMPYINEWGHQVTNEIVRQLLEQGGMYSLEKPIGDMKFITDVRYVAAMNTPGGGKNDIPNRLKRQFAIFNVPLPSVAAINGIFGKLVEGRFSRDVFCEEVVYVASKLVPLTITLWNRIQTKMLPTPAKFHYLFNMRELSKVFQGVILATRDRFNLAAGDSAVFGGNVASPEGYLLGLWIHECRRVFSDKLISYEDKNWVDKAVFDLCRDNFSSDLVKQVEEPIYFVDFLREPAVMMRPVEIVTPHPSFYYSVPGGLPEVRARVEGLQRKFNEESKVMKLELVLFTDCVTHLMRITRLLAWPGLGLLVGVGGSGKQSLSRLSAYIAGPTFYITKTYNVSNLFEHIKGLYKIAGFKGQPVYFIFTDAEVKDEGFLEYINQILMTGEVAGLLTKEDQDMIVNDIRPVMKHQAPGILDTYDNLYNFFLNRVRDNLHVVLCFSPVGAKFARRAQQFPGLINGCTIDWFCPGPKKRLTSVSGKFIDKFTMACPKEVKNQLELLMGHAHVFVTAACKEYFEKYRRYVYVTPKSYLSFLQGYKELYAKKWSFTKELAYQIEVACQKMFEPKADVNKMKAELAVKNQTAVSAKEAEALLKQISESTAIAEKEKQKVAVIVDAVTKKASEIATVKDDAERDLAAAKPALDAALEALNSIKDGDIKNLKALKKPPQIITRIFDCVLVLRMLPVTKAEYTDEKGRMVQVGNYPEAQKMMNQMSFLQDLKDFAKEQINDETVELLEPYFMSEDFTFENAQKGSGNVAGLCNWAESMAKYHNVAKVVEPKIAKLREAEAELKLATKEKNAAEERMAKVQAKLDEMQAQFDAAMAHKQALEDDAAATQRKMDSANALIGALAGEEARWTAQSKEFDVQIQRLTGDCALASAFVSYLGPFNKEFRELLLNRDFYGDCMKLNVPVTPHLQITKFLVDDSEVGEWNLQGLPTDELSIQNGIMVTRASRYPVLVDPQGQGREWIKNREEANQLKTTQLNDKLFRNHLEECLAFGRPLLIENIEEELDPLLDPVLERRLVKKGKTWVVPLADKEVDFTETFRLFCTTRLPNPHFTPELSAKVTVVDFTVTMAGLEDQLLGKLISKEKKELEDQRQQLLEEVQSYKKRIKQLEDDLLCRLSNSQGNLLDEHQELIDVLAVTKQTAQDVSEKLANASETNKRINEACEEYRPVAHRATLLYFLIAEFSVVNCMYQTSLAQFNQLYELAIDRSEKANMPSKRIHNIIEYMTYEIYLYVQRGLFERHKIIFALMLTNKVLTSAGKVKATDLDVFLKGGAALDINSVRKKPKDWIPDLVWLNIIALSAMDAFRDIPDSVFRNDGLWRQWYDQEAPEMAKVPDYEDRLNKFERMCVVKTFREDRTLIAAADYIAEALGQRFVESVPLNMEKRPGRRAMAKCPLICLLSPGPDPTKLIEDLAKKKKIKTLGVSMGQGQEVIARKHMAAASLEGHWVLLQNTHLGLGYLTEVETFLVKEENVHEDFRLWITAEPHPQFPIGLLQMGIKITNEAPVGIKAGLRASYQWVNQDMLDMVSRQEWRQLLFVMCFLHSVVQEPQFGPIGWNVPYEFNQSDLSACVQFLQNHLSEMDAKKAPQPTWETVRYMISAIQYGSRITDDFDKLLMDTFAEKYFLQPVLQPSYELFKDTRSSDGFSYRVPDSTDIETFGSYIETLPGTESPEIFGLHPNADITFRTLQVQESIVTILDTMPKGAGSGSGLSREDVVDKICEDLLSKAPPLFDKEETKEKLKKLPGGPTLPLTVHLRQEIDRLNIVTRLTTTTLKNLALAIAGTIAAERGLIDALDALFNARIPQQWLSKSWEASTLGNWFTGLLQRYDQLNKWLNLGRPKAYWMTGFFNPQGFLTAMKQEVNRKHRDKWALDDVVMSSEVTHRPKDFESLKEGAPEGVYVYGLYLDLRLDGRENRLMDSDPKKLFNPLPVLHVDGVLAKDKKRSGLYEAPKPYRVKARKGLNFITTFSVRTEDDKSKWILPGVGILCSID', 4485, 'Q39575;', 'KD00377', 'Chlamydomonas reinhardtii (Chlamydomonas smithii)', 'ODA2', '#Dynein gamma chain; flagellar outer arm', '-', '-', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(378, 'Q95NU5', 'Torsin-like protein', 'GO:0005818', 40814, 'May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. {ECO:0000269|Ref.2}.', 'MKLDYVLLLLFHLCFVNTELISVITGKIKDSGTTIAISAGAFWGLKDRLKCYLYECCHEPDVNFNYHTLDADIANLLFGQHLVKDVVVNSIKSHWYNENPRKPLVLSFHGYTGSGKNYVAEIIANNTFRLGLRSTFVQHIVATNDFPDKNKLEEYQVELRNRILTTVQKCQRSIFIFDEADKLPEQLLGAIKPFLDYYSTISGVDFRRSIFILLSNKGGGEIARITKEQYESGYPREQLRLEAFERELMNFSYNEKGGLQMSELISNHLIDHFVPFLPLQREHVRSCVGAYLRKRGRGDLVSNVDFVERVLNSLQYFPESSKAFSSSGCKRVDAKTDLEMAKIRPLLSSVHFDDEL', 356, 'Q95NU5; Q95NY6;', 'KD00378', 'Caenorhabditis elegans', 'ooc-5', '#Torsin-like protein#Abnormal oocyte formation protein 5', '-', '-', '174433'),
(379, 'P34331', 'Serine/threonine-protein kinase plk-1', 'k', 73633, 'Required for oocyte nuclear envelope breakdown before entry of oocyte into spermatheca. In meiotic cells; required for spindle dynamics and probably for spindle attachment to the chromosomes. Zygotic role in the development of the germline and nerve cord. In mitotic cells; plays a role in spindle organization and centrosome maturation. Involved in asymmetric nuclear localization of cdc-25.1 during embryogenesis which affects cell division timing. {ECO:0000269|PubMed:10660671; ECO:0000269|PubMed:18199581; ECO:0000269|PubMed:18305005; ECO:0000269|PubMed:18316412; ECO:0000269|PubMed:20823068}.', 'MNRLPNIAKPPQKSNQRKEKAPPEVPALIADKDRGTYYEKGRFLGKGGFAHCYELTNRATREVVAGKVVPKSMLVKQYQRDKVDNERILIHRELGHINIVKLFNFFEDNLNVYITLELCARRSLMELHKRRKAVTEPEARYFTHQIVDGVLYLHDLNIIHRDMKLGNLFLNDDLVVKIGDFGLATTVNGDERKKTLCGTPNYIAPEVLNKAGHSFEVDIWAVGCILYILLFGQPPFESKSLEETYSRIRHNNYTIPSIATQPAASLIRKMLDPEPTRRPTAKQVQRDGFFKSGFMPTRLPVSCLTMVPKFGGHETSMMEENVAPRGVDARSQRPLNGRAGLSALPQHIVSNNADRERAQQQAAEATFREPEDAYLSQLFHQVAVLLEQRIPGLEEEEAALDGYQSPECLPVFWISKWVDYSDKYGIGYQLCDNSVGVLFNDNSRIMLDQAGNELTYIEKSNKEHYFSMHSGEMPGLLNKKVTLLKYFRSYMNDHLVKAGEGSEQRAGDDLARLPTLRVWFRTKSAIVLHLSNGTVQINFFNDHVKMMMCPLMQAVTFIDQNKRMLTYKLNNLQRNGCPEKFLHRLKYAKTMIERLMSDANVVSQNPARQPDMPRSMAAARSASAGSRGPNQAASHLPQSASGSNIHPRR', 649, 'P34331; O61662; O76763;', 'KD00379', 'Caenorhabditis elegans', 'plk-1', '#Serine/threonine-protein kinase plk-1#2.7.11.21#Polo-like kinase 1', '-', '-', '176143'),
(380, 'Q9NTJ3', 'Structural maintenance of chromosomes protein 4', 'GO:0051383', 147182, 'Central component of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.', 'MPRKGTQPSTARRREEGPPPPSPDGASSDAEPEPPSGRTESPATAAETASEELDNRSLEEILNSIPPPPPPAMTNEAGAPRLMITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVEVHFQKIIDKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKGQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLPQTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDVAISSCCHALDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFDLVKVKDEKIRQAFYFALRDTLVADNLDQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNITKSVAVNPKEIASKGLC', 1288, 'Q9NTJ3; A6NLT9; D3DNL8; O95752; Q8NDL4; Q9UNT9;', 'KD00380', 'Homo sapiens (Human)', 'SMC4', '#Structural maintenance of chromosomes protein 4#SMC protein 4#SMC-4#Chromosome-associated polypeptide C#hCAP-C#XCAP-C homolog', '-', 'ENSG00000113810', '-'),
(381, 'Q8BSQ9', 'Protein polybromo-1', 'GO:0000776', 187188, 'Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Acts as a negative regulator of cell proliferation. {ECO:0000250}.', 'MGSKRRRATSPSSSVSGDFDDGHHSVPTPGPSRKRRRLSNLPTVDPIAVCHELYNTIRDYKDEQGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDVNLLTADFQLLFNNAKAYYKPDSPEYKAACKLWDLYLRTRNEFVQKGEADDEDDDEDGQDNQGTLADGSSPGYLKEILEQLLEAIVVATNPSGRLISELFQKLPSKVQYPDYYAIIKEPIDLKTIAQRIQNGSYKSIHAMAKDIDLLAKNAKTYNEPGSQVFKDANSIKKIFYMKKAEIEHHEMTKSSLRIRTASNLAAARLTGPSHNKSSLGEERNPTSKYYRNKRAVQGGRLSAITMALQYGSESEEDAALAAARYEEGESEAESITSFMDVSNPFHQLYDTVRSCRNHQGQLIAEPFFHLPSKKKYPDYYQQIKMPISLQQIRTKLKNQEYETLDHLECDLNLMFENAKRYNVPNSAIYKRVLKLQQVMQAKKKELARRDDIEDGDSMISSATSDTGSAKRKSKKNIRKQRMKILFNVVLEAREPGSGRRLCDLFMVKPSKKDYPDYYKIILEPMDLKIIEHNIRNDKYAGEEGMMEDMKLMFRNARHYNEEGSQVYNDAHILEKLLKDKRKELGPLPDDDDMASPKLKLSRKSGVSPKKSKYMTPMQQKLNEVYEAVKNYTDKRGRRLSAIFLRLPSRSELPDYYLTIKKPMDMEKIRSHMMANKYQDIDSMVEDFVMMFNNACTYNEPESLIYKDALVLHKVLLETRRDLEGDEDSHVPNVTLLIQELIHNLFVSVMSHQDDEGRCYSDSLAEIPAVDPNSPNKPPLTFDIIRKNVESNRYRRLDLFQEHMFEVLERARRMNRTDSEIYEDAVELQQFFIRIRDELCKNGEILLSPALSYTTKHLHNDVEKEKKEKLPKEIEEDKLKREEEKREAEKSEDSSGTTGLSGLHRTYSQDCSFKNSMYHVGDYVYVEPAEANLQPHIVCIERLWEDSAGEKWLYGCWFYRPNETFHLATRKFLEKEVFKSDYYNKVPVSKILGKCVVMFVKEYFKLCPENFRDEDVFVCESRYSAKTKSFKKIKLWTMPISSVRFVPRDVPLPVVRVASVFANADKGDDEKNTDNSDDNRAEDNFNLEKEKEDVPVEMSNGEPGCHYFEQLRYNDMWLKVGDCVFIKSHGLVRPRVGRIEKVWVRDGAAYFYGPIFIHPEETEHEPTKMFYKKEVFLSNLEETCPMSCILGKCAVLSFKDFLSCRPTEIPENDILLCESRYNESDKQMKKFKGLKRFSLSAKVVDDEIYYFRKPIIPQKEPSPLLEKKIQLLEAKFAELEGGDDDIEEMGEEDSEVIEAPSLPQLQTPLANELDLMPYTPPQSTPKSAKGSAKKESSKRKINMSGYILFSSEMRAVIKAQHPDYSFGELSRLVGTEWRNLETAKKAEYEGMMGGYPPGLPPLQGPVDGLVSMGSMQPLHPGGPPPHHLPPGVPGLPGIPPPGVMNQGVAPMVGTPAPGGSPYGQQVGVLGPPGQQAPPPYPGPHPAGPPVIQQPTTPMFVAPPPKTQRLLHSEAYLKYIEGLSAESNSISKWDQTLAARRRDVHLSKEQESRLPSHWLKSKGAHTTMADALWRLRDLMLRDTLNIRQAYNLENV', 1634, 'Q8BSQ9; E9QPW1; Q05C64; Q05CL6; Q7TMP1; Q7TNU2; Q9CV51;', 'KD00381', 'Mus musculus (Mouse)', 'Pbrm1', '#Protein polybromo-1#BRG1-associated factor 180#BAF180', '-', '-', '-'),
(382, 'P70039', 'Adenomatous polyposis coli homolog', 'GO:0000776===k', 310882, 'Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. {ECO:0000250}.', 'MAAASYDQLVKQVEALTMENTNLRQELEDNSNHLTKLETEATNMKEVLKQLQGSIEDEAMASSGPIDLLERFKDLNLDSSNIPAGKARPKMSMRSYGSREGSLSGHSGECSPVPVGSFQRRGLLNGSRESAGYMEELEKERLLLIAEHEKEEKEKRWYYAQLQNLTKRIDSLPLTENFSMQTDMTRRQLEYEARQIRAAMEEQLGTCQDMEKRVQTRVGKIHQIEEEILRIRQLLQSQVAEAAERTPQSKHDAGSRDAEKLPDGQGTSEITASGNVGSGQGSSSRADHDTTSVMSSNSTYSVPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCIAMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARASGSAALDNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEQGMDQDKNPMPAPVDHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLINDHYSVTLRRYAGMALTNLTFGDVANKATLCSMKSCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALDVKKESTLKSVLSALWNLSAHCTENKADICSVDGALAFLVSTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNAKDQEGLWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSVPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKTTHRNKQRHKQNLCSEYALDSSRHDDSICRSDNFSIGNLTVLSPYINTTVLPGSSSPRPTMDGSRPEKDRERTAGLGNYHSTTESSGNSSKRIGIQLSTTAQISKVMDEVSNIHLVQENRSSGSASEMHCMSDERNSQRKPSSNHPQSNPFTFTKAESSTRGCPVAFMKMEYKMASNDSLNSVSSTEGYGKRGQVKPSVESYSEDDESKFFSYGQYPAGLAHKIQSANHMDDNDTELDTPINYSLKYSDEQLNSGRQSPTQNERWSRPKHIIDSEMKQSEQRQPRTTKTTYSSYTENKEEKHKKFPPHFNQSENVPAYTRSRGANNQVDQSRVSSNLSNNSKASKPHCQVDDYDDDKTTNFSERYSEEEQQEDETERQNKYNIKAYASEEHHGEQPIDYSRKYSTDVPSSAQKPSFPYSNNSSKQKPKKEQVSSNSNTPTPSPNSNRQNQLHPNSAQSRPGLNRPKQIPNKPPSINQETIQTYCVEDTPICFSRGSSLSSLSSAEDEIEGRERNSRGQESNNTLQITEPKEISAVSKDGAVNETRSSVHHTRTKNNRLQTSNISPSDSSRHKSVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLMFSRCTSGSSLDSFESHSIASSIASSVASEHMISGIISPSDLPDSPGQTMPPSRSKTPPPPQTVQAKKDGSKPIVPDEERGKVAKTAVHSAIQRVQVLQEADTLLHFATESTPDGFSCASSLSALSLDEPYIQKDVQLKIMPPVLENDQGNKAEPEKEFIDNKAKKEDKRSEQEKDMLDDTDDDIDILEECIISAMPRKPSRKNKKVPQPTPGKPPPPVARKPSQLPVYKLLSSQNRLQTQKHVNFTHSDDMPRVYCVEGTPINFSTATSLSDLTIESPPSEPTNDQPNTDSLSTDLEKRDTIPTEGRSTDDTDASKPLNPTTVLDEDKAEEGDILAECIHSAMPKGKSHKPYRVKKIMDQINHTSAATSSGNSRSMQETDKNKPTSPVKPMPQSIGFKERLKKNTELKLNPNSENQYCDPRKPSSKKPSKVANEKIPNNEERTKGFAFDSPHHYTPIEGTPYCFSRNDSLSSLDFEDDDIDLSKEKAELRKEKGTKDTDQKVKYKHENRAINPMGKQDQTGPKSLGGRDQPKALVQKPTSFSSAAKGTQDRGGATDEKMENFAIENTPVCFSRNSSLSSLSDIDQENNNKETEPLKQTGTSETQLGLRRPQTSGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKRKPSKIKNEVGKSRSNSVGGILAEEPDLTLDLRDIQSPDSENAFSPDSENFDWKAIQEGANSIVSRLHQAAAAGSLSRQGSSDSDSILSLKSGISLGSPFHLTLDKEEKTITSNKGPKILKPAEKSALENKKTEEEPKGIKGGKKVYKSLITGKSRSSSDFSSHCKQSVQTNMPSISRGRTMIHIPGVRASSPSTSPVSKKGPVFKNVPSKGSNENPSSSSSPKGTKPLKSELVYGSRPSSTPGGSSKGNSRSGSRDSASSRPSPQPLSRPLQSPGRNSISPGKNGISPPNKFSQLPRTTSPSTASTKSSGSGRMSYTSPGRQLSQPNLSKQSGLPKTHSSIPRSESASKSLNQNVNTGSNKKVELSRMSSTKSSGSESDRSERPALVRQSTFIKEAPSPTLRRKLEESASFESLSSSSRADSPPRSQTQTPALSPSLPDMALSTHSIQAGGWRKMPPNLNPAAEHGDSRRRHDISRSHSESPSRLPITRSGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKQQVCSFPGPRSECSSSAKGTWRKIKESEILETPSNGSSSTIAESNCSLESKTLVYQMAPAVSKTEDVWVRIEDCPINNPRSGRSPTGNSPPVIDNVLDQGQKEEAAKDCHTRHNSGNGNVPLLENRQKSFIKVDGLDTKGTDPKSLINNQQETNENTVAERTAFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSNGENSTSRPSQIPTPVTNSTKKRDSKTETTDSSGSQSPKRHSGSYLVTSV', 2829, 'P70039; P79934;', 'KD00382', 'Xenopus laevis (African clawed frog)', 'apc', '#Adenomatous polyposis coli homolog#Protein APC', '-', '-', '399455'),
(383, 'Q9P2D7', 'Dynein heavy chain 1; axonemal', 'GO:0003777', 493953, 'Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.', 'MEQPNSKGYSLGRTPQGPECSSAPAVQVGTHRGLEYNPGKILPGSDYGLGNPPALDPKLPHLPLPPAPPTLSDLGQPRKSPLTGTDKKYPLMKQRGFYSDILSPGTLDQLGEVCRGPRMSQNLLRQADLDKFTPRVGSFEVPEDFQERMEQQCIGSTTRLLAQTDFPLQAYEPKMQVPFQVLPGQHPRKIEIERRKQQYLSLDIEQLLFSQGIDSNKLMPRHLDHQHPQTIEQGHDPIFPIYLPLKVFDNEDFDCRTPREWINMGLEPGSLDRKPVPGKALLPTDDFLGHEDPKSQKLKYKWCEVGVLDYDEEKKLYLVHKTDEKGLVRDEMGRPILNAGVTTEGRPPLQVCQYWVPRIQLLFCAEDPCMFAQRVVQANALRKNTEALLLYNLYVDCMPSDGQHVISEQSLSKIKQWALSTPRMRKGPSVLEHLSSLAREVSLDYERSMNKINFDHVVSSKPETFSYVTLPKKEEEQVPERGLVSVPKYHFWEQKEDFTFVSLLTRPEVITALSKVRAECNKVTAMSLFHSSLSKYSHLEEFEQIQSQTFSQVQMFLKDSWISSLKVAMRSSLRDMSKGWYNLYETNWEVYLMSKLRKLMELVKYMLQDTLRFLVQDSLASFSQFISDTCCSVLNCTDDMVWGDDLINSPYRPRKNPLFIMDLVLDSSGVHYSTPLEQFEASLLNLFDKGILATHAVPQLEKLVMEDIFISGDPLLESVGLHEPLVEELRATIASAVSKAMIPLQAYAKEYRKYLELNNNDIASFLKTYQTQGLLAQEVREVVLTHLREKEILDSSLPSSIIIGPFYINTDNVKQSLSKKRKALATSVLDILAKNLHKEVDSICEEFRSISRKIYEKPNSIEELAELREWMKGIPERLVGLEERIVKVMDDYQVMDEFLYNLSSDDFNDKWIASNWPSKILGQIELVQQQHVEDEEKFRKIQIMDQNNFQEKLEGLQLVVAGFSIHVEISRAHEIANEVRRVKKQLKDCQQLAMLYNNRERIFSLPITNYDKLSRMVKEFQPYLDLWTTASDWLRWSESWMNDPLSAIDAEQLEKNVVEAFKTMHKCVKQFKDMPACQEVALDIRARIEEFKPYIPLIQGLRNPGMRIRHWETLSNQININVRPKANLTFARCLEMNLQDHIESISKVAEVAGKEYAIEQALDKMEKEWSTILFNVLPYKATDTYILKSPDEASQLLDDHIVMTQNMSFSPYKKPFEQRINSWENKLKLTQEVLEEWLNCQRSWLYLEPIFSSEDINQQLPVESKRYQTMERIWKKIMKNAYENREVINVCSDLRMLDSLRDCNKILDLVQKGLSEYLETKRSAFPRFYFLSDDELLEILSQTKDPTAVQPHLRKCFENIARLLFQEDLEITHMYSAEGEEVQLCFSIYPSSNVEDWLREVERSMKASVHDIIEKAIRAYPTMPRTQWVLNWPGQVTIAGCQTYWTMEVAEALEAGNLRSQLFPQLCQQLSDLVALVRGKLSRMQRAVLSALIVIEVHAKDVVSKLIQENVVSVNDFQWISQLRYYWTNNDLYIRAVNAEFIYGYEYLGNSGRLVITPLTDRCYLTLTGALHLKFGGAPAGPAGTGKTETTKDLGKALAIQTVVFNCSDQLDFMAMGKFFKGLASAGAWACFDEFNRIDIEVLSVVAQQITTIQKAQQQRVERFMFEGVEIPLVPSCAVFITMNPGYAGRTELPDNLKALFRPVAMMVPDYAMITEISLYSFGFNEASVLAKKITTTFKLSSEQLSSQDHYDFGMRAVKTVISAAGNLKRENPSMNEELICLRAIRDVNVPKFLQEDLKLFSGIVSDLFPTIKEEDTDYGILDEAIREACRNSNLKDVEGFLTKCIQLYETTVVRHGLMLVGPTGSGKSTCYRVLAAAMTSLKGQPSISGGMYEAVNYYVLNPKSITMGQLYGEFDLLTHEWTDGIFSSFIRAGAITSDTNKKWYMFDGPVDAIWIENMNTVLDDNKKLCLSSGEIIKLTEAMTMMFEVQDLAVASPATVSRCGMVYLEPSILGLMPFIECWLRKLPPLLKPYEEHFKALFVSFLEESISFVRSSVKEVIASTNCNLTMSLLKLLDCFFKPFLPREGLKKIPSEKLSRIVELIEPWFIFSLIWSVGATGDSSGRTSFSHWLRLKMENEQLTLLFPEEGLVFDYRLEDAGISGTNDSEDEEEEYKQVAWVKWMDSSAPFTMVPDTNYCNIIVPTMDTVQMSHLLDMLLTNKKPVLCIGPTGTGKTLTISDKLLKNLALDYISHFLTFSARTSANQTQDFIDSKLDKRRKGVFGPPLGRNFIFFIDDLNMPALETYGAQPPIELLRQWMDHGGWYDRKIIGAFKNLVDINFVCAMGPPGGGRNTVTPRLMRHFNYLSFAEMDEVSKKRIFSTILGNWLDGLLGEKSYRERVPGAPHIAHFTEPLVEATIMVYATITSQLLPTPAKSHYTFNLRDLSKVFQGMLMADPAKVEDQVQLLRLWYHENCRVFRDRLVNEEDRSWFDQLLKRCMEQWEVTFNKVCPFQPILYGDFMSPGSDVKSYELITSESKMMQVIEEYIEDYNQINTAKLKLVLFMDAMSHICRISRTLRQALGNALLLGVGGSGRSSLTRLASHMAEYECFQIELSKNYGMSEWRDDVKKVLLKAGLQNLPITFLFSDTQIKNESFLEDINNVLNSGDIPNLYTADEQDQIVSTMRPYIQEQGLQPTKANLMAAYTGRVRSNIHMVLCMSPIGEVFRARLRQFPSLVNCCTIDWFNEWPAEALKSVATVFLNEIPELESSQEEIQGLIQVCVYIHQSVSKKCIEYLAELTRHNYVTPKSYLELLHIFSILIGQKKLELKTAKNRMKSGLDKLLRTSEDVAKMQEDLESMHPLLEEAAKDTMLTMEQIKVDTAIAEETRNSVQTEEIKANEKAKKAQAIADDAQKDLDEALPALDAALASLRNLNKNDVTEVRAMQRPPPGVKLVIEAVCIMKGIKPKKVPGEKPGTKVDDYWEPGKGLLQDPGHFLESLFKFDKDNIGDVVIKAIQPYIDNEEFQPATIAKVSKACTSICQWVRAMHKYHFVAKAVEPKRQALLEAQDDLGVTQRILDEAKQRLREVEDGIATMQAKYRECITKKEELELKCEQCEQRLGRAGKVRTLLLQGLQAGPAQTGARKDQGAGGSWGGCPHPLPGNPGATVGRASPRPLAQPPRAHPTGLPLQLINGLSDEKVRWQETVENLQYMLNNISGDVLVAAGFVAYLGPFTGQYRTVLYDSWVKQLRSHNVPHTSEPTLIGTLGNPVKIRSWQIAGLPNDTLSVENGVINQFSQRWTHFIDPQSQANKWIKNMEKDNGLDVFKLSDRDFLRSMENAIRFGKPCLLENVGEELDPALEPVLLKQTYKQQGNTVLKLGDTVIPYHEDFRMYITTKLPNPHYTPEISTKLTLINFTLSPSGLEDQLLGQVVAEERPDLEEAKNQLIISNAKMRQELKDIEDQILYRLSSSEGNPVDDMELIKVLEASKMKAAEIQAKVRIAEQTEKDIDLTRMEYIPVAIRTQILFFCVSDLANVDPMYQYSLEWFLNIFLSGIANSERADNLKKRISNINRYLTYSLYSNVCRSLFEKHKLMFAFLLCVRIMMNEGKINQSEWRYLLSGGSISIMTENPAPDWLSDRAWRDILALSNLPTFSSFSSDFVKHLSEFRVIFDSLEPHREPLPGIWDQYLDQFQKLLVLRCLRGDKVTNAMQDFVATNLEPRFIEPQTANLSVVFKDSNSTTPLIFVLSPGTDPAADLYKFAEEMKFSKKLSAISLGQGQGPRAEAMMRSSIERGKWVFFQNCHLAPSWMPALERLIEHINPDKVHRDFRLWLTSLPSNKFPVSILQNGSKMTIEPPRGVRANLLKSYSSLGEDFLNSCHKVMEFKSLLLSLCLFHGNALERHKFGPLGFNIPYEFTDGDLRICISQLKMFLDEYDDIPYKVLKYTAGEINYGGRVTDDWDRRCIMNILEDFYNPDVLSPEHSYSASGIYHQIPPTYDLHGYLSYIKSLPLNDMPEIFGLHDNANITFAQNETFALLGTIIQLQPKSSSAGSQGREEIVEDVTQNILLKVPEPINLQWVMAKYPVLYEESMNTVLVQEVIRYNRLLQVITQTLQDLLKALKGLVVMSSQLELMAASLYNNTVPELWSAKAYPSLKPLSSWVMDLLQRLDFLQAWIQDGIPAVFWISGFFFPQAFLTGTLQNFARKFVISIDTISFDFKVMFEAPSELTQRPQVGCYIHGLFLEGARWDPEAFQLAESQPKELYTEMAVIWLLPTPNRKAQDQDFYLCPIYKTLTRAGTLSTTGHSTNYVIAVEIPTHQPQRHWIKRGVALICALDY', 4330, 'Q9P2D7; B0I1R6; O00436; O15435; O95491; Q6ZU48; Q86YK7; Q8TEJ4;Q92863; Q9H8E6; Q9UFW6; Q9Y4Z7;', 'KD00383', 'Homo sapiens (Human)', 'DNAH1', '#Dynein heavy chain 1; axonemal#Axonemal beta dynein heavy chain 1#Ciliary dynein heavy chain 1#Heat shock regulated protein 1#HSRF-1#hDHC7', '-', 'ENSG00000114841', '-'),
(384, 'Q9JHU4', 'Cytoplasmic dynein 1 heavy chain 1', 'GO:0003777===GO:0005868', 532045, 'Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.', 'MSEPGGGEDGSAGLEVSAVQNVADVAVLQKHLRKLVPLLLEDGGDAPAALEAALEEKSALEQMRKFLSDPQVHTVLVERSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRAPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPFFKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPIITNVAKQCYERGEKPKVTDFGDKVEDPTFLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDTGLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRKLMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVIVRVLRPQVTAVAQQNQGEAPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRDLPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTIESARVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNTISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNRVQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVHELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAVMGIVTEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKYDSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQRFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQALTIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLRQNLDGLLNQLKNFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQKNEAVVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDALSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRSLERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSREGEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSENVENALSNVGGGGDVGPLQSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLSQMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCELLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKALERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDNVRGELQKRQWIVFDGDVDPEWVENLNSVLDDNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKGKEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFKLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFPMQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNVPIIDYEVSISGEWSPWQAKVPQIEVETHKVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDMVALKHFPNIDKEKAMSRPILYSNWLSKDYIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNYIVPDYMPVVYDKLPQPPTHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEISDAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQVHFLYQYSLQFFLDIYHNVLYENPNLKGATDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGKEIVLSAGSTPKIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPTTPIGQAIHRLLLIQAFRPDRLLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQADKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRTFSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPWSALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDAQTPSWLGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKARTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSPLKRTVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQLQNISQAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTASQSATLDACSFGVTGLKLQGATCSNNKLSLSNAISTVLPLTQLRWVKQTSAEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGVAVLCTE', 4644, 'Q9JHU4; E9QM71;', 'KD00384', 'Mus musculus (Mouse)', 'Dync1h1', '#Cytoplasmic dynein 1 heavy chain 1#Cytoplasmic dynein heavy chain 1#Dynein heavy chain; cytosolic', '-', '-', '13424'),
(385, 'Q1JQB2', 'Mitotic checkpoint protein BUB3', 'GO:0000777===GO:0008608', 36955, 'Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1 (By similarity). {ECO:0000250}.', 'MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMVTGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAETKPKST', 326, 'Q1JQB2; A5D9G0;', 'KD00385', 'Bos taurus (Bovine)', 'BUB3', '#Mitotic checkpoint protein BUB3', '-', '-', '539594'),
(386, 'P70032', 'Serine/threonine-protein kinase PLK1', 'GO:0000776===c;k;m', 68212, 'Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle; including the regulation of centrosome maturation and spindle assembly; the removal of cohesins from chromosome arms; the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors; and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates cdc25; pkmyt1/myt1; stag2/sa2; tpx2. Plays multiple essential roles during mitosis. Phosphorylates the N-terminal domain of cdc25; which leads to cyclin b-cdc2 activation and mitotic entry. Also required for organization of bipolar spindles; and for exit from mitosis. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating stag2/sa2. {ECO:0000269|PubMed:10567586; ECO:0000269|PubMed:11931760; ECO:0000269|PubMed:11994303; ECO:0000269|PubMed:15692562; ECO:0000269|PubMed:15964272; ECO:0000269|PubMed:19351716; ECO:0000269|PubMed:19556869; ECO:0000269|PubMed:8703070; ECO:0000269|PubMed:9831560}.', 'MAQVAGKKLTVAPEAAKPPGIPGSSSAVKEIPEILVDPRTRRRYLRGRFLGKGGFAKCYEITDLESREVFAGKIVPKTMLLKPHQKDKMTMEIAIQRSLDHRHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRRKAVTEPEARYYLKQTISGCQYLHSNRVIHRDLKLGNLFLNDEMEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLGKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYMRIKKNEYSIPKHINPVAAALIQKMLRSDPTSRPTIDDLLNDEFFTSGYIPSRLPTTCLTVPPRFSIAPSTIDQSLRKPLTAINKGQDSPLVEKQVAPAKEEEMQQPEFTEPADCYLSEMLQQLTCLNAVKPSERALIRQEEAEDPASIPIFWISKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLIMYNDGDSLQYIERNNTESYLNVRSYPTTLTKKITLLKYFRNYMSEHLLKAGANTTPREGDELARLPFLRTWFRTRSAIILHLSNGTVQINFFQDHTKIILCPLMAAVSYIDEKREFRTYKLSLIQEFGCCKELASRLRYARTMVEKLQSSKSAVAHVKASA', 598, 'P70032; Q7ZWQ6;', 'KD00386', 'Xenopus laevis (African clawed frog)', 'plk1', '#Serine/threonine-protein kinase PLK1#2.7.11.21#Plx1#Polo-like kinase 1#PLK-1', '-', '-', '380481'),
(387, 'Q9NP97', 'Dynein light chain roadblock-type 1', 'GO:0003777===GO:0005868===c;k;m', 10922, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.', 'MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYASLMHSFILKARSTVRDIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE', 96, 'Q9NP97; B1AKR5; Q5TC72; Q96IV3; Q9NQM2;', 'KD00387', 'Homo sapiens (Human)', 'DYNLRB1', '#Dynein light chain roadblock-type 1#Bithoraxoid-like protein#BLP#Dynein light chain 2A; cytoplasmic#Dynein-associated protein Km23#Roadblock domain-containing protein 1', '-', 'ENSG00000125971', '-'),
(388, 'Q13561', 'Dynactin subunit 2', 'GO:0000776===c;k;m', 44231, 'Modulates cytoplasmic dynein binding to an organelle; and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development.', 'MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELTSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGEYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVLLAKQLAALKQQLVASHLEKLLGPDAAINLTDPDGALAKRLLLQLEATKNSKGGSGGKTTGTPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELETAVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQSKVHQLYETIQRWSPIASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMIANSLKDNTTLLTQVQTTMRENLATVEGNFASIDERMKKLGK', 401, 'Q13561; B2RBK5; Q86YN2; Q9BW17;', 'KD00388', 'Homo sapiens (Human)', 'DCTN2', '#Dynactin subunit 2#50 kDa dynein-associated polypeptide#Dynactin complex 50 kDa subunit#DCTN-50#p50 dynamitin', '-', 'ENSG00000175203', '-'),
(389, 'Q39565', 'Dynein beta chain; flagellar outer arm', 'GO:0003777', 519972, 'Force generating protein of eukaryotic cilia and flagella. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.', 'MAEDEGMTAAAPSSSVKDIRFDYIRDRVCSCLKVPDSAYDKLVSGDGRTSLVQFMEEAHTKRLLIMLDGKDLSATVKPPPKFKKKTVYFLKLQETKLDNDNIKKLVIHGEISENPLETLAAISQDVFMPVLTAPANQQGWPDVVAKEVTENLHKFVSNVFVTIGQMKGQTLLPLPPQNTVPTLQPEQSMHSLKDQDKIHILESAIVTWTKQIKNVLKADPDAPLKEPGAYPGPLTELNFWSERAANLNSIHEQLTSEKTQKVVKVLELAKSTYYPAFQRLFREVEAAQQEANDNVKFLKPLRKYLDKLNMMDDFPMLVDLFKPIMHTLMLIWKHSKSYNSSTRFVTLMQEICNDLIMQACKYVPGSDLIQMEPSEAVDKLRMTLRWLGTFKNYYFEYRALSMQDTPENPWKFQNNSLFARLDSFLERCHDMMDLMSTCMQFNRLERVEIGGTKGKVLTNGVKAIHQDFTSAVEKFQQVTYDVMDVDAKQFDEDFFGFRVVIKELERRLAAIIIQAFDDCTTIGTTFKLLDSFEGLLDREVIAHDLEKKHTDLLHSYARDLKDVADLFHQYKDRPIVAKNSAPYSGAAYWVRGLMERIKDPMDRLLTMNKMVLESELFREIQRTYDHLWEEMTEYRTRAVDAWCAQVAATSDEKLNLPLLSLIEETADGIRVLGVNFDPALVRLLRETKYFLLLETSTQDKNADRNAEKAAEGGEVEVVKKAPKLSVPDSAKDLFASADTFRQQISALDLICSIYNKVQRTILAVEKPLVQQKLDAVEQALNRGLAELNWKCAEIDTYIKECMELVKDVDLVLNTIKDNVKATQGILAMWEKNLMFERKDGKTYTFDELNDAFNQLIQQRHSEIRDAGKEITKLLSSSNRVLKVSKGAASWRAYVDYFSNIVIDGFSAAIISTVRYLLSQIDPDILAKTESSPLLEIQVELVAPDIVWKPDLGEGGAKPGLRDMIKKWLQSFLEIGQLMKRLDVGEGNYAKELEEDFEVYDALNQVMMVTLANESRCEDFKNQFAKFDYLWKQDLQATLQQFITDNGVTLPDGTRDDPPLAKFEEQIVKYKNVASEIASFKDTMTMGYVKVNAKPLRQALSTWASKWVYLFTHYLQEKVVNSITELYTFMDTSNSTLDLKVMGEGVEEEPEYHPDQDPEEAAAKKAAEEEEKRKALYAIMACMRDIRRRTERGTDTMFEPLKETVTALHTFGIQLSDTVLHQLDNAEFNWRTLKKKMLNRREQLAPLQQAEAVEIRRKSDAFNERVEDFRTFFQRKAPFAVSGGELKLEQVKPAYKLLDEFRSGSLEGYPSVLGIIAESKQLQEAQDLFELYQPGYLQLQRCSEELGHLKSLWDTVGTVMFTFRDWYKTPWDKIDVDFLVEETKKLSKDIKMLNKAVRNYDVYRMLEEAIKAVLTSLPLVQDLHHPAMRERHWKLLMQTTGKHFVMDDKFCLGDLLALELHNYVDACSEIVDRAQKELNIEKQLKKIEDTWAGLSLAFSTYQDSDVMALLVDDAVNEALEADNLQLQNLSGQKYVQSNPMFLETVSKWQNNMGRVSAVLETWQNVQKKWQNLESIFIGSADIRVQLPEDSKRFDAVNADFQELMRTAPDITNVVEACTLDGRQERLENMQSMLEQCEKALQEYLETKRVAFPRFYFVSPADLLDILSKGSNPQLILRHLQKCFDNIDNLSFRKDERGDPTKIATHMHSKEGEVVEFVEDCSCDGPVEVWLQNVVDSMKLALQVEFRKAIPTYDELPRTKWIYVYSAQNTVVVSRTFFTQEINEAFDDLEEGNEEALKVELDRQVQQLADLIDEINKEQTSLDRKKLITLCTIDVHSRDLVQKLIDERVEDQMCFQWQSQLRYIQSEKTKTCQVNICDAEIAYSYEYIGNCGCLCITPLTDRCFITLTQAQRLVLGGAPAGPAGTGKTETTKDLARALGIQCYVFNCSDQMDYKAMGHTYKGLAQTGAWGCFDEFNRIPVAVLSVCSTQYKTVLDAIRAKKERFTFEDADISLKSTVMAFITMNPGYPGRAELPESLKALFRPVSMVVPDLALICEIMLMAEGFQMSKILSRKFVILYKLCEDLLSKSRHYDWKLRAIKTTLYVAGGMKRAAPELSEDKVLLRALRDFNLGKLTADDTSIFMGLLNDLFPKTLELVPRALDKAFDEAAHKAATELGYQPDDQFLLKISHVRELFVVRWSVFLLGAAGCGKTAVWRTLLRAQNSSGEKTIYQAVNPKAVTRNELYGYLHPATREWKEGLMSVTFRNMANNKTNKHQWIVLDGDIDAEWIESMNTVMDDNKMLTLASNERIPLTPSMRLLLEINHMVHCSPATVSRGGVIFINADDVGWQPVVASWIDKLEAAEYRPLLTALFTKYVDPCLEHCRRNFKTVVPLPAVNQAMTICKILEGILPKETVRGAPPPDKKLLHYHFVFACVWAFGGCMLVDKVTDYRTQFSKWWVSEWKDVQFPEKGLVYDYYVDEQNCIMVPWEDRVTKFQYIPGDFTSLFVPTVETTRLTYFLDSLVSNKHYAMFVGNTGTGKSAIMVNKLRNMDTETMSFYTINMNSLSEAPALQVILEQPLEKKSGVRYGPPGSRRMVYFVDDMNMPLVDKYDTQSSIELLRQMVDYHGWYDKVKIQLKEIINCQMAACMNPTAGSFNITPRMQRHFVTFAVQMPNAEITRAMYYQIIDGHFSSFDVDVAKMSNKLVDATCELHRNVMHNFLPSAVKFHYQFNLRDLSNITQGLTRAIKEYYREPVKVARLWVHECERVFRDRMINEADMAKFDEFRVAVTKKFFDDCGGMVAIEERPLIYASHASMTYTPEDVPVYNALSSYDVLRKTLEDKLREYNESNAVMDLVLFQQAMEHVTRIARIIDLPRGNAMLVGVGGSGKQSLARLASYICGYEVYQISVSSTYGINDFKENLLGLYRKAGTKGTPITFLMTDNQIVKEGFLVYINDLLSTGYIADLFTPEDKEAFTNAVRNEVKAAGILDSAENCWDFFIDKVRKFLHIVLCFSPVGDKFRIRARQFPALVNCTMFDWFHGWPGEALVSVAQRFLVDVPNMEEVVRENIAYHMAYAHQCVSEASERFKEAFRRYNYTTPKSYLELISLYKMLLQLKRDDLRRSKERLENGIDKIAQAAAQVTDLQRVLKEEQIVVDEKKAQTDELIVSIGKEKAIVDQAVEAGREDEEAATALQTEVSAFQAECERDLLEAEPIIAQAEAALNSLNKKELSELKSFGSPAAEIVQVAAACLVLTCGGKIPKDRDWNAGKKMMADVNSFLSSLMNFDKDNVPVVCVEVVEKDYISNPGFTPDNIKGKSAACAGLCSWVINICKYFRIYQVVAPKRAALAEANKKLDTANKKLKVIRDEVKRLQDRVALLEQSLMKATEDKNAAIAQADRTARKAQMAERLINGLSGENTRWGAEIKRLESLEGRLVGDVLIASAFVSYAGPFNMQFRKSLVDEKWLPDIIERQIPMTQGIRPLDLLTDDATKAKWANEGLPTDPLSVENGAIMSNASRWALMIDPQLQGIKWIINKETNNGLVIIQQSQPKYIDQVINCIENGWPLLIENLPVDIDAVLDPVIGKMTIKKGRNIIMKIGDAEVQYDSRFRLYLQTKLSNPHFKPEVAAQTTLVNFCVTEKGLEDQLLALVVDHERPDLQEQAAGLVRSLNEYNITLVELENNLLFNLANATGNILENIELIEGLEETKRTAVEIEEKVKLAKQTEIQIAKAREVYRPVATRGSLTYFLIDNLNALDRVYHYSMANFVFVLKKGMDMTPGGKDESKVPLAERLNQEVDLDKRVELLVETTCFVLIGYVAQGLFERHKLIVATQLCMQILRSRGELHYAKFEYLLRGPKVMGADNPLHDWVSDSVWGSVQALKELDDYQGLPEDLIGSSKRWREWMELERPEDEPLPGDWKRMQEFDKLLLFRALRPDRLTSAMGRFVTNMLGAKYVTSQPYDLERSYQDASPGTPIFVFLSPGVDVAGSVEALGKKLGFTLDNGKYASVSLGQGQEPIAMDRLSAAHKNGGWVLLQNIHLTIDWTTNQLDKKVDKLVEGAHPDFRLFLSAEPPPSLERGLPISLLQNSIKLTNEPARGLKANLRRAWNNFNEEILESCAKQAEFRAIVFALCYFHAALLERKKFGVGNLPGARSGIGWNMNYPFNTGDLLCCGQTANNYLENNVKVPWEDLRYNFGEIMYGGHIVEDYDRRLAMCYLRKYVNEGLLDNMEFFPGFAMPPNTANHRQVLEFIDEVMPPETPLAFGLHPNAEIGFKLREAESFCNSLVQLQPRESSGEGGMSAEERAKLVLDEVVDKLPDIFDMEDVRSKINPDDPNMPFVMVAIQESERMNMLLAEMKRSLLELDLGLKGDLTMTEPMERLLKALATDAVPGSWRNLAYPSLRPLGSWLGNLLARHAQLVDWTAELSTPKAVWLSGLFNPQSFLTAVMQATARRNDWPLDKTVIITEVTKKQPDQIEANSRDGAFIHGLTLEGARWDDKIGALDDSKPKELFCPMPVILVRAVTQDKAEMKDVYKCPVYTTEARFREEVFEAQLKSKHTEIKWVLAGVCLFLDVV', 4568, 'Q39565;', 'KD00389', 'Chlamydomonas reinhardtii (Chlamydomonas smithii)', 'ODA4', '#Dynein beta chain; flagellar outer arm', '-', '-', '-'),
(390, 'Q3TJM4', 'Centromere protein T', 'GO:0000776===GO:0000777===GO:0051382', 56242, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome- associated complex that binds specifically to histone H3- containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis (By similarity). {ECO:0000250}.', 'MADLSFSDGDPTVRTLLRRVLETADSRTPMRRRSTRINAQRRRSQTPYSNRQGSQTKTSARKQSHGARSVGRSTRVQGRGRLEEQTPRTLLRNILLTAPESSTVMPDPVVKPAQVPEVARSSRRESSRGSLELHLPELEPPSTLAPGLTAPGKRKQKLRLSVFQQEVDQGLPLSQEPRRSRSADVSSLASSFNLTFVLPGQPETVERPGLARRRPIRQLVNAGALLQDLEDNSLASALPGDSHRTPVAALPMDVGLEDTQPFSQSLAAFSLSGKHSLPSPSRPGVEDVERVMGPPSSGTRLQSRMSRSGPAASPSPFLEPQPPPAEPREAVGSNEAAEPKDQEGSSGYEETSARPASGELSSSTHDSLPAEQPPPSPGVAVLSSEPLESVTAKCPSRTQTAGPRRRQDPHKAGLSPYVKFFSFCTKMPVEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMRRQGLVTDQVSQHVLVERYLPLEYRQQLIPCAFSGNSVFPAQ', 515, 'Q3TJM4; Q3TPY6; Q3UPD2; Q8BTH0; Q8BTP2; Q8R5E9;', 'KD00390', 'Mus musculus (Mouse)', 'Cenpt', '#Centromere protein T#CENP-T', '-', '-', '320394'),
(391, 'Q9V3A7', 'Condensin subunit SMC4GluonLD13578p', 'k', 159883, '', 'MQKARPSKGTPKAAGGARQSGQFRVPQLTAQQQLRAQQQQEEEDAAVDALDDALIFDDEEGGTRIGDIYIPPPVPPHCSMESTGPRLIISKIVNRNFKSYAGEVELGPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLIHSSSSYPNLRSCSVAVHFKQIVDKGDGTCEDVPDSSIVIERTAMSDNSSYYQINDKRAQLKDVAKLLKKHHVDLEHNRFLILQGEVESIAMMKPKGQTENETGMLEYLEDIVGTQRYIRPLQQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNKVLDFLMRMKMEGKIPGILGRLGDLGGIDAKYDIAISTACGRLDNIVTDNYETASAAIGALKEYNVGRATFITLDKIEHHRREANSRINTPENVPRLYDLVKVEDDRVRTAFYFALRNTLVCDDLEQGTRIAYGRERYRVVTLRGEMIEMTGTMSGGGSRPIRGKMGTQVRTKTAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTTDERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRNESVKPVEAKIKKVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIKKEIDEITKEENKRNIERIEIDTKLQAAAGKMNKVKNDIPGWQAQLAPLKLNEIPGETEPQAPLKELNEEELEAETLEALQYKQTMLEEDLKTKKPNLSCIKEFNEKRLVYLDRVRVLEDITSKRNEMRDKYEEVRKRRYKEFMDGFSIITRKLKEMYQMITLGGDAELELVDSMDPFTEGVNFTVRPPKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELANFLVGIYKVSDCTDSITMLNYPPTLPTQSPVVANSQYVGGTIEGDNTIAAENQDDTPTKKSQSPPSEQIVRLISELGRDTTFAPPLESTVRDTILAQNLKQAATEVAAQPSDATGRVTTDVSLASPPSSPAILNV', 1409, 'Q9V3A7;', 'KD00391', 'Drosophila melanogaster (Fruit fly)', 'glu', '#Condensin subunit SMC4 {ECO:0000313|EMBL:AAF01416.1}#Gluon {ECO:0000313|EMBL:AAF53560.1}#3.6.1.3 {ECO:0000313|EMBL:AAF53560.1}#LD13578p {ECO:0000313|EMBL:ABX00747.1}', '-', '-', '35001'),
(392, 'P14635', 'G2/mitotic-specific cyclin-B1', 'GO:0000942===GO:0051987===c;k', 48337, 'Essential for the control of the cell cycle at the G2/M (mitosis) transition. {ECO:0000269|PubMed:17495531; ECO:0000269|PubMed:17495533}.', 'MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV', 433, 'P14635; A8K066; Q5TZP9;', 'KD00392', 'Homo sapiens (Human)', 'CCNB1', '#G2/mitotic-specific cyclin-B1', 'BIOMD0000000196,Srividhya2006_CellCycle;', 'ENSG00000134057', '-'),
(393, 'Q2HJJ0', 'Kinesin light chain 4', 'GO:0003777', 68220, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity). {ECO:0000250}.', 'MSGLVLGQRDEPAGHRLSQEEILGSTRLVSQGLEALHSEHQAVLQSLSQTIECLQQGGHEEGLVHEKARQLRRSMENIELGLSEAQVMLALANHLSTVESEKQKLRAQVRRLCQENQWLRDELAGTQQRLQRSEQAVAQLEEEKKHLEFLGQLRQYDEDGHAAEEKEGDASKDSLDDLFPNEEEEDPSNGLSRGQGAQHSGYEIPARLRTLHNLVIQYAAQGRYEVAVPLCKQALEDLERTSGRGHPVVATMLNILALVYRGQNKYKEAALLLNDALSIRESTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCQRALEIREKVLGTNHPDVAKQLNNLALLCQNQGKYEAVERYYRRALAIYEGQLGPDNPNVARTKNNLASCYLKQGKYAEAETLYKEILTRAHVQEFGSVDDDHKPIWMHAEEREEMSKIRHREGSTPYAEYGGWYKACKVSSPTVNTTLRNLGALYRRQGKLEAAETLEECALRSRKQGTDPISQTKVAELLGEGDSGRTSQEGLGGSVKFEGGEDASVAVEWSGDGSGALQRSGSLGKIRDVLRRSSELLVRKLQGSEPRPSSSNMKRAASLNYLNQPSAAPLQVSRGLSASSMDLSSSS', 616, 'Q2HJJ0;', 'KD00393', 'Bos taurus (Bovine)', 'KLC4', '#Kinesin light chain 4#KLC 4#Kinesin-like protein 8', '-', '-', '-'),
