INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1098, 'P15056', 'Serine/threonine-protein kinase B-raf', 'c;k', 84437, 'Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron. Phosphorylates MAP2K1; and thereby contributes to the MAP kinase signal transduction pathway. {ECO:0000269|PubMed:21441910}.', 'MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH', 766, 'P15056; A4D1T4; B6HY61; B6HY62; B6HY63; B6HY64; B6HY65; B6HY66;Q13878; Q3MIN6; Q9UDP8; Q9Y6T3;', 'KD01098', 'Homo sapiens (Human)', 'BRAF', '#Serine/threonine-protein kinase B-raf#2.7.11.1#Proto-oncogene B-Raf#p94#v-Raf murine sarcoma viral oncogene homolog B1', 'BIOMD0000000146,Hatakeyama2003_MAPK;', 'ENSG00000157764', '-'),
(1099, 'Q5FWP9', 'Centrosomal protein cep57l1', 'GO:0000776===GO:0000777===GO:0008608===SCL===c;k', 55108, 'Required for spindle microtubule attachment to both kinetochores and centrosomes. Also functions to tether minus-ends of spindle microtubules to centrosomes. May act by forming ring- like structures around microtubules; or by serving as a cross- linker or scaffold at the attachment site. {ECO:0000269|PubMed:17803911}.', 'MESVSKESYLPSFHQFPLCASLSEFESASSKETQSSALKNISPHPYDILQAPNSRALISALKTLQNKICRLESEKTHARDRLTNLSRAAGEHKKVLESEKRSAEWAAQEATSQKNDVAMQLNNAEQRCSLLEKQLDYMRKMMENADIQNNPIHQIPAQKEQKDMLEMQSKLQKLEVLENECLRLKATHKSSENKIQFLEEKLSVEEQERKALQDKAAQVQTSLEVNRILLSSASSQNSTQRKVKKKKQSKQKNAISKEPSSKEPLSKEPPSKCFFPKAGELPFVAGKSTTSSHSLSANVQNMLHMMKHQSPRVSQKDPKTVEHKPSILPGGSRSIPTRLMSSSTGDTLSDILLALQDELGQMSFEHQELLKHIDETKNTDMREDLERELDYLVKQMEIKSDQIIKLKRHQLNVAKLKKTAKKQPRPPSTTKPAEDEQNIGATDPCTPRNKGNLANGTGTPNSKASLELLKSVRKIQMTLKKDDIMWEK', 488, 'Q5FWP9;', 'KD01099', 'Xenopus laevis (African clawed frog)', 'cep57l1', '#Centrosomal protein cep57l1#Centrosomal protein 57kDa-like protein 1#Centrosomal protein of 57 kDa#Cep57#XCep57#Cep57-related protein#Cep57R', '-', '-', '734283'),
(1100, 'Q02647', 'Dynein light chain 1; cytoplasmic', 'GO:0005868', 10441, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 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. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}.', 'MSDENKSTPIVKASDITDKLKEDILTISKDALDKYQLERDIAGTVKKQLDVKYGNTWHVIVGKNFGSYVTHEKGHFVYFYIGPLAFLVFKTA', 92, 'Q02647; D6VT54;', 'KD01100', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DYN2', '#Dynein light chain 1; cytoplasmic', '-', '-', '852034'),
(1101, 'A4IGM9', 'Aurora kinase B', 'GO:0034501===GO:0032133', 41390, '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 (By similarity). {ECO:0000250}.', 'MSYKENLNPSSYTSKFATPSSATAAQRVLRKEPYVSTFTTPSDNLLAQRAQLARITPSASSSVPGRVAVSMDASSQNTALAELPKRKFTIDDFDIGRPLGKGKFGNVYLARDKQNKFIMALKVLFKSQLEKEGVEHQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHGRFDEQRSATFMEELADALQYCHERKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCFEFLVGMPPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQRLPLKGVMEHPWVKANSRRVLPPVFQSSSK', 360, 'A4IGM9;', 'KD01101', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'aurkb', '#Aurora kinase B#2.7.11.1#Aurora/IPL1-related kinase 2#AIRK2#XAIRK2#Serine/threonine-protein kinase 12 {ECO:0000250|UniProtKB:Q96GD4}#Serine/threonine-protein kinase aurora-B#xAurora-B', '-', '-', '549613'),
(1102, 'Q7TSP2', 'Kinesin-like protein KIF15', 'GO:0003777', 159540, 'Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. {ECO:0000250}.', 'MAPGCKSELRNVTNSHSNQPSNEDDAIKVFVRIRPAEEGARSADGEQSLCLSVLSQTALRLHSNPDPKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSDSDNFSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEVYNEQIYDLLDSASVGLYLREHIKKGVFVVGAVEQVVASAAEAYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSEAVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLREQLSQFTSGQLTPGSSLARDKEKANYMEYFLEAMLFFKKSEQEKKSLVEKITQLEDLTLKKEKFIQSNKMIVKFREDQIMRLERLQKEARGSFLPEEQDRLLSELRDEIRTLREQVEHHPRLAKYAMENHSLREENRKLKLLAPVKRAHELDAQAIARLEQAFSEVSSTETNDKGLQGLPPKAIKEPSFFTSTEKLKVQLLQIQTELNNSKQEYEEFKELTRKKQLELESELQSLQKANLNLENLLEATKVCKRQEVSQLNKIHAETLKIITTPTKAYQLCSRLVPKSSPEVGSFGFLRSQSAPDNDILNEPVPPEMSEQALEAISEELRTVQEQLSVLQVKLDEEEHKNLKLQQNVDRLEHHSTQMQELFSSERSDWSKQQQDYLTQLSDLEKQLQDAQTKNDFLKCEVHDLRIVLNSADKELSLVKLEYSTFKESQEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKFEVDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSSKEILKALETVRQEKQEEMARCEKQMAKVQELEESLLAAENVVSCLEKSRESDKELVTNLMNQIQELRTSAGEKSEAIDTLKQELQDISCKYTAAVADKEESKELIRRQEVDILELKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQEKEEVEQKKSEYNLKMKQLEHVMGSAPEYPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKMSLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLESQQLRERTWLLQTQLDDMKRQGESSSQSRPDSQQLKNEYEEEIIRERLAKNKLIEEMLKMKTDLEEVQSALDSKEKFCHRMSEEVERTRTLESRAFQEKEQLRSKLEEMYEERERTCQEMEMLRKQLEFLAEENGKLIGHQNLHQKIQYVVRLKKENIRLAEETEKLRAENVFLKERKKE', 1385, 'Q7TSP2; Q7TN17;', 'KD01102', 'Rattus norvegicus (Rat)', 'Kif15', '#Kinesin-like protein KIF15#Kinesin-like protein 2', '-', '-', '353302'),
(1103, 'Q9LJN8', 'Mitotic checkpoint protein BUB3.1', 'GO:0000776===GO:0000777===GO:0005828', 37874, '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. 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 (By similarity). Essential for gametophyte development. {ECO:0000250; ECO:0000269|PubMed:18508582; ECO:0000269|PubMed:19710914}.', 'MTTVTPSAGRELSNPPSDGISNLRFSNNSDHLLVSSWDKRVRLYDVSTNSLKGEFLHGGAVLDCCFHDDFSGFSVGADYKVRRIVFNVGKEDILGTHDKAVRCVEYSYAAGQVITGSWDKTVKCWDPRGASGPERTQVGTYLQPERVYSMSLVGHRLVVATAGRHVNIYDLRNMSQPEQRRESSLKYQTRCVRCYPNGTGYALSSVEGRVAMEFFDLSEAAQAKKYAFKCHRKSEAGRDIVYPVNSIAFHPIYGTFATGGCDGFVNIWDGNNKKRLYQYSKYPTSISALSFSRDGQLLAVASSYTFEEGEKSQEPEAIFVRSVNEIEVKPKPKVYPNPAA', 340, 'Q9LJN8;', 'KD01103', 'Arabidopsis thaliana (Mouse-ear cress)', 'BUB3.1', '#Mitotic checkpoint protein BUB3.1#Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 3.1', '-', '-', '821496'),
(1104, 'O88447', 'Kinesin light chain 1', 'GO:0003777', 61450, '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.', 'MYDNMSTMVYIKEEKLENVTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSSMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQNVRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDSDSSKEPLDDLFPNDEDEPGQGIQHSDSSAAAARQGYEIPARLRTLHNLVIQYASQGRYEVAVPSCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALGIYQTKLGPDRTPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEAEFGSVDDENKPIWMHAEEREECKGKQKDGSAFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPESMEKRRSRESLNMDVVKYESGPDGGEEA', 541, 'O88447;', 'KD01104', 'Mus musculus (Mouse)', 'Klc1', '#Kinesin light chain 1#KLC 1', '-', '-', '-'),
(1105, 'O88448', 'Kinesin light chain 2', 'GO:0003777', 66662, '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.', 'MATMVLPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLASHEAGEAEPGSQERCLLLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEMLPQEEKGDVPKDSLDDLFPNEDEQSPAPSPGGGDVAAQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGENKPIWMHAEEREESKDKRRDRRPMEYGSWYKACKVDSPTVNTTLRTLGALYRPEGKLEAAHTLEDCASRSRKQGLDPASQTKVVELLKDGSGRGHRRGSRDVAGPQSESDLEESGPAAEWSGDGSGSLRRSGSFGKLRDALRRSSEMLVRKLQGGGPQEPNSRMKRASSLNFLNKSVEEPVQPGGRVFLTAAL', 599, 'O88448;', 'KD01105', 'Mus musculus (Mouse)', 'Klc2', '#Kinesin light chain 2#KLC 2', '-', '-', '-'),
(1106, 'O88445', 'Aurora kinase C', 'GO:0032133===GO:0000780===k;m', 32907, '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. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB; AURKC phosphorylates histone H3 at ''Ser-10'' and ''Ser-28''. Phosphorylates TACC1; another protein involved in cell division; at ''Ser-228''. {ECO:0000269|PubMed:11879579; ECO:0000269|PubMed:21613325}.', 'MEPSTSTRKHFTINDFEIGRPLGRGKFGRVYLARLKENHFIVALKVLFKSEIEKEGLEHQLRREVEIQAHLQHRNILRLYNYFYDDTRIYLILEYAPGGELYKELQRHQKLDQQRTATIIQELSDALTYCHEKKVIHRDIKPENLLLGLNGEVKISDFGWSVHTPSLRRKTMCGTLDYLPPEMIAQKPYNEMVDLWCIGVLCYELLVGKPPFESSTSSETYRRIRQVDFKFPSSVPAGAQDLISKLLRYHPSERLSLAQVLKHPWVREHSRRVLPPCVHGAS', 282, 'O88445; Q9JLC2;', 'KD01106', 'Mus musculus (Mouse)', 'Aurkc', '#Aurora kinase C#2.7.11.1#Aurora 3#Aurora/IPL1-related kinase 3#ARK-3#Aurora-related kinase 3#Aurora/IPL1/Eg2 protein 1#Serine/threonine-protein kinase 13#Serine/threonine-protein kinase aurora-C', '-', '-', '-'),
(1107, 'Q17635', 'Kinetochore protein ndc-80', 'GO:0000778===GO:0051315===GO:0031262===SCL===k', 68913, '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:14522947}.', 'MFGDRRKTGGLNLNGRASIAITPTKRFTDYTGSTSVRKTDARPSLSQPRVSLFNTKNSSVAPRDVKSLVSLNGSKIYNFLVEYESSDAPSEQLIMKPRGKNDFIACFELIYQHLSKDYEFPRHERIEEEVSQIFKGLGYPYPLKNSYYQPMGSSHGYPHLLDALSWLIDIIRINSAVSEDTQNILFGDFMEQGKAQEKTLNYAWMTSTFRDYTNDRKAAENPSSSYWDDTKHRLRKYFEQSNEFEDMTKTAASALEMLNYECDEIEADKGNEASLKEEISRIRDDIRKAKDYLEQNLHVKQHMEKELAMVKSEQEEKISENEKVQKMVDDLKNKIELQKQIHGLTGKEVRQMNLDNNKDKEVVLEIQSELDRLSKETWKLKDEDFFKEQKSKFIHLAEQIMKILSGLNIQMNLEPLRAPTNERDLKDYWETLNKIWVPEISRQLHQRKLELETEQSRFSNKAVTAEERIQIQSETLCEAKKNEAREERIRRNERDSWKDARKHIEQRYEQLLNEKEVLLKQMKLDGSLEKEIEDETARMSATGEEHIQKRSQLEAGIRQILDLMVVEIAEIENKKIGFHVQCAGIEKAVL', 590, 'Q17635; Q23107;', 'KD01107', 'Caenorhabditis elegans', 'ndc-80', '#Kinetochore protein ndc-80#CeNDC-80#Hec1 homolog', '-', '-', '177873'),
(1108, 'Q7ZYL5', 'Kinesin-like protein KIF22-B', 'GO:0003777', 73168, 'Kinesin family member 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}.', 'MVLTGPPQRESVSMVKRVSMLDQHKKSSCARVRVAVRLRPYMEEKEEDKVPTACVRGLDSHSLEIVNWRNQLETMQYQFDAFYGDSASQREIYMGSVCHILPHLLIGQNASVFAYGPTGAGKTHTMLGNPDQPGVIPRAVRELLQMTRMAASAPENENWTYTITMSYVEIYQEKVMDLLEPKNKDLPIREDKDHNILIPGVTLKTINSFGDFDEHFIPASQNRTVASTKLNDRSSRSHAVLLIKVQKSQQVAPFRQLIGKLYLIDLAGSEDNRRTGNQGIRLKESGAINSSLFTLSKVVDALNQGLPRIPYRDSKLTRLLQDSLGGSAHSVMITNIAPEQTYYFDTLTALNFAAKSKQIINKPFSRETTQTVAQPAMKRPREEAEATTSSRQRKKSKTDSTESSPNSSMESTGKRKLNLASLDSAVVERLLKLDKILTEKGKKEAQLLSTPKRERMALLKKWEESQMEIERLKEKQKELEQKAMEAEARLEKSNNSDLSDSSVSENTFRAPLRGRNTSTAKVKKVLRVLPMQGNSQLQSTIEEGIPVFEKKKKKQVTCDGHENQPTWEMNMRTDLLESGKERILKLLNTGSVKELKSLQRIGDKKAKLIIGWREVNGLFKNVEELECLEGISAKQVSSFIKANILSSISS', 650, 'Q7ZYL5; Q6GPG0; Q9I9A8;', 'KD01108', 'Xenopus laevis (African clawed frog)', 'kif22-b', '#Kinesin-like protein KIF22-B#Chromokinesin kid-B#Xkid-B', '-', '-', '100337511'),
(1109, 'P34278', 'Kinetochore null protein 1', 'GO:0000776===GO:0051382===GO:0000940===k', 113231, 'Proposed to be part of the KMN network incorporating the MIS12 complex and NDC80 complex that is required for establishing the kinetochore-microtubule interface that aids in chromosome segregation during meiotic and mitotic cell division. Appears to function downstream of hcp-3 (CENP-A) and hcp-4 (CENP-C) in the kinetochore assembly hierarchy. Has a role in the correct localization of spdl-1 and the RZZ complex that is composed of rod-1; czw-1 and zwl-1. {ECO:0000269|PubMed:14522947; ECO:0000269|PubMed:15371340; ECO:0000269|PubMed:15767665; ECO:0000269|PubMed:16273096; ECO:0000269|PubMed:17129783; ECO:0000269|PubMed:18070910; ECO:0000269|PubMed:18765790}.', 'MSMEPRKKRNSILKVRQAVETIEETVMNSGPSSTTTNRRVSFHNVKHVKQYDRDHGKILDATPVKEKITDTIGSDGILTPRGGNMDISESPACTSSFQVFGGGNLDKTMDMSLETTINENNETARLFETTRDPTLLYEKIVETTTKVTERIVSMPLDDTLAMFNTTNQEDKDMSVDRSVLFTIPKVPKHNATMNRTIPMDLDESKAAGGQCDETMNVFNFTNLEAAEMDTSKLDENNTMNAIRIPINSNVMPVDMDITEHHTLIEEKKNDTFGPSQLMDISAPQVQVNDTLAIFNSPRDICNKGLGVPQNLINIASNVVPVDMDITDQAVLNAEKKNDQFETSQLMDISIPKVLVNDTMAMFNSPKHVSKSSMDLEKTIEAADKSTKYPSIADEVEDLDMDMDITEQQPCEAGNQQNDGLQLQKEDLMDISVIRDSPAVNDTMAVFQSPARVKIGANNSIIDSQKSIVFGDEMSIDETQNDGTLTLPKSNVEVTTTNDVYTSLERQEENASENVSMINESSVHSEIDKKSFMLIEEERAFMHSSMIDVAQKLEDDGSSKTPVILASQSASLATKEPSALHNSSATLNNSMELDNNTLLKTMQITTCEDISMVHESIAVELNSNKEQEQFGDETLQKNDTSNTGANFTFQGHNETSQIMNNVDSEAVNTSKISTYSAFNLSINQSISKRRRSLLNSARESPRRVALENSIMSMNGQTMEALTEYRQNKTMQTSQDSMPSMSLNDSGRDILAMNTSVRSPHLNSSKTAAPGTPSLMSQNVQLPPPSPQFEMPDFDPAVVNVVYLTSEDPSTEQHPEALKFQRIVENEKMKVQHEIDSLNSTNQLSAEKIDMLKTKELLKFSHDEREAIMIARKDAEIKFLELRLKFALEKKIESDQEIAELEQGNSKMAEQLRGLDKMAVVQKELEKLRSLPPSREESGKIRKEWMEMKQWEFDQKMKALRNVRSNMIALRSEKNALEMKVAEEHEKFAQRNDLKKSRMLVFSKAVKKIVNF', 1010, 'P34278;', 'KD01109', 'Caenorhabditis elegans', 'knl-1', '#Kinetochore null protein 1', '-', '-', '176164'),
(1110, 'P14785', 'G2/mitotic-specific cyclin-A', 'k', 56152, 'Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the CDC2 and CDK2 protein kinases to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.', 'MASFQIHQDMSNKENPGIKIPAGVKNTKQPLAVIGGKAEKNALAPRANFAVLNGNNNVPRPAGKVQVFRDVRNLNVDENVEYGAKKSNVVPVVEQFKTFSVYEDNNDTQVAPSGKSLASLVDKENHDVKFGAGQKELVDYDLDSTPMSVTDVQSPMSVDRSILGVIQSSDISVGTETGVSPTGRVKELPPRNDRQRFLEVVQYQMDILEYFRESEKKHRPKPLYMRRQKDISHNMRSILIDWLVEVSEEYKLDTETLYLSVFYLDRFLSQMAVVRSKLQLVGTAAMYIAAKYEEIYPPEVGEFVFLTDDSYTKAQVLRMEQVILKILSFDLCTPTAYVFINTYAVLCDMPEKLKYMTLYISELSLMEGETYLQYLPSLMSSASVALARHILGMEMWTPRLEEITTYKLEDLKTVVLHLCHTHKTAKELNTQAMREKYNRDTYKKVAMMESVEMSKDDFDQLCEAYNCKQKEDEHQQPDINTKSNVNLFYKF', 491, 'P14785; Q8IGR7; Q9VTP6; Q9VTP7;', 'KD01110', 'Drosophila melanogaster (Fruit fly)', 'CycA', '#G2/mitotic-specific cyclin-A', '-', '-', '39340'),
(1111, 'Q5M856', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 26189, '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}.', 'MGEDELAAFEKSINEFGDKFRYRLSDNRSQVLGLKDAFKDSIRALSEKLSLKLKEEERMAEMILEYKNQLCKQNKLIQEKKDNVLKMIAEVKGKGQEVEVLTANIQDLKEEYARKKETISTANKANEERLKRLQKSADLYRDRLGLEIRKIPGDKLQFIFTSIDPKNPESPFMFSLSINEAKEYEVSDCSPHLECLAEFQEKVRKTNNFSAFLANVRKAFIAKVHN', 226, 'Q5M856;', 'KD01111', 'Rattus norvegicus (Rat)', 'Spc25', '#Kinetochore protein Spc25', '-', '-', '295661'),
(1112, 'Q14683', 'Structural maintenance of chromosomes protein 1A', 'GO:0000776===GO:0000777===GO:0003777===SCL===c;k', 143233, 'Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is 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. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM; or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000269|PubMed:11877377}.', 'MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ', 1233, 'Q14683; O14995; Q16351; Q2M228;', 'KD01112', 'Homo sapiens (Human)', 'SMC1A', '#Structural maintenance of chromosomes protein 1A#SMC protein 1A#SMC-1-alpha#SMC-1A#Sb1.8', '-', 'ENSG00000072501', '-'),
(1113, 'Q5EA49', 'Protein MIS12 homolog', 'GO:0051382===GO:0000444', 24159, 'Part of the MIS12 complex; which may be fundamental for kinetochore formation and proper chromosome segregation during mitosis. {ECO:0000250}.', 'MSVDPMTYEAQFFGFTPQTCMLRIYIAFQDYLFEVMQAVEQVILKKLDGIPDCAISPVEIRKCTEKFLCFMKGRFDNLFGKMEQLFLQLILRIPPNVLLPEDKSQETQSYSEEEFHFLQKEIEQLQEKYKTELCTKQALLAELEEQKIVQAKLKQTLSLFDELENVGRDHGASDFREGLVFLIQNSRKLQNIRENVEKEGKRLKIS', 206, 'Q5EA49;', 'KD01113', 'Bos taurus (Bovine)', 'MIS12', '#Protein MIS12 homolog', '-', '-', '767858'),
(1114, 'P45481', 'CREB-binding protein', 'GO:0000940', 265494, 'Acetylates histones; giving a specific tag for transcriptional activation. Also acetylates non-histone proteins; like NCOA3 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1 in the presence of EP300. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2- ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. {ECO:0000250|UniProtKB:Q92793}.', 'MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKSPLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQSMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPAGFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINNGMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSASLAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLGNPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL', 2441, 'P45481; E9QPH4;', 'KD01114', 'Mus musculus (Mouse)', 'Crebbp', '#CREB-binding protein#2.3.1.48 {ECO:0000250|UniProtKB:Q92793}', 'BIOMD0000000397,Sivakumar2011_WntSignalingPathway;', '-', '-'),
(1115, 'O14645', 'Axonemal dynein light intermediate polypeptide 1', 'GO:0003777', 29662, 'May play a dynamic role in flagellar motility.', 'MIPPADSLLKYDTPVLVSRNTEKRSPKARLLKVSPQQPGPSGSAPQPPKTKLPSTPCVPDPTKQAEEILNAILPPREWVEDTQLWIQQVSSTPSTRMDVVHLQEQLDLKLQQRQARETGICPVRRELYSQCFDELIREVTINCAERGLLLLRVRDEIRMTIAAYQTLYESSVAFGMRKALQAEQGKSDMERKIAELETEKRDLERQVNEQKAKCEATEKRESERRQVEEKKHNEEIQFLKRTNQQLKAQLEGIIAPKK', 258, 'O14645; A8K387; B4DHN6; Q05BL9; Q5HYE2; Q5TGH0; Q7L0I5;', 'KD01115', 'Homo sapiens (Human)', 'DNALI1', '#Axonemal dynein light intermediate polypeptide 1#Inner dynein arm light chain; axonemal#hp28', '-', 'ENSG00000163879', '-'),
(1116, 'O42860', 'Mitotic checkpoint protein bub3', 'GO:0000778===GO:1990298===SCL===k', 35804, 'Involved in cell cycle checkpoint enforcement. Involved in recruitment of checkpoint proteins bub1 and mad3 to the kinetochores; ensuring correct spindle checkpoint function. {ECO:0000269|PubMed:15509783}.', 'MNFSKTLLKNSKDGISSVIFSPSVKNELIAGCWDGSLLHYQISENPELLGKYDLSSPILSLEYTDEKTALVGNLDGTVTTLDLNTRNHEFLGNHGKGVSCISKLRLENCFISGSWDKSFRVWDVRVKQPVEGQDIGKKIFASSSRDNILVLGCSERENLVYDIRNLKLPFQRRPSSFKYMTRSVCCNQNFEGFVSSSIEGRTSVEYINPSQEAQSKNFTFKCHRQIQKDYDIVYPVNDLKFHPIHQTLATAGGDGVVAFWDIQVRKRLRVLNPSKINISSISFNVDGSMLAIATCAQEEAAGNIYVHALESNFAAPKLKS', 320, 'O42860;', 'KD01116', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'bub3', '#Mitotic checkpoint protein bub3', '-', '-', '2541856'),
(1117, 'Q5R5Z2', 'PHD finger protein 6', 'GO:0000777', 41290, 'Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000250}.', 'MSSSVEQKKGPTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMVYCRKHKKTAHNSEADLEESFNEHELEPSSPKSKKKSRKGRPRKTNFKGLSEDTRSTSSHGTDEMESSSYRDRSPHRSSPSDTRPKCGFCHVGEEENEARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMKCTLCSQPGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNHSGNDERDEEDEERESKSRGKVEIDQQQLTQQQLNGN', 365, 'Q5R5Z2;', 'KD01117', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'PHF6', '#PHD finger protein 6', '-', '-', '100174671'),
(1118, 'Q20849', 'ROD-1', 'k', 233823, '', 'MGRLGEAKAVDLEAETSTVGLYDVCTVGRILPLLNEMSIDKKSPAWKLKPKSNERFLVLASCSDLAVFSLGEKSDYSFNTGLGGAITDFEILGSSSFFVGVIEHRRIVILSLDKQEIYLNEPAPHEIDFVVCHTTSSVCQLIFGSRSDNWHTITLPGDVAASKETNRFENWHRDQIQEFFHQAMGKTVSKSVDMSKVAGDITLISNGPLQTFASIDQQRGIHWCGLVESEFEVIGMEKQFLQVRDGGRFSLHLDTDGWIHVFDSLVSSFCHEFDMKMSPDDKILDFVIIDKNEVEVPKMFAILVLPRDGDSTKMMIYDRLNKDNCFALDSSTSTTLFAYGGSDRVLIAVEELENSLADEQDGSQIVVRQVSQSRPEMRFESLLKNNRFEEAEKFAMAFMLDVQKVYKGHVHYLMDSCDESDESFETLMTKMGQIQDHNMVAETYFTLVGMSRRCDRIRTYLTHAKKRRITDLDILKMIEALCYTWGTYRIIAGPEENEPSRPQVNETIWDLFVEALHDANPWIEIYNEFISDAQFTQARVIFSRHGKSITDYMCDDEENTISRLETLFRMFIDAISSDISKWSNVIEHVTTDILPACVMITEELIPCLESLITSLISLLEYRDSTNWPENAIKAASSYDTMTKILSNNGNTPATQCILVMYGSKLGSSAGNKPSSMSRIKKIYYDLIELKRLKDVYECSISFSVFQNMSSEQICHKILQNALANPNMTHAKIEKFVKPFMAERHLDQEQTIVNYIQMMSGAAVTNANLFGWEKQCVQLCASLMDETRRCCSIISIASTAKIPWPAELNEAVEKILASRTLLRSEIEQMHLVCKRTELYKMLSSYGFSRQDIELLTTPDSNMDIILTIRCMLAHREKASRFVDVIKLVDLLKAMQGSSQPRTLRIEYVQSFAIIHMMSHQDVTISIINYIDSLGDRERVKTISLVFSFIECVANAPATGDNVLEREKILGVGEELMSHYTCRDNNFNDPERRLKDELVLLREVQKTETKAVLLSELKDEDWQRRFLERLIESNSSMSLNLGRCSYMGISPEHLIEMILTKATVENDMDTIVDSITNYVEFINSLTDSSREMLEPIVQILSWITFRLPKLLPNETEMARADYIAFVVKRIGRVVRETLRRFSFDVISDDLDYLLQLEAFYHLGEHIIKQSLRGQENENEKQEMFRSDDDTFLPTDSSNPFSNQSSLRIFEFKRPLGTFDFSNDPALFEGVQGVLALAMVAPSVARPYDSEISPDDANEFRSSWEQLNMFLAMHSQDLLDISARVFAGSLKCWAGEYLQGIVEMEQPILSVVERMLQQKKFDFWHAVTLLGGIPLERLDRAIIDLQKRQGVRSSTKATIQYLQLAFVMSLLARNMEKVPTIVSAYEQKYLVKKLAEEGIRVSITQDFVDKVLQQAIDLRQPLSPLRLHDYVKKYVEKLIRNSKISVGEYMVRYATLLIRKASVAGRHTDREIRKEEIEKYIEAARIALRIAEEEDASCICNYLHCLLYVVCPYNYEVIQFIVTSYGKYATETVEIEFNKNLKSIMAFLWAYQRTNHISNEESIWFTKRESVLMKDEKEFEKTGRMLDPFGHSLRVVYEDDGSNMSDSYNSDLALSSDAMVYERNSVIISDLPSLAEQYLPFHAFLLRKKEEIDEIVMGIVKAELSIFNVPIWQTFLREVSWLSSRFSRSQLLSSAIFAHANKYAKFGKSLPDGERNVIYELLNSASQRHVVVSTIALLFKRIILSDVKIELLQMGVNISERWTSDLTGEEQQEMEEQSARLKDGIAKFSTELELKKNGLYNEKTADNIENVSELCSLIYNEMVQWDDSRDVLKKCQVVDKIAKANGLDLTALHEQLVFSWVEDTQTIISINHVDMNESIGGTSFLDHKDETDDQNDLRIPLFDGILDKVVVLCQRIDKKRLLTRLGSILMRGGRKATGGYTAVVRATCIILRSFTDTEVSELLSGADMFALCSTLENQLYERLFEKAEVKGDCKTDKMQLIKSLLQCPSRTHPMTALIACLIIDHEFKDPKRDISLGWDVGCVPVSANSSNS', 2049, 'Q20849;', 'KD01118', 'Caenorhabditis elegans', 'rod-1', '#ROD-1 {ECO:0000313|EMBL:CCD69392.1}', '-', '-', '177520'),
(1119, 'Q95XP9', 'Protein zwilch homolog', 'GO:0000777', 71096, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. {ECO:0000250}.', 'MPLTIEQLKQYNEKMAAKGEEDDAPAPVLLLDKYRVRVLPLTSIPFVMNHSSVSQLSLSSEDVLVVDFPSKGTGSGAGKAEKKMIFKKKIEPMEDSFEDKENVNEGGPLMTSFLTLEKLRKGMVGDVEIIGYECETSFFDANPIPLSDGVSLQRYIRLNCSEHFSPSISTLPVWISTTSSKFPSICWLAAGRTNRNVQFAAATRVLGHFNNENSERVVKQLNQACGTSQLNKYRAVYEEIRKIATENRPAPGEVTIDVRWSTKSTLVLLEHPDNAADCTIKIDLGWGDKRFFVDDEIFEQLFFVLNLADVLANPDNEVIFPMAPPANFDDLVQEMDALVEASSREDNVFVSNENFRGGDITDKVWNIVRKCNDVKQVTLLFRNFLQALAYGKIKSHAQERNKSHLASLIRISKSSEFKIPVLERLSTIDMMMEIGVESLRRRVIDIFSSQLLYPSDELEFILQTCENDLPAGNGAMNSAAISLLPITMALATANRIYELLNEKDHVILPDLTRRILQKYTASMIEKSRRGETETEYTFETTLPLLRMYKEGFMSKRPCIWTCENSNTVGANVQARVLTSLELQPSLEHINRLVNDSRPVWTATEEKPAMIKDLNADYTVVHTIFSYLPKM', 630, 'Q95XP9;', 'KD01119', 'Caenorhabditis elegans', 'zwl-1', '#Protein zwilch homolog', '-', '-', '171798'),
(1120, 'O35942', 'Serine/threonine-protein kinase Nek2', 'GO:0000776===GO:0000777===GO:0051988===c;k;m', 51243, 'Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC; CEP250 and NINL; resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGOL1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates and activates NEK11 in G1/S-arrested cells. {ECO:0000269|PubMed:14668482; ECO:0000269|PubMed:14697346}.', 'MPSRVEDYEVLHSIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEVEKQMLVSEVNLLRELKHPNIVSYYDRIIDRTNTTLYIVMEYCEGGDLASVISKGTKDRQYLEEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDSKHNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMSCLSYNEKSDIWSLGCLLYELCALMPPFTAFNQKELAGKIREGRFRRIPYRYSDGLNDLITRMLNLKDYHRPSVEEILESPLIADLVAEEQRRNLERRGRRSGEPSKLPDSSPVLSELKLKERQLQDREQALRAREDILEQKERELCIRERLAEDKLARAESLMKNYSLLKEHRLLCLAGGPELDLPSSAMKKKVHFHGESKENTARSENSESYLAKSKCRDLKKRLHAAQLRAQALADIEKNYQLKSRQILGMR', 443, 'O35942; O35959; Q3TPD7;', 'KD01120', 'Mus musculus (Mouse)', 'Nek2', '#Serine/threonine-protein kinase Nek2#2.7.11.1#Never in mitosis A-related kinase 2#NimA-related protein kinase 2', '-', '-', '18005'),
(1121, 'Q4ADK7', 'Craniofacial development protein 1', 'GO:0000777', 33400, 'May play a role during embryogenesis. {ECO:0000250}.', 'MEEFDSEDFSTSEEDEDYVPSGGEYSEDDVNELVKEDEVDGEEQTQKTKGKKRKAQSIPARKRKQGLSLEEEEEDANEESGGSSSEEEDAAAEQEKGIGAEDARKKKEDELWASFLNDVGPKSKVPPSTQVKREEETEETGSSKLLVKAEELEKPKETEKVKITKVFDFAGEEVRVTKEVDATSKEAKSFFKQNEKEKPQTNVPAALPSLPAGSGLKRSSGMSNLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP', 297, 'Q4ADK7; Q4ADK6;', 'KD01121', 'Camelus dromedarius (Dromedary) (Arabian camel)', 'CFDP1', '#Craniofacial development protein 1#Bucentaur', '-', '-', '-'),
(1122, 'Q5M823', 'NudC domain-containing protein 2', 'GO:0000777', 17674, 'May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. {ECO:0000250}.', 'MSAPFEERSGVVPCATPWGQWYQTLEEVFIEVQVPPGTRAQDIQCGLQSRHVALAVGGREILKGKLFDSTIADEGTWTLEDRKMVRIVLTKTKRDAANCWTSLLESEYAADPWVQDQMQRKLTLERFQKENPGFDFSGAEISGNYTKGGPDFSNLEK', 157, 'Q5M823;', 'KD01122', 'Rattus norvegicus (Rat)', 'Nudcd2', '#NudC domain-containing protein 2', '-', '-', '287199'),
(1123, 'Q21776', 'BUB-1', 'k', 112034, '', 'MSHIRVAFAPLDTNPSTCGLETFATQIETLSQMMTAEEMKAELYDCVRRILREQKFDQIRENEAMLRLYKVMGRSSTNLKGRGIYEQLFKKDHFTGSLKFYLQWAEECGKDQMLEEFKDVLKLARDRLSERIEMTAIESGFRDLVDEYFNGESGDMFTRPDETMDLFRFNAGSKKKRRSSVCFLQHNVPINNSGKAAFGPKTKTDLRQACIDRPNYHGISIEEFRFAKWKDTFGEDVDDDYRKRKDSGVVFVKHQVIDTDRQAREEVENRFNANLNPRRRHLSPVSEKTVDDEEEKRSRIYSPLVATKDAHRPALRSKIENPPATVTLSSDTKSASEKDVSDSDDADDDERLKIMTAGRKDGNPPDRSTSISSNYSTASARTSKSGAGLDLMAENKCLEAHAMFSDTVHLASEKTMVLGDDSVFVPERSLATTQIVTDFSVLCDPDPTMTITQERPKKVSNGLNVVYDEAAEPEESQKVEESEVQPEIVLVSPVTQTSPATMFNDIYDDEIEFGFFKPSRGNFVTSTPAQGVHLVNIDEYFGNKEEESTHEQEAPVFVAPTSSTFSKLTRRKSLAANQAVQPSVTESSKPERSDPKDSSIDCLTANLGRRLSIGADEIPNLTENNESEITGCKIRRRSEIIKQGDINPWDETLRKKLMCLVRPPQNMHEFQERAPKIQALRDCEVSGEKLHIQTLIGQGGYAKVYRAVTDDQRTVAVKYEVPSCSWEVYICDQMRNRLKDRGLELMAKCCIMEVMDAYVYSTASLLVNQYHEYGTLLEYANNMKDPNWHITCFLITQMARVVKEVHASKIIHGDIKPDNFMITRKIDDKWGKDALMSNDSFVIKIIDWGRAIDMMPLKNQRFKGRAGTEAFDCPEMVDGRSWTYQADYFGFAATMAVVVAGKYAQLTGASVGDYSLNVDIKRRNILRDACYDVINRFLNIPSCDSLPDWNILIKSFSEIWNEKFEASGWRQAVSKFNEACDLAANQK', 987, 'Q21776;', 'KD01123', 'Caenorhabditis elegans', 'bub-1', '#BUB-1 {ECO:0000313|EMBL:CAA95845.1}', '-', '-', '172468'),
(1124, 'Q02224', 'Centromere-associated protein E', 'GO:0000776===GO:0043515===GO:0051382===GO:0000940===GO:0000778===GO:0051315===GO:0003777===GO:0000779===k;m;s', 316415, 'Essential for the maintenance of chromosomal stability through efficient stabilization of microtubule capture at kinetochores. Plays a key role in the movement of chromosomes toward the metaphase plate during mitosis. Is a slow plus end- directed motor whose activity is essential for metaphase chromosome alignment. Couples chromosome position to microtubule depolymerizing activity. The highly processive microtubule- dependent motor activity of CENPE serves to power chromosome congression and provides a flexible; motile tether linking kinetochores to dynamic spindle microtubules. Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss. Required for the efficient recruitment of BUBR1; MAD1 and MAD2 to attached and newly unattached kinetochores. Stimulates mammalian BUBR1 kinase activity. Accumulates just before mitosis at the G2 phase of the cell cycle. {ECO:0000269|PubMed:17535814; ECO:0000269|PubMed:7889940}.', 'MAEEGAVAVCVRVRPLNSREESLGETAQVYWKTDNNVIYQVDGSKSFNFDRVFHGNETTKNVYEEIAAPIIDSAIQGYNGTIFAYGQTASGKTYTMMGSEDHLGVIPRAIHDIFQKIKKFPDREFLLRVSYMEIYNETITDLLCGTQKMKPLIIREDVNRNVYVADLTEEVVYTSEMALKWITKGEKSRHYGETKMNQRSSRSHTIFRMILESREKGEPSNCEGSVKVSHLNLVDLAGSERAAQTGAAGVRLKEGCNINRSLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPVSFDETLTALQFASTAKYMKNTPYVNEVSTDEALLKRYRKEIMDLKKQLEEVSLETRAQAMEKDQLAQLLEEKDLLQKVQNEKIENLTRMLVTSSSLTLQQELKAKRKRRVTWCLGKINKMKNSNYADQFNIPTNITTKTHKLSINLLREIDESVCSESDVFSNTLDTLSEIEWNPATKLLNQENIESELNSLRADYDNLVLDYEQLRTEKEEMELKLKEKNDLDEFEALERKTKKDQEMQLIHEISNLKNLVKHAEVYNQDLENELSSKVELLREKEDQIKKLQEYIDSQKLENIKMDLSYSLESIEDPKQMKQTLFDAETVALDAKRESAFLRSENLELKEKMKELATTYKQMENDIQLYQSQLEAKKKMQVDLEKELQSAFNEITKLTSLIDGKVPKDLLCNLELEGKITDLQKELNKEVEENEALREEVILLSELKSLPSEVERLRKEIQDKSEELHIITSEKDKLFSEVVHKESRVQGLLEEIGKTKDDLATTQSNYKSTDQEFQNFKTLHMDFEQKYKMVLEENERMNQEIVNLSKEAQKFDSSLGALKTELSYKTQELQEKTREVQERLNEMEQLKEQLENRDSTLQTVEREKTLITEKLQQTLEEVKTLTQEKDDLKQLQESLQIERDQLKSDIHDTVNMNIDTQEQLRNALESLKQHQETINTLKSKISEEVSRNLHMEENTGETKDEFQQKMVGIDKKQDLEAKNTQTLTADVKDNEIIEQQRKIFSLIQEKNELQQMLESVIAEKEQLKTDLKENIEMTIENQEELRLLGDELKKQQEIVAQEKNHAIKKEGELSRTCDRLAEVEEKLKEKSQQLQEKQQQLLNVQEEMSEMQKKINEIENLKNELKNKELTLEHMETERLELAQKLNENYEEVKSITKERKVLKELQKSFETERDHLRGYIREIEATGLQTKEELKIAHIHLKEHQETIDELRRSVSEKTAQIINTQDLEKSHTKLQEEIPVLHEEQELLPNVKEVSETQETMNELELLTEQSTTKDSTTLARIEMERLRLNEKFQESQEEIKSLTKERDNLKTIKEALEVKHDQLKEHIRETLAKIQESQSKQEQSLNMKEKDNETTKIVSEMEQFKPKDSALLRIEIEMLGLSKRLQESHDEMKSVAKEKDDLQRLQEVLQSESDQLKENIKEIVAKHLETEEELKVAHCCLKEQEETINELRVNLSEKETEISTIQKQLEAINDKLQNKIQEIYEKEEQFNIKQISEVQEKVNELKQFKEHRKAKDSALQSIESKMLELTNRLQESQEEIQIMIKEKEEMKRVQEALQIERDQLKENTKEIVAKMKESQEKEYQFLKMTAVNETQEKMCEIEHLKEQFETQKLNLENIETENIRLTQILHENLEEMRSVTKERDDLRSVEETLKVERDQLKENLRETITRDLEKQEELKIVHMHLKEHQETIDKLRGIVSEKTNEISNMQKDLEHSNDALKAQDLKIQEELRIAHMHLKEQQETIDKLRGIVSEKTDKLSNMQKDLENSNAKLQEKIQELKANEHQLITLKKDVNETQKKVSEMEQLKKQIKDQSLTLSKLEIENLNLAQKLHENLEEMKSVMKERDNLRRVEETLKLERDQLKESLQETKARDLEIQQELKTARMLSKEHKETVDKLREKISEKTIQISDIQKDLDKSKDELQKKIQELQKKELQLLRVKEDVNMSHKKINEMEQLKKQFEAQNLSMQSVRMDNFQLTKKLHESLEEIRIVAKERDELRRIKESLKMERDQFIATLREMIARDRQNHQVKPEKRLLSDGQQHLTESLREKCSRIKELLKRYSEMDDHYECLNRLSLDLEKEIEFQKELSMRVKANLSLPYLQTKHIEKLFTANQRCSMEFHRIMKKLKYVLSYVTKIKEEQHESINKFEMDFIDEVEKQKELLIKIQHLQQDCDVPSRELRDLKLNQNMDLHIEEILKDFSESEFPSIKTEFQQVLSNRKEMTQFLEEWLNTRFDIEKLKNGIQKENDRICQVNNFFNNRIIAIMNESTEFEERSATISKEWEQDLKSLKEKNEKLFKNYQTLKTSLASGAQVNPTTQDNKNPHVTSRATQLTTEKIRELENSLHEAKESAMHKESKIIKMQKELEVTNDIIAKLQAKVHESNKCLEKTKETIQVLQDKVALGAKPYKEEIEDLKMKLVKIDLEKMKNAKEFEKEISATKATVEYQKEVIRLLRENLRRSQQAQDTSVISEHTDPQPSNKPLTCGGGSGIVQNTKALILKSEHIRLEKEISKLKQQNEQLIKQKNELLSNNQHLSNEVKTWKERTLKREAHKQVTCENSPKSPKVTGTASKKKQITPSQCKERNLQDPVPKESPKSCFFDSRSKSLPSPHPVRYFDNSSLGLCPEVQNAGAESVDSQPGPWHASSGKDVPECKTQ', 2701, 'Q02224; A6NKY9; A8K2U7; Q4LE75;', 'KD01124', 'Homo sapiens (Human)', 'CENPE', '#Centromere-associated protein E#Centromere protein E#CENP-E#Kinesin-related protein CENPE', '-', 'ENSG00000138778', '-'),
(1125, 'Q4ADK4', 'Craniofacial development protein 1', 'GO:0000777', 33340, 'May play a role during embryogenesis. {ECO:0000250}.', 'MEEFDSEDFSTSEEDEDYVPSGGEYSEDDINELVKEDEVDGEEETQKTKGTKRKAESVLARKRKQGGLSLEEEGEEDANEESGGSSSEEEDAATGQEKGIESEDARKKKEDELWASFLNDVGPKSKVPPSTHVKTGEETEETSSSHLVKAEKLEKPQETEKVKITKVFDFAGEEVRVIKEVDATSKEAKSFFKQNEKEKPQSNISSSVPSLSAGSGLKRSSGMSSLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSQMKP', 298, 'Q4ADK4;', 'KD01125', 'Muntiacus reevesi (Reeve''s muntjac) (Chinese muntjac)', 'CFDP1', '#Craniofacial development protein 1#Bucentaur', '-', '-', '-'),
(1126, 'Q7K0E3', 'MOB kinase activator-like 4', 'c;k', 25747, '', 'MKMADGSTILRRNRPGTKSKDFCRWPDEPLEEMDSTLAVQQYIQQLIKRDPSNVELILTMPEAQDEGVWKYEHLRQFCMELNGLAVRLQKECSPSTCTQMTATDQWIFLCAAHKTPKECPAIDYTRHTLDGAACLLNSNKYFPSRVSIKESSVTKLGSVCRRVYRIFSHAYFHHRRIFDEFEAETYLCHRFTHFVTKYNLMSKENLIVPINVGENAAPGESEA', 223, 'Q7K0E3;', 'KD01126', 'Drosophila melanogaster (Fruit fly)', 'Mob4', '#MOB kinase activator-like 4#Mob as tumor suppressor protein 4#Dmob4#Mps one binder kinase activator-like 4', '-', '-', '35576'),
(1127, 'Q6AXN6', 'Small kinetochore-associated protein', 'GO:0000776===GO:0000777===GO:0051988', 34885, 'Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase. Promotes the metaphase-to-anaphase transition and is required for chromosome alignment; normal timing of sister chromatid segregation; and maintenance of spindle pole architecture. The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments. Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis; possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division. {ECO:0000250|UniProtKB:Q9Y448}.', 'MATHKAEAQETDFRTTGPPTDLEQCPFPPSSRKFPFESVAADSTEGWAVAAEHHLKRSGEDGGWEQPASGVEPSRPTTMASSKTVCDAQPHSMPSCGLSADTQTRATSKLPVKSKDAEMLRHLHTGGLEPDVTKVTKPRRENGQGKAAETASRRNIRSSYKPLSKQKPEEDLKDKNELLEAVNKQLHQKLTETQGELKDLTQKVELLEKFQDNCLAILESKGLNSGQETQESKQEPSTDPTDSMLLLETLKDELKLFNETAKKQMEELQALKVKLKLKEKERIQFLEQQTLGKDEASDFTIILEEMEQLLEM', 312, 'Q6AXN6;', 'KD01127', 'Rattus norvegicus (Rat)', 'Knstrn', '#Small kinetochore-associated protein#SKAP#Kinetochore-localized astrin-binding protein#Kinastrin#Kinetochore-localized astrin/SPAG5-binding protein#TRAF4-associated factor 1', '-', '-', '311325'),
(1128, 'E9Q5G3', 'Kinesin-like protein KIF23', 'GO:0003777', 108776, 'Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro (By similarity). {ECO:0000250}.', 'MKSAKAKTVRKPVIKKGSQTNLKDPVGVYCRVRPLSFPDQECCVEVINSTTLQLHTPEGYRLNRNGDYKETQYSFKRVFGTHTTQKELFDVVANPLVDDLIHGKNGLLFTYGVTGSGKTYTMTGSPGSGGLLPRCLNMIFNSIGSFQAKRYVFKSNDRNSMEIQCEVDALLERQKREALPIPKTPSSKRQADPEFADMINVQEFCKAEEVDEDSVYGVFVSYIEIYNNYIYDLLEEVQFDPIKPKLPQSKTLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFSIKLVQAPLDADGDNVLQEKEQITISQLSLVDLAGSERTNRTKAEGNRLREAGNINQSLMTLRTCMEVLRENQTYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEESLQVMRFAEVTQEVEVARPVDKVICGLTPGRRYRNLPRGGPVGDEPLVPEVILQSFPPLPPCKLLDINDEETLPKLADTLEKRHHLRQLMTEDLNKKCLAFKALLKEFDNSLSNKENYVQEKLNEREKVISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELESQNQKLQRQFSDKRRLEARLQGMVTETSMKWQKECERRVAATQLEMQNKLWVKDEKLKQLKAIVTEPKPEKPERPSRERDREKIIPRSVSPSPLPLSSNNIAQISNGQQLMSQPQLHRRSNSCSSISVASCISEWEQKLSPFSTPVNVTSLARHRQQEPGQSKTCIVSDRRRGMCWTEGREMVPTFSSEIGVEEDHCRRNTPIPVRHRRSRSAGSRWVDHKPASNVQTETVMQPHVPHAITVSVANEKALAKCEKYMLTHQELASDGEIQTKVIKGDVYKTRGGGQSVQFTDIETLKQELPTGSRKRRSSTLAPAQPDGTESEWTDVETRCSVAVEMRAGSQLGPGYQHHAQPKRKKP', 953, 'E9Q5G3; Q80V30; Q99PT8;', 'KD01128', 'Mus musculus (Mouse)', 'Kif23', '#Kinesin-like protein KIF23', '-', '-', '71819'),
(1129, 'Q4V8C2', 'Centromere/kinetochore protein zw10 homolog', 'GO:0000776===GO:0000777===GO:0005828===GO:0034501', 87967, '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. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (By similarity). {ECO:0000250}.', 'MASFVTEVLAHSGSLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPTMQSAQALVTQVDTLSNDIDQLKSRIETEVCRDLHISTVEFTNLKQRLERDSVVLNLLKQLQEFSSAIEEYNSALAEKKYIPAARLLEEAQECLKLLKSKKCFDLKMLKSLSMELTVQKQNILYHLGEDWQKLVVWKFPPSKDTSSLESCLQTELHLCTEQPEKEMTPLPSISSVLLAFSILGELPTKLKSFGQMLLKYILKPLVTCPSLHAVIERQPNSVSICFQSLATDSEHPPPPEAFAKIQLVLEVLQKQLLDLPLDADLEIGKVPEIVLAEMLGEVIWEDLSDCLIRNCLVYSIPTNSSKLQQYEEIIQSTEEFEKSLKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARHLMTSEIHNTVKIGPDCEETLPDLPSPDADHRLQVQVCKVQFTDAGNLEPETSLDPRSFSLPTCRISEAVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLQKLPQLAAIHHNNCMYIAHHLLTLGHQFRSRLTPILCDGTTTFVDLVPGFRRLGTECFLAQMRTQKGELLERLSSARSFANMDDEENYSAASKAVRQVLHQLKRLGIVWQDVLPVNIYCKAMGTLLNTVIAEMIGRITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSDENKNKKYQEEVPVYVSKWMPFKELMIMLQASLQEIGDRWADGKGPLATAFPSSEVKALIRALFQNTERRAAALAKIK', 777, 'Q4V8C2;', 'KD01129', 'Rattus norvegicus (Rat)', 'Zw10', '#Centromere/kinetochore protein zw10 homolog', '-', '-', '363059'),
(1130, 'C5DZ48', 'Spindle pole body component KRE28', 'GO:0000777', 42742, 'Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.', 'MKSDLDGYEVRIKSLENQTAHYSEQALLEQEQRVLASLREITQNVIAMGQENSLVEIKGELESKEESELVIDPSGFQEKIDTFVELVELLKVTHLEQETLDNFLRYTISSSNLLQINSVQDAKYVELESQVKELEQGTLESHKREIEATKGQIKNLCQELSMAQDSINETFLDTSNALEECDALLNELTQLRMEKQTSEEADTIEDDPVSQTYEDWESLQKSKLELRLLEEETSRLQSRVESYEDYQKRSRQLSNNDPRMLQNHKALELLVELWMTKFLPQPGISHLELFPQSRKFQFDVEPTFTVVITLADQTTFQNVQVYRKDAKSLVMDHGLNDEIKNSYLGTNNIYNGLNDIIHTLQRRVQAKGSN', 370, 'C5DZ48; B2G406;', 'KD01130', 'Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130NCYC 568 / NRRL Y-229) (Candida mogii)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '8205766'),
(1131, 'P18754', 'Regulator of chromosome condensation', 'k', 44969, 'Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP. Involved in the regulation of onset of chromosome condensation in the S phase. Binds both to the nucleosomes and double-stranded DNA. RCC1-Ran complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA. Plays a key role in nucleo- cytoplasmic transport; mitosis and nuclear-envelope assembly. {ECO:0000269|PubMed:1944575}.', 'MSPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISHEGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAVTKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVKDKEQS', 421, 'P18754; Q16269; Q6NT97;', 'KD01131', 'Homo sapiens (Human)', 'RCC1', '#Regulator of chromosome condensation#Cell cycle regulatory protein#Chromosome condensation protein 1', 'BIOMD0000000192,Gorlich2003_RanGTP_gradient;', 'ENSG00000166965', '-'),
(1132, 'Q5I0J4', 'Spindle and kinetochore-associated protein 2', 'GO:0000940', 16517, '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 is required for SKA1 localization (By similarity). {ECO:0000250}.', 'MEAEVDKLELMFQKADSDLDYLQYRLEYEVKINHPHSAGEKNAVAILKELSAIKSRYQALCARFKTVSVEQKETKSCICAILNKTMTMLQELQKQTNLELTLLTEEEKAVTERLKSHVPDVENGILQRNFDGEKISSKEIQRGV', 144, 'Q5I0J4;', 'KD01132', 'Rattus norvegicus (Rat)', 'Ska2', '#Spindle and kinetochore-associated protein 2#Protein FAM33A', '-', '-', '287598'),
(1133, 'Q6P1K2', 'Polyamine-modulated factor 1', 'GO:0000444===SCL===k', 23339, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. {ECO:0000269|PubMed:10419538; ECO:0000269|PubMed:11256947; ECO:0000269|PubMed:15502821; ECO:0000269|PubMed:16585270}.', 'MAEASSANLGSGCEEKRHEGSSSESVPPGTTISRVKLLDTMVDTFLQKLVAAGSYQRFTDCYKCFYQLQPAMTQQIYDKFIAQLQTSIREEISDIKEEGNLEAVLNALDKIVEEGKVRKEPAWRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLADAVLAGRRQVEELQLQVQAQQQAWQALHREQRELVAVLREPE', 205, 'Q6P1K2; A8K0C5; Q5TCJ8; Q5TCJ9; Q5TCK0; Q5TCK1; Q5TCK3; Q69YZ9;Q6PHR4; Q6ZVE6; Q86VJ6; Q8N4T6; Q9UBQ3;', 'KD01133', 'Homo sapiens (Human)', 'PMF1', '#Polyamine-modulated factor 1#PMF-1', '-', 'ENSG00000260238', '-'),
(1134, 'Q02241', 'Kinesin-like protein KIF23', 'GO:0003777', 110059, 'Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro. {ECO:0000269|PubMed:16103226; ECO:0000269|PubMed:16236794; ECO:0000269|PubMed:22522702}.', 'MKSARAKTPRKPTVKKGSQTNLKDPVGVYCRVRPLGFPDQECCIEVINNTTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQAKRYVFKSNDRNSMDIQCEVDALLERQKREAMPNPKTSSSKRQVDPEFADMITVQEFCKAEEVDEDSVYGVFVSYIEIYNNYIYDLLEEVPFDPIKPKPPQSKLLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDNVLQEKEQITISQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAEVTQEVEVARPVDKAICGLTPGRRYRNQPRGPVGNEPLVTDVVLQSFPPLPSCEILDINDEQTLPRLIEALEKRHNLRQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKEKMISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQGMVTETTMKWEKECERRVAAKQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPERPSRERDREKVTQRSVSPSPVPLSSNYIAQISNGQQLMSQPQLHRRSNSCSSISVASCISEWEQKIPTYNTPLKVTSIARRRQQEPGQSKTCIVSDRRRGMYWTEGREVVPTFRNEIEIEEDHCGRLLFQPDQNAPPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVPHAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGDIYKTRGGGQSVQFTDIETLKQESPNGSRKRRSSTVAPAQPDGAESEWTDVETRCSVAVEMRAGSQLGPGYQHHAQPKRKKP', 960, 'Q02241; B4E1K0; Q8WVP0;', 'KD01134', 'Homo sapiens (Human)', 'KIF23', '#Kinesin-like protein KIF23#Kinesin-like protein 5#Mitotic kinesin-like protein 1', '-', 'ENSG00000137807', '-'),
(1135, 'Q58EL7', 'Spindle and kinetochore-associated protein 3', 'GO:0000940', 55834, '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}.', 'MNPSERFFSKLRKLTVYLETESSSLLHTSQNLKEDEEDEETGAQALYQLHSEVRALKRQVRDQVATHDTSSADLRSFIRRCLVLKQRTTEDIDSLKKHYEKYGYRPRISRLGSTEVNCTKEAEERAERDAEKLDAAEEDEETERGDCDKVDQSVTPEKMPPPVDQLQTPKLSDFGLSALQFQRVLGEAEVPLSAAPESAIALSSPPILMNLQPPQPKTPKCSLSMEEDALTPRLEDFGISEYTMCWNNDFTMDLFNKKPPKNRSERNENVLKPHNVFSNTSSVLNKDVANKSLESPEPPEFCTPGFKIAKNHVPSTPLFNGKNDLNSPPRLNNNCPSTPELPAFETPFVSKLIKKEDREEESKIHSESQENSLRLPDLSTTNGTSWNDAPEMPKMLRYEEEALPEMPILQSNFGSSLAFKNTSGESLSRMKTGAGHMLEMKQTSVPVPEDGFNQDWCLSTPKVRVKFPAEPCTPEMPDMSSVTQDILKLVAQCKY', 495, 'Q58EL7;', 'KD01135', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'ska3', '#Spindle and kinetochore-associated protein 3', '-', '-', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1136, 'O95347', 'Structural maintenance of chromosomes protein 2', 'GO:0051383', 135656, '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}.', 'MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGKKLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFVDGVSTVARFTQCQNGKISKEAKSKAKPPKGAHVEV', 1197, 'O95347; Q6IEE0; Q9P1P2;', 'KD01136', 'Homo sapiens (Human)', 'SMC2', '#Structural maintenance of chromosomes protein 2#SMC protein 2#SMC-2#Chromosome-associated protein E#hCAP-E#XCAP-E homolog', '-', 'ENSG00000136824', '-'),
(1137, 'Q61550', 'Double-strand-break repair protein rad21 homolog', 'k', 72083, 'Cleavable component of the cohesin complex; involved in chromosome cohesion during cell cycle; in DNA repair; and in apoptosis. Plays a role in apoptosis; via its cleavage by caspase- 3/CASP3 or caspase-7/CASP7 during early steps of apoptosis: the C- terminal 64 kDa cleavage product may act as a nuclear signal to initiate cytoplasmic events involved in the apoptotic pathway (By similarity). The cohesin complex is 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 metaphase-anaphase transition; this protein is cleaved by separase/ESPL1 and dissociates from chromatin; allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. {ECO:0000250}.', 'MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTSASNLLLEPEQSTSNLNEKMNHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNGSLGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFFLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREEQQPQQQQPQPQRDVIDEPIIEEPSRLQDSVMEASRTTIEESAMPPPPPQGVKRKAGQIDPEPSIPPQQVEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEEEEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII', 635, 'Q61550; P70219; Q3TQ09; Q810A8; Q91VB9; Q9DBU4;', 'KD01137', 'Mus musculus (Mouse)', 'Rad21', '#Double-strand-break repair protein rad21 homolog#Pokeweed agglutinin-binding protein 29#PW29#SCC1 homolog', '-', '-', '19357'),
(1138, 'Q9UER7', 'Death domain-associated protein 6', 'k', 81373, 'Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML; respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activatiopn of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition; in association with the deubiquitinating USP7; prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53; thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage; its association with MDM2 and USP7 is disrupted; resulting in increased MDM2 autoubiquitination and consequently; MDM2 degradation; which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres; and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upopn neuronal activation asociates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML- NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA; and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast; in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). {ECO:0000269|PubMed:12140263; ECO:0000269|PubMed:14990586; ECO:0000269|PubMed:15364927; ECO:0000269|PubMed:16845383; ECO:0000269|PubMed:17081986; ECO:0000269|PubMed:17942542; ECO:0000269|PubMed:20504901; ECO:0000269|PubMed:20651253; ECO:0000269|PubMed:23222847; ECO:0000269|PubMed:24200965; ECO:0000269|PubMed:24530302}.', 'MATANSIIVLDDDDEDEAAAQPGPSHPLPNAASPGAEAPSSSEPHGARGSSSSGGKKCYKLENEKLFEEFLELCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLKAHSAKKKLNLAPAATTSNEPSGNNPPTHLSLDPTNAENTASQSPRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSAYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAAARHSLGLPRQQLQLMAQDAFRDVGIRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPVLARRLRENRSLAMSRLDEVISKYAMLQDKSEEGERKKRRARLQGTSSHSADTPEASLDSGEGPSGMASQGCPSASRAETDDEDDEESDEEEEEEEEEEEEEATDSEEEEDLEQMQEGQEDDEEEDEEEEAAAGKDGDKSPMSSLQISNEKNLEPGKQISRSSGEQQNKGRIVSPSLLSEEPLAPSSIDAESNGEQPEELTLEEESPVSQLFELEIEALPLDTPSSVETDISSSRKQSEEPFTTVLENGAGMVSSTSFNGGVSPHNWGDSGPPCKKSRKEKKQTGSGPLGNSYVERQRSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDSPSHGLVTSSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD', 740, 'Q9UER7; B4E1I3; F5ANJ6; F5ANJ7; F5H082; O14747; O15141; O15208;Q5STK9; Q9BWI3;', 'KD01138', 'Homo sapiens (Human)', 'DAXX', '#Death domain-associated protein 6#Daxx#hDaxx#ETS1-associated protein 1#EAP1#Fas death domain-associated protein', '-', 'ENSG00000204209', '-'),
