INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(558, 'Q15398', 'Disks large-associated protein 5', 'k;s', 95115, 'Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. {ECO:0000269|PubMed:12527899; ECO:0000269|PubMed:14699157; ECO:0000269|PubMed:15145941}.', 'MSSSHFASRHRKDISTEMIRTKIAHRKSLSQKENRHKEYERNRHFGLKDVNIPTLEGRILVELDETSQGLVPEKTNVKPRAMKTILGDQRKQMLQKYKEEKQLQKLKEQREKAKRGIFKVGRYRPDMPCFLLSNQNAVKAEPKKAIPSSVRITRSKAKDQMEQTKIDNESDVRAIRPGPRQTSEKKVSDKEKKVVQPVMPTSLRMTRSATQAAKQVPRTVSSTTARKPVTRAANENEPEGKVPSKGRPAKNVETKPDKGISCKVDSEENTLNSQTNATSGMNPDGVLSKMENLPEINTAKIKGKNSFAPKDFMFQPLDGLKTYQVTPMTPRSANAFLTPSYTWTPLKTEVDESQATKEILAQKCKTYSTKTIQQDSNKLPCPLGPLTVWHEEHVLNKNEATTKNLNGLPIKEVPSLERNEGRIAQPHHGVPYFRNILQSETEKLTSHCFEWDRKLELDIPDDAKDLIRTAVGQTRLLMKERFKQFEGLVDDCEYKRGIKETTCTDLDGFWDMVSFQIEDVIHKFNNLIKLEESGWQVNNNMNHNMNKNVFRKKVVSGIASKPKQDDAGRIAARNRLAAIKNAMRERIRQEECAETAVSVIPKEVDKIVFDAGFFRVESPVKLFSGLSVSSEGPSQRLGTPKSVNKAVSQSRNEMGIPQQTTSPENAGPQNTKSEHVKKTLFLSIPESRSSIEDAQCPGLPDLIEENHVVNKTDLKVDCLSSERMSLPLLAGGVADDINTNKKEGISDVVEGMELNSSITSQDVLMSSPEKNTASQNSILEEGETKISQSELFDNKSLTTECHLLDSPGLNCSNPFTQLERRHQEHARHISFGGNLITFSPLQPGEF', 846, 'Q15398; A8MTM6; B4DRM8; Q86T11; Q8NG58;', 'KD00558', 'Homo sapiens (Human)', 'DLGAP5', '#Disks large-associated protein 5#DAP-5#Discs large homolog 7#Disks large-associated protein DLG7#Hepatoma up-regulated protein#HURP', '-', 'ENSG00000126787', '-'),
(559, 'Q8C4X1', 'Centromere protein X', 'GO:0000777===GO:0051382', 8926, 'DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Recruited to forks stalled by DNA interstrand cross-links; and required for cellular resistance to such lesions. 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 (By similarity). {ECO:0000250}.', 'MEGNSGFRKELVSRLLHLHFRDCKTKVSGDALQLMAEFLRIFVLEAAVRGVWQAQAEDLDVVEVDQLEKVLPQLLLDF', 78, 'Q8C4X1; A2AC08; O08693; O08694; O08695; Q8BPD7;', 'KD00559', 'Mus musculus (Mouse)', 'Stra13', '#Centromere protein X#CENP-X#FANCM-interacting histone fold protein 2#Fanconi anemia-associated polypeptide of 10 kDa#Immediate-early-response protein D9#Retinoic acid-inducible gene D9 protein#Stimulated by retinoic acid gene 13 protein homolog', '-', '-', '20892'),
(560, 'Q13257', 'Mitotic spindle assembly checkpoint protein MAD2A', 'GO:0000776===GO:0000777===c;k;t', 23510, 'Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore- spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. {ECO:0000269|PubMed:10700282; ECO:0000269|PubMed:11804586; ECO:0000269|PubMed:15024386}.', 'MALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND', 205, 'Q13257; Q53F56; Q548X9; Q6IRW7; Q8IZX3;', 'KD00560', 'Homo sapiens (Human)', 'MAD2L1', '#Mitotic spindle assembly checkpoint protein MAD2A#HsMAD2#Mitotic arrest deficient 2-like protein 1#MAD2-like protein 1', 'BIOMD0000000186,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Dissociation variant;BIOMD0000000187,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Convey variant;BIOMD0000000193,Ibrahim2008_MCC_assembly_model_KDM;BIOMD0000000194,Ibrahim2008_Cdc20_Sequestring_Template_Model;', 'ENSG00000124688', '-'),
(561, 'Q6FLI2', 'DASH complex subunit SPC34', 'GO:0008608===GO:0042729', 35524, '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}.', 'MGESMNSCLEEINGCLDSITSLYFKPPGIFHNAMIRISKDGKETHTLNDKIKNLIKGCDPKEETTLFQLDPVTKSLRRKDGRQALFDYLDKRDLNMKRNRRLGHKDEKPVIHVPNEFYIREHDEELLRDSQRTKRFKAAGHGNDIDSNNTNNTTTALITELFNDDVGLMATMRKKFKENDEIKNLLMALQKGSVILDEKEGISTNNRRRTLFVEDFSTESILKLLDAVLEMFPTEEYKKAAEQYHDVFQELNEESEKLLAEIQLQKDEIEGRLKIESSKDSTTGVQKLIEKERQKIAELESQLRISN', 307, 'Q6FLI2;', 'KD00561', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'SPC34', '#DASH complex subunit SPC34#Outer kinetochore protein SPC34', '-', '-', '2890851'),
(562, 'Q9M077', 'Serine/threonine-protein kinase Aurora-1', 'GO:0032133===GO:0000780', 33972, 'Phosphorylates specifically ''Ser-10'' of histone H3 in vitro and colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. Colocalizes also with gamma-tubulin and function in microtubule organizing centers (MTOCs). In contrast with the mammalian B-type Aurora; AUR1 has no kinase activity toward ''Ser-28'' of histone H3. {ECO:0000269|PubMed:15722465; ECO:0000269|PubMed:16028112; ECO:0000269|PubMed:22150830}.', 'MAIPTETQHQEKEASDASAAAAQKRWTLSDFDIGKPLGRGKFGHVYLAREKRSNHVVALKVLFKSQLQQSQVEHQLRREVEIQSHLRHPNILRLYGYFYDQKRVYLILEYAARGELYKDLQKCKYFSERRAATYVASLARALIYCHGKHVIHRDIKPENLLIGAQGELKIADFGWSVHTFNRRRTMCGTLDYLPPEMVESVEHDASVDIWSLGILCYEFLYGVPPFEAMEHSDTYRRIVQVDLKFPPKPIISASAKDLISQMLVKESSQRLPLHKLLEHPWIVQNADPSGIYRV', 294, 'Q9M077; Q8LBX4;', 'KD00562', 'Arabidopsis thaliana (Mouse-ear cress)', 'AUR1', '#Serine/threonine-protein kinase Aurora-1#AtAur1#2.7.11.1#Aurora-like kinase 1', '-', '-', '829419'),
(563, 'Q9P258', 'Protein RCC2', 'GO:0072356===GO:0051987===k;m', 56085, 'Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1. {ECO:0000269|PubMed:12919680}.', 'MPRKKAAAAAWEEPSSGNGTARAGPRKRGGPAGRKRERPERCSSSSGGGSSGDEDGLELDGAPGGGKRAARPATAGKAGGAAVVITEPEHTKERVKLEGSKCKGQLLIFGATNWDLIGRKEVPKQQAAYRNLGQNLWGPHRYGCLAGVRVRTVVSGSCAAHSLLITTEGKLWSWGRNEKGQLGHGDTKRVEAPRLIEGLSHEVIVSAACGRNHTLALTETGSVFAFGENKMGQLGLGNQTDAVPSPAQIMYNGQPITKMACGAEFSMIMDCKGNLYSFGCPEYGQLGHNSDGKFIARAQRIEYDCELVPRRVAIFIEKTKDGQILPVPNVVVRDVACGANHTLVLDSQKRVFSWGFGGYGRLGHAEQKDEMVPRLVKLFDFPGRGASQIYAGYTCSFAVSEVGGLFFWGATNTSRESTMYPKAVQDLCGWRIRSLACGKSSIIVAADESTISWGPSPTFGELGYGDHKPKSSTAAQEVKTLDGIFSEQVAMGYSHSLVIARDESETEKEKIKKLPEYNPRTL', 522, 'Q9P258; Q8IVL9; Q9BSN6; Q9NPV8;', 'KD00563', 'Homo sapiens (Human)', 'RCC2', '#Protein RCC2#RCC1-like protein TD-60#Telophase disk protein of 60 kDa', '-', 'ENSG00000179051', '-'),
(564, 'Q9C224', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 33483, '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}.', 'MNVLLSPQPPFFPHQHEPSRRSPPRIMSQHTMASRKRKADDDDNEMSISPTGSPAINSRQLSRPSKKVRAGIELAGRPLPLPRLLETLDKSQLRAVLQTICERHPGIGHEVMVSAPRPSVNGALEVLGEYQDKLRAAIPFGNSSSEYTYFRVKQPLMALVDALGDFTPQFLPPVEQQATVSLEYLNHATKIVHDLPDFDSQQYRHHKDGAYDEISRAWALVITEAAKRGGGFHLHNGKWDQVLAKHNQQSGGKLEQAMNAMVNEVGWVGANSNAHGQGSSSDPNSILNQLINGTYGAPVQVGPF', 304, 'Q9C224;', 'KD00564', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '3877218'),
(565, 'Q98T92', 'Mps1/TTK', 'k', 99079, '', 'MDDEDISERKLKIASILDRVKSFKTKYGTDDNWTDELTFSKSSADTTEHSGIFTHLVTTKTPEEWLNCLLKLENTGLPQIDPQLLNKLIDNYSQAVGALPAEKHSHNESYAKILVHFAELKAIHDLDEAREQFQFARLNCKKFAFVHTAFAQFELSEGNFKKCKQILRRGLECGAVPCEMLNLALKNVQFKKPQLISDEDKENLAVSSSHINQGTASFQNLALGNPQRMKIESPEEYSVKTRFSYGEKLSSPEDFEDIGRKPLLNMSAKTCPLGRVPVQPATSPDTRTRKSDGSGSSSVVKRPFSSMRVPVLATLSNPKYLGDDLHCSEDIKVPSSNILPHEEQANEDSLDMKTPSSVILSVTESNLTVKRNEDLILGSTSTAVLNPQENSKPSESAPPLLPNINARLSDTTKPNNIEAEWKWKVPETPRQIFQPEMIFPAGKRKSTEPSANPGSRRVSPPAPSLSKCDPVFVCGTPVNKSQEDYMNCFRTPVVKTNLGPLAQMSTPYNNRSDYQQPQTPVGQPDCFPISAPFASSDCIVVKGRAYAVLKQIGTGGSSKVFQVMDDKKHLYAIKYVNLEEADQQTIESYQNEISHLNKLQQHCDKIIRLFDYEITDQHIYMVMECGNIDLNTWLRKKKTINPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQIQPDVTSIVKDSQVGTINYMPPESIRDTTSYAENGKPRSKISPKGDVWSLGCILYCMTYGKTPFQHITNQIAKLHSILDPGYEIEFPNIPEKDLQDVLRKCLVRNPKERISIAELLVHPYVQIQPHTQPDQQVQKETTEEMKRILGQLIGLNSPNSISRAAKNLYDQFNSGRSLDLSTLGTTVSQNTRTTK', 882, 'Q98T92;', 'KD00565', 'Xenopus laevis (African clawed frog)', 'ttk', '#Mps1/TTK {ECO:0000313|EMBL:AAK27843.1}', '-', '-', '398219'),
(566, 'Q2T9N4', 'Polyamine-modulated factor 1', 'GO:0000444', 23416, '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 (By similarity). {ECO:0000250}.', 'MAEASSVNVGSGCAEKGPEELSQEPARPGTNISRVKLFDTMVDTFLQKLVAAGSFQRFTDCYKRFYQLQPEMTQRIYDKFVTQLQTSIQEEISEIKAEGNLEAVLIALDAIVEESKDRKEQAWRPSGIPEKDLRSAMAPYLLQQRDALQRRVQRQEAENRQLADAVLAGRRQLEELQLQAQARQQAWQALHREQKELLAVLKEPE', 205, 'Q2T9N4;', 'KD00566', 'Bos taurus (Bovine)', 'PMF1', '#Polyamine-modulated factor 1#PMF-1', '-', '-', '616311'),
(567, 'Q5KU00', '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, 'Q5KU00;', 'KD00567', 'Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)', 'sconC', '#E3 ubiquitin ligase complex SCF subunit sconC#Sulfur controller C#Sulfur metabolite repression control protein C', '-', '-', '5989006'),
(568, 'Q12888', 'Tumor suppressor p53-binding protein 1', 'GO:0000777===k;t', 213574, 'Plays a key role in the response to DNA damage. May have a role in checkpoint signaling during mitosis. Enhances TP53- mediated transcriptional activation. {ECO:0000269|PubMed:12364621; ECO:0000269|PubMed:17190600; ECO:0000269|PubMed:21144835}.', 'MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLSPRKGVSQTGTPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH', 1972, 'Q12888; F8VY86; Q2M1Z7; Q4LE46; Q5FWZ3; Q7Z3U4;', 'KD00568', 'Homo sapiens (Human)', 'TP53BP1', '#Tumor suppressor p53-binding protein 1#53BP1#p53-binding protein 1#p53BP1', '-', 'ENSG00000067369', '-'),
(569, 'Q04949', 'Cytoplasmic dynein intermediate light chain DYN3', 'GO:0005868', 36825, 'Component of the cytoplasmic dynein which acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle. {ECO:0000269|PubMed:15642746}.', 'MDNCNAWDKLLSQNESTINSTETATITAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVKRSEILIPKGCDSIGLIKTVDERFEPTEVKEQHFLARYMDFIPTIDKIREDRKTTSGIDLDKLYPLEVFKVNIQEELGKMFAKYRENSRI', 312, 'Q04949; D6W0C6; Q03592;', 'KD00569', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DYN3', '#Cytoplasmic dynein intermediate light chain DYN3#Dynein protein 3', '-', '-', '855345'),
(570, 'Q6S000', 'Kinesin-related protein 12', 'GO:0003777', 168307, 'Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule''s plus end (By similarity). Required for cytokinesis. May be involved in a vesicle-mediated transport of myosin II; the Aurora kinase (aurK) and other proteins along mitotic extracellular microtubules toward the center of the cell and the cleavage furrow in order to ensure cell division coupled to mitosis. {ECO:0000250; ECO:0000269|PubMed:15546981; ECO:0000269|PubMed:18326585}.', 'MKDYISSPLSPSNKKMPDNQKISPTNTPIRKKLFENTQSPIHFISNNNNNNITTPAKGLASVIKFNSSNYGNHHHQHHHQHHNNNNNSTVSGSAIKQHLNKSTFSTSGTTLTSSSDAILLPEDKVPMSVYLRIRPLSKKEIESKESNCFTVLNTTSVSIKSSRSDSDSNKFSFSSVLPPNTTQPQLFKTITHPLIQSFLTGHNVLLLAYGVTNAGKTYTVSGSKRNPGIIPRSLDLIFKSIPNNCLKKTENLTLSNNNNNSTNNNSKDSKDILADSSDDEYTKVDNIDSSDEDDSNAKINSNLLESFSTTNTTATTNAAAAASSTTATSNGDVIQISDQFNYSIWISYYEIYKKNIYDLLDDSPSSKKKQSLKIESDNSVVNIKGLKEILVSSVEDARDIVEQGESNRKVGGTKLNATSSRSHAVLTIKLFTSPRHIPKSDIHPSQIRCSKLCIIDLAGSERASRTETTGETFKEGSSINTSLFTLGKCIEGLKQQALQQQQQQQQHSSKRQSIHHSNPIPWRESDLTRICQEYFCGNGKASMIVNVSPSSCDSEETLNVLRFSASAKEITTLSKIKPMVFLPPPPTTPSISLKKRKSMEQPINNNNNNNNNNNNNAYYNITQLQNSVNEIKKKIHLDNLLAVGQLPISNNNNNNNGKFDYISMEKDQLLDQIQIYQKKLSNYEIKFVESEVTLREEFNNELIKNYIELENQYKERLVKESQLIHDRVQSKLSLIKNVNINQTNKLNCKIEKLELQLEQQQQKTMEANNKALVIVPQTNKRTDDEWIIEITEVQTERDNIQNKLNSILFELDEQRQHNQFSLERIQQFTLQTEQLEIERENLLTEIESMQSKGQELIKLRELEMMQLKESMNSDAQKDRENLEIQHNFETSNLNNQLQMERQEKLQIIEEMRMLKLELQQFKSNQSIEQQRNNNLIKNQYYNHNHPTAATAMTTTTPPIMSTPPIMSTPIKISSVGKFKATPSKSLIKNILGAHSNSPFKNANIESSVGGGFKVQLNIPGSPIQLAPGTPNSIQSQTPDRPILDPNQYSDSGLLMQEIDDDDYLNITGGGSANDGNWTDINVNDDSASEYDDLNSSSKSFTKKPKKTKSFGTIKRIKAVAMIPANIASSALNSSTTNIDEKEKLEKLEKLEKEKERLEKERLEKEKEKERLEKEREKEKERLEKERERLEKEKEKERERLEKEREKEKESKPKVVKKTTSSSSIISKKPSSKTTSSLTNNNNNNNNNNNNNNNNNNNNNNNNNNKSISPIKTVQSPNSPSPTKLQPHSSPNTNAKEYFNLMNPQVIIHFREPETNFVPSVTANTTTSTSTSTSKSSKKTLDSLKDTPKKIANIFSSKSSKEKEASTSSKSSSKISSSTSTTSTAPKLKRFAAITASHSIENGSESSPIEVDTPPRITKKPPVPIVSKVSSKKVSSSSSSTSSSSSSAATIKRVRKIVNEKKNYLEDDDDDVITKMATETPRKTLGLRPRNLISQPIQFR', 1499, 'Q6S000; Q55FA0;', 'KD00570', 'Dictyostelium discoideum (Slime mold)', 'kif12', '#Kinesin-related protein 12#Kinesin family member 12#Kinesin-6', '-', '-', '8616448'),
(571, 'Q6S001', 'Kinesin-related protein 11', 'GO:0003777', 75439, 'Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule''s plus end (By similarity). {ECO:0000250}.', 'MNENISVSVRARPFNEKEVKDKEHCLWQFGNNNTITSLPPPITQPVSSLPPISTPIKSSSSSSTSTSAGSLKTPLKTPLKTPLKTPLKTNSTTTNTTVPASPAPTSSLTSKFVSNSYTYDHLFPPTCDNYEVYDTVARELVKSAMEGYNASIMAYGITSSGKTFTMTGSGKKNPGIIPLSIQDIFTYIQECKEREFLLRVSYLEIYNETVNDLLGVNQENFNLKIHEHPVTGVYVAGLKEEIVLSVEHVLSLISAGEAHRHVGSTSYNLQSSRSHTIFKMIIESKEVLPEGSGSGGLESPVRYSTLNLIDLAGSEKASESTISAIRNKEGSYINKSLLTLGTVISKLSEKDTGYIPYRDSKLTRVLQNSLSGNSRVAIICTITLASNNFEESHNTLKFASRAKKISNNAKVNEILDDKALLKQYRNEIAELKSKLSDALSTEKELQETLTEKEKMKITNQELLHKLVDAEKHRSLLESKINNLNKLILVSTSVNNSASKGGSGSGNGNGSRSTFVSPSQNSHHHHGDLGSITPNSFSNLLLQSPSQNNNNNSHISPLSQSTSSLTIGGGSGNGFESNELIQIQSKMAKLELELEEKNKKIDFLTSFNQDSALEKIKQLEGELVQRDMDLGLYQRESTRLQTLLSHKDEKISSLESKLRDILLKFKQIDSENTSLKSKIQEYEVMY', 685, 'Q6S001; Q54FA2;', 'KD00571', 'Dictyostelium discoideum (Slime mold)', 'kif11', '#Kinesin-related protein 11#Kinesin family member 11#Kinesin-7', '-', '-', '8627935'),
(572, 'Q502J7', 'Dynactin subunit 6', 'GO:0000777', 20929, '', 'MADPSAKQTGQKSVKIAAGAVVCVESDIRGDVTIGARTVVHPKARIIAEAGPIVIGEGNLIEEQALIINSFPENLLPNTDDVEPKPMIIGVNNVFEVGCVCQALKIGDNNVIESKADVGRSVMLTSGCIVGSCCQIHTCEVIPENTVIYGSECLRRVQTERPQPQTLQLDFLMKILPNYHHLKKTVKSSGTPARS', 195, 'Q502J7;', 'KD00572', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'dctn6', '#Dynactin subunit 6', '-', '-', '553678'),
(573, 'Q6S004', 'Kinesin-related protein 6', 'GO:0003777', 118658, 'Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule''s plus end (By similarity). {ECO:0000250}.', 'MDFENDQLYNWLQLANLESFYPNFIKKNVSCDSFLSFTMQDYGNVGITSLQDRKKLFHLLQQLKKQTPPISNTSSPVINSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSSGLRQPTSTSSLLSNNNLMSTQTQQSSSSSSSSSLSSKSNSNSDFMQKAQQLLKQRELERQQYAKQQQQQQSTQTKYQSSLKDFDITSSNKNNNLDDFFEDDNLYSQQQQQQQQQQQQQDFEFEEEEEEEDQQQQYDEEEEEEEEYEEDFYKEDLGEIDDGNVLDISDDEPDPNSSCIIVEGSPDEEDDDVEYIPQNESLVNGFGSMKIQQQQQQQFQPLQQQQQQQQQQQQQFYQQQIQQQQQQQQQQQQQQVQQQQQQFNNFNYSGLNEEQIKYYQQQAQYQQQVQQAQQAAIQQAQQAAALAQASQQQLQQQEQQRQQASNFFLDMNEYGQRIRVCVRKRPLNKKEIAKSEKDIIEVLPKKDLIVNEPKTKLDLSKFIEKHKFTFDGVFDESANNYQVYLHTAYPLVDSIFHKGKATCFAYGQTGSGKTHTQMGQQGDGLYALAARDIFHRLETYFKDQLQVCISFFEIYGGKLFDLLNERKKLACRENELQNVVIVGLSEKHVTSPQELMNCIIDGNKIRSTGSTGVNSDSSRSHAILQISLKNIKTNKLHGKFSFIDLAGSERGSDTYDNDKQTRKEGADINKSLLALKECIRALDQSSKHTPFRQSTLTQVLKDSFVGNSRTVMIANISPNQSSSEHTLNTLRYADRVKELGTSESNSNKKPVATYNIPAPLPPPDHLKQNFNDPILIPSTTTTTTTTATAINSQQPIIQQTSQPVSKIKQPVKQQQESQIPQTPQQQQQQQPPQQQPQQQQYNIPQTPQQTQQQFNIPQTPKQQQPIQTQPPMSPPKIDFVNYHRNHVDQFADILKKELISINQFESSKGSIPLENYINNIEQFLDSKQLLINHLRGIIQQHQQQPIQQQQQQQQPIQQQQQSTPQPSQLQTPQQRERARSQLQPPKPSIYSSRN', 1030, 'Q6S004; Q55F66; Q94499;', 'KD00573', 'Dictyostelium discoideum (Slime mold)', 'kif6', '#Kinesin-related protein 6#Kinesin family member 6#Kinesin-13', '-', '-', '8616484'),
(574, 'Q6AYH5', 'Dynactin subunit 2', 'GO:0000776', 44148, 'Modulates cytoplasmic dynein binding to an organelle; and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development (By similarity). {ECO:0000250}.', 'MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGDYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLADPDGALAKRLLLQLEATKSSKGSSGGKSTGGTPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQGACLMETVELLQAKVNALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQNKVHQLYETIQRWSPVASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMMASSLKDNTALLTQVQTTMRENLATVEGNFASIDARMKKLGK', 402, 'Q6AYH5;', 'KD00574', 'Rattus norvegicus (Rat)', 'Dctn2', '#Dynactin subunit 2', '-', '-', '299850'),
(575, 'Q55GF9', 'Inner centromere protein A', 'GO:0032133', 152366, 'Chromosomal passenger protein that seems to be required for chromosome segregation and the onset of cytokinesis during mitosis. Plays a key role in the abscission of daughter cells at the end of cytokinesis and in the establishment or maintenance of a bipolar spindle. {ECO:0000269|PubMed:16339076}.', 'MDSIKKNTINRINGLPINHNNLSKTSIISMDDDYNSNSSFYSTNNSILNSVTKNSNYLNNNNNNNNNNNNNNNISISNCNNNNTNNKINEQLKTFNNIFEEKGEFLKEEIDNKFNDIISLMNQSKNQLFLSLNDIDSLYDLSPLSTTSTITLENNNNNNNNLIKFKLFNNDSIKKYILPVSSKTIKFKQRQILIEQQEFNEKHNQQKHLLELQRQQVLSDQQNQFQEQHKQQLSLKQQELEAIQQDTNKVKQQLIETHDKLLIEKEKQFKQDLNSLELNLQNKFTNEYQSKEQEFNKKLEQQQQQLEKQFQQTKELLIVQETLTLKSKLTTEFQEQLKTHQDQINKQELLLKQQEYQLFLKQQEISSIQKQHQDDLSSLKSKLSSDQDQIKKQLLQQESDLLKKQQELLLKQQELDIQSKQLKEEQEKQQQQQEKQQEKQQQQQPVVVPVKPTTSTVVSATTATLIKAPIVSTTTVSTATVSKLVTNGIAKPTPLTTMKQTVTAVPTLMDNKTRLKKLVPTATTTTTKEENNKEYDKMMQELDTQPNNSNLKNLNEKKLETLKQQLTFDDSVSFSNGNDESSINLSKYLEETNKSVENTFDIMSNTLKRKNEPIQQPSSSSSQLSSSQQPSSSSSSSSSSIGLKKRLSDDKTTIVTSKPTNKVQPQSLNSNINNNVVPPSPVAAIANKLKKQQELEKLKLEEEERLRKKQEEQLAKREVEKEQERLEKKKKNDEKRKKVEENQQQRILEEEKKKKEAEDRELARKHKEDSDKKKREEEEDAKKRIQERFRETQEQERKREEFKKQQQEQELARIKKEKLQQEKLQQEKEKQEKQKQQQQQQEEEQQKKKTVQTILPTPQTPSRSANNNYDDAANTASATKAKYALSSILSMVFGATKSPHFKPSTSQDDQDDDDCEDYDGTDENSENEAKGEYQDDSDQEIEEQFENDSDESMASTESNGDIYFNKNKNSNNSNNNNDVNQSRKDKSIVFDSDSLNRNHNDSNNSSEEEEPERDPVFLTPLPKILSNMKNNNNNNTYSNSPVIKGLSPPSSVSDYSPSSESNDCFSPLTPTNNNKINNNKINNNNSNNNSFNNSNSYRGLSPAQIIESHTPKCINRSGESKTSPFLTIRNTPSPLKNSPIKFNMSSASSLSSFDSDNDSDYNDNDIDDGEILGNPNENFTTPLKNQENNNNNNSNNSNTQYPIITSPPSNEDGDENYYFEEEEIDYEYDKRVPDWAKNHNLDNSLKQQRFYDPDRIFSMIGPVYLYEIFPKQDLGGKIKDFSKVKRNLSSDWSRDCNTEKEDISYKKNMGFTNPIIVNKK', 1320, 'Q55GF9;', 'KD00575', 'Dictyostelium discoideum (Slime mold)', 'icpA', '#Inner centromere protein A#DdINCENP', '-', '-', '8616029'),
(576, 'Q0CLE0', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 34394, '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}.', 'MNSLVATPPVPPHFYEYSRLASARQMSTPTVTPNSRKRKAEDDTADHDGRMSASPTSSPAFTPRTLPSARNVKRTRPNISGRPLSLPRLLETLDTDALRGMLRSMCERHPSLADEIVHTAPRPSVSSALQVLRQYQSNLQSSFPLGGNPASDYAYNRVRQPLGQLLDALSDFTPHFLPPNETQPSVSLSYLDDATEIIHALPRWSTPQNNIERDSAYDEICKAWILVIREAAKRGGGFQLQYGGWEQKLAKHNQNSGGKLQAAVHELASCLGWMHGPDTQAYGGSGGNNDLGSIREQLLSGTYGLGTPVKVGPW', 314, 'Q0CLE0;', 'KD00576', 'Aspergillus terreus (strain NIH 2624 / FGSC A1156)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '4320973'),
(577, 'Q9BVG8', 'Kinesin-like protein KIFC3', 'GO:0003777', 92775, 'Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance. {ECO:0000250; ECO:0000269|PubMed:19041755}.', 'MVPSRRTWNLGATPSLRGLWRVGRAPEPEPGMARPAPAPASPAARPFPHTGPGRLRTGRGKDTPVCGDEDSSARSAARPALAQCRALSVDWAGPGSPHGLYLTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVRPVTKEDGEGPEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSVELGPGLRRAELGSWSSQEHLEWEPACQTPQPSARAHSAPSSGTSSRPGSIRRKLQPSGKSRPLPV', 833, 'Q9BVG8; A8K6S2; B7Z484; O75299; Q49A29; Q49AQ0; Q59G19; Q8IUT3;Q96HW6;', 'KD00577', 'Homo sapiens (Human)', 'KIFC3', '#Kinesin-like protein KIFC3', '-', 'ENSG00000140859', '-'),