(394, 'Q6CKH5', 'DASH complex subunit DAD3', 'GO:0008608===GO:0042729', 9816, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MSSELTPLQRSVLDKYRFLAESLRELSETLSDLNNTHEDSKPEAILQEMREIEVKISLVSTLLKGSVYSLVIQRRMDHQQKPSDL', 85, 'Q6CKH5;', 'KD00394', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'DAD3', '#DASH complex subunit DAD3#Outer kinetochore protein DAD3', '-', '-', '2895731'),
(395, 'P91945', 'Kinesin-like protein', 'c;k', 92440, '', 'MPSEQHTNIKVAVRVRPYNVRELEQKQRSIIKVMDRSALLFDPDEEDDEFFFQGAKQPYRDITKRMNKKLTMEFDRVFDIDNSNQDLFEECTAPLVDAVLNGYNCSVFVYGATGAGKTFTMLGSEAHPGLTYLTMQDLFDKIQAQSDVRKFDVGVSYLEVYNEHVMNLLTKSGPLKLREDNNGVVVSGLCLTPIYSAEELLRMLMLGNSHRTQHPTDANAESSRSHAIFQVHIRITERKTDTKRTVKLSMIDLAGSERAASTKGIGVRFKEGASINKSLLALGNCINKLADGLKHIPYRDSNLTRILKDSLGGNCRTLMVANVSMSSLTYEDTYNTLKYASRAKKIRTTLKQNVLKSKMPTEFYVKKIDEVVAENERLKERNKALEAKATQLERAGNSGFDPLELKTWYSKIDAVYAAARQLQEHVLGMRSKIKNINYRQTLKKELEEFRKLMCVDQRVCQEDFRRFANYMSTLTSQMEKYKEELPSWLSKMEIAYQDLESLKREVNKSKAYQILIVYVKYKDLELQLTKQNIFNNHVNAINQELVENLDLMRKSFRTACEVLNQTYDRLEDGQKLTPEIEAVFERLLRKMRFADSEANTKMAEMNPLVVPMALRSSGQEEEEPTCSLTASAKKRQRQAAQSDDDLHLSMEDFDSQDTESDSEELHRTFKRPRNLNETQVLGPCSSSSSSSTSSSSSARKALTATVTKQRNVQQRLVSDLISDQNVRGGNEKIKKALLKSNHFTAQGLQRTLAAASLAKENVKYNANYVRKSPRALMAKALAGTSTLARKPLGSASKEPPLVKFNRAASFRLKK', 814, 'P91945;', 'KD00395', 'Drosophila melanogaster (Fruit fly)', 'Klp67A', '#Kinesin-like protein {ECO:0000256|RuleBase:RU000394}', '-', '-', '-'),
(396, 'A8PUI7', 'Spindle and kinetochore-associated protein 3', 'GO:0000940', 44762, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it mediates the microtubule-stimulated oligomerization (By similarity). {ECO:0000250}.', 'MDPIRGFCGKLRSLAVTLDSETARLQRALDGEDSDFEDCPMRVLHDLNSEVRILKDDVNILLDKANLESQENIGFIKATKILMRKNSMDIMKIKEFFQKYGYTPRAKKNSVDEQEVTDSKPESSECERPEKPDLKDDLLDSAAASTSVSEKSPRSPQLSDFGLERYIVSQVLPNPPQAVNNQKEEPKILTPFSKHSLLKTPKCALKMDDFECVTPKLEHFGISEYTMCLNDDYTIGLKNVKTNSETIETEPVPNDNVFATPGLITQPLGKNNAEHTHSPLAPTFCTPGLKVPSTKTSTAMVSTNSSSNDLETKESTSLVSNSDECFENFADPSSPTISSYENLLKTPTPPEVTTIPEDIRQILSKYNSNLASPVAVRAVSPINVFLPRHGGQNMRDASNKENW', 403, 'A8PUI7;', 'KD00396', 'Bos taurus (Bovine)', 'SKA3', '#Spindle and kinetochore-associated protein 3', '-', '-', '509921'),
(397, 'Q53HL2', 'Borealin', 'GO:0032133===k;m;s', 31323, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex; it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment. {ECO:0000269|PubMed:15249581; ECO:0000269|PubMed:15260989; ECO:0000269|PubMed:16571674; ECO:0000269|PubMed:18243099}.', 'MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK', 280, 'Q53HL2; D3DPT4; Q53HN1; Q96AM3; Q9NVW5;', 'KD00397', 'Homo sapiens (Human)', 'CDCA8', '#Borealin#Cell division cycle-associated protein 8#Dasra-B#hDasra-B#Pluripotent embryonic stem cell-related gene 3 protein', '-', 'ENSG00000134690', '-'),
(398, 'Q8R2U0', 'Nucleoporin SEH1', 'GO:0000777===GO:0051315', 39775, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (By similarity). As a component of the GATOR2 complex; inhibits GATOR1 complex; an inhibitor of the amino acid-sensing branch of the TORC1 pathway (By similarity). {ECO:0000250}.', 'MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRVYEAPDVMNLSQWSLQHEVSCKLCCSCISWNPSSSRAHPPMIAVGSDDSSPNSMAKVQIFEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHILAVATKDVRIFTLKPLRKELTSSGGPTKFEIHIVAQFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILKGNGSPVNGSSQLGNSNPSLSSNIPNLQNSLNGTSASRKHS', 360, 'Q8R2U0; Q3TLC9; Q3UP79; Q9D0K7;', 'KD00398', 'Mus musculus (Mouse)', 'Seh1l', '#Nucleoporin SEH1#Nup107-160 subcomplex subunit SEH1', '-', '-', '72124'),
(399, 'A1L1L1', 'Centromere protein W', 'GO:0000776===GO:0000777===GO:0051382', 9803, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPW has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis (By similarity). {ECO:0000250}.', 'MVLSTTVCRRIRRKAPCAFLKRTLKQKKPRLSLEKRCDLLIHLNCLLFVQKLAEESRTNACESKSGVIKKDHVQAAAKVILKKSRG', 86, 'A1L1L1;', 'KD00399', 'Rattus norvegicus (Rat)', 'Cenpw', '#Centromere protein W#CENP-W#Cancer-up-regulated gene 2 protein', '-', '-', '689399'),
(400, 'Q45VK7', 'Cytoplasmic dynein 2 heavy chain 1', 'GO:0003777===GO:0005868', 492339, 'May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis. According to PubMed:8666668; it may play a role in transport between endoplasmic reticulum and Golgi or organization of the Golgi in cells. {ECO:0000269|PubMed:16061793; ECO:0000269|PubMed:16229832; ECO:0000269|PubMed:8666668}.', 'MAGSLGDVRKLFLFTTTQNYFGLRPELWDQPPLSNCPEVNNFLDDGNQMLLRVQRSEAGLAFSNTIDFDDAKDKVLVFFKLRPEVITDGNLHNNILVSSMLESPINSLYQAVRQVFAPMLLKDQEWSRNFDPKLQNLLSELEAGLGIVLRKSDTNLPKLKLKEDDTRGILTPSDEFQFWIEQAHRGSKQISKERASYFKELFETISREFYNLDSLSLLEVVDLVETTRDVVDDVWRQTEHDHYPESRMLHLLDVIGGSFGRFVQKKLGSLKLWEDPYYLVKENLKAGISICEQWVIVCSHLTGQVWQRYVPHPWKSGKYFPETLDKLGKRLEEVLAIRTIHEKLLYFLPASEERIVCLSRVFEPFTGVNPVQYNPYTEPLWKAAVSQYEKIIAPAEQKIAGKLKNYISEIQDSPQQLLQAFLKYKELVKRPTISKELMLERETLLARLGDSAKDFRLDFENRCRGIPGDPSGPLSGKNLSEVVNNIVWVRQLELKVDDTIKIAEALLSDLSGFRSFHRSAEDLLDQFKLYEQEQFDDWSREVQSGLSDSRSGLCIEANSRIMELDPNDGALKVHYSDRLVILLREVRQLSALGFVIPAKIQQVANVAQKFCKQAIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNSKAGSGGKSQITWDNPKELEGYIQKLQNAAERLATENRRLRKWHTTFCEKVVILMNIDLLRQQQRWKDGLQELRTGLATVAAQGFQASDMRAWRQHWNHQLYKALEHQYQVGLEALNENLPEINVDLTYKQGRLQFRPPFEEIRAKYYREMKRFIGIPNQFKGVGEAGDESIFSVMIDRNASGFLTIYSKAEDLFRRLSAVLHQHKEWVVIGQVDMEALVEKNLSTVHDWEKNFKALKIKGKEVERLPSAVKVDCLNINCSPVKTVIDDLIQKLFDLLVLSLKKSIQTHIHEIDTFVTEAMKVLTVIPQSVEEIGDTNVQYSNLQDRRPEILPLFQEAEDKNRLLRTVAGGGVETVSNLRAKWDKFELMMESHQLMIKDQIEVMKGNVKSRLQIYYQELDKFKARWDQLKPGDDIIETGQQNTMDQSAKSIKEKKIEFDDLEVIRKKLVDDCHHFGLEEPNFSLAYSISKDIESCAQIWALYEEFQQGLQDMAKEDWITYRAKIYLFEEFLINWHERLRKIEEHSVMTVKLQSEVDRYKMIIPILKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVADTIVEKASELKDLNSRAQGEVTIREALRELDLWGVGAVFSLIDYEDSQNHTIKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAQLDEYLQNLNHIQRKWVYLEPIFGRGALPKEQTRFNKVDEDFRSIMMDIRKDSRVTTLTTHAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFIGDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDEESKHITAMKSLEGEVVPFKSKVLLSNNVEAWLNDLALEMKQTLKQLLKECVTAGRSSQGAIDPSLFPSQILCLAEQIKFTEDVENAIKDHSLHQIEAQLVAKLERYTSVDTSSEDPGNSESGILELKLKALILDIIHNIDIVKQLNQVQVHTTDDWAWKKQVRFYMKSDHTCYVQMVDSELQYTYEYQGNAPKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVGLVKCGAWGCFDEFNRLEEAVLSAVSMQIQTIQDALKNHRTVCELLGKEVEINANSGIFITMNPAGKGYGGRQKLPDNLKQLFRPVAMSRPDNDLIAEVILYSEGFKDAKELGRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQLKKNSTKQDVNENHIVVQALRLNTMSKFTFADCTRFDALIKDVFPGIDFKEVEYDELSSALKQVFEEANYEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKSTLWRMLRAALCKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSARQVVREPQDVSSWIICDGDIDPEWIESLNSVLDDNRLLTMPSGERIQFGPNVNFVFETHDLSCASPATISRMGMIFLSDEETDLNSLIKSWLRNQPLEYRSNLENWIGDYFSKALQWVLKQNDYVVETSLVGTVMNGLSHLHGCKYHDQFIINLIRGLGGNLNMKSRLEFTKEVFNWARETPPDSHRPMDTYYDCDRGQLASYMLKKPESLTADDFSNGHILPVIQTPDMQRGLDYFKPWLSSDTKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTTSRHLLQKLSQTCMVISTNTGRVYRPKDCERLVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDENLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCAIDYPEREQLQTIYGAYLEAVLHKNLKNHSIWGSSSKIYLLAGSMVQVYEQVRAKFTVDEYSHYFFTPCILTQWVLGLFRYDLEGGSSNHPLDYVLEIVAYEARRLFRDKIVGVKELHLFDNILTSVLQGDWGSDILDNMADSFYVTWGAHHVSGGKTAPGQPLPPHGKPLGKLTSADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRNDLKHVLQLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLASGEVPGLYTLEELEPLLLPLKDQASQDGFFGPVFNYFTYRIQQNLHIVLIMDSANLNFIVNCESNPALHKKCQVLWMEGWSDSSMKKIPEMLFSETDGEEKYEKKRKDEKKRNSVDPDFIKSFLLIHESCKAYGATPSRYMTFLHVYSAISSSKKKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKQRIAEEVVKIEERKSKIDDELKEVQPLVNEAKLAVGNIRPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFDARNIPKEIRESVEELLFKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKNCLEEWTKAAGLEKFDLRRFLCTESEQLIWKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSHLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILENKDLIESLNQTKASSALIQDSLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLASFLRLFQRALQNKQDSENTEERIQCLVNSLKHMVYEYICRCLFKADQLMFALHFVRGMHPELFQENEWDTFTGVVVGDMLRKADSQQRIRDQLPSWIDQERSWAVATLKISLPSLYQTLCLEDGAFWRTYYHHSMCEQEFPSILAKKVSLFQQVLVVQALRPDRLQSAMALFACKALGLKELSPLPLNLKRLYKETLEIEPILIIISPGADPSQELQELASAERSSECYHQVAMGQGQADLAIQMLKECARNGDWLCLKNLHLVVSWLPVLEKELNTLQPKDSFRLWLTAEVHPNFTPILLQSSLKITYESPPGLKKNLMRTYESWTPEQISKRDNIHRAHALFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYHVIDRLFDGTKDVQWEFVHGLLENSIYGGRVDNYFDLRVLQSYLKQFFNSSIIDVLNQRNKKSIFPYSISLPNSCSILDYRAVIEKLPEDDKPSFFGLPANIARSSQRMISSQVISQLRILGRSVTAGCKFDREIWSNELSPVLNLWKKLNQNSNLIHQKVSPPNDRQGSPILSFIILEQFNAIRLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLTWQSRWEGPEDPLQYLRGLVARTLAIQNWVEKAEKQVLLADTLDLSELFHPDTFLNALRQETARATGCSVDSLKFVASWKGRLQEAKLQIKISGLLLEGCSFDGNRLSENQHDSPSVSSVLPCYMGWTPQGSYGPYSPDECISLPVYTSAERERVVTNIDVPCGGNQDQWIQCGAALFLKNQ', 4306, 'Q45VK7; B8JJF9; B8JJG0; O08822; Q5VI59; Q5VI60; Q5VI61; Q5VI62;Q69Z42; Q8BJL5; Q8BL87; Q8BMC7; Q8BUI9; Q8BXK5; Q9CRR8;', 'KD00400', 'Mus musculus (Mouse)', 'Dync2h1', '#Cytoplasmic dynein 2 heavy chain 1#Cytoplasmic dynein 2 heavy chain#Dynein cytoplasmic heavy chain 2#Dynein heavy chain 11#mDHC11#Dynein heavy chain isotype 1B', '-', '-', '110350'),
(401, 'A2AC93', 'Dynein intermediate chain 2; axonemal', 'GO:0003777', 70968, 'Part of the dynein complex of respiratory cilia. {ECO:0000250}.', 'MEIVYVYLKKRSEFGKQCNFSDRQAELNIDILPNPELAALYVERNPVDTGIQCSASMSEHEANTERFEMESCGVNHVEGGWPKDVNPQELEQTIRFRKKVEKDENYINAVMQLGSIMEHCIKQNNAIDIYEEYFDDEEAVEVTEEAPSAKTINVFRDPQEIKRTATHLSWHPDGNRKLAVAYSCLKFQRAPMSMNYDSYIWDLENPNRPEIALKPLSPLVTLEYNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIEFSHRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKISEPIEVVIMDISRKEQLENALGAISLEFESTLPTKFMVGTEQGIVISCNRKAKTQAEKIVCTFYGHHGPIYALQRNPFYPKNFLTVGDWTARIWSEDSRESSIMWTKYHMAYLSDGAWSPVRPAVFFTTKMDGTLDIWDLVFKQCDPALSLKVCDDPLFCLRVQDNGCLIACGSELGTTTLLEVSSSLSTLQRNEKNIASSIFERETRREKILEARHREMRLKEKGKVEGKEDDQKEEEAALDLDELVGKAEEEFFEVIFSELKRKEAEALKKKPKPRKKSSVKVEAEEEVEENVGEEEEAGGIIGIDAVEDMSEEAGEEQEDVPT', 623, 'A2AC93; A2AC94;', 'KD00401', 'Mus musculus (Mouse)', 'Dnai2', '#Dynein intermediate chain 2; axonemal#Axonemal dynein intermediate chain 2', '-', '-', '432611'),
(402, 'Q9Y812', 'Histone H3-like centromeric protein cnp1', 'GO:0051382===GO:0034501===GO:0000941===GO:0031134===GO:0000780===SCL===k', 13884, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. {ECO:0000269|PubMed:10864871}.', 'MAKKSLMAEPGDPIPRPRKKRYRPGTTALREIRKYQRSTDLLIQRLPFSRIVREISSEFVANFSTDVGLRWQSTALQCLQEAAEAFLVHLFEDTNLCAIHAKRVTIMQRDMQLARRIRGA', 120, 'Q9Y812;', 'KD00402', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cnp1', '#Histone H3-like centromeric protein cnp1#Centromere protein 1#CENP-A homolog#Silencing in the middle of the centromere protein 2', '-', '-', '2539658'),
(403, 'P47149', 'Kinetochore-associated protein NNF1', 'GO:0000776===GO:0000818===c;k', 23640, 'Acts as essential component of the kinetochore MIND complex; which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules. NNF1 is required for a number of nuclear functions. Cells depleted of NNF11 or containing a temperature-sensitive NNF1 mutation have elongated microtubules and become bi- and multinucleate. They also have a fragmented nucleolus and accumulate poly(A)+ RNA inside the nucleus. {ECO:0000269|PubMed:12455957; ECO:0000269|PubMed:14633972}.', 'MVNSHGIRYIRLKQVFNRALDQSISKLQSWDKVSSCFPQYVNSKQGAINVANCQRQLTEFWTELCQREFKEIMEERNVEQKLNELDELILEAKERYTDRDQDEVNKGPAIDELSSKELVECHLYSQRMHAIHEIDERLAKVNEMNDQLAQELKDLETQVEVEKNEIGKMYDEYLGSHTDQPANVLLVQSLNDMVLELKENY', 201, 'P47149; D6VWT1; Q06779;', 'KD00403', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'NNF1', '#Kinetochore-associated protein NNF1', '-', '-', '853576');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(404, 'Q6C710', 'Histone acetyltransferase ESA1', 'GO:0034508', 53908, 'Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4; H3; H2B; H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac; H4K8ac; H4K12ac and H4K16ac; histone H3 to form H3K14ac; histone H2B to form H2BK16ac; and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me. {ECO:0000250|UniProtKB:Q08649}.', 'MALAEADLPNGKTNGKASGSEETPAPVQKVDMNVAINELRVGCKVHVEKDGEDRVAEILSVQMRRGNLEFYVHYVEFNKRLDERIAATRVDLSQGVIWPEPEKPKKPLSGAAKESSKEKKKNPSKKQKLTDSAATTPGANSEDVMDLDNLQVNGTTQDPDNFNRDEEIEKLRTGGSMTQSSHEVARVRNLQRIVLGNHVIEPWYFSPYPIELTEEDEIYICDFTLCYFGSKKQFERFRSKSTLRHPPGNEIYRDEAVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDEKGHHLVGYFSKEKESAEGYNVACILTLPQYQRHGYGRLLIDFSYALSKAEGKTGSPEKPLSDLGLLSYRAYWADTIIELLMEKGKQEMTIEDIASVTAMTTTDVLHTLQTYNMLKYYKGQHIICLTDSVCEKYEKMLKKRRRKVNSELLKWKPPVFTAAQLRFAW', 469, 'Q6C710;', 'KD00404', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'ESA1', '#Histone acetyltransferase ESA1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}', '-', '-', '2912208'),
(405, 'P34036', 'Dynein heavy chain; cytoplasmic', 'GO:0003777===GO:0005868', 539613, 'Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.', 'MEDQQINVDSPTSGTNTPPVVTPTTSVISEQTLEETVKYLCKICPTLLDGDQSVFQNNLSNQIPPENMNKLKKFISDSKIPVLLIQKTNPTINSSNQTSTTTSSSSSSDDNTLTSSQQQSKESFNFEIEVKFGGENKSTLAIVKRIPESIVEYSSNKSIASQLQVLNLGDGSPMDTLHNYIHNSVAPFVRSYILSASKDDATTPSGGSADKSITSQNLDKEMKQSIGAVNQKIAELEISLYNCKQQVQIPEVTLAINPEIKSISKRLKETTGRTIKPDDLGDKASSPEFLNLLQAGTTTWAKNIQNVTKHNLIENLPSDVSTSQEINFWIELETSLQNIDQQLKSPEVEVTLATLRQAKRFIASAPFETDTIGVRKAMDKVQSYKTLFKDFPITPLLTATDLDSISSSVAAIFSHLKKTKNPYYPIPRYLSFLEAIGRDMCNKVYQILRQKNLMNIDYNDFEHLNRSVRALFTLWDDQFGAFRDILRDLAKKRGNERIPLIVNIDNRIQLVIIKIGKFRKQHEDLKNVVSNVLPGSQLGGGVVQTNTSNPTSPQKQEINAIEEINQAYLEFKEIDVLQLSKEGEEIWDAVVKRYNSRTDRVETYITVKLRDRLATAKNANEMFRVYQKFKDLLKRPKIRGATHEYESQLIERVKEDIRVLHDKFKMQYNNSEAYYMSQLRDLPPVSGAIIWARQIERQLDTYMKRVANVLGDSWESDAEGQKLKSESDQFRHKLNTDHIFSKWADETEKRSFDISGRILTIVKRGNKLALDINFDSHIIMLFKEVRNLQWLGFRVPLKISFISQGAKQVYPFAVSLKETLRTYAQTSGKVTPEFSTLVASYKRDVQANITEGFRLKWETIPKVDPYVRKLSTSINNFRDKVDDLIVKYSEIKKQLDGLKSCPFKSESFNEIIANIQKVVDELNLANYSNLPQWVTQLDAQVESMLIERLIDAINSWVQLIEGKEDQKDSQSTSGSSNKGGKLNRMNYSIRNKSDEENSSDLTQPQQSQQQQQTISIKPKLEKTIHEIVIRNQILSLSPPLEVARVNWIDQLHSWLNICCDLPRIQSSRYDESAMVHRGGVDSKKQSTFRDMLPKLPQGSLESAYSAITNKLEQVQQYVSIWLQYQSLWDMDSSFVYSKLGDDLNKWQLLLNQIKKSRSTFDNSSTEKQFGPLTIDYTQVQASVNNKYDYWHKDILGHFGSKLAEKMNQFYETISSSRQELEKLSVETVSTEEAVHFIIQIQDMKKKLSSWEADLRYYRTGQDLLQRQRFSFPNDWLDCERVEGEWSAFNEILNRKNATISEAIPQLQAKILQESKSINDRIKDFIDEWTANKPLQGSIKHSTALETLKIFEGRLIRLREESDRLSKAKQALDLTDTTGSSSSDQDRLVPVEEEIQDLKAVWVELSNTWQEIDSLKETAWSAIIPRKVRKSLEDTLQKLKNLPNRIRQYSAFDHAQNLIKIYLKGNAIITDLHSEAIKDRHWKILKKRLNTNWIITELTLGSIWDSDLARNENIYREVITAAQGEIALEEFLKGVREFWTTLELDLVNYQRKCKLVRGWDDLFNKLAEHLNSISAMKMSPYYKVFEEEANHWDDRLNKVRSLLDVWIDVQRRWVYLEGIFSGSGDINQLLPAESTRFKSINSEFIAILKKVSGAPLILEVLAIERIQQTMERLSDLLGKVQKALGEYLERQRSAFARFYFVGDEDLLEIIGNSKDIIKIQKHFRKMFAGLANLTLDDEKTTIIGMSSAEGETVTFKKPISIANGPKIHEWLTMVESEMKSTLATLLSESLQHFNQVDVNDHSKYSEWVDNYPTQLVLLTSQIVWSTQVDQALGGGTLQQSKIQEQLQSIEQTTQMILNNLADSVLQDLSAQKRKKFEHLITELVHQRDVVRQLQKCKNLTGNKDFDWLYHMRYYYDATQENVLHKLVIHMANATFYYGFEYLGIGERLVQTPLTDRCYLTLTQALESRMGGNPFGPAGTGKTETVKALGSQLGRFVLVFCCDEGFDLQAMSRIFVGLCQCGAWGCFDEFNRLEERILSAVSQQIQTIQVALKENSKEVELLGGKNISLHQDMGIFVTMNPGYAGRSNLPDNLKKLFRSMAMIKPDREMIAQVMLYSQGFKTAEVLAGKIVPLFKLCQEQLSAQSHYDFGLRALKSVLVSAGGIKRKCQPPQLPPITDAESKTKADQIYCQYEIGVLLNSINDTMIPKLVADDIPLIQSLLLDVFPGSQLQPIQMDQLRKKIQEIAKQRHLVTKQEWVEKILQLHQILNINHGVMMVGPSGGGKTTSWEVYLEAIEQVDNIKSEAHVMDPKAITKDQLFGSLDLTTREWTDGLFTATLRRIIDNVRGESTKRHWIIFDGDVDPEWVENLNSLLDDNKLLTLPNGERLALPNNVRVMFEVQDLKYATLATISRCGMVWFSEEILTTQMIFQNYLDTLSNEPFDPQEKEQQKRNENAQLQQQQQTTITSPILTSPPTTSSSSRSTTSTTSMIPAGLKVQKECAAIISQYFEPGGLVHKVLEDAGQRPHIMDFTRLRVLNSFFSLMNRSIVNVIEYNQLHSDFPMSPENQSNYITNRLLYSLMWGLGGSMGLVERENFSKFIQTIAITPVPANTIPLLDYSVSIDDANWSLWKNKVPSVEVETHKVASPDVVIPTVDTTRHVDVLHAWLSEHRPLILCGPPGSGKTMTLTSTLRAFPDFEVVSLNFSSATTPELLLKTFDHHCEYKRTPSGETVLRPTQLGKWLVVFCDEINLPSTDKYGTQRVITFIRQMVEKGGFWRTSDHTWIKLDKIQFVGACNPPTDAGRVQLTHRFLRHAPILLVDFPSTSSLTQIYGTFNRALMKLLPNLRSFADNLTDAMVEFYSESQKRFTPDIQAHYIYSPRELSRWDRALLEAIQTMDGCTLEGLVRLWAHEALRLFQDRLVETEEKEWTDKKIDEVALKHFPSVNLDALKRPILYSNWLTKDYQPVNRSDLREYVKARLKVFYEEELDVPLVLFNEVLDHILRIDRVFRQPQGHALLIGVSGGGKSVLSRFVAWMNGLSIYTIKVNNNYKSSDFDDDLRMLLKRAGCKEEKICFIFDESNVLESSFLERMNTLLAGGEVPGLFEGEEFTALMHACKETAQRNGLILDSEEELYKYFTSQVRRNLHVVFTMNPASPDFHNRSATSPALFNRCVLDWFGEWSPEALFQVGSEFTRNLDLENPQYIAPPVFIQEAEIMGNNLMAIPPSHRDAVVSSLVYIHQTIGEANIRLLKRQGRQNYVTPRHYLDFINQVVLLINEKRDQLEEEQLHLNIGLKKLRDTEAQVKDLQVSLAQKNRELDVKNEQANQKLKQMVQDQQAAEIKQKDARELQVQLDVRNKEIAVQKVKAYADLEKAEPAIIEAQEAVSTIKKKHLDEIKSLPKPPTPVKLAMEAVCLMLGGKKLEWADIRKKIMEPNFITSIINYDTKKMMTPKIREAITKGYLEDPGFDYETVNRASKACGPLVKWATAQTYYSEILDRIKPLREEVEQLENAANELKLKQDEIVATITALEKSIATYKEEYATLIRETEQIKTESSKVKNKVDRSIALLDNLNSERGRWEQQSENFNTQMSTVVGDVVLASAFLAYIGFFDQNFRTDLMRKWMIRLDSVGIKFKSDLSVPSFLSKPEERLNWHANSLPSDELCIENAIMLKRFNRYPLVIDPSGQAMEFLMNQYADKKITKTSFLDSSFMKNLESALRFGCPLLVQDVENIDPVLNPVLNKEIRKKGGRILIRLGDQDVDFSPSFMIFLFTRDPTAHFTPDLCSRVTFVNFTVTPSSLQSQCLHEALKTERPDTHKKRSDLLKIQGEFQVKLRILEKSLLNALSQASGNILDDDSVISTLETLKKETTEIALKVEETETVMQEISEVSALYNPMALSCSRVYFAMEELSQFHLYQFSLRAFLDIFYNLLNNNPNLVDKKDPNERLVYLSKDIFSMTFNRVTRTLLNDDKLTFALQLTIISVKGTSNEIEESEWDFLLKGGDNLTSIKETIPQLDSLLSTTQQKWLICLRQQVPSFSKLVDHIQQNSSDWKQFFGKDQVGEPIIPESWIVAQAQLSNQQSTIVSNFRKILLMKAFHSDRVLQYSHSFVCSVFGEDFLNTQELDMANIVEKEVKSSSPLLLCSVPGYDASSKVDDLALQLHKQYKSFAIGSPEGFELAEKSIYAAAKSGTWVLLKNIHLAPQWLVQLEKKLHSLSPHPSFRLFMTSEIHPALPANLLRMSNVFSYENPPGVKANLLHTFIGIPATRMDKQPAERSRIYFLLAWFHAIIQERLRYIPLGWTKFFEFNDADLRGALDSIDYWVDLYSKGRSNIDPDKIPWIAVRTILGSTIYGGRIDNEFDMRLLYSFLEQLFTPSAFNPDFPLVPSIGLSVPEGTTRAHFMKWIEALPEISTPIWLGLPENAESLLLSNKARKMINDLQKMQSSEEDGEDDQVSGSSKKESSSSSSEDKGKAKLRATITEWTKLLPKPLKQLKRTTQNIKDPLFRCFEREISTGGKLVKKITNDLANLLELISGNIKSTNYLRSLTTSISKGIVPKEWKWYSVPETISLSVWISDFSKRMQQLSEISESSDYSSIQVWLGGLLNPEAYITATRQSASQLNGWSLENLRLHASSLGKISSEGGASFNVKGMALEGAVWNNDQLTPTDILSTPISIATLTWKDKDDPIFNNSSSKLSVPVYLNETRSELLFSIDLPYDQSTSKQNWYQRSVSISSWKSDI', 4730, 'P34036; Q551T4; Q8T128;', 'KD00405', 'Dictyostelium discoideum (Slime mold)', 'dhcA', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC', '-', '-', '8620457'),
(406, 'Q2PQA9', 'Kinesin-1 heavy chain', 'GO:0003777', 109531, 'Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. {ECO:0000250|UniProtKB:Q61768}.', 'MADPAECNIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKTLRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTADKDVAITNDKPAAAIGMAGSFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKAVDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPGAVRGGGSFVQNNQPVGLRGGGGKQA', 963, 'Q2PQA9; Q9WV65;', 'KD00406', 'Rattus norvegicus (Rat)', 'Kif5b', '#Kinesin-1 heavy chain#Conventional kinesin heavy chain#Ubiquitous kinesin heavy chain#UKHC', '-', '-', '117550'),
(407, 'Q6BV14', 'DASH complex subunit DAD2', 'GO:0042729', 17148, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MDRRTVLKSTHIQQKIAEKKAELENLNEIKKFTSILTNQLDELENKLDYMAEGTESVALVLSNWQNVVKSVSLASLGLLKYSEKDYETGAPLPECLVRIKLDKDDNVGEEIQEKEEMETDDYISDQQAEESENINEEEDRQEVQTSYTD', 149, 'Q6BV14;', 'KD00407', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'DAD2', '#DASH complex subunit DAD2#Outer kinetochore protein DAD2', '-', '-', '2900775'),
(408, 'A1CXR0', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 34266, 'Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). {ECO:0000250}.', 'MNSLVATPPVPPHFYEYSRLSSPHPMSTPTHTPTNRKRKADDDGNDHDGRMSASPTNSPAFTPRSLPAPRSFKRSRPNVSGRPLSLPRLLETLDTDALRGILRSMCERHPALADEVIHTSPRPSVSSALQVLRNYQSTLQNSFPLGGNPESDYAYNRVRQPLGNLLDALSDFTPHFLPPHETQASVSLSYLDGATDIIHALPRWHSPQNNIERDSAYDEICKAWILVIREAAKRGGGIQLQYGGWDQKLAKHNQNAGGRLQAAVNELGNSLGWMHGPDSQGYGSSTGGDLVSVREQLLSGTYGLGTPVKVGPW', 313, 'A1CXR0;', 'KD00408', 'Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRR181) (Aspergillus fischerianus)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '4593400'),
(409, 'P60766', 'Cell division control protein 42 homolog', 'GO:0051988', 21259, 'Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin; actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration.', 'MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL', 191, 'P60766; A2A9U6; P21181; P25763; Q3THZ7; Q3TJK6; Q545V0; Q6P201;Q8BQ51;', 'KD00409', 'Mus musculus (Mouse)', 'Cdc42', '#Cell division control protein 42 homolog#G25K GTP-binding protein', '-', '-', '12540'),
(410, 'P34766', 'Homeobox protein pal-1', 'GO:0000777===SCL', 30334, 'Transcriptional activator. Interacts with promoter regions for tbx-8.9; tbx-9; elt-1; hnd-1; scrt-1; and vab-7 genes. Binds the sequence ATTTATGAC. Binds to the enhancer region of the hlh-1 gene promoter during embryonic body wall muscle development. Activates the gene for mab-5 in embryo development. Necessary for vab-7 expression in C blastomeres in the posterior of embryos. Required for posterior V6 neuroectoblast cell fate specification during postembryonic neurogenesis (patterning) which generates the characteristic ray lineage during male tail development. Binds to ced-3 promoter and activated expression which is crucial for tail- spike cell death. Has a role in E cell specification in endoderm development and body wall muscle development. {ECO:0000269|PubMed:10970880; ECO:0000269|PubMed:11133155; ECO:0000269|PubMed:15772128; ECO:0000269|PubMed:15772130; ECO:0000269|PubMed:16084508; ECO:0000269|PubMed:16831832; ECO:0000269|PubMed:17329362; ECO:0000269|PubMed:18277379; ECO:0000269|PubMed:2023634; ECO:0000269|PubMed:2295086; ECO:0000269|PubMed:8625851; ECO:0000269|PubMed:8861906; ECO:0000269|PubMed:9367437; ECO:0000269|PubMed:9367442}.', 'MSVDVKSDFSENESSSTPSPTTVPADVTWPHYPMMPFMQPHPLREKMLQPTFDPQIYGRWSQMGDTGFYGHPDLYPFGLPQLAANGQIPAVEAVDVKPPLSNGSSSSDSGMYPSPSDMMTPFPSTSSGAASSSELSAAAAAAANYQMRAATCYQQSVWPFMDYQQFQGFSWKMPLGNNHGKDRRSSSDGKTLPTGPGTNNVRVRTADKYRMVYSDYQRLELEKEFHTSPFITSDRKSQLSTMLSLTERQIKIWFQNRRAKDRRDKQKIRL', 270, 'P34766; C9IY23; Q18513; Q65ZB9;', 'KD00410', 'Caenorhabditis elegans', 'pal-1', '#Homeobox protein pal-1#Caudal homolog 1#Homeobox protein ceh-3#Posterior alae in males protein 1', '-', '-', '175638'),
(411, 'Q59LN9', 'Histone H3-like centromeric protein CSE4', 'GO:0000776===GO:0000777', 24442, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). {ECO:0000250}.', 'MARLSGQSSGRQTGQGTSAEAIRQQREELRRQRELRLQQQQQAERQQQRQQYRTEQSPIVPAATSSSRYSQFGIYRNQPGDVVDTLASSLPRRTTTTRPEVNRTVPRVKKRYRPGTKALREIRQYQKSTDLLIRKLPFARLVREISLDFVGPSYGLRWQSNAILALQEASESFLIHLLEDTNLCAIHAKRVTIMQKDIQLARRIRGQSWIL', 211, 'Q59LN9;', 'KD00411', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog', '-', '-', '3647750'),
(412, 'P97887', 'Presenilin-1', 'GO:0000776', 52790, 'Probable catalytic subunit of the gamma-secretase complex; an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx; cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin; thus negatively regulating Wnt signaling. May also play a role in hematopoiesis (By similarity). {ECO:0000250}.', 'MTEIPAPLSYFQNAQMSEDSHSSSVRSQNDNQERQQHHDRQRLDNPESISNGRPQSNFTRQVIEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIVSSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMIAIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVPKNPKYSTQGTEREETQDTGTGSDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSGSILTSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLIFYFATDYLVQPFMDQLAFHQFYI', 468, 'P97887; P97529;', 'KD00412', 'Rattus norvegicus (Rat)', 'Psen1', '#Presenilin-1#PS-1#3.4.23.-#Protein S182#Presenilin-1 NTF subunit#Presenilin-1 CTF subunit#Presenilin-1 CTF12#PS1-CTF12', '-', '-', '29192'),
(413, 'Q4U0G1', 'CLIP-associating protein 1-A', 'GO:0000777===GO:0005828', 161499, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules during anaphase. Plays a crucial role in chromatin-induced microtubule formation. May also act at microtubule minus ends. May be involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.', 'MEQGMDYWLGQIQQKDVGKRLQVGPDLIEYLLDRQKSIDLEQDQTLLDRMVDGLATSWVNSSNYKVALLGMDILSELVSRLQDRFRTQLGTVLPSLMDRLGDAKDSVREQDQSLLIKIMEQASNPQYVWERMFSGFKHKNFRTREGVCLCLIATLNVYGANSLTLSKIVPHICNLLGDPNSQVRDAAINCLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGTMILSASDKNFDDEDSVDGNRPSSASSSASSKAPQTARRGVSLGTARRPGPSSAAAKTGGTAKEGAGALDEEDFIRAFEDVPNVQIYSSRDLEESLNKIREILSDDKHDWEQRITALKKIRSLLLAGAAEYDNFFQQLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAIMPTVFNLVPNSAKIMATSGIVAIRLIIRHTHVPRLIPIITSNCTSKSVAVRRRCYDFLDLLLQEWQTHSLERHVSVLAETIKKGIHDADSEAKIVARKCYWGFHSHFSKEAEHLFHTLESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSTKRSPTGSTVSRASSTTSKSTPGSLQRSRSDIDVNAAATSKSKAASGASTAPFISVAALPPGSYASLGRIRTRRQSSGSTTSTASTPADTRGRSRAKVVSQSQPGSRSNSPGKLLGSSYGGIATGPQRVPQMPSSEKRSRIPRSQGCSRETSPSRIGLDRFGISQQGRIPSAMRVLSSSTDLEAAVADALLLGDSRNKKKPVRRRYEPYGMYSDDDANSDASSACSERSYSSKNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLLGLQNLLKSQRTLSRVELKRLCEIFTRMFADPHSKRVFSMFLETLVDFVIIHKDDLQDWLFILLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQIVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNSSMGSPSNTIGRTPSRHSSSRASPLTSPTNCSHGGLSPSMLDYDTENLNSDEIYSSLRGVTEAIEKFSFRSQVDLNEPVRRDSKKESELGSCDVGIASPASDLRGGTDMVEGGRMALDNKTSLLNTQPPRAFTGPRGREYNPYAYSDSINSYDKTALKEAVFDDDMDQLRDVSIDHSDLVADLLKELSNHNERVEERKGALCELLKITREDNLAVWEEHFKTILLLLLETLGDKDHAIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLAGSIHPEQCIKVLCPIIQTADYPINLAAIKMQAKVIERISKESLHQILPDIIPGLLQGYDNTESSVRKASVFCLVAIYSVIGEELKPYLAQLTGSKMKLLNLYIKRAQTTNSNSSSSSDVSTHS', 1460, 'Q4U0G1; A3KNB5;', 'KD00413', 'Xenopus laevis (African clawed frog)', 'clasp1-a', '#CLIP-associating protein 1-A#Cytoplasmic linker-associated protein 1-A#XCLASP1', '-', '-', '494817'),
(414, 'Q9UFH2', 'Dynein heavy chain 17; axonemal', 'GO:0003777', 511787, 'Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.', 'MTMAPDVRLEYLEEVASIVLKFKPDKWSKLIGAEENVALFTEFFEKPDVQVLVLTLNAAGMIIPCLGFPQSLKSKGVYFIKTKSENINKDNYRARLLYGDISPTPVDQLIAVVEEVLSSLLNQSENMAGWPQVVSEDIVKQVHRLKNEMFVMSGKIKGKTLLPIPEHLGSLDGTLESMERIPSSLDNLLLHAIETTIIDWSHQIRDVLSKDSAQALLDGLHPLPQVEFEFWDARLLNLKCIHEQLNRPKVNKIVEILEKAKSCYWPALQNVYTNVTEGLKEANDIVLYLKPLRILLEEMEQADFTMLPTFIAKVLDTICFIWATSEYYNTPARIIVILQEFCNQIIEMTRTFLSPEEVLKGLQGEIEEVLSGISLAVNVLKELYQTYDFCCVNMKLFFKDKEPVPWEFPSSLAFSRINSFFQRIQTIEELYKTAIEFLKLEKIELGGVRGNLLGSLVTRIYDEVFELVKVFADCKYDPLDPGDSNFDRDYADFEIKIQDLDRRLATIFCQGFDDCSCIKSSAKLLYMCGGLMERPLILAEVAPRYSVMLELFDAELDNAKILYDAQMAASEEGNIPLIHKNMPPVAGQLKWSLELQERLEVSMKHLKHVEHPVMSGAEAKLTYQKYDEMMELLRCHREKIYQQWVAGVDQDCHFNLGQPLILRDAASNLIHVNFSKALVAVLREVKYLNFQQQKEIPDSAESLFSENETFRKFVGNLELIVGWYNEIKTIVKAVEFLLIKSELEAIDVKLLSAETTLFWNGEGVFQYIQEVREILHNLQNRMQKAKQNIEGISQAMKDWSANPLFERKDNKKEALLDLDGRIANLNKRYAAVRDAGVKIQAMVAENAELFRADTLSLPWKDYVIYIDDMVLDEFDQFIRKSLSFLMDNMVIDESIAPLFEIRMELDEDGLTFNPTLEVGSDRGFLALIEGLVNDIYNVARLIPRLAKDRMNYKMDLEDNTDLIEMREEVSSLVINAMKEAEEYQDSFERYSYLWTDNLQEFMKNFLIYGCAVTAEDLDTWTDDTIPKTPPTLAQFQEQIDSYEKLYEEVSKCENTKVFHGWLQCDCRPFKQALLSTIRRWGFMFKRHLSNHVTNSLADLEAFMKVARMGLTKPLKEGDYDGLVEVMGHLMKVKERQAATDNMFEPLKQTIELLKTYGEEMPEEIHLKLQELPEHWANTKKLAIQVKLTVAPLQANEVSILRRKCQQFELKQHEFRERFRREAPFSFSDPNPYKSLNKVFLLKGIMEALSKSGGLFEVPVPDYKQLKACHREVRLLKELWDMVVVVNTSIEDWKTTKWKDINVEQMDIDCKKFAKDMRSLDKEMKTWDAFVGLDNTVKNVITSLRAVSELQNPAIRERHWQQLMQATQVKFKMSEETTLADLLQLNLHSYEDEVRNIVDKAVKESGMEKVLKALDSTWSMMEFQHEPHPRTGTMMLKSSEVLVETLEDNQVQLQNLMMSKYLAHFLKEVTSWQQKLSTADSVISIWFEVQRTWSHLESIFIGSEDIRTQLPGDSQRFDDINQEFKALMEDAVKTPNVVEATSKPGLYNKLEALKKSLAICEKALAEYLETKRLAFPRFYFVSSADLLDILSNGNDPVEVSRHLSKLFDSLCKLKFRLDASDKPLKVGLGMYSKEDEYMVFDQECDLSGQVEVWLNRVLDRMCSTLRHEIPEAVVTYEEKPREQWILDYPAQIWWTTEVGLAFARLEEGYENAIKDYNKKQISQLNVLITLLIGNLNAGDRMKIMTICTIDVHARDVVAKMIVESSQAFTWQAQLRHRWDEEKRHCFANICDAQIQYSYEYLGNTPRLVITPLTDRCYITLTQSLHLIMGGAPAGPAGTGKTETTKDLGRALGTMVYVFNCSEQMDYKSCGNIYKGLAQTGAWGCFDEFNRISVEVLSVIAVQVKCVQDAIRAKKKAFNFLGEIIGLIPTVGIFITMNPGYAGRAELPENLKALFRPCAMVVPDFELICEIMLMAEGFLEARLLARKFITLYTLCKELLSKQDHYDWGLRAIKSVLVVAGSLKRGDPSRAEDQVLMRALRDFNIPKIVTDDLPVFMGLIGDLFPALDVPRKRDLNFEKIIKQSIVELKLQAEDSFVLKVVQLEELLQVRHSVFIVGNAGSGKSQVLKSLNKTYQNLKRKPVAVDLDPKAVTCDELFGIINPVTREWKDGLFSTIMRDLANITHDGPKWIILDGDIDPMWIESLNTVMDDNKVLTLASNERIPLNRTMRLVFEISHLRTATPATVSRAGILYINPADLGWNPVVSSWIERRKVQSEKANLMILFDKYLPTCLDKLRFGFKKITPVPEITVIQTILYLLECLLTEKTVPPDSPRELYELYFVFTCFWAFGGAMFQDQLVDYRVEFSKWWINEFKTIKFPSQGTIFDYYIDPDTKKFLPWTDKVPSFELDPDVPLQASLVHTTETIRIRYFMDLLMEKSWPVMLVGNAGTGKSVLMGDKLESLNTDNYLVQAVPFNFYTTSAMLQGVLEKPLEKKSGRNYGPPGTKKLVYFIDDMNMPEVDKYGTVAPHTLIRQHMDHRHWYDRHKLTLKDIHNCQYVACMNPTSGSFTIDSRLQRHFCVFAVSFPGQEALTTIYNTILTQHLAFRSVSMAIQRISSQLVAAALALHQKITATFLPTAIKFHYVFNLRDLSNIFQGLLFSTAEVLKTPLDLVRLWLHETERVYGDKMVDEKDQETLHRVTMASTKKFFDDLGDELLFAKPNIFCHFAQGIGDPKYVPVTDMAPLNKLLVDVLDSYNEVNAVMNLVLFEDAVAHICRINRILESPRGNALLVGVGGSGKQSLSRLAAYISGLDVFQITLKKGYGIPDLKIDLAAQYIKAAVKNVPSVFLMTDSQVAEEQFLVLINDLLASGEIPGLFMEDEVENIISSMRPQVKSLGMNDTRETCWKFFIEKVRRQLKVILCFSPVGSVLRVRARKFPAVVNCTAIDWFHEWPEDALVSVSARFLEETEGIPWEVKASISFFMSYVHTTVNEMSRVYLATERRYNYTTPKTFLEQIKLYQNLLAKKRTELVAKIERLENGLMKLQSTASQVDDLKAKLAIQEAELKQKNESADQLIQVVGIEAEKVSKEKAIADQEEVKVEVINKNVTEKQKACETDLAKAEPALLAAQEALDTLNKNNLTELKSFGSPPDAVVNVTAAVMILTAPGGKIPKDKSWKAAKIMMGKVDTFLDSLKKFDKEHIPEACLKAFKPYQGNPTFDPEFIRSKSTAAAGLCSWCINIVRFYEVYCDVAPKRQALEEANAELAEAQEKLSRIKNKIAELNANLSNLTSAFEKATAEKIKCQQEADATNRVILLANRLVGGLASENIRWAESVENFRSQGVTLCGDVLLISAFVSYVGYFTKKYRNELMEKFWIPYIHNLKVPIPITNGLDPLSLLTDDADVATWNNQGLPSDRMSTENATILGNTERWPLIVDAQLQGIKWIKNKYRSELKAIRLGQKSYLDVIEQAISEGDTLLIENIGETVDPVLDPLLGRNTIKKGKYIKIGDKEVEYHPKFRLILHTKYFNPHYKPEMQAQCTLINFLVTRDGLEDQLLAAVVAKERPDLEQLKANLTKSQNEFKIVLKELEDSLLARLSAASGNFLGDTALVENLETTKHTASEIEEKVVEAKITEVKINEARENYRPAAERASLLYFILNDLNKINPVYQFSLKAFNVVFEKAIQRTTPANEVKQRVINLTDEITYSVYMYTARGLFERDKLIFLAQVTFQVLSMKKELNPVELDFLLRFPFKAGVVSPVDFLQHQGWGGIKALSEMDEFKNLDSDIEGSAKRWKKLVESEAPEKEIFPKEWKNKTALQKLCMVRCLRPDRMTYAIKNFVEEKMGSKFVEGRSVEFSKSYEESSPSTSIFFILSPGVDPLKDVEALGKKLGFTIDNGKLHNVSLGQGQEVVAENALDVAAEKGHWVILQVRGGQHCRNIHLVARWLGTLDKKLERYSTGSHEDYRVFISAEPAPSPETHIIPQGILENAIKITNEPPTGMHANLHKALDLFTQDTLEMCTKEMEFKCMLFALCYFHAVVAERRKFGAQGWNRSYPFNNGDLTISINVLYNYLEANPKVPWDDLRYLFGEIMYGGHITDDWDRRLCRTYLAEYIRTEMLEGDVLLAPGFQIPPNLDYKGYHEYIDENLPPESPYLYGLHPNAEIGFLTVTSEKLFRTVLEMQPKETDSGAGTGVSREEKAGSLKLLPSERKGEDLELRRGGCPGTGFQVKAVLDDILEKIPETFNMAEIMAKAAEKTPYVVVAFQECERMNILTNEMRRSLKELNLGLKGELTITTDVEDLSTALFYDTVPDTWVARAYPSMMGLAAWYADLLLRIRELEAWTTDFALPTTVWLAGFFNPQSFLTAIMQSMARKNEWPLDKMCLSVEVTKKNREDMTAPPREGSYVYGLFMEGARWDTQTGVIAEARLKELTPAMPVIFIKAIPVDRMETKNIYECPVYKTRIRGPTYVWTFNLKTKEKAAKWILAAVALLLQV', 4485, 'Q9UFH2; O00431; O15206; Q2M2Y1; Q6ZRQ2; Q8N7Q7;', 'KD00414', 'Homo sapiens (Human)', 'DNAH17', '#Dynein heavy chain 17; axonemal#Axonemal beta dynein heavy chain 17#Axonemal dynein heavy chain-like protein 1#Ciliary dynein heavy chain 17#Ciliary dynein heavy chain-like protein 1#Dynein light chain 2; axonemal', '-', 'ENSG00000268470', '-'),
(415, 'Q10951', 'Protein byr4', 'c;k', 75693, 'Has an essential role in ensuring cytokinesis and septation occur only once during mitosis. It does so by interacting with the ras1 signaling pathways; thereby suppressing them.', 'MTEVECWDDDPDFASDVDNASLFTQSIATTSASTSVDDGFSFDDSISRLNSLSISDVPSAHSRVEQWNQQVHNLNHELSSNKNRISSNVEGYEDDFSFDEEGEEGNNEFNTLRPNKYQDADVDEFNTIRASETASQRPPIPFSSDTLKKTYLSSENDARYPSVSDSPYCESEGFSSFEDDFEIDPDTDLNSILHRKQNRMDPKASFSSVEQSSLRTPSSAHNDDGFWDDFDIDFNNETESIFRKKIRSPNTINQKHPYISSTISYQPNVHQDAKYYPLCKDIFPSLANENPHSDNPNLKYSSKTLSKRDTSSHYPETLKASSKHSSPVKGNSSISSTWTPSNLKIYHSKNSMGLMDLDALKTVASNSKYRTKPKNCKTYGDGTELDTLDELPVDYEFELKLRKKQTTKVSGTPKSKHAGSTQEWHSHTTPRSTSKHENNLNNITNSAKNEHIRSQRQHKTHAAPSKELTKESLSNDQLSVKEKRRHHKKAPTLIQNLNSPRTPKIVGKMRYNPTKHCWEGNDYAIRDFDTPISPSRPALISNISTKKGIQVVGNMVYDPTRLRWIDNSISGQEAEDPFSGFDDLEDTDSTSQYLNENSGSFNGSINSIINFPDMSEIYDVGPEFEKKQFSEDIQWRKRIDGWFFSFKNDDRSRLWELYNILNAEQ', 665, 'Q10951;', 'KD00415', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'byr4', '#Protein byr4', '-', '-', '2541936'),