(1139, 'Q6DHG8', 'Spindle and kinetochore-associated protein 1', 'GO:0000940', 29669, '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}.', 'MNHCELEEVTQHINNKISMIKRLLELRAVAKDPDKRGTLLKIGQEVSAINELLDRFEKYVGKQRDLLKHLKDLEGFFQEDEQDAYHLKNNTPPHMPKRGQQAAPQGGGQVAVQSRQTDAPAAPQEQGPPRKTQRNQIKEMEFITVPEFDSIPPYMKGRVTYDQLNAAVQSINTAVTSKYKILHQPVKTLNNVSRSLQQRFKDQETKDTKGHFFVVEQDIKEFAQLKVDKRFVGMLNMLRHCQRLKEVRGGGLTRFILL', 258, 'Q6DHG8;', 'KD01139', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'ska1', '#Spindle and kinetochore-associated protein 1', '-', '-', '436865'),
(1140, 'Q96R06', 'Sperm-associated antigen 5', 'GO:0000776===GO:0000777===GO:0051988===c;k;s', 134422, 'Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase. Required for chromosome alignment; normal timing of sister chromatid segregation; and maintenance of spindle pole architecture. In complex with SKAP; promotes stable microtubule- kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle; but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes. In non-mitotic cells; upon stress induction; inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs); thereby preventing mTORC1 hyperactivation- induced apoptosis. May enhance GSK3B-mediated phosphorylation of other substrates; such as MAPT/TAU. {ECO:0000269|PubMed:11724960; ECO:0000269|PubMed:12356910; ECO:0000269|PubMed:17664331; ECO:0000269|PubMed:18055457; ECO:0000269|PubMed:21402792; ECO:0000269|PubMed:23953116}.', 'MWRVKKLSLSLSPSPQTGKPSMRTPLRELTLQPGALTNSGKRSPACSSLTPSLCKLGLQEGSNNSSPVDFVNNKRTDLSSEHFSHSSKWLETCQHESDEQPLDPIPQISSTPKTSEEAVDPLGNYMVKTIVLVPSPLGQQQDMIFEARLDTMAETNSISLNGPLRTDDLVREEVAPCMGDRFSEVAAVSEKPIFQESPSHLLEESPPNPCSEQLHCSKESLSSRTEAVREDLVPSESNAFLPSSVLWLSPSTALAADFRVNHVDPEEEIVEHGAMEEREMRFPTHPKESETEDQALVSSVEDILSTCLTPNLVEMESQEAPGPAVEDVGRILGSDTESWMSPLAWLEKGVNTSVMLENLRQSLSLPSMLRDAAIGTTPFSTCSVGTWFTPSAPQEKSTNTSQTGLVGTKHSTSETEQLLCGRPPDLTALSRHDLEDNLLSSLVILEVLSRQLRDWKSQLAVPHPETQDSSTQTDTSHSGITNKLQHLKESHEMGQALQQARNVMQSWVLISKELISLLHLSLLHLEEDKTTVSQESRRAETLVCCCFDLLKKLRAKLQSLKAEREEARHREEMALRGKDAAEIVLEAFCAHASQRISQLEQDLASMREFRGLLKDAQTQLVGLHAKQEELVQQTVSLTSTLQQDWRSMQLDYTTWTALLSRSRQLTEKLTVKSQQALQERDVAIEEKQEVSRVLEQVSAQLEECKGQTEQLELENSRLATDLRAQLQILANMDSQLKELQSQHTHCAQDLAMKDELLCQLTQSNEEQAAQWQKEEMALKHMQAELQQQQAVLAKEVRDLKETLEFADQENQVAHLELGQVECQLKTTLEVLRERSLQCENLKDTVENLTAKLASTIADNQEQDLEKTRQYSQKLGLLTEQLQSLTLFLQTKLKEKTEQETLLLSTACPPTQEHPLPNDRTFLGSILTAVADEEPESTPVPLLGSDKSAFTRVASMVSLQPAETPGMEESLAEMSIMTTELQSLCSLLQESKEEAIRTLQRKICELQARLQAQEEQHQEVQKAKEADIEKLNQALCLRYKNEKELQEVIQQQNEKILEQIDKSGELISLREEVTHLTRSLRRAETETKVLQEALAGQLDSNCQPMATNWIQEKVWLSQEVDKLRVMFLEMKNEKEKLMIKFQSHRNILEENLRRSDKELEKLDDIVQHIYKTLLSIPEVVRGCKELQGLLEFLS', 1193, 'Q96R06; O95213; Q9BWE8; Q9NT17; Q9UFE6;', 'KD01140', 'Homo sapiens (Human)', 'SPAG5', '#Sperm-associated antigen 5#Astrin#Deepest#Mitotic spindle-associated protein p126#MAP126', '-', 'ENSG00000227543', '-'),
(1141, 'Q6CUD4', 'DASH complex subunit DUO1', 'GO:0042729', 23525, '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}.', 'MVEHKLDASTISKMIPQIFDQMRRQTGSKNFASTPASISTQSLLKEQEQLDKIIPVIQNLNERIKDCKEGDMERIKETCHAMNTILDKFISIQSQASYVNSMMNNEEYLDYVASGKSEEEYISAKQREVEELEKRVKQYTTMHAPSVKPPASKIPVGNDTRKVTKPGQRNGRSGLYSISTRNNSNNSGANGRRPPGNGNNVGRRRVYR', 208, 'Q6CUD4;', 'KD01141', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'DUO1', '#DASH complex subunit DUO1#Outer kinetochore protein DUO1', '-', '-', '2891887'),
(1142, 'P53350', 'Serine/threonine-protein kinase PLK1', 'GO:0000776===GO:0000942===c;k;m;s', 68255, '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 BORA; BUB1B/BUBR1; CCNB1; CDC25C; CEP55; ECT2; ERCC6L; FBXO5/EMI1; FOXM1; KIF20A/MKLP2; CENPU; NEDD1; NINL; NPM1; NUDC; PKMYT1/MYT1; KIZ; PPP1R12A/MYPT1; PRC1; RACGAP1/CYK4; SGOL1; STAG2/SA2; TEX14; TOPORS; p73/TP73; TPT1 and WEE1. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ; NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome; an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55; ECT2; KIF20A/MKLP2; CENPU; PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1; thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1; CDC25C; FOXM1; CENPU; PKMYT1/MYT1; PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1; a key mitotic transcription regulator; leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1; FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGOL1: required for spindle pole localization of isoform 3 of SGOL1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1; a negative regulator of the APC/C complex during prophase; leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS; leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73; leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA; and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP; leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning (PubMed:8991084; PubMed:11202906; PubMed:12207013; PubMed:12447691; PubMed:12524548; PubMed:12738781; PubMed:12852856; PubMed:12939256; PubMed:14532005; PubMed:14734534; PubMed:15070733; PubMed:15148369; PubMed:15469984; PubMed:16198290; PubMed:16247472; PubMed:16980960; PubMed:17081991; PubMed:17351640; PubMed:17376779; PubMed:17617734; PubMed:18174154; PubMed:18331714; PubMed:18418051; PubMed:18477460; PubMed:18521620; PubMed:18615013; PubMed:19160488; PubMed:19351716; PubMed:19468300; PubMed:19468302; PubMed:19473992; PubMed:19509060; PubMed:19597481; PubMed:23455478; PubMed:23509069). Together with MEIKIN; 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 (By similarity). {ECO:0000250|UniProtKB:Q5F2C3; ECO:0000269|PubMed:11202906; ECO:0000269|PubMed:12207013; ECO:0000269|PubMed:12447691; ECO:0000269|PubMed:12524548; ECO:0000269|PubMed:12738781; ECO:0000269|PubMed:12852856; ECO:0000269|PubMed:12939256; ECO:0000269|PubMed:14532005; ECO:0000269|PubMed:14734534; ECO:0000269|PubMed:15070733; ECO:0000269|PubMed:15148369; ECO:0000269|PubMed:15469984; ECO:0000269|PubMed:16198290; ECO:0000269|PubMed:16247472; ECO:0000269|PubMed:16980960; ECO:0000269|PubMed:17081991; ECO:0000269|PubMed:17351640; ECO:0000269|PubMed:17376779; ECO:0000269|PubMed:17617734; ECO:0000269|PubMed:18174154; ECO:0000269|PubMed:18331714; ECO:0000269|PubMed:18418051; ECO:0000269|PubMed:18477460; ECO:0000269|PubMed:18521620; ECO:0000269|PubMed:18615013; ECO:0000269|PubMed:19160488; ECO:0000269|PubMed:19351716; ECO:0000269|PubMed:19468300; ECO:0000269|PubMed:19468302; ECO:0000269|PubMed:19473992; ECO:0000269|PubMed:19509060; ECO:0000269|PubMed:19597481; ECO:0000269|PubMed:23455478; ECO:0000269|PubMed:23509069; ECO:0000269|PubMed:8991084}.', 'MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS', 603, 'P53350; Q15153; Q99746;', 'KD01142', 'Homo sapiens (Human)', 'PLK1', '#Serine/threonine-protein kinase PLK1#2.7.11.21#Polo-like kinase 1#PLK-1#Serine/threonine-protein kinase 13#STPK13', '-', 'ENSG00000168303', '-'),
(1143, 'Q50L39', 'Baculoviral IAP repeat-containing protein 5.2-A', 'GO:0000777===GO:0032133', 18329, '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 (By similarity). Does not appear to exhibit anti-apoptotic activity. Plays a role in increasing blood vessel size during development. {ECO:0000250|UniProtKB:Q804H7; ECO:0000269|PubMed:15853809; ECO:0000269|PubMed:16759290}.', 'MMSISPIVSLRRCDNEPSMPDEWRLYKLASRLRTFSNWPFTEDCACTPERMAEAGFVHCPTDNSPDVVKCFFCLKELEGWQPEDDPMDEHKKHSPSCLFIALKKKAEELTLSEFLKLDLEHTKIKMQKQMNLHIERFQAKANEVRGHLEKLDADETQ', 157, 'Q50L39; Q5XGX1;', 'KD01143', 'Xenopus laevis (African clawed frog)', 'birc5.2-a', '#Baculoviral IAP repeat-containing protein 5.2-A#Survivin2-A {ECO:0000303|PubMed:15853809}#xSurvivin2A {ECO:0000312|EMBL:BAD98266.1}#xSvv2/SIX {ECO:0000303|PubMed:15853809}#xL_Survivin1 {ECO:0000303|PubMed:16759290}#Su1 {ECO:0000303|PubMed:16759290}', '-', '-', '-'),
(1144, 'Q9FZ06', 'Armadillo repeat-containing kinesin-like protein 3', 'GO:0003777', 100887, '', 'MSTTSGTGGVSYRNGTQRSSLRTQSSASTSSGGQKASVKSKSVLRKSSPAALGGGSSKSGGGGDAGVPGRVRVAVRLRPRNGEELIADADFADCVELQPELKRLKLRKNNWDTDTFEFDEVLTEYASQKRVYEVVAKPVVEGVLDGYNGTIMAYGQTGTGKTYTLGQLGEEDVADRGIMVRAMEDILAEVSLETDSISVSYLQLYMETVQDLLDPSNDNIAIVEDPKNGDVSLPGATLVEIRDQQSFLELLQLGEAHRFAANTKLNTESSRSHAILMVNVRRSMKTRDGLSSESNGNSHMTKSLKPPVVRKGKLVVVDLAGSERINKSGSEGHTLEEAKSINLSLSALGKCINALAENSSHVPFRDSKLTRLLRDSFGGTARTSLVITIGPSPRHRGETTSTIMFGQRAMKVENMVKIKEEFDYKSLSRRLEVQLDNLIEENERQQKAFVDEIERITVEAHNQISEAEKRYANALEDEKLRYQNDYMESIKKLEENWSKNQKKLAAERLALGEKNGLDITSNGNRSIAPALEEVSELKKLLQKEAQSKMAAEEEVNRLKHQLNEFKKVEASGNSEIMRLHKMLENETQQKEKLEGEIATLHSQLLQLSLTADETRRNLEQHGSEKTSGARDSLMSQLRLPQIQDPGNAEKPPVARLFEQVGLQKILSLLEAEDADVRIHAVKVVANLAAEEANQQQIVEAGGLTSLLMLLKNTEDETIHRVAAGAIANLAMNETNQELIMDQGGIGLLSSTAANAEDPQTLRMVAGAIANLCGNDKLQTKLRSEGGIAALLGMVRCGHPDVLAQVARGIANFAKCESRASTQGTKRGKSLLIEDGALSWIVQNAKTETAAIRRHIELALCHLAQHEGNAKEMVKEGAMWELVRISRDCSREDIRSLAHRTLTSSPTFLTELRRLRVDIR', 919, 'Q9FZ06; Q9LNA4;', 'KD01144', 'Arabidopsis thaliana (Mouse-ear cress)', 'ARK3', '#Armadillo repeat-containing kinesin-like protein 3#Phosphatidic acid kinase', '-', '-', '837799'),
(1145, 'P05205', 'Heterochromatin protein 1', 'GO:0000780===k;t', 23185, 'Structural component of heterochromatin; involved in gene repression and the modification of position-effect- variegation. Recognizes and binds histone H3 tails methylated at ''Lys-9''; leading to epigenetic repression.', 'MGKKIDNPESSAKVSDAEEEEEEYAVEKIIDRRVRKGKVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASRKDEEKSAASKKDRPSSSAKAKETQGRASSSTSTASKRKSEEPTAPSGNKSKRTTDAEQDTIPVSGSTGFDRGLEAEKILGASDNNGRLTFLIQFKGVDQAEMVPSSVANEKIPRMVIHFYEERLSWYSDNED', 206, 'P05205; A4V0F1; B6UVR4; B6UVS1; B6UVS2; B6UVS3; B6UVT2; B6UVT6;B6UVT7; Q9VLR6;', 'KD01145', 'Drosophila melanogaster (Fruit fly)', 'Su(var)205', '#Heterochromatin protein 1#HP1#Non-histone chromosomal protein C1A9 antigen', '-', '-', '34119'),
(1146, 'P63005', '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; ECO:0000269|PubMed:11056530; ECO:0000269|PubMed:11344260; ECO:0000269|PubMed:12796778; ECO:0000269|PubMed:12911752; ECO:0000269|PubMed:14507966; ECO:0000269|PubMed:14578885; ECO:0000269|PubMed:14691133; ECO:0000269|PubMed:15173193; ECO:0000269|PubMed:15473966; ECO:0000269|PubMed:16107726; ECO:0000269|PubMed:16203747; ECO:0000269|PubMed:16369480; ECO:0000269|PubMed:16481446}.', 'MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR', 410, 'P63005; O35592; P43035; P81692; Q9R2A6;', 'KD01146', 'Mus musculus (Mouse)', '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}', '-', '-', '18472'),
(1147, 'Q75PQ8', 'Origin recognition complex subunit 2', 'GO:0000939', 65850, 'Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre- replication complex necessary to initiate DNA replication (By similarity). Binds histone H3 and H4 trimethylation marks H3K9me3; H3K20me3 and H4K27me3. Stabilizes LRWD1; by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3 (By similarity). {ECO:0000250}.', 'MSTLRLKEAKVPSVQFVGDDDVLSHILDREGGTKLKKEKVQLLVNPQKVIKKAECELEKSDLEVLEDQNYVEVLGRNIQESLGNGSAVDGRNKVYSFQHRKHPEEMTKLALELAKTSGKIDPLASNDPKITKNIARKSKGHSSEKAPLENNNKNEFPSIQPHNVRKRLIASRSHCDSESEYSASSSEDDEEVAKDDEEDTNVVRCSKKSQGQNRLLPAPVSKEILPKKRKRDKAGDLVEEYFEAHSSSKVLTSDRTLQKLRRARVDQKTLRNLLSKFVPSFSTEIGQLNQQHERLFDKWILQLRLGFNIVLYGLGSKRDLLEKFRTTMLQDSIHVVINGFFPGISVKSILNSITEDVLSHMGTFQSVLDQRDWIMNRFKEDSSLELFLLIHNLDSQMLRGDNSQQILGQLSSLRNVYLIASIDHLNAPLMWDHAKQSLYNWLWYETTTYSPYTEETSYENSLLVKQSGSLPLSSLIHVLRSLTPNARGIFRLLMKYQLDNQDCPSYIGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGTDGVEYLLIPVDSGTLADFLEKEEEEES', 576, 'Q75PQ8;', 'KD01147', 'Rattus norvegicus (Rat)', 'Orc2', '#Origin recognition complex subunit 2', '-', '-', '301430'),
(1148, 'P49450', 'Histone H3-like centromeric protein A', 'GO:0051382===GO:0000939===GO:0000778===GO:0000780===k;m', 15991, '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. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro). {ECO:0000269|PubMed:20739937; ECO:0000269|PubMed:21478274}.', 'MGPRRRSRKPEAPRRRSPSPTPTPGPSRRGPSLGASSHQHSRRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTLFPKDVQLARRIRGLEEGLG', 140, 'P49450; D6W544; Q53T74; Q9BVW2;', 'KD01148', 'Homo sapiens (Human)', 'CENPA', '#Histone H3-like centromeric protein A#Centromere autoantigen A#Centromere protein A#CENP-A', '-', 'ENSG00000115163', '-'),
(1149, 'P63004', 'Platelet-activating factor acetylhydrolase IB subunit alpha', 'GO:0000776', 46670, '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. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet- activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). 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. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. {ECO:0000250; ECO:0000269|PubMed:11056532; ECO:0000269|PubMed:16144905}.', 'MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR', 410, 'P63004; O35592; P43035; P81692; Q9R2A6;', 'KD01149', 'Rattus norvegicus (Rat)', '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}', '-', '-', '83572'),
(1150, 'P49454', 'Centromere protein F', 'GO:0000776===GO:0051382===GO:0000940===c;k;m;s', 367764, 'Required for kinetochore function and chromosome segregation in mitosis. Required for kinetochore localization of dynein; LIS1; NDE1 and NDEL1. Regulates recycling of the plasma membrane by acting as a link between recycling vesicles and the microtubule network though its association with STX4 and SNAP25. Acts as a potential inhibitor of pocket protein-mediated cellular processes during development by regulating the activity of RB proteins during cell division and proliferation. May play a regulatory or permissive role in the normal embryonic cardiomyocyte cell cycle and in promoting continued mitosis in transformed; abnormally dividing neonatal cardiomyocytes. Interaction with RB directs embryonic stem cells toward a cardiac lineage. Involved in the regulation of DNA synthesis and hence cell cycle progression; via its C-terminus. Has a potential role regulating skeletal myogenesis and in cell differentiation in embryogenesis. Involved in dendritic cell regulation of T-cell immunity against chlamydia. {ECO:0000269|PubMed:12974617; ECO:0000269|PubMed:17600710; ECO:0000269|PubMed:7542657; ECO:0000269|PubMed:7651420}.', 'MSWALEEWKEGLPTRALQKIQELEGQLDKLKKEKQQRQFQLDSLEAALQKQKQKVENEKTEGTNLKRENQRLMEICESLEKTKQKISHELQVKESQVNFQEGQLNSGKKQIEKLEQELKRCKSELERSQQAAQSADVSLNPCNTPQKIFTTPLTPSQYYSGSKYEDLKEKYNKEVEERKRLEAEVKALQAKKASQTLPQATMNHRDIARHQASSSVFSWQQEKTPSHLSSNSQRTPIRRDFSASYFSGEQEVTPSRSTLQIGKRDANSSFFDNSSSPHLLDQLKAQNQELRNKINELELRLQGHEKEMKGQVNKFQELQLQLEKAKVELIEKEKVLNKCRDELVRTTAQYDQASTKYTALEQKLKKLTEDLSCQRQNAESARCSLEQKIKEKEKEFQEELSRQQRSFQTLDQECIQMKARLTQELQQAKNMHNVLQAELDKLTSVKQQLENNLEEFKQKLCRAEQAFQASQIKENELRRSMEEMKKENNLLKSHSEQKAREVCHLEAELKNIKQCLNQSQNFAEEMKAKNTSQETMLRDLQEKINQQENSLTLEKLKLAVADLEKQRDCSQDLLKKREHHIEQLNDKLSKTEKESKALLSALELKKKEYEELKEEKTLFSCWKSENEKLLTQMESEKENLQSKINHLETCLKTQQIKSHEYNERVRTLEMDRENLSVEIRNLHNVLDSKSVEVETQKLAYMELQQKAEFSDQKHQKEIENMCLKTSQLTGQVEDLEHKLQLLSNEIMDKDRCYQDLHAEYESLRDLLKSKDASLVTNEDHQRSLLAFDQQPAMHHSFANIIGEQGSMPSERSECRLEADQSPKNSAILQNRVDSLEFSLESQKQMNSDLQKQCEELVQIKGEIEENLMKAEQMHQSFVAETSQRISKLQEDTSAHQNVVAETLSALENKEKELQLLNDKVETEQAEIQELKKSNHLLEDSLKELQLLSETLSLEKKEMSSIISLNKREIEELTQENGTLKEINASLNQEKMNLIQKSESFANYIDEREKSISELSDQYKQEKLILLQRCEETGNAYEDLSQKYKAAQEKNSKLECLLNECTSLCENRKNELEQLKEAFAKEHQEFLTKLAFAEERNQNLMLELETVQQALRSEMTDNQNNSKSEAGGLKQEIMTLKEEQNKMQKEVNDLLQENEQLMKVMKTKHECQNLESEPIRNSVKERESERNQCNFKPQMDLEVKEISLDSYNAQLVQLEAMLRNKELKLQESEKEKECLQHELQTIRGDLETSNLQDMQSQEISGLKDCEIDAEEKYISGPHELSTSQNDNAHLQCSLQTTMNKLNELEKICEILQAEKYELVTELNDSRSECITATRKMAEEVGKLLNEVKILNDDSGLLHGELVEDIPGGEFGEQPNEQHPVSLAPLDESNSYEHLTLSDKEVQMHFAELQEKFLSLQSEHKILHDQHCQMSSKMSELQTYVDSLKAENLVLSTNLRNFQGDLVKEMQLGLEEGLVPSLSSSCVPDSSSLSSLGDSSFYRALLEQTGDMSLLSNLEGAVSANQCSVDEVFCSSLQTYVDSLKAENLVLSTNLRNFQGDLVKEMQLGLEEGLVPSLSSSCVPDSSSLSSLGDSSFYRALLEQTGDMSLLSNLEGVVSANQCSVDEVFCSSLQEENLTRKETPSAPAKGVEELESLCEVYRQSLEKLEEKMESQGIMKNKEIQELEQLLSSERQELDCLRKQYLSENEQWQQKLTSVTLEMESKLAAEKKQTEQLSLELEVARLQLQGLDLSSRSLLGIDTEDAIQGRNESCDISKEHTSETTERTPKHDVHQICDKDAQQDLNLDIEKITETGAVKPTGECSGEQSPDTNYEPPGEDKTQGSSECISELSFSGPNALVPMDFLGNQEDIHNLQLRVKETSNENLRLLHVIEDRDRKVESLLNEMKELDSKLHLQEVQLMTKIEACIELEKIVGELKKENSDLSEKLEYFSCDHQELLQRVETSEGLNSDLEMHADKSSREDIGDNVAKVNDSWKERFLDVENELSRIRSEKASIEHEALYLEADLEVVQTEKLCLEKDNENKQKVIVCLEEELSVVTSERNQLRGELDTMSKKTTALDQLSEKMKEKTQELESHQSECLHCIQVAEAEVKEKTELLQTLSSDVSELLKDKTHLQEKLQSLEKDSQALSLTKCELENQIAQLNKEKELLVKESESLQARLSESDYEKLNVSKALEAALVEKGEFALRLSSTQEEVHQLRRGIEKLRVRIEADEKKQLHIAEKLKERERENDSLKDKVENLERELQMSEENQELVILDAENSKAEVETLKTQIEEMARSLKVFELDLVTLRSEKENLTKQIQEKQGQLSELDKLLSSFKSLLEEKEQAEIQIKEESKTAVEMLQNQLKELNEAVAALCGDQEIMKATEQSLDPPIEEEHQLRNSIEKLRARLEADEKKQLCVLQQLKESEHHADLLKGRVENLERELEIARTNQEHAALEAENSKGEVETLKAKIEGMTQSLRGLELDVVTIRSEKENLTNELQKEQERISELEIINSSFENILQEKEQEKVQMKEKSSTAMEMLQTQLKELNERVAALHNDQEACKAKEQNLSSQVECLELEKAQLLQGLDEAKNNYIVLQSSVNGLIQEVEDGKQKLEKKDEEISRLKNQIQDQEQLVSKLSQVEGEHQLWKEQNLELRNLTVELEQKIQVLQSKNASLQDTLEVLQSSYKNLENELELTKMDKMSFVEKVNKMTAKETELQREMHEMAQKTAELQEELSGEKNRLAGELQLLLEEIKSSKDQLKELTLENSELKKSLDCMHKDQVEKEGKVREEIAEYQLRLHEAEKKHQALLLDTNKQYEVEIQTYREKLTSKEECLSSQKLEIDLLKSSKEELNNSLKATTQILEELKKTKMDNLKYVNQLKKENERAQGKMKLLIKSCKQLEEEKEILQKELSQLQAAQEKQKTGTVMDTKVDELTTEIKELKETLEEKTKEADEYLDKYCSLLISHEKLEKAKEMLETQVAHLCSQQSKQDSRGSPLLGPVVPGPSPIPSVTEKRLSSGQNKASGKRQRSSGIWENGRGPTPATPESFSKKSKKAVMSGIHPAEDTEGTEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSPRLAAQKLALSPLSLGKENLAESSKPTAGGSRSQKVKVAQRSPVDSGTILREPTTKSVPVNNLPERSPTDSPREGLRVKRGRLVPSPKAGLESNGSENCKVQ', 3210, 'P49454; Q13171; Q13246; Q5VVM7;', 'KD01150', 'Homo sapiens (Human)', 'CENPF', '#Centromere protein F#CENP-F#AH antigen#Kinetochore protein CENPF#Mitosin', '-', 'ENSG00000117724', '-'),
(1151, 'P49453', 'Centromere protein C', 'GO:0000776===GO:0000777===GO:0051382', 45065, '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. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions (By similarity). {ECO:0000250|UniProtKB:Q03188}.', 'KSEQSSFSSSSSVRNELSVYHNSRQKPPAEKTNQSSKNIGKKAAPFKKQKRANKGSSGAQVLYAKDSGGAQNESLRSNEADLAKKKNPNPSGDTGSSKNQDSMAAQNVHQKSQMSVETCTTPSKSNLILESLGLQFFGREVTLFRLKNYLTSERHSDVDDNVVQENLNDSRGEIPDSTPESKMHHKLVLPSYTPNVRRTMRTRSKPLEYWRGERIDYQARPSGGFVIGGILSPDTVSSKRKAKGNLGRIITTANRKRICLENAPIKNKFMVNLNIPLGDPLQPTRVKDPETQETVLMDLIRPRDTYQFCVEHDELKVYKTLDTPFFSSGKLIIGPLQEKGKQHVGLDTLVFYVNLGYLLCTLHETPYIVTTGDSFYVPSGNYYNIKNLLNEERVLLFTQIKS', 402, 'P49453;', 'KD01151', 'Ovis aries (Sheep)', 'CENPC', '#Centromere protein C#CENP-C#Centromere autoantigen C#Centromere protein C 1#CENP-C 1', '-', '-', '-'),
(1152, 'P49452', 'Centromere protein C', 'GO:0000776===GO:0000777===GO:0051382===GO:0000780===k', 102154, '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. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions (By similarity). {ECO:0000250|UniProtKB:Q03188}.', 'MASFHLDHLKNYHRRYCRSSRAPNIHTKKGQNMLEILQDCFEDQSKASFLDDFTESLTSSTQKKKANYSQSSSKKCPESHSKPVPVSSRTGEASLQASAEPSEAAGGSVQANEVHHGASDELDLCVGSPVVLLDANVNTLQKAASPAGQKRVASVSRSPVDRQASNKNISFKTRKRLNFEDKVTLSTAETENSVLQVEDNLSKGQEGTSSEITQKRDDLSSDVQSRSKKNFSELFLETVKRKSKSSSVVRHTAAVPFSPPPPSDMKLLEDEFIIDRSDRSFSSRLWVMIPSKDRHLSAHKPSPENTALLQGKKSREKSHSLSAMTFARNTQSDKAHPIEEAQLSVEENPATTCTDELENDCRSPENKMQSETAKTPPAWERTTKQSQRRVSKPKAAEELRKGQSSWENSNVSNTGQDKLQINSKRNMKDCEEVRNEPNPKKQKPALENKKKTNSTQTNKEKSGKKFFSGGSKNKFVPKKVTLTSRRSCRISQRPSEWWRVKSDESSVDRNPSKENNSPVVYPNKKKQTKRNHVSKRAGKKPGSSKRQKTEMSPRVQKSLNVKDSGGTVSGHDDTSRSQRKPLKIIEADPTQKSLAISRPKRGCKYRNNVMTSPNVHLKSHTEEYTSKTQMESASNSEMSKRSVWEESGPSRFKNYEMPGSSNSEMGDEQDQKSLHFTTRSFNMVPDKKLHHKLVLPSNSPNVRRSNRIRLKPLEYWRGERVDYQESSSGQLVLEIISPSSVPTKIKAQRNLGKVNKKVTKKPTHLNSHEKAKMELPLDMRLGDPFQATLAKDPETAELVPMDLIRPRDTYRFFVEQHGLKVFKTLDTIYFSTGKLVLGPYEEKGKQHVGQDILVFYVNFGDLLCTLHETPYKLTTGDSFYVPSGNHYNIKNLLNVESSLLFTQIKR', 906, 'P49452; B9EK81;', 'KD01152', 'Mus musculus (Mouse)', 'Cenpc', '#Centromere protein C#CENP-C#Centromere autoantigen C#Centromere protein C 1#CENP-C 1', '-', '-', '12617'),
(1153, 'P26449', 'Cell cycle arrest protein BUB3', 'GO:0000778===k', 38445, 'Required for cell cycle arrest in response to loss of microtubule function. Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20. The formation of a MAD1-BUB1- BUB3 complex seems to be required for the spindle checkpoint mechanism. {ECO:0000269|PubMed:15879521}.', 'MQIVQIEQAPKDYISDIKIIPSKSLLLITSWDGSLTVYKFDIQAKNVDLLQSLRYKHPLLCCNFIDNTDLQIYVGTVQGEILKVDLIGSPSFQALTNNEANLGICRICKYGDDKLIAASWDGLIEVIDPRNYGDGVIAVKNLNSNNTKVKNKIFTMDTNSSRLIVGMNNSQVQWFRLPLCEDDNGTIEESGLKYQIRDVALLPKEQEGYACSSIDGRVAVEFFDDQGDDYNSSKRFAFRCHRLNLKDTNLAYPVNSIEFSPRHKFLYTAGSDGIISCWNLQTRKKIKNFAKFNEDSVVKIACSDNILCLATSDDTFKTNAAIDQTIELNASSIYIIFDYEN', 341, 'P26449; D6W292;', 'KD01153', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'BUB3', '#Cell cycle arrest protein BUB3', '-', '-', '854191'),
(1154, 'B7ZC32', 'Kinesin-like protein KIF28P', 'GO:0003777', 108254, 'Microtubule-dependent motor protein required for mitochondrion morhology and transport of mitochondria in neuronal cells. {ECO:0000250}.', 'MPTQSVDSVKAVRVRPFSQREKNSGSKCVISMHSRTTTTTQDPKNPEHVKTFTFDLAYWSHNGFQRDKDGVLISADPSRKFAGQRDVFHDLGRGILDSAWQGYNATLLAYGQTGSGKSYSMIGFGCKQGIIPTVCEELFRAIENQGRNQEHQVMFSMLEIYKEIIRDLLSRTKKPGGLRIREDQQLGFYVEGLKSVPCENYAQIERLMEQGTKIRTTASTNMNASSSRSHLVITIQFKQVFLDRDLTKQSSINLVDLARSERQKSSGSEGDRLREGSCVNLSLTNLGSVISVLADAAMGKKVLHIPYRDSVLTKLLQSALGGNSRTALVAAVSPADICYEETLSTLRYAERERKIRNRAVANTWTLMRKSRAENSKLLPMMTFPHLLNLSEDPQLTRVLKYFIQAGTQPAPCPRPALSPPHPALRISDKHASFTNADGKVTVTPHSKCKVAVNGVPITTRTKLQHLDRLILGSNSTYLYVGFPSEWGSEDLSRFDYDFFQLERAAAEGASADKLGAADGGDGKAGPSVLAAFQDYIKLMPLVSEANQMSEEPKKGLNMELKVKNLASSDSRGYDLQKEVLVKVTHHGSHEVWIWSKAKFINRKFLMQELYQRFLDGDHGPVARDDDPFWDPVEVVRLGSAHIWLQSLAYCMKLEEQVEFLNCDGLEEAVLHTCIAPCSPTGQTHGEEDVVIDPLELLGKRMDFQIHIVRCLGVNWMKEDAKRGTQIGYRIYDLPNTIYTKPVWKSVNPQIEETVQFAALTASQEFLNYLRTNALIVDLWGLQEGCTELSCSQLGLMVTGEGHILVDTKKISTVKDISQAASNQIPELYLKLLKLEQETEPLRNINRALREENVLLKASLAKTASGQAPKPSNTLKISGMTAQLPSAGEMSQMCTQQAGSDRELAKALKVFYQSMNTARGQLFRLRRHQPPEVDQMLRPFIHQRSQMFKDLGDLRESSLWTLKMTLLL', 967, 'B7ZC32;', 'KD01154', 'Homo sapiens (Human)', 'KIF28P', '#Kinesin-like protein KIF28P#Kinesin-like protein 6', '-', 'ENSG00000223519', '-'),
(1155, 'P49449', 'Histone H3-like centromeric protein A', 'GO:0000777', 15678, '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. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro) (By similarity). {ECO:0000250}.', 'MGPRRQKRKPETPRRRPASPAPAAPRPTPSLGTSSRPLARRRHTVLKEIRTLQKTTHLLLRKSPFCRLAREICVQFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLSLHAGRVTLFPKDVQLARRIRGIQEGLG', 138, 'P49449;', 'KD01155', 'Bos taurus (Bovine)', 'CENPA', '#Histone H3-like centromeric protein A#Centromere protein A#CENP-A', '-', '-', '-'),
(1156, 'P60484', 'Phosphatidylinositol 3;4;5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN', 'c;k', 47166, 'Tumor suppressor. Acts as a dual-specificity protein phosphatase; dephosphorylating tyrosine-; serine- and threonine- phosphorylated proteins. Also acts as a lipid phosphatase; removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3;4;5-trisphosphate; phosphatidylinositol 3;4-diphosphate; phosphatidylinositol 3- phosphate and inositol 1;3;4;5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3;4;5)P3 > PtdIns(3;4)P2 > PtdIns3P > Ins(1;3;4;5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K- AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis; including correct neuron positioning; dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential; whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells; suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement.', 'MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV', 403, 'P60484; B2R904; F2YHV0; O00633; O02679; Q6ICT7;', 'KD01156', 'Homo sapiens (Human)', 'PTEN', '#Phosphatidylinositol 3;4;5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN#3.1.3.16#3.1.3.48#3.1.3.67#Mutated in multiple advanced cancers 1#Phosphatase and tensin homolog', 'BIOMD0000000205,Ung2008_EGFR_Endocytosis;BIOMD0000000424,Faratian2009 - Role of PTEN in Trastuzumab resistance;BIOMD0000000452,Bidkhori2012 - normal EGFR signalling;BIOMD0000000453,Bidkhori2012 - EGFR signalling in NSCLC;BIOMD0000000465,Koo2013 - Shear stress induced AKT and eNOS phosphorylation - Model 2;BIOMD0000000468,Koo2013 - Integrated shear stress induced NO production model;', 'ENSG00000158828', '-'),
(1157, 'Q5NVM2', 'Cytoplasmic dynein 1 intermediate chain 2', 'GO:0005868', 71457, '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 help dynein bind to dynactin 150 kDa component (By similarity). organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. Involved in membrane-transport; such as Golgi apparatus; late endosomes and lysosomes (By similarity). {ECO:0000250}.', 'MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTPESPIVFSEYWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSVLQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNADYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA', 638, 'Q5NVM2; Q5R985; Q5RDM7;', 'KD01157', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'DYNC1I2', '#Cytoplasmic dynein 1 intermediate chain 2#Cytoplasmic dynein intermediate chain 2#Dynein intermediate chain 2; cytosolic#DH IC-2', '-', '-', '100174119'),
(1158, 'P07332', 'Tyrosine-protein kinase Fes/Fps', 'k', 93497, 'Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton; microtubule assembly; cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down- stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1; PECAM1; STAT3 and TRIM28. {ECO:0000269|PubMed:11509660; ECO:0000269|PubMed:15302586; ECO:0000269|PubMed:15485904; ECO:0000269|PubMed:16455651; ECO:0000269|PubMed:17595334; ECO:0000269|PubMed:18046454; ECO:0000269|PubMed:19001085; ECO:0000269|PubMed:19051325; ECO:0000269|PubMed:20111072; ECO:0000269|PubMed:2656706; ECO:0000269|PubMed:8955135}.', 'MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR', 822, 'P07332; B2R6E6; B4DUD0; E9PC94; E9PC95; Q2VXS7; Q2VXS8; Q2VXT0;Q6GTU5;', 'KD01158', 'Homo sapiens (Human)', 'FES', '#Tyrosine-protein kinase Fes/Fps#2.7.10.2#Feline sarcoma/Fujinami avian sarcoma oncogene homolog#Proto-oncogene c-Fes#Proto-oncogene c-Fps#p93c-fes', 'BIOMD0000000579,Sengupta2015 - Knowledge base model of human energy pool network (HEPNet);', 'ENSG00000182511', '-'),
(1159, 'F8WLE0', 'Kinesin-like protein KIF28P', 'GO:0003777', 115542, 'Microtubule-dependent motor protein required for mitochondrion morhology and transport of mitochondria in neuronal cells. {ECO:0000269|PubMed:21693574}.', 'MDCEKMGKLPVPRTDSVRVAVRVRPFSQREKNSGSQCVISMHARSITIRDPKDAELVKTFTFDLAYWSHDGFQKDEDGVLIPSDPTSKFAGQSDVFHDIGRGILDSAWQGYNATLLAYGQTGSGKSYSMIGYGANKGIIPRVCEELFQAIEKQKESLEAQVMFSMLEIYNEQIRDLLSRTKAPGGLRVREDQRLGFFVEGLKWVPCEDSVQIEKLVEQGSKIRMTASTNMNASSSRSHMLIAIRFKQVFLDTALTKQSSINMVDLAGSERQRSSGSEGDRLREGSRVNLSLTNLGNVISALADLAMGKKVLHIPYRDSVLTKLLQSALGGNSRTTLIAALSPADICYEETLSTLRYAERAKKVRNRAVINTCPLVRASRAENALLLGFGGAGAAEHSACFWAEQQLGTWGTWAQLLEQARREWEQQYMALAQEQQMVKILPHLLNVNEDPQLTGVLKFFIHNGSCEVGRAASNAICLQSLGISDKHASFTNMDGKVTVAPHITGKVIVNGVPVSSRTKLQHLDRIILGSNSAFLYIGFPSERGAEDLGRFDYDFFQMERAAAEGVSVDMLGTASPGDDQADPSILAVFQDYIKLMPLVVEANQMSEELKKGLKMELKVKNLASSDSRGCDLQKEVMVKVTKQGTHEVWIWSKAKFINRKFLMEELYQRFLESRDSHVAQEDDPFWDPVEVLHLGSAHVWLQSLAHRMMLEEQVEFLNCEGLEEAVLHIQITPCSPEGWAHGEEDTVIDPLELLGKRIDFQIHIVQCLGVKWLKEDATRGIQLGYKVYDLPNTLYTKPVWQSVNPRVEESVHFAALGVSREFLNYLLTNALVVDLWGLQEGCAHLGVSQPDVLFTGEGYIMVDTKTFSSVKDITSNQVPELYQKLLKLEQETELLRDINRALRGENVYLKAALENAGSAPQGERRYHKPDNPEGATVTAAGEAKQMCAQRASSDSQLARALKVFYGGMSVARGQLLRLRQCRPPEDDQMLRPFVHQQSQMLKDLEDLLESSLQKLKSDVAFIVKKKKEYLLPRGR', 1034, 'F8WLE0;', 'KD01159', 'Rattus norvegicus (Rat)', 'Kif28p', '#Kinesin-like protein KIF28P#Kinesin-like protein 6', '-', '-', '289309');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1160, 'Q9HDZ6', 'DASH complex subunit dam1', 'GO:0000778===GO:0051315===GO:0042729===GO:0031134===GO:0000779===SCL===k', 17444, '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. {ECO:0000269|PubMed:16079914}.', 'MEKYQKATQNPLENVDNVKIESENAIPSNLQAFTKSLAVLDDNVSEFRKRMNHLSATKQILDNFNESFSSFLYGLQINAFCVDYENAPLSESFLLQAKKDQFKATLMTRTGHSISDPPYDGGVISHDPNFATADETFATNDTSFIERPETYSASR', 155, 'Q9HDZ6;', 'KD01160', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dam1', '#DASH complex subunit dam1#Outer kinetochore protein dam1', '-', '-', '2542489'),
(1161, 'G5EFM0', 'MDF-1', 'k', 78633, '', 'MNYDEDIVDEDEYEESEATMLFAEEIKKQFKREFPLKAETEKKLKQATFRRHAPVEARKINFDMTLSPVAPIELASAKKEKESAQRQLVTLREDHERMKQMMQTNQAKLAEKTIDLETNREKMLELQEQVELLKQERDDTIAECNRNVDIWTAFGKKYYTWYSMANTQLESVKLYIDNDGKFENDEEVTRLNAVPRQMYRALEQFDYDDETVEELGSGSLLEYEGVSFATRRPPSPETEREIARADQSAANFTLPQSNFTLLEDSNNTIMPEDQTMMTDGCIANRSLIDYEKDEKIQRLLLENSVLKDRLNVSSGRAERSMIFEERNRTLEFEKKALHKQLDSTFSEIEAIRIGQAGNLFNIDEKIPSSSDNSAKQLQLIDRITQLITKNNQLEKDFEAATSRMTKVMRESTDCARRNERLEDAFSSERVRSQDLENEKSRLSEQLELSNNELEKVKKQLEESQSQLDEVLSMTLTVPASEPASLPAPTDAGNSTQIFHMASNPLQDAHNEFQASESRKRKLTDAPAGDQWREQEFAELEKRLYDCESEKKVLESSYNLHKELSSKFRQVCIALTGLQIKLKDADEGICTVQSEYEGGSAQQFVFKYFYGTPRIDMLDVSCESTTEMLRKWEPLMKKYIGDRNSIPAFLAAMTLQLEQDRDFDETMHERTHTFSVLHED', 679, 'G5EFM0;', 'KD01161', 'Caenorhabditis elegans', 'mdf-1', '#MDF-1 {ECO:0000313|EMBL:AAF63494.1}', '-', '-', '179338'),
(1162, 'P45443', 'Dynein heavy chain; cytoplasmic', 'GO:0003777===GO:0031134===GO:0005868', 495578, '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.', 'MMDSVPSPPPQPSPDANGVATTPFAAVDPVKVVDHLVLLLEATLGAKRDELEAPGSLLSKVRYSDTVQRCSRFALDTQVALYIQKDLAPTTTLDGDNGAEAEEPEPTHVYTISSDLTSSPTTVAYLVLLKRPQPLDPIVPLTSQIQMLNLPGPAYLSTSGSEQGPTSSPYEILQLYLHNGLAPYFDASTKSQQLLNGARGRPDVDAKTGIPVTKKRWTELELSLSHLQQNVEIPEVSLPFHPLVQSTLEEAATKNVKPSIDLLPATVLADSTFLNNLQATVNNWIKSIQVITKMTRDPTTGTANQEINFWLSMEAALEGIENQLRSEGVMLTLDILKHAKRFQATVSFTADTGLKEAMEKVQKYNQLMRDFPLDELLSATTLTKVQESIGQIFGHLNKKLRICPYPIRRALPLVEAISGDLDEVLHRLLPGTELVKLDYEEFKGVMKQAGSIFRAWDESIKEFTNVAREVTRRRNEKFIPIKINPRHAELQSRLDYVHNFRDNHEQLQRTIINVLGPKATVNGIVTASGANGVAVVEEIGDVDAVDEVKQAWEALKDVDLLDCTREGTEKWVRAENIYNERTARVENSIIARLRDRLATAKNANEMFRVFSKFNALFVRPKIRGAIAEYQTQLIDNVKQAISSLHERFKQQYGHSEAHAMAQLHDLPPVSGAIIWARQIERQLDQYMKKVEQVLGSDWALHTEGQKLQNESDLFRKKLDTRPIFEAWLHDVQRKQISISGLLFTINRIRSAGNILELAVNFDAQVIALFKETRNLLWLNYPVPHSVNNVAKEAKRVYPFAVSLMESVRTFAQTNRQISDMSEVAVLLSGHRNDVYTLISKGIPLRWETFVNTYEVHFKPTFNPNTPLGQTGSKVSETKHVMFIREFAASVSLLQSKTLLLANIYVTVQKALNELKTCPYEASAFQSRLETIQHAVDQLNLEQYVNLGYWVERMNRQIKDVLYTRLQVAIQAWIQAFEDEDVERPSERKRLLEIASPDAAKSIGPVIKSLVHEITMRNQVIYLDPPLEYARASWFAQLQDWIGVICNLKKIKATRYTMSLSTEVVDEPRFNDLPGDCTEELLRVQTSVEKKIREIGAYVDKWLQFQSLWDLQSEHVYDVLGDQLSRWLQLLQEIRKTRQTFDTTEVSRSFGHITIDYDQVQTKVNAKYDQWQQDILIKFASRLGNRMREVYAELEKARKDLEGQAMTANSTAEAVRFITIVQSCTRQVKLWAPEIETFRQGESTLVRQRYHFQNDWLHAEQVDGMWDMLNELLARKSKIVTDQSDALRAKITAEDKVVNDKIAEIAHQWNEEKPVSGTIAPDVASATLTHFEQRITKLQEESAMVAKAKEALDLAPTPDTSLGVILEEVQDFKSVWASLSTIWKNLNELRETLWNSVQPRKIRASIDNLIKMTKEMPSRMRQYAAFEHIQNVLRQLMKVNSILGELKSEAVRDRHWTKIYKQIKPGKRYSPVSMTLGDVWDLNLVATEVIVKDIIIQAQGEMALEEFLKQVRETWTNYGLELVQYQQKCRLIRGWDDLFAKCSENLNSLQAMKHSPYYKEFEEEASSWEEKLNRVHVLFDIWIDVQRQWVYLEGVFHGNADIKHLLPIESSRFQNINSEFLAVMKKVYKQPNVLDVLNIPNVQKSLERLAELLNKIQKALGEYLEKERVSFPRFYFVGDEDLLEMIGNSNDTMRIAKHFKKMFAGLNGLVMDDEGVISGFTSKEGETVRLKKEINLVKTPRINDWLALLENGMKVTLAELLAEAVDEFTPIFSSENVDRDALIKFMNTYPSQIVVLATQVVWTTAVDQALADGGKDLQLLFDREVQVLRMLADTVLGDLEVLLRKKCEQLITECVHQRDVIEKLVKLNANSNTHYMWLLQMRYVYNPEGDFLQRLHIKMANAKLNYGFEYLGVPDRLVRTPLTDRCFLTLTQALCQRLGGSPYGPAGTGKTESVKALGLQLGRFTLVFCCDDTFDNQAMGRIFLGICQVGAWGCFDEFNRLEEKILSAVSQQIQDIQLGLKMGAEDEKAQIELDGRQIHVNANAGIFITMNPGYAGRSNLPDNLKKLFRSVAMSKPDKELIAEVMLYSQGFNQAKQLSKHTVPFFDQCSEKLSKQAHYDFGLRALKSVLVSSGGLKRARLLETGDAESLGPEDVVEPEIIVQSIRETIAPKLIKSDVEIMMEIESVCFPGVKYVPASLEKLQEAIRRLAAERQLVVNDIWMTKVLQLYQIQKIHHGVMMVGNSGSGKSAAWRLLLDALQQTENVEGVSHVIDSKVMSKEALYGNLDSTTREWTDGLFTSILRKIVDNLRGEDAKRHWIVFDGDVDPEWVENLNSVLDDNKLLTLPNGERLNLPPNVRIMFEVENLKYATLATVSRCGMVWFSEDTVTPDMMVSNYIETLRTVAFEDLDEDAVATGQSSAKALAVQSQAADLLQEFLTRDNLINEVLKEAANYEHIMEFTVARVLSTLFSLLNKAVRDIIEYNSAHVDFPMDPEQVEGYIAKKVLLALVWALTGDCPLKDRKAFGDKVAGLASFGSPPLDGTSSLIDFTVTMPQGEWQTWQQHVPTIEVNTHSVTQTDVVIPTLDTIRHEDVLYSWLAEHKPLLLCGPPGSGKTMTLFSALRKLPNMEVVGLNFSSATTPDLLIKTFEQYCEYKKTLNGVMLSPTQIGRWLVIFCDEINLPAPDKYGTQRAISFLRQLVEHNGFWRTSDKAWVTLDRIQFVGACNPPTDAGRTPMGARFLRHAPLIMVDYPGELSLMQIYGSFNAAVLKVIPSLRGYAEALTQAMVRFYLESQERFTPKIQPHYVYSPRELTRWVRGVYEAIRPLETLSVEGLIRIWAHEALRLFQDRLVDEEERKWTDDAVRRIAMEYFPTIDEHKALGGPILFSNWLSKNYVPVDREQLRDFVKARLKTFCEEEVDVPLILFNDVLEHVLRIDRVFRQPQGHLILIGVSGSGKTTLSRFVAWMNGLKVFQIKVHGKYSAEDFDEDLREVLRRCGCKGEKICFIMDESNVLDSGFLERMNTLLANAEVPGLFEGDDLAALMTACKEGAQRQGLLLDSQEELYKWFTGQIVKNLHVVFTMNPPGEDGLSSKAATSPALFNRCVLNWFGDWSDQALFQVAHELTHSVDLDRPNWTAPDTIPVAYRGLNLPPSHREAVVNAMVYIHYSLQRFNAKLLKQQGKITFLTPRHFLDFVAQYVKLYNEKREDLEEQQRHLNVGLEKLRDTVDKVRDLRVTLSEKKAQLEQKDAEANEKLQRMVADQREAEQRKNISLEIQAALEKQEAEVASRKKVVLEDLARAEPAVEEAKASVSSIKRQHLTEVRSMPTPPSGVKLALESVCTLIGHKANDWKTIQGIVRRDDFIASIVNFNNEKQMTKSLRVKMRNEFLANPEFTFEKVNRASKACGPLVQWVEAQVNYAEILDRVGPLREEVMLLEEQALQTKAEAKAVEQTISTLENSIARYKTEYAALISETQAIKAEMSRVQFKVDRSVKLLDSLSSERTRWEEGSRSFETQISTLVGDVLVAAAFLAYSGLYDQTFRKSMMEDWLHQLHLSGVQFKQHNPMTEYLSTADERLSWQENTLPVDDLCTENAIILKRFNRYPLIIDPSGRATEFLNRESKDRKLTVTSFLDDSFTKVLESSLRFGNPILIQDAEHLDPVLNHVLNKEYQKTGGRVLIQLGKQQIDFSPAFKLYLSTRDPSATFAPDICSRTTFVNFTVTQSSLQTQSLNEVLKSERPDVDERRSNLIKLQGEFKVHLRQLEKKLLQALNESRGNILDDDHVIETLETLKTEAAEISAKMSNTEGVMAEVEQITLQYNIIARSCSAVFAVLEQLHYLNHFYRFSLQYFLDIFHSVLRGNPHLANETNHNVRRDIIVKDLFVATFKRTALGLLQKDRITLAMLLAQASPYKMDKGLLDIILDERIEGKDVSIDQNTREEAFARAKKIPALKNKIDAVPEADWEKFFTEELAEDFVPKIWNDETEPNDRALMSLLLVKLFRLDRFVPAAERFVTLVFGSDLFDIVEDLKQTVDQVSAILPIALVSSPGFDASYKVDGLVERMRVRCTNIAMGSAEAEGSADKAIANAAQTGSWVLIKNVHLAPGWLQGVEKKMETLNPNPEFRLFLSMESSPKIPVNLLRASRVLMYEQPAGVRANMKDSMSSISTRSLKSPVERTRLYLLLSFLHAVVQERLRYAPNLGWKGFWEFNDADYECSAHVIDTWIDTAAHGRTNIAPSNIPWEMIRYLIVETYGGKIDDENDFKMLNQLVHTFLTPSAFDIGHKLVEVSHDAEDEQKDAATGGDLVVPSGTSLQEFMSWIQKLPEREPPTYLGLPANAEKLLLVGLGKSLIGNLKKVTDLLDEGEAIMAEASEAA', 4367, 'P45443; Q7RVH1; V5IQJ3;', 'KD01162', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'ro-1', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC#Ropy-1', '-', '-', '3878786'),
(1163, 'P45444', 'Dynein heavy chain; cytoplasmic', 'GO:0005868', 492082, '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.', 'MEVASSGVPDGAPTAISQGPLVDADAVVEYLADVLRVTLGALRSELENAGSLLSKTKYSETAQRCLRFASESQVALYVQKDLVASDHTNGTADSEEPPAEYVYTLSAEISSSSTTVASVAFIKRPAAIDPSLPISSQIQVMNLPGPAALNNTQAQQGTSLSPYEILHLLVHHGLSPYFEANTRNQDGAAKAKTDSEVKTGVPGTKKKFAELELGLLHLQQNVEIPALNLPLHEVVQAALVEAEKRGVKPSVDLIDSTLLESSAFINSIQNNVNAWIKSIQTITKMSRDADSGSAAQEINFWLSMETALEGIENQLRGDGVQLTMDILRHAKRYQATLSFVADTGLREATDLVQKYNQLMRDFPLDELLSATSLQKVRESLVLIFNHLNKKLKICPYPIKRALALVEAISGDLDSQIHSLLNGRTIMHLDYREFRTLMKTAGSIWRTWDDNLKEFTNVARESTRRRNEKFIPIKINARHDKTQERLKYINTFRVNHEQLQRTIANVLGPKSYSAEDAAAGAAADGAVIVEEIGDVDAVEEVAQAYAALKSVDVLDVSPTGTQNWITAEIAYNERTSRVENSIIARLRDRLATAKNANEMFRVFSKFNALLVRPKIRGAIGEYQTQLIDNVKQDISALHERFKQQYGHSEAHAMAQLRDLPPVSGAIVWARQIERQLDGYMRKVEDVLGEDWHLHTEGQKLQAESNLFRKKLDTRPVFETWLHDVQRRRITISGRLFNIIRNRAAGNTLELAVNFDAQIIALFKEIRNLIWLNFQVPHAVSNISKEAKRVYPYAISLMESVRTLLQTNRSILSMTDVAILLNGYMNDAQSMIVRGIPLRWESFVHSYELHVKQAALVNGALDSVIPSRGESKHVQFVREFAASAAVLQHKTAVLASINDTIQKAIHELKTCPYEFSAFKQRLDAIQAAVDKLNLENYVNLGFWVHNLNQKIEGILSERLHKAIREWMNSFQESQSGQPMQKVNGNGDTDTTAYNIEFPGLTHEISMRNQVLHLDPPLQYARATWFSHFDNWLGIICNLEKIKSSRYQISIEVQKVQLSESCFADLPQHCTNELILVYSAIETRLKEVSEYVDKWLQFQSLWDLQSEQVYDILGDDLSQWLQLLQEIRKSRATFDTSEVSRSFGNIKIDYEQVQTRVNAKYDQWQHEILLKFGSKLGNRMREVHSEIATARHDLEGKSLDSASTAHAVAFITSVQQCKRKAKVWEPEVDLFRQGQATLVRQRYQFPSDWLHVENVDGEWAALNELLGRKGKIVEEQTEALRAKIAAEDKVINDKITEAIAQWNEEKPVSGTIPPEEASRSLSMFQTRLESLQSEFEMVSKAKEALDLPPSAESSLPAILEEVQDFMSVWAALSTIWRSLNDLRDTLWTSIQPRKLRQSIDGLIKMTKEMPSRMRQYAAFEHIQNVLKQLLKVNPLLSDMKSEAVRERHWLKIYKALKPGMRFSLVSLTLGDVWDLQLAASETVIRNIIAQAQGEMALEEFLKSVRETWQNYSLDLVNYQNKCRLIRGFDDLFAKCSENLNSLQAMRHSPYYKEFEEDASSWEDKLNRVHVLFDVWIDVQRQWVYLEGVFTGNADIKHLLPLESSRFQNINSEFFAVMKKVYKSPFVLDVLAINGVQKSLERLAELLNKIQKALGEYLERERVSFPRFYFVGDEDLLEIIGNSNDIFRVAKHFKKMFAGLSGVLMDDDNNIVGFTSKEGEEVRLKKEVNLVKTPRINDWLTALESNMKLTLAELLAEAIEQFEPIYNSAEVDRTAFDDFIANYPAQIVVLASQVVWTNEVQKSLENSGTTLPTLYDAQVRILELLAVTVLGDLDPISRKKCEHLITEFVHQRDTISKLIASNATSATHYLWLLQMRYVYQADGDFLQRLYVHMANAKLNYGFEYLGVPERLVRTPLTDRCFLTLTQALCQRLGGSPYGPAGTGKTESVKALGLQLGRFTLVFCCDDTFDFQAMGRIFLGICQVGAWGCFDEFNRLEERILSAVSQQIQNIQIGLRNKETDEKSQIDLVGRRLTVNMNTGIFITMNPGYAGRSNLPDNLKKLFRSVAMSKPDKELIAEVMLFSQGFKQAKRLSQQTVPFFDHCSTRLSKQAHYDFGLRALKSVLVSSGGLKRARIANSDGDLGPDEIVEPQIIVQSLRETIAPKLVREDVATMLQIQEQDFAGVEYVPANYEALTAAIREIAREQHFVDSEMWITKILQLYQIQSIHHGVMMVGKSGSGKSSAWKILLQALQRIEGVEGVSHIIDSKVMSKEALYGSLDSTTREWTDGLFTGILRKIVDNLRGEDTKRHWIVFDGDVDPEWVENLNSVLDDNKLLTLPNGERLNLPPNVRIMFEVESLKYATLATVSRCGMVWFNEDTVTPSMIITNYVESLKTKTFEDLDDDSVPSGQSAVKTQDCQDMLSTILSQLLQTDELVHKSLGEAKKYNHIMEFTEIRALNTLFSLLNKACRNILEYNIQHVDFPLEYEQIESYISKKLLLALVWSFTGDCPLGDRKSFGEFVSGLTTIDLPIETNSSIIDFDVTLPKGTWSSWQSQVPTIDVNTHSITQTDVVIPTVDTVRHEDVLYSWLAEHKPLLLCGPPGSGKTMTLFAALRKLPNMEVVGLNFSSATTPDLLIKTFEQYCEYKKTLSGVVMSPNQIGRWLVIFCDEINLPAPDKYGTQRAISFLRQLVEQNGFWRTSDKTWVSLDRIQFVGACNPPTDAGRTPLAERFLRHSPLVMVDYPGEISLNQIYGTFNSAILKILPLLRGYSESLTKAMVQFYLESQQRFTPKIQPHYVYSPRELTRWVRGVYEAIKPLESLSVEGLVRIWAHEALRLFQDRLVTEEERAWTADAVRRIALEHFPTIDQEAALKGPILFSNWLSRNYVPVEQEQLRDFVKARLKTFCEEEVDVPLVLFNDVLEHALRIDRVFRQPQGHLILIGVSGSGKTTLSRFVAWMNGLKVFQIKVHGKYSSEDFDDDLRSVLRRAGCKGEKICFIMDESNVLDSGFLERMNTLLANAEVPGLFEGDEFSSLMTACKEGAQRQGLILDSQEELYKWFTQQIVKNLHVVFTMNPPEEGLSSKAATSPALFNRCVLNWMGDWSDQALFQVGSELTQSVDLDKPGFVAPDSIPVAYRELSLPASHRDTVINAMVYIHHSLQRFNQRLQKQQGKTTYLTPRHYLDFVAQYVKLFNEKREDLEEQQRHLNVGLEKLRDTVEKVSDLRGSLAQKKMQLEKKDAEANEKLQRMVADQREAEQRKAVSLEVQAALEKQEKEVALRKDVVLHDLARAEPAVLEAQKSVSNIKRQHLTEVRSMGNPPAGVRLALEAVCTLLGHKVDSWKTIQGIVRRDDFIASIVNYDNEKQMTKNHRLKMQNEFFSKEDFTYERVNRASKACGPLVQWVEAQVNYSAILDRVGPLRDEVGQLEEQALQTKAEAQAIENTINDLESSIATYKSEYAALISETQAIKAEMERVQFKVDRSVRLLDSLSSERTRWEEGSKSFETQISTLIGDVLIAAAFLAYAGFYDQQFRKAMTEDWVQHLVQSGISLKPHNPITEYLSNADERLAWQAHSLPVDDLSTENAIFLKRYNRYPLIIDPSGRVTEFLQKESSDRKLTVTSFLDDSFVKQLESALRFGNPILIQDAEHLDPILNHVLNKEYQKTGGRVLIQLGKQEIDFSPSFKLFLSTRDPSATFAPDVCSRTTFVNFTITQSSLQIQSLNEVLKSERDDVDRRRSDLVKAQGEFNVHLRQLEKRLLQALNESHGNILDDDNVIETLETLKKEAAEISRKMAETEGVMTEVEEITQRYSIIARSCSAVFAVLEQLHHINHFYQFSLQYFTDIFESVLHGNPHLENSGLRKMEDYQQRIQIILRDLFVTTYQRTSLGVIQKDRITLAMLLAQAAPYPMDKSIIDTILDESVEGTDLSANPEAKVQVMSAFGNMSLFKAHLPSVTAEQWDQFLGEELAENFVPKVWDENTSELDKLLRSLLLVKLCRMDRFVPAAERFIVAVFGRELYEGSTDLKDIVGQVTATAPISLSSSPGFDASYKVDALVERTHATCANIAMGSNEGLESADKAISNAASAGTWVLVKNVHLAPSWLQSLEKRLASLKPHKDFRLFLSMESSPKIPVNLIRASRVLMYEQPAGVRANMKDSLSSLSTRASKAPVEKARVYLLLCFLHAVVQERLRYAPSLGWKGFWEFNDSDYECSANIIDHWVDVVAQGRSNVAPQKLPWDMIRTLITEMYGGKVDDSDDFQQLERLVHSFLTPATFEADYKLVEGVENDECLILPGETGLPAFVEWVNKLPEREPPTYLGLPANAEKLLLVGHGKKMISDLARITSLLDEGEQLMIDA', 4345, 'P45444; C8VQK6; Q5BH62;', 'KD01163', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'nudA', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC', '-', '-', '2875894'),
(1164, 'F4I241', 'Mitotic checkpoint protein BUB3.3', 'GO:0000777', 34763, '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. 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 (By similarity). {ECO:0000250}.', 'MSGDRLEFENPIEDAVSRLRFSPQSNNLLVASWDSYLRLYDVESSSLSLELNSQAALLDCCFENESTSFTSGSDGFIRRYDLNAGTVDTIGRHDDISTSIVYSYEKGEVISTGFDEKIKFWDTRQRESLVFSTDAGGAVGCVTVSGNNLVVCVDASMHIYDLRNLDEAFQSYASQVEVPIRCITSVPYSRGYAVGSVDGRVAVDFPNTSCSSEIKYSFRCHPKSRNGRLDGVCINAIEFSPCGSGTFVTGDNEGYVISWNAKSRRRLNELPRYSNSIASLAFDHTGELLAIASSHTYQDAKEKEEAPQVFIHRL', 314, 'F4I241; F4I242; Q8LA29; Q9C795; Q9C986;', 'KD01164', 'Arabidopsis thaliana (Mouse-ear cress)', 'BUB3.3', '#Mitotic checkpoint protein BUB3.3#Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 3.3', '-', '-', '843272'),
(1165, 'Q28ER3', 'Baculoviral IAP repeat-containing protein 5.2', 'GO:0000777===GO:0032133', 17882, '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. Does not appear to exhibit anti-apoptotic activity. Plays a role in increasing blood vessel size during development (By similarity). {ECO:0000250|UniProtKB:Q50L39; ECO:0000250|UniProtKB:Q804H7}.', 'MSASLISALPPCGNEPPMPDEWRLYRLATRLSTFANWPFTEDCACTPERMAEAGFVHCPSDNSPDVVKCFFCLKELEGWQPEDDPMDEHKKHSPSCLFIALKKKAEELTLSEFLKLDLERTKIKMQKQMNQHIENFQAKANVVRGHLEKLDADETQ', 156, 'Q28ER3;', 'KD01165', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'birc5.2', '#Baculoviral IAP repeat-containing protein 5.2#Survivin 2 {ECO:0000250|UniProtKB:Q50L39}#Survivin {ECO:0000312|EMBL:CAJ83536.1}', '-', '-', '733575'),
(1166, 'O43013', 'Uncharacterized protein C2G2.14', 'GO:0051315===GO:0072766===GO:0000780', 59583, '', 'MSFNPAAGLLGKLKKLWNDTKNDYLEWERSQQGQISESVVKNHSPSKRKRRPSKEPSLSPKRRKNILNDQKKDEESIPNAGTQSQNFTHLSASKIRISDEDRIKPLVDLNQDHSFDMAYLTPASAPPPRFRFVPPKSDAKSHSAPRSLEGVTSLSDSHFNSLEANLKAISKDSNNKAHNNRYDESSLTNPEFSILVERLKSIEENLQSLQERISHCERSVSLSPSFAPPSNVKSPVQQHRSFVSSSARAKKNWGRQSNSPNSNKKTDHAYPGASMNTERGLIQNLEDSDDIHEESSDTLEEPLLINELNRTSFLNSNNNLKLNEAEENQNLLNLRSPKSSGKADNLTIKSSSNIDKVTSNDLYLDNNLQSHFKVTESQPTNLGRKEYSNSPFSIRARKDAATTSSSFESYHNTQTIQSPMKFTKATPLKDNESASVDESKVNVLSENQSLQADTATLEQLTPIPKARWNQLANKHPSLSNSAASPPVSSPGLRRSHIPVHEGLKHTRDGVAETKDALAKLREKMQERLKNHTS', 533, 'O43013;', 'KD01166', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'SPBC2G2.14', '#Uncharacterized protein C2G2.14', '-', '-', '2540281'),
(1167, 'Q0III3', 'Cytoplasmic dynein 1 intermediate chain 2', 'GO:0005868', 68377, '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 chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. Involved in membrane-transport; such as Golgi apparatus; late endosomes and lysosomes (By similarity). {ECO:0000250}.', 'MSDKSELKAELERKKQRLAQIREGKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTAESPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQVDFPPREIVTYTKETQTPVMAQPKEDEEEEDDVVTPKPPIEPEEEKTLKKDEESDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHSAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA', 612, 'Q0III3;', 'KD01167', 'Bos taurus (Bovine)', 'DYNC1I2', '#Cytoplasmic dynein 1 intermediate chain 2#Cytoplasmic dynein intermediate chain 2#Dynein intermediate chain 2; cytosolic#DH IC-2', '-', '-', '526329'),