(578, 'P78317', 'E3 ubiquitin-protein ligase RNF4', 'GO:0090234', 21319, '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:12885770; ECO:0000269|PubMed:18408734; ECO:0000269|PubMed:19307308; ECO:0000269|PubMed:20026589; ECO:0000269|PubMed:20212317; ECO:0000269|PubMed:20943951}.', 'MSTRKRRGGAINSRQAQKRTREATSTPEISLEAEPIELVETAGDEIVDLTCESLEPVVVDLTHNDSVVIVDERRRPRRNARRLPQDHADSCVVSSDDEELSRDRDVYVTTHTPRNARDEGATGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI', 190, 'P78317; B2R6D6; D6RF58; Q49AR8;', 'KD00578', 'Homo sapiens (Human)', 'RNF4', '#E3 ubiquitin-protein ligase RNF4#6.3.2.-#RING finger protein 4#Small nuclear ring finger protein#Protein SNURF', '-', 'ENSG00000063978', '-'),
(579, 'Q9H7Z6', 'Histone acetyltransferase KAT8', 'GO:0000776===k', 52403, 'Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at ''Lys-120''. {ECO:0000269|PubMed:12397079; ECO:0000269|PubMed:15923642; ECO:0000269|PubMed:20018852; ECO:0000269|PubMed:21217699; ECO:0000269|PubMed:22020126; ECO:0000269|PubMed:22547026}.', 'MAAQGAAAAVAAGTSGVAGEGEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPKHKQVKLSKK', 458, 'Q9H7Z6; A8K4Z1; G5E9P2; Q659G0; Q7LC17; Q8IY59; Q8WYB4; Q8WZ14;Q9HAC5; Q9NR35;', 'KD00579', 'Homo sapiens (Human)', 'KAT8', '#Histone acetyltransferase KAT8#2.3.1.48 {ECO:0000269|PubMed:10786633; ECO:0000269|PubMed:21217699; ECO:0000269|PubMed:22020126; ECO:0000269|PubMed:22547026}#Lysine acetyltransferase 8#MOZ; YBF2/SAS3; SAS2 and TIP60 protein 1#MYST-1#hMOF', '-', 'ENSG00000120071', '-'),
(580, 'Q9UIL4', 'Kinesin-like protein KIF25', 'GO:0003777', 40686, 'Negative regulator of amino acid starvation-induced autophagy. {ECO:0000269|PubMed:22354037}.', 'MTWTSGQLQREKQARPGSGAVLAFPDDKDLRVYGPAESQSAVFGDVCPLLTSLLDGYNVCVMAYGQTGSGKSYTMLGRHSDDGPVLPLDPQSDLGIIPRVAEELFRLILENTSRSPKVEVSIVEVYNNDIFDLLAKDSIAAVSGVKREVVTAKDGRTEVALLASEAVGSASKLMELVHGGLQLRAKHPTLVHADSSRSHLIITVTLTTASCSDSTADQACSATLPREQTEAGRAGRSRRASQGALAPQLVPGNPAGHAEQVQARLQLVDSAGSECVGVSGVTGLALREMACISRSLAALAGVLGALLEHRGHAPYRNSRLTHLLQDCLGGDAKLLVILCISPSQRHLAQTLQGLGFGIRARQVQRGPARKKPPSSQTEGKRRPD', 384, 'Q9UIL4; O94775; Q5SZU9;', 'KD00580', 'Homo sapiens (Human)', 'KIF25', '#Kinesin-like protein KIF25#Kinesin-like protein 3', '-', 'ENSG00000229921', '-'),
(581, 'Q0CA59', 'E3 ubiquitin ligase complex SCF subunit sconC', 'GO:0051382===GO:0031518', 18372, '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}.', 'MSTSPTLVFTSSDGVDITVDRDVAERSLLIKNMLEDLGETGEAIPIPNVNEAVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKGLLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE', 161, 'Q0CA59;', 'KD00581', 'Aspergillus terreus (strain NIH 2624 / FGSC A1156)', 'sconC', '#E3 ubiquitin ligase complex SCF subunit sconC#Sulfur controller C#Sulfur metabolite repression control protein C', '-', '-', '4353802'),
(582, 'P49793', 'Nuclear pore complex protein Nup98-Nup96', 'GO:0000776', 197283, 'Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC.', 'MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFGFGTSTGTSNSLFGTANTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGNTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGLFSSSTTNSAFSYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTPNTGFSFGNTSTLGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQPNTGFGAVGSTLFGNNKLTTFGTSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNNSGSSIFGSKPAAGTLGTGLGTGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTSTAILGFGAPQAPVALTDPNASAAQQAVLQQHLNSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNHDSEDLASPSEYPENGERFSFLSKPVDENHQQDGDDDSLVSRFYTNPIAKPIPQTPESAGNKNNSSSNVEDTFIALNMRAALRNGLEGSSEETSFHDESLQDDRDEIENSAFQIHPAGIVLTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVIVYVDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHFSKYGLQDSDEEEEEHPPKTTSKKLKTAPLPPAGQATTFQMTLNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVPDSVLEESVPEDQEPVSASTQIASSLGINPHVLQIMKASLLVDEEDVDAMEQRFGHFPSRGDTAQEICSPRLPISASHSSKSRSIVGGLLQSKFASGTFLSPSASVQECRTPRTSSLMNVPSTSPWSVPLPLATVFTVPSPAPEVPLKTVGIRRQPGLVPLEKSITYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLHGSHELENHQVAESMEYGFLPNPVAVKSLSESPFKVHLEKLGLRQRKLDEDLQLYQTPLELKLKHSTVHVDELCPLIVPNPGVSVIHGYADWVKKSPRDLLELPIVKHWSLTWTLCEALWGHLKELDSQLDEPSEYIQTLERRRAFSRWLSHTAAPQIEEEVSLTRRDSPIEAVFSYLTGSRISEACCLAQQSGDHRLALLLSQLVGSQSVRELLTMQLADWHQLQADSFIHDERLRIFALLAGKPVWQLSEQKQINVCSQLDWKRTLAIHLWYLLPPTASISRALSMYEEAFQNTCEGDKYACPPLPSYLEGSGCVVEEEKDPQRPLQDVCFHLLKLYSDRHYGLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSEQCEGVLQASYAGQLESEGLWEWAIFVFLHIDNSGMREKAVRELLTRHCQLSETPESWAKETFLTQKLCVPAEWIHEAKAVRAHMESNKHLEALYLFKAGHWNRCHKLVVRHLASDAIINENYDYLKGFLEDLAPPERSSLIQDWETSGLVYLDYIRVIEMLHRIQQVDCSGYELEHLHTKVTSLCNRIEQIPCYNAKDRLAQSDMAKRVANLLRVVLSLQHTPDATSNSTPDPQRVPLRLLAPHIGRLPMPEDYALEELRGLTQSYLRELTVGSQ', 1816, 'P49793; D3ZMW4;', 'KD00582', 'Rattus norvegicus (Rat)', 'Nup98', '#Nuclear pore complex protein Nup98-Nup96#Nuclear pore complex protein Nup98#98 kDa nucleoporin#Nucleoporin Nup98#Nup98#Nuclear pore complex protein Nup96#96 kDa nucleoporin#Nucleoporin Nup96#Nup96', '-', '-', '81738'),
(583, 'Q9W4X9', 'Centromere/kinetochore protein zw10', 'GO:0000776===GO:0005828===GO:0000940===GO:1990423===k', 82263, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin; Mad2 complexes and spindly/CG15415 onto kinetochores. {ECO:0000269|PubMed:15886105; ECO:0000269|PubMed:17576797}.', 'MEEEAPRFNVLEEAFNGNGNGCANVEATQSAILKVLTRVNRFQMRVRKHIEDNYTEFLPNNTSPDIFLEESGSLNREIHDMLENLGSEGLDALDEANVKMAGNGRQLREILLGLGVSEHVLRIDELFQCVEEAKATKDYLVLLDLVGRLRAFIYGDDSVDGDAQVATPEVRRIFKALECYETIKVKYHVQAYMLQQSLQERFDRLVQLQCKSFPTSRCVTLQVSRDQTQLQDIVQALFQEPYNPARLCEFLLDNCIEPVIMRPVMADYSEEADGGTYVRLSLSYATKEPSSAHVRPNYKQVLENLRLLLHTLAGINCSVSRDQHVFGIIGDHVKDKMLKLLVDECLIPAVPESTEEYQTSTLCEDVAQLEQLLVDSFIINPEQDRALGQFVEKYETYYRNRMYRRVLETAREIIQRDLQDMVLVAPNNHSAEVANDPFLFPRCMISKSAQDFVKLMDRILRQPTDKLGDQEADPIAGVISIMLHTYINEVPKVHRKLLESIPQQAVLFHNNCMFFTHWVAQHANKGIESLAALAKTLQATGQQHFRVQVDYQSSILMGIMQEFEFESTHTLGSGPLKLVRQCLRQLELLKNVWANVLPETVYNATFCELINTFVAELIRRVFTLRDISAQMACELSDLIDVVLQRAPTLFREPNEVVQVLSWLKLQQLKAMLNASLMEITELWGDGVGPLTASYKSDEIKHLIRALFQDTDWRAKAITQIV', 721, 'Q9W4X9;', 'KD00583', 'Drosophila melanogaster (Fruit fly)', 'mit(1)15', '#Centromere/kinetochore protein zw10#Mitotic 15 protein', '-', '-', '47874'),
(584, 'Q99PW8', 'Kinesin-like protein KIF17', 'GO:0003777', 116373, 'Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules.', 'MASESVKVVVRCRPMNKRERELSCQSVVTVDSARGQCFIQNPGAADEPPKQFTFDGAYYIEHFTEQIYNEIAYPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGLPDPPCQRGIIPRAFEHVFESVQCAENTKFLVRASYLEIYNEDVHDLLGADTKQRLELKEHPEKGVYVKGLSMHTVHNVAQCERVMETGWKNRAVGYTLMNKDSSRSHSIFTINIEIYAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHIPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIKNKPRINEDPKDALLREYQEEIKRLKAILAQQMGPGNLSALLSTQTPPGPVQSEEKLLSPTTVQQDTEAEKQLIREEYEERLARLKADYEAEQESRVRLQEDITAMRNSYDVKLSTLQENLRKEKETEAILKAEVLCKTEVMSRAELASGPEYSPPLQYETAVKPTILSMPDMPPSGKVTKSQAPLAFEEPHGETSRSEFSFESNECSTLEDSATSEAFPGPEEFSNMEFSMAAALTESRYLPEEYLGGQEAAASPLEAERYVQENEPSLEPLRILASLQDPFAEVEAKLARLSSTVAMSDSSQTVVPQIPKQPSSADLLEPSDTKSEADVAVADNVVLGTEPDVNLRVAEEVVSEAETGVWMESEAQVAHVAQVSEEAQPQPLLAMVSVRRESVGVEVAVLTEEELQPVDQQQVLARLQLLEQQVVGGEQAKNKDLREKHKRRKRYADERKKQLVAALQNSDEDGGDWVLLNVYDSIQEEVRAKSKLLEKMQRKLRAAEVEIKDLQSEFQLEKIDYLATIRRQERDSMLFQQLLEQVQPLIRRDCNYSNLEKIRRESSWDEDNGFWKIPDPIILKTSLPVVPTGTQNKPARKTSAVDSGEPHMQEEDRYKLMLSRSDSENIASNYFRSKRASQILSTDPMKSLTYHNSPPGLNSSLSNNSALPPTQTPEMPQPRPFRLESLDIPFSKAKRKKSKNSFGGEPL', 1038, 'Q99PW8; A2AM73;', 'KD00584', 'Mus musculus (Mouse)', 'Kif17', '#Kinesin-like protein KIF17#MmKIF17', '-', '-', '16559'),
(585, 'P49792', 'E3 SUMO-protein ligase RanBP2', 'k;s', 358199, 'E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP; karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single- stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at ''Lys-490'' which is essential for the proper assembly of PML-NB. {ECO:0000269|PubMed:11792325; ECO:0000269|PubMed:12032081; ECO:0000269|PubMed:15378033; ECO:0000269|PubMed:15931224; ECO:0000269|PubMed:22194619}.', 'MRRSKADVERYIASVQGSTPSPRQKSMKGFYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEDGWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLQSFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKMGQHSSNVQWRALSELAALCYLIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLNLSRGKQDFLKEIVETFANKSGQSALYDALFSSQSPKDTSFLGSDDIGNIDVREPELEDLTRYDVGAIRAHNGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPHETSRLETNAPESICILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIHRKAVPGNVAKLRLLVQHEINTLRAQEKHGLQPALLVHWAECLQKTGSGLNSFYDQREYIGRSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQASEIVEYEEDAHITFAILDAVNGNIEDAVTAFESIKSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIKIIDDSDSNLSVVKKLPVPLESVKEMLNSVMQELEDYSEGGPLYKNGSLRNADSEIKHSTPSPTRYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHRWPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDDYFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLPTQAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDGYSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQKNSGFRRSDDMFTFHGPGKSVFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSILKAPGTNVAMASNQAVRIVKEPTSHDNKDICKSDAGNLNFEFQVAKKEGSWWHCNSCSLKNASTAKKCVSCQNLNPSNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQNTKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCAACQNPRKQSLPATSIPTPASFKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANATRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQNPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQNPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQCPSKQNQTTAISTPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLKCVACDASKPTHKPIAEAPSAFTLGSEMKLHDSSGSQVGTGFKSNFSEKASKFGNTEQGFKFGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENGTGFQAQDISGQKNGRGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFSSQYGKMANKANTSGDFEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGPTLEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPRESPCGKIAVAVLEETTRERTDVIQGDDVADATSEVEVSSTSETTPKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKSNNSETSSVAQSGSESKVEPKKCELSKNSDIEQSSDSKVKNLFASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTPTAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLDGSEKCRPLEENTADNEKECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSITKSISSPSVSSETMDKPVDLSTRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQKGHVSLAAELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITITECGQI', 3224, 'P49792; Q13074; Q15280; Q53TE2; Q59FH7;', 'KD00585', 'Homo sapiens (Human)', 'RANBP2', '#E3 SUMO-protein ligase RanBP2#6.3.2.-#358 kDa nucleoporin#Nuclear pore complex protein Nup358#Nucleoporin Nup358#Ran-binding protein 2#RanBP2#p270', '-', 'ENSG00000169629', '-'),
(586, 'Q5RFM4', 'Centromere/kinetochore protein zw10 homolog', 'GO:0000777', 88901, '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}.', 'MASFVTEVLAHSGRLEKEDLGARISRLTRRVEEIKGEVCNMISKKYSEFLPSMQSAQGLITQVDKLSEDIDLLKSRIESEVRRDLHVSTGEFTDLKQQLERDSIVLSLLKQLQEFSTAIEEYNCALTEKKYVTGAQRLEEAQKCLKLLKSRKCFDLKILKFLSMELTIQKQNILYHLGEEWQKLIVWKFSPSKDTSSLESYLQTELHLYTEQSHKEEKTPMPPISSVLLAFSVLGELHSKLKSFGQMLLKYILRPLASCPSLHAVIESQPNIVIIRFESIMTNLEYPSPSEVFTKIRLVLEVLQKQLLDLPLDTDLENEKTSTVPLAEMLGDMIWEDLSEYLIKNCLVYSIPTNSSKLQQYEEIIQSTEEFENALKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARNLMTSEIHNTVKIIPDSKINVPELPTPDEDNKLEVQKVSNTQYNEVMNLEPENTLDQHSFSLPTCRISESVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLQKLPQLAAIHHNNCMYIAHHLLTLGHQFRLRLAPILCDGTATFVDLVPGFRRLGTECFLAQMRAQKGELLERLSSARNFSNMDDEENYSAASKAVRQVLHQLKRLGIVWQDVLPVNIYCKAMGTLLNTAISEVIGKITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSEESKNKKYQEEVPVYVPKWMPFKELMMMLQASLQEIGDRWADGKGPLAAAFSSSEVKALIRALFQNTERRAAALAKIK', 779, 'Q5RFM4;', 'KD00586', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'ZW10', '#Centromere/kinetochore protein zw10 homolog', '-', '-', '100171445'),
(587, 'Q9US25', 'Chromodomain helicase hrp1', 'GO:0000780', 158549, 'Seems to play a role in mitotic chromosome segregation and maintenance of chromatin structure. Has ATPase activity.', 'MEPEHSNYDLKNHPTSVQESTLNGSAVTDPQFGNTTNSLPSMNGLLNHENSFASQQSLSSSAFDDSEIVTSTANSTVVSSALSTPKIDDAQNSDDVRVDGTRRSSRAKRPVYRDFSYTEIDEHEIPIPKKRKSKPAPKQKKSVASDDEDAYDKRHRFSINSASGTEIRTSLRSSKGKSVNYNEQEFYDDFEDEEEEVEEQVEEEYEPIIDFVLNHRKRADAQDDDPKSSYQYLIKWQEVSHLHNTWEDYSTLSSVRGYKKVDNYIKQNIIYDREIREDPTTTFEDIEALDIERERKNMLFEEYKIVERIVASETNEEGKTEYFVKWRQLPYDNCTWEDADVIYSMAPNEVYQFLQRENSPYLPYKGVFYNTRPPYRKLEKQPSYIKGGEIRDFQLTGINWMAYLWHRNENGILADEMGLGKTVQTVCFLSYLVHSLKQHGPFLIVVPLSTVPAWQETLANWTPDLNSICYTGNTESRANIREYEFYLSTNSRKLKFNILLTTYEYILKDKQELNNIRWQYLAIDEAHRLKNSESSLYETLSQFRTANRLLITGTPLQNNLKELASLVNFLMPGKFYIRDELNFDQPNAEQERDIRDLQERLQPFILRRLKKDVEKSLPSKSERILRVELSDMQTEWYKNILTKNYRALTGHTDGRGQLSLLNIVVELKKVSNHPYLFPGAAEKWMMGRKMTREDTLRGIIMNSGKMVLLDKLLQRLKHDGHRVLIFSQMVRMLNILGEYMSLRGYNYQRLDGTIPASVRRVSIDHFNAPDSPDFVFLLSTRAGGLGINLNTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVNVYRFLSKDTVEEDILERARRKMILEYAIISLGVTEKSKNSKNDKYDAQELSAILKFGASNMFKATENQKKLENMNLDDILSHAEDRDSSNDVGGASMGGEEFLKQFEVTDYKAEDLNWDDIIPEEEMERIEEEERMLAAQRAKEEERERREEEERENDEDHPSRTYKRTTKSITKRQQRREEMVREKEIRLLYRAMIKFGLVDERFDTIVKEAELQATDPKRIYSLSADMVKACDEAVERLGADDTKNKQPRKAILIEFKGVKNINAETVTLRVKDLTHLHRAYKGLDPLKQIIGYPIRSVHSWNCSWGIKEDSMLLAGINKHGFGCWQAIKNDPDLGLHDKIFLDEAKNDKESRYVPSAVHLVRRGEYLLSVVREHPDLFVVKTDQPTKRKYNRKAPTKSSTRQTTLDGSISNTKKSSRTKKKKEEETNRGDETSPEGTVGEDEVEEEPRQAEPPKRALRSNSGKAASNKRTTRNSMKTHSAMDTLTAVAALDAELDNMSNEKAKEEVDHVKSENGESVNEPNTEDLSLETEENTTVSDISPLVKNEA', 1373, 'Q9US25; Q92369; Q9UU28;', 'KD00587', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hrp1', '#Chromodomain helicase hrp1#3.6.4.-#ATP-dependent helicase hrp1', '-', '-', '2542363'),
(588, 'Q9US26', 'Kinetochore protein fta2', 'GO:0000778===GO:0000941===GO:0051315===k', 40505, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. Fta2; fta3 and fta4 associate with the central core (cnt) and inner repeat (inr) region of the centromere. {ECO:0000269|PubMed:16079914}.', 'MSGRRYSQISQQEGSSSSDDSDSQQKKTKRTVAHRSPNTTLNGMPRVDSRARPNENSGQSKSSNGRVDTDRKMDLLRKRSNLVHQTLLLEKEVRVRRNAINQRDDSFLSGFIKSLLEIDSSVVIYNTENPDNPKTKQVMPSAEPKKHVKLNSSISSIRFTQHEFEAESEKIIHHSLKGDIEYLPSFKFLLEIKVRTIDYALLFITYKIPHFARKELSSFSDSAIQCLDIVALLRAFSLFAHHYSYRCNTWFYLSKHMKKVASANMDAQCFYVQNSFYKITILYEIKFDDLGFVQPNYCISYILKNQNEKIVSITSKLLNQLDKRFSEFVSLFGFREGSLLLLQALFKPHLG', 351, 'Q9US26;', 'KD00588', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'fta2', '#Kinetochore protein fta2#Sim4 complex subunit fta2#Sim4-mal2-associated protein 2', '-', '-', '2542367'),
(589, 'P23258', 'Tubulin gamma-1 chain', 'c;k;m', 51170, 'Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation; centrosome duplication and spindle formation.', 'MPREIITLQLGQCGNQIGFEFWKQLCAEHGISPEGIVEEFATEGTDRKDVFFYQADDEHYIPRAVLLDLEPRVIHSILNSPYAKLYNPENIYLSEHGGGAGNNWASGFSQGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFERTCRQYDKLRKREAFLEQFRKEDMFKDNFDEMDTSREIVQQLIDEYHAATRPDYISWGTQEQ', 451, 'P23258; Q53X79; Q9BW59;', 'KD00589', 'Homo sapiens (Human)', 'TUBG1', '#Tubulin gamma-1 chain#Gamma-1-tubulin#Gamma-tubulin complex component 1#GCP-1', '-', 'ENSG00000131462', '-'),
(590, 'B2GUZ2', 'Spindle and kinetochore-associated protein 3', 'GO:0000940', 46352, '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}.', 'MNPIQSFHCKLRSLATVLDGETARLLRALDGEDSEDFEDSSARILCDLYSEVQTLKDDVNAHLDKARLESRESTHFIKAAKVLMKKNSADIIKLREFFQKYGYQARDKEDSACEHRVSNSSPGLAVCKDTQEPGVKQELSEPRVPRGSAPEEPLRSPQLSDFGLQRYMVSQGPANPRQETVSLKEDRASETTPAKDPSVQVLKTPRCALKMDDFECVTPKLEHFGISEYTMCLNEDYTMGLKNMKSIKSSPLSGVGGEAVETGPVTSDNSFAIPGPMIQQLEKNDVEYINSPLPPKFCTPGLKIPSSMDSTDLVSIDYPLSKPNSSPTDLEDKDCAPLILNSDECYQSFADPHSPTITSYENFTTPSPPKVTAIPEDILQMLKYNSNLASPIDVKAMPLRRGFTSKGQSTRGAANKENW', 419, 'B2GUZ2;', 'KD00590', 'Rattus norvegicus (Rat)', 'Ska3', '#Spindle and kinetochore-associated protein 3', '-', '-', '361047'),
(591, 'A8WFU8', 'Kinesin-like protein KIF22', 'GO:0003777', 70593, '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}.', 'MAQRVAVNDGAAGSKRTSRVRVAVRLRPYMDKQDEKSEGSCVRGLGPQKLEIINWRNATETLQYQFDVFHGEETTQQEVFLTSVKPILPHILNGQNASVFAYGPTGAGKTHTMLGSQEQPGVIPRAVKEVFNLVGAQKKEQDGWEYSIGMSYLEIYNEKVLDLLSPGSQDLPIREDKDRNILIPGLTHTPLSSFADFDTHFIPASLNRTTASTKLNQRSSRSHAILLIKVVKSQRGPPHRQQTGKLYLVDLAGSEDNRRTGNQGIRLKESGAINLSLFTLSKVVDALNTGAGGRVPYRDSKLTRLLQDSLGGSAHSVMITNIAPEYKYYFDTFSALNFAAKSKQIVNRPFVRETVLAPTIAPGKRTREEQEAGGSGEPQNKRSKEGKKAEHSPSPPLHPQSSPDSSVLDRLLALEKMMMGSAERERLNLLKTVAQSRKEIQMLKEKQKELEDKANMFNKQKETTEKESKDALLFKTDLPPLHRKQSTAAKPRKQQAVVTPLQVSQVQPLQQCAVVCKPSQTLVKKKRVQTEVCDGKENIGVDLPPVEDVNWESRLDPALLEQSRKKILQTLNSGSLKELKSLQQIGDKKAKLIMGWREINGDFTQVEDLKKIEGVTVKRFSSFIKANILSSMGK', 634, 'A8WFU8;', 'KD00591', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'kif22', '#Kinesin-like protein KIF22', '-', '-', '561788'),
(592, 'Q0DV28', 'Armadillo repeat-containing kinesin-like protein 1', 'GO:0003777', 104750, '', 'MAANGRASVRPVERHGAPPRPAGRSRSVAPPSRRPSPSPSRARPAAADNDGGSDSCRVRVAVRLRPKNSEDLAHGADFDSCVELQPECKKLKLKKNNWSCESYRFDEVFSENASQKRVYEVVAKPVVESVLEGYNGTVMAYGQTGTGKTYTVGRLGNDDPSEGGIMVRALEHILSVMSLETDSVAISFLQLYLESVQDLLAPEKTNIPIVEDPKTGEVSLPGAAKVEIRDLEHVFQLLQIGEMNRHAANTKMNTESSRSHAILIIHIQRSSRIEDGSNTSLPNGTDNLFPDNLPLVLKSKLLIVDLAGSERIDKSGSEGHMIEEAKFINLSLTSLGKCINALAENSPHIPTRDSKLTRILRDSFGGTARTSLIVTIGPSSRHFSETSSTIMFGQRAMKIVNTIRIKEEVDYESLYKKVEHEVDHLTSEMERQQKLKNSEKMQLEKKLKESEASLNDLKVTSNMQIENMAMEKRQLESTIKRLMLDLEKEKGKNNILSEQIIHLETSLDENKQKQLENISNTNILADTTKSHEKKIRELLKQLEDERSRSASMNDHLNVLQQQLSDAQNYFQKNIACELEKQLSRTTEEFASQISSLEERIADLISEKELVYEELKSTQEKMQQEMRHRQGLEDEILRLKQSLADNCSEESKALCGMVRSGSGLGSVPFMSKSGKSRELLSSQRSNISKIFEEVGLPNVLALLKSDELEVQIHAVKVVANLAAEDVNQEKIVEEGGLDALLSLLETSENTTIHRVTAGAIANLAMNGSNQGLIMNKGGARLLANIASKTNDPQTLRMVAGALANLCGNEKLHVMLKQDGGIKALLGMFRTGHNEVIAQIARGMANFAKCESRVISQGHRKGRSLLIEEGVLNWMVANSSAFSASTRRHIELAFCHLAQNEDNARDIILTGGIKELLRISRESSRDDTRNLAKKALNSNPAFFKEIQ', 945, 'Q0DV28; Q10RM7;', 'KD00592', 'Oryza sativa subsp. japonica (Rice)', 'Os03g0152900', '#Armadillo repeat-containing kinesin-like protein 1', '-', '-', '4331654'),