(416, 'P47167', 'Central kinetochore subunit MCM22', 'GO:0000778===k', 27568, 'Component of the central kinetochore; which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle- microtubule attachments and proper chromosome segregation. {ECO:0000269|PubMed:9987135}.', 'MDVEKDVLDVYIKNLENQIGNKRYFLKQAQGAIDEITKRSLDTEGKPVNSEVFTELLRKPMFFSERADPIGFSLTSNFLSLRAQSSSEWLSLMNDQSVDQKAMLLLQNNINSDLKELLRKLQHQMTIMDSKKQDHAHIRTRKARNKELWDSLADFLKGYLVPNLDDNDESIDSLTNEVMLLMKRLIEHDLNLTLNDFSSKTIPIYRLLLRANIITVIEGSTNPGTKYIKLIDFNETSLT', 239, 'P47167; D6VWV3;', 'KD00416', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MCM22', '#Central kinetochore subunit MCM22#Minichromosome maintenance protein 22', '-', '-', '853599'),
(417, 'O70126', 'Aurora kinase B', 'GO:0000776===GO:0034501===GO:0032133===GO:0000779===GO:0000780===k', 39384, 'Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint; a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C; leading to retain abscission- competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin; CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA; DES/desmin; GPAF; KIF2C; NSUN2; RACGAP1; SEPT1; VIM/vimentin; GSG2/Haspin and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process; whereas histone H3 is phosphorylated at ''Ser-10'' and ''Ser-28'' during mitosis (H3S10ph and H3S28ph; respectively). AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells; inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. {ECO:0000269|PubMed:11784863; ECO:0000269|PubMed:24034696}.', 'MAQKENAYPWPYGSKTSQSGLNTLSQRVLRKEPATTSALALVNRFNSQSTAAPGQKLAENKSQGSTASQGSQNKQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSRTFDEQRTATIMEELSDALTYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSVPSGAQDLISKLLKHNPWQRLPLAEVAAHPWVRANSRRVLPPSAL', 345, 'O70126; Q61882; Q8C6C1;', 'KD00417', 'Mus musculus (Mouse)', 'Aurkb', '#Aurora kinase B#2.7.11.1#Aurora 1#Aurora- and IPL1-like midbody-associated protein 1#Aurora/IPL1-related kinase 2#ARK-2#Aurora-related kinase 2#STK-1#Serine/threonine-protein kinase 12#Serine/threonine-protein kinase 5#Serine/threonine-protein kinase aurora-B', '-', '-', '20877'),
(418, 'P27361', 'Mitogen-activated protein kinase 3', 'c;k;m', 43136, 'Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context; the MAPK/ERK cascade mediates diverse biological functions such as cell growth; adhesion; survival and differentiation through the regulation of transcription; translation; cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis; mitosis; and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus; and seem to participate in the regulation of transcription upon stimulation. However; other substrates are found in the cytosol as well as in other cellular organelles; and those are responsible for processes such as translation; mitosis and apoptosis. Moreover; the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics; including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2; BCL6; ELK1; ERF; FOS; HSF4 or SPZ1); cytoskeletal elements (such as CANX; CTTN; GJA1; MAP2; MAPT; PXN; SORBS3 or STMN1); regulators of apoptosis (such as BAD; BTG2; CASP9; DAPK1; IER3; MCL1 or PPARG); regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2; FRS2 or GRB10). Protein kinases (such as RAF1; RPS6KA1/RSK1; RPS6KA3/RSK2; RPS6KA2/RSK3; RPS6KA6/RSK4; SYK; MKNK1/MNK1; MKNK2/MNK2; RPS6KA5/MSK1; RPS6KA4/MSK2; MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1; DUSP4; DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets; thereby extending the specificity of the cascade. {ECO:0000269|PubMed:10393181; ECO:0000269|PubMed:10617468; ECO:0000269|PubMed:12110590; ECO:0000269|PubMed:12356731; ECO:0000269|PubMed:12974390; ECO:0000269|PubMed:15788397; ECO:0000269|PubMed:15952796; ECO:0000269|PubMed:16581800; ECO:0000269|PubMed:19265199; ECO:0000269|PubMed:8325880; ECO:0000269|PubMed:9155018; ECO:0000269|PubMed:9480836}.', 'MAAAAAQGGGGGEPRRTEGVGPGVPGEVEMVKGQPFDVGPRYTQLQYIGEGAYGMVSSAYDHVRKTRVAIKKISPFEHQTYCQRTLREIQILLRFRHENVIGIRDILRASTLEAMRDVYIVQDLMETDLYKLLKSQQLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLINTTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINMKARNYLQSLPSKTKVAWAKLFPKSDSKALDLLDRMLTFNPNKRITVEEALAHPYLEQYYDPTDEPVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP', 379, 'P27361; A8CZ58; B0LPG3; Q8NHX1;', 'KD00418', 'Homo sapiens (Human)', 'MAPK3', '#Mitogen-activated protein kinase 3#MAP kinase 3#MAPK 3#2.7.11.24#ERT2#Extracellular signal-regulated kinase 1#ERK-1#Insulin-stimulated MAP2 kinase#MAP kinase isoform p44#p44-MAPK#Microtubule-associated protein 2 kinase#p44-ERK1', 'BIOMD0000000251,Nakakuki2010_CellFateDecision_Core;BIOMD0000000288,Wang2009 - PI3K Ras Crosstalk;BIOMD0000000424,Faratian2009 - Role of PTEN in Trastuzumab resistance;BIOMD0000000427,Bianconi2012 - EGFR and IGF1R pathway in lung cancer;BIOMD0000000430,Sarma2012 - Interaction topologies of MAPK cascade (M4_K2_USEQ);BIOMD0000000431,Sarma2012 - Interaction topologies of MAPK cascade (M4_K2_PSEQ);BIOMD0000000432,Sarma2012 - Interaction topologies of MAPK cascade (M4_K2_QSS_USEQ);BIOMD0000000433,Sarma2012 - Interaction topologies of MAPK cascade (M4_K2_QSS_PSEQ);BIOMD0000000477,Mol2013 - Immune Signal Transduction in Leishmaniasis;BIOMD0000000557,Reiterer2013 - pseudophosphatase STYX role in ERK signalling;', 'ENSG00000102882', '-'),
(419, 'Q6AYL9', 'Kinetochore protein Nuf2', 'GO:0000777===GO:0031262', 54556, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (By similarity). {ECO:0000250}.', 'METLSFPRYNIAEIVVHIRNKLLTGADGKNLSKSDFLPNPKPEVLYMIYMRALQLVYGVRLEHFYMMPVNIEVMYPHIMEGFLPVSNLFFHLDSFMPICRVNDFEIADILYPKANRTSRFLSGIINFIHFRETCLEKYEEFLLQNKSSVDKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQDFRQKTTLLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEVMEKYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSILKESLNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTMIEDCNKVQEKRDAVCEQVTAINQDIHKIKSGIQQLRDAEKREKLKSQEILVDLKSALEKYHEGIEKTTEECCTRIGGKTAELKRRMFKMPP', 464, 'Q6AYL9;', 'KD00419', 'Rattus norvegicus (Rat)', 'Nuf2', '#Kinetochore protein Nuf2#Cell division cycle-associated protein 1', '-', '-', '304951'),
(420, 'P0CP41', 'Probable kinetochore protein NUF2', 'GO:0000777', 54350, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSQQNRRVQQNTAAFPLLTAHDILECLAALDIPAQMEDLTKPTAQSTQSIYGSLLEVLMGASINSIEGPKQALLGMMEYKVLSFRSMKRTQINLSRQEMYSDTLQFMMFFKHCRRLALLCGIPDFAISDLARPDANRLRKVLSGIMNFAKFRDERMQTQARFQENLQKHQKKAVDLRRKTEELETQFQEITARNAAERPQSEQAQKRNELLKSELLELNSQRLKEVQEYEELKKERQTLLEQVNHNNRIVTQLELQIGSAKSRLVQSPDRIKRHISEMSFAIQSEKAKLASFQQKARELTNRLEVIGALEVDLRGLIDLEHSIQDQRAKTEEAKRSKSALEARLEGRQIESQGLAAKLEQLQRQLQNASHKLARQEETRKGMRERGARRIDELKAEYKVRARERGEWQKQRDDLLAEQKELESEMAAFVTKHENEINEFLHAYWTMRRQAEDYMNTMTVKLGLQVQL', 467, 'P0CP41; Q55Z49; Q5KNG4;', 'KD00420', 'Cryptococcus neoformans var. neoformans serotype D (strain B-3501A(Filobasidiella neoformans)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '4933903'),
(421, 'O82265', 'Sister-chromatid cohesion protein 3', 'GO:0051455===k', 125759, 'Essential component of cohesin complex; a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase; the complex is cleaved and dissociates from chromatin; allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Required for centromere cohesion maintenance at anaphase I and for the monopolar orientation of the kinetochores during both male and female meiosis. Also involved in mitosis. {ECO:0000269|PubMed:16176934; ECO:0000269|PubMed:19533160}.', 'MEDSPQGLKRSRDPDQDQDDDSGEAGKADGSGGENQERSSDQIELDDDDFQETRPKPKRSRTHPPQQNLIEVVKGNGDLISKAVKIWVERYEDSPSLATTELLSMLFQACGAKYSIKDDLLDETDVDDVVVSLVNLARAGELEDYQSSRKKELKNFKENLVSFWNNLIIECQNGPLFDRVLFDKCMDYIIALSCTPPRVYRQTATLMGLQLVTSFISVANTLGSQRETTQRQLNAESKKRADGPRVDSLNKRLSVTHEQITTLEDMMRKIFTGLFVHRYRDIDNDIRMSCIQSLGIWILSYPSLFLQDLYLKYLGWTLNDKNAGVRKASLLALQKLYEMDENVPTLGLFTQRFSNRMIEMADDVDMSAAVCAIGLVKQLLRHQLIPDDDLGPLYDLLIDQPQEIRRAIGELVYDHLIAQKFNSSPSSLTGHDDSSSEIHIFRMLQILREFSTDPILCVYVIDDVWEYMKAMKDWKCIISMLLDQNPRTGSTTDEDSTNLIRLLFVSIRKAVGEKIIPSTDNRKQYHSKAQREIFENNRKDITVAMMKNYPQLLRKFMADKAKVSSLVEIIIFMKLELYSLKRQEQSFKAAVRLIKDAFFKHGEKEALRSCVKAITFCASESKGELQDFSRGKLKDLEDELLDKITSAIREVKDGNDEYSLLVNLKRLYELQLSKPVLVESMFDEIALTLHNFRNLDEEVICFLLLNMHMYLAWYLHSIINCEAISEASLSSLISKRDTLFEELSYFLNGIEESKKYGNQLSNRICAILAETWCLFRKSNYDSGKLERLGYCPDSVFLEKFWKLCAEMFNTSDETDEEDENKEYIEETNRDVSVIAACKLVASDVVPKDYLGPEIISHLGMHGPGVTGIIKNLITFLRKKEDDISNIYLESLKRAYHRYSSELSSGREESRVDKCLEEWRELAGGLSGMYIGAARNKYRLEILSVVKEGVEFAFRDAPKQLLFLEVAILPFATRLSVSDIIDIKKDVQGRIVHVNTDEDPSGWRPCFTFLETLEEKCLKNEDLQDDKEAANVRRRGRPRKRPETERKRLFDEQSGSDEDESISGGSDREDKLDEDAPLIETIRSAARRKALKGERSKGH', 1098, 'O82265; Q8LFH0; Q9XGM9;', 'KD00421', 'Arabidopsis thaliana (Mouse-ear cress)', 'SCC3', '#Sister-chromatid cohesion protein 3#AtSCC3#Stromalin protein', '-', '-', '819410'),
(422, 'P0CP40', 'Probable kinetochore protein NUF2', 'GO:0000777', 54295, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSQQNRRVQQNTAAFPLLTAHDILECLAALDIPAQMEDLTKPTAQSTQSIYGSLLEVLMGASINSIEGPKQALLGMMEYKVLSFRSMKRTQINLSRQEMYSDTLQFMMFFKHCRRLALLCGIPDFAISDLARPDANRLRKVLSGIMNFAKFRDERMQTQARFQENLQKHQKKAVDLRRKTEELETQFQEITARNAAERPQSEQAQKRNELLKSELLELNSQRLKEVQEYEELKKERQTLLEQVNHNNRIVTQLELQIGSAKSRLVQSPDRIKRHISEMSFAIQSEKAKLASFQQKARELTNRLEVIGALEVDLRGLIDLEHSIQDQRAKTEEAKRSKSALEARLEGRQIESQGLAAKLEQLQRQLQNASHKLARQEETRKGMRERGARRIDELKAEYKVRARERGEWQKQRDDLLAEQKELESEMAAFVTKHENEINEFLHAYWTMRRQAEDYMNTMTVKLGLQTAI', 467, 'P0CP40; Q55Z49; Q5KNG4;', 'KD00422', 'Cryptococcus neoformans var. neoformans serotype D (strain JEC21ATCC MYA-565) (Filobasidiella neoformans)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '3253916'),
(423, 'P41004', 'Structural maintenance of chromosomes protein 4', 'GO:0000939', 150653, 'Central component of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.', 'MSDKGIFRTSSTPSIVDVTPDRGERPRKLVRSVLESPSQKDVASIVKIEQTPSRPFFNDFLKKRITDSLNERPNLLNKFMSAQDGTPSKSTGFNERSSQLVSEFTTTEDIENCEETTQVLPPRLVVYELRLTNFKSYAGTQIVGPFHPSFSSIVGPNGSGKSNVIDALLFVFGFRASKLRQSKASALIHKSATHPSLDSCDVEITFKEVNSDFTYVDGSELTVRRTAYKNNTSKYFVNGVESSFSAVSNLLKEKGIDLNHKRFLILQGEVESIAQMKPRAISEGDDGLLEYLEDIIGTSKYKPIIEENMQELSNSDDICAEKESRLKLVLSEKAKLEDSKNSVLSFLKDENELFMKQNQLYRTILYETRNKKTLVQNLLNSLEGKLQAHLEKFEQTERDISEKNEEVKSLREKAAKVKNDCTSEKKTRQSYEQQTVKIEEQLKFLLNKEKKLKKSIEALSFEKSEAENSLSSHDIDSQKLNSEIADLSLRLQQEELSLDDIRKSLQGKTEGISNAIEEKQKAMAPALEKINQLTSEKQILQVELDMLLNKENDLINDVESSQSSLDKLRNDAEENRNILSSKLKVLSDLKGEKKDVSKNIERKKETVHNTYRNLMSNRTKLEEMKASLSSSRSRGNVLESLQRLHESDNLNGFFGRLGDLATIDEAYDVAISTACPALNHIVVDNIETGQKCVAFLRSNNLGRASFIILKELAQKNLARIQTPENVPRLFDLLRFNDQKFAPAFYNVLQNTLVAKNLEQANRIAYGKTRWRVVTLSGQLIDKSGTMTGGGTRVKKGGMSSAITSDVSPASVETCDKQVQLEDTRYRQHLSELESLNQRFTEISERIPSAELEISKLQLDVSACDRLVAGEERRILQLKSDLKSIRNNNERKRNLQNKISNMDKEVEAININNEGLVTEIKTLQDKIMEIGGIRYRIQKSKVDDLHEQLKFVKDKLNKMSFKKKKNEQRSQSFQVELSNLTSEYDTTTESIATLKTELQSLNKYVDEHKSRLREFENALWDINSSIDELVKFIEFESKQMNSVKAERIELENQIQEQRTALSEVGNNENKYLKLMSNLKLHNLTEFCDQTTMDSTFPEYSEDELSSVDKSELVSNISVLKKKTEDREVDINVLSEYRRCNKEAEKRDSDYQSELQKRTDLKKVVTDLQSQRLDEFMYGFGIISMKLKEMYQIITMGGNAELELVDSLDPFSEGVLFSVMPPKKSWKNISNLSGGEKTLSSLALVFALHNYKPTPLYVMDEIDAALDFKNVSIVANYIKERTKNAQFIVISLRSNMFELSSRLVGIYKTANMTKSVTINNKEILTD', 1324, 'P41004; Q9UTW4; Q9UUF8;', 'KD00423', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cut3', '#Structural maintenance of chromosomes protein 4#Cell untimely torn protein 3#Chromosome segregation protein cut3', '-', '-', '2539817'),
(424, 'P41003', 'Structural maintenance of chromosomes protein 2', 'GO:0000939===k', 134137, 'Central component of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.', 'MKIEELIIDGFKSYAVRTVISNWDDQFNAITGLNGSGKSNILDAICFVLGITNMSTVRAQNLQDLIYKRGQAGITRASVTIVFNNRDPASSPIGFENHPQVSVTRQIIMGGTSKYLINGHRALQQNVQNLFQSVQLNINNPNFLIMQGRITKVLNMKATEILSMIEEASGTRMFEERKEKAFRTMQRKEAKVEEINTLLREEIEPRLTKLRTEKKTFLEYQHIYNDLERLSHLCTAYDYYKLSLKVEELTVQASQKHSHIAEMESSLQTSKQEVLILKEKIKKIEDERMRQMSVSSDRTLDSQLQTVNENITRISTSIELKNTALEEEHGDLQQIRGKAKELETLLRGKRKRLDEVLSVYEKRKDEHQSISKDFKSQEELISSLTTGLSTTEGHETGYSRKLHEARDTLNDFKAEKETNRLKLEGLNKQISLTKPKKAEATKRCDQLNREIDILQNHVEKLKMSLKNTNSDITGEDVLQQKLKQLAKDRGNLLNELDALKSKLAYMEFTYTDPTPNFDRSKVKGLVAQLLTLNEENYDKQTALEITAGGRLYNLIVETEKIGAQLLQKGNLKRRVTIIPLNKITSFVASAERVGAAKKISNNKAQLALELIGYDDELLPAMQYVFGSTLVCDTPESAKKVTFHPSVKLKSVTLDGDVYDPSGTLTGGSVNKSAGPLLQIQKLNSLQLKLQVVTSEYEKLETQLKDLKTQNANFHRLEQEIQLKQHELTLLIEQRETDSSFRLLSDYQQYKDDVKDLKQRLPELDRLILQSDQAIKKIERDMQEWKHNKGSKMAELEKEFNQYKHKLDEFTPILEKSENDYNGVKLECEQLEGELQNHQQSLVQGESTTSLIKTEIAELELSLVNEEHNRKKLTELIEIESAKFSGLNKEIDSLSTSMKTFESEINNGELTIQKLNHEFDRLEREKSVAITAINHLEKENDWIDGQKQHFGKQGTIFDFHSQNMRQCREQLHNLKPRFASMRKAINPKVMDMIDGVEKKEAKLRSMIKTIHRDKKKIQDTVKSIDRFKRSALEKTWREVNSSFGEIFDELLPGNSAELQPPENKEFTDGLEIHVKIGSIWKDSLAELSGGQRSLVALALIMSLLKYKPAPMYILDEIDAALDLSHTQNIGRLIKTKFKGSQFIIVSLKEGMFTNANRLFHVRFMDGSSVVQAR', 1172, 'P41003; Q9P7E2;', 'KD00424', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cut14', '#Structural maintenance of chromosomes protein 2#Cell untimely torn protein 14#Chromosome segregation protein cut14', '-', '-', '2541319'),
(425, 'P17676', 'CCAAT/enhancer-binding protein beta', 'GO:0000779', 36106, 'Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Binds to regulatory regions of several acute-phase and cytokines genes and probably plays a role in the regulation of acute-phase reaction; inflammation and hemopoiesis. The consensus recognition site is 5''-T[TG]NNGNAA[TG]-3''. Plays an important role in adipose tissue differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG) as well as other adipogenesis key player genes. {ECO:0000269|PubMed:20829347}.', 'MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSGHC', 345, 'P17676; A8K671; Q96IH2; Q9H4Z5;', 'KD00425', 'Homo sapiens (Human)', 'CEBPB', '#CCAAT/enhancer-binding protein beta#C/EBP beta#Liver activator protein#LAP#Liver-enriched inhibitory protein#LIP#Nuclear factor NF-IL6#Transcription factor 5#TCF-5', 'BIOMD0000000543,Qi2013 - IL-6 and IFN crosstalk model (non-competitive);BIOMD0000000544,Qi2013 - IL-6 and IFN crosstalk model;', 'ENSG00000172216', '-'),
(426, 'Q6BNN6', 'Probable kinetochore protein SPC25', 'GO:0000777', 26658, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSTANKSPIDEFESLQSLMNDFSAKFDTALTQKRSAIINDKQLHYVKVNELKNQETQLQSDIEGLKQKEIKVKDTIKRTMEDLQMQQLKVDELARKQDSLLDEKDELQTEIDNLSSQVQTTTDSLEKSSNNLAEQLRKDYPELLKYEQHLGLKIEVIGQDSLKFVFSNIDPNDLDKEVWCELLVGGELFKVGDSFPPLAPDIITLLENEFNHHREFVKFLKTVRALLMDLI', 231, 'Q6BNN6;', 'KD00426', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '2902758'),
(427, 'Q8C4M7', 'Centromere protein U', 'GO:0000777', 46370, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression (By similarity). {ECO:0000250}.', 'MAARRSLRYSGNPGAKHSKNTLRSTYSRKQKAGPKPRPKDVFDFSNNSDASSIPGALEEEEETYETFDPPLHSTAIYAEDELSKHCVSSSSLATHRGKASRNLDPSEDEASGNESIKVSTKKPRRKLEPISGESDSSADDVRRRVASAEGPRSQQRQAAPAAPSPPERPAEPVTPRRTRLHSAQLSPVDETPATQSQLKTQKKVRPSPGRRKRPRRGHTDTDGSESMHIWCLEGKRQSDITELDVILSVFEKTFLEYKQRVESESCNQAINKFYFKMKGELIRMLKEAQMLKALKMKNTKIIANMEKKRQRLIEVQDELIRLEPQLKQLQTKYDDLKERKSSLKKSKHFLSNLKQLCQDYSNVQEKGPKGTGKYDSSSLPALLFKARSILGAENHLRTINYQLGKLLELD', 410, 'Q8C4M7; Q6UNA2; Q9D9U1;', 'KD00427', 'Mus musculus (Mouse)', 'Cenpu', '#Centromere protein U#CENP-U#MLF1-interacting protein', '-', '-', '71876'),
(428, 'P38989', 'Structural maintenance of chromosomes protein 2', 'k', 133928, 'Central component of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.', 'MKVEELIIDGFKSYATRTVITDWDPQFNAITGLNGSGKSNILDAICFVLGIASMSTVRASSLQDLIYKRGQAGVTKASVTIVFDNTDKSNSPIGFTNSPQISVTRQVVLGGTSKYLINGHRAPQQSVLQLFQSVQLNINNPNFLIMQGKITKVLNMKPSEILSLIEEAAGTKMFEDRREKAERTMSKKETKLQENRTLLTEEIEPKLEKLRNEKRMFLEFQSTQTDLEKTERIVVSYEYYNIKHKHTSIRETLENGETRMKMLNEFVKKTSEEIDSLNEDVEEIKLQKEKELHKEGTISKLENKENGLLNEISRLKTSLSIKVENLNDTTEKSKALESEIASSSAKLIEKKSAYANTEKDYKMVQEQLSKQRDLYKRKEELVSTLTTGISSTGAADGGYNAQLAKAKTELNEVSLAIKKSSMKMELLKKELLTIEPKLKEATKDNELNVKHVKQCQETCDKLRARLVEYGFDPSRIKDLKQREDKLKSHYYQTCKNSEYLKRRVTNLEFNYTKPYPNFEASFVHGVVGQLFQIDNDNIRYATALQTCAGGRLFNVVVQDSQTATQLLERGRLRKRVTIIPLDKIYTRPISSQVLDLAKKIAPGKVELAINLIRFDESITKAMEFIFGNSLICEDPETAKKITFHPKIRARSITLQGDVYDPEGTLSGGSRNTSESLLVDIQKYNQIQKQIETIQADLNHVTEELQTQYATSQKTKTIQSDLNLSLHKLDLAKRNLDANPSSQIIARNEEILRDIGECENEIKTKQMSLKKCQEEVSTIEKDMKEYDSDKGSKLNELKKELKLLAKELEEQESESERKYDLFQNLELETEQLSSELDSNKTLLHNHLKSIESLKLENSDLEGKIRGVEDDLVTVQTELNEEKKRLMDIDDELNELETLIKKKQDEKKSSELELQKLVHDLNKYKSNTNNMEKIIEDLRQKHEFLEDFDLVRNIVKQNEGIDLDTYRERSKQLNEKFQELRKKVNPNIMNMIENVEKKEAALKTMIKTIEKDKMKIQETISKLNEYKRETLVKTWEKVTLDFGNIFADLLPNSFAKLVPCEGKDVTQGLEVKVKLGNIWKESLIELSGGQRSLIALSLIMALLQFRPAPMYILDEVDAALDLSHTQNIGHLIKTRFKGSQFIVVSLKEGMFANANRVFRTRFQDGTSVVSIM', 1170, 'P38989; D6VTR1;', 'KD00428', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SMC2', '#Structural maintenance of chromosomes protein 2#DA-box protein SMC2', '-', '-', '850589'),
(429, 'O75151', 'Lysine-specific demethylase PHF2', 'GO:0000777===SCL===k', 120775, 'Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself; and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters; where PHF2 mediates demethylation of dimethylated ''Lys-9'' of histone H3 (H3K9me2); followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated ''Lys-4'' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA. {ECO:0000269|PubMed:20129925; ECO:0000269|PubMed:21167174; ECO:0000269|PubMed:21532585}.', 'MATVPVYCVCRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEKTHGKSTLKKKRTWHKHGPGQAPDVKPVQNGSQLFIKELRSRTFPSAEDVVARVPGSQLTLGYMEEHGFTEPILVPKKDGLGLAVPAPTFYVSDVENYVGPERSVDVTDVTKQKDCKMKLKEFVDYYYSTNRKRVLNVTNLEFSDTRMSSFVEPPDIVKKLSWVENYWPDDALLAKPKVTKYCLICVKDSYTDFHIDSGGASAWYHVLKGEKTFYLIRPASANISLYERWRSASNHSEMFFADQVDKCYKCIVKQGQTLFIPSGWIYATLTPVDCLAFAGHFLHSLSVEMQMRAYEVERRLKLGSLTQFPNFETACWYMGKHLLEAFKGSHKSGKQLPPHLVQGAKILNGAFRSWTKKQALAEHEDELPEHFKPSQLIKDLAKEIRLSENASKAVRPEVNTVASSDEVCDGDREKEEPPSPIEATPPQSLLEKVSKKKTPKTVKMPKPSKIPKPPKPPKPPRPPKTLKLKDGGKKKGKKSRESASPTIPNLDLLEAHTKEALTKMEPPKKGKATKSVLSVPNKDVVHMQNDVERLEIREQTKSKSEAKWKYKNSKPDSLLKMEEEQKLEKSPLAGNKDNKFSFSFSNKKLLGSKALRPPTSPGVFGALQNFKEDKPKPVRDEYEYVSDDGELKIDEFPIRRKKNAPKRDLSFLLDKKAVLPTPVTKPKLDSAAYKSDDSSDEGSLHIDTDTKPGRNARVKKESGSSAAGILDLLQASEEVGALEYNPSSQPPASPSTQEAIQGMLSMANLQASDSCLQTTWGAGQAKGSSLAAHGARKNGGGSGKSAGKRLLKRAAKNSVDLDDYEEEQDHLDACFKDSDYVYPSLESDEDNPIFKSRSKKRKGSDDAPYSPTARVGPSVPRQDRPVREGTRVASIETGLAAAAAKLSQQEEQKSKKKKSAKRKLTPNTTSPSTSTSISAGTTSTSTTPASTTPASTTPASTSTASSQASQEGSSPEPPPESHSSSLADHEYTAAGTFTGAQAGRTSQPMAPGVFLTQRRPSASSPNNNTAAKGKRTKKGMATAKQRLGKILKIHRNGKLLL', 1096, 'O75151; Q4VXG0; Q8N3K2; Q9Y6N4;', 'KD00429', 'Homo sapiens (Human)', 'PHF2', '#Lysine-specific demethylase PHF2#1.14.11.-#GRC5#PHD finger protein 2', '-', 'ENSG00000197724', '-'),
(430, 'Q10198', 'Kinetochore protein ndc80', 'GO:0000778===GO:0051315===GO:0051455===GO:0031617===c;k', 71859, 'Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Acts as a component of the essential kinetochore-associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:15728720}.', 'MQDSSSYARRYSQAPSSSNLRTTTFGFNGLGTSRTSLAPQRTLVNARQSIDPDGLSSRVLTPTMRPSLAPNTRRSSVRVSNASFISQTPNITSIKDPRPLSDRRYQQECATQVVNYLLESGFSQPLGLNNRFMPSTREFAAIFKHLYNKLDPNFRFGARYEEDVTTCLKALNYPFLDSISRSRLVAIGSPHVWPAILGMLHWVVSLIQCTEKAVAMVYTVEQNSLDDHLVDKVLFDYLVRTYHLYLDESPEESEPEKELKATFNQQNQDLYNQTEALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQLDRNLNMIGSKISELRKEVFDTDLLIQASIDSLEKKVQKFNSLAYRIGIVPIAAIRSANNDFELEINPEGPNYINLDLKNKVRPFINEVRRSITLEFHEEQNKSLKLQEHVDTVNDLIAELQDELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHNSMLQLDQRIQSINIEADQIAHACMEYKNNIYKEVAFVLGEIIHFKLHVQDSLEDLKMDYQKELDDLSRSEL', 624, 'Q10198;', 'KD00430', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ndc80', '#Kinetochore protein ndc80#NMS complex subunit ndc80', '-', '-', '2540097');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(431, 'Q96M86', 'Dynein heavy chain domain-containing protein 1', 'GO:0003777', 533644, '', 'MVPEERRVGLSSDETSSDSLKSWHSICVLDSKEQPLACQQKQRQFVKPVTESEQPTVLELLLAELRTLFSAVLQDSSPAAWRYLHAVLGLLPPYRELLVGHLDLLPFLEQLYCWAPWVQTHLHLDLLGAIVQAFPPDSSLLDSASHADCCPQKRRLHHRPPCPACPFVQAQWSRQQVKEELATWLRPLTLPELQRCLGIVGAQVALEEAVWLDGLSLLPLALAADIPVRYESSDTDNAEVEPVGRKETRSQLDYEVPREKAFQKSSTGFSPETSFLDSQVMTALKMERYLKKIHFLYLNVAPSRYFRPYSLMVVPPDKVNPEHYIFSPFGILHVHPVEGSETMTLGTWHHHCVLWQQLQFIPFFKYCLLRKSFTCWKKNVRLQGLHRLQKFLENHLLLAVPHFGAGLLHISRLLQELHSVSWLPQELDRCYELLDLQTALAEEKHKALRLLHRCLNLCTSILRLVHEDTYHMQQCLQERVQNCDRIRTGQGSIYLQRVQHKQLEQKLKQAEAWWLQLGKFARLVDYMICQSLISVLEEQITSFVANILQAPRQKPFLSSQLVFDDHGQLSHVPCVENMIQTLTGGLQSVKTSALQVVQSADLKTSSDSLYSEEEDEEEDSKDEFLMPKFQGQPSDAVSIFCGPNVGLVWPWKSHPIAGILEVRGCRLRGQYFPHNYKQLEEDLDNNPKIQQALNIQQVLLEGVLCKVQEFCREHHWITGIYEFLQSWGPQKLEDMRGGPIKNYVTLVSRLNVWQARVSSMPIELLTKGGLLLLSCHDVQAEMESKLNSIRKDILAHVQNECWNLSQQLMTELTDFMHIFRTINSDIHAIAQCTQKLNEANEQYVELEERMEYVRALHELIRNHFSLFSAENEALDISVRRQFGESPIPPCPPPPQPHLLHCPLLAPQLLDMWEAFQFEKSQASEFLLSKRHAIMPKLQQLMAAALAELEGLLAKALSGPFMDPTQDQRSTEHQLVSLERQFQNTVSDLSELHHAYAIFTEDETPVPLPICGTRPIVQQQRIWHLYRVISENISEWKCMAFAKFSPAMAQEKTEGWLTEAARMSTTLELHSPVLQHCMRILGEFRSYLPLLTKLGSLHPQSLNCQCLLRALGLGSLQTIELLTLGQLLTYPLLEFADRINQVWQNENERIHAQETIRRLQRYWEARQLRLLNFILHVPYEPPASERSKRQVLRSPQWEVVDKDSGTFILSDYSNLQDSIQESLQVLSKILAIEKSGDLNKIALEWVAIMHGLGALLEVWLTFQQKWIFLNKVLHEMKIQFPNADLNSRFKVMDDQYRTLMRISVADPMVLSLVVPSAERSPYFQGQQLQQLLQAGSVELEGIIMSLESVLYGVCAHFPRLFFLSDSELVALLAARLESCEAQLWVRRCFPHVHAVSFRSCPTGEKNTDDWESSPNTQTQVEALAVLGAGGEEVKLQGPLPLHPDLPKWLASLEKCLRLALVHMLQGCVAARLARGPSLGEALKQLPKQNKLYLQLYVQHWIDLVQAFPWQCVLVAEEVVWRAEMEEALLEWGTLAMVSMHMRKLEVLVNFMRAQRASQGGQSLPSVRQTSLLSALLVMAVTHRDIAQLLEQHQVSDLTDFHWVRQLKYHLGSPHIIPKSPLQSLKTIASSEPSLSPAACWIDVLGRSFLYNYEYLGPRLGPLPSLLPERPALVLLLALEEVACGTVLGPNGVGKRAIVNSLAQALGRQLVMLPCSPQIEAQCLSNYLNGALQGGAWLLLEKVHQLPPGLLSALGQRLGELHHLYAPLYQEASRNTSTIDPTQPQLLGSSFFEKHHVSVRLGYGCLLVLRALSSAVPANLHLLLRPVALALPDLRQVAELTLLGAGMRDAFQMATRLSKFFSLERELVSGPLPCRLPLLKQILEDTIRTLNVTKEEPKCQKPRSLAAIEEAALLRSPLFSILNGLHLHNLRGLLCALFPSASQVLAEPMTYKLMKPLVVEELQQVGLDPSPDILGSLEQLSQALSRASGILLLGPAGSGKTTCWHSLFKIQNRLAAMEDTSTQGCQPVEITHLYPSGLSPQEFLGWLEGSCWHHGIFPKVLRAAGQCNNMGQKRQTEESIGIQHWIICDGASNGAWLDSITCLLSELPQLSLPSGQQIARPPGTFLLMEVADTTGISPTVVGCCALVWCGGEQTWQCILSALMASLPYEYRLQHRTVAELNHMAEVLVPATLRFLTCQGVSSLLQVHGQQAVCAGVAEVTSMARILHSLLDLHLRLKEEKAPGPEDLSYSDPVAQSFRSSKSSFLNRSQVDSDDVPDKCREHLLAVSSFLFALIWGFGAHLPSRFWPIFDTFIRDSISRLSNYPEPPPSALVFDLHVSPEDGTLVPFTGQYLSSHIKGTLGTFHPSIQTERLLYVVDLLLSGGQPVLLAGEAATGKSAFVEVLVEPHHPYIYSPIHPAFSSSHLRLLLSRGIQGQTQASPQPGHHQDSKPSLLFLLEDLHLATSDPEKSCQPVLETLRQAMDGTVYAHSTLELQTLQPTVNFLATVTVPGYCERPLCPRLFRLFTVLALESMTQATLLERHVPIIQAWLERFPSVERERALARGLVRASVEAWEAVCNCFMPSPLHPHYHFSLHSVSHLLSSLQLLPNRTGSRGFVDYPNHQEHLRRVSGLRGTCLTVMMATRNVVRLWLHEAQRTFCDRLDSPRERSYCAKLLLVVAQSVFCCGPGPQHLGKDHQESEEEEEEERVPEVESEGELAQWEDFSNSNSETEEEEEPYGLQVARVSNSRDPSLTPSIGPVSRGMKESISHKIRQEKGTRASNYRLQVRRSFKTWWQKKPQMDLISPLLLPVLLLHPQEKPSDLVFSQELILGPNSETPNLYLERQWEKLEEQLATSAAQLKLSPHLARCHSMAQHVARLVRVLARPRQHGLLLSGALGTGRHTAITLASSICQAHFFHLPSGSEEAILQCLRDASWHAGMLSQPVALLVPSGVDLTTLHRLLALATSGSFPGQYTEADLDRIGEHLPRENLGVKQNIKKEMVLQRFHQQVCSHLHLFFLIGDKQAHKQLPSTLFLRLLQLATASIDRYEPWDQAALAKVAQHHLEGAQSVPLDDGSWKYPDLQASIPSVAKAMALIHLSATHYHEHLCPALPLVTPKTFLDFLDTFLMLQQQTILKIKNKAQRVQNALENLRMLIKEHGTHANLIFDLEQQLKDSGKSLSMFQQQLEQSKLLYKQQLEECRHQENLIENLARQRDALQAQREAFLEQMSKAFLEPLSQLQVADFEEIRSYRAPPESVVRVTDAMCDLFHHETGWASAKQLLCTEDFYQELVFFPKEKITDSELIKLHLILKAPGMDDAALRAVSRPAASLAAWLWAVLHYGLAHCRGLPTDLLLQQVEATLTREQARLGYYQFQAQETLEHNLALAKMVEDAQASHNCVAKTLSQAQCGQYHKWPMKAALLTPMRAWTTQLQKLKGRCMTVFGDTLLCSAAIIYLGPFPPLRRQELLDEWLALCRGFQEALGPDDVAQALKRKQKSVSIPPKNPLLATHSPFSILSLLSSESEQYQWDGNLKPQAKSAHLAGLLLRSPTHYSSCRWPLLLDPSNEALIWLDPLPLEENRSFAPALTEGRGKGLMRNQKRESKTDMKEEDDESEESNEAEDQTKEQKAEERKNEQEKEQEENEEKEEEKTESQGSKPAYETQLPSLPYLSVLSGADPELGSQLQEAAACGLPVLLTNVELGLGCEELQWLLQREQLSPPQVQPGFCLYLSTTLSLCAMEKVLGCELLKGLNVLDLGLNMEILEEQMLHEILCREYPELETRWQDLKIRALDTCKAVEAAEERLLTMLLFQNPKRQKPAKFLRNIVRAQGKLCQLRAHCEELEGQKLQEMVLWAPYRPVVWHGMAMVKALSQLQNLLPLFCMSPENWLAVTKQALDSMKPREINHGEDLASHLLQLRAHLTRQLLGSTVTALGLTQVPLVGALGALALLQATGKASELERLALWPGLAASPSTVHSKPVSDVARPAWLGPKAWHECEMLELLPPFVGLCASLAGHSSAWQAYLSLSSTVLGPAPGPGPEPLSLLQKLILWRVLRPECLAGALADFTTSLLGRPLDENTYAPTMPFKHSQATQPMLILLPPPGHPSATLHPLTVIQKLAAKYQQGQKQLQVIALGSEAWDPVSVVVSTLSQAMYEGHWLVLDNCHLMPHWPKELLQLLLELLGRAKVVADLESEQLLDQPESRNVSTVHRDFRLWLIVPAESSASLPAVLTQHSMPVFWNQSLELGHVLIDSVELAQQVLYMQPPTQALPLLLLHGLLLHRQLYGTRLQAHRGRWSQVTLTQVLQTQDQLWASLSNPRAAMQELAASVFYGGPLGDTEDREALISLTQACLSPSSGSWVQPHTPQSLLATLMPLPELRELDAMAECKAQMHLLPSPPEPRLCGLSEGPQAWLLRRQSRALLSALQRSSPVWVPESRRGAQLAERRLRQRLVQVNRRLESLQDLLTHVIRQDESDAPWSVLGPNARRPLEGVLETEALELSQLVGTLQRDLDCLLQQLKGAPPCPSRRCAAVAHALWTGRLPLPWRPHAPAGPQPPWHWLRQLSRRGQLLVRYLGVGADASSDVPERVFHLSAFRHPRRLLLALRGEAALDQNVPSSNFPGSRGSVSSQLQYKRLEMNSNPLHFRVENGPNPTVPERGLLLIGLQVLHAEWDPIAGALQDSPSSQPSPLPPVSISTQAPGTSDLPAPADLTVYSCPVYMGGPLGTAKLQSRNIVMHLPLPTKLTPNTCVQRRVHVCSPPLS', 4753, 'Q96M86; Q2NKK8; Q6UWI9; Q8NAA2; Q8TEE6; Q9NSZ9;', 'KD00431', 'Homo sapiens (Human)', 'DNHD1', '#Dynein heavy chain domain-containing protein 1#Dynein heavy chain domain 1-like protein#Protein CCDC35', '-', 'ENSG00000179532', '-'),
(432, 'P28025', 'Kinesin-like protein KIF11-B', 'GO:0003777', 120114, 'Plus end-directed motor protein required for establishing a bipolar spindle. Associates with both interphase and spindle microtubules. May be involved in nuclear divisions taking place during the development of unfertilized eggs. {ECO:0000269|PubMed:15583027}.', 'MSSQNSFMASKKEDKGKNIQVVVRCRPFNQLERKASSHSVLECDSQRKEVYVRTGEVNDKLGKKTYTFDMVFGPAAKQIEVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSSDEEFTWEQDPLAGIIPRTLHQIFEKLSENGTEFSVKVSLLEIYNEELFDLLSPSPDVGERLQMFDDPRNKRGVIIKGLEEISVHNKDEVYHILERGAARRKTASTLMNAYSSRSHSVFSVTIHMKETTVDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHIPYRESKLTRILQDSLGGRTKTSIIATVSPASINLEETVSTLDYANRAKSIMNKPEVNQKLTKKALIKEYTEEIERLKRELAAAREKNGVYLSSENYEQLQGKVLSQEEMITEYTEKITAMEEELKSISELFADNKKELEECTTILQCKEKELEETQNHLQESKEQLAQESFVVSAFETTEKKLHGTANKLLSTVRETTRDVSGLHEKLDRKKAVDQHNFQVHENFAEQMDRRFSVIQRTVDDYSVKQQGMLDFYTNSIDDLLGASSSRLSATASAVAKSFASVQETVTKQVSHSVEEILKQETLSSQAKGDLQQLMAAHRTGLEEALRSDLLPVVTAVLDLNSHLSHCLQNFLIVADKIDSHKEDMNSFFTEHSRSLHKLRLDSSSALSSIQSEYESLKEDIATAQSMHSEGVNNLISSLQNQLNLLGMETQQQFSGFLSKGGKLQKSVGSLQQDLDLVSSEAIECISSHHKKLAEQSQDVAVEIRQLAGSNMSTLEESSKQCEKLTSSINTISQESQQWCESAGQKIDSVLEEQVCYLHSSKKHLQNLHKGVEDSCGSSVVEITDRVNAQRQAEEKALTSLVEQVRDDQEMVGEQRLELQEQVQSGLNKVHSYLKEELRNDVPTGTTPQRRDYAYPSLLVKTKPRDVLLEQFRQQQQEYLESISSVISEAVEPPVEQDSLEDEPPVAVNDSVISERSCIDLSMTCQEKGGIRFFQQKKALRKEKENRGNTTLLERSKIMDEVDQALTKSKLPLRMQN', 1067, 'P28025;', 'KD00432', 'Xenopus laevis (African clawed frog)', 'kif11-b', '#Kinesin-like protein KIF11-B#Kinesin-5#Kinesin-related motor protein Eg5-1#XLEg5K1#XlEg5', '-', '-', '397908'),
(433, 'O14343', 'Kinesin-like protein 5', 'GO:0000778===GO:0051315===SCL===k', 99059, 'Has a role in establishing metaphase during mitosis. Required for chromosome segregation where it generates tension during kinetochore capturing. {ECO:0000269|PubMed:11967147}.', 'MSRQSSITVTVRVRPFSTAESANLIASSDRLSFGTSSSLRNPGSGRQIRRVVKVLDGRVLVFDPPDETTATLSATNRRLSTSQQSLARLSRKSNNSAGFGRDLRYAFDRVFDETATQQQVYERTARPLLDNILDGFNATIFAYGATGCGKTHTISGTMQDPGLIYLTLKELFERMDHLRDEKIFDLRLSYLEIYNETIRDLLVSPTPNQAKPLNLREDADRRITVPGLTSLSPESLEEIIDIIMKGNANRTMSPTEANAASSRSHAVLQVTLIQKPRTAGINEDHTLATLSIIDLAGSERATATKLRGSRLFEGANINKSLLALGNCINALCDPHRRAHVPYRDSKLTRLLKFSLGGNCRTVMIVCVSPSSVHYEETHNTLKYANRAKNIKTEVLRNMISVDRHVSQYVKAIVELREQISELENRLAQIDLSSQSNGSDQDAVTQSFAHESKLAEARNLLRMTFEETLPLQNDTINKVEKVKHFDDSIRVLKYWLSCYERILPNSADERVFLVRSKLESLLTRRAEIIADIDPELVYQKFQRSVSHIINTYKQEGATMYADVLQDEVDLLKSIIENQVLDAQNKVDEFTPVLESLLRSSFKASSLLKEGGMQELFSILEKWLLGIGLGEKPNISVLSESYKLNSTSDDSRTINRDRVHSFPTQPLLNNNLPRMFFVKSPKKPVVFSKRSPKKRVRFDDSMSTSDSGASAYNSPIQTSKLKNMNFFNTMHMPSTPAHKRPENKNQIDVEINLTSPVSPMLEDKPEPGLLIKSPLEKKQEVNSESTQLDQLLAEDSSTDDVSLPHLDTIDLDGSPVPKVPDLNFSRANMDSPTFILNNEAIHNFDFSKPKTRQSLSSLTTLHLSNPANIIRKSLSMAENEEEKAT', 883, 'O14343;', 'KD00433', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'klp5', '#Kinesin-like protein 5', '-', '-', '2540361'),
(434, 'P11709', 'Nuclear fusion protein BIK1', 'GO:0000776===GO:0000778===c;k', 51092, 'Required for nuclear fusion; chromosome disjunction; and nuclear segregation during mitosis. Probably required for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation.', 'MDRYQRKIGCFIQIPNLGRGQLKYVGPVDTKAGMFAGVDLLANIGKNDGSFMGKKYFQTEYPQSGLFIQLQKVASLIEKASISQTSRRTTMEPLSIPKNRSIVRLTNQFSPMDDPKSPTPMRSFRITSRHSGNQQSMDQEASDHHQQQEFGYDNREDRMEVDSILSSDRKANHNTTSDWKPDNGHMNDLNSSEVTIELREAQLTIEKLQRKQLHYKRLLDDQRMVLEEVQPTFDRYEATIQEREKEIDHLKQQLELERRQQAKQKQFFDAENEQLLAVVSQLHEEIKENEERNLSHNQPTGANEDVELLKKQLEQLRNIEDQFELHKTKWAKEREQLKMHNDSLSKEYQNLSKELFLTKPQDSSSEEVASLTKKLEEANEKIKQLEQAQAQTAVESLPIFDPPAPVDTTAGRQQWCEHCDTMGHNTAECPHHNPDNQQFF', 440, 'P11709; D6VQY6;', 'KD00434', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'BIK1', '#Nuclear fusion protein BIK1', '-', '-', '850328'),
(435, 'P28023', 'Dynactin subunit 1', 'GO:0003777===GO:0005868', 141930, 'Required for the cytoplasmic dynein-driven retrograde movement of vesicles and organelles along microtubules. Dynein- dynactin interaction is a key component of the mechanism of axonal transport of vesicles and organelles.', 'MAQSKRHMYNRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKILKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRDQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEAKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEESTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCSILISTMNKLATAMQEGEYDAERPPSKPPPVEPWPAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQTLLRKKEKEFEETMDALQADIDQLEAEKTELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGGTPGQAPGALPGPGPVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKFSLPPHEGPGGNLLSGALYRKTSQLLEKLNQLSTYTHVVDITRSSPACKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHGRLIS', 1280, 'P28023;', 'KD00435', 'Rattus norvegicus (Rat)', 'Dctn1', '#Dynactin subunit 1#150 kDa dynein-associated polypeptide#DAP-150#DP-150#p150-glued', '-', '-', '29167'),
(436, 'O88271', 'Craniofacial development protein 1', 'GO:0000777', 32921, 'May play a role during embryogenesis. May modulate tooth organogenesis since alterations of this protein function affect tooth organs size as well as individual cell fate and survival. In embryonic cells; blockage of the function results in increased number of apoptotic cells; reduced proliferation; alterations in cell shape and fibronection matrix synthesis. {ECO:0000269|PubMed:10415329; ECO:0000269|PubMed:11992732; ECO:0000269|PubMed:12153613}.', 'MEEFDSEDFSTSDEDEDYLPSGGEYSEDDVNELVKEDEVDGEEQAEKTKGKRRKAQGIPARKRKQSGLLLEEEEDGKEDSGGSSSEEDEEEQEGGLGSENARKKKEDELWASFLNDVGPKSKAAPGSQTKVAEETEEISSNKPLVKADELDKPRESEKVKITKVFDFAGEEVRVTKEVDAASKEAKSFLKQTEREKPQALVTSPATPLPAGSGIKRASGMSSLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP', 295, 'O88271; O70565; Q9JMA5;', 'KD00436', 'Mus musculus (Mouse)', 'Cfdp1', '#Craniofacial development protein 1#27 kDa craniofacial protein#Bucentaur#Protein Cp27', '-', '-', '23837'),