(1168, 'Q8IW41', 'MAP kinase-activated protein kinase 5', 'c;k', 54220, 'Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3; ERK3/MAPK6; ERK4/MAPK4; HSP27/HSPB1; p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras- induced senescence and phosphorylating p53/TP53. Involved in post- transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3; enabling expression of miR-34b and miR-34c; 2 post-transcriptional regulators of MYC that bind to the 3''UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear; but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4); ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5; which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation; inducing F-actin rearrangement. {ECO:0000269|PubMed:17254968; ECO:0000269|PubMed:17728103; ECO:0000269|PubMed:19166925; ECO:0000269|PubMed:21329882; ECO:0000269|PubMed:9628874}.', 'MSEESDMDKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALRHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKIDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDSVYIHDHENGAEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDTLQSFSWNGRGFTDKVDRLKLAEIVKQVIEEQTTSHESQ', 473, 'Q8IW41; B3KVA5; O60491; Q86X46; Q9BVX9; Q9UG86;', 'KD01168', 'Homo sapiens (Human)', 'MAPKAPK5', '#MAP kinase-activated protein kinase 5#MAPK-activated protein kinase 5#MAPKAP kinase 5#MAPKAP-K5#MAPKAPK-5#MK-5#MK5#2.7.11.1#p38-regulated/activated protein kinase#PRAK', '-', 'ENSG00000234608', '-'),
(1169, 'Q4WTT8', 'E3 ubiquitin ligase complex SCF subunit sconC', 'GO:0051382===GO:0031518', 18141, 'Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes; which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression; probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}.', 'MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE', 158, 'Q4WTT8;', 'KD01169', 'Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSA1100) (Aspergillus fumigatus)', 'sconC', '#E3 ubiquitin ligase complex SCF subunit sconC#Sulfur controller C#Sulfur metabolite repression control protein C', '-', '-', '3511133'),
(1170, 'A8XSQ8', 'Homeobox protein pal-1', 'GO:0000777', 30296, '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 (By similarity). {ECO:0000250|UniProtKB:P34766}.', 'MSVDVKSEFSENDSSSSSSSPTNVNNVAWPNYQMMPFMNAQPLRDKMLQPSFDPQLYGRWPQMGEAGFYGHSDIYSTFALPQLSTNGQILPTAEVVEVKPPLSNGSSSSDSGMYPSPNDLTPFPSTSSGIGASSSSSDLQAAAAAAANYQMRAATCYQQSVWPFMDYQQPFPWKMPLGSAGKERRASSDTKSLPTGPGTNNVRVRTADKYRMVYSDYQRLELEKEFHTSAFITSDRKSQLSTMLSLTERQIKIWFQNRRAKDRRDKQKIRL', 271, 'A8XSQ8;', 'KD01170', 'Caenorhabditis briggsae', 'pal-1', '#Homeobox protein pal-1 {ECO:0000250|UniProtKB:P34766}#Posterior alae in males protein 1 {ECO:0000250|UniProtKB:P34766}', '-', '-', '8584037'),
(1171, 'Q91WD7', 'Kinesin-like protein KIF18A', 'GO:0005828', 100935, 'Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase; thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression (By similarity). {ECO:0000250}.', 'MSGTEEDLCHRMKVVVRVRPENTKEKAVQFCKVVHVVDKHILSFDPKQEEISFFHRKKTTNFDITKRQNKDLKFVFDAVFDETSTQMEVFEHTTKPILHSFLNGYNCTVFAYGATGSGKTHTMLGSAAEPGVMYLTMLDLFKCIDEIKEEKECSTAVSYLEVYNEQIRDLLTNSGPLAVREDSQKGVVVQGLTLHQPKSSEEILQLLDNGNKNRTQHPTDVNAVSSRSHAVFQIYLRQQDKTASINQNVRIAKMSLIDLAGSERASVSGAKGSRFVEGTNINKSLLALGNVINALANTKRRNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSLFYDDTYNTLKYANRAKEIKSSLKSNVLNLNSHISQYVKICNMQKAEILMLKEKLKAYEEQKALSDRNDCAKLVHSNPEDRETERFQEILNCLFQNREGIRQEYLKLEMLLKANALKSSYHQQCHKQIEMMCSEDKVEKATCKRDHRLEKLKTNSCFLEKKKEEVSKQFDENTNWLHRVENEMRLLGQNGDIPEALNKELHCHHLHLQNKELKTQMAHMTALACLQEQQHKQTEAVLNALLPVLRKQYWKLKETGLSNAAFDSDFKDIEHLVERKKVVAWADQTNEHSNRNDLPGISLLMTFPQLEPIQSISCCTSVSDPNVLKLTPQRRTRRKIIPSPLKVQHTQKSALSESTQLNDSFSKELQPIVYTPEDCKKAQDLFPSLTRTSSQSANVMNDNSQKALCRIESPLSRTECKQGLYSTSTLCDSIRGLKNKWPEQEPLASSKSSVHRIESSSFSTKDSMPESAGVPSYMAMTTAAKRKWKQMSSTSNASIKSDESCGFAKRIRRDNSSVKPMQENRLKVGYKRNTNKTNSNMLRKFRRNTSKENVQ', 886, 'Q91WD7; Q3TP77; Q8BLL1;', 'KD01171', 'Mus musculus (Mouse)', 'Kif18a', '#Kinesin-like protein KIF18A', '-', '-', '228421'),
(1172, 'Q750P7', 'DASH complex subunit SPC19', 'GO:0008608===GO:0051987===GO:0042729', 16850, '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}.', 'MDISLDESCVALESSVKLLGKTLERLAEQGEHSRRLTSTLLRSKRVFELVSEYDLQRARLDVIEEVEPVVEKLCSKLEKSLNKLERERATLQQTYELNQLRLNNRLAGSGGRRPVVMGTSTTEELGRLREAKQRKAALEREIAEVRGT', 148, 'Q750P7;', 'KD01172', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'SPC19', '#DASH complex subunit SPC19#Outer kinetochore protein SPC19', '-', '-', '4622861'),
(1173, 'Q9HDY7', 'Uncharacterized protein PB1A10.02', 'GO:0051382===GO:0000780===k', 37694, '', 'MCNRQPKAVDLPPNYSCPHLLSFQSVEFNTNPTACDDVFCKRIESEKKYNDFLESLFKKYGRDTSDIADEVDLATGEIIVNNGHLEALKTKDDIWDPTFNNLEISASNGYEKKLDSSIGNPGEKAVSPVHIEDFQSPQIYKFKNLSLRDEMVSDCVFADEVPLASLFVENVCNETIPSQSCVRLKINDKTRKVDASALEKKSCLLPNSSGTLTDQRGLDTIKHKSIEQNEILHVISDTLSSPRRRNPLLSSPKTPLRRSFSKSKVRNSNSTKRRNFISLISMISPRPNLSTHHFNLGFQPLSQQTSFSGSSTQNPHSSSTCKKAFCFQCISESKKC', 336, 'Q9HDY7;', 'KD01173', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'SPAPB1A10.02', '#Uncharacterized protein PB1A10.02', '-', '-', '2543449'),
(1174, 'P46100', 'Transcriptional regulator ATRX', 'k', 282586, 'Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3- containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S- phase and telomeres; and the in vitro remodeling of H3.3- containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomers. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according (PubMed:24500201) is not sufficient to decrease chromatin condensation at telomers nor to increase expression of telomeric RNA in fibroblasts. May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone H2AFY; particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele; required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. {ECO:0000269|PubMed:12953102; ECO:0000269|PubMed:14990586; ECO:0000269|PubMed:20504901; ECO:0000269|PubMed:20651253; ECO:0000269|PubMed:21029860; ECO:0000269|PubMed:22391447; ECO:0000269|PubMed:22829774; ECO:0000269|PubMed:24500201}.', 'MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLAMNQNTDKISGSGSNSDMMENSKEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQSLPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKVDSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLIETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAMDAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVTKELYVKLTPVSLSNSPIKGADCQEVPQDKDGYKSCGLNPKLEKCGLGQENSDNEHLVENEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNSDEECNETVKEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQSETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNLKTSQEGSSDDAERKQERETFSSAEGTVDKDTTIMELRDRLPKKQQASASTDGVDKLSGKEQSFTSLEVRKVAETKEKSKHLKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKKQSKKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKLPEREEICHFPKGIKQIKNGTTDGEKKSKKIRDKTSKKKDELSDYAEKSTGKGDSCDSSEDKKSKNGAYGREKKRCKLLGKSSRKRQDCSSSDTEKYSMKEDGCNSSDKRLKRIELRERRNLSSKRNTKEIQSGSSSSDAEESSEDNKKKKQRTSSKKKAVIVKEKKRNSLRTSTKRKQADITSSSSSDIEDDDQNSIGEGSSDEQKIKPVTENLVLSSHTGFCQSSGDEALSKSVPVTVDDDDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPEEGKKRTGKQNEENPGDEEAKNQVNSESDSDSEESKKPRYRHRLLRHKLTVSDGESGEEKKTKPKEHKEVKGRNRRKVSSEDSEDSDFQESGVSEEVSESEDEQRPRTRSAKKAELEENQRSYKQKKKRRRIKVQEDSSSENKSNSEEEEEEKEEEEEEEEEEEEEEEDENDDSKSPGKGRKKIRKILKDDKLRTETQNALKEEEERRKRIAEREREREKLREVIEIEDASPTKCPITTKLVLDEDEETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRVMKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQYYLDHLTGVGNNSEGGRGKAGAKLFQDFQMLSRIWTHPWCLQLDYISKENKGYFDEDSMDEFIASDSDETSMSLSSDDYTKKKKKGKKGKKDSSSSGSGSDNDVEVIKVWNSRSRGGGEGNVDETGNNPSVSLKLEESKATSSSNPSSPAPDWYKDFVTDADAEVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELASREKTEDKDKPLIYKGEGKWLRNIDYYRLDGSTTAQSRKKWAEEFNDETNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNELTELYTFEPDLLDDPNSEKKKKRDTPMLPKDTILAELLQIHKEHIVGYHEHDSLLDHKEEEELTEEERKAAWAEYEAEKKGLTMRFNIPTGTNLPPVSFNSQTPYIPFNLGALSAMSNQQLEDLINQGREKVVEATNSVTAVRIQPLEDIISAVWKENMNLSEAQVQALALSRQASQELDVKRREAIYNDVLTKQQMLISCVQRILMNRRLQQQYNQQQQQQMTYQQATLGHLMMPKPPNLIMNPSNYQQIDMRGMYQPVAGGMQPPPLQRAPPPMRSKNPGPSQGKSM', 2492, 'P46100; D3DTE2; P51068; Q15886; Q59FB5; Q59H31; Q5H9A2; Q5JWI4;Q7Z2J1; Q9H0Z1; Q9NTS3;', 'KD01174', 'Homo sapiens (Human)', 'ATRX', '#Transcriptional regulator ATRX#3.6.4.12#ATP-dependent helicase ATRX#X-linked helicase II#X-linked nuclear protein#XNP#Znf-HX', '-', 'ENSG00000085224', '-'),
(1175, 'O94534', 'Spindle pole body component alp14', 'GO:0000778===GO:0051315===c;k', 89446, 'Required for bipolar spindle formation and proper chromosome segregation. Has a role in connecting the kinetochores and the plus end of pole to chromosome microtubules. Also required for the activation of the spindle checkpoint pathway. {ECO:0000269|PubMed:11432827; ECO:0000269|PubMed:14742702}.', 'MSQDQEEDYSKLPLESRIVHKVWKVRLSAYEECSKSFSLSADGSDNCFELWNNQSELWKSVLTDSNVAAQEAGTAAFVAYCRFSDPSHLLKAREISVLSISEKCLTSPRAGTRENALEALMLLVEADSAAPVIESIIPSLSARSPKVIASNVAAIASLVEQFGAKVIPSKMIIPHISNLFGHADKNVRKEASRLTVNIYRWTGDPLKDLLFKDLRPVQTKELESLFAELPTEPPKQTRFLKSQQPTSEPNVETQVEEQPALENEESEPEPSDDQFDLVEEVDVLPNVDPNLETLMASSKWKDRKEALDKLLPVLSQPKIKDNDFFNLVAILTKSVSKDANIMVVINAAHCIQAMAKGLRSNFSKYASTSINALLERSKEKKANVIESLSSAMDAVLATSSLDDLAELIASFAGNKNPQIKSSCFSLFSRSFSNMTSLPSKFTVDTCAKACVPGVSDTFEPVRSAAAEALGVLMKLVGERAINQYLSPLDDIRKSKIRSFYETATVKAKAPTKKSKVKPSKQEESKVVVPSNAKAVKKSVVPSSPVVPSPRKATNKSLSMDVSKGNAFENGPLLPRPTTRPVSRGLSRGTSSSLQQKVKASTPLNSGALNETVQNLKNMELDDPAPQPAKHSRVDRYEHPKVLEDNDSTISSLESLKRENEELREQLKVEHEENISMQKQLSELKGELNTLRSARKASPIGDRKPAFMRRANTDFLELSTSPSFQRSVREFEPTRPKLYSSIDVNQRSPLASAKTNGNFTFHAELPRSPFSSRANNINPDWTKAIDLAAKLKQKITEMKQTDQRHQGLIH', 809, 'O94534;', 'KD01175', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'alp14', '#Spindle pole body component alp14#Altered polarity protein 14', '-', '-', '2539497'),
(1176, 'Q23542', 'DNC-1; isoform a', 'c;k', 148430, '', 'MSFEIGTRVKTSSGNGRVVFCGQTQFAEGDWVGVILDTATGKNNGTVQNVQYFECEPNFGVFVKSSAVELEDASKRSGLKAPAASAIRKDSSVMSRSAGSKASPGSSPGMSPAASSEKLTGRQTGMGPRSMSKLADPNESRMVREFSNLSQSSVASSRASASASKPRPQFTAPDPRRQSLAPPKKASTTTAPVSKPSLSKPRQSLAPSKPAEVTPQKPVPAAQASEAGDPPNELPLPTMTESGTELPKESVLSRAKKIDDTGPAAPMSPLSTTAAARPRTTSVSSSAQESSTEIEYLRNQVKELTEKLEAARVKRKEDHTKVMELDRVSFELRSSEEVRSRLIQKITELEKQIGDERIAKEQLQAWQDENKVLLSDHQDTMEMATIEKELAEERADSLQNDVLTLTEKLESMETELEILKEEMANGGGAAQVGNSVQMKQIEIQNDKLKDALIKLRDLNAQATLDRQKAVDEAERLKTENSELIRVAENLKRQTEIAESKIAGFQEQIDAAMGAEAMVTQLTDKNFNMEERIMQLEETIEDMEEARDLDEQLAEVQKQQVKDLMKEIEQLKIHIHELNGRIRDEQKHAVDLSQTILKFRERMANLNSQIQDQKDQVLSLEEQLHGHISVDNDRASMVNQLQISANRNFAEDVERQVNAIEVEFARRQAGYLKAFLPDNFSRVGGENDSILLVVMLPRLAAKTKLFASLAAQCFPQVPGGMRREHVTKSHKGEQWAHVARVNYLANSINAALGKLESAIGETTVEVLIKLTETYGEMSTHEKTVDQYLELLKKSRFDENTSLDSFVRPLVYFQNMFSLHIGGDGFNAAHWVSEICASLSAGLAYCRVNTQRISYFLQESITAGEVYNMLQTLNDEFAACESVILKAYRLLPGNVSGSEQKILKLESEFTEDLLNSVVQLDKMVSILQEVCANGALSFGGISETEGFDEKRVKEMINAVLGKQDGYIAIDKTFDPIRALIKSLRDSLEKVNSTLESAKMEHSAPEKKSFPPLLDRAHHRKQAAQEAEGLRWQMEKKDNEMLELRKQMKARIEDVSNYKLRLDMAESRLNSTDKAEGDKVKHLEEKINQMVADHRRKQIEYDESMDALQREMKEVESDNLELKQRANKISKEALWKNIQSMETRSSGSPSVPMSTSIDEGGASRGEVVFLENQLNKQTNARKRAELEVRKLKGELAQAGSKRFSAVPGLISGPITLESQTRQDLLLKLIDNLHDESLRLRREEVNHQAYVPSNPKISTEKMVEEMEIFNVKREQFFDKLNSVNRRLRRVWFDAWGEEYPFEIAAKSRPIVAVPEPKKFEEISAKWGIVW', 1326, 'Q23542;', 'KD01176', 'Caenorhabditis elegans', 'dnc-1', '#DNC-1; isoform a {ECO:0000313|EMBL:CAA93427.2}', '-', '-', '177987'),
(1177, 'O96019', 'Actin-like protein 6A', 'k', 47461, 'Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors- specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. 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). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones 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. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction; tumor suppressor mediated growth arrest and replicative senescence; apoptosis; and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation; DNA replication and probably DNA repair. {ECO:0000250; ECO:0000269|PubMed:14966270}.', 'MSGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGDKGKQGGPTYYIDTNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHPVLMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKRKEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGAERLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQSFTDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP', 429, 'O96019; B3KMN1; D3DNR9; Q8TAE5; Q9BVS8; Q9H0W6;', 'KD01177', 'Homo sapiens (Human)', 'ACTL6A', '#Actin-like protein 6A#53 kDa BRG1-associated factor A#Actin-related protein Baf53a#ArpNbeta#BRG1-associated factor 53A#BAF53A#INO80 complex subunit K', '-', 'ENSG00000136518', '-'),
(1178, 'Q755C4', 'Spindle assembly checkpoint kinase', 'GO:0005828===GO:0034501===GO:0000778===GO:0008608===GO:0032133', 42445, '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}.', 'MDADAILKKDQRRSSLKQRNLLLSMRLNQTTATNGAPPQARVQPGKGYRNPGKVLSPIRNQEMSPGKRPTLEISELKNVSPINQAHKTGKARAGGVPLSKLQNLKLADFEIGKVLGKGKFGRVYCVRHIESGFVCALKAMEKKDIIQYNIEKQFRREVEIQSSLRHPNLTQLYGYFHDEKRVYLLMEYLVNGELYKHLKGRSHFNDVVASYYVYQMADALDYMHERNILHRDIKPENIIIGFNNTIKLTDFGWSVITPKGSKRKTLCGTVDYLSPELIRSREYNEKVDVWALGVLTYELLVGSPPFEEESKELTYKRILKRNLIFPDHVDTEARHLISRLLEYDPGDRIPLKEVKKHPWIEKNKPFW', 367, 'Q755C4;', 'KD01178', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'IPL1', '#Spindle assembly checkpoint kinase#2.7.11.1#Aurora kinase', '-', '-', '4621676'),
(1179, 'P16522', 'Anaphase-promoting complex subunit CDC23', 'GO:0000777===k', 73114, 'Component of the anaphase promoting complex/cyclosome (APC/C); a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and; in the presence of ubiquitin-conjugating E2 enzymes; it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis; the APC/C is activated by CDC20 and targets securin PDS1; the B-type cyclin CLB5; and other anaphase inhibitory proteins for proteolysis; thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1; degradation of CLB5 allows activation of the APC/C by CDH1; which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. {ECO:0000269|PubMed:10871279; ECO:0000269|PubMed:12413490; ECO:0000269|PubMed:12609981; ECO:0000269|PubMed:7925276; ECO:0000269|PubMed:8423787}.', 'MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEFLLQVFPNFTFLKAYNATISYNNLDYVTAESRFDDIVKQDPYRLNDLETYSNILYVMQKNSKLAYLAQFVSQIDRFRPETCCIIANYYSARQEHEKSIMYFRRALTLDKKTTNAWTLMGHEFVELSNSHAAIECYRRAVDICPRDFKAWFGLGQAYALLDMHLYSLYYFQKACTLKPWDRRIWQVLGECYSKTGNKVEAIKCYKRSIKASQTVDQNTSIYYRLAQLYEELEDLQECKKFMMKCVDVEELLEGIVTDETVKARLWLAIFEIKAGNYQLAYDYAMGVSSGTSQEIEEARMLARECRRHM', 626, 'P16522; D3DLB5;', 'KD01179', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CDC23', '#Anaphase-promoting complex subunit CDC23#Cell division control protein 23', '-', '-', '856571'),
(1180, 'Q74Z51', 'DASH complex subunit DAD4', 'GO:0008608===GO:0042729', 8160, '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}.', 'MENPHEKVQVGILARIVGNVERLNQSVATLNQELERINTRNRNLELMGQMCEHYGRATAFNLKTTGNRQGPV', 72, 'Q74Z51;', 'KD01180', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DAD4', '#DASH complex subunit DAD4#Outer kinetochore protein DAD4', '-', '-', '4623324'),
(1181, 'Q14204', 'Cytoplasmic dynein 1 heavy chain 1', 'GO:0003777===GO:0005868===c;k;m', 532408, '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.', 'MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVERSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPFFKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPTFLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDTGLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRKLMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVIVRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRDLPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTIESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNTISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNRVQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVHELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAVMGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKYDSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQRFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQALTIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLRQNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQKNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDALSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRSLERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSREGEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSENVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLSQMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCELLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKALERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLDDNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKGKEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFPMQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETHKVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKDYIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNYIVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEISDAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVLYENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGSTPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDRLLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQADKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRTFSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPWSALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSWLGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKRTVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGVTGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGVAVLCTE', 4646, 'Q14204; B0I1R0; Q6DKQ7; Q8WU28; Q92814; Q9Y4G5;', 'KD01181', 'Homo sapiens (Human)', 'DYNC1H1', '#Cytoplasmic dynein 1 heavy chain 1#Cytoplasmic dynein heavy chain 1#Dynein heavy chain; cytosolic', '-', 'ENSG00000197102', '-'),
(1182, 'Q14203', 'Dynactin subunit 1', 'GO:0000776===c;k;m', 141695, '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.', 'MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFELSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGPQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLLVAALEELAFKASEQIYGTPSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGAIPGQAPGSVPGPGLVKDSPLLLQQISAMRLHISQLQHENSILKGAQMKASLASLPPLHVAKLSHEGPGSELPAGALYRKTSQLLETLNQLSTHTHVVDITRTSPAAKSPSAQLMEQVAQLKSLSDTVEKLKDEVLKETVSQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGFGQRHRLVLTQEQLHQLHSRLIS', 1278, 'Q14203; A8MY36; B4DM45; E9PFS5; E9PGE1; G5E9H4; O95296; Q6IQ37;Q9BRM9; Q9UIU1; Q9UIU2;', 'KD01182', 'Homo sapiens (Human)', 'DCTN1', '#Dynactin subunit 1#150 kDa dynein-associated polypeptide#DAP-150#DP-150#p135#p150-glued', '-', 'ENSG00000237737', '-'),
(1183, 'Q6P9L6', 'Kinesin-like protein KIF15', 'GO:0003777', 160120, 'Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. {ECO:0000250}.', 'MAPGCKSELRNVTNSHSNQPSNEGDAIKVFVRIRPAEEGARSADGEQSFCLSVLSQTTLRLHSNPDPKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSDSDNFSHNLRGIIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEVYNEQIYDLLDSASVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSETVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGNGKQRHICYRDSKLTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLKEQLSQFTSGQITPESLLARDKEKTNYIEYFLEAMLFFKKSEQEKKSLIEKITQLEDLTLKKEKFIQSNKMIVKFREDQIMRLERLHKEGRGSFLPEEQDRLLSELRDEVQTLREHVEHHPRLAKYAMENHSLREENRRLKLLAPVKRAHEIDAQSIARLEKAFAEVSSTETNDKGLQGFSPKALKESSFFTNTEKLKAQLLQIQTELNNSKQEYEEFKELTRKKQLELESELQSLQKANLNLENLLEATKVCKRQEVSQLNKLHAETLKIITTPTKAYQLCSRLVPKSSPEVGSFGFLCTESSSRLDNDILNEPVPPEMSEQALEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQQNVDKLEHHSTQMQELFSSERSDWTKQQQEHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYSTFKENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVDILELKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKTPPHFQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLESQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERLAKNKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFLEMEMLKKQLEFLAEENGKLVGHQNLHQKIQYVVRLKKENIRLTEETEKLRAENLFLKEKKKEF', 1387, 'Q6P9L6; O35065; Q70MX5;', 'KD01183', 'Mus musculus (Mouse)', 'Kif15', '#Kinesin-like protein KIF15#Kinesin-like protein 2#Kinesin-like protein 7', '-', '-', '209737'),
(1184, 'Q6ZMV9', 'Kinesin-like protein KIF6', 'GO:0003777', 92569, '', 'MVKQTIQIFARVKPPVRKHQQGIYSIDEDEKLIPSLEIILPRDLADGFVNNKRESYKFKFQRIFDQDANQETVFENIAKPVAGSVLAGYNGTIFAYGQTGSGKTFTITGGAERYSDRGIIPRTLSYIFEQLQKDSSKIYTTHISYLEIYNECGYDLLDPRHEASSLEDLPKVTILEDPDQNIHLKNLTLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTIHLSSKEPGSATVRHAKLHLVDLAGSERVAKTGVGGHLLTEAKYINLSLHYLEQVIIALSEKHRSHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRNLDESISTCRFAQRVALIKNEAVLNEEINPRLVIKRLQKEIQELKDELAMVTGEQRTEALTEAELLQLEKLITSFLEDQDSDSRLEVGADMRKVHHCFHHLKKLLNDKKILENNTVSSESKDQDCQEPLKEEEYRKLRDILKQRDNEINILVNMLKKEKKKAQEALHLAGMDRREFRQSQSPPFRLGNPEEGQRMRLSSAPSQAQDFSILGKRSSLLHKKIGMREEMSLGCQEAFEIFKRDHADSVTIDDNKQILKQRFSEAKALGESINEARSKIGHLKEEITQRHIQQVALGISENMAVPLMPDQQEEKLRSQLEEEKRRYKTMFTRLKALKVEIEHLQLLMDKAKVKLQKEFEVWWAEEATNLQVNSPAVNSLDHTKPFLQTSDSQHEWSQLLSNKSSGGWEVQDQGTGRFDVCDVNARKILPSPCPSPHSQKQSSTSTPLEDSIPKRPVSSIPLTGDSQTDSDIIAFIKARQSILQKQCLGSN', 814, 'Q6ZMV9; Q2MDE3; Q2MDE4; Q5T8J6; Q6ZWE3; Q86T87; Q8WTV4;', 'KD01184', 'Homo sapiens (Human)', 'KIF6', '#Kinesin-like protein KIF6', '-', 'ENSG00000164627', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1185, 'Q2NL05', 'Kinesin-like protein KIF2A', 'GO:0003777', 74994, '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}.', 'MVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEDIEPSPETPPPPTSSAKVNKIVKNRRTVASIKNEPPPRDNRVVGSARARPSQLPEQSSSAQQNARRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVNATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLAHKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTVDPTAAGDVRPIMHHPPNQIDDLEAQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWLEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL', 660, 'Q2NL05;', 'KD01185', 'Bos taurus (Bovine)', 'KIF2A', '#Kinesin-like protein KIF2A', '-', '-', '768014'),
(1186, 'Q9ERR1', 'Nuclear distribution protein nudE-like 1', 'GO:0000776===GO:0000777', 38366, '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. Plays a role; together with DISC1; in the regulation of neurite outgrowth. 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. {ECO:0000269|PubMed:12796778; ECO:0000269|PubMed:15208636; ECO:0000269|PubMed:15473966; ECO:0000269|PubMed:16107726; ECO:0000269|PubMed:16203747}.', 'MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYVPGSVNCGVMNSNGPECPRSGRATFFHKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV', 345, 'Q9ERR1; Q9D0Q4; Q9EPT6;', 'KD01186', 'Mus musculus (Mouse)', 'Ndel1', '#Nuclear distribution protein nudE-like 1#Protein mNudE-like#Protein Nudel#mNudE-L', '-', '-', '83431'),
(1187, 'Q10728', 'Protein phosphatase 1 regulatory subunit 12A', 'GO:0000776', 115283, 'Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex; involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN- dependent suppression of HIF1A activity (By similarity). {ECO:0000250}.', 'MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMENNQPQKTFKNKETLIIEPEKNASRIESLEQEKADEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPMASVTNAHTASTQAAPAAVTTPTLSSNQGTPTSPVKKFPTSTTKISPKEEERKDESPASWRLGLRKTGSYGALAEITASKEAQKEKDTAGVIRSASSPRLSSSLDNKEKEKDNKGTRLAYVAPTIPRRLGSTSDIEEKENRESSNLRTSSSYTRRKWEDDLKKNSSINEGSTYHRSCSFGRRQDDLISCSVPSTTSTPTVTSAAGLQKSFLSSTSTTAKTPPGSSPAGTQSSTSNRLWAEDSTEKEKDSAPTAATILVAPTVVSAAASSTTALTTTTAGTLSSTSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKDKEEKEKQDKEKQEEKKESEVSREDEYKQKYSRTYDETYARYRPVSTSSSSTPSSSSLSTLGSSLYASSQLNRPNSLVGITSAYSRGLTKDNEREGEKKEEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQERQSDTEDGSSKRDTQTDSVSRYDSSSTSSSDRYDSLLGRSASYSYLEERKPYGSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSLLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK', 1032, 'Q10728; Q62937; Q9WU33;', 'KD01187', 'Rattus norvegicus (Rat)', 'Ppp1r12a', '#Protein phosphatase 1 regulatory subunit 12A#MBSP#Myosin phosphatase-targeting subunit 1#Myosin phosphatase target subunit 1#Protein phosphatase myosin-binding subunit#Protein phosphatase subunit 1M#PP-1M#Serine/threonine protein phosphatase PP1 smooth muscle regulatory subunit M110', '-', '-', '116670'),
(1188, 'Q6J1J1', 'Baculoviral IAP repeat-containing protein 5', 'GO:0000777===GO:0032133', 16341, '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 cytokinesis 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}.', 'MGAQSLPPAWQLYLKDHRVSTFKNWPFLEGCACTPERMAAAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLSEFLKLDKERTKNKIAKETNNKQKEFEETAKKVRCAIEQLAALE', 142, 'Q6J1J1; Q32LI0;', 'KD01188', 'Bos taurus (Bovine)', 'BIRC5', '#Baculoviral IAP repeat-containing protein 5#Apoptosis inhibitor survivin', '-', '-', '414925'),
(1189, 'Q9ES39', 'Nuclear distribution protein nudE homolog 1', 'GO:0000776===GO:0000777', 38528, 'Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post- mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex (By similarity). {ECO:0000250}.', 'MEDSGKTFGSEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQAETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAHTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPMPSSGETKRTDMAVQATGSAPSTPITHQGSSSGLNTPETFRCGLGSPSSGTPLTPAARISALNIVGDLLRKVGALESKLASCKNFMYDQSPSRKSGPALGRGTKNRDGIDRRPGSTAVGDKGSGKRLEFAKPSSQLSSPALPSTQGVVKLLL', 344, 'Q9ES39; Q642F3;', 'KD01189', 'Rattus norvegicus (Rat)', 'Nde1', '#Nuclear distribution protein nudE homolog 1#NudE#rNudE', '-', '-', '83836'),
(1190, 'Q92922', 'SWI/SNF complex subunit SMARCC1', 'k', 122867, 'Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). May stimulate the ATPase activity of the catalytic subunit of the complex. 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). {ECO:0000250}.', 'MAAAAGGGGPGTAVGATGSGIAAAAAGLAVYRRKDGGPATKFWESPETVSQLDSVRVWLGKHYKKYVHADAPTNKTLAGLVVQLLQFQEDAFGKHVTNPAFTKLPAKCFMDFKAGGALCHILGAAYKYKNEQGWRRFDLQNPSRMDRNVEMFMNIEKTLVQNNCLTRPNIYLIPDIDLKLANKLKDIIKRHQGTFTDEKSKASHHIYPYSSSQDDEEWLRPVMRKEKQVLVHWGFYPDSYDTWVHSNDVDAEIEDPPIPEKPWKVHVKWILDTDIFNEWMNEEDYEVDENRKPVSFRQRISTKNEEPVRSPERRDRKASANARKRKHSPSPPPPTPTESRKKSGKKGQASLYGKRRSQKEEDEQEDLTKDMEDPTPVPNIEEVVLPKNVNLKKDSENTPVKGGTVADLDEQDEETVTAGGKEDEDPAKGDQSRSVDLGEDNVTEQTNHIIIPSYASWFDYNCIHVIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLTGDVCAVMRVHAFLEQWGLVNYQVDPESRPMAMGPPPTPHFNVLADTPSGLVPLHLRSPQVPAAQQMLNFPEKNKEKPVDLQNFGLRTDIYSKKTLAKSKGASAGREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLENSDASLGPLAYQPVPFSQSGNPVMSTVAFLASVVDPRVASAAAKAALEEFSRVREEVPLELVEAHVKKVQEAARASGKVDPTYGLESSCIAGTGPDEPEKLEGAEEEKMEADPDGQQPEKAENKVENETDEGDKAQDGENEKNSEKEQDSEVSEDTKSEEKETEENKELTDTCKERESDTGKKKVEHEISEGNVATAAAAALASAATKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREKEALEQQRQQLLTERQNFHMEQLKYAELRARQQMEQQQHGQNPQQAHQHSGGPGLAPLGAAGHPGMMPHQQPPPYPLMHHQMPPPHPPQPGQIPGPGSMMPGQHMPGRMIPTVAANIHPSGSGPTPPGMPPMPGNILGPRVPLTAPNGMYPPPPQQQPPPPPPADGVPPPPAPGPPASAAP', 1105, 'Q92922; Q17RS0; Q6P172; Q8IWH2;', 'KD01190', 'Homo sapiens (Human)', 'SMARCC1', '#SWI/SNF complex subunit SMARCC1#BRG1-associated factor 155#BAF155#SWI/SNF complex 155 kDa subunit#SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1', '-', 'ENSG00000173473', '-'),
(1191, 'Q7Z3B3', 'KAT8 regulatory NSL complex subunit 1', 'GO:0000777===SCL===k', 121025, '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:0000269|PubMed:20018852; ECO:0000269|PubMed:22547026}.', 'MAAMAPALTDAAAEAHHIRFKLAPPSSTLSPGSAENNGNANILIAANGTKRKAIAAEDPSLDFRNNPTKEDLGKLQPLVASYLCSDVTSVPSKESLKLQGVFSKQTVLKSHPLLSQSYELRAELLGRQPVLEFSLENLRTMNTSGQTALPQAPVNGLAKKLTKSSTHSDHDNSTSLNGGKRALTSSALHGGEMGGSESGDLKGGMTNCTLPHRSLDVEHTTLYSNNSTANKSSVNSMEQPALQGSSRLSPGTDSSSNLGGVKLEGKKSPLSSILFSALDSDTRITALLRRQADIESRARRLQKRLQVVQAKQVERHIQHQLGGFLEKTLSKLPNLESLRPRSQLMLTRKAEAALRKAASETTTSEGLSNFLKSNSISEELERFTASGIANLRCSEQAFDSDVTDSSSGGESDIEEEELTRADPEQRHVPLRRRSEWKWAADRAAIVSRWNWLQAHVSDLEYRIRQQTDIYKQIRANKGLIVLGEVPPPEHTTDLFLPLSSEVKTDHGTDKLIESVSQPLENHGARIIGHISESLSTKSCGALRPVNGVINTLQPVLADHIPGDSSDAEEQLHKKQRLNLVSSSSDGTCVAARTRPVLSCKKRRLVRPNSIVPLSKKVHRNSTIRPGCDVNPSCALCGSGSINTMPPEIHYEAPLLERLSQLDSCVHPVLAFPDDVPTSLHFQSMLKSQWQNKPFDKIKPPKKLSLKHRAPMPGSLPDSARKDRHKLVSSFLTTAKLSHHQTRPDRTHRQHLDDVGAVPMVERVTAPKAERLLNPPPPVHDPNHSKMRLRDHSSERSEVLKHHTDMSSSSYLAATHHPPHSPLVRQLSTSSDSPAPASSSSQVTASTSQQPVRRRRGESSFDINNIVIPMSVAATTRVEKLQYKEILTPSWREVDLQSLKGSPDEENEEIEDLSDAAFAALHAKCEEMERARWLWTTSVPPQRRGSRSYRSSDGRTTPQLGSANPSTPQPASPDVSSSHSLSEYSHGQSPRSPISPELHSAPLTPVARDTPRHLASEDTRCSTPELGLDEQSVQPWERRTFPLAHSPQAECEDQLDAQERAARCTRRTSGSKTGRETEAAPTSPPIVPLKSRHLVAAATAQRPTHR', 1105, 'Q7Z3B3; A8K5E4; Q6AW85; Q8IYH1; Q9BRH0; Q9NTE7; Q9UFT0; Q9ULF3;', 'KD01191', 'Homo sapiens (Human)', 'KANSL1', '#KAT8 regulatory NSL complex subunit 1#MLL1/MLL complex subunit KANSL1#MSL1 homolog 1#hMSL1v1#NSL complex protein NSL1#Non-specific lethal 1 homolog', '-', 'ENSG00000214401', '-'),
(1192, 'P0CR67', 'Probable kinetochore protein SPC25', 'GO:0000777', 30873, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MAPTTYAVPPRPASLHFLLESSTSKNGVPSLDLRWEPFQRHIESFLNAIDAYTQAARTEIVARATDHTAAVRDLKADKEEMERGIQLQRESEGEMLATLEAERHVVADLNASLSHLQSSLTKIKEKSSALDAELQSERKEVKAMQAEKERQTNVLNNMRERDTTELKQLEEALGWRVEGIKQDQLLMRFTLIDPEDPAREFSIIVDVSKQVYSVPNCDPPIPSLPDLVRQLNFDRDLFAFIKRVRIAFRALIPNPPNPSTKFDDLTGPSRSR', 272, 'P0CR67; Q55S37; Q5KGI8;', 'KD01192', 'Cryptococcus neoformans var. neoformans serotype D (strain B-3501A(Filobasidiella neoformans)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '4936355'),
(1193, 'P32479', 'Protein HIR1', 'k', 93858, 'Component of the HIR complex; which cooperates with ASF1 to promote replication-independent chromatin assembly. The HIR complex is also required for the periodic repression of three of the four histone gene loci during cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. DNA- binding by the HIR complex may repress transcription by inhibiting nucleosome remodeling by the SWI/SNF complex. The HIR complex may also be required for transcriptional silencing of centromeric; telomeric and mating-type loci in the absence of CAF-1. {ECO:0000269|PubMed:10445029; ECO:0000269|PubMed:11404324; ECO:0000269|PubMed:11412995; ECO:0000269|PubMed:11756556; ECO:0000269|PubMed:11782447; ECO:0000269|PubMed:11937489; ECO:0000269|PubMed:12524332; ECO:0000269|PubMed:12975325; ECO:0000269|PubMed:15057281; ECO:0000269|PubMed:16020781; ECO:0000269|PubMed:16039596; ECO:0000269|PubMed:16264190; ECO:0000269|PubMed:16303565; ECO:0000269|PubMed:16449659; ECO:0000269|PubMed:8417331; ECO:0000269|PubMed:9001207; ECO:0000269|PubMed:9504914; ECO:0000269|PubMed:9671488; ECO:0000269|PubMed:9671489}.', 'MKVVKFPWLAHREESRKYEIYTVDVSHDGKRLATGGLDGKIRIWSIDSILRCMELESLTPEIPLPQDLQMPLCSMSRHTGSITCVKFSPDGKYLASGSDDRILLIWALDEEQSSQPAFGSEHEREHWTVRKRLVAHDNDIQDICWAPDSSILVTVGLDRSVIVWNGSTFEKLKRFDVHQSLVKGVVFDPANKYFATTSDDRTMKIFRYHKTGDISFTIEHIITEPFKESPLTTYFRRPSWSPDGQHIAVPNATNGPVSSVAIVNRGTWDTNVSLIGHDAPTEVARFNPRLFERNAGVKQKKDDDPENALVGQNDDKVHHFDKNIDSVVATAGQDKSLAVWSTSRPRPILVAFDIANKSITDMSWNPDGSLLFVASLDSSITLFKFENNELGKPIPLEKNMEQLYRYGVDKDSLDFPESINQLLLEDQTKSFKHTKISTSKLGENHPTLATNSASNQKDNNDASVSRSEHINILIPKRKKDAILNKAVTLKSGKKRVAPTLISTSSSSPFSNGIKKPTLDSKRIENNVKSSTKTINSKNTLLNVPEGVEKKISISSFPLPRLGIHSLIMGTKERSAWKISNSELENDDADNAGGKGSDGTSNSIDDIAVLSEEENDFHRMTLNAKLTQEKIWSEEPTTRCLLQSDVIPDTDVVVLEGGSLDDIAVLEIRNGVERSIQFDSEALLDNPTRILGYQGGKRTIETFIPEVIICAIGSKDCKCWCLASANGSIYILSYNGQQRIPKICLGHKVIKMVTSSKYLLVLTERGLFFAWDLLDLKLVLRNVPILPILNGQPIHGNKVRINKVIKCFRLDGSSCDLLLEVGDPKNVYKWTKDLGCWSLYK', 840, 'P32479; D6VPZ2;', 'KD01193', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'HIR1', '#Protein HIR1#Histone transcription regulator 1', '-', '-', '852275'),
(1194, 'P0CR66', 'Probable kinetochore protein SPC25', 'GO:0000778===GO:0051455===GO:0031617', 30873, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MAPTTYAVPPRPASLHFLLESSTSKNGVPSLDLRWEPFQRHIESFLNAIDAYTQAARTEIVARATDHTAAVRDLKADKEEMERGIQLQRESEGEMLATLEAERHVVADLNASLSHLQSSLTKIKEKSSALDAELQSERKEVKAMQAEKERQTNVLNNMRERDTTELKQLEEALGWRVEGIKQDQLLMRFTLIDPEDPAREFSIIVDVSKQVYSVPNCDPPIPSLPDLVRQLNFDRDLFAFIKRVRIAFRALIPNPPNPSTKFDDLTGPSRSR', 272, 'P0CR66; Q55S37; Q5KGI8;', 'KD01194', 'Cryptococcus neoformans var. neoformans serotype D (strain JEC21ATCC MYA-565) (Filobasidiella neoformans)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '3257932'),
(1195, 'Q6DFL2', 'Biorientation of chromosomes in cell division protein 1', 'GO:0000777', 18343, 'Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000250}.', 'MAESGSGTSGGSSSVGGVSNPASLAPGDSQLIALIVEQLKSRGQFDGFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNADMNKNQLRNGLRQSVIQSGMLEAGVDRIISQVVDPKLNHIFRPQIEKAIHEYLTAQTKEDSAPPLPPGPPEPQEQEPPEPSQSVS', 169, 'Q6DFL2;', 'KD01195', 'Xenopus laevis (African clawed frog)', 'bod1', '#Biorientation of chromosomes in cell division protein 1#Biorientation defective protein 1#Protein FAM44B', '-', '-', '446336'),
(1196, 'P67775', 'Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform', 'k;m', 35594, 'PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2; mitogen-stimulated S6 kinase; and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at ''Ser-259''. {ECO:0000250; ECO:0000269|PubMed:10801873; ECO:0000269|PubMed:22613722; ECO:0000269|PubMed:9920888}.', 'MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL', 309, 'P67775; P05323; P13197;', 'KD01196', 'Homo sapiens (Human)', 'PPP2CA', '#Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform#PP2A-alpha#3.1.3.16#Replication protein C#RP-C', 'BIOMD0000000543,Qi2013 - IL-6 and IFN crosstalk model (non-competitive);BIOMD0000000544,Qi2013 - IL-6 and IFN crosstalk model;', 'ENSG00000113575', '-'),
(1197, 'O48626', 'Centromere/kinetochore protein zw10 homolog', 'GO:0000777', 83934, 'May be required for accurate chromosome segregation. Required for proper maturation of seed storage proteins. Forms a complex with MAG2; MIP2 and MIP3 on the endoplasmic reticulum that may be responsible for efficient transport of seed storage proteins. {ECO:0000269|PubMed:24118572; ECO:0000305}.', 'MPEIDALFESINVRDLLAGHDLNDPTTPLSAPDLRLLINRLESHSLRIKSKVQSYLVAHHSDFSELFSLCQDTVSRTRLISDDVSDVLQLVSDRPIDVEIRSVVDEITEKTKEVKLKRESLDLVNAIVGICEALQETKEALKNGRFRFAAERIRELKVVLRIGEEEDGEPVAYALLRKEWSNCFDEIQEVLAKFMENAVRFELDSSRIRIKYQLSVGETAGIALSTVLEAMEVIGILDYGLAKAADSIFKHVITPAVTHASTFAAVEDLCKSAGEVTEATLRLEQSSDHKFEDVDGDAMYSGILKVVKFICSSLCFGNVTWIHSFGRLTWPRISELIISKFLSKVVPEDASKLADFQKIIERTSQFEAALKELNFVSSSDAESRLSKYAEDVEVHFASRKKIEILAKARNLLLQCNFTIPQDIAMRNAKHIVCLLFSSERCVVSEAASQLMNLVHKTLEDVCVSSARVASEFYNAARDSILLYEAVVPVKLEKQLDGLNEAAVLLHNDCLYLFEEILGLAFEYRASFPSSIKEYAVFADIAPRFKLMAEEVLQKQVHLVISSLREAIDSADGFQNTHQIKQFKSAEFSIDQVVFSLKNVHMIWEPVLRPKTYKQSMCAVLESVFRRIARDILLLDDMAADETFELQKLIYLMLKNLSSVLDSVRSADETSRPLDDIIPSLRKTRKLAELLDMPLMSITSAWESGELFRCNFTRTEVQDFIKAIFTDSPLRKECLWRIDEVNQ', 742, 'O48626; O48775; Q8GY19;', 'KD01197', 'Arabidopsis thaliana (Mouse-ear cress)', 'ZW10', '#Centromere/kinetochore protein zw10 homolog#AtZW10#MAG2-interacting protein 1 {ECO:0000303|PubMed:24118572}', '-', '-', '817851'),
(1198, 'Q9UTI4', 'Monopolar attachment protein 1', 'GO:0000941===GO:0051455===SCL===k', 19612, 'Plays an important role in chromosome segregation during meiosis I by allowing meiotic rec8 to establish cohesion at the centromeric central core and thereby promote the side-by-side structure of kinetochores at meiosis I. Enables monopolar attachment during meiosis I (PubMed:16303567; PubMed:16325576). Required to facilitate kinetochore mono-orientation during meiosis I; when kinetochores on sister chromosomes face the same direction and are thus captured and pulled by spindle fibers from the same pole (PubMed:25533956). Acts in collaboration with plo1 (PubMed:25533956). {ECO:0000269|PubMed:16303567; ECO:0000269|PubMed:16325576; ECO:0000269|PubMed:25533956}.', 'MAINNENELEYKLIKKNKNPKISNSKKKNSTRPALQDKTNQTLPIHQNQAFSNILPSDFSIIKTPETKTADDFPVNGYEGLNILKFDLELFYKLKPVATSTPKSCMRTGSNLFLNETVKHVPDERLVSNIKNTQTKDSITRDSAYYHRKTMTESIIKTLAAFDAEVDEIILF', 172, 'Q9UTI4;', 'KD01198', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'moa1', '#Monopolar attachment protein 1#Meiotically up-regulated gene 159 protein', '-', '-', '2542808'),
(1199, 'Q7YRC6', 'Aurora kinase B', 'GO:0034501===GO:0032133', 39442, '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 (By similarity). {ECO:0000250}.', 'MAQKENAYPWPYGRQTAQPGLNTLPQRVLRKEPVTPSALVLMSRSNAQPTAAPGQKVVENSSGTPNIPKRSFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLQHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSRTFDEQRTATIMEELADALTYCHAKKVIHRDIKPENLLLGLRGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRTHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPPSVPLGAQDFIYKLLKHNPSERLPLAQVSAHPWVRTHSRRVLPPSAPQSVP', 344, 'Q7YRC6;', 'KD01199', 'Bos taurus (Bovine)', 'AURKB', '#Aurora kinase B#2.7.11.1#Aurora 1#Aurora- and IPL1-like midbody-associated protein 1#AIM-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', '-', '-', '-'),
(1200, 'Q9CYC5', 'Kinetochore-associated protein DSN1 homolog', 'GO:0000444', 39553, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. {ECO:0000250|UniProtKB:Q9H410}.', 'MTSVTRSEDQEPTMSETQDRPLQPSLKPLEALPQSSAYQEMMTQGVSEEKNHLGSNPGEGESCGADHQEGSQLRSFHLSPQEQSIRPQDRRQSWRRASMKEVNRRKSLAPFHPGITELCRSISVKLAQSQRLGALLLSSFQFSVEKLEPFLKNTKDFSLECFRAKASSLSEELKHFTDRLGNDGTLQKCFVEDSKEKAADFSLEASVAEVKEYITKFSLERQAWDRLLLQYQNEVPPEEMPRGSTETRITEVKVDPAAYLRSSQKEVLSTKPDYQRIVQDQNQVFAYVELVMDELQGSVKQLQALMDESTQYLQKVSVQLKKRSMDQLDSSPARKLLKLPLQSSPSTQ', 348, 'Q9CYC5; Q9CYF2; Q9DA26;', 'KD01200', 'Mus musculus (Mouse)', 'Dsn1', '#Kinetochore-associated protein DSN1 homolog', '-', '-', '66934'),
(1201, 'P55854', 'Small ubiquitin-related modifier 3', 'GO:0000776===k', 11637, 'Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport; DNA replication and repair; mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I; and can be promoted by an E3 ligase such as PIAS1-4; RANBP2 or CBX4 (PubMed:11451954; PubMed:18538659; PubMed:21965678). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269|PubMed:11451954; ECO:0000269|PubMed:18538659; ECO:0000269|PubMed:21965678}.', 'MSEEKPKEGVKTENDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVPESSLAGHSF', 103, 'P55854; B2R5X4; B4DUW4; Q53HI9; Q6FGD4; Q9BWR4;', 'KD01201', 'Homo sapiens (Human)', 'SUMO3', '#Small ubiquitin-related modifier 3 {ECO:0000305}#SUMO-3 {ECO:0000305}#SMT3 homolog 1 {ECO:0000312|HGNC:HGNC:11124}#SUMO-2 {ECO:0000303|PubMed:10692421}#Ubiquitin-like protein SMT3A {ECO:0000303|PubMed:9119407}#Smt3A {ECO:0000303|PubMed:9119407}', '-', 'ENSG00000184900', '-'),
(1202, 'Q9ULI4', 'Kinesin-like protein KIF26A', 'GO:0003777', 194590, 'Atypical kinesin that plays a key role in enteric neuron development. Acts by repressing a cell growth signaling pathway in the enteric nervous system development; possibly via its interaction with GRB2 that prevents GRB2-binding to SHC; thereby attenating the GDNF-Ret signaling. Binds to microtubules but lacks microtubule-based motility due to the absence of ATPase activity (By similarity). {ECO:0000250}.', 'MVGRGVPLCAAQPAVAEGGPAREPPPLLEVSPRKRLPAGPDQDPCGSRPAPEGAGAGPEQGHSAGGGGWCRHCHTKLVELKRQAWKLVSGPGTTLRDPCLSALLLDKLPAPGALPACRPEAERRCDVCATHLQQLTREAMHLLQAPASHEDLDAPHGGPSLAPPSTTTSSRDTPGPAGPAGRQPGRAGPDRTKGLAWSPGPSVQVSVAPAGLGGALSTVTIQAQQCLEGMWSVSRVNSFLPPACLAEAAVAAVAVADTVRECPPVAGPDGLSKAWGRGGVCTSALVTPTPGSVGGSTGPSAAASFFIRAMQKLSLASKRKKPHPPPPPATRGTSTYPTDFSGVLQLWPPPAPPCLLRAASKTKDNPGSIGKVKVMLRIWPAQGAQRSAEAMSFLKVDPRKKQVILYDPAAGPPGSAGPRRAATAAVPKMFAFDAVFPQDSEQAEVCSGTVADVLQSVVSGADGCIFSFGHMSLGKSYTMIGKDSSPQSLGIVPCAISWLFRLIEERRERTGTRFSVRVSAVEVCGRDQSLRDLLAEVAPGSLQDTQSPGVYLREDPVCGAQLQNQSELRAPTAEKAAFYLDAALAARSTSRAGCGEDARRSSHMLFTLHVYQYRMEKCGRGGMSGGRSRLHLIDLGSCEAAAGRAGEAAGGPLCLSLSALGSVILALVNGAKHVPYRDHRLTMLLRESLATAGCRTTMIAHVSDAPAQHAETLSTVQLAARIHRLRRKKAKYASSSSGGESSCEEGRARRPPHLRPFHPRTVALDPDRTPPCLPGDPDYSSSSEQSCDTVIYVGPGGAALSDRELTDNEGPPDFVPIIPALSRHRPSKGPRDADHFRCSTFAELQERLECMDGNEGPSGGPGGTDGAQASPARGGRKPSPPEAASPRKAVGTPMAASTPRGSSGPDTHQGTPEPCKAIVWGDQREDSSAWPELLVPEKAAVSGGRRPLPSPAPPPPQLLEACRAPEEPGGGGTDGVARTPPVGMSGQVAGSPMLPGATCPRLAAGSRCPERGLLTTTVTLQRPVELNGEDELVFTVVEELSLGALAGAGRPTSLASFDSDCSLRALASGSRPVSIISSINDEFDAYTSQAPEGGPLEGAAWAGSSHGSSISSWLSEVSVCTADSRDPTPQPRFSPDSLAGLDPGGPPALDGSLGDGSSGFLGPDRPDSPGPTWGPCPGEVAAVAPSRPGREPQAGPSRWASAAQTIHSSLPRKPRTASATTRVGCARLGQSPPGRGGLFEDPWLLRVGECDTQAASAGRAPSPTLGSPRLPEAQVMLACAQRVVDGCEVAARAARRPEAVARIPPLRRGATTLGVTTPAVSWGDAPTEVVACSGSLKASPTSKKGLAPKAGFLPRPSGAAPPAPPTRKSSLEQRSSPASAPPHAVNPARVGAAAVLRGEEEPRPSSRADHSVPRATSSLKARASKVEAAHRLAGHASLERYEGLAHSSSKGREAPGRPPRAVPKLGVPPSSPTHGPAPACRSGAAKAVGAPKPPVGGGKGRGLVAGGSRALGPSVKLSTASVTGRSPGGPVAGPRAAPRAGPSVGAKAGRGTVMGTKQALRAAHSRVHELSASGAPGRGGSSWGSADSDSGHDSGVNVGEERPPTGPALPSPYSKVTAPRRPQRYSSGHGSDNSSVLSGELPPAMGRTALFHHSGGSSGYESLRRDSEATGSASSAPDSMSESGAASPGARTRSLKSPKKRATGLQRRRLIPAPLPDTTALGRKPSLPGQWVDLPPPLAGSLKEPFEIKVYEIDDVERLQRPRPTPREAPTQGLACVSTRLRLAERRQQRLREVQAKHKHLCEELAETQGRLMLEPGRWLEQFEVDPELEPESAEYLAALERATAALEQCVNLCKAHVMMVTCFDISVAASAAIPGPQEVDV', 1882, 'Q9ULI4; Q8TAZ7; Q96GK3; Q9UFL3;', 'KD01202', 'Homo sapiens (Human)', 'KIF26A', '#Kinesin-like protein KIF26A', '-', 'ENSG00000066735', '-'),
(1203, 'P87297', 'DASH complex subunit dad1', 'GO:0000776===GO:0042729===GO:0031134===GO:0000779', 10523, '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. Mediates interaction between the DASH and sim4 complexes leading to loading of DASH onto the kinetochore. {ECO:0000269|PubMed:16079914}.', 'MSSENMDITENIQNEQNKDFDDIDFERRRRLLTLQISKSMNEVVNLMSALNKNLESINGVGKEFENVASLWKEFQNSVLQKKDREMLDAP', 90, 'P87297;', 'KD01203', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dad1', '#DASH complex subunit dad1#Outer kinetochore protein dad1', '-', '-', '2542311'),
(1204, 'P50528', 'Serine/threonine-protein kinase plo1', 'SCL===c;k;m', 77302, 'Required to form a bipolar spindle; the actin ring and septum. Functions upstream of the whole septum formation pathway; including actin ring formation (regulated by late septation genes) and septal material deposition (regulated by early septation genes). Behaves as a "septum-promoting factor"; and could also be involved in inducing other late events of cell division (PubMed:12615979; PubMed:12815070; PubMed:7744248). Together with moa1; 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:12615979; ECO:0000269|PubMed:12815070; ECO:0000269|PubMed:25533956; ECO:0000269|PubMed:7744248}.', 'MASVAIKEPKTAITPKKKSKASRLCFTPPTNLHNNKKNIFYTRYDCIGEGGFARCFRVKDNYGNIYAAKVIAKRSLQNDKTKLKLFGEIKVHQSMSHPNIVGFIDCFEDSTNIYLILELCEHKSLMELLRKRKQLTEPEVRYLMMQILGALKYMHKKRVIHRDLKLGNIMLDESNNVKIGDFGLAALLMDDEERKMTICGTPNYIAPEILFNSKEGHSFEVDLWSAGVVMYALLIGKPPFQDKEVKTIYRKIKANSYSFPSNVDISAEAKDLISSLLTHDPSIRPSIDDIVDHEFFHTGYMASTLPDEILHSMPIWPSSQSKSSFQRNLDFVASASGVGFGNSAGVEKNKPYALRTDEVDNDRILPSVLSPRDRVNPVMKIGPETKPVPSKLSTALHAARKSTDGSLGSRVKVLREESQSFVPTKSAVTEQVEPIQLIRSLSANTVSRLSKVGNMKSDIWISVKKTALKIGMALEAHTHALTSEDADSEPVLFITKWVDYSNKYGLGYQLSDESVGVHFNDDTSLLFSADEEVVEYALHPKDTEIKPYIYPASKVPESIRSKLQLLKHFKSYMGQNLSKAVQDESFEKPKNSTSNTMLFMQHYLRTRQAIMFRLSNGIFQFNFLDHRKVVISSTARKIIVLDKERERVELPLQEASAFSEDLRSRLKYIRETLESWASKMEVS', 683, 'P50528;', 'KD01204', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'plo1', '#Serine/threonine-protein kinase plo1#2.7.11.21', '-', '-', '2541957'),