(593, 'Q9W584', 'FI07204pMeiotic 38; isoform A', 'k', 36997, '', 'MDNASSTFGQSDFDWDAINVGDYQLDHSQNFFARANKENNRSLSNVNPLLLCTTPQKIGREQRDGDFDGKLISAGDLKKESPKDTTEASKDALTIKPKVEPHDVPELKLKTELQELAQVSPLDNGPEPQDDIKQIVPLNWGKDGDDDEKHMTEADQHLVHQERPPGVGAKLRLEWSPPRHREHEGAGASATSAAPKAYQFKDVYESKRQQAMRKRSEEESKARQFHSRPMPNFKAMHKRMNELAVIHKITVPRTPETLKHSQSNVERRRDDDPADQARLHPAGTRSRPFHLRSEQRVRDRREFDAAVQVSLEQKKKEVKTKSSSP', 325, 'Q9W584;', 'KD00593', 'Drosophila melanogaster (Fruit fly)', 'mei-38', '#FI07204p {ECO:0000313|EMBL:ACH92374.1}#Meiotic 38; isoform A {ECO:0000313|EMBL:AAF45636.1}', '-', '-', '31104'),
(594, 'B4PPG0', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25629, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAIIMAESSYERRVKALYEKQIRMEALEGKFIKKVYKFNSNLLDVKEAVLRHQRKVGKLQKVVMERREELEKRVSFMEELAQELEATKLRNLAMKDQIKQRKMLARQRKNEIMERIHTLSKTTGTYVNHEALPARVKGVTVLRGDKRDQLIPFDLNATDAEGLDSLCQHLESLNVDVSQWQQLVSLAMDVAMEARAPITPPKEAANCKSIIEIDLTSPTSHQA', 223, 'B4PPG0; Q64EW4;', 'KD00594', 'Drosophila yakuba (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6536885'),
(595, 'O60216', 'Double-strand-break repair protein rad21 homolog', 'k', 71690, 'Cleavable component of the cohesin complex; involved in chromosome cohesion during cell cycle; in DNA repair; and in apoptosis. 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. Also 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. {ECO:0000269|PubMed:11875078; ECO:0000269|PubMed:12417729}.', 'MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFSLNQSRVEEITMREEVGNISILQENDFGDFGMDDREIMREGSAFEDDDMLVSTTTSNLLLESEQSTSNLNEKINHLEYEDQYKDDNFGEGNDGGILDDKLISNNDGGIFDDPPALSEAGVMLPEQPAHDDMDEDDNVSMGGPDSPDSVDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPREDQQQQHQQRDVIDEPIIEEPSRLQESVMEASRTNIDESAMPPPPPQGVKRKAGQIDPEPVMPPQQVEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEDDEEEEDEDASGGDQDQEERRWNKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEPYSDIIATPGPRFHII', 631, 'O60216; A8K0E0; Q15001; Q99568;', 'KD00595', 'Homo sapiens (Human)', 'RAD21', '#Double-strand-break repair protein rad21 homolog#hHR21#Nuclear matrix protein 1#NXP-1#SCC1 homolog', '-', 'ENSG00000253327', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(596, 'Q9VSW5', 'Kinesin-like protein at 67A; isoform AKinesin-like protein at 67A; isoform CRE52076p', 'k', 92350, '', 'MPSEQHTNIKVAVRVRPYNVRELEQKQRSIIKVMDRSALLFDPDEEDDEFFFQGAKQPYRDITKRMNKKLTMEFDRVFDIDNSNQDLFEECTAPLVDAVLNGYNCSVFVYGATGAGKTFTMLGSEAHPGLTYLTMQDLFDKIQAQSDVRKFDVGVSYLEVYNEHVMNLLTKSGPLKLREDNNGVVVSGLCLTPIYSAEELLRMLMLGNSHRTQHPTDANAESSRSHAIFQVHIRITERKTDTKRTVKLSMIDLAGSERAASTKGIGVRFKEGASINKSLLALGNCINKLADGLKHIPYRDSNLTRILKDSLGGNCRTLMVANVSMSSLTYEDTYNTLKYASRAKKIRTTLKQNVLKSKMPTEFYVKKIDEVVAENERLKERNKALEAKATQLERAGNSGFDPLELKTWYSKIDAVYAAARQLQEHVLGMRSKIKNINYRQTLKKELEEFRKLMCVDQRVCQEDFRRFANYMSTLTSQMEKYKEELPSWLSKMEIAYQDLESLKREVNKSKAYQILIVYVKYKDLELQLTKQNIFNNHVNAINQELVENLDLMRKSFRTACEVLNQTYDRLEDGQKLTPEIEAVFERLLRKMRFADSEANTKMAEMNPLAVPVALRSSAQEEEEPTCSLTASAKKRQRQAAQSDDDLHLSMEDFDSQDTESDSEELHRTFKRPRNLNETQVLGPCSSSSSSSTSSSSSARKALTATVTKPRTVQQRLVSDLISDQNVRGGNEKIKKALLKSNHFTAQGLQRTLAAASLAKENVKYNANYVRKSPRALMAKALAGTSTLARKPLGSASKEPPLVKFNRAASFRLKK', 814, 'Q9VSW5;', 'KD00596', 'Drosophila melanogaster (Fruit fly)', 'Klp67A', '#Kinesin-like protein at 67A; isoform A {ECO:0000313|EMBL:AAF50296.1}#Kinesin-like protein at 67A; isoform C {ECO:0000313|EMBL:AHN58024.1}#RE52076p {ECO:0000313|EMBL:AAL49055.1}', '-', '-', '39068'),
(597, 'Q299P8', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 26565, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MTDLKASEGDLSDYYMRLKKIFSNETRLQSREASISKRSSRVHKNILSAKEAIERQERDFGKLQKVLLNRNQELERRFTLGEALAQQLEVTRQRNADMEAQLLRHTTEGRQRSNELMECMHSLKQATGTYINHEAFPARLNGVSVVRADDGDIKLIPFSLDGNDADGLHTLWRSLHTRTDNASKWRKLISDQEVAGASPVTPSGSERPKATSKHSNFMPTSIIEIDLTSPTNDAS', 235, 'Q299P8;', 'KD00597', 'Drosophila pseudoobscura pseudoobscura (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '4801418'),
(598, 'P79065', 'Tip elongation protein 1', 'k', 52607, 'Has a role in stabilizing and targeting the growing tips of the microtubules along the long axis of the cell; directing them to the ends of the cell. Acts as a cargo for tea2. {ECO:0000269|PubMed:11007487; ECO:0000269|PubMed:15177031}.', 'MFPLGSVVEVITGERGFVRYAGEVENRKGVYVGLELLPEFAEFGKNRGVVDGREYFKTKNNEKTGIFVPFDKCKLASSISSSPSPKIDGTAASIGMGFPPMSPNLQSSIPRLTNVSSSSNLSMNTISSTALTPTEKILQKRIEDLLYERQNHQQQLEEVLATVDQLQSLVTNFNDQQDEVDELRERITLKEERIQQMRNEASQRRFEFKTTIECLEESSNRAIETYENRIAELEAQLEMYMSGKSEDDLLFSLQQERDYALNQVEILQERVDTLMKQKANSSTANEKLSHMESSSPTLTNASFESPKRGKGSNDLPENHPQRRQTLEFYEIEIEVLREKVEKLQALSDEKDFYISKLEKSLDRNDTTPVPSDEKLSNYAAEKENLVSRISELEHTIEQLTINNERDNERMSPAEFELETTQEVEENDSDSHDDEETWCEVCETNNHSLQECPTVFGSTDEA', 461, 'P79065;', 'KD00598', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'tip1', '#Tip elongation protein 1#Protein noc1', '-', '-', '2543044'),
(599, 'Q09591', 'Mitotic chromosome and X-chromosome-associated protein mix-1', 'k', 140342, 'Essential protein required for both chromosome condensation and X-chromosome dosage compensation depending on its binding partners. Member of a dosage compensation complex that associates specifically with hermaphrodite X chromosomes to reduce their gene expression during interphase.', 'MHIKSIHLDGFKSYQKHTDILDFSPTFNAITGYNGSGKSNILDSICFIMGINKLDNIRAKSMHELISHGGTKAIVQVRFDNTDKRCSPFGMEHLDEIVVQRIITAQATGKGCATSYTLNGHAATNGKMQDFFRGVGLNVNNPHFLIMQGRITTVLNMKPEEILGMVEEAAGTKMYDQKKKDAEKTMFLKDAKLKEVDRIFQSSIDPRMVKFREDRKNMVEVTRLKKLKENFSRKYEAFQYFQTCEAVKKSAKEIEDAKKGIEDLGEKFNQLDLDLKNKEDEKKKMEESRDDQHEEAALSAAHLSKQSIMLQKETVKNQLVETINKLKKEGEQINKSLSKDREVLDAKRKEHEDSKAANSKDIQSQSDDEALVTKYRNDLESLTRGTIANDKGEHVSIESEIQSCKSTASQMSSGITAAKKRGERLHNQIKHLEGEKATLSARSKSDIGSADNYQKEVDEINKQLQLLGFNIDADTEKREHAAKLHESITKLKDMDTRLLNSYKDGRYALNYQRPPLHIDKFDEKRDVFGYVAHLIKMKPGCEQFAVAADIALGGVLGNVVVSTQDIARILIDGKAFTSRKTMIPVSENARNASSYNTLPDVKLRRAKEIAEKYNDTVTKMIDLIEYPDFISNTILNAVGQILVVDSLDVAREIAYDEVAKTRMITRRGDDVRTNGIMTGGYNDPGNKPALIALEPMYARRPQIEAQQRELDALNRELQLTEASSQKCRDLNNQLATAMRKLAQVKTNINNSEFGIVVRDLKVHSEEYEKNQAEIEATVKTLKDVEDKIKTLESMKNKDKNSQEKRKKELTALLQKAEQTVAQNKNRGEKARREVMLLQATVEEMEKTIKKDEGIWEQKKKECDELEEKLPNAIAALKDAELEQKAAQAKLNDLKNNQRQISTRLGKIAKECDALIREKAKTKSKREEKEKELTSLQQSEASNRKEARSKLKKFEWLSDEEAHFNKKGGLYDFEGYTVSKGKDEIKELTDKIETLERSCCIQNVSNLDTCEAKVLDIKNKRERITEDFNMLKKTIATLDKKKVDELIRAHESVNKDFGQIFNCLLPDAHASLVPPEGKTVCEGLEVKVSFGGVVKDSLHELSGGQRSLVALSLILAMLKFKPAPLYILDEVDAALDLSHTANIGMMIKTHFHHNQFIIVSLKQGMFSNADVLFQTRFADGHSTCTRLNGGDIAVLCQDKVLQAQALELTDAGKAKKDAAAKKGAQKNDKEPPKKKPIVVDDDDFE', 1244, 'Q09591;', 'KD00599', 'Caenorhabditis elegans', 'mix-1', '#Mitotic chromosome and X-chromosome-associated protein mix-1#Lethal protein 29#Structural maintenance of chromosomes protein 2', '-', '-', '174669'),
(600, 'Q1LZG6', 'G2/mitotic-specific cyclin-B1', 'GO:0000942===GO:0051987', 47658, 'Essential for the control of the cell cycle at the G2/M (mitosis) transition. {ECO:0000250}.', 'MALRITRNTKISAENKAKISMAGAKRVPVAAVATSKPGLRPRTALGDIGNKVSEQPQAKLPLKKEAKTLASGKVTAKKVPKPLEKAPVPVPEPQPEPEPEPEHVKEDKLSPEPILVDTPSPSPMETSGCAPAEEYLCQAFSDVILAVSDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVKPKYLMGREVTGNMRAILIDWLVQVQIKFRLLQETMYMTVSIIDRFMQDTYVPKKMLQLVGVTAMFVASKYEEMYPPEIGDFAFVTDNTYTKFQIRQMEMKILRALNFSLGRPLPLHFLRRASKIGEVDVELHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKVLDNGEWTPTLQHYLSYTEESLLVVMQHLAKNVVMVNRGLTKHMTIKNKYATSKHAKISTLAQLNSALVQDLAKAVAKV', 427, 'Q1LZG6;', 'KD00600', 'Bos taurus (Bovine)', 'CCNB1', '#G2/mitotic-specific cyclin-B1', '-', '-', '327679'),
(601, 'Q9JHD1', 'Histone acetyltransferase KAT2B', 'GO:0000776', 91769, 'Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4); and also with nucleosome core particles. Also acetylates non-histone proteins; such as ACLY. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK- ARNTL/BMAL1 heterodimers (By similarity). {ECO:0000250}.', 'MAEAGGAGSPALPPAPPHGSPRTLATAAGSSASCGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRGDLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMDRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPSKERQTTIELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTKVFGRTLLRSVFTIMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSPLGIQTVISPPVTGTALFSSNSTSHEQINGGRTSPGCRGSSGLEANPGEKRKMNNSHAPEEAKRSRVMGDIPVELINEVMSTITDPAGMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHEILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPQIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPKDPEQLYSTLKNILQQVKNHPNAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLRNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCASILEKFFFSKIKEAGLIDK', 813, 'Q9JHD1; Q3U142; Q640M9;', 'KD00601', 'Mus musculus (Mouse)', 'Kat2b', '#Histone acetyltransferase KAT2B#2.3.1.48#Histone acetyltransferase PCAF#Histone acetylase PCAF#Lysine acetyltransferase 2B#P300/CBP-associated factor#P/CAF', '-', '-', '18519'),
(602, 'Q9P225', 'Dynein heavy chain 2; axonemal', 'GO:0003777', 507698, '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}.', 'MSSKAEKKQRLSGRGSSQASWSGRATRAAVATQEQGNAPAVSEPELQAELPKEEPEPRLEGPQAQSEESVEPEADVKPLFLSRAALTGLADAVWTQEHDAILEHFAQDPTESILTIFIDPCFGLKLELGMPVQTQNQLVYFIRQAPVPITWENFEATVQFGTVRGPYIPALLRLLGGVFAPQIFANTGWPESIRNHFASHLHKFLACLTDTRYKLEGHTVLYIPAEAMNMKPEMVIKDKELVQRLETSMIHWTRQIKEMLSAQETVETGENLGPLEEIEFWRNRCMDLSGISKQLVKKGVKHVESILHLAKSSYLAPFMKLAQQIQDGSRQAQSNLTFLSILKEPYQELAFMKPKDISSKLPKLISLIRIIWVNSPHYNTRERLTSLFRKVCDCQYHFARWEDGKQGPLPCFFGAQGPQITRNLLEIEDIFHKNLHTLRAVRGGILDVKNTCWHEDYNKFRAGIKDLEVMTQNLITSAFELVRDVPHGVLLLDTFHRLASREAIKRTYDKKAVDLYMLFNSELALVNRERNKKWPDLEPYVAQYSGKARWVHILRRRIDRVMTCLAGAHFLPRIGTGKESVHTYQQMVQAIDELVRKTFQEWTSSLDKDCIRRLDTPLLRISQEKAGMLDVNFDKSLLILFAEIDYWERLLFETPHYVVNVAERAEDLRILRENLLLVARDYNRIIAMLSPDEQALFKERIRLLDKKIHPGLKKLHWALKGASAFFITECRIHASKVQMIVNEFKASTLTIGWRAQEMSEKLLVRISGKRVYRDLEFEEDQREHRAAVQQKLMNLHQDVVTIMTNSYEVFKNDGPEIQQQWMLYMIRLDRMMEDALRLNVKWSLLELSKAINGDGKTSPNPLFQVLVILKNDLQGSVAQVEFSPTLQTLAGVVNDIGNHLFSTISVFCHLPDILTKRKLHREPIQTVVEQDEDIKKIQTQISSGMTNNASLLQNYLKTWDMYREIWEINKDSFIHRYQRLNPPVSSFVADIARYTEVANNVQKEETVTNIQFVLLDCSHLKFSLVQHCNEWQNKFATLLREMAAGRLLELHTYLKENAEKISRPPQTLEELGVSLQLVDALKHDLANVETQIPPIHEQFAILEKYEVPVEDSVLEMLDSLNGEWVVFQQTLLDSKQMLKKHKEKFKTGLIHSADDFKKKAHTLLEDFEFKGHFTSNVGYMSALDQITQVRAMLMAMREEENSLRANLGIFKIEQPPSKDLQNLEKELDALQQIWEIARDWEENWNEWKTGRFLILQTETMETTAHGLFRRLTKLAKEYKDRNWEIIETTRSKIEQFKRTMPLISDLRNPALRERHWDQVRDEIQREFDQESESFTLEQIVELGMDQHVEKIGEISASATKELAIEVALQNIAKTWDVTQLDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMILTVQRQWMYLENIFLGEDIRKQLPNESTLFDQVNSNWKAIMDRMNKDNNALRSTHHPGLLDTLIEMNTILEDIQKSLDMYLETKRHIFPRFYFLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLRIQKVGGPSSKWEAVGMFSGDGEYIDFLHSVFLEGPVESWLGDVEQTMRVTLRDLLRNCHLALRKFLNKRDKWVKEWAGQVVITASQIQWTADVTKCLLTAKERADKKILKVMKKNQVSILNKYSEAIRGNLTKIMRLKIVALVTIEIHARDVLEKLYKSGLMDVNSFDWLSQLRFYWEKDLDDCVIRQTNTQFQYNYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSGLAQTGAWGCFDEFNRINIEVLSVVAHQILCILSALAAGLTHFHFDGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFRPIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLLLSMRDMNIAKLTSVDAPLFNAIVQDLFPNIELPVIDYGKLRETVEQEIRDMGLQSTPFTLTKVFQLYETKNSRHSTMIVGCTGSGKTASWRILQASLSSLCRAGDPNFNIVREFPLNPKALSLGELYGEYDLSTNEWTDGILSSVMRTACADEKPDEKWILFDGPVDTLWIENMNSVMDDNKVLTLINGERIAMPEQVSLLFEVEDLAMASPATVSRCGMVYTDYADLGWKPYVQSWLEKRPKAEVEPLQRMFEKLINKMLAFKKDNCKELVPLPEYSGITSLCKLYSALATPENGVNPADGENYVTMVEMTFVFSMIWSVCASVDEEGRKRIDSYLREIEGSFPNKDTVYEYFVDPKIRSWTSFEDKLPKSWRYPPNAPFYKIMVPTVDTVRYNYLVSSLVANQNPILLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRTKQTIKYIREMFLMAAMGPPGGGRTVISPRLRSRFNIINMTFPTKSQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATLDMYNTVVQRFLPTPTKMHYLFNLRDISKVFQGMLRANKDFHDTKSSITRLWIHECFRVFSDRLVDAADTEAFMGIISDKLGSFFDLTFHHLCPSKRPPIFGDFLKEPKVYEDLTDLTVLKTVMETALNEYNLSPSVVPMQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYTTFQIEVTKHYRKQEFRDDIKRLYRQAGVELKTTSFIFVDTQIADESFLEDINNILSSGEVPNLYKPDEFEEIQSHIIDQARVEQVPESSDSLFAYLIERVQNNLHIVLCLSPMGDPFRNWIRQYPALVNCTTINWFSEWPQEALLEVAEKCLIGVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLELRRHNYVTPTKYLELLSGYKKLLGEKRQELLAQANKLRTGLFKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIAVEEIKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLLAAAFLSYMGPFLTNYRDEIVNQIWIGKIWELQVPCSPSFAIDNFLCNPTKVRDWNIQGLPSDAFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGGQGLKIIDLQMSDYLRILEHAIHFGYPVLLQNVQEYLDPTLNPMLNKSVARIGGRLLMRIGDKEVEYNTNFRFYITTKLSNPHYSPETSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLHTSKITATEVTEQLETSETTEINTDLAREAYRPCAQRASILFFVLNDMGCIDPMYQFSLDAYISLFILSIDKSHRSNKLEDRIDYLNDYHTYAVYRYTCRTLFERHKLLFSFHMCAKILETSGKLNMDEYNFFLRGGVVLDREGQMDNPCSSWLADAYWDNITELDKLTNFHGLMNSFEQYPRDWHLWYTNAAPEKAMLPGEWENACNEMQRMLIVRSLRQDRVAFCVTSFIITNLGSRFIEPPVLNMKSVLEDSTPRSPLVFILSPGVDPTSALLQLAEHMGMAQRFHALSLGQGQAPIAARLLREGVTQGHWVFLANCHLSLSWMPNLDKLVEQLQVEDPHPSFRLWLSSIPHPDFPISILQVSIKMTTEPPKGLKANMTRLYQLMSEPQFSRCSKPAKYKKLLFSLCFFHSVLLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEYEETPWDALKYLIAGINYGGHVTDDWDRRLLTTYINDYFCDQSLSTPFHRLSALETYFIPKDGSLASYKEYISLLPGMDPPEAFGQHPNADVASQITEAQTLFDTLLSLQPQITPTRAGGQTREEKVLELAADVKQKIPEMIDYEGTQKLLALDPSPLNVVLLQEIQRYNTLMQTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKAYPSQKPLAAWTRDLAMRVEQFELWASRARPPVIFWLSGFTFPTGFLTAVLQSSARQNNVSVDSLSWEFIVSTVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVCLMPTIHFRPAESRKKSAKGMYSCPCYYYPNRAGSSDRASFVIGIDLRSGAMTPDHWIKRGTALLMSLDS', 4427, 'Q9P225; A8K992; B5MDX5; O15434; Q6PIH3; Q6ZR42;', 'KD00602', 'Homo sapiens (Human)', 'DNAH2', '#Dynein heavy chain 2; axonemal#Axonemal beta dynein heavy chain 2#Ciliary dynein heavy chain 2#Dynein heavy chain domain-containing protein 3', '-', 'ENSG00000183914', '-'),
(603, 'Q5R9K7', 'Kinesin heavy chain isoform 5A', 'GO:0003777', 117357, 'Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH; NFM and NFL). {ECO:0000250}.', 'MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSGPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQQELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVERHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNSLFQNYQNLYLQATPSSTSDMYFANSCTGSGATSSGGPLASYQKANMDNGNATDIKDNRSDLPCGYEAEDQAKLFPLHQETAAS', 1032, 'Q5R9K7;', 'KD00603', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'KIF5A', '#Kinesin heavy chain isoform 5A', '-', '-', '100172845'),
(604, 'Q92793', 'CREB-binding protein', 'GO:0000940', 265351, '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:0000269|PubMed:11154691; ECO:0000269|PubMed:12738767; ECO:0000269|PubMed:12929931; ECO:0000269|PubMed:14645221; ECO:0000269|PubMed:9707565}.', 'MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGKSPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLAETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASKQSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEMMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAGFPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNSMPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVISMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHLGNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL', 2442, 'Q92793; D3DUC9; O00147; Q16376; Q4LE28;', 'KD00604', 'Homo sapiens (Human)', 'CREBBP', '#CREB-binding protein#2.3.1.48 {ECO:0000269|PubMed:24616510}', 'BIOMD0000000395,Sivakumar2011 - Hedgehog Signaling Pathway;', 'ENSG00000080603', '-'),
(605, 'Q6CW48', 'DASH complex subunit DAD1', 'GO:0042729', 10779, '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}.', 'MTEEVQQLSTGDKYFIEQRSLILQEINESMDAILNQLNGLNITLENSIAVGKEFENVSQIWKLFYNGLESEEQNMETVGVADSEHITEDVNPEGK', 95, 'Q6CW48;', 'KD00605', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'DAD1', '#DASH complex subunit DAD1#Outer kinetochore protein DAD1', '-', '-', '2896954'),
(606, 'Q99661', 'Kinesin-like protein KIF2C', 'GO:0000777===GO:0003777===k;m', 81313, '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:0000269|PubMed:19060894; ECO:0000269|PubMed:21820309}.', 'MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATKGKEIDFDDVAAINPELLQLLPLHPKDNLPLQENVTIQKQKRRSVNSKIPAPKESLRSRSTRMSTVSELRITAQENDMEVELPAAANSRKQFSVPPAPTRPSCPAVAEIPLRMVSEEMEEQVHSIRGSSSANPVNSVRRKSCLVKEVEKMKNKREEKKAQNSEMRMKRAQEYDSSFPNWEFARMIKEFRATLECHPLTMTDPIEEHRICVCVRKRPLNKQELAKKEIDVISIPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKAQNASKGIYAMASRDVFLLKNQPCYRKLGLEVYVTFFEIYNGKLFDLLNKKAKLRVLEDGKQQVQVVGLQEHLVNSADDVIKMIDMGSACRTSGQTFANSNSSRSHACFQIILRAKGRMHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIATISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQLIQMETEEMEACSNGALIPGNLSKEEEELSSQMSSFNEAMTQIRELEEKAMEELKEIIQQGPDWLELSEMTEQPDYDLETFVNKAESALAQQAKHFSALRDVIKALRLAMQLEEQASRQISSKKRPQ', 725, 'Q99661; B3ITR9; Q5JR88; Q6ICU1; Q96C18; Q96HB8; Q9BWV8;', 'KD00606', 'Homo sapiens (Human)', 'KIF2C', '#Kinesin-like protein KIF2C#Kinesin-like protein 6#Mitotic centromere-associated kinesin#MCAK', '-', 'ENSG00000142945', '-'),
(607, 'Q8K327', 'Chromosome alignment-maintaining phosphoprotein 1', 'GO:0000777===GO:0034501===GO:0051315===GO:0031134', 87561, 'Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore (By similarity). {ECO:0000250}.', 'MEVCQELRKPALSLECGHCSFRGTDYENVQLHMGSIHPEFCDDMDAGGLGKLIFYQKSAKLFHCHKCFFTSKLYANVYYHITARHAASDKWSEQPKEQPSKDTESGKSPSPPERQNPAFDPAEARPTPALPMEAQKTSPSLCPESQASGPPVLEPQGAGPLISPEPQAPCLPAEASKAAPVPCPERVDPPCELPELEKPERGPSPESVKSALVSSKPPKHSSFADTGAAPSALSPESPVLATSPEPWGPSLSASPESRKPARTASPEPRKPSPAESPELWKPFPAIASEPRRPTPAVSPGSWKPGPPGSPRPWKSSPSATSGPWKSSKPVQPMSPGPWKPIPSVSPGPWKPAPSMSTASWKSSVSSGSWKTPPTSPESWKSGPPELRKTALPLSPEHWKAVPPVSPELRRPGPPLSPEIRSPAGSPELKKPSSSPDLWKVSPDQRKTSPASLDFPEPQKSSCGSPPDLWKSSFIMESQKPNVFSETRKHTASGSSESPKVASDIWKPVLSIDAEPRKSTLFPEPTKAVLPASPEPRKRALFPESRKHVFLPELPKSAVFSDAQKAPELSEEIQLEAVDNAKCDSLAQEGLLATPKKLLDEALSPSSKKLKKDSQENSDAELSSSEYIRADLDTLDTKGQESSSDQEQVDVESIDFSKENKMEMGSTEQAKNVLQFTEEKEAFISEEEIAKYMKRGKGKYYCKICCCRAMKKGAVLHHLVNKHNVHSPYKCTICGKAFLLESLLKNHVAAHGQSLLKCPRCNFESNFPRGFKKHLTHCQSRHNEEVNKKLMEALESPLEEQQI', 802, 'Q8K327; Q3UZ85; Q6ZPI1;', 'KD00607', 'Mus musculus (Mouse)', 'Champ1', '#Chromosome alignment-maintaining phosphoprotein 1#Zinc finger protein 828', '-', '-', '101994'),