(437, 'Q9NBD7', 'CLIP-associating protein', 'GO:0051315===c;k', 165576, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Required for several aspects of mitotic spindle formation including the formation of the overlapping central spindle microtubules and kinetochore attachment. Required for the incorporation of tubulin subunits at the plus ends of kinetochore microtubules during poleward microtubule flux. Acts antagonistically to Klp10A and Klp67A to maintain metaphase spindle length. Also required for guidance of CNS axons downstream of Abl. May function to identify a subset of microtubules that probe the peripheral growth cone domain; where guidance signals exert their influence on cytoskeletal organization. Also required during oogenesis for the organization of the polarized microtubule network inside the 16-cell cyst that ensures oocyte differentiation. {ECO:0000269|PubMed:10747094; ECO:0000269|PubMed:10899121; ECO:0000269|PubMed:12034769; ECO:0000269|PubMed:12538517; ECO:0000269|PubMed:15207236; ECO:0000269|PubMed:15240569; ECO:0000269|PubMed:15592460; ECO:0000269|PubMed:16303556; ECO:0000269|PubMed:16723741}.', 'MAYRKPSDLDGFIQQMPKADMRVKVQLAEDLVTFLSDDTNSIVCTDMGFLIDGLMPWLTGSHFKIAQKSLEAFSELIKRLGSDFNAYTATVLPHVIDRLGDSRDTVREKAQLLLRDLMEHRVLPPQALIDKLATSCFKHKNAKVREEFLQTIVNALHEYGTQQLSVRVYIPPVCALLGDPTVNVREAAIQTLVEIYKHVGDRLRPDLRRMDDVPASKLAMLEQKFDQVKQEGLLLPSALKNTNGNGVGLDEADNIGLRERPTRMIKRPLHSAVSSSLRPKPNVNDVTGDAGAVTMESFESSFEVVPQLNIFHAKDMDDIYKQVLVIISDKNADWEKRVDALKKIRALLILSYHTQPQFVAVQLKELSLSFVDILKEELRSQVIREACITIAYMSKTLRNKLDAFCWSILEHLINLIQNSAKVIASASTIALKYIIKYTHAPKLLKIYTDTLNQSKSKDIRSTLCELMVLLFEEWQTKALERNATVLRDTLKKSIGDADCDARRHSRYAYWAFRRHFPELADQIYGTLDIAAQRALEREREGGGGGGTGTGTGTAPETRRTVSRIGRTPGTLQKPTPSMRSISAVDTAAAQRAKVRAQYTLYSRQRKPLGPNNSNQASMTGAAASGSLPRPRLNSNSGGTPATTPGSVTPRPRGRAGVSQSQPGSRSTSPSTKLRDQYGGIGNYYRGATGAIPKKASGIPRSTASSRETSPTRSGGGLMKRSMYSTGAGSRRTPERNNPVRPSAAARLLAQSREAEHTLGVGDDGQPDYVSGDYMRSGGMRMGRKLMGRDESDDIDSEASSVCSERSFDSSYTRGNKSNYSLSGSHTRLDWSTQRAPFDDIETIIQFCASTHWSERKDGLISLTQYLADGKELTQQQLKCVLDMFRKMFMDTHTKVYSLFLDTVTELILVHANELHEWLFILLTRLFNKLGTDLLNSMHSKIWKTLQVVHEYFPTQLQLKELFRIISDSTQTPTTKTRIAILRFLTDLANTYCKSSDFPSDQSQACERTVLKLAQLAADQKSMELRSQARSCLVALYNLNTPQMTLLLADLPKVYQDSARSCIHSHMRRQSQSCNSGANSPSSSPLSSSSPKPLQSPSVGPFASLQSHHHQLSISSTSPRSRQSSVEQELLFSSELDIQHNIQKTSEEIRHCFGGQYQTALAPNGFNGHLQYHDQGQQDSCASLSSNSKTQSSANTTQSNTPESATMRLDNLERERTTQNAKSPTDDAKVITVSINMAENGELILASNLMESEVVRVALTLTKDQPVELLQTSLTNLGICIKGGNCELPNKHFRSIMRMLLNILEAEHTDVVIAGLHVLSKIMRSNKMRHNWMHFLELILLKIIQCYQHSKEALRDIDSMIPRIAPSLPLDLSINIVNPVIATGEFPTNLCAIKILLEVTEHHGSEITDAHLDIVFPNLARSADDTQSMVRKAAVFCIVKLYFVLGEEKVKPKLSVLNPSKVRLLNVYIEKQRNCISGGGSSTKNSSAASSS', 1491, 'Q9NBD7; A4V279; Q9NL57;', 'KD00437', 'Drosophila melanogaster (Fruit fly)', 'chb', '#CLIP-associating protein#Misexpression suppressor of ras 7#Protein Multiple asters#Mast#Protein Orbit#Protein chromosome bows', '-', '-', '43901'),
(438, 'P38991', 'Spindle assembly checkpoint kinase', 'GO:0005828===GO:0000778===GO:0008608===GO:0032133===k', 42946, 'Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by selectively detaching kinetochore-microtubule attachments that are not under tension. Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis. Phosphorylates RGD1 in vitro. {ECO:0000269|PubMed:10975519; ECO:0000269|PubMed:11853667; ECO:0000269|PubMed:12408861; ECO:0000269|PubMed:23454383}.', 'MQRNSLVNIKLNANSPSKKTTTRPNTSRINKPWRISHSPQQRNPNSKIPSPVREKLNRLPVNNKKFLDMESSKIPSPIRKATSSKMIHENKKLPKFKSLSLDDFELGKKLGKGKFGKVYCVRHRSTGYICALKVMEKEEIIKYNLQKQFRREVEIQTSLNHPNLTKSYGYFHDEKRVYLLMEYLVNGEMYKLLRLHGPFNDILASDYIYQIANALDYMHKKNIIHRDIKPENILIGFNNVIKLTDFGWSIINPPENRRKTVCGTIDYLSPEMVESREYDHTIDAWALGVLAFELLTGAPPFEEEMKDTTYKRIAALDIKMPSNISQDAQDLILKLLKYDPKDRMRLGDVKMHPWILRNKPFWENKRL', 367, 'P38991; D6W3G1;', 'KD00438', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'IPL1', '#Spindle assembly checkpoint kinase#2.7.11.1#Aurora kinase#Increase-in-ploidy protein 1', '-', '-', '855892'),
(439, 'P31111', 'Synaptonemal complex protein ZIP1', 'k', 100035, 'Required for meiotic chromosome synapsis and cell cycle progression. May act as a molecular zipper to bring homologous chromosomes in close apposition. ZIP1 may encode the transverse filaments of the synaptonemal complex.', 'MSNFFRDSSMGFKPRPNIFAKLRVRDVDSDSSANTVVENSSNCLDVGSSIEGDDTFKKPHKTSTEQELITSMSLSQRNHGYSDDMEIGSPKKTTSTDQYNRILKNDVAAIENDTDEDFEITEVREVSEGVAKETKESHGDPNDSETTLKDSKMHEYTMTNGKAPLHTSINNSSTSSNDVLLEAFTNTQRICSNLKQELQKQQQDNAKLKVRLQSYASNSDKINEKVGKYKSCLETLQERIATLTSHKNNQETKLKDLRQNHQLYQRRISGFKTSIENLNKTINDLGKNKKEADAELMKKGKEIEYLKRELDDCSGQLSEEKIKNSSLIQEMGKNREEMIKSIENFFSEDKAHHLLQFNKFEERVHDLFEKKLQKHFDVAKDTLNVGLRNTTVELSSNTETMLKQQYEDIKENLEQKMSSSKDEMAKTINELSVTQKGLIMGVQEELLTSSGNIQTALVSEMNNTRQELLDDASQTAKNYASLENLVKAYKAEIVQSNEYEERIKHLESERSTLSSQKNQIISSLGTKEAQYEDLVKKLEAKNIEISQISGKEQSLTEKNENLSNELKKVQDQLEKLNNLNITTKSNYENKISSQNEIVKALVSENDTLKQRIQQLVEIKENEQKDHTTKLEAFQKNNEQLQKLNVEVVQLKAHELELEEQNRHLKNCLEKKETGVEESLSDVKTLKQQVIVLKSEKQDITAEKLELQDNLESLEEVTKNLQQKVQSQKRELEQKIKELEEIKNHKRNEPSKKGTQNFTKPSDSPKKNATTSNLFPNNSAAIHSPMKKCPKVDHISKSRINSSKETSKFNDEFDLSSSSNDDLELTNPSPIQIKPVRGKIKKGSNCMKPPISSRKKLLLVEDEDQSLKISKKRRRK', 875, 'P31111; D6VSR5;', 'KD00439', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'ZIP1', '#Synaptonemal complex protein ZIP1', '-', '-', '851879'),
(440, 'Q9JHY7', 'Baculoviral IAP repeat-containing protein 5', 'GO:0000777===GO:0032133', 16692, 'Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokenesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). {ECO:0000250}.', 'MGATALPPIWQMYLKDHRIYTFKNWPFLEDCSCTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQVEELTVSEFLKLDKQRAKNKIAKETNNKQKEFEETRRTVRQSIEQLAALR', 142, 'Q9JHY7;', 'KD00440', 'Rattus norvegicus (Rat)', 'Birc5', '#Baculoviral IAP repeat-containing protein 5#Apoptosis inhibitor survivin', '-', '-', '64041'),
(441, 'Q8C0N1', 'Kinesin-like protein KIF2B', 'GO:0000777===GO:0003777', 75469, 'Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. Has microtubule depolymerization activity (By similarity). {ECO:0000250}.', 'MASQFCLPLAPRLSPLKPLKSHFTDFQVGICVAIQRSDKRIHLAVVTEINRENSWVTVEWVEKGVKKGKKIELETVLLLNPALASLEHQRSRRPLRPVSVVPSTAIGDQRTATKWIAMIPHRNETPSGDSQTLMIPSNPCLMKRKKSPCLREIEKLQKQREKRRRLQLEIRARRALDINTGNPNFETMRMIEEYRRRLDSSKMSSLEPPEDHRICVCVRKRPLNQRETTMKDLDIITIPSHNVVMVHESKQKVDLTRYLENQTFCFDHAFDDKASNELVYQFTARPLVESIFRKGMATCFAYGQTGSGKTHTMGGAFLGKAQDCSKGIYALVAQDVFLLLKTPAYEKLELKVYGTFFEIYGGKVYDLLNWKKKLQVLEDGNQQVQVVGLQEQEVSCVEEVLNLVELGNSCRTSGQTSVNAHSSRSHAVFQLILKAGGKLHGKFSLVDLAGNERGADTAKATRKRQLEGAEINKSLLALKECIRALGKNKSHTPFRASKLTQVLRDSFIGQNSYTCMIATISPGMTSCENTLNTLRYANRVKELALEARPYHHCVSPPGHEVPLMIENDNTNSGKSLQRDEVIQIPTVEKEEEKESDELTSKKEPAASWSRSNQWWEAIQETAEGVNGDVDFCIAQSLSVLEQKIGVLTDIQKKLQSLREDLQKKSQVE', 668, 'Q8C0N1;', 'KD00441', 'Mus musculus (Mouse)', 'Kif2b', '#Kinesin-like protein KIF2B', '-', '-', '73470'),
(442, 'Q7TSY8', 'Shugoshin-like 2', 'GO:0000776===GO:0000777===GO:0000779===GO:0000780===k', 130277, 'Cooperates with PPP2CA to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Has a crucial role in protecting REC8 at centromeres from cleavage by separase. During meiosis; protects centromeric cohesion complexes until metaphase II/anaphase II transition; preventing premature release of meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is thus essential for an accurate gametogenesis. May act by targeting PPP2CA to centromeres; thus leading to cohesin dephosphorylation. Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. {ECO:0000269|PubMed:18084284; ECO:0000269|PubMed:18765791}.', 'MEYPGIKVDTVTSGIQRRVKGRIAKTNLNVSLASKIKAKILNNSSIFKISLKHNNRALARALSKEKENSRRITTEKMQLQKEVEKLNFENTFLRLKLNTLNKKLVEIESHVSNDLLTAIEISSLSEFHQGSFLLSATKKQRNSKQCKPAHLPYARVLLTSENDDDDGADDKWQTKCNNRTISKTSPDSTSSVSRQPSSLHQCNLKAFPPKEDNQKTCGSGHLEHTSSVDILPNESHSDQSPKSSLSEMKTAPSPSLRREKLSHGNVTMRKKCVSSTPDILYVTDLDHQPTSSPGSNWNNEIHGHTNETSNNTQRNAECFLDLPSESSSEPDAKRMELVQKNTDSFHFQKTVYDAADMELTATDIGKIVAVSKSKKNQNKKKADCRKETFRKVKGASSDKKRESSKRECKDGSEVGAEEEADAARAERGAGVLDGRGDSEEPNCISSTEQPSQVNTQKKRTLQNSSDQENIQNTKRRQTYTTDEQEETNPFSRHSVKFLQDGKFDLCQKTLHHNLSKPSRQTFVIRKSEKDNLFPNQEDKDTISENLEVTNEFHIDDLSIEANENVCDHETQTMLDLKKSVSAQQNQTKINKTKQKINRRTKIISVMSQVYEDNDKDIHVLEKDNFPFHTQANKETTSGNLESSKEFESPLLFTRDNGSLRDCKTQNVLDLHKQIPDLYPDRNESQISKIPRQKVNRKTEVISGVKCFSNDQGVHCSEKDKSLLLQKDKDFPGTLKDLSEFDTPAFCNKDSAKSCDYKSEMLLGLKKHDPNMQPACQDDSKAGKKLRQKVNRKTEIISKITQIHENDRGSTHDSLNKKLCQKVNISKIISQMNQIYETINEDGNGFKSSIKDCEDIKSCDFGEINSNKKENYDPIQDPCTLVKKTKRKGSCKAGSSLAGAKNRCGLQLTDSSQVQSVPLDSGLRHHPNEADSGPGEQTNLPKMQKQSAGRSLGDAFSVSLGKEGSRPAKAVSKMTPKSKKRKLPLGCSPETHGTVEITPNTDLAKAVDSQQTEKENYLEKEKIAKRKPDFCTKVLKPLSETCSSNIKNSSLDSMCKSSLPLSISSRKTLMLEESSSLESTCIFQVGDAAHEKITTGTRNPHHRTQKSTPGSRTSLVLVDTSSVSDTNPANPENESEGQSSHPMRRKRQCVPLNLTEPSLRSKMRR', 1164, 'Q7TSY8; Q811I4; Q8C9C4; Q8CGJ4; Q9CS55;', 'KD00442', 'Mus musculus (Mouse)', 'Sgol2', '#Shugoshin-like 2#Shugoshin-2#Sgo2', '-', '-', '68549'),
(443, 'Q0MS45', 'Presenilin-2', 'GO:0000776', 50138, 'Probable catalytic subunit of the gamma-secretase complex; an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins (By similarity). {ECO:0000250}.', 'MLTFMASDSEEEVCDERTSLMSAESPTPRSCQEGRQGLEDGESAAQWRSQDSEEDHEEDPDRYVCSGVPGRPPGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLITSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLFLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEVFEPPLPGYPGEELEEEEERGVKLGLGDFIFYSVLVGKAAATGSGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI', 448, 'Q0MS45;', 'KD00443', 'Sus scrofa (Pig)', 'PSEN2', '#Presenilin-2#PS-2#3.4.23.-#Presenilin-2 NTF subunit#Presenilin-2 CTF subunit', '-', '-', '780410'),
(444, 'Q9WU62', 'Inner centromere protein', 'GO:0000776===GO:0000777===SCL===k', 101209, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Probably acts through association with AURKB or AURKC. Seems to bind directly to microtubules. Controls the kinetochore localization of BUB1 (By similarity). {ECO:0000250}.', 'MGTTAPGPICLLDLCDQKLLDFVCNVDNKDFMWLKEIEEEAERMFIREFSNEPELMPKTPSQKNRRKKRRVSNIQDENRDPVRKRLSRRKSRSSQVGTRHLRSKPVTIVEENGFPVLQRITRATAAAAAAAAAASVASASSSSTAGSPTVLTKKAVVEISTSERLSAELQLTKLKGSLPPSPVSQGTLTSEEELTPKKSEAGKLDSVTVNSLKATPQSPKNRGVGEGRSVSKLKIARASWGLQDSPGSTDSPWQERVLSPILLNNILPTTAKSPLGNIRSVRRSLISQDSQVPLASKYNLVAKQENGSRRSSRRIAKKAGKEPEASARIICHSYLERLLNVEVPQNVGLEQEPVEVAEPEEAEEEQEVSKNSGCPSKPRSATKIAISTPTSKPAAAGQTTTVEEQEAELDQTDGHREPPQSVRRKRSYKQAISEPDEEQLEDEELQPCQNKTPSPPCPANKVVRPLRTFLHTVQKNQMLMTPTLASRSSVMKSFIKRNTPLRVDPKCSFVEKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARRLAEQREQERRREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQLQEEQAKKAKEVAAARKVLNMTVDVQSPVCTSYQMTPQGPKSIPKISVDDYGMDLNSDDSTDDESHPRKPIPSWAKGTQLSQAIVHQYYHPPNILELFGSILPLDLEDIFKKRKTRYHKRTSSAVWNSPPLKATMVPSSGD', 880, 'Q9WU62; Q7TN28; Q8BGN4; Q8CGI4;', 'KD00444', 'Mus musculus (Mouse)', 'Incenp', '#Inner centromere protein', '-', '-', '16319'),
(445, 'Q9WTU0', 'Lysine-specific demethylase PHF2', 'GO:0000777', 120814, 'Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself; and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters; where PHF2 mediates demethylation of dimethylated ''Lys-9'' of histone H3 (H3K9me2); followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated ''Lys-4'' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA (By similarity). {ECO:0000250}.', 'MATVPVYCVCRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEKTHGKSTLKKKRTWHKHGPGPTPDVKPVQNGSQLFIKELRSRTFPSAEDVVSRVPGSQLTVGYMEEHGFTEPILVPKKDGLGLAVPAPTFYVSDVENYVGPERSVDVTDVTKQKDCKMKLKEFVDYYYSTNRKRVLNVTNLEFSDTRMSSFVEPPDIVKKLSWVENYWPDDALLAKPKVTKYCLICVKDSYTDFHIDSGGASAWYHVLKGEKIFYLIRPASANISLYERWRSASNHSEMFFADQVDRCYKCTVKQGQTLFIPSGWIYATLTPVDCLAFAGHFLHSLSVEMQMRAYEVERRLKLGSLTQFPNFETACWYMGKHLLEAFKGSHKSGKQLPPHLVQGAKILNGAFRSWTKKQALAEHEDELPEHFRPSQLIKDLAKEIRLSENASKTVRPEVNAAASSDEVCDGDREKEEPPSPVETTPPRSLLEKVSKKKTSKTVKMPKPSKIPKPPKSPKPPKTLKLKDGSKKKGKKCKESASPTIPNLDLLEAHTKEALTKMEPPKKGKTPKSVLSVPNKDTVHTQNDMERLEIREQTKSKSEAKWKYKNSKPDSLLKMEEEQRLEKSPLAGNKDKFSFSFSNRKLLGSKALRPPSSPGVFGALQSFKEDKAKPVRDEYEYVSDDGELKIDEFPIRRKKSAPKRDLSFLLDKKEALLMPTSKPKLDSAVYKSDDSSDEGSLHIDTDTKPGRNAKVKKESGSSAAGILDLLQASEEVGALEYNPNSQPPASPSTQEAIQGMLSMANLQASDSCLQTTWGTGQAKGGSLAAHGARKIGGGNKGTGKRLLKRTAKNSVDLEDYEEQDHLDACFKDSDYVYPSLESDEDNPVFKSRSKKRKGSDDAPYSPTARVGPSVPRQDRPVREGTRVASIETGLAAAAAKLSQQEEQKNRKKKNTKRKPAPNTASPSISTSASASTGTTSASTTPASTTPASTTPASTTPASTSTASSQASQEGSSPEPPPESHSSSLADHEYTAAGTFSGSQAGRASQPMAPGVFLTQRRPSASSPNNTAAKGKRTKKGMATAKQRLGKILKIHRNGKLLL', 1096, 'Q9WTU0; Q6A023; Q80WA8;', 'KD00445', 'Mus musculus (Mouse)', 'Phf2', '#Lysine-specific demethylase PHF2#1.14.11.-#GRC5#PHD finger protein 2', '-', '-', '18676'),
(446, 'Q8N2Z9', 'Centromere protein S', 'GO:0000777===k', 15893, 'DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Required for optimal chromatin association of the FA core complex. Required for efficient damage-induced monoubiquitination and focus formation of FANCD2. Stabilizes FAAD24; FANCM and STRA13/CENPX in the FA core complex. Plays a role in DNA interstrand cross-linking (ICL) repair and in recovery of replication forks stalled by topoisomerase I-DNA cleavage intermediates induced by camptothecin. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation. Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. {ECO:0000269|PubMed:19620631; ECO:0000269|Ref.7; ECO:0000269|Ref.8}.', 'MEEEAETEEQQRFSYQQRLKAAVHYTVGCLCEEVALDKEMQFSKQTIAAISELTFRQCENFAKDLEMFARHAKRTTINTEDVKLLARRSNSLLKYITDKSEEIAQINLERKAQKKKKSEDGSKNSRQPAEAGVVESEN', 138, 'Q8N2Z9; Q8NFE5; Q8NFG5;', 'KD00446', 'Homo sapiens (Human)', 'APITD1', '#Centromere protein S#CENP-S#Apoptosis-inducing TAF9-like domain-containing protein 1#FANCM-interacting histone fold protein 1#Fanconi anemia-associated polypeptide of 16 kDa', '-', 'ENSG00000251503', '-'),
(447, 'Q9D2Z8', 'Kinesin-like protein KIF12', 'GO:0003777', 70706, '', 'MEERGSPDGDPARNLEQGPEGSETPIQVVLRVRPMSTVELRRGEQSALHCSGTRTLQVSPDVAFRFGAVLDGARTQEDVFRACGVKRLGELALRGFSCTVFTFGQTGSGKTYTLTGPPPQGEGVPVPPSLAGIMQRTFTWLLDRVQHLDSPVTLRASYLEIYNEQVWDLLSLGSPRPLPVRWTKARGFYVEQLRVVEFGSLEALMELLQMGLSRRRSSSHTLNQASSRSHALLTLHISRPTSQQVPPVDLGEPPVGGKLCFVDLAGSEKVAATGSQGQLMLEANSINRSLLALGHCISLLLDPQRKQNHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRITTRPQGPKSPGVKPPQQVENELLRLQEENRHLRFQLDQMHTTAPGAHGARMAWAQRNLYGMLQEFMLENERLRKEMRQLRSSRDLARAEQRVLAQQVHDLERRLLSACPLPQQGSTPVCPCRMVPAASCHALPPLCYCHHFCPLCRVPLAHWTCPRRECHMPQVLEPEAPGHISQSVWPPPWAPPPSPGSAKPPRERSQSDWTQTRVLAEMLMGEEVVPSAPPLSAGPSNMPYGLRGGSGIPNLTPRLETLTQQINSSLHLSQRQPQPSEDTQSPGQGLSSC', 642, 'Q9D2Z8; O35061;', 'KD00447', 'Mus musculus (Mouse)', 'Kif12', '#Kinesin-like protein KIF12', '-', '-', '16552'),
(448, 'Q28DR7', 'Dynactin subunit 6', 'GO:0000777', 21918, '', 'MRQDVSLLSTSGSQKNPLGNVKIAPGAVVCVESEIKGDVTIGPRTVVHPKARIYAEAGPIIIGEGNLIEEQAFIRNSFPENIAPDSDVEPKTMIIGTNNVFEVGCYSQAMKMGDNNVIESKAFVGRNVILTSGCIIGACCQVDTCEVIPENTVIYGSDCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKTTKNISTPMKS', 201, 'Q28DR7;', 'KD00448', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'dctn6', '#Dynactin subunit 6', '-', '-', '733845'),
(449, 'Q5R9Y9', 'Kinesin-like protein KIF2A', 'GO:0003777', 84099, 'Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity (By similarity). {ECO:0000250}.', 'MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEEIEPSPETPPPPASSAKVNKIVKNRRTVASIKNDPPPRDNRVVGSARARPSQFPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKEFGISPSDIPFSQGSGSRPDLSPSYEYDDFSPSVTRVKELTVDPTAAGDVRPIMHHPPNQIDDLETQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWLEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL', 744, 'Q5R9Y9;', 'KD00449', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'KIF2A', '#Kinesin-like protein KIF2A', '-', '-', '100174485'),
(450, 'O15066', 'Kinesin-like protein KIF3B', 'GO:0003777', 85125, 'Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro (By similarity). {ECO:0000250}.', 'MSKLKSSESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKDALLREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEEGDDKDDYWREQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKSKIMNRAFFDEEEDHWKLHPITRLENQQMMKRPVSAVGYKRPLSQHARMSMMIRPEARYRAENIVLLELDMPSRTTRDYEGPAIAPKVQAALDAALQDEDEIQVDASSFESTANKKSKARPKSGRKSGSSSSSSGTPASQLYPQSRGLVPK', 747, 'O15066; B2RMP4; B4DSR5; E1P5M5;', 'KD00450', 'Homo sapiens (Human)', 'KIF3B', '#Kinesin-like protein KIF3B#HH0048#Microtubule plus end-directed kinesin motor 3B#Kinesin-like protein KIF3B; N-terminally processed', '-', 'ENSG00000101350', '-'),
(451, 'P28033', 'CCAAT/enhancer-binding protein beta', 'GO:0000779', 31446, 'Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Binds to regulatory regions of several acute-phase and cytokines genes and probably plays a role in the regulation of acute-phase reaction; inflammation and hemopoiesis. The consensus recognition site is 5''-T[TG]NNGNAA[TG]-3''. Plays an important role in adipose tissue differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG) as well as other adipogenesis key player genes. {ECO:0000269|PubMed:19324970; ECO:0000269|PubMed:19641492}.', 'MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAADFAAPAPAHHDFLSDLFADDYGAKPSKKPADYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKTVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC', 296, 'P28033;', 'KD00451', 'Mus musculus (Mouse)', 'Cebpb', '#CCAAT/enhancer-binding protein beta#C/EBP beta#AGP/EBP#Interleukin-6-dependent-binding protein#IL-6DBP#Liver-enriched transcriptional activator#LAP', '-', '-', '12608'),
(452, 'A7MD70', 'Protein Spindly', 'GO:0043515===GO:0034501===GO:0000940', 68964, 'Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. {ECO:0000255|HAMAP-Rule:MF_03041}.', 'MSDLEDEIKVLRRKVQDGEEALQRAGQYGLQLLDEKMELHNRLEEQRTEMSNVIEALEQDKYTLQREVELKIRMLESLRSEFDLVRTQQKHQMEQQQTLLERNHAVEISDLKNKVVKMKTDLEEAQLAEKQMRHKLDQQAEALNSKTEELRALTERAHETMSSEILELQVQKMELESAMATLEQELQEAQYKDEQLHLANTTLQRQLERLTEEKEEREKEAVSCYNALEKAREANQDLQIQLEQVLQQAQDPNSKGNSLFSEVEDKRAAMERQLNSMKRNYDSLQKQHVLTKQHMHHMKMQIATLMQLQGNRADPAQLERLQFMLSDKNKEIESLMMKVRELEKEKMAVKDHHPHPPSNEGELKDETYYTDLLKMQLANSKKDAEKLKEELSMARMKALSESQRVLELERKLYGTEQALKLRHSDNMKLQVKLEELKIKYTPNEVNKAQVQKRRREKFPVPEENSASVKDETTTQDTELSKNSNEKAEEKTPSHPVEKPVVIPLQSEHPTEPNPVLSRESKSVRICEDPPVCIPDAPRSPVNDSNSKNVDQTHQSSEEEENWRTEKKRKKYQQPTHVSSQKTMANECAQQ', 590, 'A7MD70; A4IGD1;', 'KD00452', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'spdl1', '#Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041}#Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041}#Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041}', '-', '-', '568360'),
(453, 'P87066', 'Tubulin alpha chain', 'GO:0005828', 49968, 'Tubulin is the major constituent of microtubules. It binds two moles of GTP; one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.', 'MREVISINVGQAGCQIGNACWELYSQEHGIRPDGYLQEGLDRPKGGEEGFSTFFSETGSGKYVPRALYVDLEPNVIDEVRTGVYKDLFHPEQLIAGKEDAANNYARGHYTVGREILDDILDRVRRMSDQCDGLQGFLFTHSLGGGTGSGLGSLLLEQLSLDYGKKSKLEFAVYPAPQVSTSVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDMCRRNLDIARPNFSSLNNLIAQVVSSVTASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYAPVFSKSRATHEANSVSEITQSCFEPGNQMVKCDPRTGKYMATCLLYRGDVVTRDVQNAVAQVKSKKTVQLVDWCPTGFKIGICYQPPTAIKGSELASASRAVCMLSNTTAIAEAWRRIDRKFDLMYSKRAFVHWYVGEGMEEGEFTEAREDLAALERDYIEVGTDSFPEEEEEY', 448, 'P87066;', 'KD00453', 'Candida albicans (Yeast)', 'TUB1', '#Tubulin alpha chain', '-', '-', '-'),
(454, 'O75177', 'Calcium-responsive transactivator', 'GO:0000776===GO:0000777===GO:0000780', 42990, 'Transcriptional activator which is required for calcium- dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex; a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons; transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx; RB1 is dephosphorylated by calcineurin; which leads to release of the repressor complex. At the same time; there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism; which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter; and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP (By similarity). {ECO:0000250}.', 'MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILEYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALTQSGSSQGLHSQGSLSDAISTGLPPSSLLQGQIGNGPSHVSMQQTAPNTLPTTSMSISGPGYSHAGPASQGVPMQGQGTIGNYVSRTNINMQSNPVSMMQQQAATSHYSSAQGGSQHYQGQSSIAMMGQGSQGSSMMGQRPMAPYRPSQQGSSQQYLGQEEYYGEQYSHSQGAAEPMGQQYYPDGHGDYAYQQSSYTEQSYDRSFEESTQHYYEGGNSQYSQQQAGYQQGAAQQQTYSQQQYPSQQSYPGQQQGYGSAQGAPSQYPGYQQGQGQQYGSYRAPQTAPSAQQQRPYGYEQGQYGNYQQ', 396, 'O75177; A6NNE3; A8K620; B3KWR8; E1P5H7; Q5JXJ3; Q6MZV9; Q6NTH3;Q6XYD9; Q8NE69; Q9BR55; Q9H4K6;', 'KD00454', 'Homo sapiens (Human)', 'SS18L1', '#Calcium-responsive transactivator#SS18-like protein 1#SYT homolog 1', '-', 'ENSG00000184402', '-'),
(455, 'Q3ZBK3', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 26608, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (By similarity). {ECO:0000250}.', 'MVEDELALFDKSINEFWNKFKSTVSDTSCQMVGLRETYKDSIKAFAEKLSVKLKEEERMVEMFLEYQNQICRQNKLIQEKKENLLKLIAEVKDKKQEVEALTANIQDLKEEYARKKETISTANKANEERLKRLQKSADLYKDRLGLEIRKIYGDKLQFIFTDIDPKHPDRPFMFSLCLNEARDYEVSDCAPRLECLAEFQEKVRQTNNFSAFLANVRKAFTALVYN', 226, 'Q3ZBK3;', 'KD00455', 'Bos taurus (Bovine)', 'SPC25', '#Kinetochore protein Spc25', '-', '-', '505011'),
(456, 'Q3ZBK8', 'Centromere protein O', 'GO:0000777===GO:0034508', 33893, 'Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Modulates the kinetochore-bound levels of NDC80 complex (By similarity). {ECO:0000250}.', 'MELANTLRQDGESRGGVLAHLERLETQVSKSRKKLEEPQNAQALEARIHELKRLRDKLRAEVKQRQARVKASTANVEPDQILEISEQEILERKQENMKAILQAYRFTGISGKLTSRGVCVCISTAFEGNLLDSYFVDLVMEKPLWIHHHSVPVFIPLEEISAKYLQTNTRHFLFVLWEYLNAYSGRKYQADRLQSDFAAFLVGPLQRNSLCNLLSFTYKVKPEGQSFPFCARLLYKDLTTTLPTDVTVTSQGTEALPSTWEEQRAAHENLFFTKPLHQVFTSFAKKGEKLDMSLVS', 296, 'Q3ZBK8;', 'KD00456', 'Bos taurus (Bovine)', 'CENPO', '#Centromere protein O#CENP-O', '-', '-', '767930'),
(457, 'Q66LG9', 'CENP-CCentromere protein C', 'k', 78935, '', 'MADVSRSSSLYTEEDPLQAYSGLSLFPRTLKSLSNPLPPSYQSEDLQQTHTLLQSMPFEIQSEHQEQAKAILEDVDVDVQLNPIPNKRERRPGLDRKRKSFSLHLTTSQPPPVAPSFDPSKYPRSEDFFAAYDKFELANREWQKQTGSSVIDIQENPPSRRPRRPGIPGRKRRPFKESFTDSYFTDVINLEASEKEIPIASEQSLESATAAHVTTVDREVDDSTVDTDKDLNNVLKDLLACSREELEGDGAIKLLEERLQIKSFNIEKFSIPEFQDVRKMNLKASGSNPPNRKSLSDIQNILKGTNRVAVRKNSHSPSPQTIKHFSSPNPPVDQFSFPDIHNLLPGDQQPSEVNVQPIAKDIPNTSPTNVGTVDVASPFNDSVVKRSGEDDSHIHSGIHRSHLSRDGNPDICVMDSISNRSSAMLQKNVDMRTKGKEVDVPMSESGANRNTGDRENDAEINEETDNLERLAECASKEVTRPFTVEEDSIPYQQGASSKSPNRAPEQYNTMGGSLEHAEHNQGLHEEENVNTGSASGLQVENAPEVHKYSHKQTNKRRKRGSSDSNVKKRSKTVHGETGGDKQMKTLPHESRAKKQTKGKSNEREEKKPKKTLTHEGKLFSCRKSLAAAGTKIEGGVRRSTRIKSRPLEYWRGERFLYGRIHESLTTVIGIKYASPGEGKRDSRASKVKSFVSDEYKKLVDFAALH', 705, 'Q66LG9;', 'KD00457', 'Arabidopsis thaliana (Mouse-ear cress)', 'CENP-C', '#CENP-C {ECO:0000313|EMBL:AAU04629.1}#Centromere protein C {ECO:0000313|EMBL:AEE29346.1}', '-', '-', '838135'),
(458, 'Q6NYW6', 'CLIP-associating protein 2', 'GO:0000777', 140303, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. May be involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (By similarity). {ECO:0000250}.', 'MALSLSQDRSFDDDDSVDGSRPSSAQAAFKVPKVPKKPAESASSSRRPSATGAAKSGASKEGAGAVDEEDFIKAFTDVPTVQIYSTRDLEDNLNKIREVLSDDKHDWDHRANALKKIRSLLVAGATDYDCFYQHLRLLDGAFKLSAKDLRSQVVREACITVAYLSTLLGNKFDHGAEGIVPVLFNLIPNCAKVMATSGTAAIRIIIRHTHVPRLIPLIASNCTSKSVAVRRRCYEFLDLLLQEWQTHSLERHAAVLVESIKKGIRDADAEARVEARKAYWGLRAHFPGEAESLYNSLESSYQRTLQSCLKSSGSVASLPQSDRSSSSSQESLNRPLSKWSAAPGRVPAGSKSSGSPASLQRSRSDVDVNAAAGAKARHSGQAGGAGRVTTGLTPGSYASLGRLRTKQTLSTASSVGSSQVDSRGRTRSKMASQSQRSDDSDCTPGSQSATPVGAGSRSGSPGRVLASTALSTLSTGAQRVSAAPGSHRRSRIPRSQGCSRDSSPTRLSVAPSNISHIYNGSKGARGSRIPRPSVSQGCSREASRESSRDTSPVRSFTPLGSGLGMSQSSRLSSSVSAMRVLNTGSDVEEALADALKKPARRRYDTYGMYSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASANWSERKEGLMGLQALLKNHRTLSRVELKRLCEIFTRMFADPHSKRDPRGFGTVESGISSASFKRVFSMFLETLVDFIAVHKEDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRESFPNDLQFTILMRFTVDQTQTPNLKVKVAILKYIETLTLQMEPQDFVNTGETRLAVSRIITWTTEPKSSDVRKAAQSVLISLFQLNTPEFTMLLGALPKTFQDGATKLLQNHLRNTGNTAQASIGSPLTRHTPRSPASWSSPLTSPTNTSQNTPSPSAFDYDTENMNSEEIYSSLRGVSQAIQNFSVRSQEDMTEPPRKREGDGGEETVDSGRTALDNKTSLLNTMPLLSSSPRPSRDYQPVNYSDSSFGSSSFNKSLKDADQEESLTDDSGVDQSEVVAELLKELSNHSERVEERKAALCELMRLIRETQLHVWDEHFKTILLLLLETLGDGEHVIRALALRVLKEILNRQPWRFKNYAELTIMKALEAHKDPHKEVVRAAEEAASMLATSISPDQCIKVLCPIIQSADYPINLAAIKMLTKVIDRLPKEGLIQMLPEIVPGLIQGYDNSESSVRKACVFCLVAIYAVIGEDLKPHLSQLSGSKLKLLNLYIKRAQSGSSGSDQSSDVGGQGL', 1288, 'Q6NYW6;', 'KD00458', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'clasp2', '#CLIP-associating protein 2#Cytoplasmic linker-associated protein 2', '-', '-', '404604'),
(459, 'O61308', '227 kDa spindle- and centromere-associated protein', 'GO:0000777', 227218, 'May play a role in the organization of the spindle apparatus and its interaction with the centromeres.', 'MEGTCSEEENLAKRVTPTAVTSGTYGTHVVDTTDLALSDVVIGCGSTIYETSDSIGSDVMLGLSSHGVSSVSGLDRDLNSFKKRIDANTEEQREHADMMVGLQRKIEEYRRRIVDAEKQVSIQKANDDVSFSIKETADTWLPDMKSDAADYEWASRLDEERRRNDELHMQITQQQVDLQRLQKYFEANMQEKEKIYQTREKNLAYYLNAEQRKMLDLWEELQRVRRQFADYKEQTERDLENQKNEVAKVTQSVGGMAGRLNTSSHGDSGLVQDVVLLEAMRRFRELQAVPVGASADDYNALMKKYEETVERVIELESHGDGSTAKMLSLEAELRRTKDKFIECSEFLRKLGDLAAGSYRGDERTSKIVSLSPGGMSLPSEIYRSVRNILRNHDSEMQHIQRKLKNSDTQVCELTTRLEGTEEARRRSDKQLVDAKREINIQQRAVDDANRELRRVEDRLHIMESEKIVAENARQQLEEEVRRLTLQVDQSKADGERRVVEEGEIQKRIVEDEYRSMISELTRRMNAFQDENKRLKNDLGCTKERLKNVEFEYNSTVRKLEDKDIALKHLEDTKLDLLKDLENQRTRYDAVTNELDTLQTTFETSTKNIAQLEANIKEINLMRDEISKEKDSLAQKLADVTHKLEIETVRREDIQRSCVGHSEDVEKQRLQIIEYEREVMALRRLNDELDTNVKTGQAKVTSLENSIISVQTEVTKLTTLNDKLQKEKQSIMSSKQKADTDVDLLKEKLRKLEQECDKLKEENKALHEDEQIARQMCKEEASRIHLLERDLKDAMTEVEELKKQLQKMDEENSERLESVLRTKISSDTVDTSEIAEYTEVKVKELREKYKADLERLQSNKDDLERRVQILEDELAERQRIVERQRTEMNDLKLEYQLESDRLRAEMATVELKYQSEVEDERDQRSRDADSWKVTSEELRSKISFMEKMLEEAKHRETVLREEATEWEEKHDIISNESLKLRNEIERIRSDAEEDIQKWKKDVHMAQNELKNLERVCETLRSQLTAANDRVASLNTTINEQTSKIRELNSHEHRLEEDLADSRATSSAIENDLGNATGRLRSSEEHNAILQSENRKSKTEIEALKHQIDTIMNTKESCESEVERLKKKIVQTTTITKEQNEKIEKLRIEHDHLERDYREKTKEVDRLKEVEKTFELKVNRARQELDEFSKKLIVTETERNAISGEAQKLDKEVQLVKEQLQYKSDEFHKALDELANAHRISEEGRVNAIHQLEARRFEIDDLKSRLENSEQRLATLQQEYVNADKERGALNDAMRRFQATISRSVVAEEHVDVSTIETQMQKLMSRIEAIERERNEYRDSLNRLKNRCSTSYSSVDRQETVYRTFEERVISAEDERRKVELKLSSMKEMLKSQEEKLKQRDEERRNLKSNIVTFELEARAKDAQIRHLNDLLKRVQAELENSQNDNRALRERQEQYETNRIHLEQRLPTDEGEPRVKALMAAFATERQSLSDSLKKLASQLQISETKNADLRDDAERLKRDLLKAERVEEDLRRNLVEQTEIMRENQQLRSQLGVAQSDLANASGRKQQLEGELAAVRAELRDHKQHLHDAISRIAELQRQLQDANAEKSRLTDRIIGLEKTIGTLRNTETELRAQLSTAADERKALNSELEEMRRRIVQMESEKKDVDNQLEEVNKARIIMTKKIEILETEKHSAELVISETASQREAIERSLNALERENKELYKNCAQLQQQIAQLEMDNGERLIALTTKQKEDHEKFVAAVKAEKVQVERIVENRDRAQKSRIRQLENQLSMMREQLDNERARSHQMSERFIVNETNRRVSSSSFRLSGDAAGVAAATILHPQTDRLDYVFANRSALSSYYTVPTEQHASRGKEAYRTSSTIKSSEGTTRESYTYQSRTVSSNIIEQANGMTSSASGEGMSRAYPPTEVNQGDVTGRKSRPATRKQQMKSTFSE', 1955, 'O61308;', 'KD00459', 'Parascaris univalens', 'PUMA1', '#227 kDa spindle- and centromere-associated protein#PUMA1', '-', '-', '-'),
(460, 'Q13547', 'Histone deacetylase 1', 'c;k', 55103, 'Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A; H2B; H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation; cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Deacetylates SP proteins; SP1 and SP3; and regulates their function. Component of the BRG1-RB1-HDAC1 complex; which negatively regulates the CREST- mediated transcription in resting neurons. Upon calcium stimulation; HDAC1 is released from the complex and CREBBP is recruited; which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates ''Lys-310'' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses; via histone deacetylase (HDAC) recruitment; a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes; such as PER1; mediated by the large PER complex or CRY1 through histone deacetylation. {ECO:0000269|PubMed:12837748; ECO:0000269|PubMed:16478997; ECO:0000269|PubMed:17000776; ECO:0000269|PubMed:17704056; ECO:0000269|PubMed:17996965; ECO:0000269|PubMed:19081374; ECO:0000269|PubMed:19343227}.', 'MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA', 482, 'Q13547; Q92534;', 'KD00460', 'Homo sapiens (Human)', 'HDAC1', '#Histone deacetylase 1#HD1#3.5.1.98', '-', 'ENSG00000116478', '-'),
(461, 'Q5R1W1', 'Septin-7', 'GO:0000777', 50290, 'Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements (By similarity). {ECO:0000250}.', 'SARSAAAEERSVNSSTMVAQQKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKGLEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKIF', 434, 'Q5R1W1;', 'KD00461', 'Pan troglodytes (Chimpanzee)', 'SEPT7', '#Septin-7#CDC10 protein homolog', '-', '-', '463349'),
(462, 'B0BM28', 'Spindle and kinetochore-associated protein 1', 'GO:0000940', 28952, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis; when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it mediates the interaction with microtubules (By similarity). {ECO:0000250}.', 'MDPGDLDELCSHVNSKISLIKKTLQLRNIGQDPSLNSVLSKIAFEMHSLYNLLNNLETEVQRQETIANSLRELQATVERDFTEASHLKENIPPHLPKRTQSSSSAPDEAPEMVVKVAAPEPAKKPSKEKPIKEMELITVHEFGTVPAYMKNRLTYEQINNIIEELNKAVVGKYKILHQPLKSLSNQARKQLSRYKEEETKDTKGQFFIVDQDIKDFTQVKVDKRFHGMLSILRHCHRLREIRGKGLVRYIIC', 252, 'B0BM28;', 'KD00462', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'ska1', '#Spindle and kinetochore-associated protein 1', '-', '-', '100144953'),
(463, 'Q9S7T7', 'Sister chromatid cohesion 1 protein 1', 'GO:0051455===k', 71228, 'Involved in chromosome condensation; pairing and segregation during meiosis. Responsible for cohesion between replicated sister chromatids.', 'MLRLESLIVTVWGPATLLARKAPLGQIWMAATLHAKINRKKLDKLDIIQICEEILNPSVPMALRLSGILMGGVVIVYERKVKLLFDDVNRFLVEINGAWRTKSVPDPTLLPKGKTHARKEAVTLPENEEADFGDFEQTRNVPKFGNYMDFQQTFISMRLDESHVNNNPEPEDLGQQFHQADAENITLFEYHGSFQTNNETYDRFERFDIEGDDETQMNSNPREGAEIPTTLIPSPPRHHDIPEGVNPTSPQRQEQQENRRDGFAEQMEEQNIPDKEEHDRPQPAKKRARKTATSAMDYEQTIIAGHVYQSWLQDTSDILCRGEKRKVRGTIRPDMESFKRANMPPTQLFEKDSSYPPQLYQLWSKNTQVLQTSSSESRHPDLRAEQSPGFVQERMHNHHQTDHHERSDTSSQNLDSPAEILRTVRTGKGASVESMMAGSRASPETINRQAADINVTPFYSGDDVRSMPSTPSARGAASINNIEISSKSRMPNRKRPNSSPRRGLEPVAEERPWEHREYEFEFSMLPEKRFTADKEILFETASTQTQKPVCNQSDEMITDSIKSHLKTHFETPGAPQVESLNKLAVGMDRNAAAKLFFQSCVLATRGVIKVNQAEPYGDILIARGPNM', 627, 'Q9S7T7; Q3E9L1; Q9SQI1;', 'KD00463', 'Arabidopsis thaliana (Mouse-ear cress)', 'SYN1', '#Sister chromatid cohesion 1 protein 1#Protein DETERMINATE INFERTILE 1#SCC1 homolog 1', '-', '-', '830432');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(464, 'O36024', 'Kinetochore protein fta1', 'GO:0000776===GO:0000778===GO:0051315===SCL', 32337, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. {ECO:0000269|PubMed:16079914}.', 'MTLRDHHFYNVTYTAYRLSPLFGFEYSNLTEIGKKLTRFLRYGTDRTGYFTNSTRFADLIIEKATFTEFGNTSSFPKFLKLDISYETSSDLEVKRKGQMFFFESFRKFSHAEADRTRLSLEGNSVFFSLALVRMDGALWMAVEQFLQQEFDTQILPCLIAPEILLEFLKIWQNHVNSQTALPLELTWTTGNPNLSSVTISIRPEDLKKIFRSSSFFYPILMEHIKRCTSLDLTNSVFSLSKVNTDCAILTSSGKLKIFSKAQNIVFDVLLALEPMQLPEY', 280, 'O36024;', 'KD00464', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'fta1', '#Kinetochore protein fta1#Sim4 complex subunit fta1#Sim4-mal2-associated protein 1', '-', '-', '2543650'),