(1205, 'Q8CBY8', 'Dynactin subunit 4', 'GO:0005868', 53057, 'Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton.', 'MASLLQSERVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSQHTIHVVDKYSLGTRLQRPRAGASISTLAGLSLREGEDQKEVKIEPAQAVAEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDLQPVSASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLLECDEGDPDNINSTAKVVVPPKELILAGKDAAAEYDELAEPQDFQDDPDIVAFRKANKVGIFIKVTPQREEGEVTVCFKMKHDFKNLAAPIRPVEEGDQGTEVIWLTQHVELSFGPLLP', 467, 'Q8CBY8; Q923A0; Q9D4X0;', 'KD01205', 'Mus musculus (Mouse)', 'Dctn4', '#Dynactin subunit 4#Dynactin subunit p62', '-', '-', '67665'),
(1206, 'P50524', '26S proteasome regulatory subunit rpn12', 'GO:0061638', 30899, 'Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.', 'MSTLDLNHLADLYDRKDWNACKKELLKLKVELAKQNLFVPTSDKEKASFARNVFEYGVLVSIQTCDIESFARYASQVIPFYHDSLVPSSRMGLVTGLNLLYLLSENRIAEFHTALESVPDKSLFERDPYVEWVISLEQNVMEGAFDKVASMIRSCNFPEFSYFMKIVMSMVRNEIATCAEKVYSEIPLSNATSLLYLENTKETEKLAEERGWDIRDGVIYFPKEANALETEDGMLIDEEDELELPPTASKHTISSIRQLLSYTSELEQIV', 270, 'P50524; Q9UUC3;', 'KD01206', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rpn12', '#26S proteasome regulatory subunit rpn12', '-', '-', '2540025'),
(1207, 'G5EDN2', 'Putative alpha 2 mannosyltransferaseT27F7.4', 'k', 57191, '', 'MRTTLRLLAKLVVFRCISVYLVASWFVPDEVYQSAEVAHHLVYGTGHLSWEWRHSLRSFFHPALIAVIIKFLDILSLSSQPLIYHIPRLAHALLFALADFSFYKICLRLCKTKGIAENSFVTYLSSWFVFYCAPRTLSNSLETSLTLIALNWFPFETKNFKGPTWPYIALGVLTIIIRPTVALIWLVFGVYHLYHSPTPVRLIFQLVLPVTLPILIVTTLIDSWAYGTPTIPLWNFLQFNVVQGGSALFGVHPWYWYIVSGIPAVLTVQMIPIIVGLLGPNIFRPSLLPFFATITYIIVHSLLPHKEQRFLLPIIPLLCIYAGGAFQNLKKWRGSAMAVMIAINIGIALFTSRYHQVGPFTAPRRIMEEWRGHHGKLSVAALMPCYSIPGHAFWHDHLDNLRLLDCSPDLEQLRGPTELDESDQFHGNATKWLIETFSLEHHKYQRVLMYEKYYETSRRWFESNGWYQCIEKIWHSIALTSSREDNYMIVLCRNGY', 496, 'G5EDN2;', 'KD01207', 'Caenorhabditis elegans', 'PIG-B', '#Putative alpha 2 mannosyltransferase {ECO:0000313|EMBL:CAD24083.1}#T27F7.4 {ECO:0000313|EMBL:CCD72091.1}', '-', '-', '13184808'),
(1208, 'Q4R1J6', 'Baculoviral IAP repeat-containing protein 5.1-B', 'GO:0000777===GO:0032133', 18803, '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). CPC. Does not appear to exhibit anti-apoptotic activity. {ECO:0000250; ECO:0000269|PubMed:15853809}.', 'MYSAKNRFVQSVQRLQDFRNMYDYEARLATFADWPFTENCKCTPENMAKAGFVHCPTENEPDVACCFFCLKELEGWEPDDDPWNEHSKRSVNCGFLSLTKCVNDLTMEGFLRLEGDRIKSFYRKFSTVVLQYVEEEMTAATKRLLEYFSNQHQCSIDLDH', 160, 'Q4R1J6; Q5HZ94; Q8AXI6;', 'KD01208', 'Xenopus laevis (African clawed frog)', 'birc5.1-b', '#Baculoviral IAP repeat-containing protein 5.1-B#Survivin1-B {ECO:0000303|PubMed:15853809}#Survivin {ECO:0000312|EMBL:AAN76690.1}#XSurvivin1B {ECO:0000312|EMBL:BAE02678.1}#xL_Survivin2 {ECO:0000303|PubMed:16759290}#Su2 {ECO:0000303|PubMed:16759290}', '-', '-', '398418'),
(1209, 'B0Y3B5', 'E3 ubiquitin ligase complex SCF subunit sconC', 'GO:0051382===GO:0031518', 18141, 'Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes; which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression; probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}.', 'MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE', 158, 'B0Y3B5;', 'KD01209', 'Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163(Aspergillus fumigatus)', 'sconC', '#E3 ubiquitin ligase complex SCF subunit sconC#Sulfur controller C#Sulfur metabolite repression control protein C', '-', '-', '-'),
(1210, 'Q9N2L7', 'Serine/threonine-protein kinase plk-2', 'k', 72071, 'May be required for cell division and may have a role during G1 or S phase. {ECO:0000250|UniProtKB:P53350}.', 'MQRVQPSAARVKSQKKEKAPPDVPDVILDGERKTRYEKGKFLGKGGFAHCYELRNKSTGELFAGKVVPKALLIKQYQRDKMAQEVQIHRNLQHRNVVKLYHFFEDKSNVYITLELCPRRSLMELHKRRKAVTEPEARYFTYQIVEGVLYLHNLKIVHRDLKLGNLFLNDELQVKIGDFGLATTCDNDERKKTLCGTPNYIAPEVLNKIGHSFEVDLWAIGCILYILLFGHPPFESKSLEETYSRIKNNNYVIPTSASAAASQLIRVLLDPVPSRRPNARAVCRDHFFKSGFMPARLPVSCLTMVPHLNDDEYAEENVSPSGTIDQRGPHQAGRSGLSAIPAHLVSRNSERQQTHRMEAYRQPTDCYLSNLLAQVNDLLATPTADIDDAEAALDSYQSPEALPVFWISKWVDYSDKYGIGYQLCDNSVGVLFNDNSRIMLDTAGTQLTYIEKTEKEHYFDMESAIPSGLQKKMTLLKYFRSYMNDHLLQAGQQVTRKVGDDLARLPTLRVWFRTKSAIVLHLSNGTVQINFFNDHIKMVLCPLMQAVTFIDENKRMFTYKFSHLAENGCPEKFLHRIQYAKCMIQRLVEEHTKEETKHNAPAANAVRLPSTSSNVRLESAADIQPAYPSSSRR', 632, 'Q9N2L7;', 'KD01210', 'Caenorhabditis elegans', 'plk-2', '#Serine/threonine-protein kinase plk-2#2.7.11.21#Polo-like kinase 2', '-', '-', '171838'),
(1211, 'Q8GS71', 'Kinesin-like protein FRA1', 'GO:0003777', 116734, 'Microtubule-dependent motor protein involved in the control of the oriented deposition of cellulose microfibrils (PubMed:12468730). Its motor activity is directed toward the microtubule''s plus end. It possesses at least twice the processivity of conventional kinesin and has the potential to drive long-distance transport of cargo along cortical microtubules (PubMed:21914648). {ECO:0000269|PubMed:12468730; ECO:0000269|PubMed:21914648}.', 'MESTPPPDDCSVKVAVHIRPLIGDERIQGCQDCVTVVTGKPQVQIGSHSFTFDHVYGSSGSPSTEMYEECAAPLVDGLFQGYNATVLAYGQTGSGKTYTMGTGCGDSSQTGIIPQVMNALFTKIETLKQQIEFQIHVSFIEIHKEEVQDLLDPCTVNKSDTNNTGHVGKVAHVPGKPPIQIRETSNGVITLAGSTEVSVSTLKEMAACLDQGSVSRATGSTNMNNQSSRSHAIFTITVEQMRKINTDSPENGAYNGSLKEEYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINKGLLALGNVISALGDEKKRKDGAHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIRNKPVVNRDPVSSEMLKMRQQVEYLQAELSLRTGGSSCAEVQALKERIVWLETANEELCRELHEYRSRCPGVEHSEKDFKDIRADDIVGSVRPDGLKRSLHSIESSNYPMVEATTGDSREIDEEAKEWEHKLLQNSMDKELYELNRRLEEKESEMKLFDGYDPAALKQHFGKKIAEVEDEKRSVQEERNRLLAEIENLASDGQAQKLQDVHAQNLKALEAQILDLKKKQESQVQLLKQKQKSDDAARRLQDEIQSIKAQKVQLQHRMKQEAEQFRQWKASREKELLQLRKEGRKSEYERHKLQALNQRQKMVLQRKTEEAAMATKRLKELLEARKSSPREHSAGTNGFGTNGQTNEKSLQRWLDHELEVMVNVHEVRHEYEKQSHVRAALAEELAVLRQVDEFAVKGLSPPRGKNGFARASSLSPNARMARISSLENMLVISSNSLVAMASQLSEAEERERAFTNRGRWNQLRSMGEAKNLLQYMFNSLAETRCQLWEKDVEIKEMKDQFKEIVGLLRQSELRRKEAEKELKLREQAIATSLGTPPSSVKHVAEDLSTPSPMTVPAQKQLKFTPGIANGKVRGPAAFLDTNKKMVPMGQVSMRKLSAVGKQGGRLWRWKRSHHQWIVQFKWKWQKPWRLSEWIRTSDETLLKSKPRLKALPNKIM', 1035, 'Q8GS71; Q9FIJ9;', 'KD01211', 'Arabidopsis thaliana (Mouse-ear cress)', 'FRA1', '#Kinesin-like protein FRA1 {ECO:0000305}#Protein FRAGILE FIBER 1 {ECO:0000303|PubMed:12468730}', '-', '-', '834833'),
(1212, 'Q8TAQ2', 'SWI/SNF complex subunit SMARCC2', 'k', 132879, 'Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. 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). {ECO:0000250}.', 'MAVRKKDGGPNVKYYEAADTVTQFDNVRLWLGKNYKKYIQAEPPTNKSLSSLVVQLLQFQEEVFGKHVSNAPLTKLPIKCFLDFKAGGSLCHILAAAYKFKSDQGWRRYDFQNPSRMDRNVEMFMTIEKSLVQNNCLSRPNIFLCPEIEPKLLGKLKDIIKRHQGTVTEDKNNASHVVYPVPGNLEEEEWVRPVMKRDKQVLLHWGYYPDSYDTWIPASEIEASVEDAPTPEKPRKVHAKWILDTDTFNEWMNEEDYEVNDDKNPVSRRKKISAKTLTDEVNSPDSDRRDKKGGNYKKRKRSPSPSPTPEAKKKNAKKGPSTPYTKSKRGHREEEQEDLTKDMDEPSPVPNVEEVTLPKTVNTKKDSESAPVKGGTMTDLDEQEDESMETTGKDEDENSTGNKGEQTKNPDLHEDNVTEQTHHIIIPSYAAWFDYNSVHAIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQVDAESRPTPMGPPPTSHFHVLADTPSGLVPLQPKTPQQTSASQQMLNFPDKGKEKPTDMQNFGLRTDMYTKKNVPSKSKAAASATREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLEDSEASLGPLAYQPIPFSQSGNPVMSTVAFLASVVDPRVASAAAKSALEEFSKMKEEVPTALVEAHVRKVEEAAKVTGKADPAFGLESSGIAGTTSDEPERIEESGNDEARVEGQATDEKKEPKEPREGGGAIEEEAKEKTSEAPKKDEEKGKEGDSEKESEKSDGDPIVDPEKEKEPKEGQEEVLKEVVESEGERKTKVERDIGEGNLSTAAAAALAAAAVKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREREALEYQRQQLLADRQAFHMEQLKYAEMRARQQHFQQMHQQQQQPPPALPPGSQPIPPTGAAGPPAVHGLAVAPASVVPAPAGSGAPPGSLGPSEQIGQAGSTAGPQQQQPAGAPQPGAVPPGVPPPGPHGPSPFPNQQTPPSMMPGAVPGSGHPGVAGNAPLGLPFGMPPPPPPPAPSIIPFGSLADSISINLPAPPNLHGHHHHLPFAPGTLPPPNLPVSMANPLHPNLPATTTMPSSLPLGPGLGSAAAQSPAIVAAVQGNLLPSASPLPDPGTPLPPDPTAPSPGTVTPVPPPQ', 1214, 'Q8TAQ2; F8VTJ5; Q59GV3; Q92923; Q96E12; Q96GY4;', 'KD01212', 'Homo sapiens (Human)', 'SMARCC2', '#SWI/SNF complex subunit SMARCC2#BRG1-associated factor 170#BAF170#SWI/SNF complex 170 kDa subunit#SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 2', '-', 'ENSG00000139613', '-'),
(1213, 'Q7RXR3', 'Histone H3-like centromeric protein hH3v', 'GO:0034501===GO:0000941', 17337, '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}.', 'MPPKKGGVTKSKAVSKKAAAVPTPKATPPGRRKSRASSVQPGDPVPQGKKRRYRPGTLALKEIRNYQRTTDLLVAKLPFARLVREIAMQFRPMDEEMRWQSQAILALQEAAEAFLVHLFEDTNLCAIHAKRVTIMQKDIQLARRIRGVWGGAGWV', 155, 'Q7RXR3;', 'KD01213', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'hH3v', '#Histone H3-like centromeric protein hH3v#CENP-A homolog', '-', '-', '3872805'),
(1214, 'Q9UTG8', 'DASH complex subunit dad2', 'GO:0000778===GO:0042729===GO:0031134===GO:0000779===SCL===k', 10319, '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:11193425; ECO:0000269|PubMed:16079914}.', 'MLQARIEEKQKEYELICKLRDSSNDMVQQIETLAAKLETLTDGSEAVATVLNNWPSIFESIQIASQHSGALVRIPPSTSNTNASATEQGDVEEV', 94, 'Q9UTG8;', 'KD01214', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dad2', '#DASH complex subunit dad2#High osmolarity sensitivity protein 2#Outer kinetochore protein dad2', '-', '-', '2542418'),
(1215, 'Q9H1H9', 'Kinesin-like protein KIF13A', 'GO:0003777', 202308, 'Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane; endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR- containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation; required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abcission step in cytokinesis: mediates translocation of ZFYVE26; and possibly TTC19; to the midbody during cytokinesis. {ECO:0000269|PubMed:19841138; ECO:0000269|PubMed:20208530}.', 'MSDTKVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTKQGERKPPKVFAFDYCFWSMDESNTTKYAGQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFKRISLEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGKGKSKFVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNEDPNAKVIRELREEVEKLREQLSQAEAMKAPELKEKLEESEKLIKELTVTWEEKLRKTEEIAQERQRQLESMGISLEMSGIKVGDDKCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPQHCEIDIASDGDVTLTPKENARSCVNGTLVCSTTQLWHGDRILWGNNHFFRINLPKRKRRDWLKDFEKETGPPEHDLDAASEASSEPDYNYEFAQMEVIMKTLNSNDPVQNVVQVLEKQYLEEKRSALEEQRLMYERELEQLRQQLSPDRQPQSSGPDRLAYSSQTAQQKVTQWAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLTDYQVTLQIPAANLSANRKRGAIVSEPAIQVRRKGKSTQVWTIEKLENKLIDMRDLYQEWKEKVPEAKRLYGKRGDPFYEAQENHNLIGVANVFLECLFCDVKLQYAVPIISQQGEVAGRLHVEVMRVTGAVPERVVEDDSSENSSESGSLEVVDSSGEIIHRVKKLTCRVKIKEATGLPLNLSNFVFCQYTFWDQCESTVAAPVVDPEVPSPQSKDAQYTVTFSHCKDYVVNVTEEFLEFISDGALAIEVWGHRCAGNGSSIWEVDSLHAKTRTLHDRWNEVTRRIEMWISILELNELGEYAAVELHQAKDVNTGGIFQLRQGHSRRVQVTVKPVQHSGTLPLMVEAILSVSIGCVTARSTKLQRGLDSYQRDDEDGDDMDSYQEEDLNCVRERWSDALIKRREYLDEQIKKVSNKTEKTEDDVEREAQLVEQWVGLTEERNAVLVPAPGSGIPGAPADWIPPPGMETHIPVLFLDLNADDLSANEQLVGPHASGVNSILPKEHGSQFFYLPIIKHSDDEVSATASWDSSVHDSVHLNRVTPQNERIYLIVKTTVQLSHPAAMELVLRKRIAANIYNKQSFTQSLKRRISLKNIFYSCGVTYEIVSNIPKATEEIEDRETLALLAARSENEGTSDGETYIEKYTRGVLQVENILSLERLRQAVTVKEALSTKARHIRRSLSTPNVHNVSSSRPDLSGFDEDDKGWPENQLDMSDYSSSYQDVACYGTLPRDSPRRNKEGCTSETPHALTVSPFKAFSPQPPKFFKPLMPVKEEHKKRIALEARPLLSQESMPPPQAHNPGCIVPSGSNGSSMPVEHNSKREKKIDSEEEENELEAINRKLISSQPYVPVEFADFSVYNASLENREWFSSKVDLSNSRVLEKEVSRSPTTSSITSGYFSHSASNATLSDMVVPSSDSSDQLAIQTKDADSTEHSTPSLVHDFRPSSNKELTEVEKGLVKDKIIVVPLKENSALAKGSPSSQSIPEKNSKSLCRTGSCSELDACPSKISQPARGFCPREVTVEHTTNILEDHSFTEFMGVSEGKDFDGLTDSSAGELSSRRSLPNKTGGKTVSDGLHHPSQLHSKLENDQVIIPEAAFWVLCCQ', 1805, 'Q9H1H9; A0JP21; A0JP22; F2Z382; Q5THQ2; Q5THQ3; Q9H193; Q9H194;Q9H1H8;', 'KD01215', 'Homo sapiens (Human)', 'KIF13A', '#Kinesin-like protein KIF13A#Kinesin-like protein RBKIN', '-', 'ENSG00000137177', '-'),
(1216, 'Q940B8', 'Kinesin-13A', 'GO:0003777', 89082, 'Internal motor kinesin involved in trichome morphogenesis. Participates in regulating the formation of Golgi- associated vesicles. {ECO:0000269|PubMed:15574882; ECO:0000269|PubMed:19939242}.', 'MGGQMQQNNAAAATALYDGALPTNDAGDAVMARWLQSAGLQHLASPVASTGNDQRHLPNLLMQGYGAQTAEEKQRLFQLMRNLNFNGESTSESYTPTAHTSAAMPSSEGFFSPEFRGDFGAGLLDLHAMDDTELLSEHVITEPFEPSPFMPSVNKEFEEDYNLAANRQQRQQTEAEPLGLLPKSDKENNSVAKIKVVVRKRPLNKKETAKKEEDVVTVSDNSLTVHEPRVKVDLTAYVEKHEFCFDAVLDEDVSNDEVYRATIEPIIPIIFQRTKATCFAYGQTGSGKTFTMKPLPIRAVEDLMRLLRQPVYSNQRFKLWLSYFEIYGGKLFDLLSERKKLCMREDGRQQVCIVGLQEYEVSDVQIVKDFIEKGNAERSTGSTGANEESSRSHAILQLVVKKHVEVKDTRRRNNDSNELPGKVVGKISFIDLAGSERGADTTDNDRQTRIEGAEINKSLLALKECIRALDNDQLHIPFRGSKLTEVLRDSFVGNSRTVMISCISPNAGSCEHTLNTLRYADRVKSLSKSGNSKKDQTANSMPPVNKDPLLGPNDVEDVFEPPQEVNVPETRRRVVEKDSNSSTSGIDFRQPTNYREESGIPSFSMDKGRSEPNSSFAGSTSQRNNISSYPQETSDREEKVKKVSPPRGKGLREEKPDRPQNWSKRDVSSSDIPTLTNFRQNASETASRQYETASRQYETDPSLDENLDALLEEEEALIAAHRKEIEDTMEIVREEMKLLAEVDQPGSMIENYVTQLSFVLSRKAAGLVSLQARLARFQHRLKEQEILSRKRVPR', 794, 'Q940B8; Q56WU1; Q9LUS1;', 'KD01216', 'Arabidopsis thaliana (Mouse-ear cress)', 'KINESIN-13A', '#Kinesin-13A#AtKinesin-13A', '-', '-', '820915'),
(1217, 'O81635', 'Kinesin-4', 'GO:0003777', 110009, 'Microtubule-binding motor protein.', 'MATTSEINNDLSFSVVSIVEDVLQQHSSRSSDVGLVSRKVEESSLRRYEAAGWLRDMIGVSNGKDFPGEPSEEEFRLGLRSGIVLCNVLNKVNPGSVSKVVEAPDDVADGAALSAFQYFENIRNFLVAIEEMGLPSFEASDMEKGGKSIRIVNCILALKSYSEWKLKGENGPWRYGSNMKHNFGSRKLFLRKSSEPFVSSISRTQSTDMLSTDQPLSSDGDSRSINGLVRSFIADRKHEDIPNVVESVLNKVMEEVQQRLSIHNEMMKSSSKPIPEDDSSCETVVRSQLCDARQHEEAEENSPPQVVEKKFQRTNFEHHEEQKILLNQQKHIQELKQTLYTTKAGMKLLQMKYQEDFFHLGKHLNGLAYAATGYKRVLEENRKLYNLVQDLKGNIRVYCRVRPFLPGQESGGLSAVEDIDEGTITIRVPSKYGKAGQKPFMFNKVFGPSATQEEVFSDMQPLVRSVLDGYNVCIFAYGQTGSGKTFTMTGPKELTEESLGVNYRALADLFLLSNQRKDTTSYEISVQMLEIYNEQVRDLLAQDGQTKRLEIRNNSHNGINVPEASLVPVSSTDDVIQLMDLGHMNRAVSSTAMNDRSSRSHSCVTVHVQGRDLTSGSILHGSMHLVDLAGSERVDKSEVTGDRLKEAQHINKSLSALGDVISSLSQKTSHVPYRNSKLTQLLQDSLGGSAKTLMFVHISPEPDTLGETISTLKFAERVGSVELGAARVNKDNSEVKELKEQIANLKMALVRKGNGNDVQPTAIPINRERISRRRSLETPTIRPKLPTMGNTSNNSRPQIMDLSGPEAFNDSTASSRRHSLDIHELMKSSSPAWPRQPLNGKDEDRESKSGEWIDKHEELIQNQNPNSPEQFYQSMVPQQQSLYGGKQDFEVQSITDNESDEAATSDCSDSDLLWRLSVQVNVPKVSNIQNSANPKPKKIQPRTAKLSETRSLIPSLIPAPSKRPPNTVNSQPQRPTRDGKRRLSLGT', 987, 'O81635; O04641;', 'KD01217', 'Arabidopsis thaliana (Mouse-ear cress)', 'ATK4', '#Kinesin-4#Kinesin-like protein D', '-', '-', '832758'),
(1218, 'Q20818', 'CAPG-2', 'k', 115547, '', 'MPKSNPVTPNKQPSEDWNELLTEFRGKGGRALQKTFIRKLWAVQEDIIANANPSTLRCIFFAPALLICPEGIKLSAEILPKIGVGNGLILLEKLILKFNLTDTECQRYGEVFVTAWRNAYQEANFDLTEELETDVISVMCQHALYAHRPTCTKFQNVIAAFAHAKKLDKSVDEMVTRLLNGCLYRALDAPNYIVQSSAAEVFFNFYPLIGEDTEDMDRIMENQHRYMMDLLRSDVISIRSEATKHVLKAISEFWLLIPKNIVKELMGYIIDTVAKDTVVSVRVAVFEGLNEMAFVPACLTAFEYGLKCAVDPALQDKSERVRLAAYQIISRLKNHKFISVFDIITRDDAIAKLDLENVETCRRQLIPIMHICLPISKSLDEAYYRPRVNYMLGKSRLALLSYFRLLGPMKIIDASQASKLIEMFITWAYRYLRKKDGPPLPETAEGYKKARAYLECALILYMSCKGMLMSDGDGTSKAKCDQIFGKVVKEIFEKYANTPILGTATAISSVIPKDYLKSIANDVLARLEDDDVPPEAVEPFLESAIHFNPDSVFDSFDSGLNVLVNLYGTKQSKKKRRELEDPEDVLIMTLNRLKYLLQSHSTSNLIAMKDEYRTKVLDLLKKIDLIREGIEIRLAKEEGQEHTLSDDVLLSILEFRFILPFFAATNGSEDAADRNQTIESMKNLLLWFEKNISSQMATFGEHNQDFLIQLTSTFLNCVNVSLSAYDFKTRPVEFEDEEDNENRDPREENDAAKDQATVAEVISRIVKSFCNSSTPFEIFRPALRVGTTLCDESYSEVHHEMALLLRFIPKWMNKQCDLMEDDEENIFKNHREIVESLRQFHKRVSETDYWDEDSAKRMMHHFMLFSIVSASSKNDDEAYDDPRDEDYKPPHFISLALIKFILKEKSLTEDIIEEISTNYIPEDSKYFTAEEGELKTDEKLSKLAALSQLLRILERYSKFHGKLIKEAIDKCTTRVLDCFANASDLNTVAHHILNSLSSLLDVQLPDENRL', 1010, 'Q20818;', 'KD01218', 'Caenorhabditis elegans', 'capg-2', '#CAPG-2 {ECO:0000313|EMBL:CAB01569.1}', '-', '-', '179684'),
(1219, 'A4QYI9', 'Tethering factor for nuclear proteasome STS1', 'GO:0061638', 34174, '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}.', 'MNVLLTPQPTPFPHQYETSRLSPQRSLSPYTNMTSRKRKADDNEGDEMSVSPLSSPAIPSRHLSRPSKKIRAAEASGRPLPLPRLLETLDTTQLRTVLQKICERHPDIGQEVVNGAPRPSVGSALGILRDYQQRLRGAIPYGQTSSDYTYYRVKQPLMALVDAISDFTPQFLPPIETQVTASLQYLDGATKVVHELPDWDSQAYRQHKDNAYDEISRAWALVITEASKRGGGFVLHTGGWDQMLAKHNQQSGGRLGSAMQAMASNGWIGNNSPNNQNASASSSSGSGAGGDPNSILNQLVNGTYGNPVRVGPW', 313, 'A4QYI9; G4N669;', 'KD01219', 'Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Ricblast fungus) (Pyricularia oryzae)', 'STS1', '#Tethering factor for nuclear proteasome STS1', '-', '-', '2678698');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1220, 'O08672', 'Kinesin-like protein KIFC2', 'GO:0003777', 85686, '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.', 'MYAFYSLLIYIFYSLFRRDGGAAAVSDPGDPTQKSGGQPRGRRRPDQFTSELWSELNSLAGCSESEDGQKGAEGGAAEVSLEEALMRLAEFLSVQLGAEESCGTTPDLGKPGEVPPLLTVTSQLLALLAWTRSPRGRQALLQGTQPTCPVQPSTLDGSLSQEESSSQPTPILDEVPRDETQEHQPLQLEEEQRVWQRLEQLILGQLEELRQQLEQQEEELSRLRLGVGVTDSEKRVQHLTLENEALKQSLSLTRDLLLHWGPGPLPRLSQEEAGALLELQGQLQEAQDTTEALRVQLGAQELQLQGLRGALRQLQQETEQNCRQELQQVHGQLAGLRARMASLRQGCGDLRGLVSTFTQSCQGSLSEAQGQVSWALGALSAGKAKTQLSEGNQAPPTGCSGRLLELKGNIRVLCRLRPAEGQPSSLVSVEPGQGGTITTCYRGRQHCFRLDWVFPQDASQEEVFRQLEPAVLSCLQGYSVCIFTYGQTGTGKTYSMEGPPEDPGIAPRALQLLFREMGTGGHHHVTLSMVEIYNEAVRDLLATGPPERLVVRQGPAGQGGIQVAGLTHWDVPNLETLHQMLSLGRSNRATAATVMNQHSSRSHALVTLTLRAASPPRPQGITGTLHLVDLAGSERVWKAGVASPVQRDPNGARRLREAQAINRSLLALGGVMAALRARRPHVPFRDSQLTRLLQPALWAGTTAVLLLQISTRAEDLGETICSLKFAERVGQVELGPARRRRAPRSGTPSSLSTDTPLTGTSCTPTPSPGSPPSTSPNSCSGLTLEPPGDPPP', 792, 'O08672; O08613;', 'KD01220', 'Mus musculus (Mouse)', 'Kifc2', '#Kinesin-like protein KIFC2', '-', '-', '-'),
(1221, 'Q76I89', 'Kinetochore protein NDC80 homolog', 'GO:0000776===GO:0000777===GO:0000778===GO:0000942===GO:0051315===GO:0031262', 73741, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:12829748}.', 'MRRSSTTSGSSGRQSTMVLRVQDSNKMGLQTPQTKDRGTFGKLSMSKTTSATSERKVSFFGKRASGAGGSRNSQYGMFGTEKIKDPRPLHDKAFIQQCIKQLCEFLVENGYAHNVTIKSLQSPSVKDFIKIFTFIYGFLCPSYELPDSKFEEEIPRVFKELGYPFPLSKSSMYTVGAPHTWPQIVAALIWLTDCFKLYAAMRENPSSFDDGQNWGGETDDGIVHNKLFMDYVVKCYEHFMKGGDTYEELDAEVQSKLKDLFNVDEFKIEGLAAENKRLHEEIARLEKERESEPDRLVSLRKLRSSFQADVQKYQAYLANLESHTTILDQKMKSVNEEVETTEMEVEAMKQENARLQHIFDNQKYSVADIERINHERNELQQTINKLTKELEAEEHQLWNEELKYARNKEAIETQLAEYHKLARKLKLIPISAENSKGHDFEIHFNPEAGPNCLVKYRTQIKAPLMEIVNQTEEEIRKATQRKMSLEDTLEQVNAMVAEKKSSVKTLKEEAEKLDDLYHQKLKEAEEEEQKCANELELLEKHKQLLESGVNEGLSEATNELHDIQRQYQIVMQTTTEESRKAGDNLNRLLEVITTHVVSIEKYLDEQNSKIDRDYEEFMSEDLLSTLTGILDSYKKKAESI', 640, 'Q76I89; Q5ZLT8;', 'KD01221', 'Gallus gallus (Chicken)', 'NDC80', '#Kinetochore protein NDC80 homolog#Kinetochore protein Hec1#Kinetochore-associated protein 2', '-', '-', '395134'),
(1222, 'P0C6F1', 'Dynein heavy chain 2; axonemal', 'GO:0003777', 511565, '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}.', 'MASKAEKKRKVAGRGGARAGRVVRAPQSTAGPGATEASLLPDGQEPEPESGKEDSVLGLQAFASWRLTPALHGEANTPPTLLHPQPLFHRRLTTLNLILSCSRAGTRDLALKPFFLSRTMLTGLADATWTGEHDMVLEHFVQDPAVPALTIFIDPVFGLKLELGMPVQTQNQIVYFIRQAPVPITPENFEETVQYGTVRGAYIPALLRLLSGVYVPQIFMNKSWPESIRNHFVSHLHRFLASLTDTRYKLEGHTVLYIPAEAVQMDPEVVVKDKELVQRLETSMIHWTRQIKEVLSAQESVETGENLGPLEEIEFWHNRCMDLSSISKQLVKKGVKHIESILFLAKSSYLTPFRKLAQQIQDGSRQAQSNLTFLSILREPYQELAFMKPKDISEKLPKLISLIRIIWVNSPHYNTRERLTALFRKVCECQYHFARWEDGKQGPLPCFFGAQGPQITRNLLEIEDIFHKNLQTLRAVRGGILDVKNTSWHEDYNKFRGGIKDLEVMTQNLITSAFELVRDVEHGVLLLDTFHRLATREAIMRTYEKKAVDLYMLFNSELALVNRELNKKWPYLEPYMTQYSGQAHWVRILRRRIDRVMNCLSGAHFLPHIGTGEESIHTYQQMAQAIDEMVRKTFQEWTATLDKDCIRRLDMSLLRISQEKVGMLDVNFDKTLLILFAEIDYWERLLFETPHYVMNVAERAEDLRILRENLLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKKLNWALKGASAFFITECRMHASKVQMIVNDFKASTLTIGWKAQEMSELLLVHITGKQVYRDLEFEEAQREHRMAAQQKLVKLHQDVVNIMTNSYEVFKNDGPEIQQQWLLYTIRLDHMMEDALRLNVKWSLLELSKAINGDGKTTPNPLFRVLVILQNDVRGGGSQVEFSPTLQTLASVVNDIGSHLFATISVFRHLPDILTKRKMNREPIYVLVERDEDIRKIQAQISSGMTNNASLLQNYLKTWDMYREIWEINKDSFIRRYQRLNPPVSSFDADIARYTEVANNVQKEETVLNIQFVMLDCSHLKFSLVQHCNEWQNKFTTLLKEMAAGRLADLHSYLKDNAEKISHPPQTLEELGVSLQLMDTLQHDLPNLETQIPPIHEQFTILEKYEVPVPDTVLEMLESLNGEWLTFQQILLDSEQMLKKHKEKFKTGLIHAADDFKKKAHNLLEDFEFKGPFTSTVGHTAALDQIAQMRAMLMAMRDEENNLRSNLGIFKIEQPVSKDLQILEKELDALQQVWEITRDWEESWNQWKMGCFQTLQTEAMESMAHGLFRRLTRLAKEYKDRNWEIIETTRSKIEQFKRTMPLISDLRNPALRERHWDQVKEEVQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQLDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLGEDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPGLLETLIEMNAILEDIQKSLDMYLETKRHIFPRFYFLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKVGGSSSKWEAVGMFSGDGEYIDFLHPVLLEGPVESWLGDVERAMRMTLRDLLRNCRVALKKFLNKRDKWVKDWAGQVVITASQIQWTADVTKCLMTAKERSDKKILKVSILNKYSEAIRGNLTKIMRLKIVALVTIEIHARDVLEKLYKSGLMDVSSFDWLSQLRFYWEKDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSGLAQSGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFRPIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLSDEEVLLLSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVGGTGSSKTTSWKILQASLTSLCRAGEPNYNIVREFPLNPKALSLGELYGEYDLNTNEWTDGILSSVMRVACADEKPDEKWILFDGPVDTLWIESMNSVMDDNKVLTLINGERIAMPEQVSLLFEVENLAVASPATVSRCGMVYTDYVDLGWKPYVQSWLEKRPKTEVEPLQRMFEKFINKILSFKKDNCNELVPVPEYSGIISLCKLYTVLATPENGVNPADAENYSFMVEMTFVFSMIWSVCASVDEDGRKKIDSYLREIEGSFPNKDTVYEYYVNPKMRTWTSFEEKLPKSWRYPPNAPFYKIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRVKQSIKHIRDMFLMAAMGPPGGGRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATLDVYNTVVQRFLPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTKASITRLWIHECFRVFSDRLVDTADMEAFMGILSDKLGTFFDLTFHHLCPNKRPPIFGDFLKEPKVYEDLVDLTVLKTAMETALNEYNLSPSVVPMQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQTTSFLFVDTQIADESFLEDINNILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIPESSDSLFAYLIERVRNNLHIVLCLSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYIIGVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLELRRYNYVTPTNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLIAAAFLSYMGPFLTNYRDEIINQIWIRKIRELQVPCSPRFAIDNFLTNPTKVRDWNIQGLPSDAFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQNVQEYLDPTLNPVLNKSVARIGGRMLIRIGDKEVEYNPNFRFYLTTKLSNPHYNPETSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINIDLAREAYRPCAQRASVLFFVLNDMGRIDPMYQFSLDAYIGLFILSIDKSHRSNKLEDRIEYLNDYHTYAVYRYTCRTLFERHKLLFSFHMCAKILETSGKLNMDEYNFFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFHGLMNSFEQYPRDWHLWYTNSSPEKAMLPGEWENACNEMQRMLIVRSLRQDRVAFCVTSFIVSNLGSRFIEPPVLNMKSVMEDSTPRSPLVFILSPGVDPTSALLQLAEHTGMAHRFHALSLGQGQAPIAARLLREGVNQGHWVFLANCHLSLSWMPNLDKLVEQLQVEDPHPSFRLWLSSSPHPDFPISILQASIKMTTEPPKGLKANMTRLYQLMTEAQFTHCSKPAKYKKLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFCDLSLTTPFYRLSVLDTYYIPKDGSLASYKEYISMLPSMDPPEAFGQHPNADVASQITEARTLFETLLSLQPQITPTRVGGQSREEKVLELAADVKQKIPEMIDYEGTRKLLALDPSPLNVVLLQEIQRYNKLMKTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKVYPSQKPLASWTRDLAVRVEQFETWASRARPPVLFWLSGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIVSTVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVCLMPTIHFRPAESRKKSAKGMYSCPCYYYPNRAGSTDRASFVIGIDLRSGSMTSDHWIKRGTALLMSLDS', 4456, 'P0C6F1; B1AR18; O08826; Q8C0U5;', 'KD01222', 'Mus musculus (Mouse)', 'Dnah2', '#Dynein heavy chain 2; axonemal#Axonemal beta dynein heavy chain 2#Ciliary dynein heavy chain 2', '-', '-', '-'),
(1223, 'Q19325', 'SCC-1', 'k', 73409, '', 'MFYAQFVLAKKGPLAKVWLAAHWEKKLTKAQIFETDVPQAIEEVIRPKVKMALRTVGHLLLGIVRIYSKKTRYLLADTNEAYQKMKINFRNGFSFEVDIPENAEIEEDFSNFIDKYNITVPEFHDADYNEQLIMANVSRREDITMKETVNFNVEFNIDADFDGFGDEGESWQLDHLYGSVEPLSLRPTPQPESLMEVERDRDVAANGTEISRIDADSVIFSEGPTRPNLIFDNQEGGNFMPEMNLKVENQTLENDGGVGPADMFSSMIHPVREHAVADVQNDDGMDFDYQPFEPENVEPSRPQSPESFALEPLDVEHMEGRKKRQRKARKLIVDAETMISNDAFREQQEDFSDTMRVVEMAPPTRKMFNLCVSGDLQHLSREPGCKMFNRELLQRYRRCLVTREFDLNYTMQELSDSSSFTPSMEAQAEPWEDLNLNEDIQEDIQAQGPAVDEFFNDVRMDDDDDRQPAQEMDFGDNFDFPQEVEHQECAPIPIQSGFAGENKENEDAEDWSDPFGSSNSSRRGQLEAYGFGNTSTYKEDDGKWAKRAKHILKKVSADIETSGQADFSSVTATAKNRKQAAEQFYSLLTLAKSQAISVDQSEPYGEIVIRPGANFKEACPLSSPKPMGLGNTMENSTMRTPMRPV', 645, 'Q19325;', 'KD01223', 'Caenorhabditis elegans', 'scc-1', '#SCC-1 {ECO:0000313|EMBL:CCD69206.1}', '-', '-', '173808'),
(1224, 'Q1ZXQ8', 'Centrosomal protein 224', 'GO:0000776===GO:0000777', 223812, 'Involved in regulation of microtubule dynamics. Regulates the interaction of microtubules tips with the centrosome and cell cortex. {ECO:0000269|PubMed:10769206; ECO:0000269|PubMed:12952061; ECO:0000269|PubMed:14517319; ECO:0000269|PubMed:15186508}.', 'MGDEEAPSGSIEDRINHKNWKWRVSGLEELTTKFRNSIEGSGPLFNEWGPQFKKILADINPMSQERALEPLSAFIDRCDCVNKFAASYVGVLVEKLFASTRPRAKEKTIECLLLTIEADSAEPVVEALLKGTSSTSPKILLASLAALTQALKTFGPKQIPVKLILKQFSPWFENRDKGIRDQASELFIEIYRWIGKALIPLISEALTPIQLKALQDQFEKLPTDPAVPLKYTRSEAAKALANASKGIQAKPEVVEEIDPYSLMTAVNILPKLTSEFYEGLQAKKWQERSEQMDKLVTILTNTPKIETADFSELCKALKKILADVNVMIVQKAVVSIGLLADSLRGGFTSYVKPFITPILEKFKEKKTSVLQSVHTTMDSLVGKSISLSDIIDELTATMQSKVPQIKQEVLVFICNSITNTKKPADITKVTKQLTKIFMEALNDTDSNIRDNASKAFAALGGIIGERAMTPYLNQIDPIKAKKIKDNMPAVATPVTITPQPLAPVDLKDIDLPVSSSNKKPAAATGNSKSSSTTTPTGRSSNSSPLPPPPSSSDDIKNKLIGAGIVNNEIIEGLGKTQWKDRLQAVDDILENVKGLTADSINGMSESIIQLLCDKPSLKESNFQVLSSIFSIFIQCCKNDSNFTQQRCANSYLTTCIEKLTDVKLKEISSELLFSTGESITPHAVFTSIYQFTSNHKNPKIIADSLVWIQQAIDEFGIGCCSNGIQQLKPLLDYTKQCLESTNPDVKKSAIKLLCTIKINIGATLTDFLGDVKKPTMEVLDREFQKIRDQKPPVPNRQWKGMPPPGSAPVQIEFPRVDISVKLTPAIITNLSDANWKTRSDALDEIERIIIDANRKIQPKLGGLIPALKNRLTDNNQKCTITTLNIIGMLSQAMGGQSFEKHARLLIPGILLLLGDSKKPVRDAVISCMNVIVQSDLGFDVFIGSLAAPMIQESAFTRKESLAWTIVNVTNMKAAPIPSEINTLAKGIISCLQDKSAEIRSLADNLLSILCTQIPLIEFKKELKHVKPASQPSIQTILDKYYQKTGQPIPPPSKTKQSTSSSSSSSSTTSQQSSTPSSPQPIRQQQQQQQQQPTQPQQQQQQQQRRSILQSNNGASNCEFIIFDINGKMNRQKTNQIPSWHFIEPTEEVVEILQDQVLQCFTEEFANLMFSSLPSNSQHMSDLMIGMIEQNPEAIISVLDILFRWITFKLFDTGLASQKRVLKILEILLNKLIDSEYSIGEYEASCLVPILLEKSGSATNEQIKQIFKQSIQQLEELCLPNVLFRFAIEMVTSQNWRTRVEVLNVMASIIDKNGASVCGNLKVVIPLITQNLNDSQSKQSSLLCLNKLYSHIKDECFKYSNISQQDKILIIGNNNNNNNNNNNNNNNNNNNNVQQQQQQQQQQQQQQPRKSLSTDEMSTQLIGCLELLKNYSITKENIEHTVEALKQFSGLMANGKLDDVFVNFAEEYFLVLTSILADTFPQVSKDATILRLCKYLIHTIISILSNKVVAKQCNVRCLEIVLNETIKLYSLAESNSSKQGTESELSKAFNQILLRILQNCNSTILFSTLLQMMSRTDNDQSIQHPGKYNDLLLRCLLRATKSLTTPSILEELNVETVLSEINSFLKSNPSLDEITRKTTKTLTSELYQNRTNQVVKFTKDIISKGQQQKYQYLLNLLIELVPKQFEDLINGNGNGNRISSGGSNNNNNNGGRVSSGGNNNNNSGRENINNININSSLDSPINDHHNSNNTTTTTTRSRTSTGSSNSQQQQLPTTSANTTTTTTTTTTTGKTQSTLSTLKINKEPRDYSGKTDSQKKELLIEIFKKIGNKDLTLDGIHDLYFFIREYPDYDITPNLNSSSQQFQAYITRNLKKIKDSMDAPKDKDDEVVNYQERLKVIQNTFYNQHNQPSSQVVNNNNNNNNNNNNNNNNNINNNNNNNNNSGGNENIAPQLSNTASMASNTLQRLRTLNPDQNSGSNNNNSHQNSPSTSSSNDLNSTVASLRQRLAQLTSKSNE', 2013, 'Q1ZXQ8; Q9U5Y1;', 'KD01224', 'Dictyostelium discoideum (Slime mold)', 'mtaA', '#Centrosomal protein 224#CP224', '-', '-', '8616510'),
(1225, 'Q9CU62', 'Structural maintenance of chromosomes protein 1A', 'GO:0000776', 143235, 'Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM; and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central component of cohesin complex. The cohesin complex is 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. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM; or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000250}.', 'MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEESVSGSQRTSSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ', 1233, 'Q9CU62; A2AFQ5; Q3V480; Q9CUX9; Q9D959; Q9WTU1;', 'KD01225', 'Mus musculus (Mouse)', 'Smc1a', '#Structural maintenance of chromosomes protein 1A#SMC protein 1A#SMC-1-alpha#SMC-1A#Chromosome segregation protein SmcB#Sb1.8', '-', '-', '24061'),
(1226, 'P53168', 'DASH complex subunit DUO1', 'GO:0008608===GO:0051987===GO:0042729===c;k', 27473, '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; ECO:0000269|PubMed:9817759}.', 'MSEQSQLDDSTIDKLIPQIFNEMRSNLNNTTNKFPKSTGGGASDNISANSNSIRSFNSITTQSLLKESESLDKITAMIKNVTAALKNNLPVYVNQVHEVCKSTNSILDSWINIHSQAGYIHKLMSDQTYLKLINDRLHNENVNTNDEDGSTLHNVIALKKKEILDLRQKLENRKGEKDAAPAKPPNQGLNPRYGVQSGRRPVPSAGISNNGRVRKTHVPASKRPSGIPRVTNRWTKPTASSSRKMFR', 247, 'P53168; D6VU80;', 'KD01226', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DUO1', '#DASH complex subunit DUO1#Death upon overproduction protein 1#Outer kinetochore protein DUO1', '-', '-', '852819'),
(1227, 'P53169', 'YAP1-binding protein 2', 'GO:0000778===k', 73102, 'Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced activation of YAP1. Acts in a parallele pathway to YBP1. {ECO:0000269|PubMed:11570514; ECO:0000269|PubMed:12743123; ECO:0000269|PubMed:15075262; ECO:0000269|PubMed:9990050}.', 'MYNEQVNSGKSIKEKERYLDALLKILKDNPVTLKEIGWDLPKGLLQFFSRKNINVNIHLVFSPLVSSVMECFNELAINGNPKECLLTACELVSTLHIVLTETGDSDEENEDLNDSNRNDASNITDELSVITPEIGHYMAKNTVEFIPNLKIYVLFEFMSLLLKRVDTLYPSKFLAMVTSAIIKYVTTNVQAMDDPHFILRIVYNFCTNYSPAQPSASLTDGISTNDLEKIHDDESALQKKLLANLSVFVISNCLKNHPGNIDKIYFKTLMHKKTDENEIDASVLQICHQYYEYVTSLDVHMKELLEKCLVESRSIYNSLLMNPAASTPEFKEEINQLVYEVSYAYQIKKLADEKNLELDQYGVVILSAIHYSKNGTHLLPQIDIQSAIYLYLRCTTASLFSEIYENKFLESSVRYWLWVSTTETSTEKIKCALQELPGHITTAFLQMLLMKTCNESNNDTKLTEITLLRRLLYLMPESTSFTFIFETLLHCPYITAKIAVLDILRDMMIRSPEAANRDETVGLIEQQNPGNTANSVPIMPTLPPRPYITINEDRMASIHSIALICFSAAKQKKRTQGDLLLVLTYMKFFVSLRNKWDLGLLTLINKEISESFQGEGEPELAFINISNNTLGEYIEEMNIRS', 641, 'P53169; D6VU81;', 'KD01227', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'YBP2', '#YAP1-binding protein 2 {ECO:0000303|PubMed:15075262}#YBP1 homolog protein 1 {ECO:0000303|PubMed:15075262}', '-', '-', '852820'),
(1228, 'O94494', 'Centromere protein sim4', 'GO:0051382===GO:0000941===GO:0000779===k', 31730, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. Has a role in the maintenance of core chromatin structure and kinetochore function. Required for the localization of mis6 and cnp1 to the kinetochore. {ECO:0000269|PubMed:12719471; ECO:0000269|PubMed:16079914}.', 'MNSENASLFRNILNDTENLVQPLTQDESRLALFESLVQSDQLLVEKIEKWEKKVSKFTENSKSEKRKLQLELFQEIIDLKKCIAFKPIIGKNAIDNNISDLKKNLHSNKKLEAVLKEELHQIKKFSSDLQSLKSSMGERQKQQAAMSRRGKKSIIHSAIIQEKERYEKESQELFTFLDGFLDEHAPSLLEGAQASIDKNRPGKNQPSLNFENISKKDLTEEFKQVIENLMNNSIIPGSPYIEVKNERIVSFLVLASLCTVDPQDPSKVKLIPFSDEI', 277, 'O94494;', 'KD01228', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'sim4', '#Centromere protein sim4#Silencing in the middle of the centromere protein 4', '-', '-', '2540804'),
(1229, 'O76523', 'Mitotic checkpoint control proteinMitotic checkpoint control protein Bub3', 'k', 37047, '', 'MRPPEFKLNNPPEDLISAVKFGPKSNQYMAASSWDGTLRFYDVPANQLRQKFVQDAPLLDCAFMDIVHVVSGSLDNQLRLFDVNTQAESIIGAHEEPIRCVEHAEYVNGILTGSWDNTVKLWDMREKRCVGTFEQNNGKVYSMSVIDEKIVVATSDRKVLIWDLRKDGQLHHEAGVLAQVPRPAAFVYSPTKKATVMSSIEGRVAVEYLDHDPEVQRRKFAFKCHRNREQNIEQIYPVNALSFHNVYQTFATGGSDGIVNIWDGFNKKRLCQFHEYDTSISTLNFSSDGSALAIGCSYLDQLPETPATVPHPAIYIRYPTDQETKQK', 327, 'O76523;', 'KD01229', 'Drosophila melanogaster (Fruit fly)', 'Bub3', '#Mitotic checkpoint control protein {ECO:0000313|EMBL:AAD44035.1}#Mitotic checkpoint control protein Bub3 {ECO:0000313|EMBL:AAD13398.1}', '-', '-', '-'),
(1230, 'Q06032', 'Chromosome stability protein 9', 'k', 53863, 'Component of the synapsis initiation complex (SIC) necessary for the synaptonemal complex assembly. Stabilizes the ZIP2 component to the chromosomes. The SIC complex loads onto chromosomes and nucleates ZIP1 polymerization; a molecular zipper that acts to bring homologous chromosomes in close apposition; which is required for meiotic crossover. May also be involved in double strand break repair. {ECO:0000269|PubMed:10454593; ECO:0000269|PubMed:10943844; ECO:0000269|PubMed:15035982; ECO:0000269|PubMed:15070750; ECO:0000269|PubMed:15805472}.', 'MGGYLAIVFIPQTNTKSMREKKQKCLKQVRRLSLISPKKYIMPDSIFEQPFVYCGVCHRRTSHGDPLRLTSCAHILCSQHSPLTSKVCPICRSSDISIINLVESKQLPTDIRIFFEPLPPLLESLYNVSQFQLNGLSKQCQYYQNHCLKLREKCARQQQLLYQAKIELDSMAILKKRIQELESVLNHNNVSSMSVGVLPTRNSHQNHYQPPPTVDLTVDDNSLEEFEAKSFIKKLKKNSSLRNSSKNNNGTVTPSTSGRVNKNQPLFMETLNNPNRNSIPPPGMNPNANSNLPNISTIAESTNLNRFSFSPVRVAKGFDGKLPNLDILTNNGSVSSKNISRLSSASLQPSSPLSSSSNRLILPNSNLKELHHSNTPLTSTSTQFPSALEKLKITRKRNNTISGSNRITHNLSSHVRSSGLAFSSSSNSLQQSKLPKSNILKRSNSTQQLTNTHLKSDNHLPPRSSNTVLGSSKKNNKFRRIR', 482, 'Q06032; D6VZ29;', 'KD01230', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CST9', '#Chromosome stability protein 9#Molecular zipper protein 3', '-', '-', '851110'),
(1231, 'Q76I90', 'Kinetochore protein Nuf2', 'GO:0000777===GO:0031262', 55127, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:12829748}.', 'MEALTFPRYSPDDIVAYLRSHVLVGAEARNLTKADLFATLKPEVLHMIFIRILQKVYGIRLEHFYMMPVNVDIVYPQIFEGFLPVCNLYIHMERFLPVCRVNDFQMSDVINPKAKRTARFLSGILNFVHFRECRREAYLELQLNYKSAMEKHQQLETANQELEMKLEKLNTVPVEQQAEFKQLSDDIQELEQLLSHDYRRKTAALQEVISQKKSDITERTRKLNELKVTMATLKEEQEQLKSKIVESPEELKNYKELMKETVKKLKKSKQEVIEKYEGYRDLVEVLPSCQLEVQLYQKKMERQAANVERLASVLSEVRNLEDQLESAQIELKKGKTDEMSLKRLVTAKHERLSTAEIRIKKKREDVEQYKHTVFEYFNRVQEKRGVVYDKVTAIQKEIQQMRFKIQQLNESAEEEEMKAKEIYQNLKAGLEKRHDSLIKTAKNYAASREDKIAELQKGLLRVQSPGSSS', 469, 'Q76I90; Q5ZI77;', 'KD01231', 'Gallus gallus (Chicken)', 'NUF2', '#Kinetochore protein Nuf2#Cell division cycle-associated protein 1', '-', '-', '395135'),
(1232, 'Q5R4C2', 'Sorting nexin-4', 'GO:0005868', 51967, 'May be involved in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation (By similarity). {ECO:0000250}.', 'MEQAPPDPERQLQPAPLEPLGSPDAVLGAAVGKETEGAGEESSGVDTMTHNNFWLKKIEISVSEAEKRTGRNAMNMQETYTAYLIETRSIEHTDGQSVLTDSLWRRYSEFELLRSYLLVYYPHIVVPPLPEKRAEFVWHKLSADNMDPDFVERRRIGLENFLLRIASHPLLCRDKIFYLFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFTDLKHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRKHELMQYDLEMAAQDLASKKQQCEELATGTVRTFSLKGMTTKLFGQETPEQREARIKVLEEQINEGEQQLKSKNLEGREFVKNAWADIERFKEQKNRDLKEALISYAVMQISMCKKGIQVWTNAKECFSKM', 450, 'Q5R4C2;', 'KD01232', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'SNX4', '#Sorting nexin-4', '-', '-', '100174015'),
(1233, 'Q6I6F4', 'Baculoviral IAP repeat-containing protein 5', 'GO:0000777===GO:0032133', 16393, '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 cytokinesis 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}.', 'MGASSLPPAWQLYLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLSEFLKLDKERAKNKIAKETNHKQKEFEETAKRVRCAIEQLAALE', 142, 'Q6I6F4;', 'KD01233', 'Felis catus (Cat) (Felis silvestris catus)', 'BIRC5', '#Baculoviral IAP repeat-containing protein 5#Apoptosis inhibitor survivin', '-', '-', '493835'),
(1234, 'P30822', 'Exportin-1', 'GO:0000776===GO:0034501===c;k', 124104, 'Receptor for the leucine-rich nuclear export signal (NES).', 'MEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFSTNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKSDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQAKALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELLSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLKATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERELFKTTLDYWHNLVADLFYEVQRLPATEMSPLIQLSVGSQAISTGSGALNPEYMKRFPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREFVKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDLLDLTVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFLSALTKQYKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENALMEQNRLEREKAAKIGGLLKPSELDD', 1084, 'P30822; D6VV01;', 'KD01234', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CRM1', '#Exportin-1#Chromosome region maintenance protein 1#Karyopherin-124', '-', '-', '853133'),
(1235, 'O94488', 'Microtubule organizer protein 1', 'GO:0051315', 128469, 'Required for cytoplasmic astral microtubule growth during mitosis. Involved in localizing components of the gamma- tubulin complex to the non-spindle pole body (non-SPB) microtubule organizing centers (MTOCs). Required for new microtubule nucleation from non-SPB sites during interphase. {ECO:0000269|PubMed:15004232; ECO:0000269|PubMed:15120067}.', 'MEENSSELDSNNFNVLVDNLAGLSLTDEEVRRILSPRKEGSRQLPSSTSKDEDSEEASHKYDFEIDRDSLKSDSGSPRLHQNATAPTSSTPLQSPDESVNKLNSEDEEGNSSVAPFFLDTTNFDRLNDNITTDDEQLSPVLTANQGFQSQEQYEEDSYNNYDYTSDPSSPNYISSSLDQLPHLDDEDDLQLTPIKEERNYLHSQDAPTTNALSKKISDILIPASAMKDLKDRKNALAKEFEESQPGSSLTLKEQANVIDNLRKEVFGLKLKCYFLYDQLNKFHDQEVQDIMKQNIDLKTLTMELQRAVAGYEKKISGLESRIKPDQSFNLSTPSPAPSNLITLQSRYSQALSELETTKRAFAALRKEKSKKTNYSVGAYNEDRNVLSNMLDNERREKEALLQELESLRVQLSKKVPMPAKNTDERVIETLQRSNELLRMDISMQNEALLLRKQENDRLVKQVEELTVALNSGKMNAIVEAESSKNELWDSMMVSRMKTQEQSIELTRLYKQLQDIEEDYENKLMRMEQQWREDVDQLQEYVEEITQELQDTKEVLSKSSKESDDYEEVVGKLRTEAEREIEKFEKTIRENEESISLFKEEVEKLTDEITQLSERYNDKCHEFDELQKRLQTLEEENNKAKEDSTSKTSNLLEQLKMTEAEVDSLRKENEENKQVIALKESELVKSNDNKLLLNEQIESLNDQLSQLKTEMESVTTSKESLADYLSNLKERHNDELDSLNKKLREFEGILSSNSSLKSEIEERNNQYVTLRENFDSLQNAIMETFDKQVTHCSVNHLVQQIRKLKDENKKDQSGTDKLMKKIYHCEQSLKEKTNSLETLVSEKKELKNLLDAERRSKKAIQLELENLSSQAFRRNLSGSSSPSERSQSRELKLLQASEKRLKEQVEERNSLIKNIVTRFTQLNTGSKPVNTNVEALTTISSMNQAVNMNFRELDKSIQEFKRKCQSMEREFKTELRKLDGVLEARSKRLSQLEERVKLLGAGSTSSIPNSPRASKRVSLDSEDKKLVPASPDKSAVQRGITALKRDAEGMSHIWQLRLREMEFQLKAEQEGRKRDKLGARERLQDLIRQNRSLSRQIKTDKESNSRSPSISSQEHK', 1115, 'O94488;', 'KD01235', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mbo1', '#Microtubule organizer protein 1#Morphology defective protein 20', '-', '-', '2539467'),
(1236, 'Q5SQY2', 'Biorientation of chromosomes in cell division protein 1', 'GO:0000777', 18364, 'Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000250}.', 'MADGAGAGAAGQASGPSGGSSGAGGPVNPASLPPGDPQLIALIVEQLKSRGLFDSFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNPAMNKNQLRNGLRQSVVQSGMLEAGVDRIISQVVDPKLNHIFRPQIERAIHEFLAAQKKEAVPAPPPEPESQDPPAPSQDAS', 173, 'Q5SQY2;', 'KD01236', 'Mus musculus (Mouse)', 'Bod1', '#Biorientation of chromosomes in cell division protein 1#Biorientation defective protein 1#Protein FAM44B', '-', '-', '69556'),
(1237, 'Q5I0E8', 'Kinesin-like protein KIF22', 'GO:0003777', 73056, '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}.', 'MNVRAKKKPQQREMASASSGPSRSLSKGGVSRRPPLARVRVAVRLRPFMDEAKEPPCVRGIDSCSLEVANWRKYQETLKYQFDAFYGEKSTQQDVYVGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREESAEGRPWDISVAMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLTQKPITSFSEFEQHFLPASRNRVVGATRLNQRSSRSHAVLLVKVEQRERLTPFRQREGKLYLIDLAGSEDNRRTGNQGIRLKESGAINTSLFVLGKVVDALNQGLPRIPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYQDTISALNFTARSKEVINRPFTNESLQPHALAPVKLPQKELLGPSEAKKAKGPEEESTGSPESTAAPASASQKLSLLQKLSNMDPAMLENLLSMERLLGSQGSQGIPLLNTPKRERMVLIKTVEEKNLEIERLKMKQKELEAKVLAQEALDPKEKENTPTILQPSSSCSGSVAKPLKKAVVMPLQRIQKQSESSNKIHLLKKGHKRKLESSHESEAVEKDEDYWEIQISPELLARGRKKLLHLLNEGSARDLRSLQRIGQKKAQLIVGWRELHGPFNEVEDLEQVEGISGKQVESFLKANLLSLAASQHSGPS', 657, 'Q5I0E8;', 'KD01237', 'Rattus norvegicus (Rat)', 'Kif22', '#Kinesin-like protein KIF22', '-', '-', '293502'),
(1238, 'O94483', 'High osmolarity sensitivity protein 3', 'GO:0042729===GO:0031134', 10381, 'May play a role in the progression of mitosis in an environment of high osmotic stress.', 'MRRSTIVPTSRTSSSSPSPSQMKSFQMNRLVDQLSKLQSNMSHLENHLHVTAIQAEAIRRLGALQASLLMASGRVMSEARIQKSSDAVEEDVPM', 94, 'O94483;', 'KD01238', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hos3', '#High osmolarity sensitivity protein 3', '-', '-', '2539507'),
(1239, 'Q95LT1', 'Kinesin-like protein KIF2B', 'GO:0000777===GO:0003777', 75628, 'Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. Has microtubule depolymerization activity (By similarity). {ECO:0000250}.', 'MAGQFCLPVSPRLSPLKPLKPHFGDIQVGIYVAIQRSDKRMHLAVVTEINRENSWVTVEWVEKAVKKGKKIDLETILLLNPSLDSAEDPMPVSPLAPAPSSAIGDQSTTTKRVVMIPQKNKTASGDSLDVRVPSKPCLMKQKKSPCLQEIEKVQKQREKRRRLQQEIRARRALDVNTRNPNYEIMHMIEEYRRHLDSSKISVLEPRQEHRICVCVRKRPLNQRETTLKDLDIITVPSDNVVMVHESKQKVDLTRYLENQTFCFDHAFDDKASNELVYQFTAQPLVESIFRKGMATCFAYGQTGSGKTYTMGGDFAGRAQDHSKGIYALVAQDVFLLLRNSIYEKLDLKVYGTFFEIYGGKVYDLLNWKKKLQVLEDGNQQIQVVGLQEQEVCCVEEVLNLVELGNSCRTSRQTSVNAHSSRSHAVFQIILKSGGKLHGKFSLVDLAGNERGADTTKASRKRQLEGAEINKSLLALKECILALGQNKPHTPFRASKLTQVLRDSFIGRNSSTCMIATISPGMTSCENTLNTLRYANRVKELNADGRPYHRGLYPNGHEASRMLKSHIGNSEMSLQRDEFIKIPCVQSEEQQKEIEDVERATLLGKDTTTSRKGSSQWLENIQERTGGVNHDVDFCIAQSLSILEQKIGVLTEIQKKLKLLRADLHVKSKVE', 670, 'Q95LT1; Q8WNT8;', 'KD01239', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'KIF2B', '#Kinesin-like protein KIF2B', '-', '-', '-'),
(1240, 'Q6FSC7', 'Spindle pole body component KRE28', 'GO:0000777', 42323, 'Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.', 'MEAQLHELQEEITRSSDLVLTEQDKRLQGTLREIDQSIRKLIETSDYLKLSGDADSLIDIKQLEVKSRELDSLMDLLRKLYWREESLDLFLKYTINSDAEQVPVFSDTDPKYQSLQDEVSHLRDDVMTVKNQEIDQITGEILQVAHEITEKQDQVNMLYLETTNELDKCWELLDEWQRLQDDQRITKNEDNSNRKDTELNAMEECYEEWKTLEELAVLNDNLQKQIDELEKVDNKAINSTQLAEESIVNTVQLNDLIDMWKRRIIASIHEDISEIVLYPYSRKLQLRVANRYTIIIQLDKHQTHDGKSTIHDIDLFTEQDSRIIPMRELRKQVLQECKGHSNILQALKNIINRVINNDN', 359, 'Q6FSC7;', 'KD01240', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '2888670'),
(1241, 'Q6NWW5', 'Kinesin-like protein KIF24', 'GO:0003777', 150207, 'Microtubule-dependent motor protein that acts as a negative regulator of ciliogenesis by mediating recruitment of CCP110 to mother centriole in cycling cells; leading to restrict nucleation of cilia at centrioles. Mediates depolymerization of microtubules of centriolar origin; possibly to suppress aberrant cilia formation (By similarity). {ECO:0000250}.', 'MASWLYECLCEAELAQYYPHFTALGLQKIDELAKVTMKDYSRLGVHDMNDRKRLFQLIKIIKIMQEEDKALGIPEHPLQASSLYTKPREFRSGPRRQLHFDSPSASKDKMANNETGSLSNFSVDEQKSTYLKVLEHMLPDDSQCQTKIRAPDASAADASMQTETNAPLFSSNYFSPQLGNCDIPVIQRVSHVSGYNYGIPHSCVRQITSENPWTEMEKIRVCVRKRPLGVREVRRGEVNVITVEDKETLLVHEKKEAVDLTQYILQHVFYFDEVFGEACSNQDVYLKTAHPLIQHIFNGGSATCFAYGQTGAGKTYTMIGTHQNPGLYALAAKDIFRQLKVSQSRRNLFVWISFYEIYCGQLYDLLNRRKRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAKRTFGRISFIDLAGSERAADARDSDRQTKMEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHIATEHTLNTLRYADRVKELKKGVKCCASATSQNQTSANASPKRIQSSPVTLPGDKCSPKKVKLGLQQSLTVAPGPTKVKAHPLASHVPNVPFTSGPKTPGKKSSSRGSPTPEWDMKASPRKGTTRSGHSIKKGAESAPLCSEKSQIGSKIAVGWEGRASDPGEGLLRVRLPTRGKKVQPVQPVQKQLLSRPRLLANSHHLEATQDSKVGTPAGLAPEAWTNPILQQKEREEHLRFYHQQFQQPPLLKQKLNYQPLQRLLCQHRPSEGRLQSETGFPLHSNPENRDGAQAEDLDDSDFSEDSFSHGSSQPAMKQGSTALERSGSSFFLHQDREHSPEEQAAERQQCLLFSSETDGSKKRPADSWVYSRDPIISHRRGALSQSHSPSMVCPDWSKEEDSASSGPSPKDNRAQKPSSSQVDFVHHQKPGEAQVSDIRLEAFTSEVPEQAEGSLSSPSPENGLSFPLSHVAVSGSPDQRDRVCTPLREVSENRVTHTPGRVNSSTPFQEDSGEQIQMCSANASGLMAPLTMSLLETPCHEDLSSLEQIAQDGAGYGFMAEIVGGPAAGHTVPSYDQEAALPVSSATECLWLSSSPPDNRPSGDLPALSPSPIHQHSPDKLPGREAYQTRRPILLPENHMGSKLYDDRAEETELGGSLTFPRKPSSNIHAGVPYSTPFLTSCTGSSNGVGRPWAQERKHPTGVSCQELVSSTDSNKPHYNEDIAWLRHRPISRCLDSDSPVVPSCSSKALRTYCPLTPEQAQQVIIRAHKEQLDEMAELDLKEETLMTQMDSNDFEDFVTQLDEIMALKSRCIQSLRSQLQLYLTSHRPAAAPERTVVS', 1356, 'Q6NWW5; A2BGK6; Q8BUI2; Q99PT7;', 'KD01241', 'Mus musculus (Mouse)', 'Kif24', '#Kinesin-like protein KIF24', '-', '-', '109242'),
(1242, 'Q754G5', 'Actin-related protein 4', 'GO:0051382', 53866, '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}.', 'MSNSALQVYGGDEITAVVIDPGSFTTNIGYSGTDCPQAILPSCYGKYTEGEKDELFSEQSIGLPRKDYEIHNIVQNGEVVDWEKAEKQWDWAIRSELRFETNSGMPALLTEPIWNSEENRKKSLEVLLESMDFSACYLVPTATAVSFAMGRPTCLVVDIGHDVTSVCPVVDGMTLSKSSMRSYIAGSLLNELIRSQLAPRKVIPLFQVAQRRPVFMERKFDYEIHPSLQKFVNERQFFQEFKETMLQVAPTSISKFKSEIETTSKRSIEAPWGEELVYDSLQRLEFAEQLFTPDLSQFPEDWPISKDGVVETWHNDYVPLKRNKPGTNVKDKEGTLDATPVPDENSVTSADQPNDNGKRNLEETTPDQKNEVSGLADLIYSSIMSTDVDLRTTLSHNVVITGGTSSLPGLMDRISAELNRSLPALKFRMLTSGQLRERQYQGWLGGSILASLGTFHQLWVGKQEYAEVGADRLLKDRFR', 479, 'Q754G5;', 'KD01242', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'ARP4', '#Actin-related protein 4#Actin-like protein ARP4#Actin-like protein 4', '-', '-', '4621895'),