(608, 'Q66HC9', 'Dynein intermediate chain 2; axonemal', 'GO:0003777', 70318, 'Part of the dynein complex of respiratory cilia. {ECO:0000250}.', 'MEIVYVYVKKRSEFGKQCNFSDRQAELNIDISPNPELAALYVERNPVDTGIQCSASMSEHEANTERFEMENCGVNHVEGGWPKDVNPQELEQTIRFRKKVEKDENYINAVMQLGSIMEHCIKQNNAIDIYEEYFDDEEAVEVTEEAPSAKTINVFRDPQEIKRTATHLSWHPDGNKKLAVAYSCLQFQRSPMGMSHDSYIWDLENPNRPEIALKPSSPLITLEYNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIEFSHRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKISEPTEVVIMDITRKEQLENALGAISLEFESTLPTKFMVGTEQGIVISCNRKAKTPAEKIVCTFSGHHGPIYALQRNPFYPKNFLTVGDWAARIWSEESRESSIMWTRYHMAYLSDGAWSPVRPAVFFTTKMDGTLDIWDLVFKQCDPALSLKVCDDPLFCLRVQDTGCLIACGSELGTTTLLEVSSSLSTLQRNERNIASSIFERETRREKILEARHREMRLKEKGKAEGRDDDQKEEETALDLDELVNKAEEEFFEVIFAELKRKEAEALKKKPKPKKASIEVEGEDELEDIAGEEEESGIIMGEDTGEDDMDEKNEGGAP', 619, 'Q66HC9;', 'KD00608', 'Rattus norvegicus (Rat)', 'Dnai2', '#Dynein intermediate chain 2; axonemal#Axonemal dynein intermediate chain 2', '-', '-', '360654'),
(609, 'Q6CSY9', 'DASH complex subunit DAD4', 'GO:0008608===GO:0042729', 8452, '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}.', 'MENPYEKVQSNILARIIGNVERLNQSVVILNQELRRVNTKNKNLELMSQMCENYRESVDFQLQATSKKQDPL', 72, 'Q6CSY9;', 'KD00609', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'DAD4', '#DASH complex subunit DAD4#Outer kinetochore protein DAD4', '-', '-', '2892496'),
(610, 'Q9US03', 'Kinesin-like protein 2', 'GO:0000777===k', 91043, 'Microtubule-dependent motor that is involved in microtubule organization in the mitotic spindle. Required for the polarization of interphase microtubules where it orients the microtubule plus ends toward the cell ends and the minus ends toward the cell center. Mediates minus end-directed sliding of cytoplasmic microtubules relative to each other; thereby promoting mitotic spindle disassembly. {ECO:0000269|PubMed:11694582; ECO:0000269|PubMed:16002618}.', 'MEEEGHKSLTSHLPQSSSSLSQSREIAKEFTSNIPPPTIKTNSSSSNILKPRLSLQNEVNQLKPAKFPSKMLPPGSLASVKSSSLAKKARPFTASSNPRMPKSAHPISSRSVSASSHFGRPASAVSSSLNSSDDVRSMSDESMESYNDEKSVNASALRTTEDRLRSMEMAYAQLSAKVIPSPSKRPANYKFYEQRIAMLEESLEVERSRTSELQEQFSVALREKAEAEANKIVSQKGMESLEIMLNSMKSENHQRMAMLEENHARVMETAELQHQAELQDFASNIEQKANSLIMEYKNELQSAEEHFSHKIKELTSENELKISRLQEEKDSLLKKVQEGASLAMQRVQNKHDLEKKRLQSAIQPLQEENNSLKQQIEQLQRELASETVVKENLKSSLDQQSANVQKLESTNRALESTIKTLEEDVYTMKNKIIELEGILKSANVERDGLVEKLIAEETLRRKLHNTIQELKGNIRVFCRVRPPLGDGESAQIAFPDQNSEASTIEIVAQAPGSSLTGNGIKQYAFNFDRVFSPETTNEDVFNELSQLIQSAMDGYNVCIFAYGQTGSGKTHTMSSNTGMIPSSVRMIYNRSTSLKERGWEYRMEGQFLEIYNETIIDLLASGNEEEKGKKKLEIYHDTKAGRTTITNITSEPLDTPEQVTWLLDQASKNRSVAATNANEHSSRSHSVFMLHLNGSNSTTGETCRSTLNLIDLAGSERLSSSQSVGERLKETQAINKSLSCLGDVIHALGSGKEGTYIPYRNSKLTNLLQYSLGGNSKTLMFVNISPLKQHVPETLCSLRFATKVNNTQIGTARKVTK', 817, 'Q9US03;', 'KD00610', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'klp2', '#Kinesin-like protein 2', '-', '-', '2543360'),
(611, 'O95235', 'Kinesin-like protein KIF20A', 'GO:0003777', 100278, 'Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1; involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:12939256}.', 'MSQGILSPPAGLLSDDDVVVSPMFESTAADLGSVVRKNLLSDCSVVSTSLEDKQQVPSEDSMEKVKVYLRVRPLLPSELERQEDQGCVRIENVETLVLQAPKDSFALKSNERGIGQATHRFTFSQIFGPEVGQASFFNLTVKEMVKDVLKGQNWLIYTYGVTNSGKTHTIQGTIKDGGILPRSLALIFNSLQGQLHPTPDLKPLLSNEVIWLDSKQIRQEEMKKLSLLNGGLQEEELSTSLKRSVYIESRIGTSTSFDSGIAGLSSISQCTSSSQLDETSHRWAQPDTAPLPVPANIRFSIWISFFEIYNELLYDLLEPPSQQRKRQTLRLCEDQNGNPYVKDLNWIHVQDAEEAWKLLKVGRKNQSFASTHLNQNSSRSHSIFSIRILHLQGEGDIVPKISELSLCDLAGSERCKDQKSGERLKEAGNINTSLHTLGRCIAALRQNQQNRSKQNLVPFRDSKLTRVFQGFFTGRGRSCMIVNVNPCASTYDETLHVAKFSAIASQLVHAPPMQLGFPSLHSFIKEHSLQVSPSLEKGAKADTGLDDDIENEADISMYGKEELLQVVEAMKTLLLKERQEKLQLEMHLRDEICNEMVEQMQQREQWCSEHLDTQKELLEEMYEEKLNILKESLTSFYQEEIQERDEKIEELEALLQEARQQSVAHQQSGSELALRRSQRLAASASTQQLQEVKAKLQQCKAELNSTTEELHKYQKMLEPPPSAKPFTIDVDKKLEEGQKNIRLLRTELQKLGESLQSAERACCHSTGAGKLRQALTTCDDILIKQDQTLAELQNNMVLVKLDLRKKAACIAEQYHTVLKLQGQVSAKKRLGTNQENQQPNQQPPGKKPFLRNLLPRTPTCQSSTDCSPYARILRSRRSPLLKSGPFGKKY', 890, 'O95235; B4DL79; D3DQB6;', 'KD00611', 'Homo sapiens (Human)', 'KIF20A', '#Kinesin-like protein KIF20A#GG10_2#Mitotic kinesin-like protein 2#MKlp2#Rab6-interacting kinesin-like protein#Rabkinesin-6', '-', 'ENSG00000112984', '-'),
(612, 'O59702', 'Histone deacetylase clr6', 'k', 46112, 'Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A; H2B; H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation; cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Has a role in chromatin assembly and chromosome segregation. {ECO:0000269|PubMed:12773392}.', 'MGFGKKKVSYFYDEDVGNYHYGPQHPMKPHRVRMVHNLVVNYNLYEKLNVITPVRATRNDMTRCHTDEYIEFLWRVTPDTMEKFQPHQLKFNVGDDCPVFDGLYEFCSISAGGSIGAAQELNSGNAEIAINWAGGLHHAKKREASGFCYVNDIALAALELLKYHQRVLYIDIDVHHGDGVEEFFYTTDRVMTCSFHKFGEYFPGTGHIKDTGIGTGKNYAVNVPLRDGIDDESYESVFKPVISHIMQWFRPEAVILQCGTDSLAGDRLGCFNLSMKGHSMCVDFVKSFNLPMICVGGGGYTVRNVARVWTYETGLLAGEELDENLPYNDYLQYYGPDYKLNVLSNNMENHNTRQYLDSITSEIIENLRNLSFAPSVQMHKTPGDFTFENAEKQNIAKEEIMDERV', 405, 'O59702;', 'KD00612', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'clr6', '#Histone deacetylase clr6#3.5.1.98#Cryptic loci regulator 6', '-', '-', '2540368'),
(613, 'O95239', 'Chromosome-associated kinesin KIF4A', 'GO:0003777', 139881, 'Motor protein that translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition; an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. May play a role in mitotic chromosomal positioning and bipolar spindle stabilization. {ECO:0000269|PubMed:15297875; ECO:0000269|PubMed:15625105}.', 'MKEEVKGIPVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGAYTAEQENEPTVGVIPRVIQLLFKEIDKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVNIDPQTAELNHLKQQVQQLQVLLLQAHGGTLPGSITVEPSENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQELKENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQKHLPKDTLLSPDSSFEYVPPKPKPSRVKEKFLEQSMDIEDLKYCSEHSVNEHEDGDGDDDEGDDEEWKPTKLVKVSRKNIQGCSCKGWCGNKQCGCRKQKSDCGVDCCCDPTKCRNRQQGKDSLGTVERTQDSEGSFKLEDPTEVTPGLSFFNPVCATPNSKILKEMCDVEQVLSKKTPPAPSPFDLPELKHVATEYQENKAPGKKKKRALASNTSFFSGCSPIEEEAH', 1232, 'O95239; B2R7V5; D3DVU4; Q86TN3; Q86XX7; Q9NNY6; Q9NY24; Q9UMW3;', 'KD00613', 'Homo sapiens (Human)', 'KIF4A', '#Chromosome-associated kinesin KIF4A#Chromokinesin-A', '-', 'ENSG00000090889', '-'),
(614, 'Q803H4', 'Histone H3-like centromeric protein A', 'GO:0000777', 16681, '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.', 'MPRHTSAHKRKPSTPRRRSPPASLPPPAGSRTRRHSGPSGSSPRKKHKFRPGTRALMEIRKYQKSTGLLLRKAPFSRLVREVCQMFSREHMMWQGYALMALQEAAEAFMVRLFSDANLCAIHAKRVTLFPRDIQLARRIRGVEHM', 145, 'Q803H4;', 'KD00614', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'cenpa', '#Histone H3-like centromeric protein A#Centromere protein A#CENP-A', '-', '-', '100302659'),
(615, 'Q759Q6', 'DASH complex subunit DAD2', 'GO:0008608===GO:0051987===GO:0042729', 12479, '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}.', 'MVPEDVYQSKKSELLYLQKVTGLTDTLKAQLDELSKQVHQMHDNAECVSSVLKNWDSILNSISQATLSLLQYTENDYEVGAWSNGSRPEADKEPPLPETLVRVNVANESQE', 111, 'Q759Q6;', 'KD00615', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DAD2', '#DASH complex subunit DAD2#Outer kinetochore protein DAD2', '-', '-', '4620475'),
(616, 'Q759Q5', 'Shugoshin', 'GO:0051383===GO:0000778===GO:0031134===GO:0034508', 72330, 'Plays a central role in chromosome cohesion during cell division by preventing premature dissociation of cohesin complex from centromeres after prophase; when most of cohesin complex dissociates from chromosomes arms. May act by protecting RAD21 and or REC8 from cleavage by ESP1/separase (By similarity). {ECO:0000250}.', 'MYKKVVGGWFVYLVSTQISSGRAGSARFGGHLGYPSPSVAYIMARASRKANGSKAKSNSVQEYLDLISLQKQQFDQMRANYSHQNTQLAKSNSMLMIKITDLETKISELVQENVQLRSRLSVTELRFKERLNQSFNLLEHGAFQRFDEIVNLFAVVRAQQGLRPESAAATEQAQRRFKGLEQRGVSPKVVGFDVPSSDSVRGERETLDDRAQQHQEADSMELNVEETQPLRKKRRRSSRRESLFIPSDFDFSNDSLENALKEADKSRSAKDEAPSVAEDTITEEKHRESASRTTEQGESESRTKEASGTLTQSNEDGMGNDKSLQKEGTQQEDAANFTHSIIEYFIPEEYDVGSSDVANTSKSKLEVYRDDNEIESSQSTSSGECKELTGELSSAQPPFVQIPASSQSKIKHSLKPPRTSQRKIVVDEVMPHNDYSDATRPRRTRGKAVDYKWPSLRAKMRRPTDKLVDATTVTDIHELQVPTNRKLRKQREGVADSADVHGETDHEQDPEQSPAAEDVSVGLQSINSNIQKDEVSDQPLQATEVTQALPEDLPLRQPMALKDITNKIHIVQKPKKSLAKKPIIGDVSDENSYYGDDTSASGLRLNEGDLSVFDLIGGVKCSNIPKTHRARAKAERQVGKKPAFKVST', 648, 'Q759Q5;', 'KD00616', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'SGO1', '#Shugoshin', '-', '-', '4620476'),
(617, 'Q6BVA0', 'Spindle assembly checkpoint kinase', 'GO:0000777', 47856, '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}.', 'MYCRVFTHFSLYRLYTLSDNININKTNHNKSIGLHQHRVNYMPRSMTASSSQLKRIETRIESLSESLSKSNARKPLGKFQLNTFDNNKITKLQNEKVRPSKSSHIPVKSPIRKKGHSPAQVLQNERMDTKLLLQKLPSASRHMTLDDFEIGKVLGKGKLGKVYCVKHKTSGYIAALKVMAKKDLIDLKLEKNFRREIEIQSNLIHPKISRLYGFFYDHKNVYLILEYSIHGELYHHLKVQRRFNDATASHYIYQVALALDYLHTKHIIHRDIKPENILLSTDNCIKLSDFGWSVKSSPSSSTKRLTICGTLDYLPPEMIESNEHDYTVDIWSLGILCYEFLVGKPPFEEIDKNSTYKRIAKVDLKIPSFLSSEATDLILRLLQKSPKKRITLAEVMNHPWIMNNQQYWPNEN', 412, 'Q6BVA0;', 'KD00617', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'IPL1', '#Spindle assembly checkpoint kinase#2.7.11.1#Aurora kinase', '-', '-', '2900232'),
(618, 'Q9VT70', 'Nuclear distribution protein nudE homolog', 'GO:0000776===k;s', 36239, 'Required for centrosome duplication and formation and function of the mitotic spindle. {ECO:0000250}.', 'MESPPMFNSVEDECRYWKERSKQYHKEWTDVKQEYDEFVEQSREMEIEMDATLDQKQSIIKDLTAKLTMFERENESLKLKLESHGIDMSNMEKQLETVKKDRDTMKVYLRQLEQKNDDLERAHRILNESIENFEKMLDQAYEKNALLELEVDEKGLLQEKLQRLMDETRDLKQELNVKSRFTPVVNGTSVPTANDTNTVNSSMNSSASLPNGIVANGELVKHDNAVATRATSVSVNALNGSLVNRNEYNQQHSLKSDGDETEDVPREWSANAAATPLLPAIHTSGAGRTALLLAGCRVVWILQFSVIHKPQIRNPIT', 317, 'Q9VT70; Q95RM2;', 'KD00618', 'Drosophila melanogaster (Fruit fly)', 'nudE', '#Nuclear distribution protein nudE homolog', '-', '-', '39169'),
(619, 'Q6CVQ9', 'Central kinetochore subunit MCM21', 'GO:0000777===GO:0034508', 33521, 'Component of the central kinetochore; which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle- microtubule attachments and proper chromosome segregation (By similarity). {ECO:0000250}.', 'MEETEAVQQDIEALEREIQTIKIQIANAHSGASKDEVKIPDAYKQFLSENINFSNLMRKDENTTLSINLSPRKPGTTTGQIQGIDSSIRSNFGVSSGHNEVAGFKSITDFVQWENSVRLIGVSLFPVNYDNIEFMGIRLELFDELSLKYDPPFYVILKPSVKRLGIWELFKHNLPKYINIHQHWQLITKDTDTSDSNIMKFANLCYKDLLKVHSRVQFFRKLEGNYVNDKQYSLLHIDNMGLNVSFRLGADIIKIKVDDGDDEIIDCTFNGEKNISLLGSIYGITNRFQSIIM', 293, 'Q6CVQ9;', 'KD00619', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'MCM21', '#Central kinetochore subunit MCM21#Minichromosome maintenance protein 21', '-', '-', '2897499'),
(620, 'Q8SRL5', 'Probable spindle assembly checkpoint kinase homolog', 'GO:0000777', 31717, 'Required for high-fidelity chromosome segregation during the later part of each cell cycle. 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 (By similarity). {ECO:0000250}.', 'MVEYWTLDRFEIGRLLGRGKFGQVWLAREREKGFIVALKIIPIKEIQTVETARQIRREIEIHSNLKHPNILRMYGHFHDKDNIYLILEYAGKGEFFKFLSDRGGKFGEKETSLYIRQVMLALTYMKECNVIHRDIKPENLLLGSDNQLKIADFGWAVYNADKRRMTFCGTMEYLAPEMVNNDIHDSGIDLWCLGILTYEFLMGKTPFESKNRNMREAYKKINSLKYTIPETISSNASDFISRLLVLSPGDRMELTEALNHPFIVKHHGRSSD', 272, 'Q8SRL5;', 'KD00620', 'Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)', 'IPL1', '#Probable spindle assembly checkpoint kinase homolog#2.7.11.1#Aurora kinase', '-', '-', '859393'),
(621, 'Q96U60', 'Probable kinetochore protein ndc80', 'GO:0034501===GO:0000778===GO:0051315===GO:0051455===GO:0031617===GO:0031262', 84855, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSQDSNAGLWSVRRPRETLHGVNLTSGIPAPPSTLKRQSTIGTIGTGHGRSLSGRQSLALPRPSQPLFQRSSDIGLGSVKRASVHNMNTSQFKPYGTPGSSGIPRSSQELDRRSSVYRPSARPSAVGGGPLAGGHMSFFQQAPQPAGVPRDPRPLKDRQFQNRIGQELLEYLAKNNFEMEMNHKLSDNFTKSPTQKDFNYLFQWLYHRIDPSYRFQKNIDQEVPPLLKQLRYPYEKSITKSQIAAVGGQNWSTFLGLLHWMMQLAQMLEGYARHQYDDACMEAGVDIAGDQIIFDFLTSAYQDWLNMDDEAGDEDVERALQPHVQGMAEAFERSNAKYIQELEILEGENARLLKEIQELEKSTPDPAILDNHFKIMEEDKIKFEEYNTLAMQRTEKYENRIQVLREELGKLHVELKEAEEERRQMQKAVDDQGISMQDIDRMTSERERLQRSIESASQRLEDVKKKVAEREMEASQRLDELERLVEKYNTVAYQIGLIPATAVNAKGKNLELQVTVNEGTPNFASSMQGVLGPNGQPLGGVENERLLADSTTGYQPAHILNLDLRGQVKNTFLALRKEVSERRKVAMDVMMEDHDLLDRAKEAIEDKRNEVEALGHRVRAAEEEYEKTKEVTNAQKMASDAQIEKMEKELAKMRAQLSESVQLMEQREMNTNIEYEQLTLRANALREELHTETMRMLNDVIKFKMHVQRSLEEYETFVADELEQELGIDDQEMEDEDTPMADV', 743, 'Q96U60;', 'KD00621', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'kpr-1', '#Probable kinetochore protein ndc80#Kinetochore protein 1', '-', '-', '3873692'),
(622, 'O94111', 'Dynein light chain; cytoplasmic', 'GO:0005868', 11031, '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 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}.', 'MASEKKDKLEPQIKSVDMSEDMQQEAVEVAIEAMEKYHIEKDIAQYIKREFDSRKGATWHCVVGRNFGSFVTHETKHFIYFYLGHCAILLFKTQ', 94, 'O94111; C8VTG5; Q547D6; Q5BGB0;', 'KD00622', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'nudG', '#Dynein light chain; cytoplasmic#8 kDa cytoplasmic dynein light chain', '-', '-', '2876196'),
(623, 'P32744', 'Protein CLASP-2', 'GO:0000776===GO:0000777===GO:0031134===k', 112285, '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. Essential for embryonic development. {ECO:0000269|PubMed:12885567; ECO:0000269|PubMed:15854912}.', 'MSRVISRSTPGGTCIVSKDDFLKSFEEVPKMEISSPSDFKEKLDQTIETLSKGQEDWNKRMNKLKQIRSMVVHGEDVIGREQLLSQLVRLTDCLDLSVKDLRSQILREAAITCGFLFKRFGTDVRQIAERCLPSAFAQVAVSTKVMATCGAVLTLFIVEFIQTKQIFTCIASYSTSKDKNQRRQLCALLEIVLEHWNEKIKRTVLPQIGELIKAAICDADPETRVAGRKAFSKLDALHSTEADKLFASVDSSKQKMLRASDAASSSTSINSERGTAPFRSKLSAGSIGGIRNAPNISSKFLAQRSASAIDTKQVTRMATSVSRTPNIRPMTTRTLSKIDTSPGGSKFARPTVGALGSRTSSNLRARGSVPTSQPGSRNGSPPRRPSATEAFPAEMQRVKSNLGSNSFVSSLSAEEATKLQKAMNTAKESLRQPSRNDDDEFLLPKRPTPQKATPQKSALDTSRVEEVIRACSSTSANEKREGIKMLAGIVSEPNLSNAEIKSLGAVLNRLLGESTNQIVLESISSFVKTHHPRLSDWLKLGLGKLFAKKGAEMTLNSKKQISTTISCILSSFDPTLQLKSTCELVCDPIHLMSPKSRVVLLEYLNELLGKYMERGSSFNTKEMKATILKMFSWMADQRNEQLITPHGEKVLCSLFALNNADFSALFNDFNPDYRDWAYKVLQSHGHDQHVPQQDAVSEEACVRATISTTAAQIEDFVVSRNLDMTPVKSPSTRAISSGFKRVDAEPLRPLSSEMNSQHRDEELSFNESFDRLKLNSTTHLIDDTSEQSKYVASKLAQISGDMGAQQYEGLLSIQTMLCEGSFTLWEQNFAKLLIAVFDVLSKSESDANKKVALRVLTKMCTSQASRLFDSTEMAICKVLDAAVNSQDGTMNVTADDCLKTLATHLPLAKVVNISQLILNEEKAQEPKASLVLKMMTRLFEGLQADELSPVVDDLAPCVIKSYDSPSSAVRKTAVYCLVAMVNKLGMKTMEPHLQNLSSGKLNLVQVYVNRAMSSSSHSHV', 1020, 'P32744;', 'KD00623', 'Caenorhabditis elegans', 'cls-2', '#Protein CLASP-2', '-', '-', '176280'),
(624, 'Q5F2C3', 'Meiosis-specific kinetochore protein', 'GO:0000780===SCL', 47423, 'Key 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. Acts by facilitating 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. Also required to prevent cleavage of cohesin at centromeres during meiosis I; possibly by acting as a regulator of the shugoshin-dependent protection pathway. Acts in collaboration with PLK1: required for PLK1 enrichemnt to kinetochores. Not required during meiosis II or mitosis. {ECO:0000269|PubMed:25533956}.', 'MDKIWHMGPRGDYTRKKRAGERLNLTPKPDLALPGRTEALPGLKGKGKEQGLRKITEKKELSRLTGSSSQRPSLLSVTGGEHLQENSPGQETPEEKTPPCETVTDTFEMDSLLSSTELVSGPAEQDDFSSCLPSCSNAELHTESTDERGSSFPSPELFRGSDCLDWEHPKLEDYMFYKNSTLLDTSKAVVIEKAPQFANLSAVLSSSSKNYEKRHRKIGMTLAAQHLSPEPKYASNLASVVDNAASEVVFAEKTGPPTTEKTQKKPENESEDSGPLVQTKLSSGHPDNKALCSPLSSALESTAVRYTLLPQPLEPVLKKGCILPDKQSKALLTSTPSSDIAEFVIDLSPVQNVSFEELFPNVSNYVNSSEVVPVSSLQESSSNEFSPNTSEICCIIRSSPGTRQMRRKDPAVKNRCSPPKDVPLDIIMKTNGRT', 434, 'Q5F2C3; Q3KNB2;', 'KD00624', 'Mus musculus (Mouse)', 'Meikin', '#Meiosis-specific kinetochore protein {ECO:0000303|PubMed:25533956}', '-', '-', '74847'),
(625, 'Q60FC2', 'Craniofacial development protein 1', 'GO:0000777', 33610, 'May play a role during embryogenesis. {ECO:0000250}.', 'MEEFDSEDFSTSEEDEDYVPSGGEYSEDDINELVKEDEVDVEEETHIIKGTKRKAERFMPRKRKQGGLSLEEEDEEDAGRESGGSGSEEEDTATEQEEGTESEDARKKKEDELWASFLNDVGPKSKVPPSTPVKTGEETEETSSSNLVKAEEQEKPKETEKVKITKVFDFAGEEVRVTKEVDPTSKEAKSFFKQSEKEKPQPNVPSAVSSLPAGSGLKRSSGMSSLLGKIGAKKQKMSTLEKSKLDWENFKEEEGIAEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP', 298, 'Q60FC2; Q588U7; Q867A5;', 'KD00625', 'Tragulus javanicus (Lesser Malay chevrotain) (Lesser mouse deer)', 'CFDP1', '#Craniofacial development protein 1#Bucentaur#h-type BCNT protein', '-', '-', '-'),
(626, 'O59716', 'Uncharacterized protein C3B8.8', 'GO:0000778', 17186, '', 'MLTQDEVSAQLGQYMLRGYTLLDTICPKCEKVPMMRLRDNPMFCVSCINDLKESDASEHVTVAESAPKIASLPISKTNDAERSQQTTKAPVMERTESSHQATLSVYSRLISELESQLDDRLPLPHNTEFLDVSLQRIERILNLISLAKSLMSS', 153, 'O59716;', 'KD00626', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'SPBC3B8.08', '#Uncharacterized protein C3B8.8', '-', '-', '2541054'),
(627, 'Q7K3L1', 'Guanylate kinase-associated protein mars', 'GO:0051382===c;k', 101946, 'Cell cycle regulator. {ECO:0000269|PubMed:15922738}.', 'MQRHKELYKEQSLVLSPRNHCQENRDRLQAARAKKREDCFYQNRIISVSPTPVKIKQLAAAQAALTQENVAPKLESPERLDTKPAELLKESNPKVSRQKLYLQRYMEWKIAKTKEHKQQDQKRRGAAINVPTVKQSKALPKSQTFRVPDNLASAKQKEAAPMFQPPKRCSLYMIANPTGKGKAAEPIKPSIPKPTSAAAPPSSNTVAASSALARHKSAASATKIVPAIRQNNNPVALARQKAAARPIPNTTKQTTSVRQPGIEAKKITTTIPRPTPATVTKAKTPGIRQQPPVVSTKPRLPEPPAPRTARLPNVLSKPFEKPLGNKAPVTRRANVVKPQPIRGGGGAAAKFKDTAGATSKAASHSIRMKATKIKSQYTRLQDNVRKLPQLKAELLHAATLDIPPLTPLDDIHNPFIDQATSTQCKSNNSSGHLLEAFGDTILLSPVAPVKAEGESSVKRQLLPEGKKEASGPVAKKKFDFTRYSVANSPAEDSLILDPQQTTVKEDTGDSTLVPEGTKTPPRRESNGMPNYLSPFVSVSRGKVNSRCEKEKRNSFYLSNEESPLEVRRAIESVLYFRLQLENEITRLQALCAEWEAYSKENEARLQETGGIDMINVTIGQTRLLTTKKMMQFSGLIDRCEAGATGKNSQPNDGSEDSKPVQAEDLEGWWDMLRLQSENVDKRFDNLKRWKANDWLDPDAVAEEPKQPKPKPKISRNMKIKSKAKPSSNLQQFLRKAHANMKKTKVEEPTLEDGLPATSSRHSSPRVIVVRNRRSFSPARTVLRMSTGEGRQSIAPNALLKSAILAAAEQNAAKTPPPKPRTSILKTPGTTKRQNRGVLFSAKKSVRRFQFTYEEGNISNDETVGADKLEDCEEDMSLEASTESGSLEQNPGRDSNQENEATPRTYTLRNRRVNLRPSSEFM', 921, 'Q7K3L1;', 'KD00627', 'Drosophila melanogaster (Fruit fly)', 'mars', '#Guanylate kinase-associated protein mars', '-', '-', '36498'),
(628, 'Q91637', 'Kinesin-like protein KIF2A', 'GO:0003777', 77414, 'Plus end-directed microtubule-dependent motor. May regulate microtubule dynamics during axonal growth (By similarity). 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. {ECO:0000250; ECO:0000269|PubMed:19351716}.', 'MVTSLNEDSESITVEWIENGDTKGKEIDLESIFSLNHDLAPDEEIDPGPEMPPPPAPTTKVNKIVKNRRTVAPVKNETPAKDNRVAAVGSARARPIQPIEQSASRQQNGSVSDISPDQPGKKDFGLASRRKSNCVKEVEKLQEKRERRRLQQQELREKKAQDFDATNPNYEIMCMIKDFRGSLDYRPLTTSDPIDEHRICVCVRKRPLNKKETTIKDLDVITIPIKDVVMVHEPKQKVDLTRFLENQTFRFDYAFDETAPNETVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFQMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIEIGNSCRTSGQTSANAHSSRSHAVFQIILRKKGKMHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELDPSRCRRPPPHDTSCPQTSWMTWKQCGEWGVAPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFPGTSIRWLEGLKKCLLEMTEEVDYDADSYATQLEAILEKKIDILTELRDKVKSFRAALQEEEHASKQINPKRPRAL', 682, 'Q91637;', 'KD00628', 'Xenopus laevis (African clawed frog)', 'kif2a', '#Kinesin-like protein KIF2A#Kinesin-related protein xKIF2', '-', '-', '379622'),