(465, 'Q9Z336', 'Dynein light chain Tctex-type 1', 'GO:0005868', 12452, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site. May also be a accessory component of axonemal dynein (By similarity). {ECO:0000250}.', 'MEDFQASEETAFVVDEVSNIVKEAIESAIGGNAYQHSKVNQWTTNVVEQTLSQLTKLGKPFKYIVTCVIMQKNGAGLHTASSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSI', 113, 'Q9Z336;', 'KD00465', 'Rattus norvegicus (Rat)', 'Dynlt1', '#Dynein light chain Tctex-type 1#Activator of G-protein signaling 2#AGS2#T-complex testis-specific protein 1 homolog', '-', '-', '83462'),
(466, 'P0CP16', 'Probable kinetochore protein NDC80', 'GO:0034501===GO:0000778===GO:0051315===GO:0051455===GO:0031617===GO:0031262', 78423, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MDFRRQTLVSNGGSSQPQPSVPSSAIKKASRLGPARQSLAPSQIQSRTSILGVSNSQENASHGMMGSRKSTVPGKMGDRDQLMSASRGDGGIYGRTPQMNRGIPGSVRRSSVFTSNSQGRTSMAPGVYSTAYKDPRPLRDKVFQSNCMRNVNEYLISVRYPLPLTAKTLTSPTAKEFQSIFKFLVNDLVDPGAAWGKKFEDDTLSILKDLKYPGMDSVSKTALTAPGAPQSWPNMLAMLNWLVDLCKALDNWDDPEIISDPLMVPATELPLDYPNLDDRLLWDFAAKTYSQWFDGEAEEFDEAEQELEHAYGKSYSIVLNDTEQATDRMASATVAECEKLEREIQKRNVEIQQLHVQEVCSPITDRISFADKSYKPPLKKLEDEYVQLMSDKNKFISFLDQQGQKIEKIRLRISKVKEAVISQEAELEARQSELAHIEQAVAAQNLSPDEVQRMNHERDSLTRSLEDLRNKISEASQFAYDQEMVVTKSMDRFEGLLTDYNSLAHQIGLLDSSLDVPSLAANVNYNLDVDLGAEELEEVKAVGVRMRSTIWQALQTCRETFRQEALGLGNGTIALEDEFDKLGQSVERQKEEVGNLEVRLKIVHNQAEDAQSQIASENSDTNKIITQLETEVTNMLAASQQGVLSTQSQLESTRIAFKELRHKTALFQDSVVAEVGEHIDAIIKAKEHTANSLKSIRALAETQ', 703, 'P0CP16; Q55SB3; Q5KGR0;', 'KD00466', 'Cryptococcus neoformans var. neoformans serotype D (strain JEC21ATCC MYA-565) (Filobasidiella neoformans)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '3257912'),
(467, 'P0CP17', 'Probable kinetochore protein NDC80', 'GO:0000777', 78513, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MDFRRQTLVSNGGSSQPQPSVPSSAIKKASRLGPARQSLAPSQIQSRTSILGVSNSQENASHGMMGSRKSTVPGKMGDRDQLMSASRGDGGIYGRTPQMNRGIPGSVRRSSVFTSNSQGRTSMAPGVYSTAYKDPRPLRDKVFQSNCMRNVNEYLISVRYPLPLTAKTLTSPTAKEFQSIFKFLVNDLVDPGAAWGKKFEDDTLSILKDLKYPGMDSVSKTALTAPGAPQSWPNMLAMLNWLVDLCKALDNWDDPEIISDPLMVPATELPLDYPNLDDRLLWDFAAKTYSQWFDGEAEEFDEAEQELEHAYGKSYSIVLNDTEQATDRMASATVAECEKLEREIQKRNVEIQQLHVQEVCSPITDRISFADKSYKPPLKKLEDEYVQLMSDKNKFISFLDQQGQKIEKIRLRISKVKEAVISQEAELEARQSELAHIEQAVAAQNLSPDEVQRMNHERDSLTRSLEDLRNKISEASQFAYDQEMVVTKSMDRFEGLLTDYNSLAHQIGLLDFSLDVPSLAANVNYNLDVDLGAEELEEVKAVGVRMRSTIWQALQTCREMFRQEALGLGNGTIALEDEFDKLGQSVERQKEEVGNLEVRLKIVHNQAEDAQSQIASENSDTNKIITQLETEVTNMLAASQQGVLSTQSQLESTRIAFKELRHKTALFQDSVVAEVGEHIDAIIKAKEHTANSLKSIRALAETQ', 703, 'P0CP17; Q55SB3; Q5KGR0;', 'KD00467', 'Cryptococcus neoformans var. neoformans serotype D (strain B-3501A(Filobasidiella neoformans)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '4936279'),
(468, 'O23826', '125 kDa kinesin-related protein', 'GO:0003777', 113711, 'Responsible for microtubule translocation. May be important for the organization of phragmoplast-specific arrays of microtubules. {ECO:0000269|PubMed:7983184}.', 'MSNKEKGVNVQVLLRCRPFSNDELRNNAPQVVTCNDYQREVAVSQNIAGKHIDRIFTFDKVFGPSAQQRDLYDQAIVPIVNEVLEGFNCTIFAYGQTGTGKTYTMEGECKRSKSGPNGELPQEAGVIPRAVKQVFDTLESQNAEYSVKVTFLELYNEEITDLLAPEDLKVALEDRQKKQLPLMEDGKGGVLVRGLEEEIVTSANEIFTLLERGSAKRRTAETLLNKQSSRSHSLFSITIHIKEATPEGEELIKCGKLNLVDLAGSENISRSGAREGRAREAGEINKSLLTLGRVINALVEHLGHIPYRDSKLTRLLRDSLGGRTKTCIIATVSPAVHCLEETLSTLDYAHRAKNIKNKPEVNQKMMKSTLIKDLYGEIERLKAEVYAAREKNGVYIPKERYYQEENERKAMADQIEQMGVSIENHQKQFEELQSRHDSQVQQCSDLTCKLDVTQKQLNQTSKLLAYTEEQLRQSQYTLKERDFIISEQKKAENALAHQACVLRADLEKSIQENASLFQKIAREDKLSTDNRSLVNNFQAELAKQLGSLSSTLATSVCRQTEHLQCVEKFCHNFLDSHDKAVLDLKRKINSSMALYISHFEAMQNVVRLHKATSNATLEEVSTLASSNSISTKEFLDAEAVEANSMFDELQSTLSTHQGEMAHFARELRQRFNDSTEHLTNISAIIQRFFDKLLDESKRLEKHATTVDEIQTNSIAEFEKAYEEQSKSDAEKLIADVTSLVSNHMRRQKELVGARLVDLRETVSGNRTFLDGHVSSMEGITTDAKRKWQDFYMQAEGETKENADFSAAKHCRMESLMQKCVSTAETALKRWQSTHELVNDMGNQHVLTMHSVVRNICDNNEQHVTDFDSTRESAEEDVKRNSEDIIKSIDSLSGEERGSISGVLDTTSAHSETLDVLKKDHCMQSTSIEQIALETFQQKYMDYEPTGATPIRSEPDVPSKVTIESLRAMPMEVLLEEFRENNSFESFQVKEVKPSLIPRSPFSQINN', 1006, 'O23826;', 'KD00468', 'Nicotiana tabacum (Common tobacco)', 'TKRP125', '#125 kDa kinesin-related protein', '-', '-', '-'),
(469, 'Q8L7Y8', 'Kinesin-like protein KIN12B', 'GO:0003777', 146612, 'Plus-end directed kinesin-like motor enzyme that plays a critical role in the organization of phragmoplast microtubules during cytokinesis. Constitutes a signaling module in association with serine/threonine-protein kinase TIO that is required to support phragmoplast expansion and cell-plate growth in plant cells. {ECO:0000269|PubMed:17720869}.', 'MKHFMMPRNAILRDIGESQSPNPSLTKSKSQRKIKSSKENAPPPDLNSLIPDHRSSPAKLKSPLPPRPPSSNPLKRKLIAEATADNGVAIGVSDSGVKVIVRMKPPSKGEEEEMIVKKISNDALTINEQTFTFDSIADPESTQDEIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPANGLLEEHLSGDQRGLTPRVFELLFARLSEEQAKHAERQLKYQCRCSFLEIYNEQITDLLDPSLKNLMIREDVKSGVYVENLTEEYVKNLKDLSKLLVKGLANRRTGATSVNAESSRSHCVFTCVVESHCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAVSPSQSCRSETFSTLRFAQRAKAIQNKAIVNEVMQDDVNFLREVIRQLRDELQRVKDDKGNNPTNPNAAYTTSWNARRSLSLLRSFGLGHPKSLPNGDDDGDTEMEIDEEAVERLCAQMGLSPPAEDNNQEMSRVEKINSSLQTVVLKDESYNNSHLKSSEATDVNMEDACCQTENNGSETDNALTVAETMDDGSSVQPDSITNSLHSCISDTNQGNSPSKAENIPSCQDLVIEADVSAIVSVADTSNNTEQVSVNPVSPCLSVAPVSVSPVLIPPTESASPKIRNSRKSLRTTSMSTASQKDIERANQLTPEVVEPSPAMSTEVLNLYSALSTKKSEAFPVPTRQLAASLHRGMKLLDSYRQSTALRRSTFRLSYKALECKPSTVLSKADVGVQTYPQADEIAEDNSKEVLCSRCKCRAECDAQEISDTSNLQLVPIDNSEGSEKSNFQVPKAVEKVLAGSIRREMAMEEFCTKQASEISQLNRLVQQYKHERECNAIIGQTREDKIVRLESLMDGVLSKDDFLDEEFASLMHEHKLLKDMYENHPEVLQTRIELKRVQEELESFKNFYGDMGEREVLLEEIHDLKAQLQCYTDSSLTSARRRGSLLKLTYACDPNQAPQLNTIPESVDEGPEKTLEQERLRWTEAESNWISLAEELRTELDTNRLLMEKQKRELDTEKRCAEELTEAMQMAMQGHARMIEQYADLEEKHIQLLARHRRIREGIDDVKKAAARAGVKGAESRFINALAAEISALKVQREKEVRYFRDENKSLQSQLRDTAEAVQAAGELLVRFKEAEEGLTFAQKRAMDAEYEASEAYKKVDKLKRKYETEISTVNQQHNAEPQNPIESLQASCNDDAMAKYDEPSASDGDNQWREEFQPFYKKDEELSKLAEPSWFSGYDRCNI', 1313, 'Q8L7Y8; Q9LUG0;', 'KD00469', 'Arabidopsis thaliana (Mouse-ear cress)', 'KIN12B', '#Kinesin-like protein KIN12B#Phragmoplast-associated kinesin-related protein 1-like protein#AtPAKRP1L', '-', '-', '821947'),
(470, 'P0CP02', 'Histone acetyltransferase ESA1', 'GO:0034508', 63050, 'Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4; H3; H2B; H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac; H4K8ac; H4K12ac and H4K16ac; histone H3 to form H3K14ac; and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me. {ECO:0000250|UniProtKB:Q08649}.', 'MSPSAPSTPHGRGSGSEPGTPAPSVAAGGSYTIDDVVPGVKIYVIKPLSNGQAEQRRAEILSTRPKPKPSAFAPPPPPNAPSPDPRDDTEYYVHYVEFNKRLDEWVGGSRLVLSKEMEWPKSKDEPKKKDRPAKAQPSKAPSRATGSPIPSDSLLKKAANKAAMAAGKATPGKAMPSSKLGKASKIGKAGKFPQKRKAKTEADTEAEEESNEDNDALGEEEDMDEDGDVTLITSDGAIDPSREVVAAPSNPRAAPQVFSKKQEIEKLRTSGSMTQSHSEISRVKNLNKLQIGKHEVETWYFSPYPIEYAHLPVLYICEFCLLYYPSATQLRRHRAKCTLLHPPGNEIYRHEGISFFEIDGRKQRTWCRNLCLISKCFLDHKTLYYDVDPFLYYCMTVKDDYGCHLIGYFSKEKESAEGYNVACILTLPQHQRKGYGRLLIEFSYELSKVEGKLGSPEKPLSDLGLLGYRAYWQEKIVELLLDSDYEISLDEIAQKTSITHGDIMHTCQALQMIKYYKNSHIIHLTDAVIEQHKKTKAKPRRAINPAYLKWKPPVFSRAQLAFGF', 564, 'P0CP02; Q55XW1; Q5KM33;', 'KD00470', 'Cryptococcus neoformans var. neoformans serotype D (strain JEC21ATCC MYA-565) (Filobasidiella neoformans)', 'ESA1', '#Histone acetyltransferase ESA1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}', '-', '-', '3255895'),
(471, 'Q6GLZ5', 'Septin-7', 'GO:0000777', 49469, 'Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis (By similarity). Plays a role in ciliogenesis and collective cell movements including convergent extension during gastrulation. Controls cell elongation but not polarization during convergent extension. {ECO:0000250; ECO:0000269|PubMed:20671153}.', 'MVAQQKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYAPDYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDGLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKYDTGEGMSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEEEKVNWETQQRILEQQNTSRTLEKNKKKGKIF', 425, 'Q6GLZ5;', 'KD00471', 'Xenopus laevis (African clawed frog)', 'sept7', '#Septin-7', '-', '-', '444612'),
(472, 'Q19705', 'ADP-ribosylation factor-like protein 2', 'GO:0005818', 20999, 'GTP-binding protein that functions in embryogenesis; cytokinesis; germline development and microtubulule cytoskeleton dynamics. {ECO:0000269|PubMed:12015966; ECO:0000269|PubMed:15576487}.', 'MGFLKILRKQRAREREMRILILGLDNAGKTTLMKKFLDEPTDTIEPTLGFDIKTVHFKDFQLNLWDVGGQKSLRSYWKNYFESTDALIWVVDSSDRERLLQCSEELKKLLGEERLAGASLLVLANKSDLPGAIDVNSIAQVLDLHSIKSHHWKIFSCCALSGDRLVQAMTWLCDDVGSRLFILD', 184, 'Q19705;', 'KD00472', 'Caenorhabditis elegans', 'evl-20', '#ADP-ribosylation factor-like protein 2#Abnormal eversion of vulva protein 20', '-', '-', '191632'),
(473, 'Q6FLB2', 'DASH complex subunit DAM1', 'GO:0008608===GO:0042729', 34876, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MSQDIRKEDGVRSATEYKLSMSSNPGSRRSSMADAESFNDDNMVLKNDVLREYLLPQIKDLTDSVVTLDSNMTRLNFIHDNLVDLNESFGSLLYGLMCNSWCVEFPNAPTRFDKEIRLMNEIEELSAEKSKLKSRLNSLREKPNAQTSDEKMKKPSGISQPIFQKPNVRRPRNALNDENLHKFNRENPPVYDDKREADEDTNSEASFVSNPANSKDMQLFANGSSNNDPKSRLRRKSILHTIRNSIASTSDAYDRKKQQGIQMGRVSLGGGAARVVSGRNMFEQQRTTRHSTTGIPNRVVKKRPPFK', 307, 'Q6FLB2;', 'KD00473', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'DAM1', '#DASH complex subunit DAM1#Outer kinetochore protein DAM1', '-', '-', '2890705'),
(474, 'B0BM16', 'Spindle and kinetochore-associated protein 3', 'GO:0000940', 62908, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it mediates the microtubule-stimulated oligomerization (By similarity). {ECO:0000250}.', 'MSVTGNFFSKLRSLAVTLEKETGQLEQLFSSEDNEYEEESPMRVLHDLRSDIMVLKGDFQSTLNKRLARGQELSAFIKACRVLHERTAADIEQIKETFQTYGYKPQCNANSEREQTQESGKPKENGVSPNKADVEDLQALPTLEKTASTSWDILRAPQLSDFGLAHYQLPTAWEPPKVKPCKKDPEEEKPRIMLKDPEPMNVAKTPKCALRLEEDFSQIQHFGISDCSTNLNDDYTMALINKKFQKNQNVTENAAKETCQPKNLKSLLATPSHLSHRMDWVDSPLPPVFCTPGLKVHKKEKMSLPGKPAEKKGLNANNTTLPSDTCDRNDPDSAHLEDDYECTAVKPAIDFKSTSAAPAYLSLGSNINSVYSPRPPVFCTPGLKVHKKETSSVLADPTEPKGTGCTDTPPLPSFQTNWLKSDAKEKGLDITEPVPRPDLSYRQCLEEPPTLVLNSNKYEAPAMRDYCMGTPPRPEMTVSLTEDLFKYNVKPSSPPKVSEYENMLWTPVRPEMTSCITEDISQILSKYCDNNMNPADGIWDKAGAPFGKISTEYENKENRLY', 561, 'B0BM16;', 'KD00474', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'ska3', '#Spindle and kinetochore-associated protein 3', '-', '-', '100144945'),
(475, 'Q9QZS2', 'E3 ubiquitin-protein ligase RNF4', 'GO:0090234', 21911, 'E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates ''Lys-6''-; ''Lys-11''-; ''Lys-48''- and ''Lys-63''-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly; it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively; it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor- mediated transcriptional activation. {ECO:0000269|PubMed:20681948}.', 'MSTRNPQRKRRGGTVNSRQTQKRTRETTSTPEVSLETEPIELVETVGDEIVDLTCESLEPVVVDLTHNDSVVIVEERRRPRRNGRRLRQDHADSCVVSSDDEELSRDKDVYVTTHTPRSTKDDGATGPRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI', 194, 'Q9QZS2; O35941; Q541Z6;', 'KD00475', 'Mus musculus (Mouse)', 'Rnf4', '#E3 ubiquitin-protein ligase RNF4#6.3.2.-#RING finger protein 4', '-', '-', '19822'),
(476, 'P27790', 'Major centromere autoantigen B', 'k', 65381, 'Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA; called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes (By similarity). {ECO:0000250}.', 'MGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVACSGVTRSRARSSAPRAPAAPAGPATVPSEGSGGSTPGWHTREEQPPSVAEGYASQDVFSATETSLWYDFLSDQASGLWGGDGPARQATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQGGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLAAQSLDTSGLRHVQLAFFPPGTVHPLERGVVQQVKGHYRQAMLLKAMAALEGQDPSGLQLGLVEALHFVAAAWQAVEPSDIATCFREAGFGGGLNATITTSFKSEGEEEEEEEEEEEEEEEEEGEGEEEEEEEEEGEEEGGEGEEEGEEEVEEEGEVDDSDEEEEESSSEGLEAEDWAQGVVEASGGFGGYSVQEEAQFPTLHFLEGGEDSDSDSDEEEDDEEEDEEDEDEEDDEDGDEVPVPSFGEAMAYFAMVKRYLTSFPIDDRVQSHILHLEHDLVHVTRKNHARQAGVRGLGHQS', 599, 'P27790; Q7TSG8;', 'KD00476', 'Mus musculus (Mouse)', 'Cenpb', '#Major centromere autoantigen B#Centromere protein B#CENP-B', '-', '-', '12616'),
(477, 'Q50HP4', 'DASH complex subunit dad4', 'GO:0042729===GO:0031134', 8351, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. May be necessary for growth under high osmotic stress. {ECO:0000269|PubMed:16079914}.', 'MNNPMEEQQSALLGRIISNVEKLNESITRLNHSLQLINMSNMNVELASQMWANYARNVKFHLEETHTLKDPI', 72, 'Q50HP4;', 'KD00477', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dad4', '#DASH complex subunit dad4#Outer kinetochore protein dad4', '-', '-', '5802828'),
(478, 'Q10173', 'Kinetochore protein nuf2', 'GO:0000778===GO:0051455===GO:0031617===c;k', 51911, 'Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Acts as a component of the essential kinetochore-associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:11685532; ECO:0000269|PubMed:15728720}.', 'MARKHTFPSLKRAEILECIDGLGIPFTAKELDQPTSKAVIPLYEEFLDLFMGLTRQNLEEKVNSLQDSVENFEIIHESLRFTVFYQILSQFMQNICFHDFTIQDLLKPDRNRLQLILSAVINFAKLREERLQQFDDDIQKRESLLETYTLLDAQRKDLEEKVLLSQDRKLESEAIIKQNEERNEEMFQSLIEDKRLCSQVRTEYDRIRMEASELKIRYHNVDSLMASTLEEIEKLQSSIVHSPEKLKGKIADTSLRIQNDRSQQVELDKKSKILHTKLNSLQLIEGDLNACLKVLEECLVELDKLEHATVLLSTNQELCDQIEINKKKLEFRKEQLLKQLSNAQEKLEHEQHSRNQKLEAAKQRMDNIREEYKVITQERNKKIQETEKKNAMIEMTEQKIAGMREELESQISSITMEFEKLKSHVELYIAELLRNLRSSNS', 441, 'Q10173;', 'KD00478', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'nuf2', '#Kinetochore protein nuf2#NMS complex subunit nuf2', '-', '-', '2542004'),
(479, 'Q5R9W0', 'Protein MIS12 homolog', 'GO:0051382===GO:0000444', 24140, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis. {ECO:0000250}.', 'MSVDPMTYEAQFFGFTPQTCMLRIYIAFQDYLFEVMQAVEQVILKKLDGIPDCDISPVQIRKCTEKFLCFMKGHFDNLFSKMEQLFLQLILRIPSNILLPEDKCKETPYSEEDFQHLQKEIEQLQEKYKTELCTKQALLAELEEQKIVQAKLKQTLTFFDELHNVGRDHGTSDFRESLVSLVQNSRKLQNIRDNVEKESKRLKIS', 205, 'Q5R9W0;', 'KD00479', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'MIS12', '#Protein MIS12 homolog', '-', '-', '100190827'),
(480, 'O88658', 'Kinesin-like protein KIF1B', 'GO:0003777', 204170, 'Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility (By similarity). {ECO:0000250}.', 'MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQSRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEDMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLMDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTASMGSLTSSPSSCSLNSQAGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNTGEVIVTLEPCERSETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKREKEEADLLLEQQRLDYESKLQALQKQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPVPPELLPTEMGKTHEDRPFPRTVVAVEVQDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVGSNAQDDSETTMTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDAMEDFDDEAFVDDTGSDAGTEEGSELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFPSAAMTRSGLSLEELRIVEGQGQSSEVISPPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLGFYHVQNIAVEVTESFVDYIKTKPIVFEVFGHYQQHPLHLQGQELNSPPQPSRRFFPPPMPLSRPVPATKLNTMNKTSLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAILSLNIISAKSLKSSHSSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRNLFGSGYSKSPDSNRVTGIYELSLCKMADTGSPGMQRRRRKVLDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSIPKSMSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSADIESLVDREKELATKCLQLLTHTFNREFSQVHGSISDCKLSDISPIGRDPSVSSFSSSTLTPSSTCPSLVDSRSSSMDQKTPEANSRASSPCQEFEQFQIIPTVETPYLARAGKNEFLNLVPDIEEVRAGSVVSKKGYLHFKEPLSSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMLKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQPKY', 1816, 'O88658; Q65Z71; Q8R524;', 'KD00480', 'Rattus norvegicus (Rat)', 'Kif1b', '#Kinesin-like protein KIF1B', '-', '-', '117548'),
(481, 'Q5XGF1', 'Centromere protein N', 'GO:0034508', 39701, 'Probable component of a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. {ECO:0000250}.', 'MDEWIAEFIKRIILKLPFSQTMTILKAWGFLTDSELQTLTLRYPKDITATEVVRLCEAKNATIDHAAALDFVFNHAFSNKKLWTVYQMSKTSESENDLFDASEFKLQFKKSIHAVSKNVTINFKEFGEALWIRIAWGTHNTRPNQYKATFAVYHSQTPHVFITGLGKACRPLLCQALVIASKYSQIQEMELKSRCLESLKDIVFKRFNQPFSSHHSRPHEKALTQKIVDPRVTYENMREKERVHHLTRETFGEGPLPKLELASYKLETMFRAESIMGGNLTAGNEPFRCVVKFSSPHLLEAIRSLAPAGIAEAPISTLLSCIPHKARNSFKITEKRGLHPASSQPTNF', 348, 'Q5XGF1; Q28E44;', 'KD00481', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'cenpn', '#Centromere protein N#CENP-N', '-', '-', '496510'),
(482, 'Q9VKN7', 'Aurora kinase B', 'GO:0000776===GO:0008608===GO:0032133===GO:0000780===k;m', 38301, 'Serine/threonine-protein kinase which mediates both meiotic and mitotic chromosome segregation. Required for histone H3 ''Ser-10'' phosphorylation. Phosphorylates mei-S332 within residues 124-126 and stabilizes its association with centromeres during meiosis. {ECO:0000269|PubMed:11266459; ECO:0000269|PubMed:11352945; ECO:0000269|PubMed:16824953}.', 'MTLSRAKHANRNHLPHLLAKVPEEHQEPIKNMCLKMMSHDAYGQPYDWSPRDFEMGAHLGRGKFGRVYLARERHSHYLVAMKVMFKEELRKGCVQRQVLREIEIQSRLKHPHILRLLTWFHDESRIYLALEIASEGELFKHLRGAPNHRFDEPRSAKYTYQVANALNYCHLNNVIHRDLKPENILLTSTDDLKLADFGWSAHTPNNKRRTLCGTLDYLPPEMVDGNSYDDSVDQWCLGILCYEFVVGCPPFESNSTESTYSKIRRMEISYPSHLSKGCKELIGGLLRKESKGRITLVDVMTHYWVKAGMAERELQLQKRERGKENTARN', 329, 'Q9VKN7; Q9XTQ0;', 'KD00482', 'Drosophila melanogaster (Fruit fly)', 'ial', '#Aurora kinase B#2.7.11.1#IPL1/Aurora-like protein kinase#Serine/threonine-protein kinase Ial#Serine/threonine-protein kinase aurora-B', '-', '-', '34504'),
(483, 'P0DJH7', 'Centromere protein X', 'GO:0000777===GO:0051382', 9257, 'DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Recruited to forks stalled by DNA interstrand cross-links; and required for cellular resistance to such lesions (By similarity). Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation. {ECO:0000250; ECO:0000269|PubMed:19620631; ECO:0000269|PubMed:22304917}.', 'MEEREGGFRKETVERLLRLHFRDGRTRVNGDALLLMAELLKVFVREAAARAARQAQAEDLEKVDIEHVEKVLPQLLLDFV', 80, 'P0DJH7;', 'KD00483', 'Gallus gallus (Chicken)', 'STRA13', '#Centromere protein X#CENP-X', '-', '-', '-'),
(484, 'P0DJH6', 'Centromere protein W', 'GO:0000777===GO:0051382', 8743, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPW has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000250; ECO:0000269|PubMed:19070575; ECO:0000269|PubMed:22304917}.', 'MRRTVPRGTLRKIIKKHKPHLRLAANTDLLVHLSFLLFLHRLAEEARTNAFENKSKIIKPEHTIAAAKVILKKSRG', 76, 'P0DJH6;', 'KD00484', 'Gallus gallus (Chicken)', 'CENPW', '#Centromere protein W#CENP-W', '-', '-', '421716'),
(485, 'Q12834', 'Cell division cycle protein 20 homolog', 'c;k', 54723, 'Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. {ECO:0000269|PubMed:9637688; ECO:0000269|PubMed:9734353; ECO:0000269|PubMed:9811605}.', 'MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYIPHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR', 499, 'Q12834; B2R6Z6; D3DPJ1; Q5JUY4; Q9BW56; Q9UQI9;', 'KD00485', 'Homo sapiens (Human)', 'CDC20', '#Cell division cycle protein 20 homolog#p55CDC', 'BIOMD0000000186,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Dissociation variant;BIOMD0000000187,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Convey variant;BIOMD0000000193,Ibrahim2008_MCC_assembly_model_KDM;BIOMD0000000194,Ibrahim2008_Cdc20_Sequestring_Template_Model;', 'ENSG00000117399', '-'),
(486, 'Q9WUB4', 'Dynactin subunit 6', 'GO:0000777', 20670, '', 'MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIIIGEGNLIEEQALIINAHPDNIIPDTEDTEPKPMIIGTNNVFEVGCHSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCSLNTFEAIPENTVIYGADCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKTMKGSSTPVKN', 190, 'Q9WUB4; Q8C2M9; Q9QZB8;', 'KD00486', 'Mus musculus (Mouse)', 'Dctn6', '#Dynactin subunit 6#Dynactin subunit p27#Protein WS-3', '-', '-', '22428'),
(487, 'P04551', 'Cyclin-dependent kinase 1', 'GO:1902424', 34359, 'Plays a key role in the control of the eukaryotic cell cycle. It is required for entry into S-phase and mitosis. When complexed with cig2; plays a role in G1-S phase transition. When activated and complexed with the cyclin cdc13; it leads to the onset of mitosis. p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II. Involved in cell cycle arrest induced by defective RNA splicing. Required for phosphorylation of dis1 to ensure accurate chromosome segregation and for the DNA damage checkpoint. {ECO:0000269|PubMed:16049013; ECO:0000269|PubMed:16920624; ECO:0000269|PubMed:8087848; ECO:0000269|PubMed:9042863}.', 'MENYQKVEKIGEGTYGVVYKARHKLSGRIVAMKKIRLEDESEGVPSTAIREISLLKEVNDENNRSNCVRLLDILHAESKLYLVFEFLDMDLKKYMDRISETGATSLDPRLVQKFTYQLVNGVNFCHSRRIIHRDLKPQNLLIDKEGNLKLADFGLARSFGVPLRNYTHEIVTLWYRAPEVLLGSRHYSTGVDIWSVGCIFAEMIRRSPLFPGDSEIDEIFKIFQVLGTPNEEVWPGVTLLQDYKSTFPRWKRMDLHKVVPNGEEDAIELLSAMLVYDPAHRISAKRALQQNYLRDFH', 297, 'P04551;', 'KD00487', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cdc2', '#Cyclin-dependent kinase 1#CDK1#2.7.11.22#2.7.11.23#Cell division control protein 2#Cell division protein kinase 1#p34 protein kinase', 'BIOMD0000000005,Tyson1991 - Cell Cycle 6 var;BIOMD0000000006,Tyson1991 - Cell Cycle 2 var;BIOMD0000000007,Novak1997 - Cell Cycle;BIOMD0000000111,Novak2001_FissionYeast_CellCycle;', '-', '2539869'),
(488, 'Q96DE5', 'Anaphase-promoting complex subunit 16', 'k', 11667, 'Component of the anaphase promoting complex/cyclosome (APC/C); a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of ''Lys-11''-linked polyubiquitin chains and; to a lower extent; the formation of ''Lys-48''- and ''Lys-63''-linked polyubiquitin chains. {ECO:0000269|PubMed:20360068}.', 'MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTYPKGAGEMLEDGSERFLCESVFSYQVASTLKQVKHDQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSG', 110, 'Q96DE5;', 'KD00488', 'Homo sapiens (Human)', 'ANAPC16', '#Anaphase-promoting complex subunit 16#APC16#Cyclosome subunit 16', '-', 'ENSG00000166295', '-'),
(489, 'Q6C452', 'Spindle assembly checkpoint component MAD1', 'GO:0000778', 79963, 'Central component of the spindle assembly checkpoint.', 'MSDTPSSPFIEHPETPRKALFSSNRPSPVRSTHATPSLHGTPSTASRFSRTPREDVIGLKKTISQLRYDLEALKQEQQVAQILQEEKERELEAKHKKELDRAEQAESDQVFLFNKQKELSDENRTLKEELRSLQSQHEADGRELNHELEGLKDLLNDLQSENRALVSEMNYKIEDYEHRIKAASTTTDDLLKEVENRGTALTEAKMNVVKFEQLVESLKGESLDLKQSAKDLEAVEQTKSQLSDQIKYSRELEAKVSALTVRVEAAESAQQLSQVYEEDLSSMKGKLKNMEGLRQQLAEQQLQILVHEENSAKWKAYLEKSDEFKTVEEVVTALNKARMEKASLLERAGSGVNDETRSTAEAYARLQERVTTLESELQLAQNQLKTEKKKVATSIRQHTLAANEAKFLREQLKAYDDEEVTAAGADVKQGRIDELEKLLEAVKNEKSVLEGELKEARSEQGCTVAAGTKRPRADDSVSSEVISEYTRKLQTLQQEFDEVSVEARLLAKTKEALEARLESLEKSQESRVRILELRENPTSRHEAVKQSMLDTLKAENEALMGKNENSKSVPQASLERKQLELQGVRDKLASTEKSYQRLKEVFSVKSLEFREAVYALTGYQIDILRNKKVKVTSMYAQSDEDSFTFLPDPNHKGQFAGVIDSPLTDEFSNIVDYWVKDKKDFPCFLAALNLELYERKENNGNQAS', 704, 'Q6C452;', 'KD00489', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'MAD1', '#Spindle assembly checkpoint component MAD1#Mitotic arrest deficient protein 1', '-', '-', '2911916'),
(490, 'P28867', 'Protein kinase C delta type', 'c;k', 77547, 'Calcium-independent; phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis; but acting as an anti-apoptotic protein during cytokine receptor- initiated cell death; is involved in tumor suppression; is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage; activates the promoter of the death- promoting transcription factor BCLAF1/Btf to trigger BCLAF1- mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress; interact with and activate CHUK/IKKA in the nucleus; causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis; can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14; inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP); whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment; is required for the activation of the apoptosis regulators BAX and BAK; which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1; which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL; probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl- leucyl-phenylalanine (fMLP)-treated cells; is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity; and regulates TNF-elicited superoxide anion production in neutrophils; by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5; leukotriene B4 or PMA. In collagen-induced platelet aggregation; acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1; PAR4 and CD36/GP4 receptors; regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion; whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C- terminal and regulates the interaction between MUC1 and beta- catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB; YWHAZ and YWHAH) in a sphingosine-dependent fashion. {ECO:0000269|PubMed:11976686; ECO:0000269|PubMed:11976687; ECO:0000269|PubMed:18025218; ECO:0000269|PubMed:19917613; ECO:0000269|PubMed:9705322}.', 'MAPFLRISFNSYELGSLQVEDEASQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKTTFDAHIYEGRVIQIVLMRAAEDPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMCVQYFLEDGDCKQSMRSEEEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKEFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTATNSRDTIFQKERFNIDMPHRFKVYNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRSSRKLDTTESVGIYQGFEKKPEVSGSDILDNNGTYGKIWEGSTRCTLENFTFQKVLGKGSFGKVLLAELKGKDKYFAIKCLKKDVVLIDDDVECTMVEKRVLALAWESPFLTHLICTFQTKDHLFFVMEFLNGGDLMFHIQDKGRFELYRATFYAAEIICGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENIFGEGRASTFCGTPDYIAPEILQGLKYSFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDIMEKLFERDPDKRLGVTGNIRIHPFFKTINWSLLEKRKVEPPFKPKVKSPSDYSNFDPEFLNEKPQLSFSDKNLIDSMDQEAFHGFSFVNPKFEQFLDI', 674, 'P28867; Q91V85; Q9Z333;', 'KD00490', 'Mus musculus (Mouse)', 'Prkcd', '#Protein kinase C delta type#2.7.11.13#Tyrosine-protein kinase PRKCD#2.7.10.2#nPKC-delta#Protein kinase C delta type regulatory subunit#Protein kinase C delta type catalytic subunit#Sphingosine-dependent protein kinase-1#SDK1', '-', '-', '18753'),
(491, 'Q1JQ97', 'Bardet-Biedl syndrome 4 protein homolog', 'GO:0003777', 58221, 'May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor; which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8; the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane (By similarity). {ECO:0000250}.', 'MAEEKLSARTQLPVSAESQKPVLKKAPEFPILEKQNWLIHLYYIQKDYEACKAVIKEQLQETHGLCEYAIYVQALIFRLEGNIQESLRLFQMCAFLSPQCADNLKQVARSLFLLGKHKAAIEVYNEAAKLNQKDWEICHNLGVCYIYLKQFDKAQDQLHNALHLNRHDLTYIMLGKIFLLKGDLDKAIEIYKKAVEFSPENTELLTTLGLLYLQLGIYQKAFEHLGNTLTYDPTNYKAILAAGSMMQTHGDFDVALTKYKVVACAVIESPPLWNNIGMCFFGKKKYVAAISCLKRANYLAPLDWKILYNLGLVHLTMQQYASAFHFLSAAINFQPKMGELYMLLAVALTNLEDSENAKRAYEEAVRLDKCNPLVNLNYAVLLYNQGEKRDALAQYQEMEKKVNLLKYSSSLEFDPEMVEVAQKLGAALQVGEALVWTKPVKDPKSKHQTASTSKAAGFQQPLGSNQALGQAMSSAATCRKLSSGAGGTSQLTKPPSLPLEPEPTVEAQPTEASAQTREK', 519, 'Q1JQ97;', 'KD00491', 'Bos taurus (Bovine)', 'BBS4', '#Bardet-Biedl syndrome 4 protein homolog', '-', '-', '532120'),
(492, 'P78716', 'Dynein heavy chain; cytoplasmic', 'GO:0003777', 493463, 'Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.', 'MEVTSAAAPSTGSSANGVTAAAPFPTIEPERVVEHLAAVCEIALGATRDELEQLGSLLHKARYGETVSRCTRFASDSQNVLYIQKDIANPSAVEAGADPAAPVTYNYTLSTEISSSSTTVSSLVLIKSPQPIDPTRPLTSQIFITNLPGPASLNAGVGEQGTALSPWEVLHSQVHHALVPYFDANTKSQQLANGSRGRADVDAKTGIPVTKKRLNDLELSLLHLQQNVDIPEISLTFHSIVQNVLDDAESRHTRPSLDAIPQIFSQDSTFLNRLQANVNTWIKSIQGITKLTKDPSSNANQEFNTASQEVNFWLSMESALEGIEGQLRSEGVLLTLEILKHAKRFQATVSFTADTGLKEAMDKVQKYNQLMRDFPLDELLSATSLSKAQEAIAQIFGHLNKKLRICPYPIRRALPLVEAISADLDEVLHRLLPGTELVNLDYQQFQTIMQTCDDIFRTWEENVKEFTNVAREVTRRRNEKFIPIKINKKHSELESRIKYVSTFRDNHEQLQRTIINVLGPQATIPGVTETTGSNGIVMEEMGDVDAVEEVKQAWEALHNVDLLDVTDQGKERWVRAENLYNERTTRVENSIIARLRDRLATAKTANEMFRVFSKFNALFVRPKIRGAIQEYQNQLMDHVKQAINGLHERFKQQYGHSETHAMAQLRDLPPVSGAIIWARQIEFQLDGYMRKVEAVLGPDWTMHTEGHKLQEESELFKQKLDTARIYEAWIADVGRRKISISGQLFEIARVRSAGGILELTVNFDPQVITLFKETRNLTWQSYSVPHAVTTVSKDAKRVYPYAVSLMESVRTLSQTLRQISVMGEESVLLFGYRNDVYKLISEGVPLRWESFINSHELFYSDNRQTRPLLPGGTDFGLAKNTESKHGMFIRGFAAAVSVLQQKAVSLNFIHATVEQALKELNTCPYEEAAFHSRLDTIQAAVDQLNLEQYVNLDFWVRGLNSKVQSILLTRLQSAVHAWIEAFEDDTPDDEMRRKVNNNNEEAKPDGPTMKRLVLELAMRNQVIYLDLLLEFARASWFLHLHEWLGIVCNLRKIKATRYQMSLTTTANDEPRFTDLPSECAGLLQRVYVSVEKKLHEVSAYVDKWLQFQSLWDLQSEQVYDALGEQLPRWLQLLQEIRKTRSTFDTQEVSRAFGHLTIDYDQVQTKVNAKYDQWQHEILMKFASRLGNRMREINAEIEKARKHLESQSSDASSTAQAVQFITVVQSCKRNVKTWAPEIDMFRQGQSTLVRQRYQFPNDWLHIEQIDSQWEALKEILEKKSRIVQDQTDALQAKIVAEDKLINERIAEIAAQWNEEKPVSGTIQPDVASATLSSFESRISKLQDDAQMVAKAKEALDIPASPDTSLEATLEEVRDFQSVWSNLSTIWASLNETRDVLWTAVQPRKIRSKVDDLIKSTKEMPSRMRQYAAFEHVQGILRGFLKVNSILSDLKSDAIRERHWHKIYKQIKPQKRFSPSSMTLGDVWDLNLVATEVIVKDIIAQAQGEMVLEEFLKQVRETWQNYALEMVNYQNKIGLIRGWDDLFAKCSENLNSLQAMKHSPYYKEFEEEAVAWEDKLNRVHVLFDVWIDVQRQWVYLEGVFTGNADIKHLLPIESGRFQNINSEFLAVMKKANKSPYVLEVLNIPNVQKSLERLAEMLNKIQKALGEYLEKERVSFPRFYFVGDEDLLEMIGNSNDTLRIAKHFKKMFAGLSGLVMDDETVISGFTSKEGEVVRLKKEISLAKTPKINDWLALLEGGMKSTLAELLAEAVDQYTPIFESETIDREALNGFMDAYPSQIVVLATQVVWTTAVHKSLTTGGETLKAIFDREVRVLRVLADTVLGELEVILRKKCEQQITECVHQRDTIEKLINAKANSTNHYLWQLQMRYVYEPQGEYLDRLYIKMANAKLNYGFEYLGVPERLVRTPLTDRCFLTLTQALCQRLGGSPYGPAGTGKTESVKALGVQLGRFTLVFCCDDTFDFQAMGRIFLGICQVGAWGCFDEFNRLEERILSAVSQEIQNIQLGLKQGVEDDQSQIELVGRHLHVNENTGIFITMNPGYAGRSNLPDNLKKLFRSVAMSKPDKELIAEVMLYSQGFNQAKQLSKQTVPFFDQCSGRLSKQAHYDFGLRALKSVLVSSGGLKRARLGEGSLGAEEVVEPEIIVQSIRETIAPKLIKSDVDIMATIETDCFPGVQYVPANLEALENAIRELAAERHLVVNELWMTKVLQLYQIQKIHHGVMMVGNSGSGKSAAWRLLLDALQKVEGVEGVSHVIDSKVMSKEALYGNLDSTTREWTDGLFTSILRKIVDNLRGEDSKRHWIVFDGDVDPEWVENLNSVLDDNKLLTLPNGERLNLPANVRIMFEVETLKYATLATVSRCGMVWFSEDTVSPTMMVQNYLSTLRSVPFEDLDEDSVATGHTPAKTLAVQSEFASLLHVYLTDENFILPALQRAEGYNHIMEFTTARVLTTLFSLLNKAVRDAIEYNGQHSDFPLESEQIESFISKKLLLALVWALTGDCPLTDRKSFGDDICALANFGSPPLDGNSSLIDFDVTLPKAEWAPWQNQVPSVEVNTHSITQTDVVIPTLDTVRHENVLYSWLAEHKPLLLCGPPGSGKTMTLFSALRKLPNMEVVGLNFSSATTPDLLIKTFEQYCEYKKTLNGVMLSPTQIGRWLVIFCDEINLPAPDKYGTQRAISFLRQLVEHNGFWRTSDKSWVTLDRIQFVGACNPPTDAGRTPMGARFLRHAPLIMVDYPGELSLNQIYGTFNSAVLKIIPSLRGYAEPLTHAMVRFYLESQQRFTPKIQPHYVYSPRELTRWVRGVYEAIRPLEALTIEGLIRIWAHEALRLFQDRLVAEEERQWTDESVRRIALEFFPNIDEEKALGGPILFSNWLSKNYVPVDREQLRDFVKARLKTFCEEEVDVPLILFNDVLEHVLRIDRVFRQPQGHLILIGVSGSGKTTLSRFVAWMNGLKVFQIKVHGKYSAEDFDDDLRDVLRRCGCKGEKICFIMDESNVLDSGFLERMNTLLANAEVPGLFEGDEYAALMTACKEGAQRQNLRLDSPEEMYKWFTQQIVKNLHVVFTMNPPEDGLSSKAATSPALFNRCVLNWFGDWSDQALFQVGHELTQSIDLDRSNFECPDTIPVAYRGLQLPPSHRERVVNSMVHIHYSLQRYNEKLLKQQGKVTFLRPRHFLDFVTQYIKLYNEKREDLEEQQRHLNVGLEKLRDTVDKVRDLRVSLAEKKKQLEQKDAEANEKLQRMVADQREAEQRKNTSLEIQANLEKQEAEVASRKKVVLEDLAKAEPAVEEAKASVSNIKRQHLTEVRSMGNPPQGVRLAMDAVCTLLGHRINDWKAVQGILRKDDFIASILMFDNAKQMTKGLRNKMRNDFLSNPEFTFEKVNRASKACGPLVQWVAAQVNYFDILDRVGPLKIEVEQLEDQALETKAQAKSVQNNIADLEASINTYKTEYAALISETQAIKAEMSRVQFKVDRSVRLLDSLSSERVRWEAGSKSFEIQISTLVGDVLVAAAFLAYSGLYDQTFRKSMMDDWFHQLHLSGIQYKSPNPVTEYLSTADERLGWQENALPVDDLCTENAIILKRFNRYPLIIDPSGRVTEFLQKECKDRRLTVTSFLDDTFTKQLESSLRFGNPILIQDAEHLDPILNHVLNKECQRTGGRVLIQLGKQEIDFSPAFKLYLSTRDPSATFAPDICSRTTFVNFTVTQSSLQTQSLNDVLKSERPDVDERRSNLIKLQGEFKIHLRQLEKRLLQALNESRGNILDDDNVIETLETLKTEAAEISAKMSNTEGVMAEVEEITQQYSIIARSCSAVFAVLEQLHYLNHFYQFSLQYFLDIFQSVLHGNKNLANETDHNARRDVIVHDLFVNTFKRTALGLLQKDRITLGMLLAQASPYKMDKSVIDMILDNRVEGKDLSSHPDDRENAFAQAKKLSAIKDKIDAISTEDWDKFFTEELAENAVPHIWDEKTEAIDQALLSLLLVKLFRMDRFVPAAERFVAQVFGSDIFDIVEDLKQTVTQVSATLPISLVSSPGFDASYKVDNLVERMRVKCTNIAMGSNEGLASADKAISNAAQTGSWVLVKNVHLAPTWLQSLEKRMESLNPHSDFRLFLSMESSPKIPVNLLRASRVLMYEQPAGVRANMKDSMSSLSTRATKSPVERTRLYLLLSFLHAVVQERLRYAPNLGWKGFWEFNDSDYECSAYIVDTWIDGVAGNRTNLAPQNIPWEMLRYLVTETYGGKIDDEGDFKLLSQLVTSFLTPAAYEVDHKLVDGPEGGLVVPSGTSFQDFNAWIHRLPEREPPTYLGLPANAEKLLLGGLGRSLIGNLRKVTELLDEGEQLVTEV', 4349, 'P78716;', 'KD00492', 'Fusarium solani subsp. pisi (Nectria haematococca)', 'DHC1', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC', '-', '-', '-'),