(1243, 'O55131', 'Septin-7', 'GO:0000777', 50550, '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}.', 'MSVSARSAAAEERSVNCGTMAQPKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEEEKANWEAQQRILEQQNSSRTLEKNKKKGKIF', 436, 'O55131;', 'KD01243', 'Mus musculus (Mouse)', 'Sept7', '#Septin-7#CDC10 protein homolog', '-', '-', '235072'),
(1244, 'Q6BLH9', 'DASH complex subunit DAD3', 'GO:0008608===GO:0042729', 16100, '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}.', 'MLLSPIEAQILSQYQLLAVQLNTLSSEVKQLNSTTNQNSRPSGKSSSSEDGVEATNSGSADKLLDNLRNLEMKIGLVYTLFKGAVYSLFLQYEEDQNLKNDEEQRRNDDSDEEPQNHHEIDAIEGENNDDMGDRMESQENHGH', 143, 'Q6BLH9;', 'KD01244', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'DAD3', '#DASH complex subunit DAD3#Outer kinetochore protein DAD3', '-', '-', '2903561'),
(1245, 'Q6BPZ9', 'Probable kinetochore protein NDC80', 'GO:0000777', 76023, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MNVDYPMNNIPQASSLLRKNNGKRLSMASAARTSLLGNLNLNGTSGGASGRNSNIIDSSSLSMGNTGKRRSLLSTPASINRRRQSSLLQAPMSSSQMSSQSQQASQQTQAPFNQDQRPLRDKNYQTLIQQEIYDFLLANKFELEMNHPLTFKTLKQPTQKDFVVIFQFLYNKIDPYYRFTKSIETEVFLLLKILNYPYLDGINRSQISAVGGQNWPNFLGMLYWLVKLNLSVLNLNSKVDLISPDDEFDKIFINYITQSYRAFIDERDDYSEYYDEMKSRFDELNNNIIQDIENISNENNELLNQYNELNGQLDILENSEKKSKALENDLIKFKAYIETMESRKSKWSEILNKITQEIGNCEVELNNIESVKRDYEAQIGQQGLTPNDIDNLNTERDKLSKSIDLISNSLEDLKDVYHNKQINLQKNYQSLENFLKQYNNLIYKIQLKNHNYDYNFEINFRNNTIINETPDLLKPNEIINKNLKDEKIQLLNYKSIINTNVHMHQDEQIKLQEQIDLISELIMERREEIETLEAKLTANKSTYDEIYETMINDTTTYSMQIEKLERELRSIKINTNQGFIEVENKFQNIQIEYDELLYEIHSNRSILHDKIQKIIESTIGFKINIQSNLEDLENLAFDEFEKEDKKLNKN', 650, 'Q6BPZ9;', 'KD01245', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '2902791'),
(1246, 'P25694', 'Cell division control protein 48', 'GO:0031134', 91996, 'Involved in spindle disassembly; degradation of ubiquitinated proteins and protein export from the endoplasmic reticulum to the cytoplasm. Acts as a chaperone that collects ubiquitinated substrates. Has a role in the endoplasmic reticulum- associated degradation (ERAD) pathway. Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1. Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD (PubMed:11733065; PubMed:11740563; PubMed:11813000; PubMed:11847109; PubMed:21070972; PubMed:21148305). Component of the ribosome quality control complex (RQC); a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. CDC48 may provide the mechanical force that dislodges the polyubiquitinated nascent peptides from the exit channel (PubMed:23178123; PubMed:24261871). {ECO:0000269|PubMed:11733065; ECO:0000269|PubMed:11740563; ECO:0000269|PubMed:11813000; ECO:0000269|PubMed:11847109; ECO:0000269|PubMed:21070972; ECO:0000269|PubMed:21148305; ECO:0000269|PubMed:23178123; ECO:0000269|PubMed:24261871}.', 'MGEEHKPLLDASGVDPREEDKTATAILRRKKKDNMLLVDDAINDDNSVIAINSNTMDKLELFRGDTVLVKGKKRKDTVLIVLIDDELEDGACRINRVVRNNLRIRLGDLVTIHPCPDIKYATRISVLPIADTIEGITGNLFDVFLKPYFVEAYRPVRKGDHFVVRGGMRQVEFKVVDVEPEEYAVVAQDTIIHWEGEPINREDEENNMNEVGYDDIGGCRKQMAQIREMVELPLRHPQLFKAIGIKPPRGVLMYGPPGTGKTLMARAVANETGAFFFLINGPEVMSKMAGESESNLRKAFEEAEKNAPAIIFIDEIDSIAPKRDKTNGEVERRVVSQLLTLMDGMKARSNVVVIAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEVLRIHTKNMKLADDVDLEALAAETHGYVGADIASLCSEAAMQQIREKMDLIDLDEDEIDAEVLDSLGVTMDNFRFALGNSNPSALRETVVESVNVTWDDVGGLDEIKEELKETVEYPVLHPDQYTKFGLSPSKGVLFYGPPGTGKTLLAKAVATEVSANFISVKGPELLSMWYGESESNIRDIFDKARAAAPTVVFLDELDSIAKARGGSLGDAGGASDRVVNQLLTEMDGMNAKKNVFVIGATNRPDQIDPAILRPGRLDQLIYVPLPDENARLSILNAQLRKTPLEPGLELTAIAKATQGFSGADLLYIVQRAAKYAIKDSIEAHRQHEAEKEVKVEGEDVEMTDEGAKAEQEPEVDPVPYITKEHFAEAMKTAKRSVSDAELRRYEAYSQQMKASRGQFSNFNFNDAPLGTTATDNANSNNSAPSGAGAAFGSNAEEDDDLYS', 835, 'P25694; D6VRM4;', 'KD01246', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CDC48', '#Cell division control protein 48 {ECO:0000305|PubMed:6749598}#Cell division cycle protein 48 {ECO:0000303|PubMed:6749598}', '-', '-', '851431'),
(1247, 'O88485', 'Cytoplasmic dynein 1 intermediate chain 1', 'GO:0000776===GO:0000777===GO:0003777===GO:0005868', 70725, '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 chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores.', 'MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETEALLQSIGISPEPPLVPTPMSPSSKSVSTPSDAGSQDSGDLGPLTRTLQWDTDPSVLQLQSDSELGRRLHKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSEEDEEDEEMVEPKIGHDSELENQEKKQETKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYSNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNSDTEVPTASVAIEGASALNRVRWAQGGKEVAVGDSEGRIWIYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGAVELAA', 628, 'O88485; O88486; Q80W09;', 'KD01247', 'Mus musculus (Mouse)', 'Dync1i1', '#Cytoplasmic dynein 1 intermediate chain 1#Cytoplasmic dynein intermediate chain 1#Dynein intermediate chain 1; cytosolic#DH IC-1', '-', '-', '13426'),
(1248, 'O88487', 'Cytoplasmic dynein 1 intermediate chain 2', 'GO:0005868', 68394, '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 chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. Involved in membrane-transport; such as Golgi apparatus; late endosomes and lysosomes (By similarity). {ECO:0000250}.', 'MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAAVSVQEESDLEKKRREAEALLQSMGLTTDSPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQVDFPPREIVTYTKETQTPVTAQPKEDEEEEDDVATPKPPVEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEEAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA', 612, 'O88487; Q3TGH7;', 'KD01248', 'Mus musculus (Mouse)', 'Dync1i2', '#Cytoplasmic dynein 1 intermediate chain 2#Cytoplasmic dynein intermediate chain 2#Dynein intermediate chain 2; cytosolic#DH IC-2', '-', '-', '13427'),
(1249, 'P84051', 'Histone H2A', 'k', 13363, 'Core component of nucleosome. 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.', 'MSGRGKGGKVKGKAKSRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLSGVTIAQGGVLPNIQAVLLPKKTEKKA', 124, 'P84051; P02267; Q4ABC7;', 'KD01249', 'Drosophila melanogaster (Fruit fly)', 'His2A', '#Histone H2A', '-', '-', '318855'),
(1250, 'G5EE37', 'ICP-1; isoform aIncenp-like protein ICP-1', 'k', 69920, '', 'MPPKKRAVSRKPAEPTIKLFSSIPKISSIFDEVSEAHDDAAAKVFADLYKRMSSITEELATPQFSAEQLLNAVLKPGRIDAEFVELISRQKAKPAQPSSSSHRGDDDMETDEVETDQAGPITPRAGSVATDGDFEEDILPVTLKRMQQMSISKKKTEGSISRNAAYSGTPRRNPPREAHNQATPRNIFSSTPGRMAGTPGRAAVVPRTPHRVIPFNDAEKDPNARMKHADELRMKELEKKREKARKDEEKRNAVMERRKEQERVRQEKLDQLKQKEERNANLAKLHNSAKSPTRARLMQDHAPNKAASRKIFPTAESTSTPGRGPAKKGKVEILIGSDGQKTAPVAQPTVELSPSRELQRNGSRQVKMEPMSCDDSTPPARQHKPKAKATKRSAHAASSSTSNVEAAAALAALQEQQRIQLEQEQYLLQLAEDERRKREQKEMKEKAEKERQLRAREEQEHFLAVQREEQAQLEKQREREEAELQATLARCAEKQARQEALRKTPPPAAYEMTPPRTYQNNSKNDYGLNDLNSDDETDQEDDPRKDVPAWAEFAVVRENVRRHAINPPFDVAQFFGSIGKPNLKEIFSDAVKVKKRGSSAVWKKSPSTLNTSSRTILQDISE', 622, 'G5EE37;', 'KD01250', 'Caenorhabditis elegans', 'icp-1', '#ICP-1; isoform a {ECO:0000313|EMBL:CCD69912.1}#Incenp-like protein ICP-1 {ECO:0000313|EMBL:AAG24400.1}', '-', '-', '171788'),
(1251, 'Q9VEH1', 'Altered disjunction; isoform ALD04521p', 'c;k', 69753, '', 'MTTPVPRRTKDMMALGLDSDSEDDFNTPYRPRQAAAGERKQQPVASFQVQTRGKENEPHPLPINMLPRRVSELTMMDSDSDEEDIKSNHNLNCAILNDSFVLSPSQELTNSNSNITTRRTPSAAPLKQSDSNLSFLGRFNDMGINCSSQGSPVANSEKQVAKKTAPTLQAAPSATERRPLQETETPLRNELPSTSKTKPDADFITPQVRTIGSTLAGKSRSAVSNDFRAQKVLFQTPMTVSRAAPVASDSISFSLCDTITESPDIPEPPKKAEPPKSQHPSKKSLDHVFRESDKDNVPDKVDNVEPKELVSIPAVAVPPEQPSHKTSNILKIKNHEYTIDKKLGCGGSSSVFLARRSDSGNEFALKVVDLQADPQVVQGYLNETKLLAKLQGNVCVVALYDYQLVREESKLYMVMEKGDCDLNKILQSYTTNLPLYSLMNILYQMLQAVNYIHQHGVIHSDLKPANFLMVSGRLKLIDFGIASNIAVDSTSIIKFSQAGTFNYISPEALTDTSTGNSPMRRADQPKIKISTKSDVWSLGCILYLLLYQKTPFGHIRNVYAKMSAITTPGTSIEYPAIPPYYPIMLVHMAKNCLQLNPKKRPSCTELLQYPFHMIIPLQNLQIPSRTANSN', 630, 'Q9VEH1;', 'KD01251', 'Drosophila melanogaster (Fruit fly)', 'ald', '#Altered disjunction; isoform A {ECO:0000313|EMBL:AAF55450.1}#2.7.11.- {ECO:0000313|EMBL:AAF55450.1}#LD04521p {ECO:0000313|EMBL:AAQ22555.1}', '-', '-', '42126'),
(1252, 'Q17695', 'SPDL-1', 'k', 55285, '', 'MPDDEEKLQLLADVERLKKILRQKDEMLEEMEDDLKNQGKPCSSKLSLEERAQELSEQLRDLHVEMDGKNATILDRDALIDSLRSEIDKLEKINKEFANGSVIPEHDDSNSFGESEMLRISEDCQKYKETATALYERNAELEKEAVNLKDEIESMMDHIRDLKNHMETRDEEIARLEGELFDERNSHEGKLAARGNSMFSEVIDAERKVEEDLKVLHGENRALKGMVKRLRMEVEEVEERLRSSTKRFNVTRMTTSDIDVKEMRRLRDRVCHLETERVHLWERMFIKMRSIPKREVGALITGYFKSFELSIASVKGGFDGLMKDNEKYVTIIRGLQQEVENLKADIVQLQFDNKCAHRKAAPVVNKDFEHPLLAAPLKTLNNGRPSFFIKPKNVEPMPQLGHSLSSIAVTPQKPAAKFTTRSSIKDDTSEWAERRMKAQAEKKLATPTPRYNYIKLSEPVPKFKPAVLQMPSTSETKEN', 479, 'Q17695;', 'KD01252', 'Caenorhabditis elegans', 'spdl-1', '#SPDL-1 {ECO:0000313|EMBL:CCD61463.1}', '-', '-', '174256'),
(1253, 'Q7SZ10', 'Serine/threonine-protein phosphatase PP1-gamma catalytic subunit B', 'GO:0000777', 36938, 'Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division; and participates in the regulation of glycogen metabolism; muscle contractility and protein synthesis (By similarity). Promotes nuclear envelope reassembly by targeting nuclear membrane vesicles to chromatin at the end of mitosis. Acts by dephosphorylating membrane proteins such as lamin B receptor (lbr) to regulate the binding of membrane proteins to chromatin (By similarity). {ECO:0000250}.', 'MADVDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNASRPVTPPRGIITKQAKK', 323, 'Q7SZ10; A4PB28;', 'KD01253', 'Xenopus laevis (African clawed frog)', 'ppp1cc-b', '#Serine/threonine-protein phosphatase PP1-gamma catalytic subunit B#PP-1G-B#Protein phosphatase 1 zeta {ECO:0000303|PubMed:17448463}#xPP1-zeta {ECO:0000303|PubMed:17448463}#3.1.3.16', '-', '-', '380598'),
(1254, 'E3QDN5', 'Tethering factor for nuclear proteasome STS1', 'GO:0061638', 33980, '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}.', 'MNVLLSPQPPLFQHPHETNRISPSRSLSPFHNMSTSRKRKADEDGDEMSMSPRSSPAASSRQLQRPSKKVRSNELVGRPLTLPRLLETLDPTALRTVLERICERHPDIGQEVVNSAPRPTVAAAHGVLQEYQDKMKAAIPYGETSPDYTYYRVKAPMTALIDALLDFTPQYLPPNETQTTVSLQYMDGATKIIHALPDWEPQQYRHHKENAYDEISKAWALVINEAAKRGGGLSLHTGGWDQTLAKHHEISGGRMGTAMNAMATSVSWMAHGGSSNGQQPGNPSSDQNSILNQLMSGTYGAPVRVGPW', 308, 'E3QDN5;', 'KD01254', 'Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maizanthracnose fungus) (Glomerella graminicola)', 'STS1', '#Tethering factor for nuclear proteasome STS1', '-', '-', '-'),
(1255, 'Q8SPS9', 'Dynein light chain Tctex-type 3', 'GO:0000777===GO:0005868', 13081, '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. Probably binds BUB3 as part of transport cargo. Required for the efficient progression through mitosis (By similarity). {ECO:0000250}.', 'MEEYHRHCDEVGFNADEAHNIVKECIDGVLGGEDYNQNNINQWTASIVEQSLTHLVKLGKAYKYIVTCAVVQRSAYGFHTASSCFWDTTSDGTCTVRWENRTMNCIVNVFAIAIVL', 116, 'Q8SPS9;', 'KD01255', 'Canis familiaris (Dog) (Canis lupus familiaris)', 'DYNLT3', '#Dynein light chain Tctex-type 3#T-complex-associated testis-expressed 1-like', '-', '-', '403505'),
(1256, 'Q29MB2', 'Kinesin-like protein GA13060', 'GO:0003777', 124349, '', 'MASSISRNGGFCGALQRAPPPMPPGLARRLSSRECYGVGKVKVMLRVSDRAPDKDSPLDPEFMALDKKKRQVTLTDPRNVCPPPQAAQERGPMVAAPKMFAFDNLFTAEDKQSDVCASALSEVIPAVLEGSDGCLLAMGYPSTGQPHTVLGGDVATGAGAGAATGTGTGTGSVAACSLGAAPCAIAWLYKGIQERRQKSGARFSVRVSAVGVSATKPDALSTDLLISHAAESDDSPGIYLRDDFLGGPTELRAPTAERAALFLDSALAGRLKSSGSTSTPAGGGPAPLESALIFTLHVYQYSLSRKGGVAGGRSRLHIIDLGGCANRSGGLPLSGIGNILLAILSGQRHPPHKDHPLTPLLKDCLAPITCHVAIVAHVLHEQSYQDALSTIQIASRIHRLRRRKHRVPMPLAVGLAQGLSGGGGSSAGSGADPSSSEISADTVIYMGPNDDATDGEHPPVYLPSLSAGDNRAIMSKALKGSGLEKPPTQMKAGLSSPMMMKKAMAAAGEKVKKLPGNSPMGSLKRQAAAGACSSPLVPHEQQQQQQQIAHGSPIPIPRHMVSKGSNVPSPKGSPLRRAHAGAHPGAALEQLEAGMRKITEEQWIDGPRVSRAKVAEARHLMREVNHVKQCETWVDGPKSLSCRSLTAGNLPAAGAQTQGYGFMDSHKKTMIRQWVETQTSQVFQSPATVSASNSPTALHWKLSQLKQKSLDLPERPAFPPEQQSMDLPQQCFESQPLLGQDMSLPPDGDEDQDSGPSEVPPALPLFDDPLGSRDISHDSLHRMLSRHVSREQLHEADLVASRASSSHHQHQHHRPSSQRSIDCGLQVTEEEIARTMAREQEHSMHPLSALSHCDNLSFVSSFNMACESFSECGERARHQFDQLARLHEIFTSQLAMAEVTPSAALFRTDVSSVFSEPVFRFNVGQSSVCSEPAYRLTPSPPKQPSHSPSQGSLPSLNGIMEIAGMDDYALLRQPDGASDPSLPKSEKRFAPQHDDICELDEKAMAAAVGKRNSLEDAQHKLNEITNILPLAAQSRLPLLPLNTSSEAYDSGHDSNSTPRTSKHSGISRRAESGYHSVATVRDSDESSFASGMSKGQRHRITISGGGGGGCGAGGGGSATGNYQRHSHGVGGHKKHRHRHEGNGGGNKGLCNWLLTPFSCTYPETEGEISDF', 1171, 'Q29MB2;', 'KD01256', 'Drosophila pseudoobscura pseudoobscura (Fruit fly)', 'GA13060', '#Kinesin-like protein GA13060', '-', '-', '4817387');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1257, 'Q9H1A4', 'Anaphase-promoting complex subunit 1', 'c;k', 216500, '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:18485873}.', 'MSNFYEERTTMIAARDLQEFVPFGRDHCKHHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHEKQKESWQLRKGVSEIGEDVDYDEELYVAGNMVIWSKGSKSQALAVYKAFTVDSPVQQALWCDFIISQDKSEKAYSSNEVEKCICILQSSCINMHSIEGKDYIASLPFQVANVWPTKYGLLFERSASSHEVPPGSPREPLPTMFSMLHPLDEITPLVCKSGSLFGSSRVQYVVDHAMKIVFLNTDPSIVMTYDAVQNVHSVWTLRRVKSEEENVVLKFSEQGGTPQNVATSSSLTAHLRSLSKGDSPVTSPFQNYSSIHSQSRSTSSPSLHSRSPSISNMAALSRAHSPALGVHSFSGVQRFNISSHNQSPKRHSISHSPNSNSNGSFLAPETEPIVPELCIDHLWTETITNIREKNSQASKVFITSDLCGQKFLCFLVESQLQLRCVKFQESNDKTQLIFGSVTNIPAKDAAPVEKIDTMLVLEGSGNLVLYTGVVRVGKVFIPGLPAPSLTMSNTMPRPSTPLDGVSTPKPLSKLLGSLDEVVLLSPVPELRDSSKLHDSLYNEDCTFQQLGTYIHSIRDPVHNRVTLELSNGSMVRITIPEIATSELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELKLNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKGEGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWMTNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSKQACEGNLPKGKSVLSSDVPSGTETEEEDDGMNDMNHEVMSLIWSEDLRVQDVRRLLQSAHPVRVNVVQYPELSDHEFIEEKENRLLQLCQRTMALPVGRGMFTLFSYHPVPTEPLPIPKLNLTGRAPPRNTTVDLNSGNIDVPPNMTSWASFHNGVAAGLKIAPASQIDSAWIVYNKPKHAELANEYAGFLMALGLNGHLTKLATLNIHDYLTKGHEMTSIGLLLGVSAAKLGTMDMSITRLLSIHIPALLPPTSTELDVPHNVQVAAVVGIGLVYQGTAHRHTAEVLLAEIGRPPGPEMEYCTDRESYSLAAGLALGMVCLGHGSNLIGMSDLNVPEQLYQYMVGGHRRFQTGMHREKHKSPSYQIKEGDTINVDVTCPGATLALAMIYLKTNNRSIADWLRAPDTMYLLDFVKPEFLLLRTLARCLILWDDILPNSKWVDSNVPQIIRENSISLSEIELPCSEDLNLETLSQAHVYIIAGACLSLGFRFAGSENLSAFNCLHKFAKDFMTYLSAPNASVTGPHNLETCLSVVLLSLAMVMAGSGNLKVLQLCRFLHMKTGGEMNYGFHLAHHMALGLLFLGGGRYSLSTSNSSIAALLCALYPHFPAHSTDNRYHLQALRHLYVLAAEPRLLVPVDVDTNTPCYALLEVTYKGTQWYEQTKEELMAPTLLPELHLLKQIKVKGPRYWELLIDLSKGTQHLKSILSKDGVLYVKLRAGQLSYKEDPMGWQSLLAQTVANRNSEARAFKPETISAFTSDPALLSFAEYFCKPTVNMGQKQEILDLFSSVLYECVTQETPEMLPAYIAMDQAIRRLGRREMSETSELWQIKLVLEFFSSRSHQERLQNHPKRGLFMNSEFLPVVKCTIDNTLDQWLQVGGDMCVHAYLSGQPLEESQLSMLACFLVYHSVPAPQHLPPIGLEGSTSFAELLFKFKQLKMPVRALLRLAPLLLGNPQPMVM', 1944, 'Q9H1A4; Q2M3H8; Q9BSE6; Q9H8D0;', 'KD01257', 'Homo sapiens (Human)', 'ANAPC1', '#Anaphase-promoting complex subunit 1#APC1#Cyclosome subunit 1#Mitotic checkpoint regulator#Testis-specific gene 24 protein', 'BIOMD0000000186,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Dissociation variant;BIOMD0000000187,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Convey variant;', 'ENSG00000153107', '-'),
(1258, 'Q68G30', 'Kinesin light chain 3', 'GO:0003777', 55655, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.', 'MSVQVAAPGSTGLGPERLNPEELVRQTRQVVQGLEALRAEHHSLAGHLAEALAGPGPVAGVELLEEKQQVVNHSLEAIELGLGEAQVLLALSAHVGVLEAEKQRLRAQARRLAQENTWLREELEETQRRLRASEEAVAQLEEEKSHLQFLGQLRQYDPPEESQRPDSPPRRDSLASLFPSEEEEKKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFQDVERHYARALSIYEALGGPQDPNVAKTKNNLASAYLKQNKYQQAEELYKEILSQEALPAPLGAPQGGTAGEAQQQVLRRSSSFSKLRESIRRGSEKLVSRLRGESMAGAAGMKRAMSLNMLNVDGPRAARMQLSTQHLNEASRTLSASTQDLSPR', 505, 'Q68G30; Q9ESH7;', 'KD01258', 'Rattus norvegicus (Rat)', 'Klc3', '#Kinesin light chain 3#Kinesin light chain KLCt', '-', '-', '171549'),
(1259, 'Q7Z7K6', 'Centromere protein V', 'GO:0000776===GO:0000777===GO:0034508===k', 29946, 'Required for distribution of pericentromeric heterochromatin in interphase nuclei and for centromere formation and organization; chromosome alignment and cytokinesis. {ECO:0000269|PubMed:18772885}.', 'MRRSRSSAAAKLRGQKRSGASGASAAPAASAAAALAPSATRTRRSASQAGSKSQAVEKPPSEKPRLRRSSPRAQEEGPGEPPPPELALLPPPPPPPPTPATPTSSASNLDLGEQRERWETFQKRQKLTSEGAAKLLLDTFEYQGLVKHTGGCHCGAVRFEVWASADLHIFDCNCSICKKKQNRHFIVPASRFKLLKGAEHITTYTFNTHKAQHTFCKRCGVQSFYTPRSNPGGFGIAPHCLDEGTVRSMVTEEFNGSDWEKAMKEHKTIKNMSKE', 275, 'Q7Z7K6; B2RPK2; Q3L8N5; Q8NFH6;', 'KD01259', 'Homo sapiens (Human)', 'CENPV', '#Centromere protein V#CENP-V#Nuclear protein p30#Proline-rich protein 6', '-', 'ENSG00000166582', '-'),
(1260, 'A6ZZB9', 'Spindle pole body component KRE28', 'GO:0000777', 44674, 'Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1; BIK1 and SLK19) and motors (CIN8; KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.', 'MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKILSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQETGHNFAEKQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQRLTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDMQYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEANSKFNNKYRNNTKVQIFEVMDDIISELTNE', 385, 'A6ZZB9;', 'KD01260', 'Saccharomyces cerevisiae (strain YJM789) (Baker''s yeast)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '-'),
(1261, 'Q8CJF7', 'Protein ELYS', 'GO:0000777', 247646, '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 (By similarity). Has also been proposed to function as a transcription factor which may play a specific role in hematopoietic tissues (PubMed:11952839). {ECO:0000250; ECO:0000269|PubMed:11952839}.', 'MQDLTAQVTSDLLHFPEVTIEALGEDEITLESVLRGKFAAGKNGLACLACGPQLEVVNSLTGERLSAYRFSGVNEQPPVVLAVKEFSWHKRTGLLIGLEEADGSVLCLYDLGISRVVKAVVLPGRVTAIEPIINHGGASASTQHLHPSLRWLFGVAAVVTDVGQILLIDLCLDDLSCSQNEVEASDLEVITGIPAEVPHIRERVMREGRHLCFQLVSPLGVAISTLSYINRTNQLAVGFSDGYLALWNMKSMKREYYTQLEGGRVPVHAVAFQEPENDPRNCCYLWAVQSTQDSEGDVLSLHLLQLAFGDRKCLASGQILYEGLEYCEERYTLDLAGGTFPLRGQTSNTKLLGCQSIERFPSHGDREESMREALSPDTSVSVFTWQVNIYGQGKPSVYLGLFDINRWYHAQMPDSLRSGESLHNCSYFALWSLDSVVSRTSPHHILDILVHERSLNRGVPPSYPPPEQFFNPSTFNFDATCLLDSGVIHVTCAGFQKETLTFLKKSGPTLNEVIPDSYNRCLVAGLLSPRLIDIQPSSLSQEEQLEAILSAAIQTSSLGLLTGYIRTWIIEEQPNSAANLRFVLEWTWNKVVLTKEEFDRLCVPLFDGSCRFIDPQTIQSIQQCHLLLSNLSTVLSCFAMEAQGITERGLVDLSNKHMVTQLLCQYAHMVLWFCHSGLLPEGLDDALQLSRLRYNYPVIQNYYTSRRQKSERSPRGKWNHDCLMIDGLVSQLGDEVEKLWKRDEGGTGRYPPASIHALLDIYLLDNITEASKHAITIYLLLDIMYSFPNKTDTPIESFPTAFAISWGQVKLVQGFWLLDHNDYENGLDLLFHPVTAKPASWQHSKIIEAFMSQGEHKQALRYLQTMKPTVSSSNEVILHLTVLLFNRCMVEAWNLLRQNSNRVNIEELLKHAYEVCQEMGLMEDLLKLPFTNTEQECLVKFLQSSTSVENHEFLLVHHLQRANYISALKLNQILKNNLMSDRDPRLRERSVTRNSILDQYGKILPRVQRKLAVERAKPYHLSTSSVFHEVSRPKPLSAFPKKAITGTVLTRSTFISNVLSKIGEVWASHEPRNGVSLFNSPKTEQPSPVVHSFPHPELPEAFVGTPISNTSQRISRLLDLVVHPVPQPSQCLEFIQQSPTRSPLCLLSSSLPLSSQFKRPHQNTSRPSELLLLETPLIVKKAKSLALSATSSGFAEFTPPSILRSGFRTTPLASPSLSPGRSLTPPFRVKETRISFMEEGMNTHWTDRATDDRNTKAFVSTSFHKCGLPAETEWMKTSDKNTYFPLDVPAKGPQKVVAESLATHSGRLEKLDVSKEDSTASTRSDQTSLEYHDAPSPEDLEGAVFVSPKPASSSTELTTNSTLQTERDNDKDAFKSEGAPSPVKKQIGTGDAAVEAFSELSRLDPVERAEASFAVSSVCEGETSTSNSKTSVLDGIVPIESRTSILTADHKESVANTVADVESSGSTSSKCPVTSERSLGQKLTLNLKEDEIEAHVPKENVGLPEESPRISAAPSDTHEIHLIGCENLEVQNSEEEAKNLSFDELYPLGAEKLEYNLSTIEQQFCDLPDDKDSAECDAAEVDGELFVAQSNFTLILEGEEGEAEASDSAAPNMLPKATKEKPVCHREPHNQERVTDLPSAVTADQESHKVETLPYVPEPVKVAIAENLLDVIKDTRSKEATPVAAGEAGDEDGAVIVSKAAHSSRLTNSTPKTVKEPHAETVNTSQNDDMVSSRTLTRRQHALSLNVTSEQEPSAVATPKKRTRKIKETPESSERTCSDLKVAPENQLTAQSPPAPRRGKKKDVSQGTLPSSGAVEPEPEPQGTPGRLRLRTQPPEPAAEETPSRTKVRLSSVRKGTPRRLKKSVENGQSTEILDDLKGSEAASHDGTVTELRNANLEDTQNMEYKQDEHSDQQLPLKRKRVREREVSVSSVTEEPKLDSSQLPLQTGLDVPATPRKRGRPRKVVPLEADGGTTGKEQTSPQKKDVPVVRRSTRNTPARNVSTLEKSVLVPNKEAALVVTSKRRPTKKSAEESSKDPSAAVSDLAGGAAHTESADRRDGLLAAAALTPSAQGTRTRSRRTMLLTDISEPKTEPLFPPPSVKVPKKKSKAENMEAAAQLKELVSDLSSQFVVSPPALRTRQKSISNTSKLLGELESDPKPLEIIEQKPKRSRTVKTRASRNTGKGSSWSPPPVEIKLVSPLASPVDEIKTGKPRKTAEIAGKTLGRGRKKPSSFPKQILRRKML', 2243, 'Q8CJF7; B2RRC8; Q8BVJ5; Q8VD55;', 'KD01261', 'Mus musculus (Mouse)', 'Ahctf1', '#Protein ELYS#Embryonic large molecule derived from yolk sac#Protein MEL-28#Putative AT-hook-containing transcription factor 1', '-', '-', '226747'),
(1262, 'Q07139', 'Protein ECT2', 'GO:0051988', 103131, 'Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases; like RHOA; RHOC; RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)- induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells; thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269|PubMed:17904126; ECO:0000269|PubMed:21350944}.', 'MADDSVLPSPSEITSLADSSVFDSKVAEMSKENLCLASTSNVDEEMPQVEARVIMVQDAGKQEELLKALKTIKIMEVPVIKIKESCPGKSEEKLIKSIINMEMKVPCVKMDSMEEFESLDSPEFENIFVVTDFQNSVFNDLYKADCRIVGPPVILNCAQRGEPLPFSCRPLYCTSMLNLVLCFTGFRKKEELVKLVTLVHHMGGVIRKECNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQCFCAAVDDFRNEFKVPPFQDCILSFLGFSDEEKHSMEEMTEMQGGSYLPVGDERCTHLIVEENTVKDLPFEPSKKLFVVKQEWFWGSIQMDARAGETMYLYEKANTPELKKSVSLLSLSTPNSNRKRRRLKETLAQLSRETDLSPFPPRKRPSAEHSLSIGSLLDISNTPESSIHYGETPKSCAKSSRSSTPVPPKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRGGPILAPEEIKTIFGSIPDIFDVHMKIKDDLEDLIANWDESRSIGDIFLKYAKDLVKTYPPFVNFFEMSKEMIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETVSLGEHPCDRGEQVTLFLFNDCLEIARKRHKVIGTFRSPHDRTRPPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSEELPKESWLKMLCRHVANTICKADAENLMYVADPESFEVNTKDMDSTLSRASRAIKKTSKKVTRAFSFSKTPKRALRMALSSSHSSEGRSPPSSGKLAVSRLSSTSSLAGIPSPSLVSLPSFFERRSHTLSRSTTHLI', 913, 'Q07139; Q3TZP2; Q5DTR8; Q80VE4; Q8CIH2; Q8K2A0; Q8R3E2;', 'KD01262', 'Mus musculus (Mouse)', 'Ect2', '#Protein ECT2#Epithelial cell-transforming sequence 2 oncogene', '-', '-', '13605'),
(1263, 'P06400', 'Retinoblastoma-associated protein', 'GO:0031134', 106159, 'Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated; active form of RB1 interacts with E2F1 and represses its transcription activity; leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and; in particular; that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1; SUV420H1 and SUV420H2; leading to epigenetic transcriptional repression. Controls histone H4 ''Lys-20'' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. 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 (By similarity). In case of viral infections; interactions with SV40 large T antigen; HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1''s activity. {ECO:0000250; ECO:0000269|PubMed:15084261}.', 'MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK', 928, 'P06400; A8K5E3; P78499; Q5VW46; Q8IZL4;', 'KD01263', 'Homo sapiens (Human)', 'RB1', '#Retinoblastoma-associated protein#p105-Rb#pRb#Rb#pp110', 'BIOMD0000000109,Haberichter2007_cellcycle;BIOMD0000000168,Obeyesekere1999_CellCycle;BIOMD0000000208,Deineko2003_CellCycle;BIOMD0000000228,Swat2004_Mammalian_G1_S_Transition;BIOMD0000000265,Conradie2010_RPControl_CellCycle;BIOMD0000000318,Yao2008_Rb_E2F_Switch;', 'ENSG00000139687', '-'),
(1264, 'Q9Y5N6', 'Origin recognition complex subunit 6', 'k;m', 28107, 'Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre- replication complex necessary to initiate DNA replication. Does not bind histone H3 and H4 trimethylation marks H3K9me3; H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655}.', 'MGSELIGRLAPRLGLAEPDMLRKAEEYLRLSRVKCVGLSARTTETSSAVMCLDLAASWMKCPLDRAYLIKLSGLNKETYQSCLKSFECLLGLNSNIGIRDLAVQFSCIEAVNMASKILKSYESSLPQTQQVDLDLSRPLFTSAALLSACKILKLKVDKNKMVATSGVKKAIFDRLCKQLEKIGQQVDREPGDVATPPRKRKKIVVEAPAKEMEKVEEMPHKPQKDEDLTQDYEEWKRKILENAASAQKATAE', 252, 'Q9Y5N6; B3KN89;', 'KD01264', 'Homo sapiens (Human)', 'ORC6', '#Origin recognition complex subunit 6', '-', 'ENSG00000091651', '-'),
(1265, 'Q02880', 'DNA topoisomerase 2-beta', 'k', 183267, 'Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. {ECO:0000269|PubMed:10684600}.', 'MAKSGGCGAGAGVGGGNGALTWVTLFDQNNAAKKEESETANKNDSSKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQFMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCRGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEDETQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPSDLWKEDLAAFVEELDKVESQEREDVLAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIIPEITAMKADASKKLLKKKKGDLDTAAVKVEFDEEFSGAPVEGAGEEALTPSVPINKGPKPKREKKEPGTRVRKTPTSSGKPSAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDADDDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYTFSPGKSKATPEKSLHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDSASVFSPSFGLKQTDKVPSKTVAAKKGKPSSDTVPKPKRAPKQKKVVEAVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKTSKTTSKKPKKTSFDQDSDVDIFPSDFPTEPPSLPRTGRARKEVKYFAESDEEEDDVDFAMFN', 1626, 'Q02880; Q13600; Q9UMG8; Q9UQP8;', 'KD01265', 'Homo sapiens (Human)', 'TOP2B', '#DNA topoisomerase 2-beta#5.99.1.3#DNA topoisomerase II; beta isozyme', '-', 'ENSG00000077097', '-'),
(1266, 'Q96FJ2', 'Dynein light chain 2; cytoplasmic', 'c;k;m', 10350, '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. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}.', 'MSDRKAVIKNADMSEDMQQDAVDCATQAMEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG', 89, 'Q96FJ2; B2R5B4;', 'KD01266', 'Homo sapiens (Human)', 'DYNLL2', '#Dynein light chain 2; cytoplasmic#8 kDa dynein light chain b#DLC8b#Dynein light chain LC8-type 2', '-', 'ENSG00000264364', '-'),
(1267, 'O55165', 'Kinesin-like protein KIF3C', 'GO:0003777', 89816, 'Microtubule-based anterograde translocator for membranous organelles.', 'MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQARAVGSTHMNEVSSRSHAIFVITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNTPGGPATQSTAGGGGGGGGTSGSGSSGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKKGMLGKRPRRKSSRRKKAVSAPAGYPEGAVIEAWVAEEEDDNNNNHRPPQPTLEAALEKNMENYLQEQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEDLKREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMLLRDEETMELRGTYSSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHEEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWKFQPLVPAGVNNSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAIFEMEFSHDQEQDPRVLHMERLMRLDSFLERPSTSKVRKSRSWCQSPQRPPPPSTVHASMASAPLHPATVVDHD', 796, 'O55165; O88657;', 'KD01267', 'Rattus norvegicus (Rat)', 'Kif3c', '#Kinesin-like protein KIF3C', '-', '-', '85248'),
(1268, 'Q05826', 'CCAAT/enhancer-binding protein beta', 'GO:0000779', 35030, 'Important transcriptional activator 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''. Functions in brown adipose tissue (BAT) differentiation. Regulates the transcriptional induction of peroxisome proliferator-activated receptor gamma (PPARG). Binds to the MGF and MIM-1 promoters and activates the transcription of these genes. {ECO:0000269|PubMed:8467792}.', 'MQRLVAWDAACLPIQPPAFKSMEVANFYYEADCLAALNKLHPRAAGGRSMTELTVGDHERAIDFSPYLDPLAASQQPAQPPPPAAAAGGNFEPACSSGGQDFLSDLFAEDYKGSGGGKKPDYTYISLTRHGHPCGSQSHKPGVLPGCFPPQIVETKVEPVFETLDSCKGPRKEEGGAGPGPGGMSSPYGSTVRSYLGYQSVPSGSSGNLSTSSSSSPPGTPNPSESSKSAAGAGGYSGPPAGKNKPKKCVDKHSDEYKLRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSPRC', 328, 'Q05826; Q540C6;', 'KD01268', 'Gallus gallus (Chicken)', 'CEBPB', '#CCAAT/enhancer-binding protein beta#C/EBP beta#Transcription factor NF-M#CCR protein', '-', '-', '396185'),
(1269, 'O13067', 'Condensin complex subunit 2', 'k', 77778, 'Regulatory subunit 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 topoisomerase. {ECO:0000269|PubMed:10428035; ECO:0000269|PubMed:9774278}.', 'MSTSTPQSGGRRKPETPDSAFLSPATRPQPISAAATPTLLNFTSNDDERERKLRRMSRVIDLQLSNANSPATAISPAQSRGADTPTSLLPKLNNTQISDHYSTCIKLSQENKITTKNAFGLHLIDYMGDILKHKDSELTNFKVAAGTLDASAKIYAVRVDAVHADVYKVLGGLGKESQATEDTENQETDTGPQDGRKNPKRRKCSYKTIERNLNSINRSETERKSEIDPLFQKAAASFDEFSTAGVFLSTLKCHSYHSELHFDADVKPLSTAEETEPPSPGSMDSTELKSLFLQCVEKRPLCPSLSGFRFMQWNSDAQNENLSLLMDKFKKSDHVFDINAEVEDDFVESEAPVADEFDADVCEGMDAGDIGEFAEHREACRLERKGAQLTQIGNGDIGTMCLQLSSCPGEYSYFSPRTMSMWAGPEHWRFRPRQKASTDSDQQRVKKAKKVFELNFEDDIDFEVHFRKTRAATTLTKSTLESQNKKSTTLPADFHYDPDNIARMSLRPKDRIRKTTVQESVSEPEDDIGDYDYNNPNDTSNFCPALQAADSDDDDGAFLGPESNSAGFSAENQMNITSYGESNLVAGQKVNKIEIQYAKTAKKMDMKRLKSSMWSLLANCPESQEEMPSSKEEIDAALITDEQVFSSVTHGLQKRLPPVMAQNLSVPLAFACLLHLANEKNLKLQGMDDLSDVMIMQDD', 699, 'O13067;', 'KD01269', 'Xenopus laevis (African clawed frog)', 'ncaph', '#Condensin complex subunit 2#Barren homolog#Chromosome assembly protein xCAP-H#Chromosome-associated protein H#Non-SMC condensin I complex subunit H', '-', '-', '398069'),
(1270, 'P87227', 'Inner centromere protein mis6', 'GO:0051382===GO:0034501===GO:0000941===GO:0000779===GO:0000780===k', 78513, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. Has a role in the maintenance of core chromatin structure and kinetochore function. Located in the inner regions of the centromeres and is essential for sister chromatid segregation during the G1/S phase following mitosis. Required for the localization of cnp1 to the centromere. {ECO:0000269|PubMed:10864871; ECO:0000269|PubMed:16079914}.', 'MESFENKGFLDIEEGIQWIKKNSENLSSSKKTILARLQQFHKLCSEVGLNQHSISSLLDVILSKKTHFDKNHVQLLIKCLYPNELISQTIAIRIISSLDPHGLRCSYAIQAKLLNWLIHVYEFLDGNNLLCRYYGVLFHFLDFLTLRPYISNLLVLLTKHYHVKSFRIHQLLALYQKPGNTADPYLLALILTYKQHFPDVIVGSYTYRKHGSVRLDSEWIAATKAILNRQSEDVPLETWSSEKRKRQSSLIPDLITMKNTSSSYSLEELTSVQQMGLVYEKIVFPSRIAAVLKSKLFLIFLFLKNKNVYYSRLDEWLHITLNYGLALRSGSNNQEEEVLHLLYKYLLFSPKFPKSLLQYVITFFSKPNITEENYNLLTLLVTHIPITTDSSYFNSLLKEFEQFILQKNAEFCSKHLNILWLWLFRMLNLRIASMGNNHTLLEKCLLITNHATFLVSHFSWDVSLAYQLSRLFQLYYKILTKIRKQIEPNIPPKELIYVLFFQPSAFYINSMVGLLLLTKNYQERLMDSRIDAISKFTHSYLKSLSEIILLKEKRAILSFLQLWEPFKSDYSQFLPIATRIANDHPYAQRVFSLTCAPQFFSYINGYQIYLQQTNPATGSIPLKPIQEETFGAFQSNLHLSDSWEDFQKNFIIYLKKKGYLAISDFLLSTLNR', 672, 'P87227;', 'KD01270', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis6', '#Inner centromere protein mis6#Sim4 complex subunit mis6', '-', '-', '2542304'),
(1271, 'A2APB8', 'Targeting protein for Xklp2', 'GO:0005818', 85894, 'Spindle assembly factor. Required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophosphorylation and protects the phosphorylated residue against dephosphorylation (By similarity). {ECO:0000250}.', 'MSQVPTTYSFDAPTDFINFSSLDAEEDTENIDSWFDEKANLENKFLRQRGIGEPFQGKNSLRKAKLQQGFVTPLKAVDNTYHKETEKENLQKQSIPSNDCSSLDAKRAVSGNTPVQPQRRSIRLSAQKDLEQKEKNHVASVEMKAKRCVAPATDCPPQKRMKVSHKKKLEEEEEGSAPATSRKNERETLEKAKGKHTVPGVPPAREKVLKSTEEQEIEKRLRMQQEVVELRRKNEEFKKLALAGPGQPVKKSTSQVTKTVDFHFLTDERIKQHPKNQEEYKEVNFMSELRKHSSTPARGTRGCTIIKPFNLSKGKKRTFDEAASTYVPIAQQVEAFHKRTPNRYHLRNKKDESLLPSKSVNKIARDPQTPILQTKYRTRAVTCKSTAEQEAEELEKLQQYKFKARELDPRIFESGPILPKRAPVKPPTQPVGFDLEIEKRIHERESKKKTEDEQFEFHSRPCPTKILEDVVGVPEKKVIPATVPKSPVFALKNRIRVPIKDEEEEKPVVIKAQPVPHYGVPYKPHIAEARNVEVCPFSFDTRDKERQLQKEKKIKEMQKGEVPKFKALPVPHFDTINLPEKKVKNVTQAEPFSLETDKRGAYKAEMWKHQLEEEQKQQKDAACFKARPNTVIFQEPFVPKKEKKSLAENPSGSLVQEPFQLATERRAKERQELEKKMAEVEAWKLQQLEEVRQQEEEQQKEELARLRKELVHKANPIRKYAAVEVKSSELPLTVPVSPKFSTRFQ', 745, 'A2APB8; Q3U500; Q6P9S6;', 'KD01271', 'Mus musculus (Mouse)', 'Tpx2', '#Targeting protein for Xklp2', '-', '-', '72119'),
(1272, 'Q6CV05', 'Spindle pole body component KRE28', 'GO:0000777', 41058, 'Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity). {ECO:0000250}.', 'MTHYHSEYYSEVEKFEYQVTHVTEQILQEQDRLRGSTLHEYNQTILQLVSDYEMFNSNGQCDPSEINLPLEKLESWTNSLKQIHLELESIDNFLRYAIPSDQTILNLSKFNESKYETLQAEVSELRDINVVQLQKEIESLQQQITTKSDENLLISEKIKESCLEASQDIDQCWKLLEQLEAYENANPSTEVITTTDPAFSTYNQWKWNQLAESELKHINQQLITLRATKEKLDKVFSKRSELETSPKSIETFTSYQLLSQLWRSKFIRQLLPDIANLEVYPQSGKLKFEVGIMQVIMQIESGIIKSVSLFSYELSYDRIETIKEDILGRIEHQKSLFKVLVVITDYIVNSL', 351, 'Q6CV05;', 'KD01272', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '2892376'),
(1273, 'P48467', 'Kinesin heavy chain', 'GO:0003777', 102411, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Its motor activity is directed toward the microtubule''s plus end.', 'MSSSANSIKVVARFRPQNRVEIESGGQPIVTFQGPDTCTVDSKEAQGSFTFDRVFDMSCKQSDIFDFSIKPTVDDILNGYNGTVFAYGQTGAGKSYTMMGTSIDDPDGRGVIPRIVEQIFTSILSSAANIEYTVRVSYMEIYMERIRDLLAPQNDNLPVHEEKNRGVYVKGLLEIYVSSVQEVYEVMRRGGNARAVAATNMNQESSRSHSIFVITITQKNVETGSAKSGQLFLVDLAGSEKVGKTGASGQTLEEAKKINKSLSALGMVINALTDGKSSHVPYRDSKLTRILQESLGGNSRTTLIINCSPSSYNDAETLSTLRFGMRAKSIKNKAKVNAELSPAELKQMLAKAKTQITSFENYIVNLESEVQVWRGGETVPKEKWVPPLELAITPSKSASTTARPSTPSRLLPESRAETPAISDRAGTPSLPLDKDEREEFLRRENELQDQIAEKESIAAAAERQLRETKEELIALKDHDSKLGKENERLISESNEFKMQLERLAFENKEAQITIDGLKDANSELTAELDEVKQQMLDMKMSAKETSAVLDEKEKKKAEKMAKMMAGFDLSGDVFSDNERAVADAIAQLDALFEISSAGDAIPPEDIKALREKLVETQGFVRQAELSSFSAASSDAEARKRAELEARLEALQQEHEELLSRNLTEADKEEVKALLAKSLSDKSAVQVELVEQLKADIALKNSETEHLKALVDDLQRRVKAGGAGVAMANGKTVQQQLAEFDVMKKSLMRDLQNRCERVVELEISLDETREQYNNVLRSSNNRAQQKKMAFLERNLEQLTQVQRQLVEQNSALKKEVAIAERKLMARNERIQSLESLLQESQEKMAQANHKFEVQLAAVKDRLEAAKAGSTRGLGTDAGLGGFSIGSRIAKPLRGGGDAVAGATATNPTIATLQQNPPENKRSSWFFQKS', 928, 'P48467; Q7RVK5;', 'KD01273', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'kin', '#Kinesin heavy chain', '-', '-', '3880594'),
(1274, 'Q7S9H0', 'Probable kinetochore protein nuf2', 'GO:0000778===GO:0051455===GO:0031617===GO:0031262', 53827, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MAFNPRMSILPPQPQQSRQRKKEEEAAYANMRLPDREIVGCINELGIPFTLADLQKPNPIQVQMIFEWFGELLMNKTRQTVDPAMRAAAEDVCGPELGEAMMPSDTRNLLGFYVSLRRLMLDCGVNDFSFNDLYKPTHDRLVRMLSYVINFVRFRESQTSVIDEHCNKAEQTKARIEQLYVENQNMEAQLEEMRHNRRAMEVLVQEKTVRNEELKKRLLELRRSQEKVAARLEEAKTKKGELAAELEEKTATKIALKQESAKLRPYVLQSPSALQASLAELSNTLNNDKAHIDALDRRSRALQTSTDSFSVVASDVASCIKLLEEIAIELAKEEEENVKNARQRDALTERGHNVREVERTEALLKRQLAKWVDRTAQLRTQSEEKAQKAMEKMEELRAVHRKLTEERSEKGKDIERRRVRIEQTEKKMLDLKENIENEVHAAHDEYLKMEAHIKLYITEMEQAI', 464, 'Q7S9H0;', 'KD01274', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'kpr-2', '#Probable kinetochore protein nuf2#Kinetochore protein 2', '-', '-', '3878398'),
(1275, 'Q7Z3K3', 'Pogo transposable element with ZNF domain', 'GO:0051382', 155344, 'Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms. {ECO:0000269|PubMed:20562864}.', 'MADTDLFMECEEEELEPWQKISDVIEDSVVEDYNSVDKTTTVSVSQQPVSAPVPIAAHASVAGHLSTSTTVSSSGAQNSDSTKKTLVTLIANNNAGNPLVQQGGQPLILTQNPAPGLGTMVTQPVLRPVQVMQNANHVTSSPVASQPIFITTQGFPVRNVRPVQNAMNQVGIVLNVQQGQTVRPITLVPAPGTQFVKPTVGVPQVFSQMTPVRPGSTMPVRPTTNTFTTVIPATLTIRSTVPQSQSQQTKSTPSTSTTPTATQPTSLGQLAVQSPGQSNQTTNPKLAPSFPSPPAVSIASFVTVKRPGVTGENSNEVAKLVNTLNTIPSLGQSPGPVVVSNNSSAHGSQRTSGPESSMKVTSSIPVFDLQDGGRKICPRCNAQFRVTEALRGHMCYCCPEMVEYQKKGKSLDSEPSVPSAAKPPSPEKTAPVASTPSSTPIPALSPPTKVPEPNENVGDAVQTKLIMLVDDFYYGRDGGKVAQLTNFPKVATSFRCPHCTKRLKNNIRFMNHMKHHVELDQQNGEVDGHTICQHCYRQFSTPFQLQCHLENVHSPYESTTKCKICEWAFESEPLFLQHMKDTHKPGEMPYVCQVCQYRSSLYSEVDVHFRMIHEDTRHLLCPYCLKVFKNGNAFQQHYMRHQKRNVYHCNKCRLQFLFAKDKIEHKLQHHKTFRKPKQLEGLKPGTKVTIRASRGQPRTVPVSSNDTPPSALQEAAPLTSSMDPLPVFLYPPVQRSIQKRAVRKMSVMGRQTCLECSFEIPDFPNHFPTYVHCSLCRYSTCCSRAYANHMINNHVPRKSPKYLALFKNSVSGIKLACTSCTFVTSVGDAMAKHLVFNPSHRSSSILPRGLTWIAHSRHGQTRDRVHDRNVKNMYPPPSFPTNKAATVKSAGATPAEPEELLTPLAPALPSPASTATPPPTPTHPQALALPPLATEGAECLNVDDQDEGSPVTQEPELASGGGGSGGVGKKEQLSVKKLRVVLFALCCNTEQAAEHFRNPQRRIRRWLRRFQASQGENLEGKYLSFEAEEKLAEWVLTQREQQLPVNEETLFQKATKIGRSLEGGFKISYEWAVRFMLRHHLTPHARRAVAHTLPKDVAENAGLFIDFVQRQIHNQDLPLSMIVAIDEISLFLDTEVLSSDDRKENALQTVGTGEPWCDVVLAILADGTVLPTLVFYRGQMDQPANMPDSILLEAKESGYSDDEIMELWSTRVWQKHTACQRSKGMLVMDCHRTHLSEEVLAMLSASSTLPAVVPAGCSSKIQPLDVCIKRTVKNFLHKKWKEQAREMADTACDSDVLLQLVLVWLGEVLGVIGDCPELVQRSFLVASVLPGPDGNINSPTRNADMQEELIASLEEQLKLSGEHSESSTPRPRSSPEETIEPESLHQLFEGESETESFYGFEEADLDLMEI', 1410, 'Q7Z3K3; B4DTP8; B4DYL9; B7ZBY5; E9PM80; O75049; Q3LIC4; Q5SZS1;Q5SZS2; Q5SZS3; Q5SZS4; Q8TDZ7; Q9Y4X7;', 'KD01275', 'Homo sapiens (Human)', 'POGZ', '#Pogo transposable element with ZNF domain#Suppressor of hairy wing homolog 5#Zinc finger protein 280E#Zinc finger protein 635', '-', 'ENSG00000143442', '-'),
(1276, 'O94328', 'Meiotically up-regulated gene 118 protein', 'GO:0000778===GO:0032133', 16181, 'Has a role in meiosis. {ECO:0000269|PubMed:16303567}.', 'MMNKRKRVEELGETKHRQVRQRILQEHKNDILENLAFELSDKVRRLRSNASLLASTIRMRGEMRIAAIPRAQRNMHLRDLKNHLSCNVSATPWRTKIKEFYNLDELSSQKSARQPTKTVASSSSSSSKSTTVSKSSSKSQV', 141, 'O94328;', 'KD01276', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mug118', '#Meiotically up-regulated gene 118 protein', '-', '-', '2541173'),
(1277, 'P40541', 'Cohesin subunit SCC3', 'k', 133009, '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 MCD1/SCC1 subunit of 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.', 'MTAVRRSTRIRTKSQVIEEDYDDEQNTSAQHVESDKITAKTQHEEEEEQDTGESEESSSEDDYEDQDDDDYVDTATAKRKSRKRKPKSASNTSSKRQKKKPTSAQKSAVSHAPAYHRSKKDQDQYLEIAKDFQPTELFDILSTSEDVSIEELLREWLETYSENRDKFLQEFINLLLNCCGSVARVEDHDVHSNESSNETIGEIQLLFQRQKLHEFYLLISKENKKRKNFKMGPLYQNFAEFMTKLLEVANDLQLLYVESDEDDTQIVTGNLVLDLLTWLSSFSVCKIRCFRYISTLTLYLFQDYLTQQAVNLEKNYLAKLSKQLSLEEKKKRPNNKTLEKLESTIAETQGSKVVIDSIIDNIVKLCFVHRYKDVSDLIRSESMLHLSIWIKNYPEYFLKVTFLKYFGWLLSDNSVSVRLQVTKILPHLIIQNHNSKSTDNSAIRQVFERFKTKILEVAIRDVNLDVRIHSIQVLTEASSLGYLDDSEILIISSLMFDEEFDPFKTSSFNKRSKFLSTVAKFLARVIKEKFDEFIKTHEDLPKEVDGLEVGPVVQVGIFIKILNDSLIYHLKDCAEVDSRTKIRMLTQAAEFLSPYISTHLKTICNLLISDTESNELIQKLQNSANNNSDDEDVDDEELDITPLFPIDRNSTILYLNVFHGLCAGANNPKIQTKDSVKEIVLPLFYDLLNAASIESADILCPLLESFITFSLDDWISIGYETELKKITDKTIKAFMDSTIGNSKVDMKYDIFAKFIHHIHHFEKKELQEKFLNQIATLKIHLKKFLQEKMDPNNSRDDYKDLTCSLYELYINKLTILGRDYPIEVDEELLQLFLNNFVSRIPIMFQDFDDSTAQEINFKMLVLLATWNLEKWREIIEKVRDYENSISKDLRSVWKPIAAIIGRLNTLVISLAATNETFENINSLFYLKWSACTSLMDIIVAIKIFELKLPADATTWRYSMSEQFPFYLHDNASKVLLKIFLYLESLFAKQVDVQLERVADEDANLNDLPETGFFENIETEFLLFTVKLKGLMKLNILDERFASRVALNKEKLGPLFKKIVDDTIMENPEPNKKNIQKAKSNQTQREKAPLQPNSERETDHANTENNDPDIPMTIDLEPIEESSQNNSELAPIEEHPTVVDAIDNSDEITQD', 1150, 'P40541; D6VVQ4; Q02511;', 'KD01277', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'IRR1', '#Cohesin subunit SCC3#Irregular cell behavior protein 1', '-', '-', '854786'),
(1278, 'G5EE67', 'SKR-3', 'k', 18979, '', 'MSDADSQKQIKLTSSDDKTFTVSRKVISQSKTITDIIQNLGIEESGSTSEDTIPLQKVTSTILEKIITWCEHHADDEPKKVDENKKTVDISEWDAEFMKVDQGTLFEIILAANYLDIRGLLDVTTQNVANMMKGKTPSQIRTLFNIENDFSEEEREAMKKENAWCED', 167, 'G5EE67;', 'KD01278', 'Caenorhabditis elegans', 'skr-3', '#SKR-3 {ECO:0000313|EMBL:CAB05516.1}', '-', '-', '180081'),
(1279, 'P53148', 'Spindle pole body component SPC105', 'GO:0034501===GO:0000778===GO:0031134===c;k', 104826, 'Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1; BIK1 and SLK19) and motors (CIN8; KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint. {ECO:0000269|PubMed:19893618}.', 'MNVDERSRIGGREKDAGPGKGILKQNQSSQMTSSFLENPGVRIPTRIITKKEVLDGSNTTSRINTSNLQSMVKRRVSFAPDVTLHSFTFVPEQNNEIKEPRRRKTSTNSPTKISSQEEPLVTSTQIDDARTEEKTAAEEDPDTSGMELTEPIVATPDSNKASQHDPTSMEMTEVFPRSIRQKNPDVEGESIESSQQIDDVEAVREETMELTAIHNVHDYDSISKDTVEGEPIDLTEYESKPYVPNSVSRSTGKSSDYSVERSNDKSDLSKSENKTNSSQPMEITDIFHADPQNPMSLHSDNNINNDGNEMELTQIQTNFDRDNHHIDESPSEKHAFSSNKRRKLDTVSDYAASVTTPVKEAKDTSGEDNDGDLEMMEKMSPITFSDVDNKIGTRSNDVFTIEPGTEDTGMQTATDDEEDGENVDDNGNKIVEKTRLPEIDKEGQSGIALPTQDYTLREFINEVGVGFLDTKLIDDLDKKVNFPLNSFNFVENQRIDNVFSAFYIDIPILEVEAFRCKELWRSINESKDKFKDFEAQIDKSHPPLLLQEYFSSDEKMKQLMRDQLQLVKGYSKLEAAMEWYEWRKKQLNGLELILAENLNTLKREYEKLNEEVEKVNSIRGKIRKLNEAIKEEIRSLKNLPSDSYKPTLMNRIKIEAFKQELMEHSISLSSSNDFTQEMRSLKLAIAKKSNDILTLRSEVASIDKKIEKRKLFTRFDLPKLRDTLKILESLTGVRFLKFSKATLSIAFLQLDDLRVDINLANFKNNPLSSMKVMNDSNNDDMSYHLFTMLLKNVEAEHQDSMLSNLFFAMKKWRPLLKYIKLLKLLFPVKITQTEEEEALLQFKDYDRRNKTAFFYVISLVSFAQGVFSENGQIPMKVHISTQQDYSPSREVLSDRITHKISGVLPSFTKSRIHLEFT', 917, 'P53148; D6VU52;', 'KD01279', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SPC105', '#Spindle pole body component SPC105#105 kDa spindle pole component protein', '-', '-', '852787'),
(1280, 'A6H750', 'Kinesin-like protein KIF2B', 'GO:0000777===GO:0003777', 76907, 'Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement during mitosis. Has microtubule depolymerization activity (By similarity). {ECO:0000250|UniProtKB:Q8N4N8}.', 'MASQLFRPLTPRLSSLTPVKPHFGHLQAGISVAIQRTDGRIHLAVVTEVRRDNAWVTVEWAEKGVKKGKKVALETIFLLNPALALAGPAAQGRASRSVSLAPPSVIGDQRTAARWAGKIPQRNETPSGDSLAVRVPSSPCLMTQRKSACLREIEKLQKQRERRRRLHREIRAQRARDADTGNAHYEIRRLIEECRRRLRGGRISGPEPRDGRRICVCVRKRPLNRQEATREDLDIVTIPSDNVVMVHESKQKVDLTRYLENQTFCFDHAFDDTASNELVYQFTDQPLVESIFRHGMATCFAYGQTGSGKTHTMGGGFSGRDQDCSKGIYAMVAQDVFLLLKTSAYEKLNLKVYGTFFEIYGGKVYDLLNWKKKLQVLEDGSQQIQVVGLQEQEVCCVEDMLNLVELGNSCRTSGQTSVNAHSSRSHAVFQIILKSRGKLHGKFSLVDLAGNERGADTAKANRKRQLEGAEINKSLLALKECIRALGQNKSHTPFRASKLTQVLRDSFIGQNSSTCMIATISPGMASCENTLNTLRYANRVKEITLNLRPRHRCLYPAEREMPRVLENHIRNSEMSLQGDEFIRIPCLQSEEEKETEGIKVLSSPLVDTTISWKEASQWPDNKIQDTSDEVNCNVDFCIAQLLSILEKKIDILTEIRRKLKLLQADIQKENRHGEVNGERSDLK', 683, 'A6H750;', 'KD01280', 'Bos taurus (Bovine)', 'KIF2B', '#Kinesin-like protein KIF2B', '-', '-', '538921'),
(1281, 'P60953', 'Cell division control protein 42 homolog', 'GO:0051988===k', 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. {ECO:0000269|PubMed:14978216; ECO:0000269|PubMed:15642749; ECO:0000269|PubMed:17038317}.', 'MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL', 191, 'P60953; P21181; P25763; Q7L8R5; Q9UDI2;', 'KD01281', 'Homo sapiens (Human)', 'CDC42', '#Cell division control protein 42 homolog#G25K GTP-binding protein', '-', 'ENSG00000230068', '-'),
(1282, 'P60952', '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 (By similarity). {ECO:0000250}.', 'MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL', 191, 'P60952; P21181; P25763;', 'KD01282', 'Canis familiaris (Dog) (Canis lupus familiaris)', 'CDC42', '#Cell division control protein 42 homolog#G25K GTP-binding protein', '-', '-', '403934'),
(1283, 'P41695', 'Checkpoint serine/threonine-protein kinase BUB1', 'GO:0000776===GO:0034501===GO:0000778===GO:0031134===GO:0034508===GO:0000780===k', 117868, 'Involved in cell cycle checkpoint enforcement. The formation of a MAD1-BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism. Catalyzes the phosphorylation of BUB3 and its autophosphorylation. Associates with centromere (CEN) DNA via interaction with SKP1. The association with SKP1 is required for the mitotic delay induced by kinetochore tension defects; but not for the arrest induced by spindle depolymerization or kinetochore assembly defects. {ECO:0000269|PubMed:12769845}.', 'MNLDLGSTVRGYESDKDTFPQSKGVSSSQKEQHSQLNQTKIAYEQRLLNDLEDMDDPLDLFLDYMIWISTSYIEVDSESGQEVLRSTMERCLIYIQDMETYRNDPRFLKIWIWYINLFLSNNFHESENTFKYMFNKGIGTKLSLFYEEFSKLLENAQFFLEAKVLLELGAENNCRPYNRLLRSLSNYEDRLREMNIVENQNSVPDSRERLKGRLIYRTAPFFIRKFLTSSLMTDDKENRANLNSNVGVGKSAPNVYQDSIVVADFKSETERLNLNSSKQPSNQRLKNGNKKTSIYADQKQSNNPVYKLINTPGRKPERIVFNFNLIYPENDEEFNTEEILAMIKGLYKVQRRGKKHTEDYTSDKNRKKRKLDVLVERRQDLPSSQPPVVPKSTRIEVFKDDDNPSQSTHHKNTQVQVQTTTSILPLKPVVDGNLAHETPVKPSLTSNASRSPTVTAFSKDAINEVFSMFNQHYSTPGALLDGDDTTTSKFNVFENFTQEFTAKNIEDLTEVKDPKQETVSQQTTSTNETNDRYERLSNSSTRPEKADYMTPIKETTETDVVPIIQTPKEQIRTEDKKSGDNTETQTQLTSTTIQSSPFLTQPEPQAEKLLQTAEHSEKSKEHYPTIIPPFTKIKNQPPVIIENPLSNNLRAKFLSEISPPLFQYNTFYNYNQELKMSSLLKKIHRVSRNENKNPIVDFKKTGDLYCIRGELGEGGYATVYLAESSQGHLRALKVEKPASVWEYYIMSQVEFRLRKSTILKSIINASALHLFLDESYLVLNYASQGTVLDLINLQREKAIDGNGIMDEYLCMFITVELMKVLEKIHEVGIIHGDLKPDNCMIRLEKPGEPLGAHYMRNGEDGWENKGIYLIDFGRSFDMTLLPPGTKFKSNWKADQQDCWEMRAGKPWSYEADYYGLAGVIHSMLFGKFIETIQLQNGRCKLKNPFKRYWKKEIWGVIFDLLLNSGQASNQALPMTEKIVEIRNLIESHLEQHAENHLRNVILSIEEELSHFQYKGKPSRRF', 1021, 'P41695; D6VUX1;', 'KD01283', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'BUB1', '#Checkpoint serine/threonine-protein kinase BUB1#2.7.11.1', '-', '-', '853100'),