(629, 'P62714', 'Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform', 'k', 35575, 'PP2A can modulate the activity of phosphorylase B kinase casein kinase 2; mitogen-stimulated S6 kinase; and MAP-2 kinase. {ECO:0000269|PubMed:2555176}.', 'MDDKAFTKELDQWVEQLNECKQLNENQVRTLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYPERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL', 309, 'P62714; D3DSV4; P11082; Q6FHK5;', 'KD00629', 'Homo sapiens (Human)', 'PPP2CB', '#Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform#PP2A-beta#3.1.3.16', 'BIOMD0000000394,Sivakumar2011 - EGF Receptor Signaling Pathway;', 'ENSG00000104695', '-'),
(630, 'Q91636', 'Kinesin-like protein KIF2C', 'GO:0000777===GO:0003777===k', 82586, 'Promotes ATP-dependent removal of tubulin dimers from microtubules. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. {ECO:0000269|PubMed:8548824}.', 'MERLVATRLVTGLAVKIMRSNGVIHNANITSVNMDRSSVNVEWKEGEANKGKEISFADVISVNPELLDAVLAPTNVKENMPPQRNVSSQNHKRKTISKIPAPKEVAAKNSLLSESGAQSVLRERSTRMTAIHETLPYENEMEAESTPLPIQQNSVQARSRSTKVSIAEEPRLQTRISEIVEESLPSGRNNQGRRKSNIVKEMEKMKNKREEQRAQNYERRMKRAQDYDTSVPNWEFGKMIKEFRATMDCHRISMADPAEEHRICVCVRKRPLNKQELSKKEIDIISVPSKNIVLVHEPKLKVDLTKYLENQAFRFDFSFDETATNEVVYRFTARPLVQSIFEGGKATCFAYGQTGSGKTHTMGGDFSGKSQNVSKGVYAFASRDVFLLLDQPRYKHLDLDVFVTFFEIYNGKVFDLLNKKTKLRVLEDAKQEVQVVGLLEKQVISADDVFKMIEIGSACRTSGQTFANTSSSRSHACLQIILRRGSKLHGKFSLVDLAGNERGVDTASADRITRMEGAEINRSLLALKECIRALGQNKSHTPFRESKLTQILRDSFIGENSRTCMIAMLSPGFNSCEYTLNTLRYADRVKELSPQNAETNDDNLQMEDSGGSHASIEGLQLQDDFLLKDEELSTHNSFQDALNRVGELEDKAVDELRELVQKEPEWTNLLQMTEQPDYDLENFVMQAEYLIQERSKVLIALGDSINSLRLALQVEEQASKQISKKKRSNK', 730, 'Q91636; Q5D0B4;', 'KD00630', 'Xenopus laevis (African clawed frog)', 'kif2c', '#Kinesin-like protein KIF2C#Kinesin central motor 1#xKCM1', '-', '-', '380006'),
(631, 'O95229', 'ZW10 interactor', 'GO:0000776===GO:0000777===k', 31293, 'Part of the MIS12 complex; which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase. {ECO:0000269|PubMed:15094189; ECO:0000269|PubMed:15485811; ECO:0000269|PubMed:15824131; ECO:0000269|PubMed:16732327}.', 'MEAAETEAEAAALEVLAEVAGILEPVGLQEEAELPAKILVEFVVDSQKKDKLLCSQLQVADFLQNILAQEDTAKGLDPLASEDTSRQKAIAAKEQWKELKATYREHVEAIKIGLTKALTQMEEAQRKRTQLREAFEQLQAKKQMAMEKRRAVQNQWQLQQEKHLQHLAEVSAEVRERKTGTQQELDRVFQKLGNLKQQAEQERDKLQRYQTFLQLLYTLQGKLLFPEAEAEAENLPDDKPQQPTRPQEQSTGDTMGRDPGVSFKAVGLQPAGDVNLP', 277, 'O95229; A6NNV6; Q0D2I3; Q9BWD0;', 'KD00631', 'Homo sapiens (Human)', 'ZWINT', '#ZW10 interactor#ZW10-interacting protein 1#Zwint-1', '-', 'ENSG00000122952', '-'),
(632, 'O94603', 'Putative JmjC domain-containing histone demethylation protein 1', 'k;m', 108653, 'May be a histone demethylase that specifically demethylates ''Lys-36'' of histone H3; thereby playing a central role in histone code (By similarity). Represses transcriptional silencing by negatively affecting heterochromatin stability. {ECO:0000250; ECO:0000269|PubMed:12773576}.', 'MDSWLEYDDIINQDIDIPSNDLSGSGTLCVGVHSSLLENSLNSIDSFISSKEEISWCGNQSTPIATKSHLSCINPQYVNPFDTSPVSVDTEFQDTYLLDAPSFAQPHFSERQSVDKTRSRCLSRNRRRKRHPNLHKNHQRLLGMSFPQDGFRRMPAESVNFSYFRDTGFNEPTIFPSSDTQNTRQLNLSKIATLIGYDCPLALVDVVTQKQIPNKMDMESWVKYMSLEPSKRGRIYDVLSLEVSTTKLAYYVRKPNIVRDLDLVNTVWPPGSFALGEYPHVDTYCLMSAENSYTEFHIEFGGSSAYYNILDGCKIFYLIPGTSKNWEAYTAWLTSSNDSDKKFLPNMVDVCYCVEVHSQQTILVPSGWIYAVVTPCDTISIAGNFLTFLHIYPQLSIYNLELQLGIEKEYQYPYFESIMWYTAIHFYLAFPDNSSRDGIDDIIAEYETGRLFDINAFTEQELDGFEELLNYLYIRAQILRDCDIIIDIYNEPVKISKNNGYNSAYTMVPPDLDEICVDFVQKFGAWITYHHRRSAKHPSCNCFSHLQTKLIDSGPKPANNSYQHQSNFIGVVISTNHNIIKKCQESQIQTGKNNCSFQLVKKRIKSTKKAPSWRSIIKAFKKRENTRCNFLSSLHATTFREDIVVRPKIKSFVLEQLIFQALFSFAINWTPSFFLNHSNFENIALSKETFNFGGEANCENTDTTLFTTWGDQGFRPSDSICYNDFNLLETANSDAEASIHELELQPLNAVNEREVDISQTDMTPSTALDTRVDTRVDSLPEFSNLILSPSSNDDSFQLDDLLSPSSSNLKQQIQKVVPQNSLEFSVGEKEKKAAEYSLLHTFSYKRLSMENEKPDTTKVPLKYNIQHEEMKAYRRKNDLEYIDQHFASSKSGISNGRNNNKEVNLTKAENVGIKKRRIMKNENNIYDFEDHSPVREKWGHRLRSRGAS', 948, 'O94603;', 'KD00632', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'jhd1', '#Putative JmjC domain-containing histone demethylation protein 1#1.14.11.27#Heterochromatin-destabilizing protein epe1#[Histone-H3]-lysine-36 demethylase 1', '-', '-', '2539481'),
(633, 'Q9NYP9', 'Protein Mis18-alpha', 'k', 25863, 'Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038}.', 'MAGVRSLRCSRGCAGGCECGDKGKCSDSSLLGKRLSEDSSRHQLLQKWASMWSSMSEDASVADMERAQLEEEAAAAEERPLVFLCSGCRRPLGDSLSWVASQEDTNCILLRCVSCNVSVDKEQKLSKREKENGCVLETLCCAGCSLNLGYVYRCTPKNLDYKRDLFCLSVEAIESYVLGSSEKQIVSEDKELFNLESRVEIEKSLTQMEDVLKALQMKLWEAESKLSFATCKS', 233, 'Q9NYP9; B2R562; Q542Z0;', 'KD00633', 'Homo sapiens (Human)', 'MIS18A', '#Protein Mis18-alpha#FAPP1-associated protein 1', '-', 'ENSG00000227256', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(634, 'A4L691', 'PIN2/TERF1-interacting telomerase inhibitor 1', 'GO:0000777', 36710, 'Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor (By similarity). {ECO:0000250}.', 'MSMLAERRRKQKWAVDPRNTAWSNDDSKFGQKMLEKMGWSKGKGLGAQEQGATEHIKVKVKNNHLGLGATNNNEDNWIAHQDDFNQLLAALNTCHGQETADSSDNKEKKSFSLEEKSKISKNRVHYMKFTKGKDLSSRSETDLDCIFGKRRNKKLAQDGCSNSTADEADTSLTTTTTTTSAFTIQEYFAKRMAQLKSKSQAAAPGSDLSETPIEWKKGKKKTKEAAGTDIENSPQHKAKRHKKKKRVEAERGPAAKKRDQVELQPGGPSGDECSDASVEAAEDRVQTPDTQDDVPKPRKRRAKKTLQRPGGVAVDTAPDSAPVKKKKKVSR', 331, 'A4L691;', 'KD00634', 'Rattus norvegicus (Rat)', 'Pinx1', '#PIN2/TERF1-interacting telomerase inhibitor 1#Pin2-interacting protein X1', '-', '-', '305963'),
(635, 'P41391', 'Ran GTPase-activating protein 1', 'GO:0051383', 43236, 'GTPase activator for the nuclear Ras-related regulatory protein spi1 (Ran); converting it to the putatively inactive GDP- bound state.', 'MSRFSIEGKSLKLDAITTEDEKSVFAVLLEDDSVKEIVLSGNTIGTEAARWLSENIASKKDLEIAEFSDIFTGRVKDEIPEALRLLLQALLKCPKLHTVRLSDNAFGPTAQEPLIDFLSKHTPLEHLYLHNNGLGPQAGAKIARALQELAVNKKAKNAPPLRSIICGRNRLENGSMKEWAKTFQSHRLLHTVKMVQNGIRPEGIEHLLLEGLAYCQELKVLDLQDNTFTHLGSSALAIALKSWPNLRELGLNDCLLSARGAAAVVDAFSKLENIGLQTLRLQYNEIELDAVRTLKTVIDEKMPDLLFLELNGNRFSEEDDVVDEIREVFSTRGRGELDELDDMEELTDEEEEDEEEEAESQSPEPETSEEEKEDKELADELSKAHI', 386, 'P41391;', 'KD00635', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rna1', '#Ran GTPase-activating protein 1#Protein rna1', '-', '-', '2541863'),
(636, 'Q7LL22', 'Kinetochore protein nsk1', 'GO:0000942===GO:0051315===GO:0044816===c;k', 51571, 'Ensures chromosome alignment and accurate chromosome segregation during mitosis. Promotes proper kinetochore- microtubule (k-MT) interactions during anaphase B. The phosphorylation status of nsk1 affects the proper k-MT coupling; ensuring that it interacts stably only at the correct time during mitosis. {ECO:0000269|PubMed:21965289; ECO:0000269|PubMed:22065639}.', 'MAYKLSLSAVEPLLIFPAAPFSTKKEKSTFQNNLISSDVFSSALKPLSPLKSLVADFSTHSNPSKDNQLISPPKINHREFLNEEKESDTQTRYLKQLINICNSPSKNHETSLSPSKSTIDNNERKLDNEIDNYKHDVKYSPYKGQGKTSNPSQGTTKCPGIFEEDNFFSVSPKRRKNLFEKYGKTDLGKPARVPSPKKSLSSTIKSPPSRVKLPTSILSKSPPLKVPNKNRSSTFSPLRTPTSSSKTFVIVDHSTPSPPSIRTKLEAFAPNSTFATQKRLRRLATLESSPALRSTLKSLQSKSSPVKLLKLKEEKAKIKNQLFKSEEEKDPVGKQKLPLESSLSPLDHSSAEKEMQKAPAKNKRRRTGSLETGLYPKESPTPSKKRSKRVLWSLKHIVSPGNREKHSLNSTPESIMKKDTKWPQNLAKNNINSEPNTPTKSNIDTGKAHSARAHKTRKNIQS', 462, 'Q7LL22;', 'KD00636', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'nsk1', '#Kinetochore protein nsk1#Nucleolus spindle kinetochore protein 1', '-', '-', '3361470'),
(637, 'Q558Z2', 'Sun domain-containing protein 1', 'GO:0034508', 104743, 'May have an important role in defining the spacing of the nuclear envelope lumen. Essential for centrosome attachment to the nucleus; maintenance of correct ploidy; proper mitosis; association of the centromere cluster with the centrosome and the maintenance of genome stability. Requires direct chromatin binding for inner nuclear membrane targeting. {ECO:0000269|PubMed:18266910; ECO:0000269|PubMed:19632001}.', 'MSGDYKPNYQSSPSRKRLPLQSKDQASIYKYQTPSTLNLYNNTVNNNSSNNSNNHLLHNSNPNSSYLYDSSKQYSNQINIRNNSNSNSNTNNITSKKASSSYSINNKVDHNSHNNNDDDDIEDDVDINYSTNNASSNILHNRFSNSNKDDSYIDYSTDENPKILKQPQPLYNHLNNQIQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQRNNNNNSNSSNNNNTSTTIKRNNQQIDNNSNKNIISKFIGDPWKNFYYGSNKSLWPFERNNNSNNSSNNNNKVNFKQAIWIFIFSVLFIGCLLGLFSTNFYGIHIYFPSFSTTKTNSPFNSTNNNIQFSNLITKEQLYPIIDEYFKKNEILKSYNKLFEKIENDIKYLSEREQYKDIINEIKEELKLVKLSNMDEDRVNQLISKMINHYNNNENNKQELKELLSKSIEELTKLKSDSKEQLIQISTESMNQLGQLKSESINQLGQVKSESIDKFQSTLKSLSKEEQSKIEREFNHQFNQLNKDADQLLSQHSLKIEKLREEINENQQSSLLKLTQEYKQLEERLKEFSSKLQQSISSSSMDQFESWKLVFIKDIEERINKESSKLTNQYIQLTQQFTKIQSFIKDNPSIDSLTNTIESLEGIKLLIEDILEVYSADKIAKVDYALGLAGASIEYNALHYRVSETYPPIKGSGSGSGSGGANGNSLGLYYYNLATNWIFPQPKPNPPETILDPMVNTGSCWGFYTGNGTIVIRLAKKIAITEVTMEHISSNISHHIDSAPKEFQVFGLINSSDIGQSLGVFTYDTTINRHLQTFKVNKIQSTTTTTTNQDQNDDDNIQEFSHVALRILSNHGYRYTCIYRFRVHGYQIPHPEQEQIQIIQEEQSFKQEEINQQQIEQIEQIEQIEKQQQSDEL', 905, 'Q558Z2;', 'KD00637', 'Dictyostelium discoideum (Slime mold)', 'sun1', '#Sun domain-containing protein 1', '-', '-', '8618603'),
(638, 'Q751N0', 'Cytoplasmic dynein intermediate light chain DYN3', 'GO:0005868', 41760, 'Component of the cytoplasmic dynein which acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle (By similarity). {ECO:0000250}.', 'MSSGNIWKQLLEENSEQLDQSTTETYVVCCENEDSLNQFLQQCWQIDEGEKVTNLEPLGFFTKVVSRDEENLRLNVYYAKSPLDAQTLQFLGVFLRQMETSQIRWIFLLDWLLDDKRLWLRQLRNSWAALEEAQVAPFPGGAVVVVLNPSHVTQLERNTMVWNSRRLDLVHQTLRAACLNTGSALVTLDPNTAREDVMHICALLAGLPTSRPVAMLSLQSLFIPHGADSIGKICTIAPEFPVATVFDNDFVSSTFEAAIAPELTPGPRVPSDHPWLTEPTNPPSEATAWHFDLQGRLATLYRHLGDSNKAISVTQHRFHKPRSEDYAYEFELPSKHPTIRDLIRSAAADSPNDVADSIDGLMDGIVQRNVH', 371, 'Q751N0;', 'KD00638', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DYN3', '#Cytoplasmic dynein intermediate light chain DYN3#Dynein protein 3', '-', '-', '4622627'),
(639, 'F6ZDS4', 'Nucleoprotein TPR', 'GO:0000776===GO:0005868', 273990, 'Component of the nuclear pore complex (NPC); a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs; plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase; and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153; regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Plays a limited role in the regulation of nuclear protein export. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Plays also a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally; acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). {ECO:0000250}.', 'MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLNNQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQDHLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKQENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDNQRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETREREEQETTSSKIAELQHKLENSLAELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLLSTPKRSSTSQTVSTPAPEPVIDSTEAIEAKAALKQLQEIFENYKKEKIDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLNSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINLHLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSTSNVEQYRAMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLSELKKTLSTVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMTSIRQHLEETTQKAESQLLECKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKDAVQAPLNVSLNEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNVEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQQLINQQKDPDTEEYRKLLSEKEIHTKRIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLREDLSKARTEKEGIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFEELKAQQNKAMETSTQSSGDHQEQHISVQEMQELKDTLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTVQLQSELSRLRQDLQDKTTEEQLRQQMNEKTWKTLALAKSKITHLSGVKDQLTKEIEELKQRNGALDQQKDELDVRMTALKSQYEGRISRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGNASGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPTNQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTMEAGDQVSEDTVEMPLPKKLKMVTPVGTEEEVMAEESTDGEAETQAYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTSSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDDDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGAESHQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETAAGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGISHAMGGRGGINRGNIN', 2431, 'F6ZDS4; Q8R4A0; Q921B9;', 'KD00639', 'Mus musculus (Mouse)', 'Tpr', '#Nucleoprotein TPR#NPC-associated intranuclear protein#Translocated promoter region and nuclear basket protein', '-', '-', '108989'),
(640, 'Q08490', 'Shugoshin', 'GO:0051383===GO:0000778===GO:0031134===GO:0034508===GO:0000780===c;k', 66706, 'Plays a central role in chromosome cohesion during mitosis and meiosis divisions by preventing premature dissociation of cohesin complex from centromeres after prophase; when most of cohesin complex dissociates from chromosomes arms. Probably act by protecting REC8 and RAD21 from separase degradation during anaphase. Also acts as a spindle checkpoint component required for sensing tension between sister chromatids during mitosis; its degradation when they separate preventing cell cycle arrest and chromosome loss in anaphase; a time when sister chromatids are no longer under tension. {ECO:0000269|PubMed:14752166; ECO:0000269|PubMed:15062096; ECO:0000269|PubMed:15637284}.', 'MPKRKIAPNKESSRRTVSHDDLTPQIQEFQNLMDLESQKVENIRQSYSRQNSLLAKDNSILKIKVNSLEKKISQLVQENVTLRSKTSISEAIYRERLSNQLQVIENGIIQRFDEIFYMFENVRKNENLPSSSLRTMLKRTSSRSRSCSLSSPTYSKSYTRLSNHENNLSHESSFNKDDGPDLEPKAKKRKSSRRQSMFVSTSLEPEDETGENEPMMENSSVEVPAESHESAQVEETIDALNPEEENSDSVSNFTNSIIEYSIPEENPTEPEHSSSKLEIFNDSTNMLSTVPSNPLPLPLPGPSATLPTTTSDASTVYPSSSSSTNSHPKTKIKHSMKPPRIELKKKVIDEVMPVSNMSSNSEISFTRTRRTRGKAVDYTLPSLRAKMRRPSEKLVDATTVIDIHDLQVSKRNRETSHKRKSLSQDSIPDEPQLREVVVSKDYGTPKGKKTEDEIHEDTAHLMTTSNNNSNNKNEKKLTSNNSPKKSSPLLDITNKSENKKKSTRTKKLFKNAIVNNLSDENSTTRPSKSSKGTSNNNNNYNNFDNNNSNINNVNNKSVSFRLNEDDLAVFDLFGNGKAVKHQPKTYRTKK', 590, 'Q08490; D6W2D6; O00031;', 'KD00640', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SGO1', '#Shugoshin', '-', '-', '854240'),
(641, 'Q54WX4', 'Aurora kinase', 'GO:0032133===GO:0000780', 42918, 'Part of a chromosomal passenger complex. {ECO:0000269|PubMed:18326585}.', 'MSYPNNKENSNNIGGGSFSVPSKQPQRVLQQQNTNINNHQTTSTVKSTITKPTTTGATTSTNTSTIPPTTTASSSSSSSSSSSSSSSSSSSSSSSSSQSVPKKKWCIDDFDIGKLLGMGRFGHVYLAREKKSQFIVALKVLFKNQLQTHNIEHQLRREIEIQSHLRHPNILRLFGYFYDDKRVFLIIEFAKGGECFKELQKVGSFNEQTAATYTLQIADALRYCHSKHVIHRDIKPENLLIGVGGEIKIADFGWSVHAPNTKRSTFCGTLEYLPPEVIEKKGYDQTADVWSLGILIFEFLVGRSPFTSDEEKNIFHNIQENDVYYPSSISPEAKDLISRLLVSDPHQRITLKDVINHPWIKKHAHPKSLEPTKLGLPLPSQMTY', 384, 'Q54WX4;', 'KD00641', 'Dictyostelium discoideum (Slime mold)', 'aurK', '#Aurora kinase#2.7.11.1', '-', '-', '8622000'),
(642, 'O95219', 'Sorting nexin-4', 'GO:0005868', 51909, 'May be involved in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation. {ECO:0000269|PubMed:17994011}.', 'MEQAPPDPERQLQPAPLEPLGSPDAGLGAAVGKEAEGAGEESSGVDTMTHNNFWLKKIEISVSEAEKRTGRNAMNMQETYTAYLIETRSVEHTDGQSVLTDSLWRRYSEFELLRSYLLVYYPHIVVPPLPEKRAEFVWHKLSADNMDPDFVERRRIGLENFLLRIASHPILCRDKIFYLFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFTDLKHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRKHELMQYDLEMAAQDLASKKQQCEELVTGTVRTFSLKGMTTKLFGQETPEQREARIKVLEEQINEGEQQLKSKNLEGREFVKNAWADIERFKEQKNRDLKEALISYAVMQISMCKKGIQVWTNAKECFSKM', 450, 'O95219; B3KMH0; B4DQV4; D3DNA3;', 'KD00642', 'Homo sapiens (Human)', 'SNX4', '#Sorting nexin-4', '-', 'ENSG00000114520', '-'),
(643, 'O74894', '26S protease regulatory subunit 6B homolog', 'GO:0061638', 43553, 'The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). {ECO:0000250}.', 'MNSTEEIDLYNRWKALERQLEMLDLQEGFIKEDCKSLKRELIRAQEEVKRIQSVPLVIGQFLEAIDQNTAIVGSTTGSNYVVRILSTLDRELLKPSASVALQRHSNALVDILPPEADSSISMLRPDERPDVSYADVGGLDVQKQEVREAVELPLTQGDLYRQIGIDPPRGVLLYGPPGTGKTMLVKAVANSTAANFIRVVGSEFVQKYLGEGPRMVRDVFRMARENAPAIIFIDEIDAIATKRFDAQTGADREVQRILIELLTQMDGFDQGANVKVIMATNRADTLDPALLRPGRLDRKIEFPSYRDRRQRRLVFQTITAKMLLSPEVDLDTFIMRPDASSGAQIAAIMQDAGLLAVRKSRGVILQSDIEEAYARAVKPTDMEQFAFYK', 389, 'O74894;', 'KD00643', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rpt3', '#26S protease regulatory subunit 6B homolog', '-', '-', '2539539'),
(644, 'O74896', 'MHF histone-fold complex subunit 1', 'GO:0051382', 10051, 'Component of the MHF histone-fold complex required for faithful chromosome segregation during meiosis. MHF localizes to centromeres and promotes chromosome segregation (PubMed:24026537). MHF is also the dsDNA-binding component of a FANCM-MHF complex involved in DNA damage repair and genome maintenance. FANCM-MHF promotes gene conversion at blocked replication forks; probably by reversal of the stalled fork (PubMed:20347428; PubMed:24026537). FANCM-MHF promotes non-crossover recombination both in mitotic and meiotic cells (PubMed:22723423; PubMed:24026537). {ECO:0000269|PubMed:20347428; ECO:0000269|PubMed:22723423; ECO:0000269|PubMed:24026537}.', 'MEQESELLSLNTLARILTLYFSSEKGTKITPSALELITQYLRIYSKEAVCRAYEEKKNSIMSSSENEDIVLELEDLENGIAAQLALDFS', 89, 'O74896;', 'KD00644', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mhf2', '#MHF histone-fold complex subunit 1 {ECO:0000305|PubMed:20347428}', '-', '-', '2539408'),
(645, 'Q9URT4', 'CENP-A multicopy suppressor protein 2', 'k', 78160, 'Required for proper chromosome segregation via regulation of CENP-A localization to the centromere. {ECO:0000269|PubMed:12535531}.', 'MMEKSLNTVTSLPLRVIYCIDRASAIRCLAKSQHAVPIQVLKEVEPKKVICQVDIQHVIQTVCRCSPELSCKSQGDFSVYFLDHTEPDELFVGLGYWSSLLLSPTLNAGTSNSDTVWVNGFIVEFGIQRSIEIKLRFQSLQNSFEVGTPETHTSSKFLSSTLPPSLIFDPSSSEKSDSISGSLFDTNYTCPVNINGLSKQKSVRELKSPSRPSALAETNVEELELDSLFHASNDISCSATSFSEPYILDHQAALDHPATDPVCSASSTTVNSAVSTKKRRRESSTISPESAYVAAQLQNPSEREQVHEFIKEQVRIARGRIEKKFTNVRGKNRIEEQLTLSLQEGKIPPYCQNCGTIKTANWRNATYMNITLMLCNACGIYWTSRRSMRPRNLWSTYKAFETEKPLENDAFAQLELAVYKLSQQRKLSISIFRELENAGRHSPLNRLTSLDSTHSAPDPNHISKPSVVNQQKSRGGPRTAKLKNDLRRIQSSPIVAPTPDTSFREPLSEIGSNDSWLVLPNSLSANIQNDVLRKTDFMCTDKENVAFPLKTTTKPMPKVNKEETEPTLPVCDSEKENDDLECYFRTPPKPTTLQKQQQSPSPWRSELFLSDPDQNVLTPRHKPKFDLSKALSSVAKSNNIENSPQLPERYDFSLELGLNSQLDNEERRDIPLMTDLVMPSSPPMVPADRHLSVENTC', 697, 'Q9URT4; Q9P7Z1;', 'KD00645', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ams2', '#CENP-A multicopy suppressor protein 2', '-', '-', '2539242'),