(493, 'C1BK83', 'Nucleoporin seh1', 'GO:0000777===GO:0051315', 39844, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (By similarity). Required for the regulation of the TORC1 pathway by amino acids (By similarity). {ECO:0000250}.', 'MFVARSIAADHKDLIHDVSYDFHGRRMATCSSDQSVKVWDKSDNGEWNCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKQRGLSHWIKRTTLVDSRTSVTDVKFAPKHMGLMLTTCSADGVVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSNTAYSGKVQIYEYVENTRKYAKVETLMTVTDPVHDIAFAPNLGRSFHVLAIATKDVRIFKLIPMRKESSSSGPTKLEVQLQAQFDGHNSQVWRVSWNITSTLLASSGDDGCVRLWKANYMDNWKCTGILRGDGSPVNGAAGQAGTPGAAGTPGGPASQNALQAVAGRKKAQLMPG', 364, 'C1BK83;', 'KD00493', 'Osmerus mordax (Rainbow smelt) (Atherina mordax)', 'seh1l', '#Nucleoporin seh1#Nup107-160 subcomplex subunit seh1', '-', '-', '-'),
(494, 'P36601', 'DNA repair protein rhp51', 'k', 39823, 'Required both for recombination and for the repair of DNA damage caused by X-rays. Binds to single and double-stranded DNA; in the presence of magnesium; and exhibits DNA-dependent ATPase activity. Promotes DNA strand annealing and strand exchange via DNA recombinase activity and forms helical nucleoprotein filaments. {ECO:0000269|PubMed:15899844}.', 'MADTEVEMQVSAADTNNNENGQAQSNYEYDVNVQDEEDEAAAGPMPLQMLEGNGITASDIKKIHEAGYYTVESIAYTPKRQLLLIKGISEAKADKLLGEASKLVPMGFTTATEYHIRRSELITITTGSKQLDTLLQGGVETGSITELFGEFRTGKSQICHTLAVTCQLPIDMGGGEGKCLYIDTEGTFRPVRLLAVADRYGLNGEEVLDNVAYARAYNADHQLELLQQAANMMSESRFSLLVVDSCTALYRTDFSGRGELSARQMHLARFMRTLQRLADEFGIAVVITNQVVAQVDGISFNPDPKKPIGGNILAHSSTTRLSLRKGRGEQRICKIYDSPCLPESEAIFAINSDGVGDPKEIIAPV', 365, 'P36601;', 'KD00494', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rhp51', '#DNA repair protein rhp51#RAD51 homolog', '-', '-', '-'),
(495, 'Q9P6M3', 'Kinetochore protein mis14', 'GO:0000778===GO:0000941===GO:0031617===GO:0061638===GO:0000779===k', 24122, 'Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Required for correct chromosome segregation where it has a role in the formation and/or maintenance of specialized chromatin at the centromere. {ECO:0000269|PubMed:15369671}.', 'MSSHGDASVLPKIALESINDYSYVKSVFRQAIQEKLAIHLPEQASREAGMGREDQLRIRVKEMLNELIESTFSIIQENVTINGFDANSALQDPKNSDQIEPFDLALRTRVQQLFNEVEDAHVLVARYRKSVPAQYEKAYVDAMEQQTAFLRNVKDDYVSLQDKEVENPDEQTSTTVFRKEDIDRYEQTIAKVAYLKKNLPRVVARLEKTP', 210, 'Q9P6M3;', 'KD00495', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis14', '#Kinetochore protein mis14#NMS complex subunit mis14', '-', '-', '2543482'),
(496, 'O74844', 'Kinetochore protein fta7', 'GO:0000776===GO:0000779', 28843, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. {ECO:0000269|PubMed:16079914}.', 'MEMKRRVRAVRRDQIQKRWRPLEDKQRQEIIIIFRTCSRLVLNTIKSETRKSLAEEWFMNILLKIEAPLRNLPVPRKRKESILFSQLLSSNMQLEQQLYSDLDHINVLQQELKVETARLENEQKSYEEMKQNMAINNSRLADLKSKLHPYLKKGLKISHDNFSDSNDFSFQKKLNTEDSNTSKTSTLDMYKEKLKPFTKTMQIHANKTVQLSQTIQKATLLLQRLNNTKNIGLNKSSKLKIKNI', 244, 'O74844;', 'KD00496', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'fta7', '#Kinetochore protein fta7#Sim4 complex subunit fta7#Sim4-mal2-associated protein 7', '-', '-', '2539115'),
(497, 'Q9NYC9', 'Dynein heavy chain 9; axonemal', 'GO:0003777', 511877, 'Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.', 'MRLAEERAALAAENADGEPGADRRLRLLGTYVAMSLRPAAGAWERCAGSAEAEQLLQAFLGRDAAEGPRPLLVVRPGPRGLAIRPGLEVGPESGLAGAKALFFLRTGPEPPGPDSFRGAVVCGDLPAAPLEHLAALFSEVVLPVLANEKNRLNWPHMICEDVRRHAHSLQCDLSVILEQVKGKTLLPLPAGSEKMEFADSKSETVLDSIDKSVIYAIESAVIKWSYQVQVVLKRESSQPLLQGENPTPKVELEFWKSRYEDLKYIYNQLRTITVRGMAKLLDKLQSSYFPAFKAMYRDVVAALAEAQDIHVHLIPLQRHLEALENAEFPEVKPQLRPLLHVVCLIWATCKSYRSPGRLTVLLQEICNLLIQQASNYLSPEDLLRSEVEESQRKLQVVSDTLSFFKQEFQDRRENLHTYFKENQEVKEWDFQSSLVFVRLDGFLGQLHVVEGLLKTALDFHKLGKVEFSGVRGNALSQQVQQMHEEFQEMYRLLSGSSSDCLYLQSTDFENDVSEFNQKVEDLDRRLGTIFIQAFDDAPGLEHAFKLLDIAGNLLERPLVARDTSDKYLVLIQMFNKDLDAVRMIYSQHVQEEAELGFSPVHKNMPTVAGGLRWAQELRQRIQGPFSNFGRITHPCMESAEGKRMQQKYEDMLSLLEKYETRLYEDWCRTVSEKSQYNLSQPLLKRDPETKEITINFNPQLISVLKEMSYLEPREMKHMPETAAAMFSSRDFYRQLVANLELMANWYNKVMKTLLEVEFPLVEEELQNIDLRLRAAEETLNWKTEGICDYVTEITSSIHDLEQRIQKTKDNVEEIQNIMKTWVTPIFKTKDGKRESLLSLDDRHDRMEKYYNLIKESGLKIHALVQENLGLFSADPTSNIWKTYVNSIDNLLLNGFFLAIECSLKYLLENTECKAGLTPIFEAQLSLAIPELVFYPSLESGVKGGFCDIVEGLITSIFRIPSLVPRLSPQNGSPHYQVDLDGIPDLANMRRTLMERVQRMMGLCCGYQSTFSQYSYLYVEDRKEVLGQFLLYGHILTPEEIEDHVEDGIPENPPLLSQFKVQIDSYETLYEEVCRLEPIKVFDGWMKIDIRPFKASLLNIIKRWSLLFKQHLVDHVTHSLANLDAFIKKSESGLLKKVEKGDFQGLVEIMGHLMAVKERQSNTDEMFEPLKQTIELLKTYEQELPETVFKQLEELPEKWNNIKKVAITVKQQVAPLQANEVTLLRQRCTAFDAEQQQFWEQFHKEAPFRFDSIHPHQMLDARHIEIQQMESTMASISESASLFEVNVPDYKQLRQCRKEVCQLKELWDTIGMVTSSIHAWETTPWRNINVEAMELECKQFARHIRNLDKEVRAWDAFTGLESTVWNTLSSLRAVAELQNPAIRERHWRQLMQATGVSFTMDQDTTLAHLLQLQLHHYEDEVRGIVDKAAKEMGMEKTLKELQTTWAGMEFQYEPHPRTNVPLLCSDEDLIEVLEDNQVQLQNLVMSKYVAFFLEEVSGWQKKLSTVDAVISIWFEVQRTWTHLESIFTGSEDIRAQLPQDSKRFEGIDIDFKELAYDAQKIPNVVQTTNKPGLYEKLEDIQGRLCLCEKALAEYLDTKRLAFPRFYFLSSSDLLDILSNGTAPQQVQRHLSKLFDNMAKMRFQLDASGEPTKTSLGMYSKEEEYVAFSEPCDCSGQVEIWLNHVLGHMKATVRHEMTEGVTAYEEKPREQWLFDHPAQVALTCTQIWWTTEVGMAFARLEEGYESAMKDYYKKQVAQLKTLITMLIGQLSKGDRQKIMTICTIDVHARDVVAKMIAQKVDNAQAFLWLSQLRHRWDDEVKHCFANICDAQFLYSYEYLGNTPRLVITPLTDRCYITLTQSLHLTMSGAPAGPAGTGKTETTKDLGRALGILVYVFNCSEQMDYKSCGNIYKGLAQTGAWGCFDEFNRISVEVLSVVAVQVKSIQDAIRDKKQWFSFLGEEISLNPSVGIFITMNPGYAGRTELPENLKSLFRPCAMVVPDFELICEIMLVAEGFIEAQSLARKFITLYQLCKELLSKQDHYDWGLRAIKSVLVVAGSLKRGDPDRPEDQVLMRSLRDFNIPKIVTDDMPIFMGLIGDLFPALDVPRRRDPNFEALVRKAIVDLKLQAEDNFVLKVVQLEELLAVRHSVFVVGGAGTGKSQVLRSLHKTYQIMKRRPVWTDLNPKAVTNDELFGIINPATGEWKDGLFSSIMRELANITHDGPKWILLDGDIDPMWIESLNTVMDDNKVLTLASNERIPLNPTMKLLFEISHLRTATPATVSRAGILYINPADLGWNPPVSSWIEKREIQTERANLTILFDKYLPTCLDTLRTRFKKIIPIPEQSMVQMVCHLLECLLTTEDIPADCPKEIYEHYFVFAAIWAFGGAMVQDQLVDYRAEFSKWWLTEFKTVKFPSQGTIFDYYIDPETKKFEPWSKLVPQFEFDPEMPLQACLVHTSETIRVCYFMERLMARQRPVMLVGTAGTGKSVLVGAKLASLDPEAYLVKNVPFNYYTTSAMLQAVLEKPLEKKAGRNYGPPGNKKLIYFIDDMNMPEVDAYGTVQPHTIIRQHLDYGHWYDRSKLSLKEITNVQYVSCMNPTAGSFTINPRLQRHFSVFVLSFPGADALSSIYSIILTQHLKLGNFPASLQKSIPPLIDLALAFHQKIATTFLPTGIKFHYIFNLRDFANIFQGILFSSVECVKSTWDLIRLYLHESNRVYRDKMVEEKDFDLFDKIQTEVLKKTFDDIEDPVEQTQSPNLYCHFANGIGEPKYMPVQSWELLTQTLVEALENHNEVNTVMDLVLFEDAMRHVCHINRILESPRGNALLVGVGGSGKQSLTRLAAFISSMDVFQITLRKGYQIQDFKMDLASLCLKAGVKNLNTVFLMTDAQVADERFLVLINDLLASGEIPDLYSDDEVENIISNVRNEVKSQGLVDNRENCWKFFIDRIRRQLKVTLCFSPVGNKLRVRSRKFPAIVNCTAIHWFHEWPQQALESVSLRFLQNTEGIEPTVKQSISKFMAFVHTSVNQTSQSYLSNEQRYNYTTPKSFLEFIRLYQSLLHRHRKELKCKTERLENGLLKLHSTSAQVDDLKAKLAAQEVELKQKNEDADKLIQVVGVETDKVSREKAMADEEEQKVAVIMLEVKQKQKDCEEDLAKAEPALTAAQAALNTLNKTNLTELKSFGSPPLAVSNVSAAVMVLMAPRGRVPKDRSWKAAKVTMAKVDGFLDSLINFNKENIHENCLKAIRPYLQDPEFNPEFVATKSYAAAGLCSWVINIVRFYEVFCDVEPKRQALNKATADLTAAQEKLAAIKAKIAHLNENLAKLTARFEKATADKLKCQQEAEVTAVTISLANRLVGGLASENVRWADAVQNFKQQERTLCGDILLITAFISYLGFFTKKYRQSLLDRTWRPYLSQLKTPIPVTPALDPLRMLMDDADVAAWQNEGLPADRMSVENATILINCERWPLMVDPQLQGIKWIKNKYGEDLRVTQIGQKGYLQIIEQALEAGAVVLIENLEESIDPVLGPLLGREVIKKGRFIKIGDKECEYNPKFRLILHTKLANPHYQPELQAQATLINFTVTRDGLEDQLLAAVVSMERPDLEQLKSDLTKQQNGFKITLKTLEDSLLSRLSSASGNFLGETVLVENLEITKQTAAEVEKKVQEAKVTEVKINEAREHYRPAAARASLLYFIMNDLSKIHPMYQFSLKAFSIVFQKAVERAAPDESLRERVANLIDSITFSVYQYTIRGLFECDKLTYLAQLTFQILLMNREVNAVELDFLLRSPVQTGTASPVEFLSHQAWGAVKVLSSMEEFSNLDRDIEGSAKSWKKFVESECPEKEKLPQEWKNKTALQRLCMLRAMRPDRMTYALRDFVEEKLGSKYVVGRALDFATSFEESGPATPMFFILSPGVDPLKDVESQGRKLGYTFNNQNFHNVSLGQGQEVVAEAALDLAAKKGHWVILQNIHLVAKWLSTLEKKLEEHSENSHPEFRVFMSAEPAPSPEGHIIPQGILENSIKITNEPPTGMHANLHKALDNFTQDTLEMCSRETEFKSILFALCYFHAVVAERRKFGPQGWNRSYPFNTGDLTISVNVLYNFLEANAKVPYDDLRYLFGEIMYGGHITDDWDRRLCRTYLGEFIRPEMLEGELSLAPGFPLPGNMDYNGYHQYIDAELPPESPYLYGLHPNAEIGFLTQTSEKLFRTVLELQPRDSQARDGAGATREEKVKALLEEILERVTDEFNIPELMAKVEERTPYIVVAFQECGRMNILTREIQRSLRELELGLKGELTMTSHMENLQNALYFDMVPESWARRAYPSTAGLAAWFPDLLNRIKELEAWTGDFTMPSTVWLTGFFNPQSFLTAIMQSTARKNEWPLDQMALQCDMTKKNREEFRSPPREGAYIHGLFMEGACWDTQAGIITEAKLKDLTPPMPVMFIKAIPADKQDCRSVYSCPVYKTSQRGPTYVWTFNLKTKENPSKWVLAGVALLLQI', 4486, 'Q9NYC9; A2VCQ8; O15064; O95494; Q9NQ28;', 'KD00497', 'Homo sapiens (Human)', 'DNAH9', '#Dynein heavy chain 9; axonemal#Axonemal beta dynein heavy chain 9#Ciliary dynein heavy chain 9', '-', 'ENSG00000007174', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(498, 'Q12824', 'SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1', 'k', 44141, 'Core component of the BAF (hSWI/SNF) complex. This ATP- dependent chromatin-remodeling complex plays important roles in cell proliferation and differentiation; in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable; altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling would be due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures; termed altosomes; each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. Belongs to the neural progenitors- specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons; npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A; are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. {ECO:0000250; ECO:0000269|PubMed:10078207; ECO:0000269|PubMed:12226744; ECO:0000269|PubMed:14604992; ECO:0000269|PubMed:16267391; ECO:0000269|PubMed:16314535; ECO:0000269|PubMed:9448295}.', 'MMMMALSKTFGQKPVKFQLEDDGEFYMIGSEVGNYLRMFRGSLYKRYPSLWRRLATVEERKKIVASSHGKKTKPNTKDHGYTTLATSVTLLKASEVEEILDGNDEKYKAVSISTEPPTYLREQKAKRNSQWVPTLPNSSHHLDAVPCSTTINRNRMGRDKKRTFPLCFDDHDPAVIHENASQPEVLVPIRLDMEIDGQKLRDAFTWNMNEKLMTPEMFSEILCDDLDLNPLTFVPAIASAIRQQIESYPTDSILEDQSDQRVIIKLNIHVGNISLVDQFEWDMSEKENSPEKFALKLCSELGLGGEFVTTIAYSIRGQLSWHQKTYAFSENPLPTVEIAIRNTGDADQWCPLLETLTDAEMEKKIRDQDRNTRRMRRLANTAPAW', 385, 'Q12824; O75784; O95474; Q17S11; Q38GA1; Q76N08; Q9UBH2;', 'KD00498', 'Homo sapiens (Human)', 'SMARCB1', '#SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1#BRG1-associated factor 47#BAF47#Integrase interactor 1 protein#SNF5 homolog#hSNF5', '-', 'ENSG00000099956', '-'),
(499, 'Q15013', 'MAD2L1-binding protein', 'k', 31052, 'May function to silence the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 after it has become dissociated from the MAD2L1-CDC20 complex. {ECO:0000269|PubMed:18022368}.', 'MAAPEAEVLSSAAVPDLEWYEKSEETHASQIELLETSSTQEPLNASEAFCPRDCMVPVVFPGPVSQEGCCQFTCELLKHIMYQRQQLPLPYEQLKHFYRKPSPQAEEMLKKKPRATTEVSSRKCQQALAELESVLSHLEDFFARTLVPRVLILLGGNALSPKEFYELDLSLLAPYSVDQSLSTAACLRRLFRAIFMADAFSELQAPPLMGTVVMAQGHRNCGEDWFRPKLNYRVPSRGHKLTVTLSCGRPSIRTTAWEDYIWFQAPVTFKGFRE', 274, 'Q15013; B4DLV3; E9PAT7; Q6IBB1;', 'KD00499', 'Homo sapiens (Human)', 'MAD2L1BP', '#MAD2L1-binding protein#Caught by MAD2 protein', '-', 'ENSG00000124688', '-'),
(500, 'Q69Z23', 'Dynein heavy chain 17; axonemal', 'GO:0003777', 511603, 'Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). {ECO:0000250}.', 'MPDLRIDYLETVSSVLLKFKADKWGKLIGAEENMALLTEFFDKIDNPVLVLTLNAAGMIIPCLGFPESLKSKGVYFIKMKPENITKDNYKTHLIYGDISPTTVDQLIAVVEEVLYSLLNQSENMDGWPRVVSEDIVKQVHRLKNEMFVMGGKIKGKTLLPIPEHLGSLDGTLDSMERIPSSMDNSLLHSIETIIIDWSHQIRDVLSKDSAQALLDGLHPLPRVEFEFWDARLMNLQCIHEQLNRPKVNKIVEILEKAKSCYWPALQNVYMNVTQGLKEANGIVLYLKPLRILLEEMEQADFTMLPSFIVKVLSTICFIWATSEHYNTPSRVIVILREFCNQIIEMTRTYLSPDEVLKGLQGEIEEVLGNISLSVSVLKGLFQAYDFCCANMKLFFKDRPPVPWEFPSSLAFSRMNSFFHRVQTIEDLYKTAIEFLKLEKIELGGVWGNILGNLVTQIYDEVFELVKVFAECKYDPLDPGDSSFDDDYSDFETKIQDLDRRLATIFCQAFDDCNCMESSAKLLYMCGGLLERPLILVEVVPRYSVMLEMFNTELDNAKLMYDAQMAASADGQIPPIHKNMSPVSGQLKWSLELQERLEVSMKYLKHIEHPVMSSMEAKLIYDKYDEMMGLLQSCRMKKYQQWVEGVDQDCHFNLGQPLIQRDPFTSLIQVNFSKALVAVLREVKYLNFQQQKEIPESAEKLFSENETFRKFVGNLELIVGWYNEIKTTVKDVEFPLIKSELEAIDVKLLSAETTLFWNGENVMEYIQEMREMLYNLQNRIQKAKQNVEGITQAMQEWSANPLFERKDNKKEALLDLDGRVANLNKRYAAVKEAGVRIQAMVVENAELFRADTTSQSWKDYVNYIDTVVLDEFDRFIRKSLNYLMDNMTMDESIAPLFEIRMELDKDGLTYNPSLEMGDEAGFLSLIEGLINDLYNVARLIPRLAKGRLNYKSDLEDITDLIEMREEVSSLVIGAMKVAEEYQDSFERYSYLWVDDLQEFMKNFLIFGHAPTPEELDTKTDDTIPKTPPTLAQFQQQIDSYEKLYEEVSSCENTKVFHGWLQCDCRPFKQTLLNTIKRWSFLFKRYLNNHVINSLADLESFMNITRTALKKPLKEGDYDGLVEVMGHLMKVKERQVATDSMFEPLKQTIELLKSYGEEMPEEIYLKLQELPEQWTNTKKLAIQVKQNVAPLQANEVNILRRKCQQFELKQHEFREKFRRDAPFSFSDPEPYKSLNKIYLLYGVMEALCKSASLFEVTVPDYKQLKACHREVRLLKELWDMIVMVNTSIDDWKTTKWKDINVEQMDIDCKKFAKDVRSLDKEMKPWDAFVGLDNTVKNMITSLRAVSELQNPAIRDRHWQQLMQATQVKFEMSEETTLADLLQLNLHKYEDEVRNIVDKAVKESGMEKVLKTLDITWTTMEFEHELHPRTGTMMLKSDEVLVETLEDNQVQLQNLMMSKYLSHFLKEVTSWQQKLSTADSVISIWFEVQRTWSHLESIFIGSEDIRAQLPEDSKRFDAIDQEFKALMEDAVKTPNVVEATNKPDLYNKLENLKMSLAVCEKALAEYLETKRLAFPRFYFVSSADLLDILSNGNDPVEVSRHLSKLFDSLCKLKFRLDASGKPLKFGLGMYSKEDEFVDFDKECDLSGQVEVWLNRVLDRMRATLRHEIPEAVVTYEEKPREQWIFDYPAQIWWTTEVGLAFARLEEGYENAIKDYNKKQISQLNALITLLIGNLTAGDRMKIMTICTIDVHARDVVAKMITVESSQAFTWQSQLRHRWDEEKKHCFANICDAQIKYSYEYLGNTPRLVITPLTDRCYITLTQSLHLIMGGAPAGPAGTGKTETTKDLGRALGTMVYVFNCSEQMDYKSCGNIYKGLAQTGAWGCFDEFNRISVEVLSVIAVQVKCVQDAIRAKKKKFNFLGEIISLVPTVGIFITMNPGYAGRTELPENLKALFRPCAMVVPDFELICEIMLVAEGFLDARLLARKFITLYTLCKELLSKQDHYDWGLRAIKSVLVVAGSLKRGDPTRAEDQVLMRALRDFNIPKIVTDDLPVFMGLIGDLFPALDVPRKRDLNFEKIIKQSIVELKLQAEDSFVLKVVQLEELLQVRHSVFVIGNAGSGKSQVLKSLNKTYQNLKRKPVAVDLDPKAVTCDELFGIINPATREWKDGLFSTIMRDLANLTHEGPKWIVLDGDIDPMWIESLNTVMDDNKVLTLASNERIPLNRTMRLVFEISHLRTATPATVSRAGILYINPADLGWNPVVSSWIERRKVQSEKANLIILFDKYLPTCLDKLRIGFKRITPVPEITVIQTILYLLECLLTEKNAPPDSPKELYELYFVFACFWAFGGAMFQDQLIDYRVEFSKWWINEFKTIKLPSQGTIFDYYIDPETKKFLPWTDKVPNFELDPDIPLQASLVHTTETIRIRYFIDLLMEKAWPVMLVGNAGTGKSVLMGDKLENLSTDDYLVQAVPFNFYTTSAMLQGVLEKPLEKKSGRNYGPPGTKKLIYFIDDMNMPEVDKYGTVAPHTLIRQHMDHRHWYDRQKLTLKDVHNCQYVACMNPTSGSFTIDPRLQRHFCVFAVSFPGQEALTSIYNTILAQHLSFRSAPLVIQRLSSHLVTAALALHQKVSATFLPTAIKFHYIFNLRDLSNIFQGILFSTAEILKTPLDLVRLWLHEAERVYGDKMVDEKDQETLHRVTIASVKKFFDDLGEENLFAKPNIFCHFTQGIGDPKYFPVTDVAQLNKLLKDVLDSYNEVNAVMNLVLFEDAVAHICKINRILESPRGNALLVGVGGSGKQSLSRLAAYISALDVFQITLKKGYAIPDLKMDLATQYIKSAVKNVPSVFLMTDSQVAEEQFLVLINDLLASGEIPGLFGDEDLENIISSMRPQVKSLGIADTREACWKFFIEKVRRQLKVILCFSPVGSVLRVRARKFPAVVNCTAINWFHEWPEDALVSVSARFLEETEGIEPEVKTSISLFMAYVHTTVNEMSKIYLTIERRYNYTTPKTFLEQIKLYQNLLAKKRMELVAKIERLENGLMKLQSTASQVDDLKAKLAVQETELKQKNENADKLIQVVGVETEKVSKEKAIADEEEMKVEVINKNVTEKQKACETDLAKAEPALLAAQEALDTLNKNNLTELKSFGSPPDAVVNVTAAVMILTAPGGKIPKDKSWKAAKIMMGKVDTFLDSLKKFDKEHIPEACLKAFKPYQGNPTFDPEFIRSKSTAAAGLCSWCINIVRFYEVYCDVAPKRQALEEANAELAEAQEKLSRIKNKIAELNANLSNLTSAFEKATAEKIKCQQEADATNRVISLANRLVGGLASENVRWAESVENFKSQGVTLCGDVLLISAFVSYVGYFTKKYRNELMEKFWIPYINKLKVPIPITEGLDPLTLLTDDADVATWNNQGLPSDRMSTENATILCNTERWPLIVDAQLQGIKWIKNKYGSDLQAIRLGQKSYLDIIEQAISAGDTLLIENIGETVDPVLDPLLGRNTIKKGRFIKIGDKEVEYHPSFRLILHTKYFNPHYKPEMQAQCTLINFLVTRDGLEDQLLAAVVAKERPDLEQLKANLTKSQNEFKIVLKELEDSLLARLSAASGNFLGDTALVENLETTKHTANEIEEKVQEAKITEVKINEARENYRPAAERASLLYFILNDLNKINPIYQFSLKAFNVVFEKAIQKTAPADEVKQRVINLTDEITYSVYMYTARGLFERDKLIFLAQVTFQVLSMKKELNPVELDFLLRFPFKAGVVSPVDFLQHQSWGGIKALSEMDEFKNLDSDIEGSAKRWKKLVESEAPEKEIFPKEWKNKTALQKLCMVRCMRPDRMTYAVKNFVEEKMGSKFVEGRSVEFSKSYKESSPSTPIFFILSPGVDPLKDVEALGKKLGFTIDNGKLHNVSLGQGQEVVAENALDVAAEKGHWVILQVRGSLPQNIHLVARWLGILDKKVERYSSGSHEDYRVFISAEPAPTAETHIIPQGILENAIKITNEPPTGMYANLHKALDLFTQDTLEMCTKEIEFKCILFALCYFHAVVAERRKFGAQGWNRSYPFNNGDLTISINVLYNYLEANSKVPWDDLRYLFGEIMYGGHITDDWDRRLCRTYLAEYIRVEMLEGEVLLAPGFQIPPNLDYKGYHEYIDENLPPESPYLYGLHPNAEIGFLTVTSEKLFRTVLEMQPKETDSGAGTGVSREEKVGAVPVPEGSLGSEGSLGTIGLPGTGFQVKAVLDDILEKIPETFNMAEIMAKAAEKTPYVVVAFQECERMNILTNEMRRSLKELNLGLKGELTITTDMEDLSTALFYDTVPDTWVARAYPSMMGLAAWYADLLQRIRELESWTTDFALPTTVWLAGFFNPQSFLTAIMQSMARKNEWPLDKMCLSVEVTKKNREDMTAPPREGSYVYGLFMEGARWDTQTGVIAEARLKDLTPVMPVIFIKAIPVDRMETKNIYECPVYKTRIRGPTYVWTFNLKTKEKAAKWILAAVALLLQV', 4481, 'Q69Z23; O08820;', 'KD00500', 'Mus musculus (Mouse)', 'Dnah17', '#Dynein heavy chain 17; axonemal#Axonemal beta dynein heavy chain 17#Ciliary dynein heavy chain 17', '-', '-', '-'),
(501, 'O60282', 'Kinesin heavy chain isoform 5C', 'GO:0003777', 109495, 'Mediates dendritic trafficking of mRNAs (By similarity). Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. {ECO:0000250}.', 'MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGDETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKTLKNVIQHLEMELNRWRNGEAVPEDEQISAKDQKNLEPCDNTPIIDNIAPVVAGISTEEKEKYDEEISSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEMKKALEQQMESHREAHQKQLSRLRDEIEEKQKIIDEIRDLNQKLQLEQEKLSSDYNKLKIEDQEREMKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDNDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAIRGGGGSSSNSTHYQK', 957, 'O60282; O95079; Q2YDC5;', 'KD00501', 'Homo sapiens (Human)', 'KIF5C', '#Kinesin heavy chain isoform 5C#Kinesin heavy chain neuron-specific 2', '-', 'ENSG00000168280', '-'),
(502, 'Q04087', 'Monopolin complex subunit LRS4', 'GO:0033551===k', 39354, 'Component of the monopolin complex which promotes monoorientation during meiosis I; required for chromosome segregation during meiosis. Involved in rDNA silencing. {ECO:0000269|PubMed:10082585; ECO:0000269|PubMed:12586695; ECO:0000269|PubMed:12689592}.', 'MTTLLQLLSNYYKAKLDSERIYNEYVQSQYEFASLDKLNNNKGDPKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQKALYQSKLSSKDAFIDDLKLKLKVEQISVDKHNKERTPSTGRDEQQRNSKAAHTSKPTIHLLSPIVNRDKPNNQTNDRGGNDPDSPTSQRRSRGLRSLLSSGKNTIFDSISKNLDDEINENAHIRNDTTSSKIAGKSPSRLSALQKSPELRKERNNMILKEHILRSKDDQNITSSRKLDNIELSSIGDSTAMTSRSSTVNANDILGNEENDGITKLKRVNKLTSSPVKRDCSTNKKRKLTKQRIATLPNSDEELSNNLNVDEFV', 347, 'Q04087; D6VT66;', 'KD00502', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'LRS4', '#Monopolin complex subunit LRS4#Loss of rDNA silencing protein 4', '-', '-', '852049'),
(503, 'Q8WYP5', 'Protein ELYS', 'GO:0000777===k', 252498, 'Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. {ECO:0000269|PubMed:17098863; ECO:0000269|PubMed:17235358}.', 'MRDLRAQVTSGLLPFPEVTLQALGEDEITLESVLRGKFAAGKNGLACLACGPQLEVVNSITGERLSAYRFSGVNEQPPVVLAVKEFSWQKRTGLLIGLEETEGSVLCLYDLGISKVVKAVVLPGRVTAIEPIINHGGASASTQHLHPSLRWLFGVAAVVTDVGQILLVDLCLDDLSCNQNEVEASDLEVLTGIPAEVPHIRESVMRQGRHLCFQLVSPTGTAVSTLSYISRTNQLAVGFSDGYLALWNMKSMKREYYIQLESGQVPVYAVTFQEPENDPRNCCYLWAVQSTQDSEGDVLSLHLLQLAFGNRKCLASGQILYEGLEYCEERYTLDLTGGMFPLRGQTSNTKLLGCQSIEKFRSHGDREEGVNEALSPDTSVSVFTWQVNIYGQGKPSVYLGLFDINRWYHAQMPDSLRSGEYLHNCSYFALWSLESVVSRTSPHGILDILVHERSLNRGVPPSYPPPEQFFNPSTYNFDATCLLNSGVVHLTCTGFQKETLTFLKKSGPSLNELIPDGYNRCLVAGLLSPRFVDVQPSSLSQEEQLEAILSAAIQTSSLGLLTGYIRRWITEEQPNSATNLRFVLEWTWNKVVLTKEEFDRLCVPLFDGSCHFMDPQTIQSIQQCYLLLSNLNIVLSCFASEAREITERGLIDLSNKFVVSHLICQYAQVVLWFSHSGLLPEGIDDSVQLSRLCYNYPVIQNYYTSRRQKFERLSRGKWNPDCLMIDGLVSQLGERIEKLWKRDEGGTGKYPPASLHAVLDMYLLDGVTEAAKHSITIYLLLDIMYSFPNKTDTPIESFPTVFAISWGQVKLIQGFWLIDHNDYESGLDLLFHPATAKPLSWQHSKIIQAFMSQGEHRQALRYIQTMKPTVSSGNDVILHLTVLLFNRCMVEAWNFLRQHCNRLNIEELLKHMYEVCQEMGLMEDLLKLPFTDTEQECLVKFLQSSASVQNHEFLLVHHLQRANYVPALKLNQTLKINVMNDRDPRLRERSLARNSILDQYGKILPRVHRKLAIERAKPYHLSTSSVFRLVSRPKPLSAVPKQVVTGTVLTRSVFINNVLSKIGEVWASKEPINSTTPFNSSKIEEPSPIVYSLPAPELPEAFFGTPISKASQKISRLLDLVVQPVPRPSQCSEFIQQSSMKSPLYLVSRSLPSSSQLKGSPQAISRASELHLLETPLVVKKAKSLAMSVTTSGFSEFTPQSILRSTLRSTPLASPSPSPGRSPQRLKETRISFVEEDVHPKWIPGAADDSKLEVFTTPKKCAVPVETEWLKSKDRTTSFFLNSPEKEHQEMDEGSQSLEKLDVSKGNSSVSITSDETTLEYQDAPSPEDLEETVFTASKPKSSSTALTTNVTEQTEKDGDKDVFASEVTPSDLQKQMGNLEDAETKDLLVAAEAFSELNHLSPVQGTEASLCAPSVYEGKIFTQKSKVPVLDEGLTSVETYTPAIRANDNKSMADVLGDGGNSSLTISEGPIVSERRLNQEVALNLKEDHEVEVGVLKESVDLPEEKLPISDSPPDTQEIHVIEQEKLEAQDSGEEARNLSFNELYPSGTLKLQYNFDTIDQQFCDLADNKDTAECDIAEVDGELFVAQSNFTLILEGEEGEVEPGDFASSDVLPKAANTATEEKLVCSGENDNHGQIANLPSAVTSDQKSQKVDTLPYVPEPIKVAIAENLLDVIKDTRSKEITSDTMEQSIHETIPLVSQNIMCPTKLVKSAFKTAQETSTMTMNVSQVDDVVSSKTRTRGQRIQNVNVKSAQQEASADVATPKMPGQSVRKKTRKAKEISEASENIYSDVRGLSQNQQIPQNSVTPRRGRRKKEVNQDILENTSSVEQELQITTGRESKRLKSSQLLEPAVEETTKKEVKVSSVTKRTPRRIKRSVENQESVEIINDLKVSTVTSPSRMIRKLRSTNLDASENTGNKQDDKSSDKQLRIKHVRRVRGREVSPSDVREDSNLESSQLTVQAEFDMSAIPRKRGRPRKINPSEDVGSKAVKEERSPKKKEAPSIRRRSTRNTPAKSENVDVGKPALGKSILVPNEELSMVMSSKKKLTKKTESQSQKRSLHSVSEERTDEMTHKETNEQEERLLATASFTKSSRSSRTRSSKAILLPDLSEPNNEPLFSPASEVPRKAKAKKIEVPAQLKELVSDLSSQFVISPPALRSRQKNTSNKNKLEDELKDDAQSVETLGKPKAKRIRTSKTKQASKNTEKESAWSPPPIEIRLISPLASPADGVKSKPRKTTEVTGTGLGRNRKKLSSYPKQILRRKML', 2266, 'Q8WYP5; A6NGM0; A8MSG9; A8MZ86; Q7Z4E3; Q8IZA4; Q96EH9; Q9Y4Q6;', 'KD00503', 'Homo sapiens (Human)', 'AHCTF1', '#Protein ELYS#Embryonic large molecule derived from yolk sac#Protein MEL-28#Putative AT-hook-containing transcription factor 1', '-', 'ENSG00000153207', '-'),
(504, 'Q5EE04', 'Nucleoprotein TPR', 'GO:0000776===GO:0005868', 226054, 'Component of the nuclear pore complex (NPC); a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs; plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase; and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters. May play a limited role in the regulation of nuclear protein export. May be involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally; may act as a spatial regulator of the spindle-assembly checkpoint (SAC) response (By similarity). {ECO:0000250}.', 'QEQHSQLEAAKTQVEKDMGEKISNLERELENANDLLCSTKRKGVMLSEEELTAMSPTAAAVAKVVKPGMKLTELYNAYVETQDKLLMEKQENKRITKYLDEIVKEVEAKSPILKRQREEYERMQKTVASLSAKLEQAMREIQRMQDETDKANKCSSVLERENQRLELQIKDLSQQIRVLLMELEEARGNFVQRDDVSSANISSSSEVITQHLVTYRNIEELQQQNQRLLVALRELGEAKEREEQESTSSRVSELEKELENALSELQQLREARSHQMTLVESIVRQRDMYRILLSQTTGVVLPAQDETALTSTPRKSPGVSLDGSTSTPAAVVVSDSTEAAEARAALKQLQEVFENYRKEKAENDRMLNEQHDKLQEQVTELRSQNTKISTQLEFASKRYEMLQDNVEGYRREITALQEKTQKLSATTQKQEQIINTLTHDLRAANEKLAVAEVRAENLKREKELLKMSEVRLTQERESLVAEQRGQNLLLTNLQTIQVTLERSETEIKQRYNNQIEKLEQELAQTKKKLEHEIEQRHLLGKNQDVQVLELKKQYEMELNLHNNTKELLKNSHKEISVLKQQLNSFELQLASRSSQQAANRDKDVNIEDVEEIKTKLRQSEELVNDLKERLKTATSNVEQYRSVVLNLEESLNKEKQVTEEVRKTIEVRLKESSEYQSQLEKKMMESEKEKQELRDEKHKTVEQMEQQVTQLRQSLSSLQAEVQQALQRATTSASNEQKAKQDCQEQARIAAEAQNKYERELMLHAADVEALQAAKKQLTSASAIRHKCEETAQKAGSQLLESRASWEERERMLKEEVSQIQSRCKDLEKQNGLLHEQIESLSKKMVTSVQEGALNMSFGEEGKSQEQVMEILRFVRREKEIAEARFEVAQVECLRYRQRIEHMERELHELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVLIESNKILREENEKQEQELQQLQAKIRKLESNILPLQESNAELSEKSGMLQAEKKLLEEDVRRWRARTQHLLSQQKDTDAEEYKKLLSEREVNTKRIQQLTEETGKLKTEVARTNASLNTCQSQLQSVKDDLTKIKAEKEKLQKELDAKILDIQEKIKTITQVKKIGRRYKTQYEELKVTHDKMVAEASSAKADQLQEQASQKEVQELKDSLQRSEAKVTTMQTTVDNMQKTLDDKDNEIKEHQEQISRMQAELSHLHKDLQDKTAQEEQMRQQINEKEEKTKKTLLVVRQKLAQNNGAKEQLTRENEDLKQKNANLEQQKEELEVRMSALRSQYDGRISRLERELREQQERHHEQRDEPQETTRIPQQRQITLQPTTAAGERGSANTSEPPTANIKPTPSKVTTAAVPVNKSTPRASIRPMVTPAAVSTPTSTPTATVMPTTQVDQQEVQSEGQMEHVPVFGSASGSVRSTSPNVQSSLPQPILTLQQQTQTTAFVQPTQQSHATIESPTQETPVEIVQSSPVERPTTSSTFGTYSATPSSSIPKRPREEEEDSTIETPEQIADDTDQQRTKKRKEEDIEEKTETEAVINTEDALHILTQCSNMEFPLEEEIVESPIQTSQVIESQAPEQLQNVQSTQDSLQDTPPKKTHNLVIVISDEENEDEQEGYEEEEQEDEEEDEDDAGIGEGDDSNEETGSADGNEDYEGDDAEEADGTDPDTETEDSMTAGEGNQRAADSQNIGDSGVVTAESTFSQETREQPSSASDRQGPRPPQSPRRQAHPPRLTILAPPQELGPPPAQRIPVARRQSVGRGLQLTPGVGGMQHFFDEEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQASSSHSDLGQLASQGGLGMYDTPLFLAHEEESGGRSVPTTPLQVAAPVSVFAENPAADTSDHASQSVPMVTTSTGNVPTSVDSGAADEGDEVFVEAESEGIGAESTLEMDTQQEEPVQPSEADLPSTSQDPPSSSIADTSSSKPKPRRVWLQPQPGGRPFKRSRGGSDFRGRGGINRSNI', 1997, 'Q5EE04; P79992;', 'KD00504', 'Xenopus laevis (African clawed frog)', 'tpr', '#Nucleoprotein TPR#NPC-associated intranuclear protein#Translocated promoter region and nuclear basket protein', '-', '-', '-'),
(505, 'A1A5K2', 'CLIP-associating protein 1-B', 'GO:0000777===GO:0005828===SCL', 161045, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules during anaphase. Plays a crucial role in chromatin-induced microtubule formation. May also act at microtubule minus ends. May be involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). {ECO:0000269|PubMed:16390996}.', 'MEQGMDYWLGQIQQKDVGKRLQVGPDLIEYLLDRQKSIDLEQDQTLLDRMVDGLATSWVNSSNYKVALLGMDILSALVTRLQDRFRTQIGTVLPSLMDRLGDAKDSVRDQDQNLLIKIMEQASNPQYMWERMFSGFKHKNFRTREGVCLCLIATLNVYGANSLTLSKIVPHICNLLGDPNSQVRDAAINCLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGTMILSTTDKNFDDEDSVDGNRPSSASSSASSKAPQTARRGVSLGTGRRPGTSSAAPKTGGTAKEGAGALDEEDFIRAFEDAPTVQIYSSRDLEESLNKIREILSDDKHDWEQRISALKKIRSLLLAGAAEYDNFFQQLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAVMPTVFNLVPNSTKIMATSGVVTIRLIIRHTHVPRLIPIITSNCTSKSVAVRRRCYEFLDLLLQEWQTHSLERHVSVLAETIKKGIHDADSEARIVARKCYWGFHGHFSKEAEQLFHALESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTVSRATSKSTTGSLQRSRSDIDVNAAATSKTKAASGASTAPFSSVAALPPGSYASLGRIRTRRQSSGSTTSTASTPADTRGRSRAKVVSQSQPGSRSSSPGKLLGSSYGGIATGPQRVPQMPSEKRSKIPRSQGCSRETSPSRTVLDRFGISQPGRIPSAMRVLSSSTDLEAAVADALLLGDSRNKMKPVRRRYEPYGMYSDDDANSDASSACSERSYSSKNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLVGLQNLLKSQRLLSRVELKRLCEIFTRMFADPHSKRVFSMFLETLVDFVIIHKDDLQDWLFILLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQVVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNSSMGSPSNTIGRTPSRHSSSRASPLTSPTNCSHGGLSPSMLDYDTENLNSDEIYSSLRGVTEAIEKFSFRSQVDLNEPVRRDGKKESEMGSCDAGMASPASDLRGGTDMVEGGRMALDNKTSLLNTQPPRAFTGPRGREYNPYAYSDSINSYDKTALKEAVFDDDMDQLRDVPIDHSDLVADLLKELSNHNERVEERKGALCELLKITREDNLAVWEEHFKTILLLLLETLGDKDHAIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLAGSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERISKESLHQILPDIIPGLLQGYDNTESSVRKASVFCLVAVYSVIGEELKPYLAQLTGSKMKLLNLYIKRAQTTNSNSSSSSDVSTHS', 1456, 'A1A5K2;', 'KD00505', 'Xenopus laevis (African clawed frog)', 'clasp1b', '#CLIP-associating protein 1-B {ECO:0000250|UniProtKB:Q7Z460}#Cytoplasmic linker-associated protein 1-B {ECO:0000312|Xenbase:XB-GENE-6049836}#Protein Orbit homolog#Xorbit#Xorbit/CLASP', '-', '-', '445862'),
(506, 'P70096', 'Kinesin-like protein KIF2C', 'GO:0000777===GO:0003777', 80918, 'In complex with KIF18B; constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (By similarity). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. {ECO:0000250; ECO:0000269|PubMed:14960279}.', 'MESLPARLFPGLSIKIQRSNGLIHSANISTVNVEKSCVSVEWIEGGNTKGKEIDFDDVAAINPELLQLLPLHPKDNLPLQENVTVPKQKRRSVNSKIPAPKEGLRSRSTRMSTVPEVRIATQENEMEVELPVATNSRKQFSVATGLPRPSCPAMTELPLSMVSEEAEEQVHPTRSTSSANPARRKSCIVKEMEKMKNKREEKRAQNSEIRIKRAQEYDSSFPNWEFARMIKEFRVTIECHPLTLTDPTEEHRICVCVRKRPLNKQELAKKEIDVISVPSKCLLFVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNTSKGIYAMASRDVFLLKSQPRYRNLNLEVYVTFFEIYNGKVFDLLNKKAKLRVLEDSKQQVQVVGLQEYLVNCADDVIKMLNMGSACRTSGQTFANSNSSRSHACFQILLRAKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKELSPHSGLSGEQPIQMETEEMEASSNGTSLAVNFKEEEELSSQMSSFNEAMSQIRELEERAMEELREIIQQGPGWLELSEMTDQPDYDLETFVNKAESALTQQTKHFSALREVIKALRVAMQLEEQASKQMNSKKRHQ', 718, 'P70096;', 'KD00506', 'Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)', 'KIF2C', '#Kinesin-like protein KIF2C#Kinesin-like protein 6#Mitotic centromere-associated kinesin#MCAK', '-', '-', '100689309'),
(507, 'Q5EE01', 'Centromere protein W', 'GO:0000776===GO:0000777===GO:0051382===k', 10061, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPW has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000250; ECO:0000269|PubMed:19070575; ECO:0000269|PubMed:19533040; ECO:0000269|PubMed:21695110; ECO:0000269|PubMed:22002061; ECO:0000269|PubMed:22304917}.', 'MALSTIVSQRKQIKRKAPRGFLKRVFKRKKPQLRLEKSGDLLVHLNCLLFVHRLAEESRTNACASKCRVINKEHVLAAAKVILKKSRG', 88, 'Q5EE01; A6NIR0; A6NJC2;', 'KD00507', 'Homo sapiens (Human)', 'CENPW', '#Centromere protein W#CENP-W#Cancer-up-regulated gene 2 protein', '-', 'ENSG00000203760', '-'),
(508, 'Q6C3V4', 'Probable kinetochore protein NUF2', 'GO:0000777', 52702, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSHMAYTPKKQVRTRNTHAAFPTLPIDEIVQCLPGLDCMVTEEELLRPTSKFVQSMYAQIATSLLGINRESMAPALAACAAGTEHPETQEDARMLFALQKPLYDLFVASGVTDYNISDILKPSPERLRVQLSAIINYARFREIREKWYEKMSEELNEEEEARTMRLKNQEEKLRRKVELIALIGDTPDQDLVEQHRINDSRKSELKRLHDQNLQLNDERERNKAELRVVVNRLRHKHQLMESLQEEVARLNSYVVDNPKNLQEEVVELSKRVKERETVRRMLGERVQKLDLSVDSFKDFQVDVSSCLSAFQKLSDEQEAHSKAVRKITTQKELLEHVGINSRQAEGRRDVLQQEIEAAESKIARIQQDMSESDRQTSRRMEELRRQIGTLDAERALVVQQNNTAQKRLAELENDMATERDRYEAQLKMAREEAEKLQTQFREYFVEVGRRLN', 452, 'Q6C3V4;', 'KD00508', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '2911880'),
(509, 'Q9U2C1', 'SMC-3; isoform a', 'k', 139864, '', 'MKIKEVRITGFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVEITFDNSEKRLMAFENSEVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKINELATSPDAYKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRSQFSSVDDRDKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAYVAQQTAAREEKAIRDKIGNTEQDISAANDQLRRIVARPVYNGITGVRKVIEEFKHDNRNGQHDDVINGYYGTVIELAEVPDMFRTAVEVIAQNRLFYHVVETDRIATKILRKFNEMQLPGEINFFPMNRVSAPRQRDLSNNSNARPMSDVIDYEVQYDKVFKSITANVIIVRTLDQAARDLRNEGFDVVSVDGDQMSKKGVMTGGFIDKKRSKLELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKTKESLTARVDDISDNERRHKLENANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQKREDSLKKMRLLGALPTDTFSKWQNVKPRELEKKLLECVNELKKYENVNKKALDQYMTASSQKEELTKRMAEQKKSEDSIEELLKVLENRKYEAIDLTFKQVKKNFEQVFKQLVPHGRGKMQMRAREQRDDEEGINSVELYEGISVLVSFVSDDGDSETREMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGVRFRNKVSHIDSVTREQAYDFVEDDTTHG', 1205, 'Q9U2C1;', 'KD00509', 'Caenorhabditis elegans', 'smc-3', '#SMC-3; isoform a {ECO:0000313|EMBL:CAB57898.4}', '-', '-', '176559'),
(510, 'Q8WSZ9', 'SKR-1', 'k', 19331, '', 'VSEAAKEREIKISSSDNEIFLVPRNVIRLSNTINTLLMDLGLDDEEGTNAEPIPVQNVTASILKKVISWCNHHHSDPISTEDSDNREKRTDDIGSWDVEFLKVDQGTLFELILAANYLDIKGLLDVTCKTVANMIKGKSPEEIRRTFNIKNDFTPEEEEQIRKENAWCED', 170, 'Q8WSZ9;', 'KD00510', 'Caenorhabditis elegans', 'skr-1', '#SKR-1 {ECO:0000313|EMBL:AAL34093.1}', '-', '-', '-'),
(511, 'Q86U86', 'Protein polybromo-1', 'GO:0000776===k', 192948, 'Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Acts as a negative regulator of cell proliferation. {ECO:0000269|PubMed:21248752}.', 'MGSKRRRATSPSSSVSGDFDDGHHSVSTPGPSRKRRRLSNLPTVDPIAVCHELYNTIRDYKDEQGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDVNLLTADFQLLFNNAKSYYKPDSPEYKAACKLWDLYLRTRNEFVQKGEADDEDDDEDGQDNQGTVTEGSSPAYLKEILEQLLEAIVVATNPSGRLISELFQKLPSKVQYPDYYAIIKEPIDLKTIAQRIQNGSYKSIHAMAKDIDLLAKNAKTYNEPGSQVFKDANSIKKIFYMKKAEIEHHEMAKSSLRMRTPSNLAAARLTGPSHSKGSLGEERNPTSKYYRNKRAVQGGRLSAITMALQYGSESEEDAALAAARYEEGESEAESITSFMDVSNPFYQLYDTVRSCRNNQGQLIAEPFYHLPSKKKYPDYYQQIKMPISLQQIRTKLKNQEYETLDHLECDLNLMFENAKRYNVPNSAIYKRVLKLQQVMQAKKKELARRDDIEDGDSMISSATSDTGSAKRKSKKNIRKQRMKILFNVVLEAREPGSGRRLCDLFMVKPSKKDYPDYYKIILEPMDLKIIEHNIRNDKYAGEEGMIEDMKLMFRNARHYNEEGSQVYNDAHILEKLLKEKRKELGPLPDDDDMASPKLKLSRKSGISPKKSKYMTPMQQKLNEVYEAVKNYTDKRGRRLSAIFLRLPSRSELPDYYLTIKKPMDMEKIRSHMMANKYQDIDSMVEDFVMMFNNACTYNEPESLIYKDALVLHKVLLETRRDLEGDEDSHVPNVTLLIQELIHNLFVSVMSHQDDEGRCYSDSLAEIPAVDPNFPNKPPLTFDIIRKNVENNRYRRLDLFQEHMFEVLERARRMNRTDSEIYEDAVELQQFFIKIRDELCKNGEILLSPALSYTTKHLHNDVEKERKEKLPKEIEEDKLKREEEKREAEKSEDSSGAAGLSGLHRTYSQDCSFKNSMYHVGDYVYVEPAEANLQPHIVCIERLWEDSAGEKWLYGCWFYRPNETFHLATRKFLEKEVFKSDYYNKVPVSKILGKCVVMFVKEYFKLCPENFRDEDVFVCESRYSAKTKSFKKIKLWTMPISSVRFVPRDVPLPVVRVASVFANADKGDDEKNTDNSEDSRAEDNFNLEKEKEDVPVEMSNGEPGCHYFEQLHYNDMWLKVGDCVFIKSHGLVRPRVGRIEKVWVRDGAAYFYGPIFIHPEETEHEPTKMFYKKEVFLSNLEETCPMTCILGKCAVLSFKDFLSCRPTEIPENDILLCESRYNESDKQMKKFKGLKRFSLSAKVVDDEIYYFRKPIVPQKEPSPLLEKKIQLLEAKFAELEGGDDDIEEMGEEDSEVIEPPSLPQLQTPLASELDLMPYTPPQSTPKSAKGSAKKEGSKRKINMSGYILFSSEMRAVIKAQHPDYSFGELSRLVGTEWRNLETAKKAEYEERAAKVAEQQERERAAQQQQPSASPRAGTPVGALMGVVPPPTPMGMLNQQLTPVAGMMGGYPPGLPPLQGPVDGLVSMGSMQPLHPGGPPPHHLPPGVPGLPGIPPPGVMNQGVAPMVGTPAPGGSPYGQQVGVLGPPGQQAPPPYPGPHPAGPPVIQQPTTPMFVAPPPKTQRLLHSEAYLKYIEGLSAESNSISKWDQTLAARRRDVHLSKEQESRLPSHWLKSKGAHTTMADALWRLRDLMLRDTLNIRQAYNLENV', 1689, 'Q86U86; A1L381; A1L382; A4FUJ7; Q1RMD1; Q1RMD2; Q96MS2; Q9H2T3;Q9H2T4; Q9H2T5; Q9H301; Q9H314;', 'KD00511', 'Homo sapiens (Human)', 'PBRM1', '#Protein polybromo-1#hPB1#BRG1-associated factor 180#BAF180#Polybromo-1D', '-', 'ENSG00000163939', '-'),
(512, 'P36626', 'Meiotic recombination protein rec8', 'GO:0000941===GO:0051455===k', 64011, 'Involved primarily in the early steps of meiotic recombination. Required to ensure reductional chromosome segregation. {ECO:0000269|PubMed:10440376; ECO:0000269|PubMed:16303567}.', 'MFYNQDVLTKEKGGMGVIWLAATLGSKHSLRKLHKKDIMSVDIDEACDFVAFSPEPLALRLSSNLMIGVTRVWAHQYSFFHSQVSTLHLRVRKELDHFTSKPFKNIDIQNEQTNPKQLLLAEDPAFIPEVSLYDAFNLPSVDLHVDMSSFTQPKENPNISVLETLPDSTSYLINTSQNYSLRNNVSSFVYEDSRAFSTEEPLDFEFDENGDIQELTKGTINSDPSLQAASQHSNLGSVQREYNSEEQESRIHMFEIDEDVLPLPVPLQSVMDSEHNENEPRALKRRKVQKLLEPDENIELSTRTLSQWRKNYVERMIALEATKYVRRRGASSAKKKELNKFFDWESFHPLLKPWIEKLKPSNNTPSEIDDVLRNIDTSEVEVGRDVQGELGLNIPWNTSSRSNSAINSKSHSQTGSEHSTPLLDTKYRKRLPHSPSMPSRVEFLPALESSQFHETLNSELSLQLSDDFVLYKNTQEENAHLMLSMEKECANFYEYAKTAIYENNGRITFSSLLPNDLKRPVVAQAFSHLLSLATKSAFLVKQDKPYSEISVSLNLKSTDAI', 561, 'P36626; O60051;', 'KD00512', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rec8', '#Meiotic recombination protein rec8#Cohesin rec8', '-', '-', '2540458'),