(1284, 'Q61144', 'Presenilin-2', 'GO:0000776', 49983, '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}.', 'MLAFMASDSEEEVCDERTSLMSAESPTSRSCQEGRPGPEDGESTAQWRTQESEEDCEEDPDRYACSGAPGRPSGLEEELTLKYGAKRVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLFLAVWNFGAVGMVCIHWKGPLVLQQAYLIVISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEAFEAPLPGYPGEELEEEEERGVKLGLGDFIFYSVLVGKAAATGNGDWNTTLACFIAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI', 448, 'Q61144; O54977; P97934; P97935; Q91VS3; Q9D616;', 'KD01284', 'Mus musculus (Mouse)', 'Psen2', '#Presenilin-2#PS-2#3.4.23.-#Presenilin-2 NTF subunit#Presenilin-2 CTF subunit', '-', '-', '19165'),
(1285, 'Q95QB8', 'KBP-1', 'k', 17282, '', 'MTTPSPQEISTVTLNSLSKEERKKAILALQTKKNEIKLVIDEHQKKLAEFRQSIPDGCCEMFENEKKIRLKHSSTAELLPHLQKVGSSSVDKEKMINNIRQRVEVQVADQETFKSIEERNELLRRENENLKKEVNTVAAELLQEFESYE', 149, 'Q95QB8;', 'KD01285', 'Caenorhabditis elegans', 'kbp-1', '#KBP-1 {ECO:0000313|EMBL:CCD70172.1}', '-', '-', '-'),
(1286, 'Q4IEV4', 'Histone acetyltransferase ESA1', 'GO:0034508', 58095, '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}.', 'MAGGTPGGEPTVGSGEPRLKSLATPETIKTGCIAWVEKEGQPRRAEILSIKTTKSGKQFYCNFDNFNKRLDEWVPVIRLDFTREVEWPNPEKEKPKDPKAKKAPTVQSKKTQPSKKSQKRPSKREQSTTSEANTPHPWTDFVENQNRQKSASIGPDGDSQARASVDGGETPGGGDEMEVDERETEVKREPAEFSREVEIEKLRTSGSMTQNPTEVSRIRNISKVQFGRFDLYPWYFSPYPEIFSQEDVIFICEFCLSYYGDLKAFTRHRKKCTLQHPPGNELYRNEEISFFEIDGRRQRTWCRNLCLLSKMFLDHKTLYYDVDPFLFYVMTVRTEKGCHMVGYFSKEKESADGYNVACILTMPQYQRKGYGRLLIQFSYELSRIEGKLGSPEKPLSDLGLLSYRQYWSENILEFLMGYNERDEKVTIEAISTALAMTTQDVEHTLQALRMQVYHKSDHKIVIPEKLIEQREKTKLKRKRTVDPTKIQWKPPVFTASSRTWGW', 502, 'Q4IEV4; V6R4L8;', 'KD01286', 'Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084(Wheat head blight fungus) (Fusarium graminearum)', 'ESA1', '#Histone acetyltransferase ESA1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}', '-', '-', '2786341'),
(1287, 'O13862', 'Transcriptional activator protein rdp1', 'k', 51766, 'Acts as a DNA damage-response activator of rhp51. Binds to part of the DNA damage-responsive element (DRE); (5''- NG[GT]T[GA]-3''). {ECO:0000269|PubMed:11073995}.', 'MSEHSPEASSTYAQVTSNDELSSNKIYMNADQNNSRKKEMDGSLQNNGGRLQNVNPLGGNESMSAVATSAASSLPTAENGVSLNAASPTIHSNTPTVVSHPVMSGSELKGEESHNSPGTLNGTSVANASKQPNMPNATFRCDKCDMMFVKQSGLTNHKRTYHQVETVVIIGHRRYVWRRNENGRFQCVCGRQNWRRPVNFASHAKQCPSFLAMDPNNIPPEINKVSPHDDLRPLSDSRRRARRPHPSDTIPPGASMARSDPSQVPESNPSAAAAVAAAAVAAAANLTNGVNPPEVPRNLNSSLVDAAESLANVSQQQHHRHPFARQPDYSAHSIPRTAAPYAPSMNMFAQNGPNTSLLPTAMPSDVSISSSLQQQPIHPSYDSRFSKAPQGTDALAALGYGTPSSAATLCPLYRDTPAAIVSEKLHLRLANLRIAYCEDCREFISLNAALDHRRSHHQQNITGDLVHVYSDFLDFQNC', 478, 'O13862;', 'KD01287', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rdp1', '#Transcriptional activator protein rdp1#Rhp51-DRE-binding protein 1', '-', '-', '2542539'),
(1288, 'Q61J98', 'Protein CLASP-2', 'GO:0000777', 87466, 'Probable microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Required for the formation of mitotic and meiotic spindles. Specifically promotes the polymerization of kinetochore-bound microtubules. Also required for cytoplasmic streaming (By similarity). {ECO:0000250}.', 'MSRVVSRTVPGGACVVNKDDFLKSFNDVDKVSVSSLADAKSKFDQVIAILSKSQEDWNKRRTQLQIIRSIVINCEDVIGRDQLLGQLVRLADCLDLSVKDLRSQILREAAITCSFLFEKYGNDVHQIAERCLPTAFSQLAVSTKVMATSGATLTLFLVQYVQTKQIFTCLTTYSTSKDKNQRRQLCVLLEIVIEHWNDKLKKSILPQIMELIKSAISDADPETRAAGRKAFNKLDAIHSEEADKLFASVDANKQKMLRASDAASSSTSVNSERGSAPFRSKLSAGSVGGMRNVPNISSKFLAQRSASAIDTKQVTRMTTSVSRTPNTRPMTTRTLSKVDTSPGGSKFARPTVGTLGPRTTSNLRARGSVPTSQPGSRNGSPPRRPSTTGTLPMEMQRVKSNLGSSSFVSSLTPDQAESLQKAMNTAKESLGQPSRTEDDEFLLPKRKPKTPQKSAVDISRVEAVIRACVSTSANEKRDGIKMLSIIVSEPNLSQIELKNIGQVLNRLLGEATNPVVLESVASFVKAHHSRLSEWLKLGLGKMFAKKGSEMMPIMKKHIVTTINAILSSFDPALQLKATCELMCDPIHLLSPKARVALLEYLTDLLEKHMERGSPFNTKEVKATILKMFSWMSDQRNMQQIVPHGEKVLCGLFALNAADFSALFNDFNPDYREWAYRILQAHGHNQHAPAPESPSPVRDQQVRANISNTAAQIEDFVVARNFELSAEKSPTSRGMLTSGFKRTDAEPLRPLESDMNTQRMDDISINESFDRLKVRILETTGFYAAFKVDFQE', 791, 'Q61J98; A8X9V7;', 'KD01288', 'Caenorhabditis briggsae', 'cls-2', '#Protein CLASP-2', '-', '-', '-'),
(1289, 'Q9D9Z1', 'Small kinetochore-associated protein', 'GO:0000776===GO:0000777===GO:0051988', 34728, 'Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase. Promotes the metaphase-to-anaphase transition and is required for chromosome alignment; normal timing of sister chromatid segregation; and maintenance of spindle pole architecture. The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments. Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis; possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division. {ECO:0000250|UniProtKB:Q9Y448}.', 'MAAPEAEAQETAFRTTGPPTDSEPRPFPPSSRKFPFESAAADSNEDWAVAAEHYLKGSGENGGWEQPAPGVQPSHPATMASAKTVCDAQPHSMPSCGLPADTQTRATSKLPVKSKEADLLRHLHPGGPEPDVTKVTKSRRENGQVKAAETASRRNLRNSYKPFNKQKPEEELKDKNELLEAVNKQLHQKLTETQGELKDLTQKVELLEKFQDNCLALLESKGLNPGQETLASKQEPTTDHTDSMLLLETLKDELKVFNETAKKQMEELQALKVKLKLKEEESVQFLEQQTLCKDEASDFTIILEEMEQLLEM', 312, 'Q9D9Z1; Q8K2D9;', 'KD01289', 'Mus musculus (Mouse)', 'Knstrn', '#Small kinetochore-associated protein#SKAP#Kinetochore-localized astrin-binding protein#Kinastrin#Kinetochore-localized astrin/SPAG5-binding protein#TRAF4-associated factor 1', '-', '-', '51944'),
(1290, 'Q27IK6', 'Phragmoplast orienting kinesin 2', 'GO:0003777', 315062, 'Involved in the spatial control of cytokinesis by a proper phragmoplast guidance. {ECO:0000269|PubMed:16682350}.', 'MSKETKLSRRDSDNHDDEIENVPENLRASLLSLTSNDSLKNPKHECGSKIDRTPSKPRAKNPDPALPLRTPDKYRSAAAFSKNRFGWGDKCDSITNTTNAALLNTTPKTGRVVGRAYSETNSTQNTPTKSVSKPPGSCYRGKLDGTGTVRAGGYASLYKGLSSSSGQVSTVVNSVEVPHFSLKEDPSFWMDHNVQILIRVRPLNSMERSINGYNRCLKQESSQCVAWIGPPETRFQFDHVACETIDQETLFRVAGLPMVENCLSGYNSCIFAYGQTGSGKTYTMLGEVGDLEFKPSPNRGMMPRIFEFLFARIQAEEESRRDERLKYNCKCSFLEIYNEQITDLLEPSSTNLQLREDIKSGVYVENLTECEVQSVQDILGLITQGSLNRRVGATNMNRESSRSHSVFTCVIESRWEKDSTANMRFARLNLVDLAGSERQKTSGAEGDRLKEAASINKSLSTLGHVIMVLVDVANGKPRHIPYRDSRLTFLLQDSLGGNSKTMIIANASPSVSCAAETLNTLKFAQRAKLIQNNAVVNEDSNEDVLELRRQIRLLKEELSLLKRQNISRALSFGSATANFAESQVDSPSSVMHETGQQQAGNLLVYESGGCVRMSRKQLKSLEITLAGSLRREHVADASIKKLEAEIEHLNRLVRQREEDTRSTKMMLRFREDKIQRLESLLGNHISADSFLLEENNVLSEEIQLLQAKIDKNPELTRFALENIRLLDQLRRFQEFYEEGEREILLGEVSNLRNQLFQFLDENSDWQKHVDDGIEPQGASRMSKENCSLQEELKKTCYELEKCRSNLGSCLEENAKLSREINDLQAMVSDIRACTPDEHSSVNKQKALLGTQNFEPHETLACEQANYVEEIIKLQLDLDVQKIILDEERTLRGDTEAQAVRLKFDIEVLKDQLLLISKQQKNVYSELGETKSAVAALESQNIILIQEAVELRRIKENYFELLKKQELDIPAMKSKQCDEFKDNPAEDSEIDTKFKKMQASLEKAKRLNMLYKSDIASKACGDEEMDEVCKQAEAATAEVIVCLQNELEVLQKEVNDFQSKENVTEKQVEILETQMEELQDKLRDTTMDNEQLQEQLRGKDMELLIISNEMELLTSELEEILLNGNEGLTDACYQADLISGSLPDKRIWISEQVGGLIRTLSERELMIEDLESCLEDANKKRCDIESMLKSLKGAAIVMNEAHQREFEEKETDVLLLKSQLCTKTETILRLQEKLKMAERLIYEASDCATASLIIVNRYSEVTESHTFELKQKDFQVAESTGTILSLKQQVQDLEATCKEFRSKLLEEEKNASAMEQKLEEIEETSISAMKEKLSELKGGVSDLRSCITMCQEHDKYTEAENSLSSPAHCSEGQEPGRNVVVSSCIEKTPNNNHTESMRLSSKVSSERGKVIILLKQEMESALASLKEVQVEMANLKGEKEELKASEKRSLSNLNDLAAQICNLNTVMSNMEEQYEHKMEVTDHKLKTLEHEIAKMKIEADQEYVENLCILKKFEEAQGTIREADITVNELVIANEKMRFDLEKQKKRGISLVGEKKALVEKLQELESINVKENEKLAYLEKLFESSLMGIGNLVEELATVVRKLQDESSVALTGMAKDLSELKSWVSETNSARLFLEDIWSEIIMKDCAISVLHLCHMGILLETVTGINTENGLLQRGLCVSNSSIAGLRDNNLRLRRELEMFANLKGKLLTDIKNGFERISRNEEATNLLTTKLSSFDQKISGLQYQEDLMLQRSNSMGSQLDILLKEIDLSNGDLAETLLEQERHLNQKNDFFDTEVQLYLMDLCSKDVELLVLAQTAKEYSSCLAVVDRELLDHHVIVEDLKEKLIVSQVEGELKDQCLVDNKLETVSVKEELTEAQSKIKVLSSDLDRSVQKIAEIDEVNKDFGERVIFLESSITGLQQELAMKASELYSLEHSRSVTAEELDIKERDVQVYADIVSSLKKENVSLKNKFIHFGEDQFKALDVTRLSIAKCSHLTEDSKKLEKLTRDGMAISDKMLQLICENVDKASVFADTVQSLQIDVQELLSENLNLHDELLRKDDVLKGLSFDLSLLQESASNSRDKKDETKEIMVHVEALEKTLALKTFELEDAVSHAQMLEVRLQESKEITRNLEVDTEKARKCQEKLSAENKDIRAEAEDLLAEKCSLEEEMIQTKKVSESMEMELFNLRNALGQLNDTVAFTQRKLNDAIDERDNLQDEVLNLKEEFGKMKSEAKEMEARYIEAQQIAESRKTYADEREEEVKLLEGSVEELEYTINVLENKVNVVKDEAERQRLQREELEMELHTIRQQMESARNADEEMKRILDEKHMDLAQAKKHIEALERNTADQKTEITQLSEHISELNLHAEAQASEYMHKFKELEAMAEQVKPEIHVSQAIDSSLSKGSGKPRGSGSPFRCIGLGITQQMRSEKDEELAAARLRIEELETVVSTRQKEIFLLNSKLAKVDSMTHDINRVLLGVKQNVTNCASFLDSQQVLKIAEMLQHNSSDSRERDLEVSHLKQQLNEYNEKRQGWIEEIEGKQTELVTAQIKLEEHRQYQQLLKKENELLKKENFSHKIKVMELEGEVKKLSSHQNPEWRTRDQARIKEENNVLKLQLDELNLKLRRADVSVSRAKEELAFYRASSVKNPHSNFDKTHQLSTKLKETEEDRMQLAQELLSLCTSILKAAGVTGEDFTDINPEVAEEALEQLKTKLGLLESEVHHFRLKGKAKSRRSRNPERKMPSMPSPRRSWSQSPRSMSQVPFFSSLDR', 2771, 'Q27IK6; Q9LJ60;', 'KD01290', 'Arabidopsis thaliana (Mouse-ear cress)', 'POK2', '#Phragmoplast orienting kinesin 2#Kinesin POK2', '-', '-', '821439');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1291, 'Q27IK7', 'Phragmoplast orienting kinesin-1', 'GO:0003777', 233879, 'Involved in the spatial control of cytokinesis by a proper phragmoplast guidance. Localizes TAN to the cortical division sites (CDS) during cytokinesis via direct binding. {ECO:0000269|PubMed:16682350; ECO:0000269|PubMed:21172800}.', 'MSRNVPRIEMPESEENEFASLSLFSPSRPPLNSIPDPSQIQKANHLPHFDLVQKLEGTRAQHQRTLGPEKKFEVLEGRAGNSSDSNPKIVNRNGKSRSEPNSAQSTPTRNGARVSLGGGCATGARFLQSFGGRGRIPRGVSIAESVSFAETTPHFELNEDHSFWKDHNVQVLIRLRPLGTMERANQGYGKCLKQESPQTLVWLGHPEARFTFDHVASETISQEKLFRVAGLPMVENCLSGYNSCVFAYGQTGSGKTYTMMGEISEAEGSLGEDCGVTARIFEYLFSRIKMEEEERRDENLKFSCKCSFLEIYNEQITDLLEPSSTNLQLREDLGKGVYVENLVEHNVRTVSDVLKLLLQGATNRKIAATRMNSESSRSHSVFTCTIESLWEKDSLTRSRFARLNLVDLAGSERQKSSGAEGDRLKEAANINKSLSTLGLVIMSLVDLAHGKHRHVPYRDSRLTFLLQDSLGGNSKTMIIANVSPSLCSTNETLSTLKFAQRAKLIQNNAKVNEDASGDVTALQQEIRKLKVQLTSLLKNHDSCGALSDCISSLEESRYSGTCKVAGETRQDKCHCQVKNMNDNMIGALRREKIAESALQKSEAEIERIDCLVRDMEEDAKRIKIMLNLREEKVGEMEFCTSGSLMTKECLIEENKTLKGEIKLLRDSIDKNPELTRSALENTKLREQLQRYQKFYEHGEREALLAEVTGLRDQLLDVLEAKDESFSKHVMKENEMEKEFEDCRNMNSSLIRELDEIQAGLGRYLNFDQIQSNVVASSTRGAEQAETMPTISEIQEEVAISHSKNYDRGALVKTDEGIDRSILQFKLGKLMKDLEEARTLNCKYEKDHKSQLSQQEDIEVVREQVETETARTILELQEEVIALQSEFQRRICNLTEENQSIKDTITARESEIRALNQDWEKATLELTNFIVAGSKSIKNASTQIESIICSFPQVNAWIGDYVEKAAKNCIKKEETILLLQKSLEDARILVAEMNLKLNSLKGATIALNEFQLGGNAATTEEAFNLNNDVDRMSDEVDTLESNFKANQYSILKTERHAEAALAVTKWLSDSRDQHQMMEKVQDQSVKEFGTLSSISASLSAEGNADISLSRDGHLSDATYPKGDELSTSSSDFSNCRWQHDCALNVKCQGVSSSESDAQESNNKITSAALIAKNGSAHSVYCGEGRQSVEKPLTIMMGREETEYKCSKPLSSGVYMGLMQRMDPVRTFFDRFEEVNATMKEADLTICELVKANEKSNSVTEMWLQTHEELISKEKNLMDDLEQVKSILSACEEEKQVLLNQTHTTLADMENSVSLLEEYFQEMKRGVEETVEALFSHARLAGKELLQLISNSRPSLEQIASEFMEREFTMYATYQCHIGKLIDQILDQRKQVITPNLSGQETNQSVKINAIGYNAEDEVTKKQSREEIVTGLENDEVVQSHESLLYENLYLKKELERKEALFEGLLFDFRLLQESASNKRDIKNEMDELFDALCKVQLELELKASQVHELFVHNENLENCSIDLKTALFTSQSDLEQAKQRIQILAEQNDELRALVSDLCKEKAAAEEGLDEQRDLVNRLEKEILHLTTTAEKQLLSAVKSIKENLKKTSDEKDQIVDEICSLNNKLELAYAIADEKEAIAVEAHQESEASKIYAEQKEEEVKILEISVEELERTINILERRVYDMDEEVKRHRTTQDSLETELQALRQRLFRFENFTGTMVTTNESTEEYKSHISRSTGLQGAHSQIQVLQKEVAEQTKEIKQLKEYISEILLHSEAQSSAYQEKYKTLEVMIRDFKLEDSSSSAAETISHKTEKSSTRSRGSSSPFRCIVGLVQQMKLEKDQELTMARVRVEELESLLAVKQKEICTLNTRIAAADSMTHDVIRDLLGVKMDITSYAELIDQHQVQRVVEKAQQHAEEILSKEQEVMNLKRHIDYLFKDRESCMSELNKKDTDVLATQISLDQLQERVQLLSMQNEMLKNDKSNLLRKLAELDRTVHNAQASNHRVPQTTKDTASFKLADTDYTKRLENAQKLLSHANNELAKYRKTSNNHPSTRTQGQSSGTRYR', 2066, 'Q27IK7; Q9LUT5;', 'KD01291', 'Arabidopsis thaliana (Mouse-ear cress)', 'POK1', '#Phragmoplast orienting kinesin-1#Kinesin POK1', '-', '-', '820999'),
(1292, 'Q96FN5', 'Kinesin-like protein KIF12', 'GO:0003777', 70660, '', 'MEERGSPDGDLARSLEQGPEGPETPIQVVLRVRPMSAAELRRGQQSVLHCSGTRTLQGGPEVAFRFGAVLDAARTQEDVFRACGVRRLGELALRGFSCTVFTFGQTGSGKTYTLTGPPPQGEGVPVPPSLAGIMQRTFAWLLDRVQHLGAPVTLRASYLEIYNEQVRDLLSLGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSHALLTLYISRQTAQQMPSVDPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLDPQRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRPQAPKSPVAKQPQRLETEMLQLQEENRRLQFQLDQMDCKASGLSGARVAWAQRNLYGMLQEFMLENERLRKEKSQLQNSRDLAQNEQRILAQQVHALERRLLSACYHHQQGPGLTPPCPCLMAPAPPCHALPPLYSCPCCHICPLCRVPLAHWACLPGEHHLPQVLDPEASGGRPPSARPPPWAPPCSPGSAKCPRERSHSDWTQTRVLAEMLTEEEVVPSAPPLPVRPPKTSPGLRGGAGVPNLAQRLEALRDQIGSSLRRGRSQPPCSEGARSPGQVLPPH', 646, 'Q96FN5; Q5TBE0;', 'KD01292', 'Homo sapiens (Human)', 'KIF12', '#Kinesin-like protein KIF12', '-', 'ENSG00000136883', '-'),
(1293, 'Q8LNZ2', 'Kinesin-like protein NACK2', 'GO:0003777', 106521, 'Probable plus end-directed motor protein that functions in a MAP kinase signaling pathway (ANP3-MKK6-MPK4); which is essential for somatic cell cytokinesis; especially for the cell- plate formation and its expansion. May regulates the activity and the localization of ANP3; probably by association through the non- catalytic region of the kinase. Functionally redundant with NACK1 and essential to promote the progression of cytokinesis and for cellularization (formation of the cell plate) during microgametogenesis and megagametogenesis. {ECO:0000269|PubMed:12694597; ECO:0000269|PubMed:15569152; ECO:0000269|PubMed:19825582; ECO:0000269|PubMed:20802223; ECO:0000269|PubMed:21575092; ECO:0000269|PubMed:9217006; ECO:0000269|PubMed:9224679}.', 'MMGPPRTPLSKIDKSNPYTPCGSKVTEEKILVTVRMRPLNWREHAKYDLIAWECPDDETIVFKNPNPDKAPTKYSFDKVFEPTCATQEVYEGGSRDVALSALAGTNATIFAYGQTSSGKTFTMRGVTESVVKDIYEHIRKTQERSFVLKVSALEIYNETVVDLLNRDTGPLRLLDDPEKGTIVENLVEEVVESRQHLQHLISICEDQRQVGETALNDKSSRSHQIIRLTIHSSLREIAGCVQSFMATLNLVDLAGSERAFQTNADGLRLKEGSHINRSLLTLTTVIRKLSSGRKRDHVPYRDSKLTRILQNSLGGNARTAIICTISPALSHVEQTKKTLSFAMSAKEVTNCAKVNMVVSEKKLLKHLQQKVAKLESELRSPEPSSSTCLKSLLIEKEMKIQQMESEMKELKRQRDIAQSELDLERKAKERKGSSECEPFSQVARCLSYHTKEESIPSKSVPSSRRTARDRRKDNVRQSLTSADPTALVQEIRLLEKHQKKLGEEANQALDLIHKEVTSHKLGDQQAAEKVAKMLSEIRDMQKSNLLTEEIVVGDKANLKEEINRLNSQEIAALEKKLECVQNTIDMLVSSFQTDEQTPDFRTQVKKKRLLPFGLSNSPNLQHMIRGPCSPLSGTENKDPESNVVSANSAPVSFGATPPKRDDNRCRTQSREGTPVSRQANSVDIKRMNRMYKNAAEENIRNIKSYVTGLKERVAKLQYQKQLLVCQVLELEANETGAASEYDATDESQMDWPLCFEEQRKQIIMLWHLCHISIIHRTQFYMLFKGDPADQIYMEVELRRLTWLEQHLAELGNASPALLGDEPASYVASSIRALKQEREYLAKRVNTKLGAEEREMLYLKWDVPPVGKQRRQQFINKLWTDPHNMQHVRESAEIVAKLVGFCDSGETIRKEMFELNFASPSDKKTWMMGWNFISNLLHL', 938, 'Q8LNZ2; Q8L5J2; Q8LGU3; Q9LXL3;', 'KD01293', 'Arabidopsis thaliana (Mouse-ear cress)', 'NACK2', '#Kinesin-like protein NACK2#AtNACK2#NPK1-activating kinesin 2#Protein STUD#Protein TETRASPORE', '-', '-', '823396'),
(1294, 'Q8IWB6', 'Inactive serine/threonine-protein kinase TEX14', 'GO:0000776===GO:0000777===GO:0008608', 167901, '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}.', 'MSRAVRLPVPCPVQLGTLRNDSLEAQLHEYVKQGNYVKVKKILKKGIYVDAVNSLGQTALFVAALLGLRKFVDVLVDYGSDPNHRCFDGSTPVHAAAFSGNQWILSKLLDAGGDLRLHDERGQNPKTWALTAGKERSTQIVEFMQRCASHMQAIIQGFSYDLLKKIDSPQRLVYSPSWCGGLVQGNPNGSPNRLLKAGVISAQNIYSFGFGKAMPWFQFYLTGATQMAYLGSLPVIGEKEVIQADDEPTFSFFSGPYMVMTNLVWNGSRVTVKELNLPTHPHCSRLRLADLLIAEQEHSSKLRHPYLLQLMAVCLSQDLEKTRLVYERITIGTLFSVLHERRSQFPVLHMEVIVHLLLQISDALRYLHFQGFIHRSLSSYAVHIISPGEARLTNLEYMLESEDRGVQRDLTRVPLPTQLYNWAAPEVILQKAATVKSDIYSFSMIMQEILTDDIPWKGLDGSVVKKAVVSGNYLEADVRLPKPYYDIVKSGIHVKQKDRTMNLQDIRYILKNDLKDFTGAQRTQPTESPRVQRYGLHPDVNVYLGLTSEHPRETPDMEIIELKEMGSQPHSPRVHSLFTEGTLDPQAPDPCLMARETQNQDAPCPAPFMAEEASSPSTGQPSLCSFEINEIYSGCLILEDDIEEPPGAASSLEADGPNQVDELKSMEEELDKMEREACCFGSEDESSSKAETEYSFDDWDWQNGSLSSLSLPESTREAKSNLNNMSTTEEYLISKCVLDLKIMQTIMHENDDRLRNIEQILDEVEMKQKEQEERMSLWATSREFTNAYKLPLAVGPPSLNYIPPVLQLSGGQKPDTSGNYPTLPRFPRMLPTLCDPGKQNTDEQFQCTQGAKDSLETSRIQNTSSQGRPRESTAQAKATQFNSALFTLSSHRQGPSASPSCHWDSTRMSVEPVSSEIYNAESRNKDDGKVHLKWKMEVKEMAKKAATGQLTVPPWHPQSSLTLESEAENEPDALLQPPIRSPENTDWQRVIEYHRENDEPRGNGKFDKTGNNDCDSDQHGRQPRLGSFTSIRHPSPRQKEQPEHSEAFQASSDTLVAVEKSYSHQSMQSTCSPESSEDITDEFLTPDGEYFYSSTAQENLALETSSPIEEDFEGIQGAFAQPQVSGEEKFQMRKILGKNAEILPRSQFQPVRSTEDEQEETSKESPKELKEKDISLTDIQDLSSISYEPDSSFKEASCKTPKINHAPTSVSTPLSPGSVSSAASQYKDCLESITFQVKTEFASCWNSQEFIQTLSDDFISVRERAKKLDSLLTSSETPPSRLTGLKRLSSFIGAGSPSLVKACDSSPPHATQRRSLPKVEAFSQHHIDELPPPSQELLDDIELLKQQQGSSTVLHENTASDGGGTANDQRHLEEQETDSKKEDSSMLLSKETEDLGEDTERAHSTLDEDLERWLQPPEESVELQDLPKGSERETNIKDQKVGEEKRKREDSITPERRKSEGVLGTSEEDELKSCFWKRLGWSESSRIIVLDQSDLSD', 1497, 'Q8IWB6; A6NH19; Q7RTP3; Q8ND97; Q9BXT9;', 'KD01294', 'Homo sapiens (Human)', 'TEX14', '#Inactive serine/threonine-protein kinase TEX14#Protein kinase-like protein SgK307#Sugen kinase 307#Testis-expressed sequence 14#Testis-expressed sequence 14 protein', '-', 'ENSG00000121101', '-'),
(1295, 'Q15172', 'Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform', 'c;k', 56194, 'The B regulatory subunit might modulate substrate selectivity and catalytic activity; and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.', 'MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKDATSNEQQELFCQKLQQCCILFDFMDSVSDLKSKEIKRATLNELVEYVSTNRGVIVESAYSDIVKMISANIFRTLPPSDNPDFDPEEDEPTLEASWPHIQLVYEFFLRFLESPDFQPSIAKRYIDQKFVQQLLELFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNIFLRFIYETEHFNGVAELLEILGSIINGFALPLKAEHKQFLMKVLIPMHTAKGLALFHAQLAYCVVQFLEKDTTLTEPVIRGLLKFWPKTCSQKEVMFLGEIEEILDVIEPTQFKKIEEPLFKQISKCVSSSHFQVAERALYFWNNEYILSLIEENIDKILPIMFASLYKISKEHWNPTIVALVYNVLKTLMEMNGKLFDDLTSSYKAERQREKKKELEREELWKKLEELKLKKALEKQNSAYNMHSILSNTSAE', 486, 'Q15172; B2R6D2; B7Z7L2; D3DT99; Q2NL72; Q5VVB2; Q8TBI9;', 'KD01295', 'Homo sapiens (Human)', 'PPP2R5A', '#Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform#PP2A B subunit isoform B''-alpha#PP2A B subunit isoform B56-alpha#PP2A B subunit isoform PR61-alpha#PR61alpha#PP2A B subunit isoform R5-alpha', '-', 'ENSG00000066027', '-'),
(1296, 'Q95LP1', 'Kinesin-like protein KIF2C', 'GO:0000777===GO:0003777', 75639, '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}.', 'MIDFDDVAAINPELLQLLPLHPKDNLPLQENVTIQKQKRRSVNSKIPAPKESLRTRSTRMSTVSELRVTAQENDMEVELPAAANTRKQFSVPPTHPRPSCPAVAEIPSRMVSEEVEEQVHSIRGSSSANPVNSVRRKSCIVKEVEKMKNKREEKKAQNSEMRMKRAQEYDSSFPNWEFARMIKEFRATLECHPLTMTDPIEEHRICVCVRKRPLNKQELAKKEIDVISIPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKAQNASKGIYAMASRDVFLLKNQPCYRKLGLEVYVTFFEIYNGKLFDLLNKKAKLRVLEDGKQQVQVVGLQEHLVNSADDVIKMIDMGSACRTSGQTFANSNSSRSHACFQILLRAKGRMHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIATISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQLIQMETEEMEACSNGALIPGNLSKEEEELSSQMSSFNEAMTQIRELEERAVEELKEIIQQGPDWLELSEMTEQPDYDLETFVNKAEFALAQQAKHFSALRDVIKALRLAMQLEEQASRQISSKKRPQ', 671, 'Q95LP1;', 'KD01296', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'KIF2C', '#Kinesin-like protein KIF2C#Mitotic centromere-associated kinesin#MCAK', '-', '-', '102134753'),
(1297, 'P48729', 'Casein kinase I isoform alpha', 'GO:0000777', 38915, 'Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at ''Ser-45''. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis. {ECO:0000269|PubMed:11955436; ECO:0000269|PubMed:1409656; ECO:0000269|PubMed:18305108}.', 'MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKTKSNMKGF', 337, 'P48729; D3DQG0; D3DQG1; Q4JJA0; Q5U046; Q5U047; Q6FGA2; Q71TU5;Q96HD2; Q9UDK3;', 'KD01297', 'Homo sapiens (Human)', 'CSNK1A1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', 'ENSG00000113712', '-'),
(1298, 'Q9XU12', 'Kinesin-like protein', 'c;k', 83343, '', 'MKSCRSCKENPEVQRKRAEKPWRRAPKAKSEVEKHGIGPPDSDSGEEISFPWYNVTGKMLVVGMHVEIKRSDGRIHGAVIAEVKSNGRFMVEWYEKGETKGKESSLEELLTLNPSLQAPKPTPPPQPPQKTLQASTAVNRQNGIHAQSMILDDEDTFLLDHINMIPAKGASANKRPTGAFTQHVPVRMAPPSEKPLPTRRAPSPKEDAAPAPKSTRTTAAFKPDLDSTAITVPKHTARRTVVVAPAPAPVPAPPIANMTSQRAPSPVARVPSPKNVPRSYPQQDVQPSNGNFAFAEMIRNYRAQIDYRPLSMFDGVNENRISVCVRKRPLNKKELTKAEVDVITIPSRDITILHQPQTRVDLTKYLDNQKFRFDYSFDEYANNELVYRFTAAPLVKTVFDNGTATCFAYGQTGSGKTHTMGGDFSGKKQNASMGIYALTARDVFRMLEQPQYRRKDLSVHCAFFEIYGTKTYDLLNDKAELRVLEDKMQKVQVVGLKEEQAHNEQDVLELINKGTLVRTAGTTSANANSSRSHAIFQIILRQGKKVWGKFSLIDLAGNERGQDTRECDRDTRKEGANINTSLLALKECIRGMARNSSHVPFRQSKLTMVLRDSFIGEKSRTVMISMISPGISSSDHTLNTLRYADRVKEMGTDGSGEATPIRDEELFLPPSADKSDEEYDEMVEKQEHRRVAVDHVRNLKDMSEKIIRETTIVLSNEPSAAQKAECLAKLDQLAQIVSNTRVAVENV', 747, 'Q9XU12;', 'KD01298', 'Caenorhabditis elegans', 'klp-7', '#Kinesin-like protein {ECO:0000256|RuleBase:RU000394}', '-', '-', '176511'),
(1299, 'Q3KPK4', 'Borealin', 'GO:0032133', 30934, '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. Contributes to CPC function by facilitating loading of the CPC onto chromosomes. {ECO:0000269|PubMed:15260989; ECO:0000269|PubMed:17199039}.', 'MASGKKKTSRKPKNRSVKNEKLASFIKDFDSQVKIITEEMKASVVNILKEVDSQYNIEIIKLPMAIREMCWLDYIAKGGSQKALEAAATVKVDMEEITSTVTKTPFKADKKVKKGKCKPDDETVELNPLKSVIRTKTKAKVAAKKPSTARRTRASVGNVANTSKRTSKRGRATPSASKQAETSLLGYTPAATPRIDTSIFKTPALRTPCMQEPVYTFSANGSPLAGMDELFINVPARDGKIIRLLASEVDGLDINRLDQQAFENIKLLSSRLERLCKKLK', 280, 'Q3KPK4; Q693P2;', 'KD01299', 'Xenopus laevis (African clawed frog)', 'cdca8', '#Borealin#Cell division cycle-associated protein 8#Dasra-B#DasraB#xDasraB', '-', '-', '444884'),
(1300, 'Q5A216', 'Probable kinetochore protein NDC80', 'GO:0000777', 92449, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSQTSNPIYGLRRNNGFAGGSNPSNNNNNNSNNNHNGNRISLGSATRTSSIISNNLPFRQSLLHGNYDNAINNTPSTSSLQKQSQQQQQSSQTSQTKRRSTLLSTPATTTKRRQSMMGNNLHQQHQYGSTALRHSTQPSSSMNSQFNQALQHVSPYYNPTSYSSQTPSSQPSSQQYQQQQQQANIPSSASSSQQQQSMDPRPLKDKKYQELIQKEIIRYLIDYKFEIKTNIALTENILKSPTQKNFNAIFKFLYNQLDPNYMFIKSSIEQEIVTLLKLLNYPYMHTITRSHFSAVGGNNWPTFLGILYWLVELNLSLSTLNDDDFLADDDFDKIFIEYIWKSYSLFINDEEEEEQQQQQQQQQANNGGSGGGGGDKFYNDMKIKFDQLQEKLNQELNNVEQQHENLLNKYHELNNQLKIRDDALKKTVALEEDYMKLKSYNQNVEKMMPEWNKKLEQLSNEVISYEEQMNKLQDEKKSIEMDLQQRGISIDKVNELYIKRDQLSKSIEIISNKIDDLKEKLSGRSFDLEKNFDNLENLTNQYNEITNKFNYYYYQQIQQNQQQDQQQQEEEEEEEEEEEHQLIPQFGLKLDENIKTTNERRQFTRDEIFLNINVKQERQNLLNFRNELDHQILNDRSQAMKFNEKCDIEQDKIKDQQSIIEELKIQDSLMKRKSDDLKQTIFQIQNEFNSQIESLDQQIRETKSNIQSDILQLERKLRDVNLNKSLIQEQLIGKRQKIDEDVINLTSFILKFKTNIQEKLINIADIVQDQLKKEQQQQQQQQASQQLE', 788, 'Q5A216;', 'KD01300', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '3642548'),
(1301, 'Q6P597', 'Kinesin light chain 3', 'GO:0003777', 55364, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.', 'MSVQVAAPGSAGLGPERLSPEELVRQTRQVVQGLEALRAEHHGLAGHLAEALAGQGPAAGLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHVGALEAEKQRLRSQARRLAQENVWLREELEETQRRLRASEESVAQLEEEKRHLEFLGQLRQYDPPAESQQSESPPRRDSLASLFPSEEEERKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATDLLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFEDVERHYARALSIYEALGGPHDPNVAKTKNNLASAYLKQNKYQQAEELYKEILHKEDLPAPLGAPNTGTAGDAEQALRRSSSLSKIRESIRRGSEKLVSRLRGEAAAGAAGMKRAMSLNTLNVDAPRAPGTQFPSWHLDKAPRTLSASTQDLSPH', 504, 'Q6P597; A0AVM3; A2RUT6; Q6GMU2; Q8NAL1; Q8WWJ9;', 'KD01301', 'Homo sapiens (Human)', 'KLC3', '#Kinesin light chain 3#KLC2-like#kinesin light chain 2', '-', 'ENSG00000104892', '-'),
(1302, 'Q6IPU0', 'Centromere protein P', 'k', 33165, '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}.', 'MDAELAEVRALQAEIAALRRACEDPPAPWEEKSRVQKSFQAIHQFNLEGWKSSKDLKNQLGHLESELSFLSTLTGINIRNHSKQTEDLTSTEMTEKSIRKVLQRHRLSGNCHMVTFQLEFQILEIQNKERLSSAVTDLNIIMEPTECSELSEFVSRAEERKDLFMFFRSLHFFVEWFEYRKRTFKHLKEKYPDAVYLSEGPSSCSMGIRSASRPGFELVIVWRIQIDEDGKVFPKLDLLTKVPQRALELDKNRAIETAPLSFRTLVGLLGIEAALESLIKSLCAEENN', 288, 'Q6IPU0; B3KRA5; B3KS17; Q5T9F8; Q5T9F9;', 'KD01302', 'Homo sapiens (Human)', 'CENPP', '#Centromere protein P#CENP-P', '-', 'ENSG00000188312', '-'),
(1303, 'P40568', 'Kinetochore-associated protein DSN1', 'GO:0000776===GO:0051456===GO:0000818===c;k', 65692, '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. {ECO:0000269|PubMed:12455957; ECO:0000269|PubMed:14633972}.', 'MSLEPTQTVSGTPPMLHQRTHKQVYPLRMETIPILESDSKATLQSNEPTQKDEEETEYFENKQSVSNLSPDLKFKRHKNKHIQGFPTLGERLDNLQDIKKAKRVENFNSSAPIADDNHSGDATANATANATANATANVNASAMPAPYMPYYYYYHPMNAPTPAMIPYPGSPMHSIMPNSSLQPFYSQPTAAGGPDMTTPQNISSSQQLLPAPQLFPYGSFHQQQLQQPHYIQRTRERKKSIGSQRGRRLSMLASQANGGSTIISPHKDIPEEDFYTVVGNASFGKNLQIRQLFNWCLMRSLHKLELKAKNQEEEGELEHLTKKSKLESTKAETDYVDPKRLAMVIIKEFVDDLKKDHIAIDWEDEEKYEDEDEEKILDNTENYDDTELRQLFQENDDDDDDDDEVDYSEIQRSRRKFSERRKALPKEPKKLLPNSKNVENTKNLSILTSKVNAIKNEVKEWAVTLDTSRPDLEWQELTSFSSQPLEPLSDTEEPDLAIADVETKLETKVDELRYQSHILNSHSLALNEITNSKVNKLNIETMRKISSETDDDHSQVINPQQLLKGLSLSFSKKLDL', 576, 'P40568; D6VVU0;', 'KD01303', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DSN1', '#Kinetochore-associated protein DSN1', '-', '-', '854827'),
(1304, 'Q8K1K4', 'Centromere protein I', 'GO:0000776===GO:0034508', 85403, '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. Required for the localization of CENPF; MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to kinetochores. Involved in the response of gonadal tissues to follicle-stimulating hormone (By similarity). {ECO:0000250}.', 'MATQRVTRNSQQQNRISQGSNSRQTSLLDWMVKDKSGNFKSVLKESSSVEDSTRTDDRTEGALQVAVGYFQKGPKKASLSKDKVLEKHLTTVENVALSNGLAPEAIDILLNVALSGKFGNAVNSRILKCMIPESHISEDSVLKAVSWLCVDKCSGNTKVLFYRWLVAMFDFIDHKKQISSLYGFFFASLQDDTLCPYVCHLLYLLTKRENVKPFRVRKLLDLQAKMGMQPHLQALLSLYKFFAPTLISVSLPVRKKIFFNNSKNLWTSASLAVRLRNQGAFPEPLNLPLRPTTGRSLKRKWNSHSVIPALNSANKEYGEKTASLFDYLSSERSLPLEQLQRFPQLLESIHCLELPSQMCSVLNSPLLLHYINCVKDESILLRISYWLSQALQEECVWYNINNYEQEKEFINFLDLVIRVQCFLQEGFYSCEAFLYKSLPLWDGSSCRSQYLQLLAWIPFSSFSEVKPLLSDHLAPLFFTSSIYFKCSVLQSLQELLQNWLLWLSTDAHVQPTTDSPLETTLGGSMSSVSQLIEYTGWLCVVAMRLESSSTLLLHFILDFYEKVCDIYINYDLPIVVLFPPVIFHSALLSLDATILNQLCYIMYRYRNNWTAAKKNRYLQKAKPEFSLSSKICKEYNYYLTAMVCCLWTSRPFKAGVYTDPETIENTGGTQYKSTLNIVYHPSLLSYAASFLLQESPEEMTEHLSSIQGKKWNWYLDYLYSEGFQGLKLFIKSSVHSSVPKPEENTE', 746, 'Q8K1K4; Q8BXU9;', 'KD01304', 'Mus musculus (Mouse)', 'Cenpi', '#Centromere protein I#CENP-I#FSH primary response protein 1#Follicle-stimulating hormone primary response protein', '-', '-', '102920'),
(1305, 'Q6DRJ7', 'Kinetochore protein NDC80 homolog', 'GO:0000776===GO:0000777===GO:0000778===GO:0051315===GO:0031262', 73217, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSRRPSSRYSEMPMRVTDSRMSLINATPQNKDNAFGKLNIPKPQSTTSERRTSFFGKGIGAGGQRNSMFGSYGGSEKMKDPRALHDKAFVQQCIKQLYEFLVDRGFPGSITVKALQSPSTKEFLKIYEFIYNFLEPSFQMPTAKVEEEIPRMLKDLGYPFALSKSSMYSIGAPHTWPLALGALIWLMDAVKLFGGQREQDLLFSDFSDELCDLEDRTEYNKLIMEYCSDTYNKFMQGADTFDDEDDDFLYKLKKLYNVDEALLHSQQEKHSMLMEHVERLERESQTDRLVGKRTEKLRLQTDLQKLQNYRCTLEAHKTGLENKSAGLTEELEAVEMQLEGLKQERTRLQHILENQKFTPADIERINRERNELQQTIHGLSQSLEEGEQLVWNEEVNLSKTKEKAELKVAEYNKLGRKLKLIPLSAENACGHDFEIRADYSATTITQYKTQIQNPLKNMMVEVEEEFSRLSNVNLSLEETVEQVKSNIFDKENDIKQLKEQIRKVDQQLENAMQEMALEDDKWAAELDSAETHKKLFEKNVMQGIEEAEEEVKAAQQQYHVVVQETNEKNRMVVKNMTDLFSSTVNHLFAVEKHCDEQLKRFDKLKDIVREDEADINQLTDLVENFIKKANSL', 632, 'Q6DRJ7; Q502U1;', 'KD01305', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'ndc80', '#Kinetochore protein NDC80 homolog#Kinetochore protein Hec1#Kinetochore-associated protein 2-like', '-', '-', '445386'),
(1306, 'Q7S9B6', 'Histone acetyltransferase esa-1', 'GO:0034508', 58807, '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}.', 'MSPPGGDATVGSDEKRQKGKATPDTIKMGCIAMVMKEGQLRRAEILSIKDTKSGRQFYCNFDNFNKRLDEWVPAARIDFEQDVEWPNPDKDKQKDAKTKKNNSTVSKKQPSKKNNQKKASKREQSVASDGQTPHPWTEFVESQPGKNNRQRGKTEDGTDVNASLEVGGDKGVKRKADEIDMDEDEIPAAKKQRQPSFSREQEIEKLRTSGSMTQNPTEISRIRNISKVEFGRYVLFPWYFSPYPQIFDQEDCIYICEFCLSYYGELKSFVRHRQKCTLHHPPGNEIYRDDYVSFFEIDGRRQRTWCRNLCLLSKMFLDHKTLYYDVDPFLFYVMTTRDDRGCHIIGYFSKEKESTDGYNVACILTLPQYQRKGYGRLLIQFSYELSKIEGKLGSPEKPLSDLGLLSYRQYWSENIIDILLGYNERKEACTIENIAVALAMTTQDVEHTLQALKMQVYHKGEHKIVVPEKLIKQREKSKAKQKRLIDPERIQWKPPVFTALNRTWGW', 506, 'Q7S9B6;', 'KD01306', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'esa-1', '#Histone acetyltransferase esa-1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}#Histone acetyltransferase hat-4', '-', '-', '3878365'),
(1307, 'Q6NRW2', 'Protein Spindly-B', 'GO:0043515===GO:0034501===GO:0000940', 70778, '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}.', 'MEESETVLKLRRQLKEAEEERVKAAHYGLELLESQSDLQNQLEEQRNEMTGTIENLEQEKYSLQREVELKNRMLESLTSECENIRQQQKLSLEQLEEQLERNHHRELSEIKDKLEKLKAELDEARLSEKQLKHKLDYQTEVLANKSEELRMMSERVHETMSSEMLTLQLEKTELETAKDNLEQELNELQYREQQLLLTNGNQSRQLERLQTEKEEREKEAVGYFSALEKAREANQDLQAQLDIALQQAQDPNSKGNSLFAEVEDRRSEMERQLISMKVQFQSLQKQHAFSRQQMHRMKIQIATLLQLKGSHSDPEQLERLQAMVAQKNSEIETLVMKVRQLEKSQQICENGPVASSCDGLGQGDETYYVDLLKMKLVNSSKEIDKVKDELSLQRMKALAESQRVLELERKLFTNDRHLKLSQGENMKLRVNLDEMKMKYEPDEMGKIRTQKRRKEQLPLDCLIDNTSVAVTSGTEAHGVSDATPGETCTAESSDDKKLPKEDLSLSTKDQDPSSVLLKPNEPPNGQPPKERKRVRIMEDEKDTPDLNKRNPNNCTITSIHPRSTYEESTSELKKVDEEQEKRKQERKSRLRAPPVLHVPSKPATAQCPQQ', 610, 'Q6NRW2;', 'KD01307', 'Xenopus laevis (African clawed frog)', 'spdl1-b', '#Protein Spindly-B {ECO:0000255|HAMAP-Rule:MF_03041}#Coiled-coil domain-containing protein 99-B {ECO:0000255|HAMAP-Rule:MF_03041}#Spindle apparatus coiled-coil domain-containing protein 1-B {ECO:0000255|HAMAP-Rule:MF_03041}', '-', '-', '431843'),
(1308, 'Q13042', 'Cell division cycle protein 16 homolog', 'c;k;s', 71656, '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:18485873}.', 'MNLERLRKRVRQYLDQQQYQSALFWADKVASLSREEPQDIYWLAQCLYLTAQYHRAAHALRSRKLDKLYEACRYLAARCHYAAKEHQQALDVLDMEEPINKRLFEKYLKDESGFKDPSSDWEMSQSSIKSSICLLRGKIYDALDNRTLATYSYKEALKLDVYCFEAFDLLTSHHMLTAQEEKELLESLPLSKLCNEEQELLRFLFENKLKKYNKPSETVIPESVDGLQENLDVVVSLAERHYYNCDFKMCYKLTSVVMEKDPFHASCLPVHIGTLVELNKANELFYLSHKLVDLYPSNPVSWFAVGCYYLMVGHKNEHARRYLSKATTLEKTYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAERFFSQALSIAPEDPFVMHEVGVVAFQNGEWKTAEKWFLDALEKIKAIGNEVTVDKWEPLLNNLGHVCRKLKKYAEALDYHRQALVLIPQNASTYSAIGYIHSLMGNFENAVDYFHTALGLRRDDTFSVTMLGHCIEMYIGDSEAYIGADIKDKLKCYDFDVHTMKTLKNIISPPWDFREFEVEKQTAEETGLTPLETSRKTPDSRPSLEETFEIEMNESDMMLETSMSDHST', 620, 'Q13042; A2A365; Q5T8C8; Q7Z651; Q96AE6; Q9Y564;', 'KD01308', 'Homo sapiens (Human)', 'CDC16', '#Cell division cycle protein 16 homolog#Anaphase-promoting complex subunit 6#APC6#CDC16 homolog#CDC16Hs#Cyclosome subunit 6', 'BIOMD0000000186,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Dissociation variant;BIOMD0000000187,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Convey variant;', 'ENSG00000065882', '-'),
(1309, 'Q6NRW3', 'Kinetochore protein Spc24', 'GO:0000777===GO:0031262===SCL===k', 22722, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:14738735}.', 'MLCEQISEYVDVSREIVKVMVSDSAAGALKKSLDRQEAMIDSLLDTEVQASQLIRDLMAVEEKVAQKLLDTEETKQKSSSKLQKIDRELQERMEKNASLESSIKFLQKDLEELKVMEEEIADMQREADEDTTTVIPSAVYLAKLFHNVTKIDWDYNCDPSLIKGIHYGGDIAQPISIDSNQHSKIFICNYLWSLLSTDW', 199, 'Q6NRW3;', 'KD01309', 'Xenopus laevis (African clawed frog)', 'spc24', '#Kinetochore protein Spc24#xSpc24', '-', '-', '403385'),
(1310, 'Q2KIP2', 'Serine/threonine-protein kinase haspin', 'GO:2000751', 86411, 'Serine/threonine-protein kinase that phosphorylates histone H3 at ''Ser-3'' (H3T3ph) during mitosis. This positions and activates AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion; metaphase alignment and normal progression through the cell cycle (By similarity). {ECO:0000250}.', 'MAASLPLPASGLFRTYGAAGGGRPRRRQGLAAVQWFPPQDRKRFFSSSSSDTSSGGPSQSVVSDDPDDPDFPGSPVGQRRRRAGARLAKGRPSQIATPRRLRLRSRCPQKCSTPCGALEPPSFPNGNPGSLSPDLRVCGQPRDGGELGTSASLFSSLASPGPGFPAPEDSICTDPSTFLDAASEAPSNFHLPEASLDQAPLPCSQDAATGGGRFTRLAHQAQASLRSALFSFLDPGNPEDSELGTDGKNLQEFCHDRELVGRRLESPGLSGRGKKRTTDQDSCREIESQESVQIEYEEARGCKGGIASGKSNGPERTRLSRKRKHQGTAETSLLHHCQVTKGQKMEDGSCVTQDLTRLQNACSWTKTRASFSFHKKKIVTAVSEVCSCDTLAGSLSESLMSEYSHHPVQNRTSCALSPWHSSSMYLLTPLKTQQVTDKRTSDAEKLYGECNQVGPIPFSDYLSEEKLECCEKIGEGVFGEVFQTVTNHTPVALKIIAIEGQNLVNGAHQKTFEEILPEIIISKELSLLSDEACNRTEGFIGLNSVHCVQGSYPPLLLQAWDHYHSTKGSANDRPDFFREDQLFIVLEFEFGGIDLEQMRKKLSSIATAKSILHQITASLAVAEASLHFEHRDLHWGNVLLKKTSLKELHYTLNGKKSSIPTRGLQVNIIDYTLSRLERDGIVVFCDISRDEDLFMGQGDYQFEIYRLMRKENNNCWGEYHPYNNVLWLHYLTDKILNQMTFKSKHNTPALKRMKKQIQHFYQTMLNFSSATDLLCQHSLFK', 781, 'Q2KIP2;', 'KD01310', 'Bos taurus (Bovine)', 'GSG2', '#Serine/threonine-protein kinase haspin#2.7.11.1#Germ cell-specific gene 2 protein', '-', '-', '767819'),
(1311, 'P70281', 'Synaptonemal complex protein 3', 'k', 29347, 'Component of the transverse filaments of synaptonemal complexes (SCS); formed between homologous chromosomes during meiotic prophase. Required for axial elements (AE) in meiotic cells and for assembly of the synaptonemal complex. May be important for testis development and male fertility. Required for efficient phosphorylation of HORMAD1 and HORMAD2. {ECO:0000269|PubMed:10678170; ECO:0000269|PubMed:22346761}.', 'MLRGCGDSDSSPEPLSKHLKMVPGGRKHSGKSGKPPLVDQPKKAFDFEKDDKDLSGSEEDVADEKAPVIDKHGKKRSAGIIEDVGGEVQNMLEKFGADINKALLAKRKRIEMYTKASFKASNQKIEQIWKTQQEEIQKLNNEYSQQFMNVLQQWELDIQKFEEQGEKLSNLFRQQQKIFQQSRIVQSQRMFAMKQIHEQFIKSLEDVEKNNDNLFTGTQSELKKEMAMLQKKVMMETQQQEMANVRKSLQSMLF', 254, 'P70281; Q3V2A4; Q549A7;', 'KD01311', 'Mus musculus (Mouse)', 'Sycp3', '#Synaptonemal complex protein 3#SCP-3', '-', '-', '20962'),
(1312, 'L0N7N1', 'Kinesin-like protein KIF14', 'GO:0003777', 186445, 'Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (PubMed:24949858). Plays a role in many processes like cell division; cytokinesis and also in cell proliferation and apoptosis (By similarity). During cytokinesis; targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (By similarity). Regulates cell growth through regulation of cell cycle progression and cytokinesis. During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation; resulting in positive regulation of cyclins; including CCNE1; CCND1 and CCNB1 (By similarity). During late neurogenesis; regulates the cerebellar and cerebral cortex development and olfactory bulb development through regulation of apoptosis; cell proliferation and cell division (PubMed:23308235; PubMed:24931760). Also is required for chromosome congression and alignment during mitotic cell cycle process (By similarity). Regulates cell spreading; focal adhesion dynamics; and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (By similarity). {ECO:0000250|UniProtKB:Q15058; ECO:0000269|PubMed:23308235; ECO:0000269|PubMed:24931760; ECO:0000269|PubMed:24949858}.', 'MSVHTSHSRHNIGSLEVSSSQKISASSGLVHSSRLELHLKADMSECENHDPFVNAGSKTIDINSTYVISACKKTRETPVTSDPRRLSLQRRATCGDRESSLLGSELGNRRTADTSLRLQRRHGRADYVGKWETLNPVGGNPGSDSASQASRTEAKGVNNDTRVLSSVVSVKDSNDTGLTRCKDPGPPVGASNEKVTVKDTNSRAPVGSQRQTEAMRSGHLVVQLTESKSDTPVSGGRNSHRGNAGKDTAKQVGTFGSSDTRTPVKCVLEHRWTPRHDPPPPKSPALSTPKNNGKDIPKHGSTFRSASSESRTPVKCVPEHRWTPRHDLPPPKSPALSTLKNRIASPRVKPRPKSSLFANKRESSRESTLPPEENSLVQKTFTEPDSLKVENSQVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDMKQVYSFIYDVSFWSFDECHPGYASQTTVYETLAAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLVCKGENGQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVVEGEEHDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQANGKRVFIPYRESTLTWLLKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNEDMNAKLIRELKAEIEKLKAAQRSNRNIDPERYRLCRQEITSLRMKLHQQERDMAEIQRVWKEKFEQAEKRKLQETKELQKAGVTFQMDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNGTHISEPTVLHHGDRVVLGGDHYFRFNHPVEVQKGKKLSSRNNLTTSEGPKDFEFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRLEELNNQKASHKIEELERAKQHLEQEVYVNKRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDKTFTIQPNWNSMKLSTMIQEANAISDKFKKCYIFGRHDASDKGRSDTSVRVRNLQLGISTFWSLEKFESKLAAMKELYESNGGDRDEDVFCDPADEWEPDITSTPVSSLSRRRSRSLMKNRRVSGCLHDIHPIQSMQSSHSSGLMEKPSTIYSNSSESFLPGICKELIGSSIDFLGQSFDEEKTIADSLINNLLRLHNGVIAISKAHEEQDEESQDNLFSDRAAQALTIQVACAFEQLVVLFKHWLGDFLPCTGSARLEDELRQDIKKLGGYLQLFLQGCCSDISSMVKEAQNKVMKIIQQAVQCVGQLAVLKGSKLCVLENSSKVSSTQEFMAALQDGVTSGMKSLLDSGLETAQDLRQDLSRQSAREEVTKQMKASTVEWVGSLENAVAEWRTKSFRTQAQEGSRQQVSKLLSLASEFLKLKSCLQQTVEMIVSALRGCPSDLHCLRSCTETICSLARKLHSDFSAHSASAGSCGNELPRADCEELESLAKSLLLCFECGESPGLSKPWESCSSNSKEEQCKSDRADCGKSGPRRACEPHGDATPAVSSGDCTPNRIQWV', 1674, 'L0N7N1;', 'KD01312', 'Mus musculus (Mouse)', 'Kif14', '#Kinesin-like protein KIF14 {ECO:0000305}', '-', '-', '381293'),
(1313, 'P48734', 'Cyclin-dependent kinase 1', 'GO:0034501', 34025, '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 (By similarity). {ECO:0000250}.', 'MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQFMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKSTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDSQIKKM', 297, 'P48734; Q2YDM6;', 'KD01313', 'Bos taurus (Bovine)', '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', '-', '-', '281061'),
(1314, 'Q9QXU8', 'Cytoplasmic dynein 1 light intermediate chain 1', 'GO:0000776===GO:0000777===GO:0003777===GO:0005868', 56792, '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. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress throuh the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores (By similarity). {ECO:0000250}.', 'MAAVGRVGSFGSSPPGLASTYASGPLANELASGSGGPAAGDDEDGQNLWSRILREVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGEDFPASPQRRATAAQEDRDDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKIEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVGGSPGGGAAGASTSLPPSAKKSGQKPVLSDVHAELDRITRKPASVSPTTPPSPTEGEAS', 523, 'Q9QXU8;', 'KD01314', 'Rattus norvegicus (Rat)', 'Dync1li1', '#Cytoplasmic dynein 1 light intermediate chain 1#Dynein light chain A#DLC-A#Dynein light intermediate chain 1; cytosolic', '-', '-', '252902'),
(1315, 'P62136', 'Serine/threonine-protein phosphatase PP1-alpha catalytic subunit', 'c;k;m;s', 37512, 'Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division; and participates in the regulation of glycogen metabolism; muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex; which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting; both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure; and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E; determines the circadian period length; through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the ''Ser-418'' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis; thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). {ECO:0000269|PubMed:17283141; ECO:0000269|PubMed:21712997; ECO:0000269|PubMed:23396208}.', 'MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK', 330, 'P62136; A6NNR3; B2R908; P08129; P20653; P22802; Q07161;', 'KD01315', 'Homo sapiens (Human)', 'PPP1CA', '#Serine/threonine-protein phosphatase PP1-alpha catalytic subunit#PP-1A#3.1.3.16', 'BIOMD0000000286,Proctor2010 - a link between GSK3 and p53 in Alzheimer''s Disease;BIOMD0000000488,Proctor2013 - Effect of AÎ² immunisation in Alzheimer''s disease;BIOMD0000000543,Qi2013 - IL-6 and IFN crosstalk model (non-competitive);BIOMD0000000544,Qi2013 - IL-6 and IFN crosstalk model;', 'ENSG00000213639', '-'),
(1316, 'O45406', 'Kinetochore-binding protein 3', 'GO:0000777===k', 15930, '', 'MESLNEYMDKIINRLKAVNEKDELVDEGMRKLQKCQEKIMKTRIDAQKHIDERHEQQSFEQQLLNKNMFETEQLEEKLKRLDDENKIGNEREFNKKLEAISAKWTDDVNLLKTTPNEPNDGNRKKLSNLSNILV', 134, 'O45406;', 'KD01316', 'Caenorhabditis elegans', 'kbp-3', '#Kinetochore-binding protein 3', '-', '-', '175097'),
(1317, 'Q562F6', 'Shugoshin-like 2', 'GO:0000777===k', 144739, '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 (By similarity). Essential for recruiting KIF2C to the inner centromere and for correcting defective kinetochore attachments. {ECO:0000250; ECO:0000269|PubMed:16541025; ECO:0000269|PubMed:17485487}.', 'MECPVMETGSLFTSGIKRHLKDKRISKTTKLNVSLASKIKTKILNNSSIFKISLKHNNRALAQALSREKENSRRITTEKMLLQKEVEKLNFENTFLRLKLNNLNKKLIDIEALMNNNLITAIEMSSLSEFHQSSFLLSASKKKRISKQCKLMRLPFARVPLTSNDDEDEDKEKMQCDNNIKSKTLPDIPSSGSTTQPLSTQDNSEVLFLKENNQNVYGLDDSEHISSIVDVPPRESHSHSDQSSKTSLMSEMRNAQSIGRRWEKPSPSNVTERKKRGSSWESNNLSADTPCATVLDKQHISSPELNCNNEINGHTNETNTEMQRNKQDLPGLSSESAREPNAECMNQIEDNDDFQLQKTVYDADMDLTASEVSKIVTVSTGIKKKSNKKTNEHGMKTFRKVKDSSSEKKRERSKRQFKNSSDVDIGEKIENRTERSDVLDGKRGAEDPGFIFNNEQLAQMNEQLAQVNELKKMTLQTGFEQGDRENVLCNKKEKRITNEQEETYSLSQSSGKFHQESKFDKGQNSLTCNKSKASRQTFVIHKLEKDNLLPNQKDKVTIYENLDVTNEFHTANLSTKDNGNLCDYGTHNILDLKKYVTDIQPSEQNESNINKLRKKVNRKTEIISGMNHMYEDNDKDVVHGLKKGNFFFKTQEDKEPISENIEVSKELQIPALSTRDNENQCDYRTQNVLGLQKQITNMYPVQQNESKVNKKLRQKVNRKTEIISEVNHLDNDKSIEYTVKSHSLFLTQKDKEIIPGNLEDPSEFETPALSTKDSGNLYDSEIQNVLGVKHGHDMQPACQNDSKIGKKPRLNVCQKSEIIPETNQIYENDNKGVHDLEKDNFFSLTPKDKETISENLQVTNEFQTVDLLIKDNGNLCDYDTQNILELKKYVTDRKSAEQNESKINKLRNKVNWKTEIISEMNQIYEDNDKDAHVQESYTKDLDFKVNKSKQKLECQDIINKHYMEVNSNEKESCDQILDSYKVVKKRKKESSCKAKNILTKAKNKLASQLTESSQTSISLESDLKHITSEADSDPGNPVELCKTQKQSTTTLNKKDLPFVEEIKEGECQVKKVNKMTSKSKKRKTSIDPSPESHEVMERILDSVQGKSTVSEQADKENNLENEKMVKNKPDFYTKAFRSLSEIHSPNIQDSSFDSVREGLVPLSVSSGKNVIIKENFALECSPAFQVSDDEHEKMNKMKFKVNRRTQKSGIGDRPLQDLSNTSFVSNNTAESENKSEDLSSERTSRRRRCTPFYFKEPSLRDKMRR', 1265, 'Q562F6; Q53RR9; Q53T20; Q86XY4; Q8IWK2; Q8IZK1; Q8N1Q5; Q96LQ3;', 'KD01317', 'Homo sapiens (Human)', 'SGOL2', '#Shugoshin-like 2#Shugoshin-2#Sgo2#Tripin', '-', 'ENSG00000163535', '-'),
(1318, 'Q9Z0R0', 'Serine/threonine-protein kinase haspin', 'GO:2000751', 84181, 'Serine/threonine-protein kinase that phosphorylates histone H3 at ''Ser-3'' (H3T3ph) during mitosis. This positions and activates AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion; metaphase alignment and normal progression through the cell cycle. {ECO:0000269|PubMed:10358056; ECO:0000269|PubMed:15681610}.', 'MAQAHPRSGTRLFRTYAARGVRGSQRQPGGLAEQWFQPPNLKRAFSSSLSDSNESPAVASDDPDDPDFPGSLVGQRRRRPRGSGSRNQRTLTNTPRVQRLRPRPPQKCSTPCSRLRPPPFPNCSPGCLGSDHSVCIQSRDSNELGTSASLFSSPASPGAPDPLYADSAVPGSFHLPAASLSEPSVPCPQVAATGDRYTGRALRAEASFRSSLFSLVNSGATEENKFGTDGENVKESCCERRQQMGNRLTDPDLTSPGKRKAACKKVVSQGVDQRDYEESSACKDLRVPGEISRPKRTGPLRKRKQQEATGTPPRHYHQSKKKRKASVSLWNLNTSQRDSWTKTRASFGFHKKKIITSVIEVCSSVASSSSRSLLSECSTPPIKNRAHLTVSSRCSSVYLLSPLKTLHVTDQRPSYAEKVYGECNQEGPIPFSDCLSTEKLERCEKIGEGVFGEVFQIINDQAPVALKIIAIEGLDLVNGSHQKTFEEILPEIIISKELSLLSSEAYNRTEGFIGLNSVHCVQGLYPPLLLKAWDHYNTTKRSANDRPDFFQEDQLFIILEFEFGGVDLERMKTKLSSVATAKSILHQITASLAVAEASLHFEHRDLHWGNVLLKKTNLKELRYTLNGKTSTIPTHGLQVNIIDYTLSRLERDGIVVFCDISAEEDLFTGEGDYQFEIYRLMRKENKNCWGEYHPYNNVLWLHYLTDKILNKMKFKTKCQSAAMKQIRKNLQHFHRTVLSFSSATDLLCQHSLFR', 754, 'Q9Z0R0; Q99MU9; Q9JJJ4;', 'KD01318', 'Mus musculus (Mouse)', 'Gsg2', '#Serine/threonine-protein kinase haspin#2.7.11.1#Germ cell-specific gene 2 protein#Haploid germ cell-specific nuclear protein kinase', '-', '-', '14841'),