(646, 'Q28I31', 'Histone H3-like centromeric protein A', 'GO:0000777', 17076, '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.', 'MRPGSTPASRRKSRPPRRVSPPLPTTSTRSPGRPSAPEQRKAPRATPKKRFRPGTRALMEIRKYQKSTELLIRKAPFSRLVREVCMTYACGLNYSWQSMALMALQEASEAFLVRLFEDSYLCSLHAKRVTLYVQDIQLARRIRGVTEGLG', 150, 'Q28I31;', 'KD00646', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'cenpa', '#Histone H3-like centromeric protein A#Centromere protein A#CENP-A', '-', '-', '549339'),
(647, 'Q6RT24', 'Centromere-associated protein E', 'GO:0000776===GO:0043515===GO:0000940===GO:0000778===GO:0008608===GO:0051315===GO:0051987===GO:0003777===GO:0000779===SCL===k', 286525, '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:12361599; ECO:0000269|PubMed:12925705}.', 'MAEEASVAVCVRVRPLNSREEELGEATHIYWKTDKNAIYQSDGGKSFQFDRVFDSNETTKNVYEEIAVPIISSAIQGYNGTIFAYGQTASGKTHTMMGSEDCLGVIPRAIHDIFQRIKKFPEREFLLRVSYMEIYNETITDLLCNAQKMKPLIIREDTNRTVYVSDLTEEVVYTAEMALKWLATGEKNRHYGITKMNQRSSRSHTIFRMILESREKAEPSNCDGSVKVSHLNLVDLAGSERAAQTGAEGVRLKEGCFINRNLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPASLDETLTTLQFASTAKYMKNTPYVNEVSNDEALLKRYRREIADLRKQLEEVNTKTRAQEMEKDQLAQLLDEKDLLQKVQDEKINNLKRMLVTSSSIALQQELEIKRKRRVTWCYGKMKDSNYEKEFKVPTSITTRKRKTSVTSLRENSLMKFGESAASSEFEMLNNTLESLAEVEWSSATTLLSEENVESELNSLNAQYNDLVLDYEQLRRENEDLKLKLKEKNELEEFELLEQKEERDQEMQLMHEVSNLKNLIKHAEEYNQDLENDLSSKVKLLKEKEEQIKNLQEYIDAQKSEKMKIDLSYTSDATEDLKQAMRTLSDLDTVALDAKKESAFLRSENLELKEKINELSDSRKQMESDIQMYQRQLEAKKKMQTDLDKELQLAFQEISKLSALVDGKGLLSNLELEKRITDLQKELNKEAEEKQTLQEEVNLLSELKSLPSEVETLRRELYEKSEELHIITTEREKLFSEMAHKDSRIQGLLEEIGNTRDDLATSQLSRRGSDGEWQALESLHAELEHRHAGVLEERERLKQEIGALSKEAESLAFSLDSVKAELSHKTQELEQKTVEGQERLNKMEALREELESRDSSLQSVEKEKVLLTEKLQQALKEVKALTQEKKNLKQLQESLQTERDQLRSDIQDTVNMNIDTQEQLLNALESLKQHQETINMLKMKAAEELSDNLHVKDRGGARDEAQQKMDGIDEQNESAHTLLGGGKDNEVTEEQRKIDSLMQENSGLQQTLESVRAEKEQLKMDLKENIEMSIENQEELRILRDELKRQQEVAAQEKDHATEKTQELSRTQERLAKTEEKLEEKNQKLQETQQQLLSTQEAMSKLQAKVIDMESLQNEFRNQGLALERVETEKLELAQRLHESYEEVKSITKERNDLKELQESFEIEKKQLKEYAREIEAEGLQAKEELNIAHANLKEYQEIITELRGSISENEAQGASTQDTAKSAPELQGEVPELLEQELLPVVKEARHSAEKVNGLEPVGAHSRTVHSMTMEGIEIGNLRLTKKLEESQMEISCLTREREDLRRTQETLQVECTQLKEDARRTLANHLETEEELNLARCCLKEQENKIDTLITSLSQRETELSSVRGQLALTTAELERKVQELCEKQEELTRKETSEAQGKMSELEQLRELLLAQASALQNAESDRLRLNTQLEESQEEMKTLREEREELRRMQEALHVESEQQKESMKEISSKLQELQNKEYECLAMKTINETQGSRCEMDHLNQQLEAQKSTLEKVEMENVNLTQRLHETLEEMRSVAKERDELWSMEERLTVERDQLKKSLEETVTKGMEKEEELRVAHVHLEEHQETINKLRKMVSDYTDEISHTQGDLKHTNAVVEAQNQDLREKEHQLSQVKADLRETVDQMEQLKKKLEAQSSTLESREIEKLELTQQLNENLKKITLVTKENDSLKIMDEALREERDQLRKSLQQTEARDLENQEKLRIAHMNLKEHQETIDRLMETMSEKTEEISNMKMELENVNMKLQEKVQELKTSERQRVKLKADASEAKKELKEQGLTLSKIEMENLNLAQKIHENLEEMKSVRKERDDLKKLEEILRMERDQLKDNLREAMLKAHQNHEETMKCGKGLLCAGEYCTGRLREKCFRIEKLLKRYSEMANDYECLNKVSLDLERETKTQKELSVTVRTKLSLPHTQTKEMEKLLTANQRCSLEFHRALKRLKYVLSSIARIKEEQHESINKREMAFIQEVEKQNELQIQIQSLSQTYRIPARDLQIKLSQEMDLHIEEMLKDFSENDFLTIKTEVQQVLNNRKEITEFLGKWLNTLFDTENLKSTIQKENKSIGLVNNFYHSRITAMINESTEFEERSATRSKDLDQYLKSLKETTEQLSEVYQTLTASQSVVHLHPTVQPSTRDSERPQAASGAEQLTSKNKIALGAVPYKEEIEDLKMQLVKSDLEKKATAKEFDKKILSLKATVEHQEEMIRLLRENLRGHQQAQDTSMISEQDSQLLSKPLTCGGGSGIVQSTKALILKSEYKRMGSEISKLKQQNEQLRKQNNQLLSDNSQLSNEVKTWEERTLKRDSYRETTCENSPKSPKVTRTDSKRRQNTTSQCRAQNLQDPVPKDSPKSWFFDNRSKSLPAPHPIRYFDNSSLGLCPEPDDVENVEPKTDLCQASLEKDVSQCKTQ', 2474, 'Q6RT24; O35059; Q3KQQ6; Q3V044; Q6PD00; Q7TPX4; Q80YB4; Q8BWX6;', 'KD00647', 'Mus musculus (Mouse)', 'Cenpe', '#Centromere-associated protein E {ECO:0000312|EMBL:AAR85498.1}#Centromere protein E#CENP-E {ECO:0000250|UniProtKB:Q02224}#Kinesin superfamily protein 10 {ECO:0000303|PubMed:9275178}#KIF10 {ECO:0000303|PubMed:9275178}#Motor domain of KIF10 {ECO:0000312|EMBL:BAA22386.1}', '-', '-', '229841'),
(648, 'Q54NP8', 'Kinesin-related protein 4', 'GO:0043515===GO:0003777', 222483, 'Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule''s plus end (By similarity). Cooperates with dynein in organizing spindle assembly during cell division. {ECO:0000250; ECO:0000269|PubMed:18430243}.', 'MDNNNNNNNNNNDKNDKNELNKIKVAIRVRPLNSRELGIDQKIPWSISKDTISLSQNPNINFTYDYVFGIDSNTIDVYNAIAKSIVNSSLNGINGTIFAYGQTSSGKTFSMRGTESIPGIIKLSIKDIFKSIEDSILEKDYLLKVSYLEIYNEEIKDLLNPTISNKKKLKIHEDIYKGVVVANLKEEIVISPDQIFALMNFGEERRHIGSTMMNDSSSRSHTIFRMQIQSTCKQNGTIQMSTLTLVDLAGSERVSSTGAEGVRLKEGTHINKSLMTLSKVISKLSEEKTQQHVPYRDSKLTRILQPSLGGNSKTAILCTITPATTHQEESISTLQFAKRAKRVKTNYKINQVADANTMLKKYESEILELQNQLVKSEEINSLLRNTISTQEISSNNFKLGMKRFNDAIIGGSLINENKKKKKRRNTLDPSYLLKDKIIKKKIRKSENQKIKKIKNSENNISSSSSNSSGEEDDDDKDDENNYSINQDDKDDSNYEDDDDEDEDDDEESDTDNEDDEDNDEDNDDDDDDDDEFKDNLNLIEPLDDETIKKIKDLDDSLGISGQVKVKREDLDLIYEELEENKKLIEEYESTLELLNNQLDEKEIEHKELLIIIDQWEQECTNRENQNQELLEIDQQSKQSIQQLNDKLLETKQQSKQSIDQLNLQLIDIESESSKNKKSFENVLGVFEKSYRLAERLEDKYFTKEIESKKQIETLANSYLQLETTYQQQLNINQQSQQKIQSLNNDIEQFKLVWVPLKDQVNGYFQENQMFKQYIIELEEKYNTLIDLQKEVEQNYLTNTLEQQRNDQYQIEINQLTTEYNNQIQQLESTNQKLQTQLYNLLANATQSTQTLEQQLQTSKQEIDTLTNEIEQLKNQYDIIRVDNDNLSKESLELKQILLSKTQQLEEQLSLAQQQKGNIEIIQQLESIIVDNQQSIDQLKIEFDQSQQDNQSIKQSYNQLESTLTLAQSENQRLLTENKQFITSLNEIKSLFNSIQQQKETIQLEFNQRLQSWSLDSEKYKEIISTLEQSNQKSIESYESKSLEFQEKENQFDSLLTNYNQLFSKYNDLATSNESNRLEFDQFKKDSNQSIQSLESLERSLKSENDNLLQQSNLLKSQLESIEKQKQDQLIPIQLELESKKCELSKLSSQFSEQTKQVTQLLISVDQYKISTNKLESQISDRNEEINNLKLKAIEINALKEENISLKDQLTKLKKAPKSQTDREKDMIKKELEKLREKFNAIDAKLKQAIQDKQTIQSEKQSLEREIKDLKRSHTSTETELDKLKKTHLAADVKSKDFIALNKSVEILTKSQEQLKSTIIELESDLSKKNIELEKKQEELVTLNQDKLEKEKKTNQLESDHSSATIKLENYENQITQLTSEIIDLKSKFQEFKSESESNIKQQEINLKESNDLNQQLTNDKFELTKQLSDLKVEFDKSKQLWSTRSSESNDTIKELQESIISKDKERQLTSEQLVKLTDQINLKTWEYNDLNSQCQQLTKTLQNVKSSNEQQEQSIVSLESQTSAKIKSLELEISQIQENHRLEVLELNRCKNQLSEKQTLMEQDNIQLNERIIQLLHQKTKHENEILSMESNIIDLENQTKELKSKIETAQQDFEIEKNYHTGLNETNTTTIKTMNEELTRSNQTIQQLLFKISKLEQTSLQTQQQQELQQATISAQQQKQQQLADDQEKQQLYQKIKLIEKELESTKQKNLYITEQFTLKESEYLDTITDYVCKEKEFEKSKASLKTSATKIQALNDIIKKLQEEKPQQQPVVKVSSSQVVNQNGQPIKSILKKPKLVIIPREQLQQPPQFKELTLSTLNSNDSNCEPESVSASSTLTSLQSISKYIGKRSEQTTLEHDLTSSTLNLPLQQQNKKVRLVITKNNKTSTDNLTTTSTSLKSKSSSNGENKENQNNNIIIKNN', 1922, 'Q54NP8; O15719; Q869B8;', 'KD00648', 'Dictyostelium discoideum (Slime mold)', 'kif4', '#Kinesin-related protein 4#Kinesin family member 4#Kinesin-7', '-', '-', '8624939'),
(649, 'P49768', 'Presenilin-1', 'GO:0000776===c;k', 52668, 'Probable catalytic subunit of the gamma-secretase complex; an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx; cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin; thus negatively regulating Wnt signaling. May also play a role in hematopoiesis. {ECO:0000269|PubMed:10206644; ECO:0000269|PubMed:10545183; ECO:0000269|PubMed:10593990; ECO:0000269|PubMed:10811883; ECO:0000269|PubMed:10899933; ECO:0000269|PubMed:11226248; ECO:0000269|PubMed:15341515; ECO:0000269|PubMed:16305624}.', 'MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI', 467, 'P49768; B2R6D3; O95465; Q14762; Q15719; Q15720; Q96P33; Q9UIF0;', 'KD00649', 'Homo sapiens (Human)', 'PSEN1', '#Presenilin-1#PS-1#3.4.23.-#Protein S182#Presenilin-1 NTF subunit#Presenilin-1 CTF subunit#Presenilin-1 CTF12#PS1-CTF12', '-', 'ENSG00000080815', '-'),
(650, 'P49769', 'Presenilin-1', 'GO:0000776', 52640, 'Probable catalytic subunit of the gamma-secretase complex; an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx; cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin; thus negatively regulating Wnt signaling. May also play a role in hematopoiesis (By similarity). {ECO:0000250}.', 'MTEIPAPLSYFQNAQMSEDSHSSSAIRSQNDSQERQQQHDRQRLDNPEPISNGRPQSNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVIMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYVTVALLIWNFGVVGMIAIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVPKNPKYNTQRAERETQDSGSGNDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSGSILTSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI', 467, 'P49769; Q91WK6; Q9JLP9;', 'KD00650', 'Mus musculus (Mouse)', 'Psen1', '#Presenilin-1#PS-1#3.4.23.-#Protein S182#Presenilin-1 NTF subunit#Presenilin-1 CTF subunit#Presenilin-1 CTF12#PS1-CTF12', '-', '-', '19164'),
(651, 'P30086', 'Phosphatidylethanolamine-binding protein 1', 'c;k', 21057, 'Binds ATP; opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin; neuropsin and chymotrypsin but not trypsin; tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. {ECO:0000250; ECO:0000269|PubMed:18294816}.', 'MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSGTVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK', 187, 'P30086; B2R4S1;', 'KD00651', 'Homo sapiens (Human)', 'PEBP1', '#Phosphatidylethanolamine-binding protein 1#PEBP-1#HCNPpp#Neuropolypeptide h3#Prostatic-binding protein#Raf kinase inhibitor protein#RKIP#Hippocampal cholinergic neurostimulating peptide#HCNP', 'BIOMD0000000149,Kim2007 - Crosstalk between Wnt and ERK pathways;BIOMD0000000394,Sivakumar2011 - EGF Receptor Signaling Pathway;', 'ENSG00000089220', '-'),
(652, 'P46871', 'Kinesin-II 95 kDa subunit', 'GO:0003777', 84202, '', 'MSKKSAETVKVVVRCRPMNSKEISQGHKRIVEMDNKRGLVEVTNPKGPPGEPNKSFTFDTVYDWNSKQIDLYDETFRSLVESVLQGFNGTIFAYGQTGTGKTFTMEGVRSNPELRGVIPNSFEHIFTHIARTQNQQFLVRASYLEIYQEEIRDLLAKDQKKRLDLKERPDTGVYVKDLSSFVTKSVKEIEHVMTVGNNNRSVGSTNMNEHSSRSHAIFIITIECSELGVDGENHIRVGKLNLVDLAGSERQAKTGATGDRLKEATKINLSLSALGNVISALVDGKSSHIPYRDSKLTRLLQDSLGGNAKTVMVANMGPASYNFDETITTLRYANRAKNIKNKPKINEDPKDALLREFQEEISRLKQALDKKGPSDGRKKGKKRKPGEQGGDDDIEDETEEEGDEMDEEEMYKESQQKLEEEKEKIMANQSMIAEEKQKLLSEVQKRQGEIKKEHQQKEMLEGKIKAMESKLLVGGKSIVDHTNEQQRKIEEQRLLLAEEKNRERDMERKLKEQDDKTVEIEGTFSSLQQEVEVKTKKLKKLFAKLQSYKSDIQDLQDEHARERQELEQTQNELIRELKLKKVIADNFIPVEERTKITTRAVFDEETEEWLLTPLAKAEGPSQMAKRPVSAVGNRRPIADYARMAAQMGGNPRYKAENILSVDLDMPNRTTRDYEGPSVAPRVQAALDAALQDEDDLDLEVQPEVFKAKTKLKKDKVRSKHKAVAKPGSNSQLYPQARGLIQK', 742, 'P46871;', 'KD00652', 'Strongylocentrotus purpuratus (Purple sea urchin)', 'KRP95', '#Kinesin-II 95 kDa subunit#KRP-85/95 95 kDa subunit', '-', '-', '373530'),
(653, 'P46872', 'Kinesin-II 85 kDa subunit', 'GO:0003777', 78697, '', 'MPGGSSGNDNVRVVVRCRPLNSKETGQGFKSVVKMDEMRGTVQVTNPNAPSGEPPKSFTFDTVFAPGAKQTDVYNQTARPIVDAIIEGYNGTIFAYGQTGTGKTFTMEGVRSQPELRGIIPNSFAHIFGHIAKEQENVRFLVRVSYLEIYNEEVKDLLGKDQQHRLEVKERPDVGVYVKDLSAFVVNNADDMDRIMTLGNKNRSVGATNMNESSSRSHAIFTITLERSDMGLDKEQHVRVGKLHMVDLAGSERQTKTGATGQRLKEATKINLSLSTLGNVISSLVDGKSTHIPYRNSKLTRLLQDSLGGNAKTVMCANIGPAEYNYDETISTLRYANRAKNIKNKAKINEDPKDALLREFQKEIEELKKQISESGEGLDDDEESGSEESGDEEAGEGGVKKKRKGKNPKRKLSPEIMAAMQKKIDEEKKALEEKKDMVEEDRNTVHRELQRRESELHKAQDDQKILNEKLNAIQKKLIVGGVDLLAKSEEQEQLLEQSALEMKERMAKQESMRKMMEEREQERMDIEEKYSSLQDEAHGKTKKLKKVWTMLMQAKSEVADMQAEHQREMEALLENVRELSRELRLSMLIIDSFIPQEFQEMIEQYVHWNEDIGEWQLKCVAYTGNNMRKQTPVADKDKSLAYGEADLSNVFLTYNLEGGGMKYKPSQGKSGRPKTSSGRPKTGKKKQASMASSIDALLQ', 699, 'P46872;', 'KD00653', 'Strongylocentrotus purpuratus (Purple sea urchin)', 'KRP85', '#Kinesin-II 85 kDa subunit#KRP-85/95 85 kDa subunit', '-', '-', '373466'),
(654, 'Q7KND8', 'FI09619pMad1TXBP181-like protein', 'k', 85018, '', 'MDDIRSSIDDMMDRFNDSITHSAPKKLLFNRLSASFDLGVSPNKRRRERESPERSLNDTASSLNMPANDSMASLQNSKLRTELIETKAIVIQLRNEIEKKSREHKEAILLAENKSTALKDQCDITSKKNLELQDDLKALRKRELVLKNEASRATAELNQLRLKFDESTLKLQKEKYLQKEDARDVHLCINNELSEYRRIAQRADLELQSTRNELERLRQLNEELQARASGFEQLRANHEKQTQSLKVANDRIQELEFEIQSYSDWKEVVKTSRERLASVPDLLAEVEHLRSHNKHLNTLIGDKLLLEEQVYDYKTRLEREEGARAEAASLQVKLLHMEQELKEWVKVAQDHCLANTLVSPMALRSRIEQLLKEDIIHVAEKTSSASDTKHLNTTIRDLEHKCAIYLKNIEDLNIGLKRHKNFKERLQRKLITVSKERDFYKQLVENFDKDTTLSNASVADMTQDMQVRVRMEVLERTVTGYKDMCATLEREIQSLRQQELVNEPAGEGYDSVKKELDTLRMENDRLRRRKEELEMEMMHRCLRGDFNMKDFKVVHFSENPAAEAYESTKNMMEKLQAEIERLKRRNKKLEDDNEQRLNETTSTGGMTLNFKEFNQLQAELESANGKMRKMRDCFKAAREEFRDVCYMLLGYRIDRIGANSNYRISSMFAEGPDDYLDISLNESNCLALLESPYSHTFNPPIDQQLAASNFPAFFSALTLELFQKATVTMT', 730, 'Q7KND8;', 'KD00654', 'Drosophila melanogaster (Fruit fly)', 'Mad1', '#FI09619p {ECO:0000313|EMBL:ACH95300.1}#Mad1 {ECO:0000313|EMBL:AAF58955.1}#TXBP181-like protein {ECO:0000313|EMBL:AAD22056.1}', '-', '-', '35954'),
(655, 'P46873', 'Osmotic avoidance abnormal protein 3', 'GO:0003777', 78779, 'May have a role during neurogenesis and axonal transport. {ECO:0000269|PubMed:7690265; ECO:0000269|PubMed:7714894}.', 'MAESVRVAVRCRPFNQREKDLNTTLCVGMTPNVGQVNLNAPDGAAKDFTFDGAYFMDSTGEQIYNDIVFPLVENVIEGYNGTVFAYGQTGSGKTFSMQGIETIPAQRGVIPRAFDHIFTATATTENVKFLVHCSYLEIYNEEVRDLLGADNKQKLEIKEQPDRGVYVAGLSMHVCHDVPACKELMTRGFNNRHVGATLMNKDSSRSHSIFTVYVEGMTETGSIRMGKLNLVDLAGSERQSKTGATGDRLKEATKINLSLSALGNVISALVDGKSKHIPYRDSKLTRLLQDSLGGNTKTIMIACVSPSSDNYDETLSTLRYANRAKNIKNKPTINEDPKDALLREYQEEIARLKSMVQPGAVGVGAPAQDAFSIEEERKKLREEFEEAMNDLRGEYEREQTSKAELQKDLESLRADYERANANLDNLNPEEAAKKIQQLQDQFIGGEEAGNTQLKQKRMKQLKEAETKTQKLAAALNVHKDDPLLQVYSTTQEKLDAVTSQLEKEVKKSKGYEREIEDLHGEFELDRLDYLDTIRKQDQQLKLLMQIMDKIQPIIKKDTNYSNVDRIKKEAVWNEDESRWILPEMSMSRTILPLANNGYMQEPARQENTLLRSNFDDKLRERLAKSDSENLANSYFKPVKQINVINKYKSDQKLSTSKSLFPSKTPTFDGLVNGVVYTDALYERAQSAKRPPRLASLNPK', 699, 'P46873; Q8MPT7; Q8MPT8;', 'KD00655', 'Caenorhabditis elegans', 'osm-3', '#Osmotic avoidance abnormal protein 3#Kinesin-like protein osm-3', '-', '-', '177141'),
(656, 'P46874', 'Kinesin-like protein KLP2', 'GO:0003777', 43036, 'May be related to mitotic segregation.', 'RSEKGCRKEKNQNIQVFVRLRPLNQRERDLKSLGVVEVHNNKEVVVRISQQNSITKKFTFDRAFAPYANQVEVYQEVVSPLIEEVLAGYNCTVFAYGQTGTGKTHTMVGENTGDETTWQKDPLAGIIPRALSQLFDELRISNTEYTVRVSYLELYNEELFDLLATSEDNSKLRIYEDVTRKGSNIVNGLEEITVYNKKEVFRIMAQGQERKKVASTLMNAQSSRSHTVFTIVVHMKENSLPEGEELVKIGKLNLVDLAGSENISKAGSDNPAKRERARECVNINQSLLTLGRVITALVERHPHVPYRESKLTRILQESLGGRTKTSIIATISPGHKDLEETMSTLEYLTEQRTFRTSLRSTRKYKESYIERISEEIAD', 378, 'P46874;', 'KD00656', 'Bombyx mori (Silk moth)', '', '#Kinesin-like protein KLP2', '-', '-', '-'),
(657, 'B3LFD9', '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, 'B3LFD9;', 'KD00657', 'Saccharomyces cerevisiae (strain RM11-1a) (Baker''s yeast)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '-'),
(658, 'P83917', 'Chromobox protein homolog 1', 'k', 21418, 'Component of heterochromatin. Recognizes and binds histone H3 tails methylated at ''Lys-9''; leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.', 'MGKKQNKKKVEEVLEEEEEEYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEFLQSQKTAHETDKSEGGKRKADSDSEDKGEESKPKKKKEESEKPRGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEERLTWHSYPSEDDDKKDDKN', 185, 'P83917; P23197;', 'KD00658', 'Mus musculus (Mouse)', 'Cbx1', '#Chromobox protein homolog 1#Heterochromatin protein 1 homolog beta#HP1 beta#Heterochromatin protein p25#M31#Modifier 1 protein', '-', '-', '12412'),
(659, 'P83916', 'Chromobox protein homolog 1', 'k', 21418, 'Component of heterochromatin. Recognizes and binds histone H3 tails methylated at ''Lys-9''; leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane.', 'MGKKQNKKKVEEVLEEEEEEYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEFLQSQKTAHETDKSEGGKRKADSDSEDKGEESKPKKKKEESEKPRGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEERLTWHSYPSEDDDKKDDKN', 185, 'P83916; P23197;', 'KD00659', 'Homo sapiens (Human)', 'CBX1', '#Chromobox protein homolog 1#HP1Hsbeta#Heterochromatin protein 1 homolog beta#HP1 beta#Heterochromatin protein p25#M31#Modifier 1 protein#p25beta', '-', 'ENSG00000108468', '-'),
(660, 'P51807', 'Dynein light chain Tctex-type 1', 'GO:0005868', 12483, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site (By similarity). May also be a accessory component of axonemal dynein. Plays an important role in male germ cell development and function. Candidate for involvement in male sterility. {ECO:0000250}.', 'MEDFQASEETAFVVDEVSSIVKEAIESAIGGNAYQHSKVNQWTTNVLEQTLSQLTKLGRPFKYIVTCVIMQKNGAGLHSASSCFWDSSTDGSCTVRWENKTMYCIVSTFGLSI', 113, 'P51807; Q5M8S6;', 'KD00660', 'Mus musculus (Mouse)', 'Dynlt1', '#Dynein light chain Tctex-type 1#Activator of G-protein signaling 2#AGS2#T-complex testis-specific protein 1#TCTEX-1', '-', '-', '100040531'),
(661, 'P51808', 'Dynein light chain Tctex-type 3', 'GO:0000777===GO:0005868===k', 13062, '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}.', 'MEEYHRHCDEVGFNAEEAHNIVKECVDGVLGGEDYNHNNINQWTASIVEQSLTHLVKLGKAYKYIVTCAVVQKSAYGFHTASSCFWDTTSDGTCTVRWENRTMNCIVNVFAIAIVL', 116, 'P51808; Q6ICS3;', 'KD00661', 'Homo sapiens (Human)', 'DYNLT3', '#Dynein light chain Tctex-type 3#Protein 91/23#T-complex-associated testis-expressed 1-like', '-', 'ENSG00000165169', '-'),
(662, 'P49777', 'ARS-binding protein 1', 'GO:0000780===k', 59840, 'Binds; preferentially; to the Maundrell ARS consensus sequence within ARS3002.', 'MGKIKRRAITEHEKRALRHYFFQLQNRSGQQDLIEWFREKFGKDISQPSVSQILSSKYSYLDNTVEKPWDVKRNRPPKYPLLEAALFEWQVQQGDDATLSGETIKRAAAILWHKIPEYQDQPVPNFSNGWLEGFRKRHILHAINEQPTESVVLNNTEPPNDPLSRVYDVTRLTNINDIFTMQETGLFWKLVPNGTPEVEDIKGITRFKARITLTVCCNASGTERLPLWVIGYSQSPRVFRAANVKPEVMNFKWRSNGKASMTTAIMEEWLRWFDACMEGRKVILLIDSYTPHLRAVENIRNSGNDLRNTTVITLPSTSASISQPCSEGVIYALKACYRKHWVQYILEQNELGRNPYNTTNVLRAILWLVKAWTTDISPEIIENAFNLSGVLGLFNESAVTSRALDEMIHPLRELVSEFSVQAAMRIEDFISPSEENIVDSSEDIINQIASQYMDDRAFETDEEESTEFQITTKDAMKAIELLLNYEAQQPDGNPAITISLLNYQKLLEARGGNVNLSRLRST', 522, 'P49777; Q9URU7;', 'KD00662', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'abp1', '#ARS-binding protein 1', '-', '-', '2539971'),
(663, 'B4G5J0', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 26615, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MADLKASEGDLSDYYMRLKKIFSNETRLQSREASISKRSSRVHKNIISAKEAIERQERDFGKLQKVLLNRNQELERRFTLGEALAQQLEVTRQRNADMEAQLLRHTTEGRQRSNELMECMHSLKQATGTYINHEALPARLNGVSVVRADDGDIKLIPFSLDGNDADGLHTLWRSLHTRTDNNASKWRKLISDQEVAGASPVTPSGSERPKATSKHSNFMPTSIIEIDLTSPTNDAS', 236, 'B4G5J0;', 'KD00663', 'Drosophila persimilis (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6587440'),