(513, 'Q6C061', 'Actin-related protein 4', 'GO:0051382', 47043, 'Chromatin interaction component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Is required for NuA4 complex integrity. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair (By similarity). {ECO:0000250}.', 'MTTTAPAPQVYGGDEVATLVIDTGSSYTRVGYAGEDTPKLVVSTECGLMADEDVEMEDDTSNTTKKLNKYKVGDSANLPLPNMEVLHPLTDGIVADWDAVQNIWEYSLARLNADTKTHPLMLTEPCWNTQANKLKALEIAFESLEVPASYLVKDAVASAFAAGKGNALVLDVGSEVASVTPVIDGLVLYKPARRSQYAGDYLDRQIKKVLVSRGIDLTPRFEIKNKKAVEMGEPPVFTKRELPNVTHSFTDLQVSRILSEFKDSMCQVNDVPLTPEISGEAADRVFEFPTGYSTTFGADRLSTSESLFKPSEYPFDGETVPDTARGLSEMVVDTINASNVDVRAHLANNIVITGGGSLVQGLSDRVSKDVTQALSGLKVRVAAASNQEERRHGAWIGGSVLGSLGSFHQLWVSKQEWQEKGGDYLVEKKRFK', 432, 'Q6C061;', 'KD00513', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'ARP4', '#Actin-related protein 4#Actin-like protein ARP4#Actin-like protein 4', '-', '-', '2909050'),
(514, 'Q8IYS8', 'Biorientation of chromosomes in cell division protein 1-like 2', 'GO:0000777', 18075, 'May play a role in proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000250|UniProtKB:Q96IK1}.', 'MADGGGGGSGGAGPASTRASGGGGPINPASLPPGDPQLIAIIVGQLKSRGLFDSFRRDCKADVDTKPAYQNLSQKADNFVSTHLDKQEWNPPANDNQLHDGLRQSVVQSGRSEAGVDRISSQVVDPKLNHIFRPQIEQIIHEFLVAQKEAAVPALPPEPEGQDPPAPSQDTS', 172, 'Q8IYS8; B3KXU4; Q8WW13;', 'KD00514', 'Homo sapiens (Human)', 'BOD1L2', '#Biorientation of chromosomes in cell division protein 1-like 2 {ECO:0000305}#Biorientation of chromosomes in cell division protein 1 pseudogene {ECO:0000305}#Protein FAM44C {ECO:0000305}', '-', 'ENSG00000228075', '-'),
(515, 'Q62909', 'Kinesin-like protein KIF2C', 'GO:0000777===GO:0003777', 75572, 'In complex with KIF18B; constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. {ECO:0000250}.', 'MIDIDDVAAINPELVQLLPLRPKDSLPLQENVTIPKQKRKSVNSKIPGPKEGLRSRSTRISTVSEVRIPAQENEMEVELPVSTNSRKPFPIHTGHPRPSCSTVTELPLLMISEEAEEQAHSTRSTSSANPGNSVRRKSCIVKEMEKMKNKREEKRAQNSEIRIKRAQEYDNSFPNWEFARMIKEFRVTMDCNPLTVTDPIEEHRICVCVRKRPLNKQELAKKEIDVISVPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNASKGIYAMASRDVFLLKNQPRYRSLNLEVYVTFFEIYNGKVFELLNKKAKLRVLEDSKQQVQVVGLQEYLVTCADDVIKMINMGSACRTSGQTFANSNSSRSHACFQILLRAKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKESIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQAVQMETEEMDASSHGASLTGNEEEELSSQMSSFNEAMTQIRELEERAMEELREIIQQGPSWLELSEMTDQPDYDLETFVNKAESALTQQAKQAKHFSALQEVIKALRLAMQLEEQASKQINSKKRHQ', 671, 'Q62909;', 'KD00515', 'Rattus norvegicus (Rat)', 'Kif2c', '#Kinesin-like protein KIF2C#Kinesin-related protein 2#Mitotic centromere-associated kinesin#MCAK', '-', '-', '171529'),
(516, 'B7ZNG0', 'Kinesin-like protein KIF7', 'GO:0003777', 151624, 'Essential for hedgehog signaling regulation: acts as both a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways; acting downstream of SMO; through both SUFU-dependent and -independent mechanisms. Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes. Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes; promotes the dissociation of SUFU-GLI2 complexes; GLI2 nuclear translocation and Shh signaling activation. Involved in the regulation of epidermal differentiation and chondrocyte development. {ECO:0000269|PubMed:19549984; ECO:0000269|PubMed:19592253; ECO:0000269|PubMed:19666503; ECO:0000269|PubMed:21795282; ECO:0000269|PubMed:23034632; ECO:0000269|PubMed:24952464}.', 'MGLEAQRLPGAEEAPVRVALRVRPLLPKELLHGHQSCLRVEPERGRITLGRDRHFGFHVVLGEDTGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLHEDEQGIIPRAMAEAFKLIDENDLLDCLVHVSYLELYKEEFRDLLEVGTASRDIQLREDDRGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHFNRLSSRSHTVFTVTLEQRGRTPSRLPRPAAGHLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSTLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWHPEAERVPEEQAAGARGPPRHRSETRIIHRGRRVPCPAVGSAAVAAGLGAECARCRARTSAAYSLLRELQAEPGLPGAAARKVRDWLCAVEGERSTLSSASGPDSGIESAPAEDQAAQGTSGRKGDEGTQQLLTLQSQVARLEEENRDFLAALEDAMEQYKLQSDRLREQQEEMVELRLRLELAQPGWGAPGLLQGLPPGSFVPRPHTAPLGGAHTHMLGMMPSTCLPGEEVSSEQQVVSGKEVKAEVLAQADKLRSASSTTSEEEGEEEEEEEEEEEEPPRRTLYLRRNGISNWSQRAGLSPGSPPDRKGPEVCPEEPAAAIPAPQAVGSGKVPVQTRQAPAAMASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELCEGQRQLRELEGREPQDASERSRLQEFRKRVAAAQSQVQVLKEKKQATERLVSLSAQSETRLQELERNVQLMRRQQGQLQRRLREETEQKRRLETEMNKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELRKREVILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQNQQQIRGEIDTLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNVQLLLQQGRDHLGEGLADSKRQYEARIHALEKELGRHMWINQELKQKLSAGSTAGQSQGCERRSLCLENRQCLGNEDGLHPAAPEPLWQSSLLEGVSRVWDESRDLVHAPLPLTWKRSSLCSEQGSSEESRVRETTEPPVGRVLPMGEVGLSWNFGPLPKPRWEPRRTSPGMIDVRKNPL', 1348, 'B7ZNG0; B2RUB1;', 'KD00516', 'Mus musculus (Mouse)', 'Kif7', '#Kinesin-like protein KIF7', '-', '-', '-'),
(517, 'Q9C1M7', 'Dynein heavy chain; cytoplasmic', 'GO:0003777===GO:0031134===GO:0005868', 466252, 'Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.', 'MTDDQVAQALVGYVFNVAKLFLKLGAEQDAFARTHGAKFEEWVGNGNMRTLFLVKDEEGEVQVLEELEGPEAEGPEQSGRLLLIKNRPFVDGSAPMESQVQVLHLPPRAHFDGFKSFVSFGVATMFDAVVSTNSNLEAKQESINSARRKIKDLSLSLQSLQQFIEVPDISATAHPLIKKIIAEGANPRNYTTYISDEQFADSQFLNSLQKIANGWIKSAQNLTKLTRNIEDGSATDEIRFWINLEQSLLALEKQIAIPEVEITLSILTAAKRFHATVTFISDTGLRDRILETQSYNQIMSDFPLADLQTATSFTKLGEAIESISIALKKLKVSTYPLARAVTFVEKISTELDQKLREMLPNLISSDFISFQEDYDHCIKIINQWEALLKEFTSLIRELMRKRSEKFIFMKIDTQTDSLKEVLNTVAAFRKKHDILIHVLKGIGYDTLSEDIQSIYEPVQYQDPLRDNASKWANAEAAYNQRVSLLENKLVDMLKKKLDDCKSSDSMFSIFEKYRPLMKRPRIQGAVREYQHELLHNVKDDLEHIHQQLSLQKWNSELSRLNDIPPVSASIIWSKQLTKKLQNLTSRLGLILGEDWISTSEGSQIFVECSSIMKVLNTDKLFETWVSNVSSQNFLLDEPIFKILITNEEYELHVNFDSVVGSLFKEVRNLMWMGFNVPSNIIKNSRRVRSLYPHAVMVSELLQTFVSAVQSFQERPHTWLLLKDETENIWQLLSAMITDTWDSVPLFEDDASHERAEDIQRDEPSILRLEHSIGELLSKFQQLDGLEKGLSSCLQQLEVFGKLDLQNLEVLINKIQLLVDQATLHGFHNMSGFIDYLNTRIRSYLVSTVSKILEESQLSPKKHYILQQGKKVTISPSIEETKKAWMRDFQKTLEVATNLPKITDKKFDITEGQMENFTDIGTDLSESLIKAFLRIEDACHAIDEHFQKWKKLELLWCLDELTLLERLGSDVEVSYRFLLDFMEERKAIDMVDSEITIAGDTMINNEQVYVRVSAKYDNWQRVLCEKLLENYMDHASEFDTQLVHSRRLLETSIINLGSLSKTTELIAYVDDIKNNLDLMFTRYSLLLNTQKLLQKLRFRIPQNFIHAEQIESDLVSLREICLRKEDLINKNRDAISNKLEAELLKIQEVANSLSQSWSKKKPLSVSIQPSEALSVLNTFEDSIAKVNTERELINRAAKILLVPIKLQNVLSPVIEEVNDYKAVWSSVDGLWNSFNATLSVKWADFESTAVKHRLEALMKKCQDMPPKVLQYKIFQNIAGSIEATLKSMHLLKALKEPAIKPRHWSILFKQLGASHIVSGNIDDQTFTLEDILQLNILLNEVSVKKIVIKARNENVLESSLSQMKARWRATKFDQFVHSSGLVLVKGWDVIFSNCNDDLNMITSMKNSPYFKVFEQEALEWETKLSNFYDIVLSWVEVQRQWMYLFGILAKKTEMKNLLPIEASKFASLTSEYNSLLLKLYGSEIAIDILHVHSTLPTLKRMAESLTKIRKSLNDFLETQRRLFPRFYFVGNEDLLQIIGAGDNFSEFSRHLSKLFSSVSDFIYDESLIQGVYSLEGETLLFANPVRVTPSSKLDQWMNEVDLEIKLTLSTLVKNCLESYRTSGSLKHIIEKYPFQALLLALQCTWTNKIETSMTKDNFGSICSSIDEEMASLAAVIDSYPTVTEKRKVESLIVELVHLKTITETLKNVELEQIDFHWKQTQRFYWDDNSNDPLNSITIEQSCVSFCYGFEYIGVPERLIYTPLLDSCFNAMVLALSEHMGGCPFGPAGTGKTETIKALGQNFGRMVLVFNCDDSFDFQAMSRLLFGITQVGAWGCFDEFNRLEEKILSAVSTQVEAIQLSLVQGKPEIEVLDKKGSLNSNTGIFITMNPGYAGRSELPENLKKMFREFAMMKPDALVIAEVILTILGLENPRVLAEKIVSLFKLLNDKTTSQKHYDFGLRALKSVLRNCLTILRSTTDLDSTQVLLRSLNEMVVPKLISVDEAVYEEAIADFFPGSRIKPSNEQLLSYLASYCESNQLVASDLFIKKCSQFYDIQKTQQAIILAGDAGTGKTSVWKSVINSMKRSGAKENIVYIIDTKTLKKEDLYGKLDPVTFDWKDGIFTHLLRKTLLDTMGNFKNSNIWIVFDSDLDPNYTETLNSVLDDNKVLTLPNGERLKIPPNLHILFEVQDLEHATAATVSRCGMIWFANNTLAAQDILISCLSREVATLQQDADVHDNIIATIQDIFAQFIQGSTLGNVIEATYKADHIMGVDFCRFIETAVTLLSCDIKKNKKQLSRLSQVACVRYMSKRLALVLIWAFVGGSDLETREKFSETICELLGISDIPTGSKFLLDYDVSVATQDWVPVSAEVPKTSLESHEVLIPDLIIPTVDTVRHETLLFDLLNADRPLILCGPPGSGKTMTLYNTLKRSDRFNIIGINFSKDTSVELFLKTLEQHTICTPTSRGIIMQPKAHGKQLVVFCDEINLPMLDEYGSQPVILFLRQLIEKRGFWNVQESKWVFIERIQIVGACNPPGHAGRVSITPRFLRHASIVMVDYPGQIAMEQIYETFFNAIFKLTPKLKGFASDFTKASLQVYYDCKATYTSEAHSHYIYSPRELTRWVRGIHFTISDSGNIDLAYMLELWAHESLRLFSDRLVSSSEKNIFQSILQNAITTHFPNQPLGSLESSQLLFSNWLSLNYSKVVKSEMYTFIKERLKTFAEEELDTELTIYDDMIDNILRIDRILKQVQGHGILVGPNYSGKTTITRFVAWMNGIKVVRPTIHRHFTIENFDEFLKQMLLRCGTESEKICLIIDESNILETSFLERMNTLLANSDVPGLFEADEYEALLSKIGQRISQLGLLLDTEQEMYDWFTSEISKNLHVIFNINDPDNRESTQLITSPALFNRSVINWIGTWSSRSCLHVVNEVIKNMPLDRADYTIPHHAAANLIVPDGNLVTIRDVVANLFVLFHEQYHRLLGNSQGSPSAFLTSLRRFQSLYMSKLKELEEHQRFTLVGLEKLKDTVIKVKQLNQSLSQKQVELQQKEKEARDTLDKMLVDQNEAERKQEASVEIQKILALQEKEINERRKIIMADLAVAEPAILEAQRGVKNIKKQQFTELRSMLNPPDAVKTTLEAVCVILGYSCKTWKDIQLAIRKDEFVTDIVYYNTETMMTPAMKQDIETDYLSRPKFNYESVNRASLACGPLYQWIVAQISYSEMLVKVTPLKEEMVKVENEMLQNKARLMAAGEMIKELQTSIESSKVSYSKLIREVEITKTEMESVQSKVERSIKLMESLTGEKERWIKNTEHFKDWNKNLIGNCFLSSLYESYCGPHDQSLRLKLFTIWSNTLAKFGIEYEPTYSFITDMVNPLTKVNWVACGLPDNELFVANFHIAMNSCHYPYVIDPSSTIVDTFANFYGRKMMITSFLDVGFVKQLENALRFGGCILIQDGEFFDPIISHLIAKEFKKAGGRLTVQIGDHEVDVSTSFQLIIHSKDPNSYMSSFVKTRMAVINFTVSKGSIEAQALQITLEKENPELQKQRTDLLKLNGEYKLHLRSLEDKLLESLNESDGSILENDSLISTLEQLKIESSEIAKKIEETNTVIVKVEDLVNEYNVLGEQSVLIFNLLESITQWHWFYQIPIEQFMECFSSIFATKTRENMTRSEHLLLALYEHVYMWFSHVFKDRDRMAFGILLFASYHHSRESKFFSEHFWKIIEGIASDTLGTVEHITDTKLEQLVAAANEKDYLKGLKSLLEFLPESSWHDSVPKYQNIIVACERGVDGTFKVQQLAQEMGKTVHSVALGSAESISMAEQDLIQYSGEGKWLLLQNLQMSHEWANTVLPKKLESIKANPDFRVFMTCGIQSKPLVVPLLSRSYKIAYEGEPGVLNTVCELWRTQSEELKNVKPVEKLHSKFILVWFHSIIMARCRLAPIGFTKKYDFHDGDFHAGSKFLDHIFEQSSNGKEHVDPDLVPWKLVSDTIGKIIYGGKVDDPADLDWCKRSARRMFSSDAYLNNFEVVQGLTVPIDRSSYSQYDKWFKSLDAAAERTTAWLELSDASALQNFYAHEARMICKKIIQTNGPTSLIH', 4083, 'Q9C1M7;', 'KD00517', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DYN1', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC', '-', '-', '4619795'),
(518, 'Q5RB58', 'Mitotic checkpoint protein BUB3', 'GO:0000777', 37143, 'Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1 (By similarity). {ECO:0000250}.', 'MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMATGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFLNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAETKPKSPCT', 328, 'Q5RB58;', 'KD00518', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'BUB3', '#Mitotic checkpoint protein BUB3', '-', '-', '100172494'),
(519, 'Q21952', 'Kinetochore protein Nuf2 homolog', 'GO:0000776===GO:0000777===GO:0051383===GO:0008608===k', 56722, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation in mitosis and meiosis and spindle checkpoint activity. {ECO:0000269|PubMed:11402066; ECO:0000269|PubMed:14522947; ECO:0000269|PubMed:15371539}.', 'MSNVVLIVYDPRMISKYLGQKLHMGLVADDIIKPTAEIAQQIFANFVRLVLNVSESSLTTLPLSANCDYDPELHKKSIPIIILFQCMKAFIKDNSGNKLDLTMCDLVTPAKHEHRFRKLTSFLVDFLKLHELATPAFNEISEEFSDRKFEMEKIREELLEAEKKKNDLLAKQSIRKRHEHELINEQSNAKAELKNVVNEYTETRQINEELDKQKEEAILHIQALEKEMLTGKKTIEHLNEEVLTSPEQLKQEMEERKRHIEELRDCLESSKKGLQAKLEAREICINSEKNVPVIIEKIHQWTEVREVIIDLIDVESENLRKLKEMEEQLDFMMKEMETAQKRLVEQSETHEQLRIEHTQKSEERQRRIEEITEQIANLKTSQPDVSQEIAKKKQELLALKNAHSETISQITNSCQDAVAKFAKLNAMFKETQKVAFEKNTAAAREMERLKSSLTGRLLSDYTFGSSTIDAGENTENCDPQPNDSSFSVFK', 490, 'Q21952;', 'KD00519', 'Caenorhabditis elegans', 'him-10', '#Kinetochore protein Nuf2 homolog#CeNuf2#Kinetochore protein him-10#Protein high incidence of males 10', '-', '-', '175813'),
(520, 'O13290', 'Dynein heavy chain; cytoplasmic', 'GO:1902423===GO:0031134===GO:0005868', 484318, 'Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for nuclear movement during meiotic prophase. {ECO:0000269|PubMed:10366596}.', 'MDKNDNSQCQLSTVSDEILIFLKKLLSLSVSDNLDDICETIALQSTFVDTFRSFINDEYYTVIYLYGSPCLTSSPTSPDSCTFGNMTFQWTSLLQDVFSGTSAFAIFKRFPLTDTPLTLQNMLYINQLPILKGGHKSNEIPERPINAIFLYTKYVMSCYFTAYLAMESVDDRSTIDLNSPSKGKELELTCQKFADFERSFTFFCREYQNSDTILQHHPLILSTIKHAEENNLDLSVRLLPSKVLSDSEFYKSLSNLVNVWLKTTRSLIKLFHDQISKTALEEFNFWQFYYRSLSRLNDQLHSRPVLFVLDILAFGKRFHTIASFNSETNIQCFVDKVGKIDALFKEISLDIFLSSSTLESLQLSAALLYSTFSKKWRNTGYPETRVLDFINFITEDLLKLISRLLPALGALSLSNVDFSHRTAVSSDILSLCYIRLKDFLRISGSLKEEQSYYGLKNSIKQIKAFENKLKYIQSFHEKHQQLIGALSEVYGLTHLTELEILEHLNKKEHVFNILTVFKDLQSLNVLDISLKGVNAWNSLETSYYNCMTVLEDEVIAQLKSLLQYSKTSSQMFTTLMRFQPLFFRTRVRTSISDCLHLLVNRIKQELDLLKTRFTEDVSDTELIAMNELRNLPMASSAIIWATQLKNRLHEYTKNINIIFGEDWNNFPDGFELKVECITLQKRLDTNLIFTNWINDVSSRNLNFDFDSKIFYLTQSESAESPLRLSVSIDFDPCSFCKEIRTLAHLGYNIPSQLMELASCLQRIQLIAMCLIDSVQSFNDVSFEISKTEEERFLLQEYELAVRQHIVTGLFISWNDFIVGNLSTPPKCAIGKRNFLKNIHPNVENYAYQFSSLTSLLMNKRNAISHTYMQIQEQLFQLDICEYSGDIFLTIQRKLQDLIDLLYVNGYSNLPPFVRALNLRFQDLLISRCRKFLSFFKTTILTSGNENNDLKSKFSSDMYEKLRGFLKPTNLTIQRNIIEFDPPVYRKKEDSIYLLDMCLQSVVNIPLLSIKTTAQRNCTLIGFFPVINRLESEILGIFESLLFHFDSILGYQNYWKKVEPFLNLNSLNLLLKSELFQLDQCYSLSLYLIHLKSEVDEIGKVTDFKIFSVNNTEFKSQVYLYLREWINALFDRFTFLLGKESEHLLNELDDTHSSLSTVDFTVNNTESLINSLKIFKKAGCYKLNVEHKIITYQNYEMTFNDCDAFSEFNFSLLKDITSKWKDLLESFECRRLKLENNKDEILRNFSEFAKRVNTETLSLISEWCASSLSLIKANYDEFSSTVDDFLFRFSKATEQCLMVKYIKKDLEIEIEESCDFSIQTEEIHLYKKFKDVISSNLEFIVEIKNTRWKLFDTATLSVQTTHQINALESVHTSFQHFKLFTNTKQSLNQLKDCTLLLQKLKSCPLKPVHWISLFEITKSTEQLDFEKLLVSDILGIDLQAHESFITTLLNSAVVEANLENQFNEVHSFWKNSYFSFKSFKGRNYIVVGCQELIDAVEKNMDSLNLIKTSRHFKDGDMNITDLQSKMKIIVKFLNIWKEIQQIWTHLSAIFYESTYIQQLLPELAASFFNSSKTYMHLVTLLKERSYLYKVSNIPSLLESAAKLSTTLEDSKKSLLKYFELQRHKISRLYFLGDDDLMELISNPCDPFVINKQIIKLYPGIRSLIVDTENTNINGCTTNEGNELLFDNPICLLDNTQPLHWISSLEPFLKATLFQLFSTSFQQIRDFYYNKSRNVFCKEWFLRYPSQITLLSLRCTLCHEIETGIADCCLDAVFNFINDGISSLVLLADENELSIKKKVTLMFNELLHFKETVGLLCKNSFNNYFWSREVKAFYREDHDDEAVVIKMFSLEFIYAFEYSELDDPIVYTDLTRNCFSVLLHSIASNLGGSPIGPAGTGKTETVKAVSAYLGKNVFVFNCDNAFNYKTIQRILSGLAQIGTYICFDEFNRLDSGTLSAISYDIQRIQSLVSHSDGLCQSPILLDAPTIFVTMNPGYLGRFKLPSNLKKLFRPIWMGSPDNKKICEILFLSFGFKESSLLSQVLDSFFLCCSGSLSNCLHYDFGLRAMKVVIKAAKRIKGFLKKKNTICQELEILWYAIREVLYPSLIYQDIPLFFKAEESYFNFPAVKANAFIDPDNFEVNIEQTLSKNFFGNNQYLKLKIMQLYQMSEAYNGIILLGKTGSGKSQIFRILQSALLNIGIDCIVYVISPKALTKESLFGSMNMDTREWTDGVFTKLLRKTRDSCYYKRYMFVFDDELSPEWVEAMNSLLDDNKTLTLSNGERIALQPYVKIFFEADSVASLTRATISRCGLICISNIDDNILSSTDKMLSFTSGATNYPLGSSNDEFSTVFSKVLTDEVMMNLISSCYKFSVDLQHIMNFTKQRFFTTFYSLLDQTKLFTRSSNITESLSFKELCNYLKKKICYILAWCCTGDTDAKSRERFTHWLMQNASVDLPEIKDFEHVSILDFDVSLETQSWYPIAGKTLKSSALKYAGNTVIPTLDTVRYAEFLNFSLTKNRCVIFCGPPGSGKSMLMLGTLRSRQDVEVIALNFSISTSSKSVVSFLEQSTVYYRSTGMTIMCPKNHEKVLVLFCDEINLPRSRNCLAEDVICFLRHMLEHQGFWHPLHKEWVTIKNIFVCGACNPSTDIGRNDFPERFLRRTVLIFVDYPESYSLVTIYNALLEKSALINQYKTIILNIVKASVKFYQVLRENFKSSTQGYVYTPRDLTRWLISFKNYAESYAETNNLSLIKVWYHEACRVLLDRLVSQKECSWGMTELQKVIVTDFGEFEVSVIFEKQIIFTDILKNGLEFLDFASLRPKLESLYKKFYSSHPNNTLVFVDETITHILRFHRILNNSGMHALLQGSVGLGQKAVVEFVCWLNSFSLFELQKNQTYSIEDFEDNLKSILILAGTTNCKACLAINESIAGVPGFLDLLNNLLTNSEVSNFFDQNDWAEIKKNLNKLNEFQPLKFDSEESVTEIFMNNVFQNLCVVFYVYTSADVDFQTNSLSPALLNRCTIDYYHSWDYHSMLQIANEVLQETISLNALDHDNPNLKNIKGSSIYDAVAQAVVNTHTSIVWEFKHLGKTSYFSCLHFIRFLNTFCLIFGRDANKLSKEKSRIENGFKKIKETSQGIDKFKEALSDQQNVLFSKTKTANDRLQCIIQTKQAVEAKKVYSLQAEASLQKKSFLLNEKKNSVMKEVSYAKPAVIEARKSVSDIKKAHLIELRSLSRPPMAIRITMEVVCKLLGFSATDWKNVQQLLKRDDFIPKILNYNLEKELSINLRRKIEQDYFSNPIFTFDSVNRASKACGPLLLWIKSICNYSKVLEKLEPLNSEVDRLKLEQKNAEECIQETIAACKDLDEKLLQLQEEYASMISEIHSMELQMDEVKCKMQRSIEVITDLSIERNEWSGFLNLYPKRMWNLVGESLMEASFVVYAGNLDPSMRIFLRNKCEPIISSFGFPISKSAVRTNIERCVQTSIESKYYKNLTDYSLENIYIIQENKSPLLIIDPSSQILDILPSLYKGKASDLISFSNKSFQNQIKLALLSGSAIIIKDAELWDVSIEPLLKPEFFTGSGEVQTTFAKDTITITLPLNIIFFSEVQSNELENKASKFMNVVNFTLSISLLETQMLKSVISVQEPGVFKQKDNCFTLKLSIERQIRSLQEQLLKTLCSSNENIVGTDEIVVLLKNLKEKHETIRLAYSESQSINRKVDELIRRYKLSIKSFLSVVVVFQHFISLKKSYSFSFNFIWSTFHQMLNVVLENRNQDFKSLIMDALRDLIRRCFLYIFPEDRVLFLFLLMFFFFPKETESLRKLLIVNGKTLELEQSYLNFFETCSDSNERGGLESLFFKTHASNIQNFCTEVLANTHCEEDCLKLLYDLWSSAFKVEFSNIKYDFLKIINDESESRMPTIVYLMENCEIDSLLQNAKIPQNIKKLTVSLGSAENESLADSYLKLASTEPLWLFINNIHLSTPWAEKLPSKMSNHLHKNSRIVCLSEIHNQLPHQLLCISRSIVFNKQTSFKNNLLNLLELLPTMTHTLPHNRFRLFFFLSWLHATLAEIYCFTCSSWKEPCYFDDSDFYFGTKILCNILYRNVHLEEFSWGTFKDLLLNVVYGPKVSASSDFIALDKILKRLIAQFKTQISSNILLTDNFKFILPYEITFSSAKEVIGQLPDEIPPGWLDIPENSKRKRTDIYFSMCI', 4196, 'O13290; Q9P6L0; Q9UTP8;', 'KD00520', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dhc1', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC', '-', '-', '3361400'),
(521, 'P36614', 'Serine/threonine-protein phosphatase ppe1', 'k', 35259, 'Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. Negatively regulates mis12. {ECO:0000269|PubMed:12773390}.', 'MFDLDEWIATVRKCKYLPEHQLKRLCEMVKVILMEESNIQPVRTPVTVCGDIHGQFYDLLELFRVGGELPSTNYIFMGDFVDRGYFSLETFTLFMLLKARYPDKITLLRGNHESRQITQVYGFYDECQTKYGNANVWKYCCQVFDFLTLAAVIDNKILCVHGGLSPEVRTLDQIRILARAQEIPHEGSFCDLMWSDPEDIESWTVSPRGAGWLFGSKVTTEFSQINDLTLIARAHQLVQEGYKYHFADKNLVTVWSAPNYCYRCGNVASVMKVDESLEPEFRIFSAVADEDRTVPPSRKRSEYFI', 305, 'P36614;', 'KD00521', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ppe1', '#Serine/threonine-protein phosphatase ppe1#3.1.3.16#Phosphatase esp1', '-', '-', '2538758'),
(522, 'Q6C070', 'DASH complex subunit SPC19', 'GO:0008608===GO:0042729', 19219, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore (By similarity). {ECO:0000250}.', 'MTNTLDDSIGSMQNCVSIVRDTSLKLRSRAQTPEETERIKKVLQLTRKYEEVTQSEVLAAQQRQAAEIAPQVQDLIGGVEKQISSLHSKERKLKSQSELNKSRLEQFPMTRREVVDVPRDADNVVEVTEEELQELEELQREREKLKMEISRLNLEKRKSVYGKLPQ', 166, 'Q6C070;', 'KD00522', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'SPC19', '#DASH complex subunit SPC19#Outer kinetochore protein SPC19', '-', '-', '2907882'),
(523, 'P36612', '26S protease regulatory subunit 4 homolog', 'GO:0061638', 50060, 'The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.', 'MGQAQSGNFSNFGDGANGDNKKDQKKDKPKYEPPVPTRTGRRKKKAQSGPDASAKLPTVIPTTRCRLRLLKMQRIHDHLLMEEEYVQNQERLKPQDERTQEERNRVDEIRGTPMSVGTLEEIIDDDHAIVSTAGPEYYVSIMSFVDKDMLEPGCSVLLHHKAMSIVGLLLDDTDPMINVMKLDKAPTESYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPRLVRQLFNAAEEHSPSIVFIDEIDAIGTKRYDAQSGAEREIQRTMLELLNQLDGFDTSQRDIKVIMATNRISDLDPALIRPGRIDRKILFENPDEATKRKIFTIHTSKMNLGEDVNLEELIQCKDDLSGAEIKAIVSEAGLLALRERRMRVVMDDFRQAREKVLKTKDEGGPAGGLYI', 448, 'P36612;', 'KD00523', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mts2', '#26S protease regulatory subunit 4 homolog#Protein mts2', '-', '-', '2540939'),
(524, 'O01789', 'HIM-1; isoform a', 'k', 144217, '', 'MRGGSSLDSFPGKGTLHTLEIENFKSYKGKHTIGPFTRFTAIIGPNGSGKSNLMDAISFVLGEKPSSLRVRKYADLIHGAPINKPVAKKCRVTMNYKYSDGKVKAFTRGVNNGTSEHLLDGQTVTSAAYSQEMESINIFIKARNFLVYQGAIENIAMKTPKERTQLFEELSRSHEFQAEYERLKVEMTKAEDDTQHNMNKRRGIAQEKREAKMEKDEAEKYQTMKNELAAKSTMLFLHQLFHCERTIDESKEEINAQKKTIASLEATRSKEEAKIAAVHQEHRKALREVQKMTRKLDQKETDLAEKQQNMLTLKVSVAHEHKKLEIAKKMLAAAESKAENNSTQLADLKKSKKELEKKKAAYEAEIQDMMQRGELNLSDEQVREYGQLKDQAQRESAMVQRELLMAEQVFEGDKSSLNHELRRQKEHQERVKAKEGDVRRIETQIATLAQRIKETEEETKILKADLKKIENDVVIDKSAAAEYNKELVAVVRQLSEASGDSAEGERNQRRTEALEGLKKNFPESVYGRLVDLCQPSHKRFNIATTKILQKHMNSIVCDTEETAAKAIVYLKDHRYPPETFLPNDALVVNPLNEKLREIKKPAGVKLVFDVINPQHQAARKALQFVCGNALVCESQEDAKQLAYGGGELKDRFKAVSMDGTLFQQSGVMSGGSADLRQKSKKWDEKVVKQLREKRNQLNEKIADLQKHRRRELEVESVRSKINGNEQRLAMMKRDLKNMREMQLERLQNELEGMTAEMNMLPPRISNCQEKLERSESTLKSLQTKSNEVADRIFADFCTRVGIASIRDYENREMRIKQEMEDKLRSFDDDIQKLAYEIDFVTEQDGNRKVEVEKEKVSQIDRQYKDMKKKEKTAAAALKEHTESMEQDKEVLEEKKALSHKLETEWNEVKKIAQVAMKDFTKAEKELLRLESLLTKKQYERHSLLHSVKLGQIALPLKSGSMADVEYEEDDGDDTASQSSQSATDGPSVSEEQIQREQHIKINYDSLPREYKDVDDDDGVRQMSNRLNVEIDELQKNVSKMNAPNLKANQRMAEVKEREAESTEELENARKKAKRIRQQFEKVKTDRYRRFQDFFDPVANTIDDIYKQLSRNTSAQAFLGADNMEEPYLDGIQYNCVAPGKRFRPMDNLSGGEKTIAALALLFAVHGRNPAPFFVLDEIDAALDNTNIGKVASYICESAREHMQIIVISLKEEFYNKADSLIGIFPYPAACTTSGVLTFDLTRFKQIGLNEMTENPPTPSIAT', 1262, 'O01789;', 'KD00524', 'Caenorhabditis elegans', 'him-1', '#HIM-1; isoform a {ECO:0000313|EMBL:CCD69832.1}', '-', '-', '172116');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(525, 'Q9UBB5', 'Methyl-CpG-binding domain protein 2', 'k', 43255, 'Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein; targeting GATAD2A and GATAD2B to chromatin to promote repression. May enhance the activation of some unmethylated cAMP-responsive promoters. {ECO:0000269|PubMed:10471499; ECO:0000269|PubMed:10947852; ECO:0000269|PubMed:12665568; ECO:0000269|PubMed:16415179; ECO:0000269|PubMed:24307175; ECO:0000269|PubMed:9774669}.', 'MRAHPGGGRCCPEQEEGESAAGGSGAGGDSAIEQGGQGSALAPSPVSGVRREGARGGGRGRGRWKQAGRGGGVCGRGRGRGRGRGRGRGRGRGRGRPPSGGSGLGGDGGGCGGGGSGGGGAPRREPVPFPSGSAGPGPRGPRATESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYFSPSGKKFRSKPQLARYLGNTVDLSSFDFRTGKMMPSKLQKNKQRLRNDPLNQNKGKPDLNTTLPIRQTASIFKQPVTKVTNHPSNKVKSDPQRMNEQPRQLFWEKRLQGLSASDVTEQIIKTMELPKGLQGVGPGSNDETLLSAVASALHTSSAPITGQVSAAVEKNPAVWLNTSQPLCKAFIVTDEDIRKQEERVQQVRKKLEEALMADILSRAADTEEMDIEMDSGDEA', 411, 'Q9UBB5; O95242; Q9UIS8;', 'KD00525', 'Homo sapiens (Human)', 'MBD2', '#Methyl-CpG-binding domain protein 2#Demethylase#DMTase#Methyl-CpG-binding protein MBD2', '-', 'ENSG00000134046', '-'),
(526, 'P18105', 'Kinesin-like protein Nod', 'GO:0003777', 73908, 'Required for the distributive chromosome segregation of non-exchange chromosomes during meiosis. May be a microtubule motor required to hold distributively "paired" chromosomes at the metaphase plate until anaphase.', 'MEGAKLSAVRIAVREAPYRQFLGRREPSVVQFPPWSDGKSLIVDQNEFHFDHAFPATISQDEMYQALILPLVDKLLEGFQCTALAYGQTGTGKSYSMGMTPPGEILPEHLGILPRALGDIFERVTARQENNKDAIQVYASFIEIYNEKPFDLLGSTPHMPMVAARCQRCTCLPLHSQADLHHILELGTRNRRVRPTNMNSNSSRSHAIVTIHVKSKTHHSRMNIVDLAGSEGVRRTGHEGVARQEGVNINLGLLSINKVVMSMAAGHTVIPYRDSVLTTVLQASLTAQSYLTFLACISPHQCDLSETLSTLRFGTSAKKLRLNPMQVARQKQSLAARTTHVFRQALCTSTAIKSNAANHNSIVVPKSKYSTTKPLSAVLHRTRSELGMTPKAKKRARELLELEETTLELSSIHIQDSSLSLLGFHSDSDKDRHLMPPPTGQEPRQASSQNSTLMGIVEETEPKESSKVQQSMVAPTVPTTVRCQLFNTTISPISLRASSSQRELSGIQPMEETVVASPQQPCLRRSVRLASSMRSQNYGAIPKVMNLRRSTRLAGIREHATSVVVKNETDAIPHLRSTVQKKRTRNVKPAPKAWMANNTKCFLDLLNNGNVKQLQEIPGIGPKSAFSLALHRSRLGCFENLFQVKSLPIWSGNKWERFCQINCLDT', 666, 'P18105; Q9VYW9;', 'KD00526', 'Drosophila melanogaster (Fruit fly)', 'nod', '#Kinesin-like protein Nod', '-', '-', '32107'),
(527, 'Q92769', 'Histone deacetylase 2', 'k', 55364, 'Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A; H2B; H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation; cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD; SIN3; YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1; DMAP1; PCNA; CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses; via histone deacetylase (HDAC) recruitment; a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes; such as PER1; mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A. {ECO:0000269|PubMed:19343227; ECO:0000269|PubMed:21965678}.', 'MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP', 488, 'Q92769; B3KRS5; B4DL58; E1P561; Q5SRI8; Q5SZ86; Q8NEH4;', 'KD00527', 'Homo sapiens (Human)', 'HDAC2', '#Histone deacetylase 2#HD2#3.5.1.98', '-', 'ENSG00000196591', '-'),
(528, 'P43618', 'Kinetochore-associated protein CNN1', 'GO:0000776===GO:0000777===SCL===k', 41313, '', 'MSTPRKAAGNNENTEVSEIRTPFRERALEEQRLKDEVLIRNTPGYRKLLSASTKSHDILNKDPNEVRSFLQDLSQVLARKSQGNDTTTNKTQARNLIDELAYEESQPEENELLRSRSEKLTDNNIGNETQPDYTSLSQTVFAKLQERDKGLKSRKIDPIIIQDVPTTGHEDELTVHSPDKANSISMEVLRTSPSIGMDQVDEPPVRDPVPISITQQEEPLSEDLPSDDKEETEEAENEDYSFENTSDENLDDIGNDPIRLNVPAVRRSSIKPLQIMDLKHLTRQFLNENRIILPKQTWSTIQEESLNIMDFLKQKIGTLQKQELVDSFIDMGIINNVDDMFELAHELLPLELQSRIESYLF', 361, 'P43618; D6VTS9; Q6B2K8;', 'KD00528', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CNN1', '#Kinetochore-associated protein CNN1#Co-purified with NNF1 protein 1', '-', '-', '850607'),
(529, 'Q9JMD0', 'BUB3-interacting and GLEBS motif-containing protein ZNF207', 'GO:0000776===GO:0000777===GO:0008608', 52793, 'Kinetochore-binding protein involved in spindle-assembly checkpoint signaling by regulating mitotic chromosome alignment and mediating the stability and kinetochore loading of BUB3. Mechanisms by which BUB3 is protected are unclear (By similarity). {ECO:0000250}.', 'MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDERRRLLEQKTQESQKKKQQDDSDEYDDDESAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGLHHQRKYTQSFCGENIMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTAAVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKALFPSTAQAQAAVQGPVGTDFKPLNSTPAATTTEPPKPTFPAYTQSTASTTSTTNSTAAKPAASITSKPATLTTTSATSKLIHPDEDISLEERRAQLPKYQRNLPRPGQTPIGNPPVGPIGGMMPPQPGLPQQQAMRPPMPPHGQYGGHHQGMPGYLPGAMPPYGQGPPMVPPYQGGPPRPPMGMRPPVMSQGGRY', 495, 'Q9JMD0; E9PW12; Q99LA2; Q9Z326;', 'KD00529', 'Mus musculus (Mouse)', 'Znf207', '#BUB3-interacting and GLEBS motif-containing protein ZNF207#BuGZ#49 kDa zinc finger protein#Zinc finger protein 207', '-', '-', '22680'),
(530, 'P21272', 'CCAAT/enhancer-binding protein beta', 'GO:0000779', 31503, 'Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Binds to regulatory regions of several acute-phase and cytokines genes and probably plays a role in the regulation of acute-phase reaction; inflammation and hemopoiesis. The consensus recognition site is 5''-T[TG]NNGNAA[TG]-3''. Plays an important role in adipose tissue differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG) as well as other adipogenesis key player genes. {ECO:0000269|PubMed:1934061}.', 'MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAAADFAAPAPAHHDFLSDLFADDYGAKPSKKPSDYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKAVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC', 297, 'P21272; A2VD03;', 'KD00530', 'Rattus norvegicus (Rat)', 'Cebpb', '#CCAAT/enhancer-binding protein beta#C/EBP beta#C/EBP-related protein 2#Interleukin-6-dependent-binding protein#IL-6DBP#Liver-enriched inhibitory protein#LIP#Liver-enriched transcriptional activator#LAP#Silencer factor B#SF-B', '-', '-', '24253'),
(531, 'Q59PT6', 'Probable kinetochore protein SPC25', 'GO:0000777', 27936, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MDTAERAYEKFQNQMIAFDNLKIEMNELAVDLDQQLSDKQSLILQQEQDHKQKVNDLTNQEYKLKLQAKSLKEKENATRDKLNLAMRSLEQQKSKVEDLVKKKQSLVDTKQDLESQIKQLETAIDQGTRELNKSNDNMSLQMNKNLVELNKYEIYTGLKIEVQSNELMCFKFFNLDPNDYDREFAITLNIGGSTYSIENTSPKLSDETVEQIQGKLNQGRQLSKFLKEVRTLFKDFVQY', 239, 'Q59PT6;', 'KD00531', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '3646200'),
(532, 'Q6DE08', 'Aurora kinase B-A', 'GO:0034501===GO:0032133===c;k', 41735, 'Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint; a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Phosphorylates ''Ser-10'' of histone H3 during mitosis. {ECO:0000269|PubMed:11350965; ECO:0000269|PubMed:12221116; ECO:0000269|PubMed:17199039}.', 'MSYKENLNPSSYTSKFTTPSSATAAQRVLRKEPYVSTFTTPSDNLLAQRTQLSRITPSASSSVPGRVAVSTEMPSQNTALAEMPKRKFTIDDFDIGRPLGKGKFGNVYLAREKQNKFIMALKVLFKSQLEKEGVEHQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHGRFDEQRSATFMEELADALHYCHERKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCYEFLVGMPPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQRLPLKGVMEHPWVKANSRRVLPPVYQSTQSK', 361, 'Q6DE08; Q7ZYT9; Q8JG74; Q9DF70;', 'KD00532', 'Xenopus laevis (African clawed frog)', 'aurkb-a', '#Aurora kinase B-A#2.7.11.1#Aurora/IPL1-related kinase 2-A#AIRK2-A#XAIRK2-A#Serine/threonine-protein kinase 12-A#Serine/threonine-protein kinase aurora-B-A#xAurora-B', '-', '-', '398457'),
(533, 'Q8NF99', 'Zinc finger protein 397', 'k', 61139, 'Isoform 3 acts as a DNA-dependent transcriptional repressor. {ECO:0000269|PubMed:12801647}.', 'MAVESGVISTLIPQDPPEQELILVKVEDNFSWDEKFKQNGSTQSCQELFRQQFRKFCYQETPGPREALSRLQELCYQWLMPELHTKEQILELLVLEQFLSILPEELQIWVQQHNPESGEEAVTLLEDLEREFDDPGQQVPASPQGPAVPWKDLTCLRASQESTDIHLQPLKTQLKSWKPCLSPKSDCENSETATKEGISEEKSQGLPQEPSFRGISEHESNLVWKQGSATGEKLRSPSQGGSFSQVIFTNKSLGKRDLYDEAERCLILTTDSIMCQKVPPEERPYRCDVCGHSFKQHSSLTQHQRIHTGEKPYKCNQCGKAFSLRSYLIIHQRIHSGEKAYECSECGKAFNQSSALIRHRKIHTGEKACKCNECGKAFSQSSYLIIHQRIHTGEKPYECNECGKTFSQSSKLIRHQRIHTGERPYECNECGKAFRQSSELITHQRIHSGEKPYECSECGKAFSLSSNLIRHQRIHSGEEPYQCNECGKTFKRSSALVQHQRIHSGDEAYICNECGKAFRHRSVLMRHQRVHTIK', 534, 'Q8NF99; Q9BRM2;', 'KD00533', 'Homo sapiens (Human)', 'ZNF397', '#Zinc finger protein 397#Zinc finger and SCAN domain-containing protein 15#Zinc finger protein 47', '-', 'ENSG00000186812', '-'),
(534, 'Q9UFC0', 'Leucine-rich repeat and WD repeat-containing protein 1', 'k', 70861, 'Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3; H3K20me3 and H4K27me3 in a cooperative manner with DNA methylation. Required for silencing of major satellite repeats. May be important ORC2; ORC3 and ORC4 stability. {ECO:0000269|PubMed:20850016; ECO:0000269|PubMed:20932478; ECO:0000269|PubMed:21029866; ECO:0000269|PubMed:22427655; ECO:0000269|PubMed:22645314}.', 'MGPLSARLLMQRGRPKSDRLGKIRSLDLSGLELLSEHLDPKLLCRLTQLQELDLSNNHLETLPDNLGLSHLRVLRCANNQLGDVTALCQFPKLEELSLEGNPFLTVNDNLKVSFLLPTLRKVNGKDASSTYSQVENLNRELTSRVTAHWEKFMATLGPEEEAEKAQADFVKSAVRDVRYGPESLSEFTQWRVRMISEELVAASRTQVQKANSPEKPPEAGAAHKPRARLAALKRPDDVPLSLSPSKRACASPSAQVEGSPVAGSDGSQPAVKLEPLHFLQCHSKNNSPQDLETQLWACAFEPAWEEGATSQTVATCGGEAVCVIDCQTGIVLHKYKAPGEEFFSVAWTALMVVTQAGHKKRWSVLAAAGLRGLVRLLHVRAGFCCGVIRAHKKAIATLCFSPAHETHLFTASYDKRIILWDIGVPNQDYEFQASQLLTLDTTSIPLRLCPVASCPDARLLAGCEGGCCCWDVRLDQPQKRRVCEVEFVFSEGSEASGRRVDGLAFVNEDIVASKGSGLGTICLWSWRQTWGGRGSQSTVAVVVLARLQWSSTELAYFSLSACPDKGIVLCGDEEGNVWLYDVSNILKQPPLLPAALQAPTQILKWPQPWALGQVVTKTMVNTVVANASFTYLTALTDSNIVAIWGRM', 647, 'Q9UFC0; A8K4K2; B2R9G2; Q8N0T9; Q8WV43; Q96GJ2;', 'KD00534', 'Homo sapiens (Human)', 'LRWD1', '#Leucine-rich repeat and WD repeat-containing protein 1#Centromere protein 33#CENP-33#Origin recognition complex-associated protein#ORC-associated protein#ORCA', '-', 'ENSG00000161036', '-'),