(1319, 'Q0VDD8', 'Dynein heavy chain 14; axonemal', 'GO:0003777', 399895, '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}.', 'MGRRSQWIWAMRCQMLVPVLSLHIGLARALGCGCIASKIECLIRCNAPFPLLDAVGSVASQELQSLTGTVGVTSGAAAYPRWNLARARAPPHLPGTQDPLRRVRDPTPIVASSPGRRRGSWSGGYGQEASEPGVVGLCCAVLPIHPSLALAGVGGPDLRRFQEGPQRPSDHGAAEKHMETFIPIDLTTENQEMDKEETKTKPRLLRYEEKKYEDVKPLETQPAEIAEKETLEYKTVRTFSESLKSEKTEEPKDDDVIRNIIRLREKLGWQTILPQHSLKYGSSKIAIQKITLKKPLEDDGEFVYCLPRKSPKSLYNPYDLQVVSAHTAKHCKEFWVITASFISKLDSSRTYSLDEFCEEQLQQATQALKQLEDIRNKAISEMKSTFLKVAEKNEIKEYFESKLSEDDTTHFKLPKYRRLLETFFKFVMLVDYIFQELIRQLMNTAVTLLLELFNGSAGMPFSVEKKNENLIRTFKDNSFPTGKTTNDCEELVDNSKLHAISVQKSEVKTDTDINEILNSVEVGKDLRKTYAPIFEVNLCLRIPAESDSSENSKENFHESDQCPEECVMFEDEMSENKDNCVKKHSSEELLPKAKKSKEISYNLEDIISATITPLCQDPQLSIFIDLVSIMDLPNKTGSIIHYKEQTRWPDCHILFETDPAYQNIIVNLLTIIGNSMGLVNAYSHKFIKYCTMTEKAKIMSMKISSMGELTSKEFEAILNRFRNYFRHIVNMAIEKRIGIFNVVVESSLQQLECDPTEIEEFLEHFIFLNAISSKISKLEKEFLTMSQLYSVAKHHQIHISEEQIAIFQVLLLKFSQLKSSMKLSKINKDTAITKFRDNLEACISGLHVDVGNLKAKIRTPLLLCAGTQVSTAMEMIQTLSGEAASLTNKAKAYSHYQDCFSDSQSHMHSVNVEEITQIVLSEISDIEGDLTLRKKLWEAQEEWKRASWEWRNSSLQSIDVESVQRNVSKLMHIISVLEKEIYSIFIIPSIDDISAQLEESQVILATIKGSPHIGPIKSQIMFYNDCVKSFVSSYSREKLEKVHAGLMCHLEEVADLVVLDTSNSRTKAILGALLILYVHCRDIVINLLLKNIFNAEDFEWTRHLQYKWNEKQKLCYVSQGNASFTYGYEYLGCTSRLVITPLTDRCWLTLMEALHLNLGGCPAGPAGTGKTETVKDLAKCALFAFKCNTALIKLPNSLIVLTCFGLEKTVLVMNTVMSFRFVLEGKEIRINMSCAVFITMNPRYGGGVELPDNLKSLFRPVAMMVPHYQMIAEIILFSFGFKSANSLSGKLTNLYELARKQLSQQDHYNFGLRSLKIVLIMAGTKKREFKCDTSDSLSEADETLIVIEAIREASLPKCPPEDVPLFENIIGDIFPEVTVLKVNQLALEKVIYTATQQLGLQNWSSQKEKIIQFYNQLQVCVGVMLVGPTGGGKTTVRRILEKALTLLPIADFLSVAERKSASKISERKGKVDICVLNPKCVTLSELYGQLDPNTMEWTDGLLSATIRSYVYFNTPKNTKKDIDLRLKSRISDLSNVFKLDSSDTTETDDNIFEEIEKVVKIPENHNFDWQWIILDGPVDTFWVENLNSVLDDTRTLCLANSERIALTNKIRVIFEVDNLSQASPATVSRCAMVYMDPVDLGWEPYVKSWLLKTSKIISQSGVDCLEFMIKNSVTDGLQFIRNRQKFQPYPMEDITVVITLCRILDAFFDFMGKNGGFEQSDDLNDTSSKEANSQRESVTFKDIEKRDENTWYPEKNPDKLTKIIQKLFVFAFTWAFGGALNREDEHRENIPFCPSLEPDSLAKVTYDFDKLVHELFGNSSQVGINLPTGECSIFGYFVDIEQCEFIPWSDLVPNDQTLIQRDNPTKKPEVRTNKKLLKNNDHKGVVVSTINFSTNVTAAKTKEMILKKLIRRTKDTLGAPKNNRILIFIDDMNMPVSDMYGAQPPLELIRQLLDLGGVYDTEKNTWKNIQDLSIVAACVPVVNDISPRLLKHFSMLVLPHPSQDILCTIFQIGIDGCGKKTCATLACYLTDNKLYRVPISHKCAYIEFKEVFKKVFIHAGLKGKPTVLMVPNLNIEQDSFLEDLNYIISSGRIPDLFENVELDSIAMKIRYLTEQSGHMDNRQSLLSFFQKRIYKNLHIFVIMSPEGPSFRQNCRVYPSMISSCTIDWYERWPEEALLIVANSFLKEKVNFENRENLKEKLAPTCVQIHKSMKDLNRKYFEETGRFYYTTPNSYLQFMETFAHILRAREEEMQTKRDRFHMGLSTILEATTLVTEMQEELLILGPQVEQKTKETETLMEKLRKDSQVVEKVQMLVKQDEEIVAEEVRIVEDYAQKTANELKSVLPAFDKAIVALNALDKADVAELRVYTRPPFLVLTVMNAVCILLQKKPNWATAKLLLSETGFLKKLINLDKDSIPDKVFVKLKKIVTLPDFNPHKISLVSVACCSLCQWVIALNNYHEVQKVVGPKQIQVAEAQNVLKIARQRLAEKQRGLQLISRWHNQGLPHGQYSVENAILIKNGQQWPLLIDPHRQAHKWIRQMEGSRLQKLSIEDSNYTKKIENAMKTGGSVLLQSCQASTWRKKLYLSTEIDNPHFLPSVYNFVTMINFTVTFQGLQDQLLSTVVTHEVPHLEDQRSKLLESISLDAITLEELEEKTLNLLQKALGSILDDDKIVDTLRKSKMTSNEISKRIEATKKAESEIQAIRKNYLPIATRGALLYFLVADLTQINYMYQFSLDWFHQVFVSSVVSKSKEQEHSFKREKVSPKEVHEFISISKEPNLENEKNLLDKHIKSAIDMLTKSIFKVVSSALFNEDKLCFSFRLCTVIMQNNANGNLIQDDIGFLPEEEWNIFLYSGILINIKSALSQSRLTSTFEIGESQHLQWLSDSRWRQCQYVSTHLEPFSLLCKSLLSNVSQWDTFKNSKAVYSLISTPFSSENASLEENTKPPEEKHTFCLLLRAINHTGTDLGPVGRGQWLTSTACDRHTDVCSFSFALNDGVPDVEHVQDIFYGHCVDKYHVKVLRPESLNNSVRKFITEKMGNKYLQRTGVNLKDAYKGSNARTPLILIQTHGSASIKDYIHIIQSLPDDDLPEVLGIHPEAIRSCWETQGEKFIENLIAMQPKTTTANLMIRPEQSKDELVMEILSDLLKRLPLTVEKEEIAVGTPSTLKSMMSSSIWESLSKNLKDHDPLIHCVLLTFLKQEIKRFDKLLFVIHKSLKDLQLAIKGEIILTQELEEIFNSFLNMRVPTLWQKHAYRSCKPLSSWIDDLIQRLNFFNTWAKVAYTAIQRRYMRFVTVWKQSIPSTSQKCKHPEDSENNFFEGFPSRYWLPAFFFPQAFLAAVLQDYGRSRGIAVDALTFTHHVISNTTDKDEKFSVFMPKKLNIVRRAFKGSASSHTGVYIFGLFIEGARWNREQKILEDSLPLEMCCDFPDIYFLPTKISTKTPNASNQTDSELYAFECPVYQTPERSRILATTGLPTNFLTSVYLSTKKPPSHWITMRVALLCEKNEK', 3507, 'Q0VDD8; A6NG62; A6NNL2; Q0VDD9; Q4VXC7; Q4VXG4; Q4VXG5; Q5VU33;Q5VU34;', 'KD01319', 'Homo sapiens (Human)', 'DNAH14', '#Dynein heavy chain 14; axonemal#Axonemal beta dynein heavy chain 14#Ciliary dynein heavy chain 14', '-', 'ENSG00000185842', '-'),
(1320, 'Q6FNH8', 'Probable kinetochore protein NUF2', 'GO:0000777', 54195, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MATPTQDIFPLLDLEELVICLQSCDFAMATEEHIARPTSQYVITLYKQIIENFMGISPEQVLAEQLSSRQNTEGNDESTSVDMFDGPYRETLQMLTLNKICYKFFENVGINDFNIVDLYKPEAYRTRRLLSAVVNYARFREERMFDCNQFIIQMEEMLDELKSKFDDFNYLKAQLTAIEDDDEKTPGELEDLLQKNKVLETNLKKLTILQEKLSIDYNNYKMKKQELLRELEKNSFTLIELESKKERLMNYNDDDQDLQNSLNNSIDRLTEEKKKQIGYVSKLEGNVSNLKVTVDTLEKAIEHIYDILRLLSTDLQESHRAELNIEGIKGPLTEKRTRLKNLLESNVIYKYDVLKEQLNVAETEYQRINEEHYRETLENKKLIQELEGKYNNIIHNKMQEAEVYIENEITEKKIKILQSELNDIQIQFNNEIDNIELHYSTLVGHINNYMKKLITALNNH', 460, 'Q6FNH8;', 'KD01320', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '2889456'),
(1321, 'P78966', 'Mating factor M secretion protein mam1', 'k', 150887, 'Required in S.pombe M (minus) cells for production of M- factor pheromone. Involved in the transport of the farnesyl- derivation of the M-factor pheromone.', 'MHIHSDLSLPQFEHASIDPPSYSPQKSSFEEKKHNFSITNKSLETLRSQESPCSTTFPVSDRKDALLNIPTVVDDEFQHTEELAGVSSWSDFFYLFHFSDIPLIFGTLIFTCLSAALEPLMTWTTGKVFDALSQYATSQITLGKMISLINFNSLLITIFGLASCVFSFGVRFLWQYLSAIAGKRARSLCFHVLSSKSSTFYSLTESKSGLVNSVDRCIQFYEKSISLPMFHIAENLAISLSCLIISFRYSWSLTLVVLASYPIIILVVGFINSFLSSAYEKDRKSSEKAASILEKSISAIQTVIFHSMQDTEYRYFADACSTSSKSFLRFSFLDAFQGGVSQFFLYSVFFQGLWFGNHLATTKRVNVGQVVTVFGSCLSVASSLQQILPAIPDLIKGKFSSHFIKTLCESHDPIEAAKRSAAKIKSISFERGFRFDNVSFAYPSRDENLFSLINVSVFIPFGELVHIIGPSGSGKSTFISLLLRYFSPTYGNIYLDDFPLEEIDEHVLGSTITLVCQQPVIFDMTIRENIIMRNENASESDFEEVCRLALVDEFALTFDQSYDTPCKEASLSGGQQQRIALARALLRDTEILILDEPTSALDPITKNLVMDAIRAHRKGKTTLVITHDMSQINNDELVLVIDKGHLIQRCARKELVLFEDFENNVSIDEKVLKEEADNPFILPNEESLLEKYWINYNESFSQLSRESLFTSLESPFTDIESPTIVSRRKIVEQRKLRMEKESFQETNVDQTFHLFDDKEHACSLTLIFKSIWKVKKLRWFFLLGLLTSLIQGASVPIFAYVISKCLNLFMQIDPSIGVAFWSSMVLVVAAGSGASYFFSHYIFSISAKIWCDHYRLLAVKVLFTQDQAWFDQIENYPLVLSKILVNNISDMRNMISSLIEEVFIAFTMAIIGIAWSFATGWRLAAVLVAVSPILCLTSRMFSYIYVSTERMCQDVVISTTSILHKTIVNLDTIKGYSVLSFFRENHKNSLRKSWEAFKRRAFWTSLGFAINNSLLYFVRALLFYCSSIFISKEFYTVEQMVQVLSLATFTLLMASTCIMSLPNVSASRIATSRVLKLSSLKPGNLHKSGYLKFPLVGKIEFDGVSFAYPDSERNHLALNNVSLSIEAREKVAIVGISGSGKSTLVELLRKTYPSEDIYIDGYPLTNIDTNWLLKKVAIVDQKPHLLGSTILESLLYGVDRDINSVMDALDKTYMTEVIQNLPNGLDTPLLEFSKNFSGGQIQRLAFARALLRNPRLLILDECTSALDSKSSLLLEKTIQNLSCTVLIITHQPSLMKLADRIIVMDSGIVKESGSFDELMNRHTHFWKLIHRGEWIE', 1336, 'P78966;', 'KD01321', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mam1', '#Mating factor M secretion protein mam1#Multiple drug resistance protein homolog#P-glycoprotein', '-', '-', '2540405');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1322, 'Q59S66', 'Spindle assembly checkpoint kinase', 'GO:0000777===GO:0032133===GO:0000780', 60408, '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}.', 'MMLPRNSPHRTESTLAYNNNNSNNNNNNNGSSLFQRKPLAPINSEFKISKPQHIKPNTHSHTFTTPTPKTRNTATTTTTNNNNRNNHQYRNPNLNTSLVFTPTKNSSSSSSSSHSSSLLSSSPFVEEPENQPESNHTRATSHYRTTSTSQYKSSANKDASHSLITSSKRKTSTKQTSESTNPKRRTTTTATQNTNNNKILNPSLSSSTIRFSTVSSSTSSSTTSSSSSSHTSPKPQQQLTLDDFEFGKILGKGKLGRVYCVKHKQSGLIFALKVMSKSEIMNLKLEKSLRREIEIQSNLYHINITRLYSWFHDSINIYLLLEYSIEGELYTHLKKLKRFDNIMASNYIFQITQALIFLHQRGIIHRDLKPENIMISLDNQLKLSDFGWSVQINQNQNQNQIHNQTQTQKTPHQKKQKQKRLTICGTLDYLPPEMIESKSHDFSVDIWALGILCYELLVGKPPFEAINRNITYEKIAKVDIKYPSNLDVDAIDLISKLVVKDPNKRLSLKEVLNHNWIIKNKPKWPKNIYK', 530, 'Q59S66;', 'KD01322', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'IPL1', '#Spindle assembly checkpoint kinase#2.7.11.1#Aurora kinase', '-', '-', '3645851'),
(1323, 'Q74ZG4', 'Tethering factor for nuclear proteasome STS1', 'GO:0061638', 35756, '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}.', 'MSQSVGFEWGFKAGGEGRPRAQGDGAGCAGATAAANSQQGCGHLVHMSYKVGKPKMKRRLTNEEHGGARRAKRQPAQFNVIQGQPLPVHRKIEMMDKAALQLTLLQLVAMHPEVQDSLSVLQPTSPDPAKYTELLEQKMQAVYDHIPYSKSSDMLNDYAFVRMKAAILEFLNCLIDCLLDAIPPRTTNLLQSFKFLAYGTRLLAQMPHFETESNNYYKNICYEQVSEIWNTLIRHASSDINFLSTKPSLLHYLHELKQFNEQTKGKFDIPLRLFYTIMDDYHTQTVPAAAAVASTSATVAEELNGNSKSMETLGIWNNVA', 320, 'Q74ZG4;', 'KD01323', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'STS1', '#Tethering factor for nuclear proteasome STS1', '-', '-', '4623211'),
(1324, 'Q75DE4', 'Histone H3-like centromeric protein CSE4', 'GO:0034501===GO:0000941', 23919, '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}.', 'MEQSMSSEQAERVAGRVEQLGGFQNNESINQRALLLLQRNRQRRQLLQRQEDRTRYIPDDAKRRVVERVAEPAAAESRADGAREEERAARPARPRETRRIAKKPQRYRPSDVALQEIRRYQRSTELLISRMPFARLVKEVTDQFTTVDQQMRWQSMAILALQEASEAYIVGLLEHTNLLALHAKRVTVMRKDMQLARRIRGQFI', 204, 'Q75DE4;', 'KD01324', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog', '-', '-', '4619133'),
(1325, 'P31383', 'Protein phosphatase PP2A regulatory subunit A', 'c;k;m', 70907, 'Phosphatase 2A affects a variety of biological processes in the cell such as transcription; cell cycle progression and cellular morphogenesis; and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct; albeit overlapping; subsets of substrates.', 'MSGARSTTAGAVPSAATTSTTSTTSNSKDSDSNESLYPLALLMDELKHDDIANRVEAMKKLDTIALALGPERTRNELIPFLTEVAQDDEDEVFAVLAEQLGKFVPYIGGPQYATILLPVLEILASAEETLVREKAVDSLNNVAQELSQEQLFSDFVPLIEHLATADWFSSKVSACGLFKSVIVRIKDDSLRKNILALYLQLAQDDTPMVKRAVGKNLPILIDLLTQNLGLSTDEDWDYISNIFQKIINDNQDSVKFLAVDCLISILKFFNAKGDESHTQDLLNSAVKLIGDEAWRVRYMAADRFSDLASQFSSNQAYIDELVQPFLNLCEDNEGDVREAVAKQVSGFAKFLNDPSIILNKILPAVQNLSMDESETVRSALASKITNIVLLLNKDQVINNFLPILLNMLRDEFPDVRLNIIASLKVVNDVIGIELLSDSLLPAITELAKDVNWRVRMAIIEYIPILAEQLGMQFFDQQLSDLCLSWLWDTVYSIREAAVNNLKRLTEIFGSDWCRDEIISRLLKFDLQLLENFVSRFTILSALTTLVPVVSLDVVTEQLLPFISHLADDGVPNIRFNVAKSYAVIVKVLIKDEAKYDALIKNTILPSLQTLCQDEDVDVKYFAKKSLAECQELLKN', 635, 'P31383; D6VPK2;', 'KD01325', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'TPD3', '#Protein phosphatase PP2A regulatory subunit A#PR65', '-', '-', '851217'),
(1326, 'O13024', 'Inner centromere protein A', 'GO:0032133===k', 101199, '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. {ECO:0000269|PubMed:12221116; ECO:0000269|PubMed:17199039}.', 'MNDAECLSHLLQVCARKTEEFVRTLDSKHMVWLLEIEEEARKMFSSDFNAEPELMPKTPSQKRRRKKRTSILPDENRDPSGRRISRRQSNASWSSSVRRLSVRNQNKANDDSIQEEPAQLKRMTRARAQASIKSTPVLETALPESPSQICQKNAQVKISEQERRSAEQKLIESDFELKTVPEITKDNVSETVNSAVPAVPVTPENKSRAAGKLKIAASSTPEQKAEMVDLTCESPRPANEQQLNLSNQSATPTGSKSDRRSVRRSLVVRKSSSRRASLASQFSLASKRESMTREAVRKSIRQSISQKKAAMEISSTSSQRSYQSSIEMVDDEITIKIRPETVPSETVSEEAPAAESPRRSLRSRAFKKIAISNLPDSEEPPRKVTRQMVAGNAEPTPETTEDAQNIRRKSYKRAVDELSDDERPSEEERSPPRKKTPSPPCPPSKIVRPPPHMKSFLHTVQKNQLLMMTPGSIGKNIIMKSFIKRNTPLKTDPKTEEKERQRLDALRKKEEAELQRKQKIEEGKKRKQEELKVRREERLRKVLQARERVEQLEEEKKKKIEQKFAQIDEKSEKVREDRMAEEKAKKKMTAKKQEEVECRRKQEEEARRLKVKQMEEEERRHQELLQKKREEEELERQKKIAEAKRLAEQERERQLLAEKERLRAEREKERIEKEKALQLQRELERAAQEKEQQRREAEERKKREQQERLEQERLRKEQEAKRLQEEEQRKAKEQAAVAASAPVMNVTVDMQNSPACESYEMTPKSCKVPSVKVNEDNYGMDLNSDDSTDDESQPRKPIPAWASGNLLTQAIRQQYYKPIDVDRMYGTIDSPKLEELFNKSKPRYFKRTSSAVWHSPPLSSNRHHLAVGYGLKY', 873, 'O13024; Q4V878; Q7ZXJ9;', 'KD01326', 'Xenopus laevis (African clawed frog)', 'incenp-a', '#Inner centromere protein A#XL-INCENP#xINC#xIncenp#Mitotic phosphoprotein 130', '-', '-', '398105'),
(1327, 'Q75DE8', 'DASH complex subunit ASK1', 'GO:0008608===GO:0051987===GO:0042729', 19596, '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}.', 'MARQPPAPEPTLEQLDQEITLQLQKIDANLSACFSKITKDIIPAVARYGAVCDDALSACSWLRELFQKSSDIQLATEPAAPAPAAESLFPQAPAPRAPEVTTEGHVLAVPVSSDDEPDDGSTLQRQHKRRKLSLQLQQRYGSSSSSSFVSRSPTLRTRPASSPLRAPDDPDPPAVLRFAAR', 181, 'Q75DE8;', 'KD01327', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'ASK1', '#DASH complex subunit ASK1#Associated with spindles and kinetochores protein 1#Outer kinetochore protein ASK1', '-', '-', '4619129'),
(1328, 'Q9LU93', 'Mitotic spindle checkpoint protein MAD2', 'GO:0000776===GO:0000777===GO:0005828===SCL===k;s', 23731, 'Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and delays the onset of anaphase when this process is not complete. It inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. {ECO:0000269|PubMed:19710914}.', 'MASKTAAAKDIITLHGSAAIVSEFFCYAANSILYNRAVYPEESFVKVKKYGLPMLLIEDESVKSFMSNLTSQISEWLEAGKLQRVVLVIMSKATGEVLERWNFRIETDNEVVDKGVSREKSDKEIMREIQAIMRQVASSVTYLPCLDETCVFDVLAYTDTDVAVPFTWIESDPKLIANPQMVKLHGFDTKIHKVDTLVSYKNDEWDEEE', 209, 'Q9LU93; Q67YV5;', 'KD01328', 'Arabidopsis thaliana (Mouse-ear cress)', 'MAD2', '#Mitotic spindle checkpoint protein MAD2 {ECO:0000303|PubMed:19710914}#Mitotic arrest deficient protein 2', '-', '-', '822195'),
(1329, 'Q16181', 'Septin-7', 'GO:0000777===SCL', 50680, '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. {ECO:0000269|PubMed:17803907; ECO:0000269|PubMed:18460473}.', 'MSVSARSAAAEERSVNSSTMVAQQKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKIF', 437, 'Q16181; Q52M76; Q6NX50;', 'KD01329', 'Homo sapiens (Human)', 'SEPT7', '#Septin-7#CDC10 protein homolog', '-', 'ENSG00000122545', '-'),
(1330, 'Q16695', 'Histone H3.1t', 'k', 15508, 'Core component of nucleosome. 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.', 'MARTKQTARKSTGGKAPRKQLATKVARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLMREIAQDFKTDLRFQSSAVMALQEACESYLVGLFEDTNLCVIHAKRVTIMPKDIQLARRIRGERA', 136, 'Q16695; B2R5K3; Q6FGU4;', 'KD01330', 'Homo sapiens (Human)', 'HIST3H3', '#Histone H3.1t#H3/t#H3t#H3/g', '-', 'ENSG00000168148', '-'),
(1331, 'P37276', 'Dynein heavy chain; cytoplasmic', 'GO:0000776===GO:0034501===GO:0003777===GO:0005868', 530184, '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.', 'MGDSLENPDTSVDPIVNLSIANYDAFANYLRKAVTILLPEDDVVPASLNDALDDPVNQDTIRKFLSDPQVQALYVQRNCIKEDDSEQPAEGEDEKEQVTYQISNDVHFTNSRMASLACIKRGLVVEADKSIHSQLRLINFSDGSPYETLHAFISKSLAPYFKSYVKESGRADRDGDKMAPSVEKKLAELEMGLLHLQQNIDIPEITLTAHQTVNNVIRKCAEENRKAKVADFGDKVEDSSFLNLLQNGVNRWIAEIKKVTKLNRDPGSGTALQEISFWLNLERALYRIQEKRESPEVALTLDILKHGKRFHATVSFDTDTGLKQALATVADYNPLMKDFPINDLLSATELEKIRPAVQQIFAHLRKVRNTKYPIQRCLKLIEAISRDLSQQLLKVLGTRRLMHIPFDEFERVMNQCFEIFSCWDDEYDKLQGLLRDIVKKKRDEHLKMVWRVSPAHKKLQTRMEHMRKFRRQHEQLRTVILRVLRPTKPAVGDDGNVVETKQPYSLDAADANAIEEVNLAYENVKEVDCLDITKEGSEAWEAAVKRYEEKIDRVETRITAHLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIEALHEKFKVQYPQSKSCRLSSVRDLPPVAGSIIWARQIDNQLTMYLKRVEDVLGKGWETHIEGQKLKADGDSFRAKLSISDVFHEWARKVQERNFGSTGRIFTIESTRSRIGRGNVLRLRVNFLPEIITLAKEVRNIKNLGFRVPLTIVNKAHQANQIYPYAISLIESVRTYERTLEKIEDRASIVPLVAGLRKDVLNLVSEGIGLIWESYKLDPYVIRLSECVTQFQEKVDDLLVVEEQLDVDVRSLETCPYSAATFVEILSKIQHAVDDLSLRQYSNLSVWVTRLDEEVEKKLALRLQAGIQAWTEALTGNKKEVDTSMDTDAPAQPTHKLGGDPQIQNAVHEIRITNQQMYLYPSIEEARFQIMQQFFAWQAIVTSQVRLQSTRYQVGLEKHVSQTYRNLLTKLPEGKILENAYGAIEQKVSEVRNYVDEWLRYQSLWDLQADMLYGRLGEDVNLWIKCLNDIKQSRTTFDTSDTRRAYGPIIIDYAKVQAKVTLKYDSWHKEALGKFGTLLGTEMTSFHSKVSKSRTDLEMQSIEAASTSDAVSFITYVQSLKKDMIAWDKQVEVFREAQRILERQRFQFPNTWLHVDNIEGEWSAFNEIIKRKDTAIQTQVASLQAKIVAEDKAVETRTVDFLNDWEKTKPTGGKIRPDDALQQLQIFESKYSRLKEERDNVVKAKEALELQESAVPNNSAERMNVALEELQDLRGVWSELSKVWTQIDETREKPWLSVQPRKLRQQLEAMMAQLKELPARLRMYESYEYVKKLIQSYIKVNMLIVELKSDALKERHWKQLTKQLRVNWVLSDLSLGQVWDVNLQKNEGIVKDIILVAQGEMALEEFLKQVRESWQNYELDLINYQNKCRIIRGWDDLFNKVKEHINSVAAMKLSPYYKVFEEEALTWEEKLNRINALFDVWIDVQRRWVYLEGIFSGSADIKTLLPVETSRFQSISSEFLGLMKKVTKSPKVMDVLNIPAVQRSLERLADLLGKIQKALGEYLERERTSFPRFYFVGDEDLLEIIGNSKNIARLQKHFKKMFAGVAAILLNEENNVILGISSREGEEVHFMNPVSTVEHPKINEWLSLVEKQMRFTLASLLAQAVQDIKQFRDGKIDPQAYMEWCDKYQAQIVVLAAQILWSEDVESALQQASENNQSKPMQRVLGNVESTLNVLADSVLQEQPPLRRRKLEHLINEFVHKRTVTRRLLNNGVTSPKSFQWLCEMRFYFDPRQTEVLQQLTIHMANARFFYGFEYLGVQDRLVQTPLTDRCYLTMTQALESRLGGSPFGPAGTGKTESVKALGNQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSACSQQIQTIQEALKYEMDSNKESITVELVGKQVRVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTTPDRQLIAEVMLFSQGFRSAEKLACKIVPFFKLCDEQLSNQSHYDFGLRALKSVLISAGNVKRDRIMKIKEQMKQRGDENIDEASVAENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPNVGYTRAEMKGLKEEIRKVCQEDYLVCGEGDEQGAAWMEKVLQLYQISNLNHGLMMVGPSGSGKSTAWKTLLKALERFEGVEGVAHVIDPKAISKEALYGVLDPNTREWTDGLFTHILRKIIDNVRGEINKRQWIIFDGDVDPEWVENLNSVLDDNKLLTLPNGERLSLPPNVRVMFEVQDLKFATLATVSRCGMVWFSEDVLSTEMIFENYLSRLRSIPLEDGDEDFVGVIKPAKDKEEEVSPSLQVQRDIALLLLPFFSADGIVVRTLEYAMDQEHIMDFTRLRALSSLFSMLNQAARNVLTFNAQHPDFPCSADQLEHYIPKALVYSVLWSFAGDAKLKVRIDLGDFVRSVTTVPLPGAAGAPIIDYEVNMSGDWVPWSNKVPVIEVETHKVASPDIVVPTLDTVRHESLLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQIGKWLVLFCDEINLPDMDSYGTQRVISFLRQLVEHKGFYRASDQAWVSLERIQFVGACNPPTDPGRKPLSHRFLRHVPIIYVDYPGETSLKQIYGTFSRAMLRLMPALRGYAEPLTNAMVEFYLASQDRFTQDMQPHYVYSPREMTRWVRGICEAIRPLDSLPVEGLVRLWAHEALRLFQDRLVDDSERRWTNENIDLVGQKHFPGINQEEALQRPILYSNWLSKDYMPVNREELREYVHARLKVFYEEELDVPLVLFDEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNKYTSEDFDEDLRCVLRRSGCKDEKIAFILDESNVLDSGFLERMNTLLANGEVPGLFEGDEYTTLMTQCKEGAQREGLMLDSSDELYKWFTQQVMRNLHVVFTMNPSTDGLKDRAATSPALFNRCVLNWFGDWSDSALFQVGKEFTTRVDLEKPNWHAPDFFPSVCPLVPANPTHRDAVINSCVYVHQTLHQANARLAKRGGRTMAVTPRHYLDFIHHFVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVKSIRKQQLVEVRTMANPPSVVKLALESICLLLGENATDWKSIRAVIMRENFINSIVSNFGTENITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIGDVLLSAAFIAYGGYFDQHYRLNLFTTWSQHLQAASIQYRADIARTEYLSNPDERLRWQANALPTDDLCTENAIMLKRFNRYPLIIDPSGQATTFLLNEYAGKKITKTSFLDDSFRKNLESALRFGNPLLVQDVENYDPILNPVLNRELRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDICSRVTFVNFTVTRSSLQSQCLNQVLKAERPDIDEKRSDLLKLQGEFRLRLRQLEKSLLQALNDAKGKILDDDSVITTLETLKKEAYDINQKVDETDKVIAEIETVSQQYLPLSVACSNIYFTMDSLNQVHFLYQYSLKMFLDIFSTVLYNNPKLEGRTDHSERLGIVTRDLFQVCYERVARGMIHIDRLTFALLMCKIHLKGTSESNLDAEFNFFLRSREGLLANPTPVEGLSAEQIESVNRLALRLPIFRKLLEKVRSIPELGAWLQQSSPEQVVPQLWDESKALSPIASSVHQLLLIQAFRPDRVIAAAHNVVNTVLGEDFMPNAEQELDFTSVVDKQLNCNTPALLCSVPGFDASGRVDDLAAEQNKQISSIAIGSAEGFNQAERAINMACKTGRWVLLKNVHLAPQWLVQLEKKMHSLQPHSGFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGIRANLLRTFSTVPAARMMKTPSERARLYFLLAWFHAIVQERLRYVPLGWAKKYEFNESDLRVACDTLDTWIDTTAMGRTNLPPEKVPWDALVTLLSQSIYGGKIDNDFDQRLLTSFLKKLFTARSFEADFALVANVDGASGGLRHITMPDGTRRDHFLKWIENLTDRQTPSWLGLPNNAEKVLLTTRGTDLVSKLLKMQQLEDDDELAYSVEDQSEQSAVGRGEDGRPSWMKTLHNSATAWLELLPKNLQVLKRTVENIKDPLYRYFEREVTSGSRLLQTVILDLQDVVLICQGEKKQTNHHRSMLSELVRGIIPKGWKRYTVPAGCTVIQWITDFSNRVQQLQKVSQLVSQAGAKELQGFPVWLGGLLNPEAYITATRQCVAQANSWSLEELALDVTITDAGLKNDQKDCCFGVTGLKLQGAQCKNNELLLASTIMMDLPVTILKWIKISSEPRISKLTLPVYLNSTRTELLFTVDLAVAAGQESHSFYERGVAVLTSTALN', 4639, 'P37276; Q8IRA5; Q961M8; Q9VZ83;', 'KD01331', 'Drosophila melanogaster (Fruit fly)', 'Dhc64C', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC', '-', '-', '38580'),
(1332, 'Q9VQS4', 'Spindly', 'k', 88609, '', 'MYKNLDLDTLSVDDIVEEYKLLHDRHQQLKDQSEKDAQRIYELKRNLDTALAAESYLTQELEHLSSQPVAIASGGNGQELEELRRKFKTLKEEQDVLQQDYDAKVEETRSLKDKLTAAEKNLAEKSASRSNQLHDDFFARLNALELENCELLQKLAEYEDLRIANTLAVAEKEKTIECLQDRVSCMEQNLNCKRDELEEKLQLLESCQEQLVDANAKIALLTSAPENNDRKGNSLFAEVDDQRQAMKQILAAQKKSYLDMKKIFTDSQFEIRRLKRENVAMHTELQACSTIFCSADKTYQNKLNERIRQLMTANDSLERQLNLSQERLRQLASEKSVTWLDSMLDFCKRETDELKAQLHSMRIQKAGLEERMRCVQQEMARWRFESLKSRCVLIDRENLLAEHKIVFKPMQAMEFNIKEAELKTALPRIVSVAAQSPSSSAQLHTHPETSLKSAAETTSKSFPTATEIIVLDAPLKPAIKEEVVEPLSQELKPALKDTSVKVEQELEVSESKACIKRTPIKTIMGMKIKREIDLNLEQQDAVDIKKELEAPELIPKPQLKGTPVKAKNDGVTPQMNIQEDENEETGLNSVETPAKPLMKGTPVKQRLGGIKVKSNEELLGARLPGTVTPAKPQRKGTPVKLIKLETETEDSSDEAAKESPIKQDGTLSVEILDSPTPQKPQRKGTPVRIPVIKDSTNENIRSILSKKRQVFAEDSQKAVKFSANDPIVHNLSPLERCPNGETTKENDKPKESEDNQDVKPTIKKPNIIRRIVVSSRKPIMK', 781, 'Q9VQS4;', 'KD01332', 'Drosophila melanogaster (Fruit fly)', 'Spindly', '#Spindly {ECO:0000313|EMBL:AAF51090.2}', '-', '-', '33578'),
(1333, 'O43670', 'BUB3-interacting and GLEBS motif-containing protein ZNF207', 'GO:0000776===GO:0000777===GO:0008608', 50751, '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: according to a first report; ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3 (PubMed:24462186). According to another report; the stabilization is independent of the proteasome (PubMed:24462187). {ECO:0000269|PubMed:24462186; ECO:0000269|PubMed:24462187}.', 'MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDERRRLLEQKTQESQKKKQQDDSDEYDDDDSAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTATVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKALFPSTAQAQAAVQGPVGTDFKPLNSTPATTTEPPKPTFPAYTQSTASTTSTTNSTAAKPAASITSKPATLTTTSATSKLIHPDEDISLEERRAQLPKYQRNLPRPGQAPIGNPPVGPIGGMMPPQPGIPQQQGMRPPMPPHGQYGGHHQGMPGYLPGAMPPYGQGPPMVPPYQGGPPRPPMGMRPPVMSQGGRY', 478, 'O43670; A8K6Y6; E1P660; E1P661; E1P662; Q53XS9; Q96HW5; Q9BUQ7;', 'KD01333', 'Homo sapiens (Human)', 'ZNF207', '#BUB3-interacting and GLEBS motif-containing protein ZNF207#BuGZ#Zinc finger protein 207', '-', 'ENSG00000010244', '-'),
(1334, 'O88846', 'E3 ubiquitin-protein ligase RNF4', 'GO:0090234', 21897, '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:11319220; ECO:0000269|PubMed:14987998; ECO:0000269|PubMed:15707587; ECO:0000269|PubMed:18408734; ECO:0000269|PubMed:20943951; ECO:0000269|PubMed:9710597}.', 'MSTRNPQRKRRGGAVNSRQTQKRTRETTSTPEISLEAEPIELVETVGDEIVDLTCESLEPVVVDLTHNDSVVIVEERRRPRRNGRRLRQDHADSCVVSSDDEELSKDKDVYVTTHTPRSTKDEGTTGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI', 194, 'O88846;', 'KD01334', 'Rattus norvegicus (Rat)', 'Rnf4', '#E3 ubiquitin-protein ligase RNF4#6.3.2.-#RING finger protein 4#Small nuclear ring finger protein#Protein SNURF', '-', '-', '29274'),
(1335, 'P45970', 'Spindle apparatus protein lin-5', 'GO:0000777===GO:0005828===SCL===c;k', 93440, 'Essential component of the spindle apparatus required for spindle positioning and chromosome movement. Acts to recruit or anchor gpr-1/gpr-2 complex to the spindle and cortex. Also involved; directly or indirectly; in cytokinesis and in the coupling of DNA replication; centrosome duplication and mitotic division. {ECO:0000269|PubMed:10629219; ECO:0000269|PubMed:12730122}.', 'MSVSTSVVKSMLQLTNYFGSNFTPKTETISSLAELWERHGSMIASMMSCDTREFGTADKFYEVIFRKIATTSLSFMTDSLEPKLAASGDSLEICKFYALFLEYMRKDHSGMLTRALEQASSENRVDTAVLLDMFLFFDNVYSESTADDWWACLRRDDEDQEASSGFRTPKRNNYSLTSLQTPTATARRLRTASSTARRSPIAEAVDSPTMKFMRSERELKQSKARIFGLEQMLGDLEDDKTKLSAENRTLKLSNSDLKSDIAKLKGIAEEAQFRAEELSCDLEAKKDEVHNILQQLNESRMTLRSEQRSLEEADIKKENLTAKLKTVTEDNGKLMKQARELRDLNDYEFARFRQQEQELTETLRATQDQMADLQEQLTGVEKIRASLKSENESLSASVEELSVASLRNKQDADNSKTMLSEELARFEETVDKLRQEKLEALSMANSRIDALRLEHSEREKMMKSTNARLQADLDEERNEKKRLMNLWNELNEKSLNVDKAVHKSNEEFQSMGSCLQNAKRQIEQLEVACKSKDDIIKFQEEQNKRAANLIKNEKAIRDQASAQFAEKLAILKNSLAEKENETVTLKENFASVVMKHKAELEEKELFLQSRVDLIQRLEHEVADLREKESAEIKKSTWMGERIKIFQQAPMRGSRIRCGSPDSLPDFLADNGPTITEEELRAQLATFPRKSIAPSVDDNEFDKGTPIGFKSNMYDGRESICSLDFFDRSSLQRSSMRSESIQLASPSSAGEFKQPFTPSGVTKERVGVLTARNEKVKPHLKCSYASEVGSTNSPSADEENIKKSKKKNRRDSIFSAFSSKKQ', 821, 'P45970;', 'KD01335', 'Caenorhabditis elegans', 'lin-5', '#Spindle apparatus protein lin-5#Abnormal cell lineage protein 5', '-', '-', '174267'),
(1336, 'B8NSJ0', 'E3 ubiquitin ligase complex SCF subunit sconC', 'GO:0051382===GO:0031518', 18465, 'Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes; which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression; probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}.', 'MATPTLTFTSSDGVDIPVERDVAERSQLIKNMLEDLGETGEPIPIPNVNEAVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKGLLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEDR', 161, 'B8NSJ0;', 'KD01336', 'Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JC12722 / SRRC 167)', 'sconC', '#E3 ubiquitin ligase complex SCF subunit sconC#Sulfur controller C#Sulfur metabolite repression control protein C', '-', '-', '7911670'),
(1337, 'P45975', 'Histone-lysine N-methyltransferase Su(var)3-9', 'k', 71904, 'Histone methyltransferase that specifically trimethylates ''Lys-9'' of histone H3 using monomethylated H3 ''Lys- 9'' as substrate. H3 ''Lys-9'' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting Su(var)205/HP1 to methylated histones. Mainly functions in heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin at pericentric regions. Involved in heterochromatic gene silencing including the modification of position-effect-variegation. {ECO:0000269|PubMed:14630943}.', 'MATAEAQIGVNRNLQKQDLSNLDVSKLTPLSPEVISRQATINIGTIGHVAHGKSTVVKAISGVQTVRFKNELERNITIKLERLSEKKIKNLLTSKQQRQQYEIKQRSMLRHLAELRRHSRFRRLCTKPASSSMPASTSSVDRRTTRRSTSQTSLSPSNSSGYGSVFGCEEHDVDKIPSLNGFAKLKRRRSSCVGAPTPNSKRSKNNMGVIAKRPPKGEYVVERIECVEMDQYQPVFFVKWLGYHDSENTWESLANVADCAEMEKFVERHQQLYETYIAKITTELEKQLEALPLMENITVAEVDAYEPLNLQIDLILLAQYRAAGSRSQREPQKIGERALKSMQIKRAQFVRRKQLADLALFEKRMNHVEKPSPPIRVENNIDLDTIDSNFMYIHDNIIGKDVPKPEAGIVGCKCTEDTEECTASTKCCARFAGELFAYERSTRRLRLRPGSAIYECNSRCSCDSSCSNRLVQHGRQVPLVLFKTANGSGWGVRAATALRKGEFVCEYIGEIITSDEANERGKAYDDNGRTYLFDLDYNTAQDSEYTIDAANYGNISHFINHSCDPNLAVFPCWIEHLNVALPHLVFFTLRPIKAGEELSFDYIRADNEDVPYENLSTAVRVECRCGRDNCRKVLF', 635, 'P45975; Q9VFA6;', 'KD01337', 'Drosophila melanogaster (Fruit fly)', 'Su(var)3-9', '#Histone-lysine N-methyltransferase Su(var)3-9#2.1.1.43#Histone H3-K9 methyltransferase#H3-K9-HMTase#Lysine N-methyltransferase 1#Protein suppressor of variegation 3-9', '-', '-', '41483'),
(1338, 'P45973', 'Chromobox protein homolog 5', 'GO:0000776===k', 22225, 'Component of heterochromatin that recognizes and binds histone H3 tails methylated at ''Lys-9'' (H3K9me); leading to epigenetic repression. In contrast; it is excluded from chromatin when ''Tyr-41'' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. {ECO:0000269|PubMed:19783980}.', 'MGKKTKRTADSSSSEDEEEYVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSESNKRKSNFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKETAKS', 191, 'P45973; B2R8T9;', 'KD01338', 'Homo sapiens (Human)', 'CBX5', '#Chromobox protein homolog 5#Antigen p25#Heterochromatin protein 1 homolog alpha#HP1 alpha', '-', 'ENSG00000094916', '-'),
(1339, 'Q5R481', 'Septin-7', 'GO:0000777', 50680, '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}.', 'MSVSARSAAAEERSVNSSTMVAQQKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKIF', 437, 'Q5R481; Q5R4Y5; Q5R8T4;', 'KD01339', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'SEPT7', '#Septin-7', '-', '-', '100173884'),
(1340, 'Q7TQ72', 'Protein MIS12 homolog', 'GO:0000777', 24161, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis. {ECO:0000250}.', 'MSVDPMAYEAQFFGFTPQTCLLRIYIAFQDHLFEVMQAVEQVILKKLEGIPDCEISSIQTRKCTEKFLCFMKGRFDNLFGKMEQLILQSILQIPPNILLPEDKCQETNPFSEEKFQLLKQEIKELQEKYKVELCTEQALLAELEEQKTVKAKLRETLTFFDELENIGRYQGTSNFRESLVSLVQNCRKLQDIRDNVEKEGKRLETQ', 206, 'Q7TQ72;', 'KD01340', 'Rattus norvegicus (Rat)', 'Mis12', '#Protein MIS12 homolog#Liver regeneration-related protein LRRG112', '-', '-', '501706'),
(1341, 'Q9R1T4', 'Septin-6', 'GO:0000777', 49620, 'Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis.', 'MAAADIARQVGEDCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVGLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHSYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPVIAKSDAISKSELAKFKIKITSELVSNGVQIYQFPTDDESVSEINGTMNAHLPFAVVGSTEEVKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHARHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQEEKKKLEDKKKCLDEEMNAFKQRKAAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCIE', 434, 'Q9R1T4; A2A3V9; A2A3W0; Q3TRH9; Q3TUA2; Q542H3; Q6A0C4; Q8C2L2;Q8C848; Q91XH2; Q9CZ94;', 'KD01341', 'Mus musculus (Mouse)', 'Sept6', '#Septin-6', '-', '-', '56526'),
(1342, 'Q59VQ3', 'Spindle assembly checkpoint component MAD2', 'GO:0000776', 24540, 'Central component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Plays a key role in virulence; probably through cell cycle checkpoint functions; especially those monitoring the integrity of DNA and chromosome segregation; which might be required for the pathogen to repair damage caused by host defense. {ECO:0000269|PubMed:12100546}.', 'MPSSLEPSSKLALKGSSKIVCDYFEFALNSILYQRGIYPQEDFVTVKKYDLPMVINDDYDVQKYINNIMKQIKKWIYGSLMSKFIIVIVSKTNLENIERWEFNIETKDQEETTENGDGDGDGVGKSRQEIQKEIRTIIRQITSSVSYLPVLKDDDEYTFNVLVYTDPNTSVPIEWCDTQGDGKVLDGDNVDNVKFTSFSTDIHQVGTSVSYKYE', 214, 'Q59VQ3; Q59VU9;', 'KD01342', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'MAD2', '#Spindle assembly checkpoint component MAD2 {ECO:0000303|PubMed:12100546}', '-', '-', '3644665'),
(1343, 'O74689', 'Nuclear distribution protein nudE', 'GO:0000776', 64640, 'Required for nuclear migration within hyphae during vegetative growth. {ECO:0000269|PubMed:12631710; ECO:0000269|PubMed:16467375}.', 'MPSADEPSSTRTNGTSSRSDQLAYYKKQYEQLESELADFQASSRELEAELEKEIEASEKRERQLKEKVDNLRYEVEEWKSKYKQSKSEASTAQNALQKEITSLRDANLTLQLKLRDTEVANDDYERQARHTTSSLEDMESKYNQALEREVLLDMEYKQGEQERESLRIENQRLRDELNDLKIETEIVQERLRNNNRRRRPAPLGRSPSTPHTPEIFDRSPGESTVSSPLFSTPPTKLSLTLASATATPPSPPMSETSSSMRKSLTAASGFPLQKASASESFGTRSLYGNRPQRFQAHSRATSYAFSNGRSTPSATTTRPSLPKANNTTANRPSGIPKSGSLHQIRGLIGKMQKLEERVQSAKSKLPPPSETASRASSRAGSMLDASPGAATIAMRRDTRKRLSGSSFSSSVRDGDGAPSYVTSSRPSYGTRTQGDSRPSSRTSFSSSLSHSTHPSVTPSNRPESRQSRTKTPLGHYSTNPTTESRRPRSSLSNPAGQSTPINGMTYIDEDEDLAEQFNMRATISSTRPTRLPSFSNPAFSTPTGLKKRSTSGMSGIPAPRTLRRGNTMGPPKTKPKPVAGDLGETF', 586, 'O74689; C8V2D2; Q5B005;', 'KD01343', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'nudE', '#Nuclear distribution protein nudE', '-', '-', '2871059'),
(1344, 'O43684', 'Mitotic checkpoint protein BUB3', 'GO:0000776===GO:0000777===GO:0008608===k', 37155, '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. {ECO:0000269|PubMed:10198256; ECO:0000269|PubMed:15525512; ECO:0000269|PubMed:18199686}.', 'MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMVTGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAETKPKSPCT', 328, 'O43684; A6NJ42; B2R6E7; D3DRE9; O43685;', 'KD01344', 'Homo sapiens (Human)', 'BUB3', '#Mitotic checkpoint protein BUB3', 'BIOMD0000000186,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Dissociation variant;BIOMD0000000187,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Convey variant;BIOMD0000000193,Ibrahim2008_MCC_assembly_model_KDM;', 'ENSG00000154473', '-'),
(1345, 'Q24JY3', 'Kinetochore protein Spc24', 'GO:0000777===GO:0031262', 22756, '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}.', 'MAAFRDMEEVSQGLLSLLGANRAEAQQRRLLGRHEQKVERLLETQDGAEKWLREILTTEKEVAQRLLDAKEQAHQGGVEVRQLEAELQRASEEDAHLKANLLQLTRELEELKEIEADLERQEKEVDEDTTVTIPSAVYVAQLYRRISKIEWDYECEPGMIKGIHHGPSVAQPIHLDSTQLSKKFISDYLWNLVDTEW', 197, 'Q24JY3;', 'KD01345', 'Bos taurus (Bovine)', 'SPC24', '#Kinetochore protein Spc24', '-', '-', '509117'),
(1346, 'O43683', 'Mitotic checkpoint serine/threonine-protein kinase BUB1', 'GO:0000776===GO:0000777===GO:0000780===k', 122375, 'Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore; being required for the subsequent localization of CENPF; BUB1B; CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Plays an important role in defining SGOL1 localization and thereby affects sister chromatid cohesion. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of 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. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. {ECO:0000269|PubMed:10198256; ECO:0000269|PubMed:15020684; ECO:0000269|PubMed:15525512; ECO:0000269|PubMed:15723797; ECO:0000269|PubMed:16760428; ECO:0000269|PubMed:17158872; ECO:0000269|PubMed:19487456}.', 'MDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTETHLPAQARTSEPLHNVQVLNQMITSKSNPGNNMACISKNQGSELSGVISSACDKESNMERRVITISKSEYSVHSSLASKVDVEQVVMYCKEKLIRGESEFSFEELRAQKYNQRRKHEQWVNEDRHYMKRKEANAFEEQLLKQKMDELHKKLHQVVETSHEDLPASQERSEVNPARMGPSVGSQQELRAPCLPVTYQQTPVNMEKNPREAPPVVPPLANAISAALVSPATSQSIAPPVPLKAQTVTDSMFAVASKDAGCVNKSTHEFKPQSGAEIKEGCETHKVANTSSFHTTPNTSLGMVQATPSKVQPSPTVHTKEALGFIMNMFQAPTLPDISDDKDEWQSLDQNEDAFEAQFQKNVRSSGAWGVNKIISSLSSAFHVFEDGNKENYGLPQPKNKPTGARTFGERSVSRLPSKPKEEVPHAEEFLDDSTVWGIRCNKTLAPSPKSPGDFTSAAQLASTPFHKLPVESVHILEDKENVVAKQCTQATLDSCEENMVVPSRDGKFSPIQEKSPKQALSSHMYSASLLRLSQPAAGGVLTCEAELGVEACRLTDTDAAIAEDPPDAIAGLQAEWMQMSSLGTVDAPNFIVGNPWDDKLIFKLLSGLSKPVSSYPNTFEWQCKLPAIKPKTEFQLGSKLVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLVGELYSYGTLLNAINLYKNTPEKVMPQGLVISFAMRMLYMIEQVHDCEIIHGDIKPDNFILGNGFLEQDDEDDLSAGLALIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLPHLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRLIVLLLECKRSRK', 1085, 'O43683; E9PC26; F5GXI5; O43430; O43643; O60626; Q53QE4;', 'KD01346', 'Homo sapiens (Human)', 'BUB1', '#Mitotic checkpoint serine/threonine-protein kinase BUB1#hBUB1#2.7.11.1#BUB1A', '-', 'ENSG00000270778', '-'),
(1347, 'P37285', 'Kinesin light chain 1', 'GO:0003777', 63745, '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. {ECO:0000269|PubMed:19861499}.', 'MHDNMSTMVYMKEEKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSSMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDSDSSKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGSSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAALRSRKQGLDNVHKQRVAEVLNDPENVEKRRSRESLNVDVVKYESGPDGGEEVSMSVEWNGMRKMKLGLVK', 560, 'P37285;', 'KD01347', 'Rattus norvegicus (Rat)', 'Klc1', '#Kinesin light chain 1#KLC 1', '-', '-', '171041'),
(1348, 'Q24141', 'Shugoshin', 'GO:0000780===k', 44402, 'Plays a central role in chromosome cohesion during meiosis and mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase; when most of cohesin complex dissociates from chromosomes arms. May act by protecting or Rad21 from cleavage by Sse/separase. Required during meiosis in both males and females. {ECO:0000269|PubMed:10654079; ECO:0000269|PubMed:7585942; ECO:0000269|PubMed:9490715; ECO:0000269|PubMed:9869638}.', 'MGSKVEQQYKLLNAELMDQVQKQRLEIGEYRKRVISLEREIMDIREEHVLQNHRQRMENISIVRSLMLSLNVDSDSLAVRQEPAPAAQINRPSGPRRSSREICKDMRRTCALARTTRPISPRRSSSVTSTVSSTSRRSSAEVQSEVVTTRIPEDRRANKPTPPPRRPAELVFDEDDSDDDFDEAVSPVEETQTEQNEENNRLFSIIEENGSEGESTDSSSSCEAIYCDTTFESSPPNAQVTVTPSGRALREVDTNIPVAVSLSRGKETGKGSWLAISVAVEDSPQEPSIQCPRLAVTRPSQSSGIFPDVNGLTPRRSLFNGIGKMAGSTSTPKSFLVEEMPSIRTRSRTAANKKSENTDMSSSFCNNSARPSRSCRPTSLVEPSLKNKLRNGSKGKAKAKK', 401, 'Q24141;', 'KD01348', 'Drosophila melanogaster (Fruit fly)', 'mei-S332', '#Shugoshin#Meiotic protein S332', '-', '-', '37523'),
(1349, 'Q9N2X3', 'KBP-4', 'k', 11524, '', 'MQKSIDDMINEVLAVKVEKLPKTQDFSDLQEVCASKLQIINKEMDEADRKLEETLEKRKLVEKQLEDLQEQYKVKEFAFSLQKEFQDELKKVAEEIF', 97, 'Q9N2X3;', 'KD01349', 'Caenorhabditis elegans', 'kbp-4', '#KBP-4 {ECO:0000313|EMBL:CCD62277.1}', '-', '-', '175273'),
(1350, 'Q873B7', 'Probable kinetochore protein spc25', 'GO:0000778===GO:0051455===GO:0031617', 30198, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSRKSVMSSTFEPSLSTSRQPLGPSLADTLPSINFGFDELRDRMAKFTAKFDAFIEQGRKRVLEERNQFRMNVAELQEDQRMKKKDIEILQLKTNTYQQTMAKEAAETREMQAAIASLTEQRDKQAAMRDALKEQIAATQREIDARLAAQRAHAAQLEAQARYNVPELDFWVTNLCMRIEGAGAEDRLKFVYTHIDERNWEREAWFELSMSGRDYDVRHCRPKLEREKVEKVLDRVNETRELVVLLKGMRELFVEAMKS', 259, 'Q873B7; A7UWW1; Q7SCC6;', 'KD01350', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'kpr-4', '#Probable kinetochore protein spc25#Kinetochore protein 4', '-', '-', '5847309'),
(1351, 'Q8NCM8', 'Cytoplasmic dynein 2 heavy chain 1', 'GO:0003777', 492622, 'May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis. May play a role in transport between endoplasmic reticulum and Golgi or organization of the Golgi in cells (By similarity). {ECO:0000250}.', 'MANGTADVRKLFIFTTTQNYFGLMSELWDQPLLCNCLEINNFLDDGNQMLLRVQRSDAGISFSNTIEFGDTKDKVLVFFKLRPEVITDENLHDNILVSSMLESPISSLYQAVRQVFAPMLLKDQEWSRNFDPKLQNLLSELEAGLGIVLRRSDTNLTKLKFKEDDTRGILTPSDEFQFWIEQAHRGNKQISKERANYFKELFETIAREFYNLDSLSLLEVVDLVETTQDVVDDVWRQTEHDHYPESRMLHLLDIIGGSFGRFVQKKLGTLNLWEDPYYLVKESLKAGISICEQWVIVCNHLTGQVWQRYVPHPWKNEKYFPETLDKLGKRLEEVLAIRTIHEKFLYFLPASEEKIICLTRVFEPFTGLNPVQYNPYTEPLWKAAVSQYEKIIAPAEQKIAGKLKNYISEIQDSPQQLLQAFLKYKELVKRPTISKELMLERETLLARLVDSIKDFRLDFENRCRGIPGDASGPLSGKNLSEVVNSIVWVRQLELKVDDTIKIAEALLSDLPGFRCFHQSAKDLLDQLKLYEQEQFDDWSRDIQSGLSDSRSGLCIEASSRIMELDSNDGLLKVHYSDRLVILLREVRQLSALGFVIPAKIQQVANIAQKFCKQAIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNSKAGSGGKSQITWDNPKELEGYIQKLQNAAERLATENRKLRKWHTTFCEKVVVLMNIDLLRQQQRWKDGLQELRTGLATVEAQGFQASDMHAWKQHWNHQLYKALEHQYQMGLEALNENLPEINIDLTYKQGRLQFRPPFEEIRAKYYREMKRFIGIPNQFKGVGEAGDESIFSIMIDRNASGFLTIFSKAEDLFRRLSAVLHQHKEWIVIGQVDMEALVEKHLFTVHDWEKNFKALKIKGKEVERLPSAVKVDCLNINCNPVKTVIDDLIQKLFDLLVLSLKKSIQAHLHEIDTFVTEAMEVLTIMPQSVEEIGDANLQYSKLQERKPEILPLFQEAEDKNRLLRTVAGGGLETISNLKAKWDKFELMMESHQLMIKDQIEVMKGNVKSRLQIYYQELEKFKARWDQLKPGDDVIETGQHNTLDKSAKLIKEKKIEFDDLEVTRKKLVDDCHHFRLEEPNFSLASSISKDIESCAQIWAFYEEFQQGFQEMANEDWITFRTKTYLFEEFLMNWHDRLRKVEEHSVMTVKLQSEVDKYKIVIPILKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVADTIVAKAADLKDLNSRAQGEVTIREALRELDLWGVGAVFTLIDYEDSQSRTMKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAELDEYLQNLNHIQRKWVYLEPIFGRGALPKEQTRFNRVDEDFRSIMTDIKKDNRVTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFIGDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDEKSKHITAMKSLEGEVVPFKNKVPLSNNVETWLNDLALEMKKTLEQLLKECVTTGRSSQGAVDPSLFPSQILCLAEQIKFTEDVENAIKDHSLHQIETQLVNKLEQYTNIDTSSEDPGNTESGILELKLKALILDIIHNIDVVKQLNQIQVHTTEDWAWKKQLRFYMKSDHTCCVQMVDSEFQYTYEYQGNASKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVGLVKCGAWGCFDEFNRLEESVLSAVSMQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPAGKGYGGRQKLPDNLKQLFRPVAMSHPDNELIAEVILYSEGFKDAKVLSRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQLNKSGTTQNANESHIVVQALRLNTMSKFTFTDCTRFDALIKDVFPGIELKEVEYDELSAALKQVFEEANYEIIPNQIKKALELYEQLCQRMGVVIVGPSGAGKSTLWRMLRAALCKTGKVVKQYTMNPKAMPRYQLLGHIDMDTREWSDGVLTNSARQVVREPQDVSSWIICDGDIDPEWIESLNSVLDDNRLLTMPSGERIQFGPNVNFVFETHDLSCASPATISRMGMIFLSDEETDLNSLIKSWLRNQPAEYRNNLENWIGDYFEKALQWVLKQNDYVVETSLVGTVMNGLSHLHGCRDHDEFIINLIRGLGGNLNMKSRLEFTKEVFHWARESPPDFHKPMDTYYDSTRGRLATYVLKKPEDLTADDFSNGLTLPVIQTPDMQRGLDYFKPWLSSDTKQPFILVGPEGCGKGMLLRYAFSQLRSTQIATVHCSAQTTSRHLLQKLSQTCMVISTNTGRVYRPKDCERLVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDENLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCSIDYPEREQLQTIYGAYLEPVLHKNLKNHSIWGSSSKIYLLAGSMVQVYEQVRAKFTVDDYSHYFFTPCILTQWVLGLFRYDLEGGSSNHPLDYVLEIVAYEARRLFRDKIVGAKELHLFDIILTSVFQGDWGSDILDNMSDSFYVTWGARHNSGARAAPGQPLPPHGKPLGKLNSTDLKDVIKKGLIHYGRDNQNLDILLFHEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTITSLVSHMHGAVLFSPKISRGYELKQFKNDLKHVLQLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLKDQASQDGFFGPVFNYFTYRIQQNLHIVLIMDSANSNFMINCESNPALHKKCQVLWMEGWSNSSMKKIPEMLFSETGGGEKYNDKKRKEEKKKNSVDPDFLKSFLLIHESCKAYGATPSRYMTFLHVYSAISSSKKKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVVKIEERKNKIDDELKEVQPLVNEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFDARNISKEIRESVEELLFKNKGSFDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTCLEEWTKSAGLEKFDLRRFLCTESEQLIWKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILENKDLIESLNQTKASSALIQESLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLAAFLRLFQRALQNKQDSENTEQRIQSLISSLQHMVYEYICRCLFKADQLMFALHFVRGMHPELFQENEWDTFTGVVVGDMLRKADSQQKIRDQLPSWIDQERSWAVATLKIALPSLYQTLCFEDAALWRTYYNNSMCEQEFPSILAKKVSLFQQILVVQALRPDRLQSAMALFACKTLGLKEVSPLPLNLKRLYKETLEIEPILIIISPGADPSQELQELANAERSGECYHQVAMGQGQADLAIQMLKECARNGDWLCLKNLHLVVSWLPVLEKELNTLQPKDTFRLWLTAEVHPNFTPILLQSSLKITYESPPGLKKNLMRTYESWTPEQISKKDNTHRAHALFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYNIIDRLFDGAKDVQWEFVHGLLENAIYGGRIDNYFDLRVLQSYLKQFFNSSVIDVFNQRNKKSIFPYSVSLPQSCSILDYRAVIEKIPEDDKPSFFGLPANIARSSQRMISSQVISQLRILGRSITAGSKFDREIWSNELSPVLNLWKKLNQNSNLIHQKVPPPNDRQGSPILSFIILEQFNAIRLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLAWQSKWEGPEDPLQYLRGLVARALAIQNWVDKAEKQALLSETLDLSELFHPDTFLNALRQETARAVGRSVDSLKFVASWKGRLQEAKLQIKISGLLLEGCSFDGNQLSENQLDSPSVSSVLPCFMGWIPQDACGPYSPDECISLPVYTSAERDRVVTNIDVPCGGNQDQWIQCGAALFLKNQ', 4307, 'Q8NCM8; O00432; Q16693; Q3C1U8; Q4AC93; Q6ZMX7; Q6ZUM6; Q7Z363;Q8N977; Q92815; Q9HAE4;', 'KD01351', 'Homo sapiens (Human)', 'DYNC2H1', '#Cytoplasmic dynein 2 heavy chain 1#Cytoplasmic dynein 2 heavy chain#Dynein cytoplasmic heavy chain 2#Dynein heavy chain 11#hDHC11#Dynein heavy chain isotype 1B', '-', 'ENSG00000187240', '-'),
(1352, 'Q03188', 'Centromere protein C', 'GO:0000776===GO:0000777===GO:0051382===GO:0000780===SCL===k', 106834, '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. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions. {ECO:0000269|PubMed:19482874; ECO:0000269|PubMed:21529714}.', 'MAASGLDHLKNGYRRRFCRPSRARDINTEQGQNVLEILQDCFEEKSLANDFSTNSTKSVPNSTRKIKDTCIQSPSKECQKSHPKSVPVSSKKKEASLQFVVEPSEATNRSVQAHEVHQKILATDVSSKNTPDSKKISSRNINDHHSEADEEFYLSVGSPSVLLDAKTSVSQNVIPSSAQKRETYTFENSVNMLPSSTEVSVKTKKRLNFDDKVMLKKIEIDNKVSDEEDKTSEGQERKPSGSSQNRIRDSEYEIQRQAKKSFSTLFLETVKRKSESSPIVRHAATAPPHSCPPDDTKLIEDEFIIDESDQSFASRSWITIPRKAGSLKQRTISPAESTALLQGRKSREKHHNILPKTLANDKHSHKPHPVETSQPSDKTVLDTSYALIGETVNNYRSTKYEMYSKNAEKPSRSKRTIKQKQRRKFMAKPAEEQLDVGQSKDENIHTSHITQDEFQRNSDRNMEEHEEMGNDCVSKKQMPPVGSKKSSTRKDKEESKKKRFSSESKNKLVPEEVTSTVTKSRRISRRPSDWWVVKSEESPVYSNSSVRNELPMHHNSSRKSTKKTNQSSKNIRKKTIPLKRQKTATKGNQRVQKFLNAEGSGGIVGHDEISRCSLSEPLESDEADLAKKKNLDCSRSTRSSKNEDNIMTAQNVPLKPQTSGYTCNIPTESNLDSGEHKTSVLEESGPSRLNNNYLMSGKNDVDDEEVHGSSDDSKQSKVIPKNRIHHKLVLPSNTPNVRRTKRTRLKPLEYWRGERIDYQGRPSGGFVISGVLSPDTISSKRKAKENIGKVNKKSNKKRICLDNDERKTNLMVNLGIPLGDPLQPTRVKDPETREIILMDLVRPQDTYQFFVKHGELKVYKTLDTPFFSTGKLILGPQEEKGKQHVGQDILVFYVNFGDLLCTLHETPYILSTGDSFYVPSGNYYNIKNLRNEESVLLFTQIKR', 943, 'Q03188; Q6PIR0; Q8IW27; Q9P0M5;', 'KD01352', 'Homo sapiens (Human)', 'CENPC', '#Centromere protein C#CENP-C#Centromere autoantigen C#Centromere protein C 1#CENP-C 1#Interphase centromere complex protein 7', '-', 'ENSG00000145241', '-'),
(1353, 'O13816', 'Cohesin subunit psc3', 'k;t', 110652, '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 rad21 subunit of the cohesin 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:11069892}.', 'MSESVTTGSDDDGGDRESSPVMLSQSFDPMSSSSNSSSEENSDDDYEKTISSKKRHPRPNSKGVNVKRSRRNAIVEEDPQEEIFNNLFAFLLDQKVDTMDIAVSWFADYAKDNQSALANLINFILKCCGCNRAINVFDVQDQDSASATLSQIQLSVERTSTRDYPLNSKNLKFRNFRKRLTGLLSNFVSQLSIRNYLYNSTVFEDIMSWVVAMSSSTMRPIRHTATVFCLNIMTFLCEKSKELLNEHAIATKQLEKEEKRSRVNRNRINELNNSLGEIVKQQDTLTTYLNDYFDSVFVHRYRDVEPKIRVDCLQELGVWINTVPSIFFSGSYLRYLGWMLSDINTTVRLTVVKVLRKFFETDSFIGGLRHFSSRFKERILEMSCVDADIGVRVASIRLCNAMRTCGFLENSEILKVLKLILDINPRVQREAVLFLCKVVDESVNEKIDLWGEEDYILKAFSQTSLTTFSVHWIKFSQMCKLLEEVRLSYQSSFDYDTLLRIFQKNGNFITPITQALLNACEIDSIYQSWEDISNFVLFDNYTSTLKDPIDSILSFCKLNDFQESILLQLLSASIQTVCNNNFITPKTVHNKQAAETTNDQNKDKDLLYLNLLPYINSITERNSASPTLLHDSLRLLFSMDLTEMTDPQLSRHFELLINNLKKFFLTNNDLQIIQGCTILFLRLDSIPALKEDLKLLVTDICDQTVTEFLKNFGSFNIQDAVITKDEFVIFEACLTRIEGCTSLKDFSDYPEFDIIYERLVSLLSRVPNSYEDTLKFSAINTLQSLLFWFFLRKDNPADEEKKKDDETKVFNCLINIMNNDSSKILQLQAARTFLETVIMKEGVKASHYNDDNRVSEEHNFLKPQFLDALLKILEGWLYTYAKVGQFPFKRLTQASSPHTQISLDKNPLNRRLLEHVCCDLTSKLLIVVSLSNTITPEFSQQFCELRGHYGPKLSAIVDEFLN', 962, 'O13816; Q38G50; Q9US16;', 'KD01353', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'psc3', '#Cohesin subunit psc3#SCC3 homolog', '-', '-', '2542387'),
(1354, 'Q3T0L1', 'Centromere protein H', 'GO:0000776===GO:0000777===GO:0051382', 28064, '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 (By similarity). {ECO:0000250}.', 'METQSEEQAVTKPADSGGEGGPPQVAGAQAARPEDRMTLLLRLRAQTKQQLLEYKSMVDANEEKTPEQIMQEKQIEAKIEELENEVEEAKTAFEMKKLALDRMQLSTALKKHLEKVDIKTSVLMDNMKQILNLNKLIMKSQQETWDLEEKLLDVRKKRLQLKQASERKLLEIQTEKNKQKDDLDSMENSDKIKAIQQNLETEIQITTVIQHVFQNLILGSKVNWAEDPALKETVLQLEKNLTMI', 244, 'Q3T0L1;', 'KD01354', 'Bos taurus (Bovine)', 'CENPH', '#Centromere protein H#CENP-H', '-', '-', '505284'),
(1355, 'Q6XXM1', 'Histone H3-like centromeric protein A', 'GO:0051382===GO:0000939===GO:0000778===SCL', 15243, '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:14563550; ECO:0000269|PubMed:15870271}.', 'MPRPKPRSPRRRGRPPPAAPPPPPARPRARRYRPGQRALREIRRYQSSTALLLRRQPFARVVREICLLFTRGVDYRWQAMALLALQEAAEAFLVHLLEDAYLCSLHARRVTLYPKDLQLARRLRGLQGEGF', 131, 'Q6XXM1;', 'KD01355', 'Gallus gallus (Chicken)', 'CENPA', '#Histone H3-like centromeric protein A#Centromere protein A#CENP-A#GgCENP-A', '-', '-', '100113359'),