(664, 'O14777', 'Kinetochore protein NDC80 homolog', 'GO:0000776===GO:0000777===GO:0000942===GO:0008608===GO:0051315===GO:0031262===c;k', 73913, '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. {ECO:0000269|PubMed:12351790; ECO:0000269|PubMed:14654001; ECO:0000269|PubMed:14699129; ECO:0000269|PubMed:15062103; ECO:0000269|PubMed:15235793; ECO:0000269|PubMed:15239953; ECO:0000269|PubMed:15548592; ECO:0000269|PubMed:16732327; ECO:0000269|PubMed:9315664}.', 'MKRSSVSSGGAGRLSMQELRSQDVNKQGLYTPQTKEKPTFGKLSINKPTSERKVSLFGKRTSGHGSRNSQLGIFSSSEKIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAMKESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLFNVDAFKLESLEAKNRALNEQIARLEQEREKEPNRLESLRKLKASLQGDVQKYQAYMSNLESHSAILDQKLNGLNEEIARVELECETIKQENTRLQNIIDNQKYSVADIERINHERNELQQTINKLTKDLEAEQQKLWNEELKYARGKEAIETQLAEYHKLARKLKLIPKGAENSKGYDFEIKFNPEAGANCLVKYRAQVYVPLKELLNETEEEINKALNKKMGLEDTLEQLNAMITESKRSVRTLKEEVQKLDDLYQQKIKEAEEEDEKCASELESLEKHKHLLESTVNQGLSEAMNELDAVQREYQLVVQTTTEERRKVGNNLQRLLEMVATHVGSVEKHLEEQIAKVDREYEECMSEDLSENIKEIRDKYEKKATLIKSSEE', 642, 'O14777; Q6PJX2;', 'KD00664', 'Homo sapiens (Human)', 'NDC80', '#Kinetochore protein NDC80 homolog#Highly expressed in cancer protein#Kinetochore protein Hec1#HsHec1#Kinetochore-associated protein 2#Retinoblastoma-associated protein HEC', '-', 'ENSG00000080986', '-'),
(665, 'P02557', 'Tubulin beta chain', 'GO:0005828', 50923, 'Tubulin is the major constituent of microtubules. It binds two moles of GTP; one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.', 'MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVIRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMMAAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQGLDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVSEYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFE', 457, 'P02557; D6VTJ3;', 'KD00665', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'TUB2', '#Tubulin beta chain#Beta-tubulin', '-', '-', '850506'),
(666, 'Q03898', 'Filament protein FIN1', 'GO:0000778', 33186, 'Forms cell-cycle specific filaments between the spindle pole bodies of dividing yeast cells.', 'MSNKSNRRSLRDIGNTIGRNNIPSDKDNVFVRLSMSPLRTTSQKEFLKPPMRISPNKTDGMKHSIQVTPRRIMSPECLKGYVSKETQSLDRPQFKNSNKNVKIQNSDHITNIIFPTSPTKLTFSNENKIGGDGSLTRIRARFKNGLMSPERIQQQQQQHILPSDAKSNTDLCSNTELKDAPFENDLPRAKLKGKNLLVELKKEEEDVGNGIESLTKSNTKLNSMLANEGKIHKASFQKSVKFKLPDNIVTEETVELKEIKDLLLQMLRRQREIESRLSNIELQLTEIPKHK', 291, 'Q03898; D6VSB6;', 'KD00666', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'FIN1', '#Filament protein FIN1#Filaments in between nuclei protein 1', '-', '-', '851708'),
(667, 'Q4I0J6', 'Probable kinetochore protein NDC80', 'GO:0034501===GO:0000778===GO:0051315===GO:0051455===GO:0031617===GO:0031262', 82885, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSQDTGLWSVRRPRETLGGISANSAIPQPGSTMKRSSSNIGGNYPGSHVRSMSGSRHSLAMPRPSQPMFQRSSSGTNLVDLGLSSVKRSSFAPKSTFTPGTATKRASTDGDRRSSVYRPRQSTVPAVSHHQSFFQTTPAPAGVPRDPRPLKDRSFQARIGQEIMEYMVQHNFEMEMKHVLSQNVLKSPTQKDFNYMFQWLYHRIDPSHKFQKNIDQEVPPLLKQMRYPFERSITKSQIAAVGGQNWSTFLGLLHWMMQLAQMLDGYVNCQYDEACMEAGIDVSGDRIIFDFLSNGYRDWLAMDEDLGDEEAERVLAPHVQSMAAAFERSNSKYTSELDMLEAENARLLKEIEDLEKSTPDPAVLDHHFKIMEEDKVKFEEYNALAMQRSEKYESRSQVLQEELDKLLEELQEADEERRSLQKAVDAQGISMQDIDRMTAERERLQRGIESASQRLEEVKKKVSEREAEASRKLDELEQMVDRYNTMAYQIALIPSTAANAKGREFELQVTVADDSDFTTSIMKSGPSSADRLVVDSTTGHQAGHILNLDLRGKIRNSFISLRKEISDRRATAMDEMIKDHDLLDGIKEAIEDRRGEVEALNHRVRAAEEEYEKTKEVTTAQKLASDAHIEKMEKELSRMRAGLSENVQILEQREINTTIEYEQLVLQANALREELHTEIDRMLNDVIKFKIHVQKSLDDYEGFVTEELEKELGSDEMQEDTQRMDM', 726, 'Q4I0J6; V6RV41;', 'KD00667', 'Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084(Wheat head blight fungus) (Fusarium graminearum)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '2791374'),
(668, 'Q15435', 'Protein phosphatase 1 regulatory subunit 7', 'k', 41564, 'Regulatory subunit of protein phosphatase 1. {ECO:0000250}.', 'MAAERGAGQQQSQEMMEVDRRVESEESGDEEGKKHSSGIVADLSEQSLKDGEERGEEDPEEEHELPVDMETINLDRDAEDVDLNHYRIGKIEGFEVLKKVKTLCLRQNLIKCIENLEELQSLRELDLYDNQIKKIENLEALTELEILDISFNLLRNIEGVDKLTRLKKLFLVNNKISKIENLSNLHQLQMLELGSNRIRAIENIDTLTNLESLFLGKNKITKLQNLDALTNLTVLSMQSNRLTKIEGLQNLVNLRELYLSHNGIEVIEGLENNNKLTMLDIASNRIKKIENISHLTELQEFWMNDNLLESWSDLDELKGARSLETVYLERNPLQKDPQYRRKVMLALPSVRQIDATFVRF', 360, 'Q15435; B4DFD4; B5MCY6; Q9UQE5; Q9UQE6; Q9Y6K4;', 'KD00668', 'Homo sapiens (Human)', 'PPP1R7', '#Protein phosphatase 1 regulatory subunit 7#Protein phosphatase 1 regulatory subunit 22', '-', 'ENSG00000115685', '-'),
(669, 'Q9UIS9', 'Methyl-CpG-binding domain protein 1', 'k', 66607, 'Transcriptional repressor that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binding is abolished by the presence of 7-mG that is produced by DNA damage by methylmethanesulfonate (MMS). Acts as transcriptional repressor and plays a role in gene silencing by recruiting AFT7IP; which in turn recruits factors such as the histone methyltransferase SETDB1. Probably forms a complex with SETDB1 and ATF7IP that represses transcription and couples DNA methylation and histone ''Lys-9'' trimethylation. Isoform 1 and isoform 2 can also repress transcription from unmethylated promoters. {ECO:0000269|PubMed:10454587; ECO:0000269|PubMed:10648624; ECO:0000269|PubMed:12665582; ECO:0000269|PubMed:12697822; ECO:0000269|PubMed:12711603; ECO:0000269|PubMed:14555760; ECO:0000269|PubMed:14610093; ECO:0000269|PubMed:15327775; ECO:0000269|PubMed:9207790; ECO:0000269|PubMed:9774669}.', 'MAEDWLDCPALGPGWKRREVFRKSGATCGRSDTYYQSPTGDRIRSKVELTRYLGPACDLTLFDFKQGILCYPAPKAHPVAVASKKRKKPSRPAKTRKRQVGPQSGEVRKEAPRDETKADTDTAPASFPAPGCCENCGISFSGDGTQRQRLKTLCKDCRAQRIAFNREQRMFKRVGCGECAACQVTEDCGACSTCLLQLPHDVASGLFCKCERRRCLRIVERSRGCGVCRGCQTQEDCGHCPICLRPPRPGLRRQWKCVQRRCLRGKHARRKGGCDSKMAARRRPGAQPLPPPPPSQSPEPTEPHPRALAPSPPAEFIYYCVDEDELQPYTNRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQCLQFAMKRLLPSVWSESEDGAGSPPPYRRRKRPSSARRHHLGPTLKPTLATRTAQPDHTQAPTKQEAGGGFVLPPPGTDLVFLREGASSPVQVPGPVAASTEALLQEAQCSGLSWVVALPQVKQEKADTQDEWTPGTAVLTSPVLVPGCPSKAVDPGLPSVKQEPPDPEEDKEENKDDSASKLAPEEEAGGAGTPVITEIFSLGGTRFRDTAVWLPRSKDLKKPGARKQ', 605, 'Q9UIS9; A4UTZ0; B4DXJ5; E9PEC5; K7ELI2; K7EQZ4; K7ESN0; O15248;O95241; Q7Z7B5; Q8N4W4; Q9UNZ6; Q9UNZ7; Q9UNZ8; Q9UNZ9;', 'KD00669', 'Homo sapiens (Human)', 'MBD1', '#Methyl-CpG-binding domain protein 1#CXXC-type zinc finger protein 3#Methyl-CpG-binding protein MBD1#Protein containing methyl-CpG-binding domain 1', '-', 'ENSG00000141644', '-'),
(670, 'O14782', 'Kinesin-like protein KIF3C', 'GO:0003777', 89426, 'Microtubule-based anterograde translocator for membranous organelles. {ECO:0000250}.', 'MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQTRAVGSTHMNEVSSRSHAIFIITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNTAGGAATPSSGGGGGGGGSGGGAGGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPQVNEDPKDTLLREFQEEIARLKAQLEKRGMLGKRPRRKSSRRKKAVSAPPGYPEGPVIEAWVAEEEDDNNNNHRPPQPILESALEKNMENYLQEQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEDLRREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMMLRDEETMELRGTYTSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHDEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWKFQPLVPAGVSSSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAVFEMEFSHDQEQDPRALHMERLMRLDSFLERPSTSKVRKSRSWCQSPQRPPPSTTHASLASASLRPATVADHE', 793, 'O14782; O43544; Q4ZG18; Q53SX5; Q562F7;', 'KD00670', 'Homo sapiens (Human)', 'KIF3C', '#Kinesin-like protein KIF3C', '-', 'ENSG00000084731', '-'),
(671, 'P24386', 'Rab proteins geranylgeranyltransferase component A 1', 'k', 73476, 'Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB; and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides; a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation. {ECO:0000269|PubMed:18532927; ECO:0000269|PubMed:7957092}.', 'MADTLPSEFDVIVIGTGLPESIIAAACSRSGRRVLHVDSRSYYGGNWASFSFSGLLSWLKEYQENSDIVSDSPVWQDQILENEEAIALSRKDKTIQHVEVFCYASQDLHEDVEEAGALQKNHALVTSANSTEAADSAFLPTEDESLSTMSCEMLTEQTPSSDPENALEVNGAEVTGEKENHCDDKTCVPSTSAEDMSENVPIAEDTTEQPKKNRITYSQIIKEGRRFNIDLVSKLLYSRGLLIDLLIKSNVSRYAEFKNITRILAFREGRVEQVPCSRADVFNSKQLTMVEKRMLMKFLTFCMEYEKYPDEYKGYEEITFYEYLKTQKLTPNLQYIVMHSIAMTSETASSTIDGLKATKNFLHCLGRYGNTPFLFPLYGQGELPQCFCRMCAVFGGIYCLRHSVQCLVVDKESRKCKAIIDQFGQRIISEHFLVEDSYFPENMCSRVQYRQISRAVLITDRSVLKTDSDQQISILTVPAEEPGTFAVRVIELCSSTMTCMKGTYLVHLTCTSSKTAREDLESVVQKLFVPYTEMEIENEQVEKPRILWALYFNMRDSSDISRSCYNDLPSNVYVCSGPDCGLGNDNAVKQAETLFQEICPNEDFCPPPPNPEDIILDGDSLQPEASESSAIPEANSETFKESTNLGNLEESSE', 653, 'P24386; A1L4D2; O43732;', 'KD00671', 'Homo sapiens (Human)', 'CHM', '#Rab proteins geranylgeranyltransferase component A 1#Choroideremia protein#Rab escort protein 1#REP-1#TCD protein', '-', 'ENSG00000188419', '-'),
(672, 'Q803Q2', 'Nuclear distribution protein nudE-like 1-B', 'GO:0000776', 38443, 'Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. 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 (By similarity). {ECO:0000250}.', 'MDTEMMPKFSSKDEEIDYWKCLSLKYKKSCHDAQEELQEFQEGSRELEAELEAQLGQAEHRIRDLQSENQRLKSEVDILKEKLEQQYAQSYKQISMLEDDLLQTRGIKEQLHKYVRELEQANDDLERAKRATITSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERTSDVTRMSAPSSPTLDIDKTDSAVQASLSLPATPVGKTMEHPFIGTKALTNGCGNGSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQAARKNYTTGNGNLINSNATKFSHSLHTTYFDKTTMNGLDPGALSAAIASPRAVSPPGLLPLSV', 344, 'Q803Q2;', 'KD00672', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'ndel1b', '#Nuclear distribution protein nudE-like 1-B', '-', '-', '333957');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(673, 'O59757', 'Kinetochore protein spc7', 'GO:0000777===GO:1990299===GO:0000941===GO:0051315===GO:0031617===GO:0000779===SCL===k', 153593, '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.', 'MPTSPRRNSIATTDNVIGRNKSRKRPHSLGGPGALQELKEHTNPAKGILKSYSSFSVDPAFTGDEDFNDIHTQINNTVIGISSNVMAASKRLQMEDLQQLSRETSRKSLNRRVSFASHARVRWYPKDHQSDSEKSTSNHSTPERTFASDAKNHSPKGPTTTSFSRNETQSSPHSHSASIISDGSDMDIASPIRSTESDMVSEALNAGHPPPSLYPENDDLSIQNPTKALPEAEKALDVHDATREQVNDREETNMDLTIQFQEADSFLSHSESIKGLSSSEQGTVYSLKASHDPSNQTQLSSPNKSSSPTSIEISDFSKNNENHDQSENKEEEEDMMLTRPIEIPQHFSPIARPLTSQEAIVDMDITSNNINLSPVSHFSNGLDLQNLEEAPMNLTRPINANPHLTNHSPNDLTNGEEEMDTTSAFNIENSHLTLLSPIRPSSRSMEEQIMDLTQPISSTNAPTHLNEDDLNQFTSNISSSSKPRKDNNKTANSSKPIPDSEDFMDITRPFNILSPSKEALSEEQPMELTSTVFPCENSTSHLEVEEAAMDETVAFQIRGNNVELPSADKENAEREEIPSYSDKSENFNTTSFTNHERSPNGNNNLKFSKDPNSSSPSRHVVATPTDKLGTRKRRLRYSTSSFDQSTLRRNRLATIRNARKSISTLNDRELLPVNFFEKKVNSGLYKSVERSENYRLGATPLTAEKPFTTEKPLSSLPEEVSRQPTDDKGEQVSNADVDSGLSKTERLTIQQTNEIKHVPTNTTSSVKLPQQPSNEDEKERITTADYADSTSLERLESQEPNRNELVQVGSSNAGNTTSVGMNEHEKSPVKLSKGVSNVDTSLGASTINTNILNQDSGPNEEIPVGNEPEFDTMPTLPNVEPISLSDFLKMTGIEFLDNLTIAKRRETLLPNAEENKKCSIQELLESFYIQFPLLELYKFSCQQLQDYIAEGKDFVTKIEEETLKENPLLFYEYRKASSDMRVLMDSQFLMMKTFARLQAKGDWYEWREGLMQGIKHELNLNLTGMQRSLTHLMDVANVIHPYAQEIQERYNGSITTVQTLKKQKEFANQYDSTLLAQAQEKLEKLKVEVERRRRLLSEKEERRKELAIKIEQVTNSCSDLELRTNAEQDFYAKNQDFEFDEIKRYEEQLLNLKNELGWTIVSLTAGGIKLATNNTALSPYSAEVTVEILRQNFQVNVDIACKFPNESNACSSNVLEHVASSFSKWHSKVFSRNLRLLKKYLNDVSICWEQIVYLVQDFQRLWYHWPFLSVENDDKSIIINVELYLRSVSSKVKVVFGLPIDTIYQTTEVGKFYASTSVAVKQMYAESEGDSYVSEVLNTLSEVVHCTSTYALSSACLTVWNKYS', 1364, 'O59757;', 'KD00673', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'spc7', '#Kinetochore protein spc7#NMS complex subunit spc7', '-', '-', '2539155'),
(674, 'O94643', 'Kinetochore protein mis17', 'GO:0000778===GO:0061638===k', 49666, '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 correct chromosome segregation where it has a role in the formation and/or maintenance of specialized chromatin at the centromere. {ECO:0000269|PubMed:15369671; ECO:0000269|PubMed:16079914}.', 'MENNSHNVDERRAARMRGAERYKIQNVEFSLDQNLLANLESSTSSSTRSSPASNQQNLEIVSQSEAYHKISDLDDSTSIFSISDQENILERRISEEVVRENSVSSIENVSSSAVARETQSSANILVKDNHFFSHKQKKIQRESIPFHKRDNIETSDAYSSSILENSPPNKVQRLSSLDSSQDSFQEEHPGNVTGTTFSSQAPEERIASPISTSSPESLTNQSSSLQSSLQTSSMAPRNLLDQSTEKDIVVGASDELVRIELTKLSKEAGGSKTLNELDAVQQFFQEFIKENEPLEPYVVKVKNAFVEQVSIRLLELIDLLDANRILSTACKKAANEKLAVQRDLSKLREDRLSVQRKKIQLRNEYIKLSHQQNFLDDIDDFFSQCETVKNELENVTTTPNSTEAFSEINEYASALSKNYGLESQLVELQSLLTQFYQKFLS', 441, 'O94643;', 'KD00674', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis17', '#Kinetochore protein mis17#Sim4 complex subunit mis17', '-', '-', '3361327'),
(675, 'P38937', 'Tethering factor for nuclear proteasome cut8', 'GO:0061638', 30622, '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 like mitotic cyclin and cut2. Required for normal progression of anaphase. {ECO:0000269|PubMed:11084332; ECO:0000269|PubMed:16096059; ECO:0000269|PubMed:8065367}.', 'METLSYSQIKKRKADFDEDISKRARQLPVGEQLPLSRLLQYSDKQQLFTILLQCVEKHPDLARDIRGILPAPSMDTCVETLRKLLINLNDSFPYGGDKRGDYAFNRIREKYMAVLHALNDMVPCYLPPYSTCFEKNITFLDAATNVVHELPEFHNPNHNVYKSQAYYELTGAWLVVLRQLEDRPVVPLLPLEELEEHNKTSQNRMEEALNYLKQLQKNEPLVHERSHTFQQTNPQNNFHRHTNSMNIGNDNGMGWHSMHQYI', 262, 'P38937;', 'KD00675', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cut8', '#Tethering factor for nuclear proteasome cut8#Cell untimely torn protein 8', '-', '-', '2542184'),
(676, 'P15348', 'DNA topoisomerase 2', 'k', 164396, 'Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.', 'MENGNKALSIEQMYQKKSQLEHILLRPDSYIGSVEFTKELMWVYDNSQNRMVQKEISFVPGLYKIFDEILVNAADNKQRDKSMNTIKIDIDPERNMVSVWNNGQGIPVTMHKEQKMYVPTMIFGHLLTSSNYNDDEKKVTGGRNGYGAKLCNIFSTSFTVETATREYKKSFKQTWGNNMGKASDVQIKDFNGTDYTRITFSPDLAKFKMDRLDEDIVALMSRRAYDVAASSKGVSVFLNGNKLGVRNFKDYIDLHIKNTDDDSGPPIKIVHEVANERWEVACCPSDRGFQQVSFVNSIATYKGGRHVDHVVDNLIKQLLEVLKKKNKGGINIKPFQVRNHLWVFVNCLIENPTFDSQTKENMTLQQKGFGSKCTLSEKFINNMSKSGIVESVLAWAKFKAQNDIAKTGGRKSSKIKGIPKLEDANEAGGKNSIKCTLILTEGDSAKSLAVSGLGVIGRDLYGVFPLRGKLLNVREANFKQLSENAEINNLCKIIGLQYKKKYLTEDDLKTLRYGKVMIMTDQDQDGSHIKGLLINFIHTNWPELLRLPFLEEFITPIVKATKKNEELSFYSLPEFEEWKNDTANHHTYNIKYYKGLGTSTSKEAKEYFQDMDRHRILFKYDGSVDDESIVMAFSKKHIESRKVWLTNHMDEVKRRKELGLPERYLYTKGTKSITYADFINLELVLFSNADNERSIPSLVDGLKPGQRKVMFTCFKRNDKREVKVAQLSGSVAEMSAYHHGEVSLQMTIVNLAQNFVGANNINLLEPRGQFGTRLSGGKDCASARYIFTIMSPLTRLIYHPLDDPLLDYQVDDGQKIEPLWYLPIIPMVLVNGAEGIGTGWSTKISNYNPREIMKNLRKMINGQEPSVMHPWYKNFLGRMEYVSDGRYIQTGNIQILSGNRLEISELPVGVWTQNYKENVLEPLSNGTEKVKGIISEYREYHTDTTVRFVISFAPGEFERIHAEEGGFYRVFKLTTTLSTNQMHAFDQNNCLRRFPTAIDILKEYYKLRREYYARRRDFLVGQLTAQADRLSDQARFILEKCEKKLVVENKQRKAMCDELLKRGYRPDPVKEWQRRIKMEDAEQADEEDEEEEEAAPSVSSKAKKEKEVDPEKAFKKLTDVKKFDYLLGMSMWMLTEEKKNELLKQRDTKLSELESLRKKTPEMLWLDDLDALESKLNEVEEKERAEEQGINLKTAKALKGQKSASAKGRKVKSMGGGAGAGDVFPDPDGEPVEFKITEEIIKKMAAAAKVAQAAKEPKKPKEPKEPKVKKEPKGKQIKAEPDASGDEVDEFDAMVEGGSKTSPKAKKAVVKKEPGEKKPRQKKENGGGLKQSKIDFSKAKAKKSDDDVEEVTPRAERPGRRQASKKIDYSSLFSDEEEDGGNVGSDDDGNASDDDSPKRPAKRGREDESSGGAKKKAPPKKRRAVIESDDDDIEIDEDDDDDSDFNC', 1447, 'P15348; Q9VIW2;', 'KD00676', 'Drosophila melanogaster (Fruit fly)', 'Top2', '#DNA topoisomerase 2#5.99.1.3#DNA topoisomerase II', '-', '-', '35225'),
(677, 'O59751', 'Kinesin-like protein 6', 'GO:0000778===GO:0051315===SCL===k', 87796, 'Has a role in establishing metaphase during mitosis. Required for chromosome segregation where it generates tension during kinetochore capturing. {ECO:0000269|PubMed:11967147}.', 'MKEGSSISVAVRVRPFTEREKGLLAETPKSKEFLGDGSLAVSNTSSNTFCTNGIRKIVRVLDDNVLIFDPPEENPLAKVQKSLLPAGKRFRDVRYAFDRLFGEEASQEDVYKGTTEPLLDSVLQGYNATVFAYGATGCGKTHTISGRPDDPGIIFLTMRALLDRVEGLKRTMNVDISVSYLEIYNEKIRDLLVQDPLSMEKPKSLNICEDAEQNVSVPGLSYFTPTNLEEVMEIIIRGNSNRTMSPTEANAVSSRSHAVLQIYITQTPKSGEKQEESESQNSHKVRSVFSFIDLAGSERASATKNRGKRLVEGANINRSLLALGNCINSLCEPRRRQHVPYRDSKLTRLLKFSLGGNCRTCMIVCISPSSEHYDETHNTLKYGNRAKNIKTKVSRNVVSVDRHVSEYVRTIYELRQKVSILQKRIAEESKQLALNKEVRKISSREIKMLDARSMLKNSFDGSRDLQKSLIEHVRTLRRIEDEITLTKMWISIAKESDAMSGHNIKSVETRLAKLYDQRSLITAKVNPEEICKTFQNSISHIVSSFKGEGADMYADMLQDDVDLLKSIIENQILDAKHESETFSSTSRKLIQNLFLLFPLLPGNAIDVNESLARAFDQLVGIVPSEPTIQVPNLIEKGKAPLLSMFEIPRSPSRFKARSPSKAARVLKKPLKKRVRFSEVPTTSSVPPVEIKNKDSKPKVEKSLDKHNMNNDRSFLVPSRDARNSLTSLSLHSNVAKNKSSHSSKWPTHTLSPIITTALKQPVRRISLVSQPLQKTGGTENTPNA', 784, 'O59751; Q9UTZ7;', 'KD00677', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'klp6', '#Kinesin-like protein 6', '-', '-', '2539700'),
(678, 'Q64EV9', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25447, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAKAVDESTYEQRVRALYDKQIRMEAREAGVIKKISKFNSNLLDLKEAVVRHHQKVGKVRKVKMLRCGELEKRANFMEELTQELEATKQRNLVMRDQIKQLNVLARQHRNEVMESIHTLSKTTGTYLNHEALPARVKGVTVLRNDNSDQLIPFDLKATDVEGLESLCQHLQGFNIDAFQWRQLVSLATEMSMDSHTTPTTPPKEAAEGKSIIEIDLTSPTSHI', 223, 'Q64EV9;', 'KD00678', 'Drosophila lutescens (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '-'),
(679, 'O94640', 'NAD-dependent histone deacetylase sir2', 'k', 53442, 'Involved in silencing within the mating-type region; at the telomeres; and according to PubMed:12867036 also within centromeric DNA regions. Required for the localization of swi6 to the telomeres; silent mating type region; and according to PubMed:12867036 to the centromeric DNA regions. According to PubMed:15545655 not required for the localization of swi6 to centromeric foci. Deacetylates histone H3 on ''Lys-9'' and ''Lys-16'' of histone H4. This has a direct role in heterochromatin assembly. {ECO:0000269|PubMed:12867036; ECO:0000269|PubMed:15545655}.', 'MASNPLDNNMPTTPVEEKIPVASYSPSSSGSSSGASLLVDIMCGSKETEDEEVDSDEWDKPETENISDLDERSEMVRYLRASGYAKFLEKYLIEEELPVRSILKKLGINLPSALEEFEDIDLLPLLKEVLKREVARRIKLPHFNTFEDVVNLLKKAKNVVVLVGAGISTSLGILDFRSDNGFYARLARHGLSEPSEMFDIHTFRENPEIFYTFARDLLPETNHYSPSHAFIRLLEKKNKLSTLFTQNIDNLEKKTGLSDNKIIQCHGSFATATCIKCKHKVDGSELYEDIRNQRVSYCNECGKPPLKLRRVGQNKKEKHYFSDGDSESSEDDLAQPGIMKPDITFFGEALPDSFFNKVGSGELEETDLLICIGTSLKVAPVSELISVIPPTTPQIYISRTPVRHTQFDVNFLSPYCDWVIVEICKRAGWLNELQALCDLPECHSGSKTRAFETDLDIKFEEPSTYHITSTTNGSC', 475, 'O94640; Q6H8I3;', 'KD00679', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'sir2', '#NAD-dependent histone deacetylase sir2#3.5.1.-#Regulatory protein sir2#Silent information regulator 2', '-', '-', '3361342'),