(535, 'Q27802', 'Cytoplasmic dynein 2 heavy chain 1', 'GO:0003777', 490483, 'May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis (By similarity). {ECO:0000250}.', 'MPAEDARKEYLLSSCGSQLGLSASDDAITSLYSARELNTFLDDGNCSVLSAKLNSSGGNKKVYLSNKVDPSDTGEKVIAFFKLRPDVISPDNVQSSILTVSMMDSPAGALLHAVDKVFAPLLIEDEKYNRSFNPKLQSLLSELRAGLKSLVRKQDPSQGGPVKRGDNDFAGILTPSDEFQHWSEVAMSGRNQDAKERAEHFLSFFETVSREFDVLDTLSLEEAQELVETTQDAVDDVWKQGEFDPYPEKRMAHLLEVIGSAFGRFIQRKLGEFDLWLDPFHKVKQALLSGIAICEKWVSSCEKLTEQFWKRDPMHPWNGAKFTPEGLSQLSKRLQEISTLRTIHEQLIRLLSKGEQEEVRLKDVFSAFSGLNPLQYNPYTEPHWRAAVSQYERAINPAERRIAIKLRSQFRNVEGNPNQLLREFQKYKELVSRESVRKEVVSERETLLGQLQVYLKSIRDDFNVRTSESSPPTGKNLPEVVNNIVWVRQLEAKVEQTSQVADTLLNDLSGFGRFRRDAGDLLDELRNWRQDQFDSWSSEMQAAISDPNKPLSLQMTGRLMEFETKNNELIVSYSERLVTLMREVRQLQALGYPVAAKIQHTAAIAQKFYKHGVILKQVAHFHNSIAEQMIPSQRNMMLQSALAFERIIKNPRTGSKDAGQGKVQVTWENPKELEEYITKLQAAAEKLTTENRRLRKWHYTVCDKVVSLMSIDLLRQQPRWKEGLQEIRGIMASLESQGYKSQDMKSWKMHWDRQLYKALEHQYQMGLEALNENLPEIKVELTYRQQALQFRPPIEEIRAKYYREMKKFISLPYHFRGIGDTGEPLIYPAIIERNASGFLNVYKMAEVLFSKLEKAKDIFKNWVVLGSVDLDKLLETHLHTVTDWERNFKALKARGRDSEKLPSQVKVYCVTVSTAPVKGTIDDHIQRLFDSLLSSLRRSITESVTEIEKFLKDGMEALATMPQTVEEIGNANAKHAELEAKKPEMRPMFDRAEAKNKLLRTVAGGGVDQFTQLHAHWEKFELMMESHQLMIKEQVNVMKSNVESRVDAFRAELEKFSARWNHAKPSPEVIESGDKESCLRAVELVKEKKVEFDEMQKTKNSLIFDCKHFELEEPFFSIANDLEVDFDQQTTMWTLYEEFSNGLSVLETEDWIVFRSKTYQFDDFLTTWTEKLKSGGPDVEHTIMTVRLSKDIDKYKTVSPLLKYLSSDIFTQEHWMDLYRMLKMPRSKTVERMTFGDILATADHIVANADGLKDLFNRAKGEVSIREALRELDVWGVGACFSLTEYSDSTDHQLMLIKDWKDLVTQVGDNQSLLQSLKDSPYYKGFADKATIWEQRLADLDEYLQNLNQIQRKWVYLEPIFGRGALPKEQGRFRRVDDDFRSIMMDVARDNRVLSLVGRSGLRTTLTTLLDQLQRCQKALNEFLEEKRSILPRFYFIGDDDLLEILGQSQNPAVIQSHLKKLFAGIHSVEFDQGCKHITAMKSLEGEVVPLLKAVEITPEVEIWLGDLAKEMKSTLRKLLVDCLKDQQSSSSGVGVDPTKYPSQILGLAAQIQFTEQCETAIRDNSLQDLLIELEQQLEGYTSADISGAAGERNAAIHVLELKLKALILDTIHSLDVVQLLQKENVTSLDNWLWQKQLRYYLDNTKTAIMRMVDAEFQYTYEYQGNAAKLVHTPLTDKCYLTLTQGMHMGMGGNPYGPAGTGKTESVKALGGLFGRQVLVFNCDEGVDVKSMGRIFIGLVKCGAWGCFDEFNRLEEAVLSAVSMQIQTIQAALKQKKPKVDLLDRTIDIDPNSGIFITLNPAGKGYGGRQKLPDNLKHVFRPVAMSRPDNEQIAEVILFSEGFKDGKSLGRKLVAIFNLAKELLTPQQHYDWGLRALKTVLRGCGNLLQIARQQAGQDRSKVQEPKLVVQALRVNTLSKLTFSDGIRFDALVKDVFPGVELKDIEYMTLADAIRQHCKEHNLVVMETQVKKALELYEQLRQRMGVVVVGPSGSGKSTTWQILRAALNNTGQVVKQYTMNPKAMPRTQLLGHIDMDTREWSDGVLTYSARQVVREPQEIHSWIICDGDIDPEWIESLNSVLDDNRLLTMPSGERIQFGPNVNFLFETHDLSCASPATISRMGMIFMSDEDTEIKDLVQSWLSHQAEESRNRLAAWIEDHFYRALEWVMRQGDFVVDTSLVGVVMNGLSHLRGAECISDFTIKLIRGLGANLPEATRMNFAKEVFHMTREQPPDPRRILDTYFDERTGSLATYTMQDNDELSASDFNNPSSLPVIRTPDVQRCLDFFNPWLEADNRQPFILVGPDGCGKGMVLRHCFAQLRSTQIATIHCNAQTSPTHLLQKLQQMCMVLSTNTGRVYRPKDCENLVLYLKDLNLPKPDKWGTCQLLAFLQQVLTYHGFYDDKLEWVGLDGVQIVASMNAAHTVGRHPLSTRFTSIVRICSIGYADREQLQGIYSAYLRPVLHRSLGNHPVWSSPSKVSMLAGSMISIYEQVRSKFTIDDHSHYLFTPRDLTQWVLGLLRYDLGGSSESTSEHVLEVLSYEARRLFCDRLVGEEARNRFDNILNGTLQADWNAGQILQNLNGHYYVTWGARTETSSGGSLPPAGKSLGRLSASDLKEVIKKAKKTFARENRELDIQIFHEVLDHVARVDRVLTQPRGSLLLAGRSGVGRRTAASLVAHCHRTELFSPNLSRAYGLKQFKNDLKTAMQQAGVEGNQVVLLLEDHQFIQPQFLELINSLLSSGEIPGLYSPEELEPLLAPIRDQASEEGFRGTLISYYASRILTNLHVVLIMDSKNASFAVNCQSNPAFYKSCSVQWMEGWSKESMKEIPRLLLRHHKGDTKDEGSKEDRKRHRKVSGGDEIIRNFLEIHKSSSVRHSTPRRYMTFLHTYLDVYRRKKQGVEEKQKHLQAGVAKLNEAKALVAELNSKAAKQSALLAEKQKEADEALKKIQTSMEKAGEQRREIEILKQQADEENVKLEKRKRVIDEELAEIEPQVQAAKSAVGSIKSESLSEIRAMRAPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVKEEISTFDARKINKDLREGTEQLLKKHASSFDPQNAKRASVAAAPLAAWVKANVKYSYALEKIEPLETEQNQLKKNLEKAVGRIEKLSKGLADVDHRVDEYKRRFQKLNEEAAKLKYELEKEQETIASAENLIGKLEGEYQRWNNQVSELNTELETLPKKAQCAAGFITYLTSSPEDERKQKLAEWSKLCGLERFDMRRFLSTESEQLTWKGEGLPSDELSVENAVMILQTNDMSIKSSLRPFLIDPSLRATEWLKTHLKEARLEVINQQDANFSTALELAVRFGKTLIIQEMDKIEPVLYPLLRADLISQGPRFVVQIGDKVIDYHEDFRLFMTTRNPNPEIPPDAASIISEINFTTTRAGLTGQLLAATIQHEKPELEVRKTELLKQEEDLKIQLAQLEESLLETLAKAEGNILENKALLESLNKTKESSQTITQSLVESVQLQESLDQERAAYLPLAENGSALFFVISDLAKLNNMYRFSLGAFLRLFSKALQGRMDGSSTEMRIQKLIKSLQMLVYEYVCQSLFKADRLMFALHLVHGMHPNHFKENEWEAFLGQIVADVRDSQQSGSMPSWVDQDRHKALASFMATFPSVGQSLSLTDNGLWGHFNRSSQCEHEFPTSLEKKISPFQQLLLIQAIRPDRLQSAMTFFAQRGLGMKELTTPTINLKRLCQDTVPSEPILIIISPGADPTQELQEVAAEVIGADHYHEVAMGQGQADIAMQLLHECSRNGEWLCLKNLHLVTAWLPVLEKEMNALSPHENFRLWLTAESHPKFPTILLQSSLKITYEAPPGIKKNLLRSYDSWTPEFIGRENNVVRAQALFALAWFHAICQERRNFIPQGWTKFYEFSMSDLRAGADIIDRLCHGKGKEVQFEFIYGLFENAIYGGRVDNPFDMRVLRSYLAQYFNKEMLGGSSARRSKKLPGGNSIPVSSYYKDFTELVSKFPDDDKPSFFGLPANIERSSQRIISVQVISQLKILRRSDEAAEKFDTEKWNTELGPILSLWKKLNQGSNLIQTKAQPPSDRSGTQGPIDSFIQLERYNALQLVQFVHSTLAALSKVIRGTSLLTSEVQALASNLLKQETPLSWQSKWEGPEDPVLYLKTIVSRTMAIQGWVEKAQRNNLLSDTLNLSELFHPDTFLNALRQQTARDSKTSMDSLKFACRWSGNISGAKYQVKIGGLHLEGCTFDGQRLSENQRDSPSVCSVPACSVAWVLKDTPNTYHASESISLPVYFTEQREKIVTHLVLPCGGEQDHWIQTGAALFLQNQ', 4318, 'Q27802;', 'KD00535', 'Tripneustes gratilla (Hawaian sea urchin) (Echinus gratilla)', 'DYH1B', '#Cytoplasmic dynein 2 heavy chain 1#Dynein heavy chain isotype 1B', '-', '-', '-'),
(536, 'Q8WUM0', 'Nuclear pore complex protein Nup133', 'GO:0000777===k', 128979, 'Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11684705}.', 'MFPAAPSPRTPGTGSRRGPLAGLGPGSTPRTASRKGLPLGSAVSSPVLFSPVGRRSSLSSRGTPTRMFPHHSITESVNYDVKTFGSSLPVKVMEALTLAEVDDQLTINIDEGGWACLVCKEKLIIWKIALSPITKLSVCKELQLPPSDFHWSADLVALSYSSPSGEAHSTQAVAVMVATREGSIRYWPSLAGEDTYTEAFVDSGGDKTYSFLTAVQGGSFILSSSGSQLIRLIPESSGKIHQHILPQGQGMLSGIGRKVSSLFGILSPSSDLTLSSVLWDRERSSFYSLTSSNISKWELDDSSEKHAYSWDINRALKENITDAIWGSESNYEAIKEGVNIRYLDLKQNCDGLVILAAAWHSADNPCLIYYSLITIEDNGCQMSDAVTVEVTQYNPPFQSEDLILCQLTVPNFSNQTAYLYNESAVYVCSTGTGKFSLPQEKIVFNAQGDSVLGAGACGGVPIIFSRNSGLVSITSRENVSILAEDLEGSLASSVAGPNSESMIFETTTKNETIAQEDKIKLLKAAFLQYCRKDLGHAQMVVDELFSSHSDLDSDSELDRAVTQISVDLMDDYPASDPRWAESVPEEAPGFSNTSLIILHQLEDKMKAHSFLMDFIHQVGLFGRLGSFPVRGTPMATRLLLCEHAEKLSAAIVLKNHHSRLSDLVNTAILIALNKREYEIPSNLTPADVFFREVSQVDTICECLLEHEEQVLRDAPMDSIEWAEVVINVNNILKDMLQAASHYRQNRNSLYRREESLEKEPEYVPWTATSGPGGIRTVIIRQHEIVLKVAYPQADSNLRNIVTEQLVALIDCFLDGYVSQLKSVDKSSNRERYDNLEMEYLQKRSDLLSPLLSLGQYLWAASLAEKYCDFDILVQMCEQTDNQSRLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHATLLGLANMETRYFAKKKTLLGLSKLAALASDFSEDMLQEKIEEMAEQERFLLHQETLPEQLLAEKQLNLSAMPVLTAPQLIGLYICEENRRANEYDFKKALDLLEYIDEEEDININDLKLEILCKALQRDNWSSSDGKDDPIEVSKDSIFVKILQKLLKDGIQLSEYLPEVKDLLQADQLGSLKSNPYFEFVLKANYEYYVQGQI', 1156, 'Q8WUM0; B2RAZ8; Q5T8N0; Q9H9W2; Q9NV71; Q9NVC4;', 'KD00536', 'Homo sapiens (Human)', 'NUP133', '#Nuclear pore complex protein Nup133#133 kDa nucleoporin#Nucleoporin Nup133', '-', 'ENSG00000069248', '-'),
(537, 'Q62209', 'Synaptonemal complex protein 1', 'k', 115935, 'Major component of the transverse filaments of synaptonemal complexes (SCS); formed between homologous chromosomes during meiotic prophase.', 'MEKQKPFTLFVPPRLSSSQVSAVKPQTAGGDSNYFKTANKCTEGDFGVPFTMSSRENIDKDPAFQKLSILPMLEQVANSGSCHYQEGVNDSDFENSEPMSRLYSKLYKEAEKIKKWKVSIESELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATIHWCNLLKETCARSAEKTNKYEYEREETRQVYVDLNSNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYQKEVNNKENQVSELLIQSAEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELSEKKDHLTSELEDIKMSMQRSMSTQKALEEDLQIATKTISQLTEVKEAQMEELNKAKTTHSFVVTELKATTCTLEELLRTEQQRLEKNEDQLKLITVELQKKSNELEEMTKFKNNKEVELEELKNILAEDQKLLDEKKQVEKLAEELQEKEQELTFLLETREKEVHDLQEQVTVTKTSEQHYLKQVEEMKTELEKEKLKNTELTASCDMLLLENKKFVQEASDMALELKKHQEDIINCKKQEERLLKQIENLEEKEMHLRDELESVRKEFIQQGDEVKCKLDKSEENARSIECEVLKKEKQMKILESKCNNLKKQVENKSKNIEELHQENKTLKKKSSAEIKQLNAYEIKVSKLELELESTKQRFEEMTNNYQKEIENKKISEGKLLGEVEKAKATVDEAVKLQKEIDLRCQHKIAEMVALMEKHKHQYDKIVEERDSELGLYKNREQEQSSAKIALETELSNIRNELVSLKKQLEIEKEEKEKLKMAKENTAILKDKKDKKIQASLLESPEATSWKFDSKTTPSQNISRLSSSMDSGKSKDNRDNLRASAKSILPTTVTKEYTVKTPTKKSIYQRENKYIPTGGSNKKRKTAFEFDVNSDSSETADLLSLVSEEDVSNRLYDNNPPDSHLLVKTPKQTPLSLSTPASFMKFGSLKKMREDRWTTIAKIDRKRRLKEAEKLFS', 993, 'Q62209; B2RQK2; E9QP17; O09205; P70192; Q62329;', 'KD00537', 'Mus musculus (Mouse)', 'Sycp1', '#Synaptonemal complex protein 1#SCP-1', '-', '-', '20957'),
(538, 'Q4X0I7', 'Probable kinetochore protein spc24', 'GO:0000778===GO:0051455===GO:0031617', 22783, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MLLDEDPATLIHHTIGNFNIQPDKQAVTRINDSLSTLQQSRELRMRDAESALRKLSRNLHALTAQHEEAVSSHDSAKHAAQMVELDTKKFRIAKAATELEIESERLEGELEMLKERLAELEAQGLEGDEATRREREADDATILRLKIYRSLGIDIEADEAGNFSKAVIRNSRKGDVHVVNMDPKFSRFFYANYFWSTMQG', 200, 'Q4X0I7;', 'KD00538', 'Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSA1100) (Aspergillus fumigatus)', 'spc24', '#Probable kinetochore protein spc24', '-', '-', '3513168'),
(539, 'Q96ST3', 'Paired amphipathic helix protein Sin3a', 'GO:0000776===k', 145175, 'Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in he control of the circadian rhythms. Required for the transcriptional repression of circadian target genes; such as PER1; mediated by the large PER complex through histone deacetylation. {ECO:0000269|PubMed:12150998}.', 'MKRRLDDQESPVYAAQQRRIPGSTEAFPHQHRVLAPAPPVYEAVSETMQSATGIQYSVTPSYQVSAMPQSSGSHGPAIAAVHSSHHHPTAVQPHGGQVVQSHAHPAPPVAPVQGQQQFQRLKVEDALSYLDQVKLQFGSQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPDLIMGFNTFLPPGYKIEVQTNDMVNVTTPGQVHQIPTHGIQPQPQPPPQHPSQPSAQSAPAPAQPAPQPPPAKVSKPSQLQAHTPASQQTPPLPPYASPRSPPVQPHTPVTISLGTAPSLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALTEQEVYAQVARLFKNQEDLLSEFGQFLPDANSSVLLSKTTAEKVDSVRNDHGGTVKKPQLNNKPQRPSQNGCQIRRHPTGTTPPVKKKPKLLNLKDSSMADASKHGGGTESLFFDKVRKALRSAEAYENFLRCLVIFNQEVISRAELVQLVSPFLGKFPELFNWFKNFLGYKESVHLETYPKERATEGIAMEIDYASCKRLGSSYRALPKSYQQPKCTGRTPLCKEVLNDTWVSFPSWSEDSTFVSSKKTQYEEHIYRCEDERFELDVVLETNLATIRVLEAIQKKLSRLSAEEQAKFRLDNTLGGTSEVIHRKALQRIYADKAADIIDGLRKNPSIAVPIVLKRLKMKEEEWREAQRGFNKVWREQNEKYYLKSLDHQGINFKQNDTKVLRSKSLLNEIESIYDERQEQATEENAGVPVGPHLSLAYEDKQILEDAAALIIHHVKRQTGIQKEDKYKIKQIMHHFIPDLLFAQRGDLSDVEEEEEEEMDVDEATGAVKKHNGVGGSPPKSKLLFSNTAAQKLRGMDEVYNLFYVNNNWYIFMRLHQILCLRLLRICSQAERQIEEENREREWEREVLGIKRDKSDSPAIQLRLKEPMDVDVEDYYPAFLDMVRSLLDGNIDSSQYEDSLREMFTIHAYIAFTMDKLIQSIVRQLQHIVSDEICVQVTDLYLAENNNGATGGQLNTQNSRSLLESTYQRKAEQLMSDENCFKLMFIQSQGQVQLTIELLDTEEENSDDPVEAERWSDYVERYMNSDTTSPELREHLAQKPVFLPRNLRRIRKCQRGREQQEKEGKEGNSKKTMENVDSLDKLECRFKLNSYKMVYVIKSEDYMYRRTALLRAHQSHERVSKRLHQRFQAWVDKWTKEHVPREMAAETSKWLMGEGLEGLVPCTTTCDTETLHFVSINKYRVKYGTVFKAP', 1273, 'Q96ST3; B2RNS5; Q8N8N4; Q8NC83; Q8WV18; Q96L98; Q9UFQ1;', 'KD00539', 'Homo sapiens (Human)', 'SIN3A', '#Paired amphipathic helix protein Sin3a#Histone deacetylase complex subunit Sin3a#Transcriptional corepressor Sin3a', '-', 'ENSG00000150459', '-'),
(540, 'P30622', 'CAP-Gly domain-containing linker protein 1', 'GO:0000776===k;m;s', 162246, 'Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. {ECO:0000269|PubMed:12433698; ECO:0000269|PubMed:17563362; ECO:0000269|PubMed:17889670}.', 'MSMLKPSGLKAPTKILKPGSTALKTPTAVVAPVEKTISSEKASSTPSSETQEEFVDDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTRPSKLTRKVQAEDEANGLQTTPASRATSPLCTSTASMVSSSPSTPSNIPQKPSQPAAKEPSATPPISNLTKTASESISNLSEAGSIKKGERELKIGDRVLVGGTKAGVVRFLGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKANAVRRVMATTSASLKRSPSASSLSSMSSVASSVSSRPSRTGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLEQKSQISEDPENTQTKLEHARIKELEQSLLFEKTKADKLQRELEDTRVATVSEKSRIMELEKDLALRVQEVAELRRRLESNKPAGDVDMSLSLLQEISSLQEKLEVTRTDHQREITSLKEHFGAREETHQKEIKALYTATEKLSKENESLKSKLEHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGLGTETAEFAELKTQIEKMRLDYQHEIENLQNQQDSERAAHAKEMEALRAKLMKVIKEKENSLEAIRSKLDKAEDQHLVEMEDTLNKLQEAEIKVKELEVLQAKCNEQTKVIDNFTSQLKATEEKLLDLDALRKASSEGKSEMKKLRQQLEAAEKQIKHLEIEKNAESSKASSITRELQGRELKLTNLQENLSEVSQVKETLEKELQILKEKFAEASEEAVSVQRSMQETVNKLHQKEEQFNMLSSDLEKLRENLADMEAKFREKDEREEQLIKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERDVEELQLKLTKANENASFLQKSIEDMTVKAEQSQQEAAKKHEEEKKELERKLSDLEKKMETSHNQCQELKARYERATSETKTKHEEILQNLQKTLLDTEDKLKGAREENSGLLQELEELRKQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNAKLQNELDTLKENNLKNVEELNKSKELLTVENQKMEEFRKEIETLKQAAAQKSQQLSALQEENVKLAEELGRSRDEVTSHQKLEEERSVLNNQLLEMKKRESKFIKDADEEKASLQKSISITSALLTEKDAELEKLRNEVTVLRGENASAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDTQADEDERAQESQIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGDDLNNYDSDDQEKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRGEERPYCEICEMFGHWATNCNDDETF', 1438, 'P30622; A0AVD3; Q17RS4; Q29RG0;', 'KD00540', 'Homo sapiens (Human)', 'CLIP1', '#CAP-Gly domain-containing linker protein 1#Cytoplasmic linker protein 1#Cytoplasmic linker protein 170 alpha-2#CLIP-170#Reed-Sternberg intermediate filament-associated protein#Restin', '-', 'ENSG00000130779', '-'),
(541, 'B4HGE0', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25678, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAIIMTESSYERRVKALYEKQIRMEALEAKFIKKVYKFNSNLWDVKEAACRHQRKVGKLQKVIMERREELDKRVSFIEELDRELEATKLRSLAMKDRIKQQKMLARQRKNEIMESIHTLSKTTGTYINQEALPARVKGVTVLRGDKRNQLIPFDLKSTDVEGLDSLCQHLESLNVDMAQWQQLISLAMDVAMESRAPTTPPKEAANCNSIIEIDLTSPTCHI', 222, 'B4HGE0; Q64EW5;', 'KD00541', 'Drosophila sechellia (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6606601'),
(542, 'P43605', 'N-acetyltransferase ECO1', 'k', 31845, 'Required for establishment of sister chromatid cohesion during S phase but not for its further maintenance during G2 or M phases or for loading the cohesin complex onto DNA. Interacts with the three known alternate replication factor C (RFC) complexes; suggesting that these complexes have essential but redundant activity in cohesion establishment. Acts by acetylating the cohesin complex component SMC3. In vitro; possesses acetyltransferase activity where it can acetylate itself and components of the cohesin complex (MCD1; IRR1 and PDS5); but is unable to acetylate histones. {ECO:0000269|PubMed:12665596; ECO:0000269|PubMed:15668154; ECO:0000269|PubMed:9990855; ECO:0000269|PubMed:9990856}.', 'MKARKSQRKAGSKPNLIQSKLQVNNGSKSNKIVKCDKCEMSYSSTSIEDRAIHEKYHTLQLHGRKWSPNWGSIVYTERNHSRTVHLSRSTGTITPLNSSPLKKSSPSITHQEEKIVYVRPDKSNGEVRAMTEIMTLVNNELNAPHDENVIWNSTTEEKGKAFVYIRNDRAVGIIIIENLYGGNGKTSSRGRWMVYDSRRLVQNVYPDFKIGISRIWVCRTARKLGIATKLIDVARENIVYGEVIPRYQVAWSQPTDSGGKLASKYNGIMHKSGKLLLPVYI', 281, 'P43605; D6VTQ7;', 'KD00542', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'ECO1', '#N-acetyltransferase ECO1#2.3.1.-#Chromosome transmission fidelity protein 7#Establishment of cohesion protein 1', '-', '-', '850584'),
(543, 'Q9LX99', 'Kinesin-like protein KCA1', 'GO:0003777', 141036, 'Kinesin-like protein required for chloroplast movements and anchor to the plasma membrane. Mediates chloroplast movement via chloroplast actin (cp-actin) filaments. Required for the chloroplast avoidance response under high intensity blue light. May act as a mitotic kinesin. {ECO:0000269|PubMed:15247388; ECO:0000269|PubMed:20418504}.', 'MADQRSKTNRWNWEVSGFEPRKSSSNASFAESTGHRTTGPLLRRNSISTPSLPPKQAIASKVNGLKEKVKLAKEDYLELRQEATDLQEYSNAKLDRVTRYLGVLAEKSRKLDQFVLETEARISPLINEKKRLFNDLLTAKGNIKVFCRARPLFEDEGPSVIEFPGDCTICVNTSDDTLSNPKKDFEFDRVYGPHVGQAALFSDVQPFVQSALDGSNVSILSYGQTNAGKTYTMEGSNHDRGLYARCFEELFDLANSDSTSTSRFSFSLSVFEIYNEQIRDLLSETQSNLPNINMDLHESVIELGQEKVDNPLEFLGVLKSAFLNRGNYKSKFNVTHLIVSIHIYYSNTITGENIYSKLSLVDLAGSEGLIMENDSGDHVTDLLHVMNSISALGDVLSSLTSGKDSIPYDNSILTRVLADSLGGSSKTLMIVNICPSVQTLSETISCLNYAARARNTVPSLGNRDTIKKWRDVASDARKELLEKERENQNLKQEVVGLKKALKDANDQCVLLYSEVQRAWKVSFTLQSDLKSENIMLVDKHRLEKEQNSQLRNQIAQFLQLDQEQKLQMQQQDSAIQNLQAKITDLESQVSEAVRSDTTRTGDALQSQDIFSPIPKAVEGTTDSSSVTKKLEEELKKRDALIERLHEENEKLFDRLTERSMAVSTQVLSPSLRASPNIQPANVNRGEGYSAEAVALPSTPNKNNGAITLVKSGTDLVKTTPAGEYLTAALNDFDPEEYEGLAAIADGANKLLMLVLAAVIKAGASREHEILAEIRDSVFSFIRKMEPRRVMDTMLVSRVRILYIRSLLARSPELQTIRVSPVECFLEKPNTGRSKSTSRGSSPGRSPVRYLDTQIHGFKVNIKAERRNKLASVVSRMRGLEQDAGRQQVTGVKLREMQDEAKSFAIGNKALAALFVHTPAGELQRQIRLWLAENFEFLSVTSDDVSGGNGGQLELLSTAIMDGWMAGLGAAVPPHTDALGQLLSEYAKRVYTSQMQHMKDIAGTLAAEEAEDAGQVSKLRSALESVDHKRRKILQQMKSDAALLNLEEGSSPIPNPSTAAEDSRLASLISLDGILKQVKEITRQASVHVLSKSKKKALLESLDELTERMPSLLDIDHPCAQREIATAHQLVETIPEQEDTNILEQSHDRRPSLESISSGETDVSQWNVLQFNTGSSAPFIIKCGGNNNSELVIKADARVQEPKGGEIVRVVPRPSVLVNMSLEEMKQMFVQLPEALSLLALARTADGTRARYSRLYKTLAMKVPSLKDLVSELE', 1273, 'Q9LX99; B3H459; O23652; Q0WVP0;', 'KD00543', 'Arabidopsis thaliana (Mouse-ear cress)', 'KCA1', '#Kinesin-like protein KCA1#Geminivirus Rep-interacting motor protein#Geminivirus replication protein-interacting protein#Kinesin CDKA-1-associated protein 1#Kinesin-like protein for actin based chloroplast movement 1', '-', '-', '830911'),
(544, 'Q9UBC3', 'DNA (cytosine-5)-methyltransferase 3B', 'k', 95751, 'Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co- repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing (By similarity). In association with DNMT1 and via the recruitment of CTCFL/BORIS; involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Function as transcriptional corepressor by associating with ZHX1. {ECO:0000250; ECO:0000269|PubMed:16357870; ECO:0000269|PubMed:17303076; ECO:0000269|PubMed:18413740; ECO:0000269|PubMed:18567530}.', 'MKGDTRHLNGEEDAGGREDSILVNGACSDQSSDSPPILEAIRTPEIRGRRSSSRLSKREVSSLLSYTQDLTGDGDGEDGDGSDTPVMPKLFRETRTRSESPAVRTRNNNSVSSRERHRPSPRSTRGRQGRNHVDESPVEFPATRSLRRRATASAGTPWPSPPSSYLTIDLTDDTEDTHGTPQSSSTPYARLAQDSQQGGMESPQVEADSGDGDSSEYQDGKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRKAMYHALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNTQPVVNKSKVRRAGSRKLESRKYENKTRRRTADDSATSDYCPAPKRLKTNCYNNGKDRGDEDQSREQMASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFFTSDTGLEYEAPKLYPAIPAARRRPIRVLSLFDGIATGYLVLKELGIKVGKYVASEVCEESIAVGTVKHEGNIKYVNDVRNITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYSRPKEGDDRPFFWMFENVVAMKVGDKRDISRFLECNPVMIDAIKVSAAHRARYFWGNLPGMNRPVIASKNDKLELQDCLEYNRIAKLKKVQTITTKSNSIKQGKNQLFPVVMNGKEDVLWCTELERIFGFPVHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE', 853, 'Q9UBC3; A2A2E2; B4DSM8; B4DSU1; E1P5M6; E1P5M7; E7EN63; E9PBF2;Q9UBD4; Q9UJQ5; Q9UKA6; Q9UNE5; Q9Y5R9; Q9Y5S0;', 'KD00544', 'Homo sapiens (Human)', 'DNMT3B', '#DNA (cytosine-5)-methyltransferase 3B#Dnmt3b#2.1.1.37#DNA methyltransferase HsaIIIB#DNA MTase HsaIIIB#M.HsaIIIB', '-', 'ENSG00000088305', '-'),
(545, 'O01775', 'NEKL-2', 'k', 40504, '', 'MDNYEKVRVVGRGAFGVCWLCRGKNDASHQKVIIKLINTHGMTEKEENSIQSEVNLLKKVQHPLIIGYIDSFIMDNQLGIVMQYAEGGTLERLINDQRAIKDSNMREYFPEKTVLDYFTQILIALNHMHQKNIVHRDLKPQNILMNRRKTVLKLSDFGISKELGTKSAASTVIGTPNYLSPEICESRPYNQKSDMWSLGCVLYELLQLERAFDGENLPAIVMKITRSKQNPLGDHVSNDVKMLVENLLKTHTDKRPDVSQLLSDPLVLPYLISIHCDLGRIEPPPTDKRKPSASLSSRLRTYPTQSTLRPYSLSSNAPTTHLTQLTPMPSHIDSGFFSSGRTSNQRTQSRSQVHSKY', 357, 'O01775;', 'KD00545', 'Caenorhabditis elegans', 'nekl-2', '#NEKL-2 {ECO:0000313|EMBL:CCD64899.1}', '-', '-', '191199'),
(546, 'P22087', 'rRNA 2''-O-methyltransferase fibrillarin', 'k', 33784, 'S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2''-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of ''Gln-105'' of histone H2A (H2AQ104me); a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239). {ECO:0000269|PubMed:24352239}.', 'MKPGFSPRGGGFGGRGGFGDRGGRGGRGGFGGGRGRGGGFRGRGRGGGGGGGGGGGGGRGGGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVEFSHRSGRDLINLAKKRTNIIPVIEDARHPHKYRMLIAMVDVIFADVAQPDQTRIVALNAHTFLRNGGHFVISIKANCIDSTASAEAVFASEVKKMQQENMKPQEQLTLEPYERDHAVVVGVYRPPPKVKN', 321, 'P22087; B5BUE8; O75259; Q6IAT5; Q9UPI6;', 'KD00546', 'Homo sapiens (Human)', 'FBL', '#rRNA 2''-O-methyltransferase fibrillarin#2.1.1.-#34 kDa nucleolar scleroderma antigen#Histone-glutamine methyltransferase', '-', 'ENSG00000105202', '-'),
(547, 'Q5RAN6', 'Nucleoporin SEH1', 'GO:0000777===GO:0051315', 39671, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (By similarity). As a component of the GATOR2 complex; inhibits GATOR1 complex; an inhibitor of the amino acid-sensing branch of the TORC1 pathway (By similarity). {ECO:0000250}.', 'MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNAMAKVQIFEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHILAIATKDVRIFTLKPVRKELTSSGGPTKFEIHIVAHFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILKGNGSPVNGSSQQGTSNPSLGSNIPSLQNSLNGSSAGRKHS', 360, 'Q5RAN6;', 'KD00547', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'SEH1L', '#Nucleoporin SEH1#Nup107-160 subcomplex subunit SEH1', '-', '-', '100172610'),
(548, 'Q32N93', 'Inner centromere protein B', 'GO:0032133', 102938, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Probably acts through association with aurkb or aurkc. Seems to bind directly to microtubules (By similarity). {ECO:0000250}.', 'MNDAECLSHLLQVCSRKTEEFVRTLDTKHMVWLLEIEEEARKMFSSDFNAEPELMPKTPSQKRRRKKRTSILPDENRDPSGRRISRRRSSANWSSSVRRLSVRNQIKANDDSIQEGPAQPKRMTRARAQASIMCPPAVEQALPESPSQLCQKSVQVKISEHERRSAEQKLRESEIEDSEMKTDVQPIPEITKDHISEIMNAAGPPPIPDIPAVPVTPENKSRAAGKLKISGSSTPIQTAAVVDLTCESPRPANELVNEQPLNLSNESATPTGSKSDRRSVRRSLVVRKSSSRRASLVSQFSLVSKRESMTREAVRKSIRQSISKKKAAMETSSTSSQRSCHSSIEMVDDEITIKIRPETAPSETVSEEAPAAESPRSSLRSRAFKKIAISNLSESEEPPRRVTRQMVAVDAEPTPETADDAQNNRRKSYKRAVDELSDDERPSEGECSPPRKKTPSPPCPPSKIVKPPPHMKSFLHTVQKNQFLMMTPGSIGKNITLKSFIKRNTPLKPDPKSEEKERQRLDALRKKEEAELQRKQKIEEGKKRKQEELKLRREDRLRKVLQARERVEQLEEEKKKKFEQKFAQIDEKSEKVREDRMAEEKAKKKTMVKKQEEVECRRKQEEEARKLKAKQMEEEERRHQELLQKKREEEEMERQKKMAEAKRLAEQERERQVFAEKERLRAERERERIEREKALQLQRELERAAQEKEQQRREAEERKKREQQQRLEQERLERLRTEQEVKRLQEEQQRKAKEQAAAAAAPVMNVTVDMQNSPACESYEMTPKSYKVPSVKANADNYGMDLNSDDSTDDESQPRKPIPAWASGNLLAQAVSQQYYKPIDADHMYGTIDSPKLEELFNKSKPRYFKRTSSAVWHSPPLSNRHHLAVGYGLKY', 892, 'Q32N93;', 'KD00548', 'Xenopus laevis (African clawed frog)', 'incenp-b', '#Inner centromere protein B', '-', '-', '398822'),
(549, 'Q19131', 'NPP-5', 'k', 91812, '', 'MTDLFASGDNSSNSFDDSNDEIARKNETAFKYTTIFHTNLSEKLYHELCALAFGEFDIPQGQISPLMWTRLHEIYSEVEMQTRKLPAGSNYSASSQKYANEAVQIASVLSIYTALAHEYDETVEVSLLSKLVVEDVEFRRIYALLLWSEKAISEQQYEKGLGDKVRKLEGIKSSRINSMMALKRPTFGAANAPKDASLDPDAPGTKEDQALEQMAMNVFFQLIRSGETSKAANLAIDLGMGAIGAQLQLHSMLRNPLDIPLEASKQNFGEYKRSRRAKYYQMTQKLIEQSQGSEDDAYWMLISAIRGNIQPMLKAGKSVIEKVWAYANSAVLARILAAEGAMTQETISTLFNVPLTSKSILDELRSEADRTKEVYILLRVIDDMLNDDIEDLYKFANETVGEFVPNDKNCQVNMLALDIFFHLVAVSYASGFEPNDDGNAVIILGFDDLRARSGTSSHKKMAAFYSRFLPEDMKLPEIVETMKAVDSDEEREILAESLKQSDIDFGRCACTLIEQIRKDDKTKVVTLEEQIDHWHWLLIGGEETALAALEECNRLVRKVMLSTPIDESVIRQIIRKALHFEVPKLLSQAVENEATVLSLITDGTLFEQKPGSQLAINKIEHAALEFYGLCSFVDVNNFMITIALKLGLMFKYTPITDDELSMIGGVKRLDNTTAADWEASLRVRARAEQTLREEVLKKRAAEHNTRVGMVQQHLDTVLPMLRGLVNNIGVRPEYFLSPRANGDPMRVHRKEIQEIRNLFLPQFFILLAQAAVRLDDTTNFNDFFTSFNNDLGLDQEWMVFIKAFYAELNLKVE', 813, 'Q19131;', 'KD00549', 'Caenorhabditis elegans', 'npp-5', '#NPP-5 {ECO:0000313|EMBL:CAA91316.1}', '-', '-', '174779'),
(550, 'P17210', 'Kinesin heavy chain', 'GO:0003777', 110399, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent; anterograde transport of mitochondria. {ECO:0000269|PubMed:16717129; ECO:0000269|PubMed:2522352}.', 'MSAEREIPAEDSIKVVCRFRPLNDSEEKAGSKFVVKFPNNVEENCISIAGKVYLFDKVFKPNASQEKVYNEAAKSIVTDVLAGYNGTIFAYGQTSSGKTHTMEGVIGDSVKQGIIPRIVNDIFNHIYAMEVNLEFHIKVSYYEIYMDKIRDLLDVSKVNLSVHEDKNRVPYVKGATERFVSSPEDVFEVIEEGKSNRHIAVTNMNEHSSRSHSVFLINVKQENLENQKKLSGKLYLVDLAGSEKVSKTGAEGTVLDEAKNINKSLSALGNVISALADGNKTHIPYRDSKLTRILQESLGGNARTTIVICCSPASFNESETKSTLDFGRRAKTVKNVVCVNEELTAEEWKRRYEKEKEKNARLKGKVEKLEIELARWRAGETVKAEEQINMEDLMEASTPNLEVEAAQTAAAEAALAAQRTALANMSASVAVNEQARLATECERLYQQLDDKDEEINQQSQYAEQLKEQVMEQEELIANARREYETLQSEMARIQQENESAKEEVKEVLQALEELAVNYDQKSQEIDNKNKDIDALNEELQQKQSVFNAASTELQQLKDMSSHQKKRITEMLTNLLRDLGEVGQAIAPGESSIDLKMSALAGTDASKVEEDFTMARLFISKMKTEAKNIAQRCSNMETQQADSNKKISEYEKDLGEYRLLISQHEARMKSLQESMREAENKKRTLEEQIDSLREECAKLKAAEHVSAVNAEEKQRAEELRSMFDSQMDELREAHTRQVSELRDEIAAKQHEMDEMKDVHQKLLLAHQQMTADYEKVRQEDAEKSSELQNIILTNERREQARKDLKGLEDTVAKELQTLHNLRKLFVQDLQQRIRKNVVNEESEEDGGSLAQKQKISFLENNLDQLTKVHKQLVRDNADLRCELPKLEKRLRCTMERVKALETALKEAKEGAMRDRKRYQYEVDRIKEAVRQKHLGRRGPQAQIAKPIRSGQGAIAIRGGGAVGGPSPLAQVNPVNS', 975, 'P17210; Q9V7L9;', 'KD00550', 'Drosophila melanogaster (Fruit fly)', 'Khc', '#Kinesin heavy chain', '-', '-', '36810'),
(551, 'Q9HGK9', 'Uncharacterized protein C800.13', 'GO:0000776===GO:0000778===GO:1903394===GO:0000780', 54324, '', 'MASHNYETPLKSSSFQHLVGTLSQRRHFTPSRSRYTPRSAQRTVTPHKRRALARRNSLARRRSNVFSATTPRDILRMLSRALAKNPVPSPAESESSERRHTPQTNSQKSQKTPRLSSNKRRTLKNDAKQRNSQSPGTDTSDANLTIQSIEAPRRAPQRLSDFFTPDGRRVSNIRDSLISEKRLENNIDQVQESALSTASSNRLIDLKNDEVPIFRIPLSDYETDDMDDGTPLQRHVATLNQYQSPIFNLGPDILEDEPSYSSRASRSRQSSLSSRLSELPSKRASLEILRRENTFPADPIQEFGEKAYNERELMEEISNFEPLLDDNLLENANEAVNSPVVDAPMDADSALEIPNDEDNGEILNKLKDSPFKKPKRRYSKSSTLVLPETNIRKLANSYSQKKIAGSVIEELTTASELFFKQIANDLSAFADHAHRKTIDTQDVVLLMKRQRKISEKKSLSSLMQQYLSREIAPPAIKRT', 479, 'Q9HGK9; Q9UU65;', 'KD00551', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'SPBC800.13', '#Uncharacterized protein C800.13', '-', '-', '2540915'),
(552, 'Q6AYJ4', 'Meiotic recombination protein REC8 homolog', 'GO:0000778', 67874, 'Required during meiosis for separation of sister chromatids and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome arms by separin during anaphase I allows for homologous chromosome separation in meiosis I and cleavage of REC8 on centromeres during anaphase II allows for sister chromatid separation in meiosis II (By similarity). {ECO:0000250|UniProtKB:Q8C5S7}.', 'MFYYPNVLQRHTGCFATIWLAATRGSRLVKREYLKVNVVKTCEEILNYVLVRVQPPMPGLPRPRFSLYLSAQLQIGVIRVYFQQCQYLVEDIQHILEHLHRAQLRIRIDMEEADLPSLLLPNCLAMMETLEDAPEPFFGTMSVDPTLPSPFDIPQIRHLLEAATPEKIREETLPEATPEPRKPDRTLAMVQSPEVITLQEAEPIRMLRIEGEQDLPEISRGDLDLLIAEEDDAILLEERQRGRLLRQRRASPPLDESKEEPRALEGDGLVSSLSPPAPAQVEGIREPLPDQAFPPEVQKMPGWEPGVLLTEVTPPQELRLPAPPSIEKRPPSPQRPPRRRRRGRQLLFWDKETQISREKFEEQLQTGAHCCEYPVVQPPKRKLMSPAELFRTPTLSGWLSPELLALWTHCAQVPPRMLRQRPQLETEETVEEERVADKEERRKTEALSEIEVLREAQEPSGPLMLSSELSLEVAEEEKSRTSFIPPEERWAWIEERQPEPPALPMLPELPEVPMEMPPGPELLSSEAVLRAVALELQANREPDFSSLVPPLSSRKLASRVFYLLLVLSAQKILLVDQQKPYGRLLIRLGPKFP', 593, 'Q6AYJ4; Q6QQR2;', 'KD00552', 'Rattus norvegicus (Rat)', 'Rec8', '#Meiotic recombination protein REC8 homolog#Cohesin Rec8p', '-', '-', '290227'),
(553, 'P50749', 'Ras association domain-containing protein 2', 'k', 37790, 'Potential tumor suppressor. Acts as a KRAS-specific effector protein. May promote apoptosis and cell cycle arrest. Stabilizes STK3/MST2 by protecting it from proteasomal degradation. {ECO:0000269|PubMed:12732644; ECO:0000269|PubMed:16012945; ECO:0000269|PubMed:19525978}.', 'MDYSHQTSLVPCGQDKYISKNELLLHLKTYNLYYEGQNLQLRHREEEDEFIVEGLLNISWGLRRPIRLQMQDDNERIRPPPSSSSWHSGCNLGAQGTTLKPLTVPKVQISEVDAPPEGDQMPSSTDSRGLKPLQEDTPQLMRTRSDVGVRRRGNVRTPSDQRRIRRHRFSINGHFYNHKTSVFTPAYGSVTNVRINSTMTTPQVLKLLLNKFKIENSAEEFALYVVHTSGEKQKLKATDYPLIARILQGPCEQISKVFLMEKDQVEEVTYDVAQYIKFEMPVLKSFIQKLQEEEDREVKKLMRKYTVLRLMIRQRLEEIAETPATI', 326, 'P50749; A6NIX9; A8K5Z3; Q17S06; Q53HD0; Q6AHZ2; Q8IZA5;', 'KD00553', 'Homo sapiens (Human)', 'RASSF2', '#Ras association domain-containing protein 2', '-', 'ENSG00000101265', '-'),
(554, 'Q6AYJ2', 'Biorientation of chromosomes in cell division protein 1', 'GO:0000777', 18352, 'Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000250}.', 'MADSAGAGAAGQASGPAGGSSGAGGTVNPASLPPGDPQLIALIVEQLKSRGLFDSFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNPAMNKNQLRNGLRQSVVQSGMLEAGVDRIISQVVDPKLNHIFRPQIERAIHEFLAAQKKEAVPAPPPEPEGQDPPAPSQDAS', 173, 'Q6AYJ2;', 'KD00554', 'Rattus norvegicus (Rat)', 'Bod1', '#Biorientation of chromosomes in cell division protein 1#Biorientation defective protein 1#Protein FAM44B', '-', '-', '287173'),
(555, 'P50748', 'Kinetochore-associated protein 1', 'GO:0000777===GO:0005828===k', 250749, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. {ECO:0000269|PubMed:11146660; ECO:0000269|PubMed:11590237; ECO:0000269|PubMed:15824131}.', 'MWNDIELLTNDDTGSGYLSVGSRKEHGTALYQVDLLVKISSEKASLNPKIQACSLSDGFIIVADQSVILLDSICRSLQLHLVFDTEVDVVGLCQEGKFLLVGERSGNLHLIHVTSKQTLLTNAFVQKANDENRRTYQNLVIEKDGSNEGTYYMLLLTYSGFFCITNLQLLKIQQAIENVDFSTAKKLQGQIKSSFISTENYHTLGCLSLVAGDLASEVPVIIGGTGNCAFSKWEPDSSKKGMTVKNLIDAEIIKGAKKFQLIDNLLFVLDTDNVLSLWDIYTLTPVWNWPSLHVEEFLLTTEADSPSSVTWQGITNLKLIALTASANKKMKNLMVYSLPTMEILYSLEVSSVSSLVQTGISTDTIYLLEGVCKNDPKLSEDSVSVLVLRCLTEALPENRLSRLLHKHRFAEAESFAIQFGLDVELVYKVKSNHILEKLALSSVDASEQTEWQQLVDDAKENLHKIQDDEFVVNYCLKAQWITYETTQEMLNYAKTRLLKKEDKTALIYSDGLKEVLRAHAKLTTFYGAFGPEKFSGSSWIEFLNNEDDLKDIFLQLKEGNLVCAQYLWLRHRANFESRFDVKMLESLLNSMSASVSLQKLCPWFKNDVIPFVRRTVPEGQIILAKWLEQAARNLELTDKANWPENGLQLAEIFFTAEKTDELGLASSWHWISLKDYQNTEEVCQLRTLVNNLRELITLHRKYNCKLALSDFEKENTTTIVFRMFDKVLAPELIPSILEKFIRVYMREHDLQEEELLLLYIEDLLNRCSSKSTSLFETAWEAKAMAVIACLSDTDLIFDAVLKIMYAAVVPWSAAVEQLVKQHLEMDHPKVKLLQESYKLMEMKKLLRGYGIREVNLLNKEIMRVVRYILKQDVPSSLEDALKVAQAFMLSDDEIYSLRIIDLIDREQGEDCLLLLKSLPPAEAEKTAERVIIWARLALQEEPDHSKEGKAWRMSVAKTSVDILKILCDIQKDNLQKKDECEEMLKLFKEVASLQENFEVFLSFEDYSNSSLVADLREQHIKAHEVAQAKHKPGSTPEPIAAEVRSPSMESKLHRQALALQMSKQELEAELTLRALKDGNIKTALKKCSDLFKYHCNADTGKLLFLTCQKLCQMLADNVPVTVPVGLNLPSMIHDLASQAATICSPDFLLDALELCKHTLMAVELSRQCQMDDCGILMKASFGTHKDPYEEWSYSDFFSEDGIVLESQMVLPVIYELISSLVPLAESKRYPLESTSLPYCSLNEGDGLVLPVINSISALLQNLQESSQWELALRFVVGSFGTCLQHSVSNFMNATLSEKLFGETTLVKSRHVVMELKEKAVIFIRENATTLLHKVFNCRLVDLDLALGYCTLLPQKDVFENLWKLIDKAWQNYDKILAISLVGSELASLYQEIEMGLKFRELSTDAQWGIRLGKLGISFQPVFRQHFLTKKDLIKALVENIDMDTSLILEYCSTFQLDCDAVLQLFIETLLHNTNAGQGQGDASMDSAKRRHPKLLAKALEMVPLLTSTKDLVISLSGILHKLDPYDYEMIEVVLKVIERADEKITNININQALSILKHLKSYRRISPPVDLEYQYMLEHVITLPSAAQTRLPFHLIFFGTAQNFWKILSTELSEESFPTLLLISKLMKFSLDTLYVSTAKHVFEKKLKPKLLKLTQAKSSTLINKEITKITQTIESCLLSIVNPEWAVAIAISLAQDIPEGSFKISALKFCLYLAERWLQNIPSQDEKREKAEALLKKLHIQYRRSGTEAVLIAHKLNTEEYLRVIGKPAHLIVSLYEHPSINQRIQNSSGTDYPDIHAAAKEIAEVNEINLEKVWDMLLEKWLCPSTKPGEKPSELFELQEDEALRRVQYLLLSRPIDYSSRMLFVFATSTTTTLGMHQLTFAHRTRALQCLFYLADKETIESLFKKPIEEVKSYLRCITFLASFETLNIPITYELFCSSPKEGMIKGLWKNHSHESMAVRLVTELCLEYKIYDLQLWNGLLQKLLGFNMIPYLRKVLKAISSIHSLWQVPYFSKAWQRVIQIPLLSASCPLSPDQLSDCSESLIAVLECPVSGDLDLIGVARQYIQLELPAFALACLMLMPHSEKRHQQIKNFLGSCDPQVILKQLEEHMNTGQLAGFSHQIRSLILNNIINKKEFGILAKTKYFQMLKMHAMNTNNITELVNYLANDLSLDEASVLITEYSKHCGKPVPPDTAPCEILKMFLSGLS', 2209, 'P50748; A7E2C4; B3KSG2;', 'KD00555', 'Homo sapiens (Human)', 'KNTC1', '#Kinetochore-associated protein 1#Rough deal homolog#HsROD#Rod#hRod', '-', 'ENSG00000184445', '-'),
(556, 'P41838', 'Poly(A)+ RNA export protein', 'k', 38626, 'Required for mitotic cell growth as well as for spore germination. Functions in cell cycle progression through trafficking of proteins required for mitosis. Has a role in the mRNA export process. {ECO:0000269|PubMed:15990877; ECO:0000269|PubMed:9301023}.', 'MSLFGQATTSTVSNATGDLKKDVEVAQPPEDSISDLAFSPQAEYLAASSWDSKVRIYEVQATGQSIGKALYEHQGPVLSVNWSRDGTKVASGSVDKSAKVFDIQTGQNQQVAAHDDAVRCVRFVEAMGTSPILATGSWDKTLKYWDLRQSTPIATVSLPERVYAMDCVHPLLTVATAERNICVINLSEPTKIFKLAMSPLKFQTRSLACFIKGDGYAIGSVEGRCAIQNIDEKNASQNFSFRCHRNQAGNSADVYSVNSIAFHPQYGTFSTAGSDGTFSFWDKDSHQRLKSYPNVGGTISCSTFNRTGDIFAYAISYDWSKGYTFNNAQLPNKIMLHPVPQDEIKPRPKKGR', 352, 'P41838;', 'KD00556', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rae1', '#Poly(A)+ RNA export protein', '-', '-', '2539741'),
(557, 'P70478', 'Adenomatous polyposis coli protein', 'GO:0000776', 310533, 'Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity). {ECO:0000250}.', 'MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTELETEASNMKEVLKQLQGSIEDETMTSGQIDLLERLKEFNLDSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRAFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRAAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRVRQLLQSQAAEAERSSQSKHETASHEAERQLEGQGVAESNLATSGSGQSSAARVDHETAGVLSSSGTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEQGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMHGLTDDHYSVTLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQNLYGDYVFDASRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLSTYHSATENPGTSSKRGLQLSATAAQIAKVMEEVSALHTSQDDRSPASAAELHCVAEERTAARRSSASHTHPNTHNFAKSESSNRTCSMPYAKVEYKRSSNDSLNSVTSSDGYGKRGQMKPSVESYSEDDEGKFCSYGQYPADLAHKIHSANHMDDNGGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHVIEDEIKQNEQRQSRSQNTNFPVYSENTDDKHLKFQQHFGQQECVSPYRSRGTNGSETNRMGSSHAVNQNVNQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKHHVDQPIDYSLKYATDISSSQKPSFSFSKTPSVQGTKTEHNSPSSEAASAPSSNAKRQSQLHPSSAQRNGQTPKGTACKVPSINQETMQTYCVEDTPICFSRCSSLSSLSSAEDEIGCDQTTQEADSANTLQIAEIKENDVTRSAQDPASDVPAVSQSTRTKPSRLQASGLASESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLVFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIVSPSDLPDSPGQTMPPSRSKTPPPPPPPQPVQTKREVPKTKVPAAEQREGGPKQTAVSAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETEPEQPEESNENQDKEVEKPDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKLAQTASKLPPPVARKPSQLPVYKLLPSQSRLQAQKHVSFTPGDDVPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGDGVRASVQSGEFEKRDTIPTEGRSTDEAQRGKVSSIAIPDLDGSKAEEGDILAECINSALPKGRSHKPFRVKKIMDQVQQASMTSSGTNKNQIDTKKKKPTSPVKPMPQNTEYRTRVRKNTDSKVNVNTEETFSDNKDSKKQSLKNNPKDLNDKLPDNEDRVRGGFTFDSPHHYAPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKGKESKDSEAKVTCHTEPSSSQQSARKAQASTKHPVNRGPSKPLLQEQPTFPQSSKDVPDRGAATDEKLQNFAIENTPVCFSRNSSLSSLSDVDQENNNNEETGPVRDAEPANAQGQPGKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLRECISSAMPKKRRPSRLKGEGEWQSPRKVGSVLAEDLTLDLKDIQRPESEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAAACLSRQASSDSDSILSLKSGVSLGSPFHLTPDQEEKPFTSHKGPRILKPGEKSTLEAKKIESENKGIKGGKKVYKSLITGKIRSNSEISSQMKQPLQTNMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGPVATTSPRGTKPAVKSELSPITRQTSHISGSNKGPSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISTPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLSKQTGLSKNASSIPRSESASKGLNQMNNSNGSNKKVELSRMSSTKSSGSESDRSERPALVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSVQAGGWRKLPPNLSPTIEYSDGRPSKRHDIARSHSESPSRLPVNRAGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSVPGPRQMKENQVPTKGTWRKIKESEISPTNTVSQTTSSGAASGAESKTLIYQMAPAVSRTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSISEKGNPSIKDSKDTQGKQSVGSGSPVQTVGLENRLNSFIQVEAPEQKGTETKAGQGSPAPVAETGETCMAERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVGSSTKKRDSKTDSTESSGAQSPKRHSGSYLVTSV', 2842, 'P70478;', 'KD00557', 'Rattus norvegicus (Rat)', 'Apc', '#Adenomatous polyposis coli protein#Protein APC', '-', '-', '24205');