(1356, 'P45962', 'Kinesin-like protein klp-3', 'GO:0003777', 67323, '', 'MDSHVGEVDIFQQCKYIHEVELVNMKLQMRILETHIETKDRLLRNLEDIIDEQESRIANMEDFIQGRATSYTNRSNMLKGISVLSLDFGNLSEENLRLKNALSQMQKVARVNELLETDEDYESDMTSNEDRFALSRDSSCSVPRSVSPQPTGDVIKPYPQMVQSMREEGHWKKLQRCAEELKTEKDELKRLALDTKDAFNVCMAEMRMMLTSKTTDFFRVLIERYKAEMEKRKQLHNQLVELNGNIRVFYRIRPQLASETDNQKPVVVIDEMDNGVVHVSNTTGTRKTSAGADKVIPTDFSQDQIFNEVSPIITSCIDGYNVCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLAIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKATTVGRLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVNFAEKIGQVFTKSGTMKREPTRRSMTGISSGQRREIPASPRK', 598, 'P45962; Q7JMP3; Q7JMP4;', 'KD01356', 'Caenorhabditis elegans', 'klp-3', '#Kinesin-like protein klp-3', '-', '-', '191697'),
(1357, 'P51608', 'Methyl-CpG-binding protein 2', 'k', 52441, 'Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA; with a preference for 5-methylcytosine (5mC) (By similarity). {ECO:0000250}.', 'MVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSAEPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIEVKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVPLLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAAEKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS', 486, 'P51608; O15233; Q6QHH9; Q7Z384;', 'KD01357', 'Homo sapiens (Human)', 'MECP2', '#Methyl-CpG-binding protein 2#MeCp-2 protein#MeCp2', '-', 'ENSG00000169057', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1358, 'Q9VMS5', 'Bub1 homologue; isoform ABub1 homologue; isoform BBub1 homologue; isoform CLD22858p', 'k', 125488, '', 'MAMHSYMRQGSGSGGGAGAVAAGAPPLASPDEMHGFLNDKQAWEHAISLYQGPDPLDHWYNYICWYENHAQSDPELKYRETLERCLTVYEHNDYYRQDVRLVRLWLKYIAMQTDPLHFYQVLFQRGTGRQVAAFYIGWAAYYESREEYKDAEAVFNLAFQEKAQSTSELQHAHTKFAYARSLFYQRQQQQQQQQQQHQQHPPQDALQQLTNYAQQQMPQSYNQHRPQPYQQNVYQQYHPQAQAHQAPQPHQPAPQQQLPPEQQVPYQTHYQERPRYEPHPATQSPTAIPPSQVQQQSHYAPVAESHYAPAQQSQLPPQQTTVPQLHAQQPQQQQNGNGNPPPQQSPPVTNEVAGLRLPRNFHAYGRNNHETWKPALTLEEPDDPSRVCHYAKQLVYPPGAGVEYSPEEILARKFKQLMDQKAKPSEPPEQEQQTLYDSYETEKSYYMTAVDGALYGQNTSSGQENTGEEDEDNDAEEGEEEEDGGEENEEDDSDEEEEDDEEEEEHSGPYTNGVQFSAQTTFEQENRSIKIKFRKEPSSTYSAYTIENVYQQQQQQQQEQHQIIHQPPQAVHHPSPDPAPASPIPIQRQRNGSHHHFHPYMLGQTSTPKSEANGYRRARTKVKRSKFQPDLCSNSNSASSVADVASSSVLAGAPGTFNDNANFSFSSATALDNSNSSLALAVDRLNFRDTSQQQILHPVNKTLQIHNNNNNTSNNNNGTSTMADFSTFQENSYFATQHDTEAQERRLSKAVETIARHMDKEAIDPFNSELCRAFLAKLDFPGNHDAHASYKIVQTPLPKISNTRTLNVLEGVTFSIDKEVGRGSYGSVYKATDSRTGNVVALKYQKPPNTWEIYICDQVLKRIKEPEVLPGVMDISTAIIAPNASLIATEFSPFGSLLDINNKIRQATTKVMHESLVMHFSAQICNIVDHLHRQHIIHADIKPDNFLLMRVPNVDSPLPSLRLIDFGCAIDMTLFPDGEKTKFRKVVQTDGFTCIEMQEGRSWSYETDLFCIAATVHVMLFGDYMQPQKKGSSWEIRQKLPRYLKKHVWTKFFGDLLNMQADKLPALHEMRLIFEEEAYRMDSELQKQIRTLSNILHRR', 1099, 'Q9VMS5;', 'KD01358', 'Drosophila melanogaster (Fruit fly)', 'Bub1', '#Bub1 homologue; isoform A {ECO:0000313|EMBL:AAF52236.1}#2.7.11.- {ECO:0000313|EMBL:AAF52236.1}#Bub1 homologue; isoform B {ECO:0000313|EMBL:AHN54137.1}#2.7.11.- {ECO:0000313|EMBL:AHN54137.1}#Bub1 homologue; isoform C {ECO:0000313|EMBL:AHN54136.1}#2.7.11.- {ECO:0000313|EMBL:AHN54136.1}#LD22858p {ECO:0000313|EMBL:AAL39653.1}', '-', '-', '33758'),
(1359, 'Q7TME2', 'Sperm-associated antigen 5', 'GO:0000776===GO:0000777===GO:0051988', 129993, 'Essential component of the mitotic spindle required for normal chromosome segregation and progression into anaphase. Required for chromosome alignment; normal timing of sister chromatid segregation; and maintenance of spindle pole architecture. In complex with SKAP; promotes stable microtubule- kinetochore attachments. May contribute to the regulation of separase activity. May regulate AURKA localization to mitotic spindle; but not to centrosomes and CCNB1 localization to both mitotic spindle and centrosomes. In non-mitotic cells; upon stress induction; inhibits mammalian target of rapamycin complex 1 (mTORC1) association and recruits the mTORC1 component RPTOR to stress granules (SGs); thereby preventing mTORC1 hyperactivation- induced apoptosis. May enhance GSK3B-mediated phosphorylation of other substrates; such as MAPT/TAU (By similarity). {ECO:0000250}.', 'MWRVKTLNLGLSPSPQKGKPAMSTPLRELKLQPEALADSGKGPSMISALTPYLCRLELKERCNNSSPVDFINTENNFLSEQFSHPSTHIEACQRESDPTPESNSLFHTLEEAIETVDDFVVDPRDDSIVESMVLLPFSLGQQQDLMLQAHLDTTAERTKSSLNESLGLEDLVGKEVAPCVEDSLTEIVAIRPEQPTFQDPPLGPSDTEDAPVDLVPSENVLNFSLARLSPSAVLAQDFSVDHVDPGEETVENRVLQEMETSFPTFPEEAELGDQAPAANAEAVSPLYLTSSLVEMGPREAPGPTVEDASRIPGLESETWMSPLAWLEKGVNTSVMLQNLRQSLSFSSVLQDAAVGNTPLATCSVGTSFTPPAPLEVGTKDSTSETERLLLGCRPPDLATLSRHDLEENLLNSLVLLEVLSHQLQAWKSQLTVPHREARDSSTQTDSSPCGVTKTPKHLQDSKEIRQALLQARNVMQSWGLVSGDLLSLLHLSLTHVQEGRVTVSQESQRSKTLVSSCSRVLKKLKAKLQSLKTECEEARHSKEMALKGKAAAEAVLEAFRAHASQRISQLEQGLTSMQEFRGLLQEAQTQLIGLHTEQKELAQQTVSLSSALQQDWTSVQLNYGIWAALLSWSRELTKKLTAKSRQALQERDAAIEEKKQVVKEVEQVSAHLEDCKGQIEQLKLENSRLTADLSAQLQILTSTESQLKEVRSQHSRCVQDLAVKDELLCQLTQSNKEQATQWQKEEMELKHIQAELLQQQAVLAKEVQDLRETVEFIDEESQVAHRELGQIESQLKVTLELLRERSLQCETLRDTVDSLRAELASTEAKHEKQALEKTHQHSQELRLLAEQLQSLTLFLQAKLKENKAESEIILPSTGSAPAQEHPLSNDSSISEQTPTAAVDEVPEPAPVPLLGSVKSAFTRVASMASFQPTETPDLEKSLAEMSTVLQELKSLCSLLQESKEEATGVLQREICELHSRLQAQEEEHQEALKAKEADMEKLNQALCLLRKNEKELLEVIQKQNEKILGQIDKSGQLINLREEVTQLTQSLRRAETETKVLQEALEGQLDPSCQLMATNWIQEKVFLSQEVSKLRVMFLEMKTEKEQLMDKYLSHRHILEENLRRSDTELKKLDDTIQHVYETLLSIPETMKSCKELQGLLEFLS', 1165, 'Q7TME2; B1AQC8; Q8CH61;', 'KD01359', 'Mus musculus (Mouse)', 'Spag5', '#Sperm-associated antigen 5#Mastrin#Mitotic spindle-associated protein p126#MAP126', '-', '-', '54141'),
(1360, 'Q8IBG1', 'Dynein heavy chain-like protein MAL7P1.162', 'GO:0003777', 582332, '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 (By similarity). {ECO:0000250}.', 'MELEKTHLINYFLEICPTVLDCSRKELQSVLIKKEEEKIRKFLLDKNINLIVIGKEGNDNVEREMDDKENDNVDINMNEEYNSMRTSNLDNKYNNFLFVELMINYKCVTKSISIAFMKRNKENFLSLNDKIDNRNKINLSNELLMFVCGQNDCNTPLDLVYLYLSQGFNNIFDAASGYGQNISGPDSSHFNYGTKKDVENMFSINNKYIGYEGENKVSNILMNNVSKKLNELLISMKNAQIDLNIPIINLHVDKRIKKLLEENPNVDDMKPDKLKQLCESQEFINQLQKDVTKWIEDIQKLTRLNGEFKSGGSALSEINFWIGYENALYQLESQLKNPEVILTLHILKNAKRYFATMSFDSDIQLKQSKEYVLNVNILMKDFPIEDLLGATSIQQIIQAVRNIFNHLKKLKNTTKYPLSRSYNFVESLSRDLNNTMKKVLCTQSLMNMDYEEFDVLISGCVEIFRLWNEEMRIFKDMVRELIKKRSFNERAPAKMVFEHIHLQERLDEIKKFRKQHEKFKSVISTVFGSNNKSLGINLYKDINTAYNIFLSLDPLDLSKNGEDNWEKAKLSYESKVNRVESQITFKLRDQLGGSKTSAEMFHAFSKFNPLFFRPKIRGAIQEYQNTLIQIVVDDLRKLQMIYINGYLKSDSQKVSTIRDIPLVAGSIIWAKQIERKLEDSLKRIENVLGRGWEQHSEGKILRQNIDNFKNLLSQNKTFEKWLKNIKSADKFDMYDNIINIKKLGGNNYEILANYDFQFFNIFKEVRYLQSINLRVPYSIKVKADETKLIYPYALTLQKTFRTYMKICISMDNQAKDVPFNQTIKKLVAAIHNTVQNKIKEGIYLHWDSDIIETYVRKLSETINTFEFMVDEAMNKNKIVLDSLEKMKTCEVCFDCNELKSLIEIIQKKADELYLEHYRNVHIWIEELNIHINKILTERLEEIIKTWTCEFVNWPNNGKRFICKENIHEFKIKNQKFYLHPSIDSMRQIWFSKLSDAINIICGITRIKNIYQKKEKTNEKIQIKSKGKNTNNEKDDDYIYYTNDSNNKNNIYKNKCDDNNNNIVINDVILDNTYKYIIYFIDKKIYDNAIKSINDMVDKAQKYESIWLQYKTLWQIEIGDIISSFGEDIETWKIFMNEIKQTENTFDTLDTEKYFGPIVIDYRILQSKVSSKFEIWQKEIVSEFSKKLGEKTLYLKEEIEKALYDLNTQSELKNETEITAMHILSMTPKDIVGIMNTYDMDILSKTCNSIYNFIEKINEINKKEELEWSKKCDLLKQSEVLLEKQRYTFPTNWLYIDNIIGKLETVKQICKYQIKLIKDYLPYIQSMVLDFDRKVQNNIKELFEEWNKNKPSHGNANSTKALQIITTFEERIDIINEQYEISEKIRKLLELENSESEIGFHVSPNILKEEINCVKGIWDELKIIYSNICDMKKMLWSNVDPKDVKHRLNNLLESIKKIPAKYRQYEIFDNVQNEIQQYLKTYSLLLDLKSESLKERHWKLILQKLNIKIYYNKLTLGNLWSLHLCIHENVLSEILNQAQGEMALEQFLRGLKDTWNEYELELVQYQNKCKLIKGWNDIFSTIDDHLNAIQSMKISSYIKIFEEETFTWDDKLNRLRNLLDVWMNVQRKWVYLEGVLKGSSDIKSLLPQEYNRFKIIDSDFINIMKKTSDKPKLLELFQMEGFQKQLDRLSDSLSKIQKALGEYLEKQRNKFPRFYFVGDEDLLEMIGNSKDAKIIQRNVNKMFAGINSFILKENTNDIILGMSSREGEEVLFLEALNISSFNTLKEWLIVLEKSMKSSLEFYLDEAAKEILEMDMIECTKIENNKILLWSEKYPNQIILLCLQILWTTNIENELINFSKNPPDESNTLFHKSEKICLNLLEFLAVNVVKQKDHRTRQKFVQMITELVHQRDVIRILIDKNVNNVNSFIWLQYMRYYWDSKKKENKINLIIKMADATFEYGYEYLGMCEKLVQTELTDACFLTLTQALKMKLGGNPFGPAGTGKTESVKALGAQLGRYVLVFNCDESFDFTAMGRIFVGLCQVGAWGCFDEFNRLEERILSAVSEQILTIQTSLVQRKNEIEILNKKIGLNKNVGIFVTMNPGYAGRSNLPDNLKQLFRSFAMIEPNKQLIVEVTLFSQGFISAEHLSSKIVSLFDLCSEQLSKQPHYDFGLRSLKSVLNSAGNLKRLTLLKDESKYVQNNQIGFNETLDNNNNNDNNNERKTTTNTNESNIISMEQTLLLKSVCDTVYPKLVSSDIILIQSLLKGVFPNVNVGDLEEKGLINEIHRLCKLRHFTPEEKWITKICQIYQIMKLQHGVMLVGDVGTGKSSAWKILLDSLEALDNIKGVSYVIDAKSLDKEEIYGKLDNINLEWTDGVFTGILRKIIYNSSTQSGNTNKRHWIVFDGDVDPEWAENLNSVLDDNKLLTLPNGERLPIPESVRILFEVDTLKHATLATVSRCGMIWFSRDILSPIILFKHKLNMLKYGDNDYPRKMDKFKLLLINNNERITEKNQNGNENGNENEKKNINIINNNNSNNSNNIYSMNHMNNYNVNANEHNLQQFDNIDSENIMDNIRMNSRIFFEENEQETSSSYIIRTIPYRAVNIISDYFEENEFVHQCLVEAENYEHVMDYEYIRVIESTCLLLQKGFDNLVKKNEKINNTLSDDDIEKYISKWLVVSILWGIGGSLNLETREKFSMFVQSICSIPLPNDLLSKGKMPNMDNTNKISNTLLDYQPNIEDGEWINWKELVQIIDVDRTEISDATLVIETMDTIRHETILEGWLHLKKPFILCGPPGSGKTMTLTSVLKKSSEFDIASLNFSSGSLPNLLLQTFDHYCEYVKTTSELVLRPLQPGKWLIIFADEINLPTPDKYDTQRIIMFMRQIYESQGFWKYDVNNNSWNWVKIERITFAGACNPPTDAGRNPLSNRFLRHTSVLYVDFPGYESLKQIYGTFNRAILRKFPQSSHMADNLTQAMVDFYTKFSETFTIDMQPHYIYSPRELTRWKLALYETLESCDELKTKDLVRLCICEGLRIFQDRLIYKKEKKETDKIIDDIFKYSFPDITKEDLLRPILFNSYMKNYYTEIDKKDLKVLILSKLKIFNEEEINVQLVLFDDVLDHITRIDRVLRLPLGHLLLVGASGAGKTILSRFVSWINGLSVFQIRAGRNYTTESFEADLRHIMKRAGIKEEKITFIFDESNVLGPAFLERMNALLASGEVPGLFEGDNYITLINECKSAYRSNIGLDESDIFKKFTKQVQQNLHIVFTMNPANPDFANRQATSPALFNRCVIDWFGDWPYSALLQVASEFIFNLILPDNNFYMDYVGNEDGPIKGKIQYKNNKAYFLSRAIVEIHNSVVHINNVLMKKGNRYNYMTPRDFLDFIKHFLKIIDEKKEEVSSQKNHLNSGLNKLKDTEIQVAELRNSLAIKKKTLAEKDLEAEEKMKLMIEQQTETEDKKKKAEILSKKLDEQFIIIDQRKEVVRKELSEVEPKFREAEEAVKNIPKKNFDELRAMANPPILVRNAVEAVAILIMNEGDKNVTWEDARKIMKGQDFINKVLYLDKKAVKPQTSSQIKKRINNNDWDVERINKASRAAGPLAKWVESVITFLNILETVQPLEKEIEKLQEETKVAEDQYNEQRDIICELEKKLVQYKNDYAQLISQVQNIKQEMEMVENKIKRSINLIDNLKSEKERWSETFINLEEASETFVGDCLIAAAFCAYIGFFEHYERQRLKRTWGEIIKMHYIKYRNDLSFIEFLSRPSERLQWIGNELPSDDLSIENAIIINNYIRYPMIIDPSDQATTFLLNQYSDKKILKTSFSDKNFIKNLESALRFGSTLLVYDVEKIDAILNSVLNQETHKQGGRLLITIGDSEVDFSPSFNLFLTSRDAHFQFTPDLCSRVTFVNFTLTPSSLQNQCLNMILKNERPDIDKKRCDLLKLQGEYKVKIRELEESLLLELSNVKGNILDDDNVISTMEKLKVQGAEASKEVNIAEEVMVEVENVSNQYLFLAQGSARIYFILQHLCNINFLYQYDLNFFFNIMKDMFNNDHLLSIVKKKDHYKERLKVLEDLLFSLTYNRVARGLLQEDRYVFGLQLCYVKSIINPNIDMDQSYLHYLLKDHYSNQEIDEFEHKKIEKNLLPEYNDEQINALNNLIKHKSFSNLKKCILNNKQKWIELLHSAEPEELVCSILNDMNMSEESMDKSDEMLNKNKNLNILNNVEFGKDDDIPEEKRYINNDNTNMDTTTKNNNNMNNNNNMNNNNNYMLQNKNDISSCLKESLIIKAIRPDKLENCFNKIINHILGRDFLWIPELSMNDFEKYVKENANGNIPIVLISSPGFDPSNKVQQLSEKCKIPLFSIAMGSEEGYISAERVIFTAQSNGGWVLLKNIHISTKWLHELEKNIHKATTNKNFRLFLTMEFNPRIPQSLMRISLTFMFEPPVGIKFSILRSFSLFLENRELCEPKIARLRLYFIVSYLHAIILERRRYTPIGWTKKYEFSDSDLMCALSVVDSWLDKASTKIGKNVSEHIDPCNIPWEAIKKILNEAIYGGRLDNMVDQKILDTFIDHLMNSNSFETDFKLNICNSTSLNKDFLVSPDLFRNINDYINWTNNMSNTDLPAWLGFGQQAEGLLTTRTNFSIISKWNILYSKSRSDVYEPLPHSPLTKSLNEEKYISFEQYKIKNIKEKTIKDKDKNKDEDKNKNKENDDNNKKHIGNNKLVISSSERTESETSESSCTVSRSIHVYSNNENILFINKILENLPQNIPCLEKNEEKLRNAVFRCFERENNLFSDLLKLIKTNLNQLKNVLEEKVKYTNKIRALAKDLNSFNVPSNWLLDGNTTNLNLTNWLKELINRLYQIIVITLEFNEKSCIDINEKKKQKNINIENNEDHNLNDFYKRNNDNILSHFKLNNKEKKLSINFIWLGGLFYPRAFITATRQLSAFKFKNSLDDLELSVLIGNNNNMKYDDMIHFTITCLSIEGAEWSNKDNVN', 4985, 'Q8IBG1; C0H4Q3;', 'KD01360', 'Plasmodium falciparum (isolate 3D7)', 'MAL7P1.162', '#Dynein heavy chain-like protein MAL7P1.162', '-', '-', '2654986'),
(1361, 'Q60LV7', 'Kinesin-like protein vab-8', 'GO:0003777', 118647, 'Required for posterior migration of cells and axon growth cones during nervous system assembly. {ECO:0000250}.', 'MEACTSKSSLLLHSPLRTIPKLRLCTTISSEDVAYGRCNLTDQHLQIEGKNYSKNTFDHIFRTDATQDDMYSAFLSDMINSVFAGNDATVLAMGAKANGKDERLYGNSVSRNGLIQMAITQLMNAIDDNKDPEERIQVRMSAIMVSQKDSSIVDLLSPFNDPRHRVVKLVDDARTGVFLDNESEIRVETIDQALFYLNTAVDHRLIQDEQTHRTSHVFISLSLYSYKMGDKMQGGRRRLCFLDMGIGERNSTNGGMTMPALGSILLAMVQRNKHIPSRDSSVCQLIRCALSTSRFTTFLFSFGSKNDDNENIAHLACKIARTRVKSVMGHGRKPSGTFSSGTMDSNGSSSSFGTTTITPGGTPRTQRRFELESGSELSAAETVIFLGPSCSRTTSPASTTMPSTPTSIRPLHRTTRNHSGVDPVSKPLSVETKSSPTHNCHDGCIHSIPPMLRGHTPFLSPHLKLYDELCSPPNSSCASPVLSAPNAFGGKTAERRDDFGIMIAQPHIPLMKAKSKYNLDDGKMKQIMQWMETSEAPPILFSSPCYENSATSLDELRECVGILSHPLEDIIEQEEESMRTSTATTGGSKKDHPLRILSKQDLNIDSEAKDKDETELELVMAASLSSMRSHDILAKLEAMRNAQSGQNGQNGNIGTSQSNTDMDVSEMDMYRRASHLEEYAMQRVREIEDNKMKNKKKVKLGLNCCQQQSMISSGSTVVDWSQIERKKEREKDAMEEEKRKEVLRERRAKLKITELEIKRERNMIDKELDDKKGIANSIARQLQHFSLSPCRGGRTHRSVSTHRIDPPNASLPSTPTMSHKKMIGGSLAKLSASGASGSGPPSSPSLGYHQSLPRHSKLPTAVNGRRSSAERDRKTSKNSRNASSKERRSSGSKEELQWRSPYAQMTSPKTYGGPGTSSSGRGSSAPGSDFETPVVSATEKTANGTMPRSKRQSYSASSGYESANDYHIYATTNKKANILEKKRNEEKLFLVRQADEIRHRQWQLKKELEEAKRAIGQEEDAKMIANSSDQRLNGLSRTTMVDAMLQENRILEKRLIACRNHSMLVTTFI', 1069, 'Q60LV7; A8Y3Z4;', 'KD01361', 'Caenorhabditis briggsae', 'vab-8', '#Kinesin-like protein vab-8#Variable abnormal morphology protein 8', '-', '-', '-'),
(1362, 'Q96BD8', 'Spindle and kinetochore-associated protein 1', 'GO:0000940===k', 29484, '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. {ECO:0000269|PubMed:17093495; ECO:0000269|PubMed:19289083}.', 'MASSDLEQLCSHVNEKIGNIKKTLSLRNCGQEPTLKTVLNKIGDEIIVINELLNKLELEIQYQEQTNNSLKELCESLEEDYKDIEHLKENVPSHLPQVTVTQSCVKGSDLDPEEPIKVEEPEPVKKPPKEQRSIKEMPFITCDEFNGVPSYMKSRLTYNQINDVIKEINKAVISKYKILHQPKKSMNSVTRNLYHRFIDEETKDTKGRYFIVEADIKEFTTLKADKKFHVLLNILRHCRRLSEVRGGGLTRYVIT', 255, 'Q96BD8; B2R9Y6; B4E0P4;', 'KD01362', 'Homo sapiens (Human)', 'SKA1', '#Spindle and kinetochore-associated protein 1', '-', 'ENSG00000154839', '-'),
(1363, 'Q14807', 'Kinesin-like protein KIF22', 'GO:0000776===GO:0003777===k;s', 73262, 'Kinesin family that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA.', 'MAAGGSTQQRRREMAAASAAAISGAGRCRLSKIGATRRPPPARVRVAVRLRPFVDGTAGASDPPCVRGMDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGAEGRPWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQPHALGPVKLSQKELLGPPEAKRARGPEEEEIGSPEPMAAPASASQKLSPLQKLSSMDPAMLERLLSLDRLLASQGSQGAPLLSTPKRERMVLMKTVEEKDLEIERLKTKQKELEAKMLAQKAEEKENHCPTMLRPLSHRTVTGAKPLKKAVVMPLQLIQEQAASPNAEIHILKNKGRKRKLESLDALEPEEKAEDCWELQISPELLAHGRQKILDLLNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQMESFLKANILGLAAGQRCGAS', 665, 'Q14807; B2R5M0; B7Z265; O60845; O94814; Q53F58; Q9BT46;', 'KD01363', 'Homo sapiens (Human)', 'KIF22', '#Kinesin-like protein KIF22#Kinesin-like DNA-binding protein#Kinesin-like protein 4', '-', 'ENSG00000079616', '-'),
(1364, 'Q9DBS5', 'Kinesin light chain 4', 'GO:0003777', 68613, '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}.', 'MSGLVLGQRDEPAGHRLSQEEILGSTKVVSQGLEALHSEHQAVLQSLSHTIECLQQGGHEEGLVHEKARQLRRSMENIELGLSEAQVMLALASHLSTVESEKQKLRAQVRRLCQENQWLRDELAGTQQRLQRSEQAVAQLEEEKKHLEFLRQLRQYDEDGHGMEEKEGEATKDSLDDLFPNEEEEDSGNDLSRGQGAAAAQQGGYEIPARLRTLHNLVIQYAAQGRYEVAVPLCKQALEDLERTSGRGHPDVATMLNILALVYRDQNKYKEAAHLLNDALSIRESTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCQRALEIREKVLGTDHPDVAKQLNNLALLCQNQGKYEAVERYYQRALAIYESQLGPDNPNVARTKNNLASCYLKQGKYSEAEALYKEILTCAHVQEFGSVDDDHKPIWMHAEEREEMSRSRPRDSSAPYAEYGGWYKACRVSSPTVNTTLKNLGALYRRQGKLEAAETLEECALRSRKQGTDPISQTKVAELLGEGDGRKAIQEGPGDSVKFEGGEDASVAVEWSGDGSGTLQRSGSLGKIRDVLRRSSELLVRKLQGTEPRPSSSSMKRAASLNYLNQPNAAPLQVSRGLSASTVDLSSSS', 619, 'Q9DBS5; Q3TCC5;', 'KD01364', 'Mus musculus (Mouse)', 'Klc4', '#Kinesin light chain 4#KLC 4#Kinesin-like protein 8', '-', '-', '74764'),
(1365, 'Q8TF09', 'Dynein light chain roadblock-type 2', 'GO:0003777===GO:0005868===c;k;m', 10855, '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.', 'MAEVEETLKRIQSHKGVIGTMVVNAEGIPIRTTLDNSTTVQYAGLLHHLTMKAKSTVRDIDPQNDLTFLRIRSKKHEIMVAPDKEYLLIVIQNPCE', 96, 'Q8TF09;', 'KD01365', 'Homo sapiens (Human)', 'DYNLRB2', '#Dynein light chain roadblock-type 2#Dynein light chain 2B; cytoplasmic#Roadblock domain-containing protein 2', '-', 'ENSG00000168589', '-'),
(1366, 'Q8R0G9', 'Nuclear pore complex protein Nup133', 'GO:0000940', 128620, 'Involved in poly(A)+ RNA transport. {ECO:0000250|UniProtKB:Q8WUM0}.', 'MFPSVSSPRTPGPGTRRGPLVGIGPTSTPRASRRGLSLGSAVNSPVLFSPAGRRSSVSSRGTPTRIFPHHSISESVNYDVRVFGSSLPVKIMEALTMAEADEQLSVHVDEGGWACLVCTEKLLIWKIAVSPVTKLSVCKELQLPPSDFHGSADLVALSYAATSGEVHSVQAVSVMVATKEGSIRYWPSLAREDTYSDTCVDLGGEKMCRFLTAVQGGSFILSSVGSQLVRLIPESSGKIHQHVLPQGQGMLSGIGRRVSSLFGILSPTSDLMLASVLWDRGGSSFYTLTSSNISKWELDDSSEKQVHSWDVHRTLKESITDAVWGSESNYEAIKEGVNIQYLDLKQNCDGLLILAAAWHLGDSPCLVYYSVITVEDNGNQMSDAVTVEVTQYNPPFQSEDLIACRLMVPNFSSQMTYLYMENAVFVCSTGTGKFSLPQEKIVFDTQGDGILGAGSCAGVPILFSRNSGLVSVTPRENVSLLAEDLEESLTSSVGGRGSESMVFETTTKNETVAHEDKTKLLKAAFLQYCRKDLGRAQIMADELFSSHTDLDSDPELDKAVTQISVDLIDDYPASDPRWAESVPQEAPGLSNTSLIILHQLEDKMKAHCLLVDFLHQVGLFRRLSSYPIRGTPMSTRLLLCEHAEKLSAAITLKNHHSRLPDLVNSAILLALNKRECEVPNSLTPADVFFREVSQVDTICECLLEHEEQVLREVALVSQEWAEVAIDVNTVLKDMLQAATHYRLNKSSMYSQEEVLGKEPEYVPWTATSGPSGIRTAVMRQHGIILKMVYPQADSKLRNVVMEQLVALIDCFLDSYVSQLKSLEKSSDQERYSSLEVEYLQKRSELLSPLLTLGQYPWAASLAEKYCDFDILVQMCEQTDNQARLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHTTLLGLANMETRYFAKKKTLLGLSKLAALASDISEDRLQEKIEAMAEQERFLLHQETLPEQLLTERQLSLSAMPVLTAPQLISLYICDENRRANEYDFKKALDLLEYIDEEEDVSIDDLKLEILCRALQRDDWSGSDGKDDPIEVSKDSVFVKILQKLIKDGIQLSEYLPEVTDLLRAEQLGSLKSNSYFEFVLKANYEYYVQGQM', 1155, 'Q8R0G9; E9QLJ8;', 'KD01366', 'Mus musculus (Mouse)', 'Nup133', '#Nuclear pore complex protein Nup133#133 kDa nucleoporin#Nucleoporin Nup133', '-', '-', '234865'),
(1367, 'Q96JB1', 'Dynein heavy chain 8; axonemal', 'GO:0003777', 514664, '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}.', 'MMKLYIDNAAPDKLKGLCIFFVRCRNDVAINVKTIQEEALFTVLDASKGLLNGIRDMLANIFLPAVLATNNWGALNQSKQGESEKHIFTETINRYLSFLDGARISIEGTVKLKTIDNVNFSKLHTFEEVTAAASNSETVHQLEEVLMVWYKQIEQVLIESEQMRKEAGDSGPLTELEHWKRMSAKFNYIIEQIKGPSCKAVINVLNVAHSKLLKNWRDLDARITDTANESKDNVRYLYTLEKVCQPLYNHDLVSMAHGIQNLINAIRMIHGVSRYYNTSERMTSLFIKVTNQMVTACKAYITDGGLNHVWDQETPVVLKKIQDCIFLFKEYQASFHKTRKLISESSGEKSFEVSEMYIFGKFEAFCKRLEKITEMITVVQTYSTLSNSTIEGIDIMAIKFRNIYQGVKKKQYDILDPRRTEFDTDFLDFMTKINGLEVQIQAFMNSSFGKILSSQQALQLLQRFQKLNIPCLGLEINHTIERILQYYVAELDATKKLYHSQKDDPPLARNMPPIAGKILWVRQLYRRISEPINYFFKNSDILSSPDGKAVIRQYNKISYVLVEFEVVYHTAWIREISQLHYALQATLFVRHPETGKLLVNFDPKILEVVRETKCMIKMKLDVPEQAKRLLKLESKLKADKLYLQGLLQYYDELCQEVPSVFVNLMTPKMKKVESVLRQGLTVLTWSSLTLESFFQEVELVLDMFNQLLKKISDLCEMHIDTVLKEIAKTVLISLPESGATKVEDMLTLNETYTKEWADILNHKSKHVEEAVRELISIFEQIYEVKYTGKVGKQSEQRKHVVFGSETGEGENNDYEANIVNEFDTHDKEDEFKKECKEVFAFFSHQLLDSLQKATRLSLDTMKRRIFVASLYGRKQSEDIISFIKSEVHLAIPNVVMIPSLDDIQQAINRMIQLTLEVSRGVAHWGQQQIRPIKSVIPSPTTTDVTHQNTGKLLKKEERSFEEAIPARKLKNFYPGVAEHKDISKLVLLLSSSVNSLRKAAHEALQDFQKYKTLWTEDRDVKVKEFLANNPSLTEIRSEILHYATFEQEIDELKPIIVVGALELHTEPMKLALSIEAKAWKMLLCRYLNEEYKKKMSYMIAFINEYLKKLSRPIRDLDDVRFAMEALSCIRDNEIQMDMTLGPIEEAYAILNRFEVEVTKEESEAVDTLRYSFNKLQSKAVSVQEDLVQVQPKFKSNLLESVEVFREDVINFAEAYELEGPMVPNIPPQEASNRLQIFQASFDDLWRKFVTYSSGEQLFGLPVTDYEVLHKTRKELNLLQKLYGLYDTVMSSISGYYEILWGDVDIEKINAELLEFQNRCRKLPKGLKDWQAFLDLKKRIDDFSESCPLLEMMTNKAMKQRHWDRISELTGTPFDVESDSFCLRNIMEAPLLKHKDDIEDICISAIKEKDIEAKLTQVIENWTNQNLSFAAFKGKGELLLKGTESGEIITLMEDSLMVLGSLLSNRYNAPFKKNIQNWVYKLSTSSDIIEEWLVVQNLWVYLEAVFVGGDIAKQLPQEAKRFQNIDKSWIKIMQRAHENPNVINCCVGDETMGQLLPHLHEQLEVCQKSLTGYLEKKRLLFPRFFFVSDPVLLEILGQASDSHTIQPHLPAVSDNINEVTFHAKDYDRIMAVISREGEKIVLDNSVMAKGPVEIWLLDLLKMQMSSLHNIIRSAFYQISDSGFQLLPFLSHFPAQVGLLGIQMLWTHDSEEALRNAKDDRKIMQVTNQKFLDILNTLISQTTHDLSKFDRVKFETLITIHVHQRDIFDDLVKMHIKSPTDFEWLKQSRFYFKEDLDQTVVSITDVDFIYQNEFLGCTDRLVITPLTDRCYITLAQALGMNMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDEFNRIELPVLSVAAQQIYIVLTARKERKKQFIFSDGDCVDLNPEFGIFLTMNPGYAGRQELPENLKIQFRTVAMMVPDRQIIMRVKLASCGFLENVILAQKFYVLYKLCEEQLTKQVHYDFGLRNILSVLRTLGSQKRARPEDSELSIVMRGLRDMNLSKLVDEDEPLFLSLINDLFPGLQLDSNTYAELQNAVAHQVQIEGLINHPPWNLKLVQLYETSLVRHGLMTLGPSGSGKTTVITILMKAQTECGRPHREMRMNPKAITAPQMFGRLDTATNDWTDGIFSTLWRKTLKAKKGENIFLILDGPVDAIWIENLNSVLDDNKTLTLANGDRIPMAPSCKLLFEVHNIENASPATVSRMGMVYISSSALSWRPILQAWLKKRTAQEAAVFLTLYEKVFEDTYTYMKLNLNPKMQLLECNYIVQSLNLLEGLIPSKEEGGVSCVEHLHKLFVFGLMWSLGALLELESREKLEAFLRQHESKLDLPEIPKGSNQTMYEFYVTDYGDWEHWNKKLQPYYYPTDSIPEYSSILVPNVDNIRTNFLIDTIAKQHKAVLLTGEQGTAKTVMVKAYLKKYDPEVQLSKSLNFSSATEPMMFQRTIESYVDKRIGSTYGPPGGRKMTVFIDDINMPVINEWGDQITNEIVRQMMEMEGMYSLDKPGDFTTIVDVQLIAAMIHPGGGRNDIPQRLKRQFTVFNCTLPSNASIDKIFGIIGCGYFDPCRSFKPQICEMIVNLVSVGRVLWQWTKVKMLPTPSKFHYIFNLRDLSRIWQGMLTIKAEECASIPTLLSLFKHECSRVIADRFITPEDEQWFNAHLTRAVEENIGSDAASCILPEPYFVDFLREMPEPTGDEPEDSVFEVPKIYELMPSFDFLAEKLQFYQRQFNEIIRGTSLDLVFFKDAMTHLIKISRIIRTSCGNALLVGVGGSGKQSLSRLASFIAGYQIFQITLTRSYNVTNLTDDLKALYKVAGADGKGITFIFTDSEIKDEAFLEYLNNLLSSGEISNLFARDEMDEITQGLISVMKRELPRHPPTFDNLYEYFISRSRKNLHVVLCFSPVGEKFRARSLKFPGLISGCTMDWFSRWPREALIAVASYFLSDYNIVCSSEIKRQVVETMGLFHDMVSESCESYFQRYRRRAHVTPKSYLSFINGYKNIYAEKVKFINEQAERMNIGLDKLMEASESVAKLSQDLAVKEKELAVASIKADEVLAEVTVSAQASAKIKNEVQEVKDKAQKIVDEIDSEKVKAESKLEAAKPALEEAEAALNTIKPNDIATVRKLAKPPHLIMRIMDCVLLLFQKKIDPVTMDPEKSCCKPSWGESLKLMSATGFLWSLQQFPKDTINEETVELLQPYFNMDDYTFESAKKVCGNVAGLLSWTLAMAIFYGINREVLPLKANLAKQEGRLAVANAELGKAQALLDEKQAELDKVQAKFDAAMNEKMDLLNDADTCRKKMQAASTLIDGLSGEKIRWTQQSKEFKAQINRLVGDILLCTGFLSYLGPFNQIFRNYLLKDQWEMELRARKIPFTENLNLISMLVDPPTIGEWGLQGLPGDDLSIQNGIIVTKATRYPLLIDPQTQGKTWIKSKEKENDLQVTSLNHKYFRTHLEDSLSLGRPLLIEDIHEELDPALDNVLEKNFIKSGTTFKVKVGDKECDIMDTFKLYITTKLPNPAFTPEINAKTSVIDFTVTMKGLENQLLRRVILTEKQELEAERVKLLEDVTFNKRKMKELEDNLLYKLSATKGSLVDDESLIGVLRTTKQTAAEVSEKLHVAAETEIKINAAQEEFRPAATRGSILYFLITEMSMVNIMYQTSLAQFLKLFDQSMARSEKSPLPQKRITNIIEYLTYEVFTYSVRGLYENHKFLFVLLMTLKIDLQRGTVKHREFQALIKGGAALDLKACPPKPYRWILDMTWLNLVELSKLPQFAEIMNQISRNEKGWKSWFDKDAPEEEIIPDGYNDSLDTCHKLLLIRSWCPDRTVFQARKYIADSLEEKYTEPVILNLEKTWEESDTRTPLICFLSMGSDPTNQIDALAKKLKLECRTISMGQGQEVHARKLIQMSMQQGGWVLLQNCHLGLEFMEELLETLITTEASDDSFRVWITTEPHDRFPITLLQTSLKFTNEPPQGVRAGLKRTFAGINQDLLDISNLPMWKPMLYTVAFLHSTVQERRKFGPLGWNIPYEFNSADFSASVQFIQNHLDECDIKKGVSWNTVRYMIGEVQYGGRVTDDFDKRLLNCFARVWFSEKMFEPSFCFYTGYKIPLCKTLDQYFEYIQSLPSLDNPEVFGLHPNADITYQSNTASAVLETITNIQPKESGGGVGETREAIVYRLSEDMLSKLPPDYIPHEVKSRLIKMGHLNSMNIFLRQEIDRMQRVISILRSSLSDLKLAIEGTIIMSENLRDALDNMYDARIPQLWKRVSWDSSTLGFWFTELLERNAQFSTWIFEGRPNVFWMTGFFNPQGFLTAMRQEVTRAHKGWALDTVTIHNEVLRQTKEEITSPPGEGVYIYGLYMDGAAWDRRNGKLMESTPKVLFTQLPVLHIFAINSTAPKDPKLYVCPIYKKPRRTDLTFITVVYLRTVLSPDHWILRGVALLCDIK', 4490, 'Q96JB1; O00438; Q5JYI2; Q5T2M3; Q5T2M4; Q5TG00; Q9UEM4;', 'KD01367', 'Homo sapiens (Human)', 'DNAH8', '#Dynein heavy chain 8; axonemal#Axonemal beta dynein heavy chain 8#Ciliary dynein heavy chain 8', '-', 'ENSG00000124721', '-'),
(1368, 'Q6CUV0', 'Probable kinetochore protein SPC25', 'GO:0000777', 26120, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MGIDDFNELKLKMDDFQSKIHQFLIKNNQDLATKSETYWNSESEKIKKIEALKDKLRQLEEHQISLEEEFESSQREVSEVNAQSKAFLTKRDKLIGEREFLHKELDKLDILLKEQTKDLEREKQSRLLQSSKDTNEVALFETLLGLHISANAQDAITFHFTSRTVDVSPQLSITLDVSQDTYKITDSNPKLPQIIKNDLLNNLAATDDLRSFLKAARSHLSALTEAT', 227, 'Q6CUV0;', 'KD01368', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '2892694'),
(1369, 'O13924', 'Serine/threonine-protein kinase haspin homolog hrk1', 'GO:0034501===GO:2000751', 56521, 'Serine/threonine haspin-like protein kinase involved in cell cycle regulation. Acts in chromosomal passenger complex (CPC) targeting to centromeres by phosphorylating histone H3 at ''Thr3'' (H3T3ph). {ECO:0000269|PubMed:20929775}.', 'MESRSKVKTYGKNRRYINKDIEIWASLDERPCALKPRNIENFNNQERSDLEHIHSKPKKDSLLSWNILLKKGSYKENELLAKRNQNLVPTVIIPASPRDNASKSVVSKKEVVNLSSSVALSGKPANNSKLDPLHRLLQIVAQEDALPFSQFVKSQTFEIQKIGEASYSEVYQASNADDVPVVWKVIPFGEDGQAQYADVLNEVQISQWIKVDGFANLHQVVVVKGTYPSLLLEEWDRYLMQNGSENDRPDSYSSTQLYCVLCLDHSGTDLEHFELRSWRECWSVFYETLKILSLVETRYEFEHRDLHWGNILIRKADRSEEEVSFLLNEISLDDIESVDFPGSQDKADDFDNILQVTLIDFTLARASYSQGIISYNEFNDPDLFNGVDDYQFDIYRLMSRVTKGRWAQFFPITNVLWLHYLIHQLLHKKNLSSPLTETETLMRSRLKQIFRLIDPVKTMQFQQAEDSIRSKSTVTSATSLLNWVRQKY', 488, 'O13924;', 'KD01369', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hrk1', '#Serine/threonine-protein kinase haspin homolog hrk1#2.7.11.1', '-', '-', '2541959'),
(1370, 'Q5R7D8', 'Dynactin subunit 6', 'GO:0000777', 20713, '', 'MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQALIINAYPDNITPDTEDPEPKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPQTLQLDLLMKILPNYHHLKKTMKGSSTPVKN', 190, 'Q5R7D8;', 'KD01370', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'DCTN6', '#Dynactin subunit 6#Dynactin subunit p27', '-', '-', '100174616'),
(1371, 'Q8IX90', 'Spindle and kinetochore-associated protein 3', 'GO:0000940===k', 46359, '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. {ECO:0000269|PubMed:19289083; ECO:0000269|PubMed:19360002}.', 'MDPIRSFCGKLRSLASTLDCETARLQRALDGEESDFEDYPMRILYDLHSEVQTLKDDVNILLDKARLENQEGIDFIKATKVLMEKNSMDIMKIREYFQKYGYSPRVKKNSVHEQEAINSDPELSNCENFQKTDVKDDLSDPPVASSCISEKSPRSPQLSDFGLERYIVSQVLPNPPQAVNNYKEEPVIVTPPTKQSLVKVLKTPKCALKMDDFECVTPKLEHFGISEYTMCLNEDYTMGLKNARNNKSEEAIDTESRLNDNVFATPSPIIQQLEKSDAEYTNSPLVPTFCTPGLKIPSTKNSIALVSTNYPLSKTNSSSNDLEVEDRTSLVLNSDTCFENLTDPSSPTISSYENLLRTPTPPEVTKIPEDILQLLSKYNSNLATPIAIKAVPPSKRFLKHGQNIRDVSNKEN', 412, 'Q8IX90; A2A330; A2A331; B2RBY2; Q5VZV5; Q86WR2; Q8NBG1; Q96D22;', 'KD01371', 'Homo sapiens (Human)', 'SKA3', '#Spindle and kinetochore-associated protein 3', '-', 'ENSG00000165480', '-'),
(1372, 'Q0P5A1', 'Dynactin subunit 3', 'GO:0000777', 21192, 'Together with dynein may be involved in spindle assembly and cytokinesis. {ECO:0000250}.', 'MAAVTDVQRLQARVEELERWVYGPGGSRGSRKVADGLVKVQVALGNIASKRERVKVLYKKIEDLIKYLDPEYIDRIALPDASKLQFILAEEQFILSQVALLEQVEALVPMLDSTHIKAVPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAAKQVKPVEE', 186, 'Q0P5A1;', 'KD01372', 'Bos taurus (Bovine)', 'DCTN3', '#Dynactin subunit 3', '-', '-', '514327'),
(1373, 'U3H042', 'Kinetochore protein Sos7', 'GO:0051382===GO:0034501===GO:0000778===GO:0051315===GO:0031617===SCL', 30523, '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. Essential for chromosome segregation and bipolar sister chromatid association. Required for kinetochore targeting of MIND; but not Ndc80 complex components. {ECO:0000269|PubMed:22711988}.', 'MDQNKSTQATGNGKKTEEINELLESFIKEGPKLLWGSTNLKYEDQISRSSEHELQQYRELFTRLKFSYIEQGTKERYLRAILDDPPMLVEAEDNEKLETTNSSLKGRLKSEKREVDLLTEELKTTSRELSSNYESVMEECKNTKSTLSKLESLESELLKLQQDSSTKTPILPEVEAAIHDLESELNITNESIETIDGKIDNDEKYFIQLTKNLSLLEKEYKIASERSNQIKAAIHTRTPDADAKKQVQNWYTSMLEIYDQLLQK', 264, 'U3H042;', 'KD01373', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'sos7', '#Kinetochore protein Sos7#Suppressor of spc7 protein', '-', '-', '3361402'),
(1374, 'Q9VS01', 'CG18156-PARE19545p', 'k', 21150, '', 'MDFNSLAYDQKFFNFTAAQLSAEREHIVQDIIKKGIGQIIDKIKTPATAELLEAEKETVERRFQASASKGLKALRELDSKVFHVPPHVLHPEHMFVENQYTSEEEEQKTARLEELKAKYRENMAMLAHLKIEEEKYAAMEDLIQKEIEMQDRVQRSCSSLNITKLKQFWNQVPLQIKKETD', 181, 'Q9VS01;', 'KD01374', 'Drosophila melanogaster (Fruit fly)', 'Mis12', '#CG18156-PA {ECO:0000313|EMBL:AAF50629.1}#RE19545p {ECO:0000313|EMBL:AAL48781.1}', '-', '-', '38762'),
(1375, 'E1BSW7', 'Centromere protein S', 'GO:0000777', 15619, '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. 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 (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}.', 'MEAAGGEQRELLIQRLRAAVHYTTGCLCQDVAEDKGVLFSKQTVAAISEITFRQCENFARDLEMFARHAKRSTITSEDVKLLARRSNSLLKYITQKSDELASSNMEQKEKKKKKSSAAKGRKTEENETPVTESEDSNMA', 139, 'E1BSW7;', 'KD01375', 'Gallus gallus (Chicken)', 'APITD1', '#Centromere protein S#CENP-S', '-', '-', '771417'),
(1376, 'Q9Z0W3', 'Nuclear pore complex protein Nup160', 'GO:0000776', 158232, 'Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11684705}.', 'MAAAGSLERSFVELSGAERERPRHFREFTVCDIGTASAAFGTVKYSESAGGFYYVESGKLFSITRNRFIHWKTSGDTLELVEESLDLNLLNNAVRLKFQNYNILPGGVHVSETQNHVIILILTNQTVHRLILPHPSRMYRSELVTESQMQSIFTDIGKVDFRDPCNSQLIPSVPGLSPGSTTSAAWLSSDGEALFALPSASGGIFVLKLPPYDVPGIASVVELKQSSVMQRLLTGWMPTAIRGDHGPSDRALSLAVHCVEHDAFIFALCQDHKLRMWSYKDQMCLMVADMLEYVPVNKDLRLTAGTGHKLRLAYSPSMGLYLGIYMHAPKRGQFCVFQLVSTENNRYSLDHISSLFTSQETLVDFALTSTDIWALWHDAENQTIVKYINFEHNVAGQWNPVFMQPLPEEEIVIRDDQDPREMYLRSLFTPGHFINAALCKALQIFCRGTERNLDLSWNELKKEITLAVENELQGSVTEYEFSQDEFRTLQQEFWCKFYACVLQYQEALSHPLALHLNPVTNMVCLLKKGYLSFLVPSSLVDHLYLLPDEHLLTEDETTISDDADVARDVLCLIKCLRMIGESVTMDMAVLMETSCYNLQSPEKAAEHILEDLITIDVENVMEDICSKLQEIRNPVHAIGLLIREMDYETEVEMEKGFDPAQPLNVRMNLSQLYGSSTAGYIVCRGVYKIASTRFLICRDLLILQQLLTRLGDAVILGAGQLFQAQQDLLHRTAPLLLSYYLIKWASQCLATDVPVDTLESNLQHLSVLELTDSGALMANKLVSSPQTIMELFFQEVARKQIISHLFSQPKAPLSQTGLNWPEMITAVTGYLLQLLWPSNPGCLFLECLMGNCQYVQLQDYIQLLHPWCQVNVGSCRFMLGRCYLVTGEVQKALECFCQAASEVGKEEFLDRLIRSEDGEIVSTPKLQYYDKVLRLLDVVGLPELVIQLATSAITEAGDDWKSQATLRTCIFKHHLDLGHNSQAYEALTQIPDSSRQLDCLRQLVVVLCERSQLQDLVEFPYVNLHNEVVGIIESRARAVDLMTHNYYELLYAFHIYRHNYRKAGTVMFEYGMRLGREVRTLRGLEKQGNCYLAAINCLRLIRPEYAWIVQPASGAVSDRPGASPKRNHDGECTAAPTNRQIEILELEDLEKEYSLARIRLTLARHDPSVIAIAGSSSAKEMSALLVQAGLFDTAISLCQTFTLPLTPVFEGLAFKCIKLQFGGEAAQGEAWSWLATNQLSSVITTKESSATDEAWRLLSTYLERYKVQNNLYHHCVINKLLSHGVPLPNWLINSYKKVDAAELLRLYLNYDLLEEAVDLVSEYVDAVLGKGHQYFGIEFPLSATAPMVWLPYSSIDQLLQALGENSANSHNIILSQKILDKLEDYQQKVDKATRDLLYRRDL', 1402, 'Q9Z0W3; Q3TBI7; Q3TP11; Q3U250; Q6A0A7; Q7TME1; Q9CZD9;', 'KD01376', 'Mus musculus (Mouse)', 'Nup160', '#Nuclear pore complex protein Nup160#160 kDa nucleoporin#Gene trap locus 1-13 protein#GTL-13#Nucleoporin Nup160', '-', '-', '59015'),
(1377, 'Q9C0G6', 'Dynein heavy chain 6; axonemal', 'GO:0003777', 475983, '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 (By similarity). {ECO:0000250}.', 'MTFRATDSEFDLTNIEEYAENSALSRLNNIKAKQRVSYVTSTENESDTQILTFRHITKAQEKTRKRQQPIKLEPLPVLKVYQDHKQPEYIHEQNRFQLMTAGIIKRPVSIAKKSFATSSTQFLEHQDAVKKMQIHRPYVEVFSPSPPKLPHTGIGKRGLFGTRSSAYPKYTFHDREEVVKANIRDPLQIIKIIRENEHLGFLYMIPAVPRSSIEYDTYNLKVVSYENINKNDYYTISQRAVTHIYNEDIEFIEIDRWEQEYLYHRELTKIPIFSLFRKWKAFSVWRKNVRSKKITGCQKSLQKNLFIVNPHLRPALLKINELCYHLSFMGLCYIEKCHTYTLQEFKAAQVIRLAEVTERLGEFRNEAKYVVRRACRFALRAAGFVPDDCAFGPFEDYHKVQSSGSFINTPHELPTYGDSEKMTYTEQASKRHYCMRLTCFIRLNDYLIENTMHILTVNAVNSLLNHLTDKLKRTPSADVIQKWITEEKPEVPDKKGTLMVEKQEEDESLIPMFLTELMLTVQSLLFEPSLEDFLDGILGAVNHCQNTVLSVPNLVPDSYFDAFTSPYINNKLEGKTCGTGPSLAAVFEDDKNFHTIISQIKETIQAAFESARIYAATFEKFQIFFKENESLDLQALKLQEPDINFFSEQLEKYHKQHKDAVALRPTRNVGLLLIDTRLLREKLIPSPLRCLEVLNFMLPRQSKKKVDAIIFEAQDAEYKLEFVPTTTTEYVHSLLFLDEIQERIESLEDEGNIVTQMYKLMEQYQVPTPPEDFAVFATMKPSIVAVRNAIDKSVGDRESSIKQFCVHLGSDLEELNNEVNEVKLQAQDPQILDISADQDKIRLILNNLQSVLADLQKRAFQYKSYQKNFKVEVSKFEALEEVSAELKLKQLLWDSFSEWDKLQQEWLKSKFDCLDPEVLNGQVSKYAKFVTQLEKGLPPNSVVPQLKYKVEKMKEKLPVIIDLRNPTLKARHWAAIEQTVDATLVDAEIPLTLERLSQLHVFDFGQEIQDISGQASGEAALEAILKKVEDSWKTTEFVILPHRDSKDVFILGGTDDIQVLLDDSTINVATLASSRYLGPLKTRVDEWQKQLALFNQTLEEWLTCQRNWLYLESIFNAPDIQRQLPAEAKMFLQVDKSWKEIMRKVNRLPNALRAATQPGLLETFQNNNALLDQIQKCLEAYLESKRVIFPRFYFLSNDELLEILAQTRNPQAVQPHLRKCFDSISKLEFALMPPAEGKIPGIDGEPEKVYTNDILAMLSPEGERVSLGKGLKARGNVEEWLGKVEEAMFTSLRRLCKAAIADYQGKLRTDWVVAGHPSQVILTVSQIMWCRDLTECLETEHSNHIQALKNFEKVNFERLNALAAIVQGSLPKLHRNILTALITIDVHARDIVTELVQSKVETVESFDWQRQLRYYWDIDLDNCVARMALSQYTYGYEYLGACPRLVITPLTDRCYLCLMGALQLDLGGAPAGPAGTGKTETTKDLAKALAIQCVVFNCSDGLDYKMMGRFFSGLAQSGAWCCFDEFNRIDIEVLSVIAQQLITIRNAKAAKLSRFMFEGREIKLVMTCAAFITMNPGYAGRTELPDNLKALFRPFAMMVPNYALIAEVILYSEGFESSKILARKMTQMYKLCSEQLSQQDHYDFGMRAVKSVLVMAGSLKRENPDLNEDVVLIRALQDSNLPKFLTDDALLFSGIISDLFPGVQIPEHDYGILQSTIVDVMNRQNLQPEMCMVRKVIQFYETMLVRHGVMLVGPTGGGKTTVYRILAETLGNLQKLGIENSFYQAVKTYVLNPKSITMGELYGEVNNLTLEWKDGLMALSVRAAVNDTSEDHKWIISDGPVDALWIENMNTVLDDNKMLCLANSERIKLTPQIHMLFEVQDLRVASPATVSRCGMVFVDPEELKWMPYVKTWMKGISKKLTEETQEYILNLFQRYVDEGLHFINKKCSQAIPQVDISKVTTLCCLLESLILGKDGVNLAMEQTKLNTILCQTFVFCYLWSLGGNLTENYYDSFDTFIRTQFDDNPDARLPNSGDLWSIHMDFDTKRLDPWERIIPTFKYNRDVPFFEMLVPTTDTVRYGYLMEKLLAVKHSVLFTGITGVGKSVIAKGLLNKIQESAGYVPVYLNFSAQTSSARTQEIIESKLERKRKNILGAPGNKRIVIFVDDLNMPRLDRYGSQPPIELLRQYQDFGGFYDRNKLFWKEIQDVTIISACAPPGGGRNPVTPRFIRHFSMLCLPMPSEHSLKQIFQAILNGFLSDFPPAVKQTASSIVEASVEIYNKMSVDLLPTPAKSHYVFNLRDLSKCVQGILQCDPGTIREEIQIFRLFCHECQRVFHDRLINNEDKHYFHVILTEMANKHFGIAIDLEYFLNKPIIFGDFIKFGADKADRIYDDMPDIEKTANVLQDYLDDYNLTNPKEVKLVFFQDAIEHVSRIARMIRQERGNALLVGVGGTGKQSLTRLAAHICGYKCLQIELSRGYNYDSFHEDLRKLYKMAGVEDKNMVFLFTDTQIVVEEFLEDINNILNSGEVPNLFEKDELEQVLAATRPRAKEVGISEGNRDEVFQYFISKVRQKLHIVLCMSPVGEAFRSRCRMFPSLVNCCTIDWFVQWPREALLSVSKTFFSQVDAGNEELKEKLPLMCVNVHLSVSSMAERYYNELRRRYYTTPTSYLELINLYLSMLSEKRKQIISARDRVKNGLTKLLETNILVDKMKLDLSALEPVLLAKSEDVEALMEKLAVDQESADQVRNTVQEDEATAKVKAEETQAIADDAQRDLDEALPALDAANKALDSLDKADISEIRVFTKPPDLVMTVMEAISILLNAKPDWPSAKQLLGDSNFLKRLLEYDKENIKPQILAKLQKYINNPDFVPEKVEKVSKACKSMCMWVRAMDLYSRVVKVVEPKRQKLRAAQAELDITMATLREKQALLRQVEDQIQALQDEYDKGVNEKESLAKTMALTKARLVRAGKLTAALEDEQVRWEESIQKFEEEISNITGNVFIAAACVAYYGAFTAQYRQSLIECWIQDCQSLEIPIDPSFSLINILGDPYEIRQWNTDGLPRDLISTENGILVTQGRRWPLMIDPQDQANRWIRNKESKSGLKIIKLTDSNFLRILENSIRLGLPVLLEELKETLDPALEPILLKQIFISGGRLLIRLGDSDIDYDKNFRFYMTTKMPNPHYLPEVCIKVTIINFTVTKSGLEDQLLSDVVRLEKPRLEEQRIKLIVRINTDKNQLKTIEEKILRMLFTSEGNILDNEELIDTLQDSKITSGAIKTRLEEAESTEQMINVAREKYRPVATQGSVMYFVIASLSEIDPMYQYSLKYFKQLFNTTIETSVKTENLQQRLDVLLEQTLLTAYVNVSRGLFEQHKLIYSFMLCVEMMRQQGTLSDAEWNFFLRGSAGLEKERPPKPEAPWLPTATWFACCDLEESFPVFHGLTQNILSHPISIRLGSFETYINPQKWEGYSKMKHEDKHMRQEKEAAHQDPWSAGLSSFHKLILIKCCKEEKVVFALTDFVIENLGKQFIETPPVDLPTLYQDMSCNTPLVFILSTGSDPMGAFQRFARESGYSERVQSISLGQGQGPIAEKMVKDAMKSGNWVFLQNCHLAVSWMLAMEELIKTFTDPDSAIKDTFRLFLSSMPSNTFPVTVLQNSVKVTNEPPKGLRANIRRAFTEMTPSFFEENILGKKWRQIIFGICFFHAIIQERKKFGPLGWNICYEFNDSDRECALLNLKLYCKEGKIPWDALIYITGEITYGGRVTDSWDQRCLRTILKRFFSPETLEEDYKYSESGIYFAPMADSLQEFKDYIENLPLIDDPEIFGMHENANLVFQYKETSTLINTILEVQPRSSTGGEGKSNDEIVQELVASVQTRVPEKLEMEGASESLFVKDLQGRLNSLTTVLGQEVDRFNNLLKLIHTSLETLNKAIAGFVVMSEEMEKVYNSFLNNQVPALWSNTAYPSLKPLGSWVKDLILRTSFVDLWLKRGQPKSYWISGFFFPQGFLTGTLQNHARKYNLPIDELSFKYSVIPTYRDQAAVIEAAKTVQFGQELPMDMELPSPEDGVLVHGMFMDASRWDDKEMVIEDALPGQMNPVLPVVHFEPQQNYKPSPTLYHCPLYKTGARAGTLSTTGHSTNFVVTVLLPSKRSKDYWIAKGSALLCQLSE', 4158, 'Q9C0G6; A0PJN9; B5MEE0; B7ZL99; O95493; Q53QZ1; Q53TE5; Q8N1W6;Q92861; Q96BL6; Q9H030; Q9H5E1;', 'KD01377', 'Homo sapiens (Human)', 'DNAH6', '#Dynein heavy chain 6; axonemal#Axonemal beta dynein heavy chain 6#Ciliary dynein heavy chain 6', '-', 'ENSG00000115423', '-'),
(1378, 'P26358', 'DNA (cytosine-5)-methyltransferase 1', 'k', 183165, 'Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand; that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B 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. {ECO:0000269|PubMed:16357870; ECO:0000269|PubMed:18413740; ECO:0000269|PubMed:18754681}.', 'MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD', 1616, 'P26358; A0AV63; B7ZLW6; Q9UHG5; Q9ULA2; Q9UMZ6;', 'KD01378', 'Homo sapiens (Human)', 'DNMT1', '#DNA (cytosine-5)-methyltransferase 1#Dnmt1#2.1.1.37#CXXC-type zinc finger protein 9#DNA methyltransferase HsaI#DNA MTase HsaI#M.HsaI#MCMT', '-', 'ENSG00000130816', '-'),
(1379, 'Q09725', 'Sister chromatid cohesion protein mis4', 'GO:0051315', 180725, 'Plays a structural role in chromatin. Chromatid cohesion molecule required for equal sister chromatid separation in anaphase. May form a stable link between chromatids in S phase that is split rather than removed in anaphase. Also required for spindle-kinetochore interaction in early mitosis and inhibit sister chromatid separation until the cleavage of Rad21 in anaphase. {ECO:0000269|PubMed:11882285}.', 'MLFEMTPETFKKVNSSNRIIKGLQYTPLASSIPLENGLQNVLYPSSKFQNEPLQLNSEESSIMQRYVDMLNPGATFVNDSETFNFYKNALSAMITEPAMPAMRVNASPVLDQKVCNSDSLSELNDFTKSLIQPSMLMCEPKEKPDASSINTNRSSSDNGFLTPSSSPRSPSCSRVFNAVQLCSPKKSKDDITTPKKRLMEDTYSPRESPSKIQRLQDVLLKQLQDTRLLISQVIEAENSEDFSSNSLFIKREDDDGKHISSHAIEKLYMALTKLSRLGACDKLLEEGSIILVKQILEKELKELPVACYSIINLHDSLTQFPNLDFILKTTALVLFIIFLVPSFKKLQNEESILHLLNILHSIFEYTVPEAIDNIVQSKTSDARTSEIQHLSVLLQKVANVLNILSKVAHEIPLSEAVVIRIVYLFPKVSTLDNSFKTKLPNCNSSSFDFLKAPLFQTLQYLFRLYPYQRDFIIEESLTNFSHLPTARSVSRTYRLSNGKSIQYYSTLFVRLIQSCSIQNLFDSEIVQSESKSTEALHSGNLTEHLKTVESILSKSRHEEYRIANHIVAYLLSRSLKQNKTESDNSFAILTKILLEDLLNMLSLPEWCGTETIIRQFAMNLVMTVTNDKQAVSSKNAALDLISLIVNKVLALFDLSLFEKHNIPAPTNFNDIISFIPSITRLNELSQVSFNHFYFLCKGDISLENILPYNYNKWFSFLLQLRKVCNDSEALKIIDNCIDKNMQKSQEGFQGPSPFKADENDEDIFIISLYHSSLFLNLKFFVSLIIGFLDSPQASLRTKCLRIINQMKTIPSILRTHPEVLAQIISKSNDQSAIVRDTVLDLLGTYIMAYRETIPQIYGCIISGISDPSTIVRKRAIKQLCEVYEATEDLNIRVDIASKLLTRSNDEEETISELSLEVLEKLWFSPASNELDCQKGYEQLTFLEKQKLRVQYFPILKLCAEPSTERHVLLVTSLKTMLTSKEEINLSTLHTQIRLLLSCLFNQLIEVVTEDQVDESTKGILYEIMSTLFVFSRAFPFLFDLSYLHLLKPYLRSASTIEEQRFLYYVVAIFRQVLPFQKEISESFLRSLESVLLQRLTKAGTATLMEIVPCLCSLFTRLNDYERLKKIVVSCLKSLEEARHSENNFQKMVRLIDLIGLFSRYGDLNRINDDWKHSLDFISPECDDAYVILLGYFQKLLKDAKGQLRIHIIDNMSRICLRETSLFISPLMLSTLDMIIAENNVNEVSVLFKSFLELLAADEDLIFEADQKLSLKGKQNVQSNKSVDRDMLKGTKDKQWIEGVSASLMQHFLPCILDSCFSKNLRYSMLGIEILKCIIHQGLVNPRMCFSTIIALESNAIKETREVAILLHTELHRRHESLIDGLYAQSADLIFSLQKTEEYQTFKLGEFSPFQSAYTIVSADKSSKSRKKLIMQILKPLKLDGIDLPSFTEEKVSFVSFCCVCLAGIPYVSIEEPLMIISTVDSVLATIGPTITGWMKKLDHERFKILAGINLCNLIYLKRYIKYAFSISDSSRPIREKKPLTLLNRGYVDLITSDAKPDIVSKLVIKLFEEENILSGEDQVEGEQLTVV', 1587, 'Q09725;', 'KD01379', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis4', '#Sister chromatid cohesion protein mis4#SCC2 homolog', '-', '-', '2542657'),
(1380, 'Q66JL0', 'Nuclear distribution protein nudE homolog 1', 'GO:0000776', 39553, 'Required for centrosome duplication and formation and function of the mitotic spindle. {ECO:0000250}.', 'MDDLENNIFNSVEEEIIYWKSVAMKYKTCSEEAQQELQEFQEASREYEAELEAQLQQIEGRNRDLFSENNRLRMELDGIKEKYEEQHSENYVQICSLEGDLSQTKAVRDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPKSNMGSPETERMDTSVKASVAIPSAPLTPLSQRGCASTLTSPLSFRTSLDDGYSGTPLTPCARISALNIVGDLLRKVGALESKLASCRNFVHEQSPNRPLTSVSARMNKTREGIENRLSMASGSSVEKGLIKRLEFGSLPSNTPVQGMHSPQGVVKMII', 349, 'Q66JL0;', 'KD01380', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'nde1', '#Nuclear distribution protein nudE homolog 1', '-', '-', '493358'),
(1381, 'Q09732', 'Sister chromatid cohesion protein dcc1', 'GO:0051455', 41954, 'Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Replication factor C (RFC) complex has an essential but redundant activity in sister chromatid cohesion establishment. An RFC-like complex (ctf18-RFC) is formed where ctf18 replaces rfc1 in the RFC complex along with the association of dcc1 and ctf8. This complex is required for efficient establishment of chromosome cohesion during S-phase. Acts as a PCNA loader; loading PCNA onto primed templates. {ECO:0000269|PubMed:15226378}.', 'MEANEERCILLKYPHPSSDISSEYLLLELDDDLLKTLEENPEEEIVFKSDFDKKASVLCTSDKTYAVRQVVQSNSYLLFDELSPTDWVLNDTCYSFLEVERIYGFIFSDDKISYWDEDSVELKPISLTKDQFIRSVPASRNEVDSFLQKNFFMVKNEFLYRLSPSYICSIIDWIFVIAQQLHIDFASFEFKILKKPAMDDEFDWDSVICVLESISSPIKDNVLPKKFNIDLELTTFWYGRFLLEGINSISSDEFIQLWDNRLPYPCKGLPSLNLLKGYYFHDTPNTIQYLSGDQLPREPSRRFQSLFQLKSKWLYEELWSFVKDLALSKSRVEALILKYGRKQTSRDGVYINSRGTW', 357, 'Q09732;', 'KD01381', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dcc1', '#Sister chromatid cohesion protein dcc1#Defective in sister chromatid cohesion protein 1', '-', '-', '2543078'),
(1382, 'Q6P0N0', 'Mis18-binding protein 1', 'k', 129085, 'Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038; ECO:0000269|PubMed:17339379}.', 'MIATPLKHSRIYLPPEASSQRRNLPMDAIFFDSIPSGTLTPVKDLVKYQNSSLKLNDHKKNQFLKMTTFNNKNIFQSTMLTEATTSNSSLDISAIKPNKDGLKNKANYESPGKIFLRMKEKVLRDKQEQPSRNSSLLEPQKSGNNETFTPNRVEKKKLQHTYLCEEKENNKSFQSDDSSLRASVQGVPLESSNNDIFLPVKQKIQCQQEKKAPLHNLTYELPTLNQEQENFLAVEARNKTLTRAQLAKQIFHSKESIVATTKSKKDTFVLESVDSADEQFQNTNAETLSTNCIPIKNGSLLMVSDSERTTEGTSQQKVKEGNGKTVPGETGLPGSMKDTCKIVLATPRLHITIPRRSKRNISKLSPPRIFQTVTNGLKKNQVVQLQEWMIKSINNNTAICVEGKLIDVTNIYWHSNVIIERIEHNKLRTISGNVYILKGMIDQISMKEAGYPNYLIRKFMFGFPENWKEHIDNFLEQLRAGEKNREKTKQKQKTGRSVRDIRKSMKNDARENQTDTAQRATTTYDFDCDNLELKSNKHSESPGATELNMCHSNCQNKPTLRFPDDQVNNTIQNGGGDDLSNQELIGKKEYKMSSKKLKIGERTNERIIKSQKQETTEELDVSIDILTSREQFFSDEERKYMAINQKKAYILVTPLKSRKVIEQRCMRYNLSAGTIKAVTDFVIPECQKKSPISKSMGTLENTFEGHKSKNKEDCDERDLLTVNRKIKISNLEKEQMLTSDFKKNTRLLPKLKKIENQVAMSFYKHQSSPDLSSEESETEKEIKRKAEVKKTKAGNTKEAVVHLRKSTRNTSNIPVILEPETEESENEFYIKQKKARPSVKETLQKSGVRKEFPITEAVGSDKTNRHPLECLPGLIQDKEWNEKELQKLHCAFASLPKHKPGFWSEVAAAVGSRSPEECQRKYMENPRGKGSQKHVTKKKPANSKGQNGKRGDADQKQTIKITAKVGTLKRKQQMREFLEQLPKDDHDDFFSTTPLQHQRILLPSFQDSEDDDDILPNMDKNPTTPSSVIFPLVKTPQCQHVSPGMLGSINRNDCDKYVFRMQKYHKSNGGIVWGNIKKKLVETDFSTPTPRRKTPFNTDLGENSGIGKLFTNAVESLDEEEKDYYFSNSDSA', 1132, 'Q6P0N0; D3DSA7; Q86V14; Q96PY4; Q9NUR5; Q9Y4X9;', 'KD01382', 'Homo sapiens (Human)', 'MIS18BP1', '#Mis18-binding protein 1#Kinetochore-associated protein KNL-2 homolog#HsKNL-2#P243', '-', 'ENSG00000129534', '-'),
(1383, 'O93308', 'Structural maintenance of chromosomes protein 1A', 'GO:0000776', 142628, 'Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is 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.', 'MGFLKLIEIENFKSYKGRQIIGPFHRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEDSGEEKVFSRVIVGGSSEYKINNKVVQLSEYSDSLEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEAERYQRLKDEVARAQIQLQLFKLYHNESEIEKLNKELSVKNKGIEKDKKHMDKVEEELKDKKKELGKMMREQQAIEKEIKEKDAELNQKLPQYIKAKENPSHKIKKFRAAKKSLQNAQKQYKKRKADMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLRELEENQKRIEKLEEYIATSKQSLEEQKNLEETLTEEVEMAKRRIDEINSELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDERLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLAMNMQEKSKLESELANFSPRINDIKRIIQSRDREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDYEKNQLKEDQGKVQTWEQSVKKDDNEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHLMEDIRKKLGSANKEVTHLQKEVTAIETKLEQKRSDRHNLLQACKMSDIKLPLSKGTMDDISQEEGSSQGEESASSSQRSSTVYAKEALIEIDYSDLSEDLKDAVADDDIKQEMSALHQKINEQQSILQRISAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQTKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPSPFFVLDEIDAALDNTNIGKVANYIKEQSMSNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPND', 1232, 'O93308;', 'KD01383', 'Xenopus laevis (African clawed frog)', 'smc1a', '#Structural maintenance of chromosomes protein 1A#SMC protein 1A#SMC-1A#xSMC1', '-', '-', '100379087'),
(1384, 'Q7M6U3', 'Inactive serine/threonine-protein kinase TEX14', 'GO:0000776===GO:0000777===GO:0008608', 162541, '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. {ECO:0000269|PubMed:16549803; ECO:0000269|PubMed:19020301; ECO:0000269|PubMed:20176808; ECO:0000269|PubMed:22405274}.', 'MSRGAPFPVPCPVLLGTFTDDSLEAQLHEYAKQGNCVKLKKILKKGVCVDAVNTQGQSALFVAALLGHVKLVDVLVDYGSDPNHRCFDGSTPVHAAAFSGNQWILSKLLTAGGDLRLHDEKGRNPQAWALTAGKDRSTQMVEFMQRCTSHMKAIIQGFSYDLLKKIDSPQRLIGSPPWFGSLIQGSPNSSPNRQLKPGIISAQNIYSFGFGKFYLTSGMQLTYPGSLPVIGEKEVVQADDEPTFSFFSGPYMVMTNLVWNRSRVTVKELNLPTRPHCSRLRLADLLIAEQEHSSNLRHPNLLQLMAVCLSRDLEKIRLVYERITVGTLFSVLHERRSQFPVLHMEVIVHLLLQVADALIYLHSRGFIHRSLSSYAVHIVSAGEARLTNLEYLTESQDSGAHRNVTRMPLPTQLYNWAAPEVVLQKAATVKSDIYSFSVIIQEILTDSIPWNGLDGSLVKETIALGNYLEADVRLPEPYYDIVKSGIHAKQKNRTMNLQDIRYILKNDLKEFIGAQKTQPTESPRGQSYEPHPDVNICLGLTSEYQKDPPDLDIKELKEMGSQPHSPTDHSFLTVKPTLAPQTLDSSLSAQKPDNANVPSPPAACLAEEVRSPTASQDSLCSFEINEIYSGCLTLGTDKEEECLGTAASPEGDRPNQGDELPSLEEELDKMERELHCFCEEDKSISEVDTDLLFEDDDWQSDSLGSLNLPEPTREAKGKTSSWSKTDEYVSKCVLNLKISQVMMQQSAEWLRKLEQEVEELEWAQKELDSQCSSLRDASLKFANAKFQPAVGPPSLAYLPPVMQLPGLKQPENGGTWLTLARSPGNEREFQEGHFSKKPEKLSACGWKPFTQVSEESRGDCSELNNQLPTLRGPGKQSTGEQLPSTQEARESLEKNTNQNSRSMASVSSEIYATKSRNNEDNGEAHLKWRLAVKEMAEKAVSGQLLLPPWNPQSSAPFESKVENESTPLPRPPIRGPESTEWQHILEYQRENDEPKGNTKFGKMDNSDCDKNKHSRWTGLQRFTGIRYPFFRNHEQPEQNEASQASCDTSVGTEKFYSTSSPIGDDFERFQDSFAQRQGYVEENFQIREIFEKNAEILTKPQFQAIQCAEDKQDETLGETPKELKEKNTSLTDIQDLSSITYDQDGYFKETSYKTPKLKHAPTSASTPLSPESISSAASHYEDCLENTTFHVKRGSTFCWNGQEAMRTLSAKFTTVRERAKSLESLLASSKSLPAKLTDSKRLCMLSETGSSNVSAAFVTSTHATKRKSLPRELAEATSQQHLDELPPPAQELLDEIEQLKQQQVSSLASHENTARDLSVTNKDKKHLEEQETNSSKDSSFLSSREIQDLEDTERAHSSLDEDLERFLQSPEENTALLDPTKGSTREKKNKDQDVVEQKRKKKESIKPERRESDSSLGTLEEDELKPCFWKRLGWSEPSRIIVLDQSDLSD', 1450, 'Q7M6U3; B2KGL0; Q3UT36; Q5NC10; Q5NC11; Q8CGK1; Q8CGK2; Q99MV8;', 'KD01384', 'Mus musculus (Mouse)', 'Tex14', '#Inactive serine/threonine-protein kinase TEX14#Testis-expressed sequence 14#Testis-expressed sequence 14 protein', '-', '-', '83560');