(680, 'P25054', 'Adenomatous polyposis coli protein', 'GO:0000776===GO:0051988===c;k', 311646, 'Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. {ECO:0000269|PubMed:10947987; ECO:0000269|PubMed:17599059; ECO:0000269|PubMed:19151759; ECO:0000269|PubMed:19893577; ECO:0000269|PubMed:20937854}.', 'MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRIRQLLQSQATEAERSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKRHVDQPIDYSLKYATDIPSSQKQSFSFSKSSSGQSSKTEHMSSSSENTSTPSSNAKRQNQLHPSSAQSRSGQPQKAATCKVSSINQETIQTYCVEDTPICFSRCSSLSSLSSAEDEIGCNQTTQEADSANTLQIAEIKEKIGTRSAEDPVSEVPAVSQHPRTKSSRLQGSSLSSESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLMFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTAQTKREVPKNKAPTAEKRESGPKQAAVNAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPKESNENQEKEAEKTIDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKPAQTASKLPPPVARKPSQLPVYKLLPSQNRLQPQKHVSFTPGDDMPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGEGVRGGAQSGEFEKRDTIPTEGRSTDEAQGGKTSSVTIPELDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASASSSAPNKNQLDGKKKKPTSPVKPIPQNTEYRTRVRKNADSKNNLNAERVFSDNKDSKKQNLKNNSKVFNDKLPNNEDRVRGSFAFDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKAKENKESEAKVTSHTELTSNQQSANKTQAIAKQPINRGQPKPILQKQSTFPQSSKDIPDRGAATDEKLQNFAIENTPVCFSHNSSLSSLSDIDQENNNKENEPIKETEPPDSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKKPSRLKGDNEKHSPRNMGGILGEDLTLDLKDIQRPDSEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLETKKIESESKGIKGGKKVYKSLITGKVRSNSEISGQMKQPLQANMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGQTATTSPRGAKPSVKSELSPVARQTSQIGGSSKAPSRSGSRDSTPSRPAQQPLSRPIQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQMSQQNLTKQTGLSKNASSIPRSESASKGLNQMNNGNGANKKVELSRMSSTKSSGSESDRSERPVLVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPASPTRSQAQTPVLSPSLPDMSLSTHSSVQAGGWRKLPPNLSPTIEYNDGRPAKRHDIARSHSESPSRLPINRSGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSISGTKQSKENQVSAKGTWRKIKENEFSPTNSTSQTVSSGATNGAESKTLIYQMAPAVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKANPNIKDSKDNQAKQNVGNGSVPMRTVGLENRLNSFIQVDAPDQKGTEIKPGQNNPVPVSETNESSIVERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVNNNTKKRDSKTDSTESSGTQSPKRHSGSYLVTSV', 2843, 'P25054; D3DT03; Q15162; Q15163; Q93042;', 'KD00680', 'Homo sapiens (Human)', 'APC', '#Adenomatous polyposis coli protein#Protein APC#Deleted in polyposis 2.5', '-', 'ENSG00000134982', '-'),
(681, 'G5ECG0', '2P40TAC-1', 'c;k', 28543, '', 'MSLNTTFTKEDGTEVVIPFNGSQNGHPENEEPEVEEAAEPSSSVETLCGATRGDIIVMKHTTKALTELIERLLHSDEFEVRRCSNGQIISQGRCNGTTPGNGIGGGGASSEELEKALKDRDAARAEADKLHANYATLFASFNTVREAANDIRGEYEDARDKLKLAAAEVDEWQAKFLAVKDNANSELERASVEYDDLLRSHDENTKGLRLRVKRQEIELSSKNDEIKVLTNRVSELSQICDQLLNDVDVSDGMSVISTDA', 260, 'G5ECG0;', 'KD00681', 'Caenorhabditis elegans', 'tac-1', '#2P40 {ECO:0000313|EMBL:AAG49387.1}#TAC-1 {ECO:0000313|EMBL:CAA21677.1}', '-', '-', '175133'),
(682, 'Q3TRR0', 'Microtubule-associated protein 9', 'GO:0005818', 73511, 'Involved in organization of the bipolar mitotic spindle. Required for bipolar spindle assembly; mitosis progression and cytokinesis. May act by stabilizing interphase microtubules (By similarity). {ECO:0000250}.', 'MSDEIFSTTLAYTKSPKATKRTSFQDELIRAITARSARQRSSEYSDDFDSDEIVSLGEFSDTSTDESLVRKKMNDFHISDDEEKNSPRLSFLKTKKVNRAISNDALDSSTPGSEGSSPDAQEDVTGDSLPKSQNDDREVGREIITVKPTPRMHPVKRSTSSGETSSGLDADGHFKPSPQPRSMLKKSSHTEEGVRPGVDKEHSISEASAPTPSLPRQNGTELQTEEKIYSENLDLEDSLLQSLTSSSFKESPGGCTSPGSQEKVPIKDHDGEPTEIWDSLLSNENEGSSVLVNCVTPELEQPKDGQVAADDLEEEREKGGFTEDDLTTDPLLSTSPSVITPTEPAEPAKKANEDRNTKNKKTTNNRVSSASGRLMTSEFLKRSGPTKRSPSAATSSHYLGSLKVLDQKQPRKQSLEPDKADHIRAAVYQEWLEKKNVYLHEMHRIKRIESENLRIQNEQKKAAKREEALASFEAWKAMKEKEAKRIAAKKRLEEKNKKKTEEENAMRKGEALQAFEKWKEKKLEYLKEKTRREKEYERAKKQKEEEAVAEKKKDSLTAFEKWSERKEALLKQKEKEKINERRKEELKRAEKKDKDKQAISEYEKWLEKKERQERIERKQKKRHSFLESETHPPWSPPSRTAPSKVF', 646, 'Q3TRR0; Q3UUD1; Q3UX85; Q3UXE7; Q5M8N8; Q6P8K1; Q8BMM4; Q8BYP7;', 'KD00682', 'Mus musculus (Mouse)', 'Map9', '#Microtubule-associated protein 9#Aster-associated protein', '-', '-', '213582'),
(683, 'A2BGR3', 'DNA excision repair protein ERCC-6-like', 'GO:0000777', 163227, 'DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin (By similarity). {ECO:0000250}.', 'MESNNVEEVTDKFGGCLSLDTEKMGKYDRYRQKGKEAALNGELPRALELFQLAYQLQPSEKLKKRIQAIQDLIQREDEEDEEEEEEFVNVNNSGLKLYKGLYDKLYDHQKEGVAFLYSLYRDGRKGGILADDMGLGKTIQVISFLSGMYDAELANHTLLVMPTSLIKNWVREFAKWTPGMRVKEFHGSSKTERNRNLERIQRKGGVIITTYQMLINNYEQLGSNGHREFKWDYVILDEAHKIKTSSTKTAKSAHAIPAKNRVLLTGTPVQNNLREMWALFDFACQGSLLGTSKTFKTEYENPITRAREKDATPGEKALGLRISQNLTDIIKPYFLRRTKADVQQKKLKLEEGFEEEEDQENKCPNAREGVEMPSLTRKNDLIVWTYLSSVQEDIYNKFISLDQIKELLTTTRSPLAELTVLKKLCDHPRLLSQRAVIQLGLERGSDSELVHSDESESAVSQIDNISDHTLIEESGKLQFVVSLMECLREEGHRTLIFSQSRKMLDIMERVLRNRNFRLLRLDGTVTQLAEREKRISLFQTDKRYTIFLLTTQVGGVGITLTGANRVVIFDPSWNPATDAQAVDRAYRIGQTENVIIYRLITCGTVEEKIYRRQVFKDSLIRQTTGDKKNPFRYFSKQELRELFKLEDTRSSSTQQQLQAMHAQSRRSDTSLDHHIARLHSMEMFGISDHDLMFTKEPAADEDDPEDAESHHYIQTRVQKAQELMQAESELHGQLLDSMAQNTEPAWLRQMGQPNSSIRDRPAPPRIKNEPVTVDLTHNSFDEPEFEEDEQNLPSAEDAEMETASEDVEVIGDEDLGDKVISSEVEVVGEEVEVVAEEVEDAGEVEVVSEEVEGVGVEVEDVGVEVEDAGVEVEDAGVEVEDAGVEVEDAGEVEVVSGEGQVQPKSPQSGGEWNLQIVKTEVSPIAEKFADVITLDDTSDEADSSDFNTESKQQNSSQRFQSPSLQFPKLDDLSGASNTLGNEEVEPEKCHSQVLSSPLSQHEATTDEPFKAEMEMPHGNFNLLLEDSADMYFPEDEEVHEVEESAAEESPEFQLQMDVSGERLEEPSINHDKQNNGEFVNYNDSEVSKRESLLKIRSTPNESVDDSFVHSVRTKKRQVISDTEEEEEEEEESEKPCLTSSPFIDAISRLGSSTPKAVLVDGARLRRSLNASVASRRSFVVSLLENESDEESNEDKTKSSGASETCADELVEEVQTSSGDNSKSYETSEANGTLADELVEEEGEYREGKNTSDKVSESNETHSEEFAEEEKPSGDKSESYEISEASETHTDNSEEEIIGDHTGSYKISESSEADESVVEEEEPSGETLNTEESEMGEEEESAELIAGQEQEEWHSAVLESTGDVELDSNETMDQCAPKTVPVETHVLPVSSTNTAAEASDNKYNLLVLSGKQSLAEGRKQEALDFFLKAIDINTGDPEIQLLIIQLYRQLSQ', 1451, 'A2BGR3; A7E225;', 'KD00683', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'ercc6l', '#DNA excision repair protein ERCC-6-like#3.6.4.12#ATP-dependent helicase ERCC6-like', '-', '-', '100005291'),
(684, 'Q4R8E8', 'Spindle and kinetochore-associated protein 2', 'GO:0000940', 14068, '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}.', 'MEAEVDKLELMFQKAESDLDYIQYRLEYEIKTNHPDSASEKNPVTLLKELSALKSRYQTLYARFKPVAVEQKETKSRICATVNKTMNVIQKLQKQTDLELSPLTKEEKTAAEQFKSHMPDL', 121, 'Q4R8E8;', 'KD00684', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'SKA2', '#Spindle and kinetochore-associated protein 2#Protein FAM33A', '-', '-', '101865188'),
(685, 'Q19642', 'CZW-1', 'k', 87993, '', 'MASSEGSYRDLEKKLKNGLTSISQDIVDKYGNLKVSLNVNATAKLIFDRLENLEDIAEMSTRNLSNLIDQTAKDSPEMLAEIKSQAQSCENLVEFLQSMKNVEEQLIIMRSKTTNRVEWGTAILACKDFLNDTNMLLEGIGRDGFDMSVPLKHFAAEYSVLSYNCRYQLSADYERAMNVPKLSKQKCGDRTNVSFSVFNVGSVEDQKMLNETLSAMNMIGQLPERLDAWKIVILNVFCEAIVASRDGVDVYIVDNPTPDQTRFLINQKPRGKKDKTIDVAKVLESMEVFFTKLHSVLHSHELLDATGKTFTSMIGSVIEEQLITMILKDVIAIAAPVTETADEDQEMFINLLQIGEVFVERMKELGFFSQKAKLLFTLDTDTIFVTRRCFAIVSKANKLINETYDKLVTVGVDDSAIKDIDLLAKAHTHAEHFAKEYGKDLGRLWSHNEDSQFPSFFAFQKCTVSESTINFVNLLRDNVKAAFACEDEGARAKLALTAENIVRLYVILTPRKHAELFSSIPNMAAIFYNNCHYISHCIMTMSFEASGDNQKTLLEPLLLDSVIRLRTVAADCMEKTLTRCRREMTAYLEDHSIFEHLPASYKTTKNTFAAAEEMSESADILVPREEPKIIKCLAACLLHIRLIAKNLREPLTEVVYCKVIGSLVSFLLDSLVRHVVTTSDFRENDANVMADVFKRLLEVVANIVAYKEQTKVTDFCAREYFRLNEIVFVLGNRMQDIEHRWFNAKGPMAEHLSRSEVVGLIKALFADSQHRSDLIARL', 778, 'Q19642;', 'KD00685', 'Caenorhabditis elegans', 'czw-1', '#CZW-1 {ECO:0000313|EMBL:CCD67719.1}', '-', '-', '177587'),
(686, 'Q7KNS3', 'Lissencephaly-1 homolog', 'GO:0000776===GO:0000777===GO:0005828===GO:0051383===GO:0034501', 46460, '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 nuclear migration during cell division; mitotic spindle formation and the removal of mitotic checkpoint proteins from kinetochores at the metaphase to anaphase transition. Required for several aspects of neurogenesis including neuroblast proliferation; neuronal cell differentiation; dendritic growth; branching and maturation and axonal transport. Required for synchronized cell divisions in the germline; fusome integrity and oocyte differentiation. Acts together with BicD; Egl; dynein and microtubules to determine oocyte identity during oogenesis. Also required for nurse cell to oocyte transport during oocyte growth and for the positioning of the nucleus in the oocyte. {ECO:0000255|HAMAP-Rule:MF_03141; ECO:0000269|PubMed:10498683; ECO:0000269|PubMed:10559989; ECO:0000269|PubMed:10993674; ECO:0000269|PubMed:11056531; ECO:0000269|PubMed:16105886; ECO:0000269|PubMed:16107559}.', 'MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFALMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLSGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR', 411, 'Q7KNS3; A4UZJ3; O96698; Q5BI20; Q8SXJ6;', 'KD00686', 'Drosophila melanogaster (Fruit fly)', 'Lis-1', '#Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141}#DLis-1#Dlis1#Lissencephaly1', '-', '-', '36791'),
(687, 'Q9H3R5', 'Centromere protein H', 'GO:0000776===GO:0000777===GO:0043515===GO:0051382===GO:0051383===k', 28481, '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. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate. {ECO:0000269|PubMed:14536089; ECO:0000269|PubMed:16875666; ECO:0000269|PubMed:18007590}.', 'MEEQPQMQDADEPADSGGEGRAGGPPQVAGAQAACSEDRMTLLLRLRAQTKQQLLEYKSMVDASEEKTPEQIMQEKQIEAKIEDLENEIEEVKVAFEIKKLALDRMRLSTALKKNLEKISRQSSVLMDNMKHLLELNKLIMKSQQESWDLEEKLLDIRKKRLQLKQASESKLLEIQTEKNKQKIDLDSMENSERIKIIRQNLQMEIKITTVIQHVFQNLILGSKVNWAEDPALKEIVLQLEKNVDMM', 247, 'Q9H3R5; A8K3Y1;', 'KD00687', 'Homo sapiens (Human)', 'CENPH', '#Centromere protein H#CENP-H#Interphase centromere complex protein 35', '-', 'ENSG00000153044', '-'),
(688, 'P24860', 'G2/mitotic-specific cyclin-B1', 'GO:0000942===GO:0051987', 48052, 'Essential for the control of the cell cycle at the G2/M (mitosis) transition.', 'MALRVTRNTKINAENKAKVSMAGAKRVPVTVTAASKPGLRPRTALGDIGNKVSEELQARVPLKREAKTLGTGKGTVKALPKPVEKVPVCEPEVELAEPEPEPELEHVREEKLSPEPILVDNPSPSPMETSGCAPAEEYLCQAFSDVILAVSDVDADDGADPNLCSEYVKDIYAYLRQLEEEQSVRPKYLQGREVTGNMRAILIDWLIQVQMKFRLLQETMYMTVSIIDRFMQNSCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTNNTYTKHQIRQMEMKILRVLNFSLGRPLPLHFLRRASKVGEVDVEQHTLAKYLMELSMLDYDMVHFAPSQIAAGAFCLALKILDNGEWTPTLQHYLSYSEDSLLPVMQHLAKNVVMVNCGLTKHMTVKNKYAASKHAKISTLAQLNCTLVQNLSKAVTKA', 430, 'P24860;', 'KD00688', 'Mus musculus (Mouse)', 'Ccnb1', '#G2/mitotic-specific cyclin-B1', '-', '-', '268697'),
(689, 'P46870', 'Kinesin-like protein KLP1', 'GO:0003777', 83020, 'May play a role in rotation or twisting of the central pair microtubules of the flagella axoneme.', 'MVKQAVKVFVRTRPTATSGSGLKLGPDGQSVSVNVPKDLSAGPVNNQQEQFSFKFDGVLENVSQEAAYTTLAHEVVDSLMAGYHGTIFAYGQTGAGKTFTMSGGGTAYAHRGLIPRAIHHVFREVDMRADKMYRVHVSYLEIYNEQLYDLLGDTPGTSDALAVLEDSNSNTYVRGLTLVPVRSEEEALAQFFLGEQGRTTAGHVLNAESSRSHTVFTIHVEMRTSDAASERAVLSKLNLVDLAGSERTKKTGVTGQTLKEAQFINRSLSFLEQTVNALSRKDTYVPFRQTKLTAVLRDALGGNCKTVMVANIWAEPSHNEETLSTLRFASRVRTLTTDLALNESNDPALLLRRYERQIKELKAELAMRDTLSGKGRVSYDDLTDDELRELHATCRRFLHGEAEPEDLPADSMKRVRETFKALRAVHVAIKADMATQMATLRRATEEGSGAAARGGDSAGPSGVGDVDLRATGGFTVGHAPLDARPPVRSELGSPGAGASGAEALGEPRSPGGGLHAQASSHTDAGSNWGDAGPLSSPGGTRLAGIFGVSGDRNAVFRRYKVDVGEGRELAASLKAASIALADTKASIRSLGASVNDAKQRIDELSSALALRRGATPAGGDGEVLDSEAYALMQELKSAKSRYRTDFDSLKSAREELEPQIQAVAVARAGLLEAFDRWAAAQSDTTLKRMATAGRAMSGIAPGEEDEMDAGEQFERMQIARISERDPDSLAFHTALKRTGAAVSRPATVATGGNAKAAAMATRKMEHTQAVNRGLAR', 776, 'P46870;', 'KD00689', 'Chlamydomonas reinhardtii (Chlamydomonas smithii)', 'KLP1', '#Kinesin-like protein KLP1', '-', '-', '-'),
(690, 'O59767', 'Mitotic spindle checkpoint component mad3', 'GO:0000778===SCL===k', 36086, 'Has a role in transducing the anaphase inhibitory signal to the anaphase promoting complex (APC). Forms part of the mad2 feedback control. {ECO:0000269|PubMed:11909965}.', 'MEPLDAGKNWVHMDVIEQSKENIEPRKAGHSASALAKSSSRNHTEKEVAGLQKERMGHERKIETSESLDDPLQVWIDYIKWTLDNFPQGETKTSGLVTLLERCTREFVRNPLYKDDVRYLRIWMQYVNYIDEPVELFSFLAHHHIGQESSIFYEEYANYFESRGLFQKADEVYQKGKRMKAKPFLRFQQKYQQFTHRWLEFAPQSFSSNTNSVNPLQTTFESTNIQEISQSRTKISKPKFKFSVYSDADGSGKDGQPGTWQTLGTVDQRRKENNISATSWVGEKLPLKSPRKLDPLGKFQVHCDEEVSKE', 310, 'O59767;', 'KD00690', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mad3', '#Mitotic spindle checkpoint component mad3', '-', '-', '2539219'),
(691, 'Q9H0H5', 'Rac GTPase-activating protein 1', 'GO:0051988', 71027, '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. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269|PubMed:10979956; ECO:0000269|PubMed:11085985; ECO:0000269|PubMed:11278976; ECO:0000269|PubMed:11782313; ECO:0000269|PubMed:14729465; ECO:0000269|PubMed:15642749; ECO:0000269|PubMed:16103226; ECO:0000269|PubMed:16129829; ECO:0000269|PubMed:16236794; ECO:0000269|PubMed:19468300; ECO:0000269|PubMed:19468302; ECO:0000269|PubMed:23235882; ECO:0000269|PubMed:9497316}.', 'MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEEQKSALAFLNRGQPSSSNAGNKRLSTIDESGSILSDISFDKTDESLDWDSSLVKTFKLKKREKRRSTSRQFVDGPPGPVKKTRSIGSAVDQGNESIVAKTTVTVPNDGGPIEAVSTIETVPYWTRSRRKTGTLQPWNSDSTLNSRQLEPRTETDSVGTPQSNGGMRLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPTLIGTPVKIGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHTKMDVANLAKVFGPTIVAHAVPNPDPVTMLQDIKRQPKVVERLLSLPLEYWSQFMMVEQENIDPLHVIENSNAFSTPQTPDIKVSLLGPVTTPEHQLLKTPSSSSLSQRVRSTLTKNTPRFGSKSKSATNLGRQGNFFASPMLK', 632, 'Q9H0H5; Q6PJ26; Q9NWN2; Q9P250; Q9P2W2;', 'KD00691', 'Homo sapiens (Human)', 'RACGAP1', '#Rac GTPase-activating protein 1#Male germ cell RacGap#MgcRacGAP#Protein CYK4 homolog#CYK4#HsCYK-4', '-', 'ENSG00000161800', '-'),
(692, 'P46863', 'Bipolar kinesin KRP-130', 'GO:0003777===k', 121163, 'Important role in mitotic dividing cells. Microtubule motor required for spindle body separation. Slow plus-end directed microtubule motor capable of cross-linking and sliding apart antiparallel microtubules; thereby pushing apart the associated spindle poles during spindle assembly and function.', 'MDISGGNTSRQPQKKSNQNIQVYVRVRPLNSRERCIRSAEVVDVVGPREVVTRHTLDSKLTKKFTFDRSFGPESKQCDVYSVVVSPLIEEVLNGYNCTVFAYGQTGTGKTHTMVGNETAELKSSWEDDSDIGIIPRALSHLFDELRMMEVEYTMRISYLELYNEELCDLLSTDDTTKIRIFDDSTKKGSVIIQGLEEIPVHSKDDVYKLLEKGKERRKTATTLMNAQSSRSHTVFSIVVHIRENGIEGEDMLKIGKLNLVDLAGSENVSKAGNEKGIRVRETVNINQSLLTLGRVITALVDRAPHVPYRESKLTRLLQESLGGRTKTSIIATISPGHKDIEETLSTLEYAHRAKNIQNKPEVNQKLTKKTVLKEYTEEIDKLKRDLMAARDKNGIYLAEETYGEITLKLESQNRELNEKMLLLKALKDELQNKEKIFSEVSMSLVEKTQELKKTEENLLNTKGTLLLTKKVLTKTKRRYKEKKELVASHMKTEQVLTTQAQEILAAADLATDDTHQLHGTIERRRELDEKIRRSCDQFKDRMQDNLEMIGGSLNLYQDQQAALKEQLSQEMVNSSYVSQRLALNSSKSIEMLKEMCAQSLQDQTNLHNKLIGEVMKISDQHSQAFVAKLMEQMQQQQLLMSKEIQTNLQVIEENNQRHKAMLDSMQEKFATIIDSSLQSVEEHAKQMHKKLEQLGAMSLPDAEELQNLQEELANERALAQQEDALLESMMMQMEQIKNLRSKNSISMSVHLNKMEESRLTRNHRIDDIKSGIQDYQKLGIEASQSAQAELTSQMEAGMLCLDQGVANCSMLQVHMKNLNQKYEKETNENVGSVRVHHNQVEIICQESKQQLEAVQEKTEVNLEQMVDARQQLITEDRQRFIGHATVATDLVQESNRQFSEHAEHQRQQLQICEQELVRFQQSELKTYAPTGTTPSKRDFVYPRTLVATSPHQEIVRRYRQELDWSDLDTTATIDECSEGEHDVSMHSVQELSETETIMNSTPIEPVDGVTVKRGCGTTRNSNSNALKPPVATGGKRSSSLSRSLTPSKTSPRGSPAFVRHNKENVA', 1066, 'P46863; Q8T0A6; Q9W0I8;', 'KD00692', 'Drosophila melanogaster (Fruit fly)', 'Klp61F', '#Bipolar kinesin KRP-130#Kinesin-like protein Klp61F', '-', '-', '38135'),
(693, 'Q50HP3', 'DASH complex subunit spc19', 'GO:0042729===GO:0031134', 17494, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. May be necessary for growth under high osmotic stress. {ECO:0000269|PubMed:16079914}.', 'MSYLDGLQQCVDSLQISIGTLSSSIDTLESGIHDFPRIKHILKVQRHFNLISEDELSARQAKFEEIVKPILSKAFQRLEDSISSLQRQEDSLKTKYELQEARLDMLKNRPATSAFSVTTESSEQLKAIIAKRQKLVYTLERYTLQLQQKRGH', 152, 'Q50HP3;', 'KD00693', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'spc19', '#DASH complex subunit spc19#Outer kinetochore protein spc19', '-', '-', '5802726'),
(694, 'P46865', 'Kinesin-like protein K39', 'GO:0003777', 106168, '', 'MHPSTVRREAERVKVSVRVRPLNERENNAPEGTKVTVAAKQAAAVVTVKVLGGSNNSGAAESMGTARRVAQDFQFDHVFWSVETPDACGATPATQADVFRTIGYPLVQHAFDGFNSCLFAYGQTGSGKTYTMMGADVSALSGEGNGVTPRICLEIFARKASVEAQGHSRWIVELGYVEVYNERVSDLLGKRKKGVKGGGEEVYVDVREHPSRGVFLEGQRLVEVGSLDDVVRLIEIGNGVRHTASTKMNDRSSRSHAIIMLLLREERTMTTKSGETIRTAGKSSRMNLVDLAGSERVAQSQVEGQQFKEATHINLSLTTLGRVIDVLADMATKGAKAQYSVAPFRDSKLTFILKDSLGGNSKTFMIATVSPSALNYEETLSTLRYASRARDIVNVAQVNEDPRARRIRELEEQMEDMRQAMAGGDPAYVSELKKKLALLESEAQKRAADLQALEREREHNQVQERLLRATEAEKSELESRAAALQEEMTATRRQADKMQALNLRLKEEQARKERELLKEMAKKDAALSKVRRRKDAEIASEREKLESTVAQLEREQREREVALDALQTHQRKLQEALESSERTAAERDQLLQQLTELQSERTQLSQVVTDRERLTRDLQRIQYEYGETELARDVALCAAQEMEARYHAAVFHLQTLLELATEWEDALRERALAERDEAAAAELDAAASTSQNARESACERLTSLEQQLRESEERAAELASQLEATAAAKSSAEQDRENTRATLEQQLRESEARAAELASQLEATAAAKMSAEQDRENTRATLEQQLRDSEERAAELASQLESTTAAKMSAEQDRESTRATLEQQLRDSEERAAELASQLESTTAAKMSAEQDRESTRATLEQQLRESEERAAELASQLESTTAAKMSAEQDRESTRATLEQQLRDSEERAAELASQLEATAAAKSSAEQDRENTRAALEQQLRDSEERAAELASQ', 955, 'P46865;', 'KD00694', 'Leishmania chagasi', 'KIN', '#Kinesin-like protein K39', '-', '-', '-'),
(695, 'P46867', 'Kinesin-like protein Klp68D', 'GO:0003777', 88207, 'Plus-end directed microtubule motor that may be used for anterograde axonal transport and could conceivably move cargos in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors. {ECO:0000269|PubMed:7525600}.', 'MSAKSRRPGTGSSQTPNECVQVVVRCRPMSNRERSERSPEVVNVYPNRGVVELQNVVDGNKEQRKVFTYDAAYDASATQTTLYHEVVFPLVSSVLEGFNGCIFAYGQTGTGKTFTMEGVRGNDELMGIIPRTFEQIWLHINRTENFQFLVDVSYLEIYMEELRDLLKPNSKHLEVRERGSGVYVPNLHAINCKSVEDMIKVMQVGNKNRTVGFTNMNEHSSRSHAIFMIKIEMCDTETNTIKVGKLNLIDLAGSERQSKTGASAERLKEASKINLALSSLGNVISALAESSPHVPYRDSKLTRLLQDSLGGNSKTIMIANIGPSNYNYNETLTTLRYASRAKSIQNQPIKNEDPQDAKLKEYQEEIERLKRLIGPQQQQRSEKQVTAKKQRVKKPKKETVTKEMSDSLQVSTIEQPVEDDSDPEGAESESDKENEAEVAKSNEELERERVENSKLAAKLAELEGQLVRGGKNLLDTYSERQIELEKKLVEIAERKKREIEIQQQLELQEETTLEIRERNVSLEQEVELKKRKLSKCYAKYLALQQELNDCKSDHNQDLRELEMAQNELVKELKRQLLIIDNFVPIEVKQRLYTQAKYDEEQEEWKFSSMSLPTPPGGDGKFSSKRPVSHPQRRRPTSEYALQEAKSNSPSSLRFKSENIVNYELEMPCRTTQEYRTPKVSASLQAVLAQAMQTGGDDIDIVDSHTNSLRSRLENIINANANGGAGPGAGVAVGSSIPNVRNIKSSRGLPSAASNLDSNRRPPTGRLPAKKPASAYPKARGLVNK', 784, 'P46867; Q961H5; Q9VTN8;', 'KD00695', 'Drosophila melanogaster (Fruit fly)', 'Klp68D', '#Kinesin-like protein Klp68D', '-', '-', '39332'),
(696, 'P46869', 'Kinesin-like protein FLA10', 'GO:0003777', 86672, 'Probably involved in flagellar assembly and maintenance. May play a role in flagellar synthesis.', 'MPPAGGGSESVKVVVRCRPLNGKEKADGRSRIVDMDVDAGQVKVRNPKADASEPPKAFTFDQVYDWNCQQRDVFDITARPLIDSCIEGYNGTIFAYGQTGTGKSHTMEGKDEPPELRGLIPNTFRYVFEIIARDSGTKEFLVRSSYLEIYNEEVRDLLGKDHSKKMELKESPDRGVYVKDLSQFVCKNYEEMNKVLLAGKDNRQVGATLMNQDSSRSHSIFTITIECIEKLESAAAQKPGAKKDDSNHVRVGKLNLVDLAGSERQDKTGATGDRLKEGIKINLSLTALGNVISALVDGKSGHIPYRDSKLTRLLQDSLGGNTKTVMVANIGPADWNYDETMSTLRYANRAKNIQNKPKINEDPKDAMLRQFQEEIKKLKEQLAARAAGGGGPITMPSGGGSPTQKIVERTEEVDPDIDAIKAQMRAELEAKMKSDISTEALDKAREEAEAAAKKQLQAIIDDQGKTEAQKKAARDALKKQAEEARAIAGAIEKEKQEKAVLESRIKEMEGKIVVGGVNMLEKVDELKQKSEDIKREAAIRKRQEEEAKRRLEELQAAQVDADAKFASLDEEINVKSRQLKKLFEKYQGKKGELADLQEQFQREREGMLEDYRILTQQIKLKNLIIACFIPPDYQDKIMQHCHWQDYDSSWNIDCIAYAGNAVRTNQELQAQEDKEHDAAAENERLKNCFFSYEQFEAAGAGSKQGGGGGGGGGGAARPGSSAGRAVGSAARRTGGKAGGKDITDIGSLRDSVNWGDDDDKKKGAIPKAKGLVKDTVDPRLRASKLK', 786, 'P46869;', 'KD00696', 'Chlamydomonas reinhardtii (Chlamydomonas smithii)', 'FLA10', '#Kinesin-like protein FLA10#Protein KHP1', '-', '-', '5727085'),
(697, 'Q9NSP4', 'Centromere protein M', 'GO:0000777===k', 19737, '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. {ECO:0000269|PubMed:16716197}.', 'MSVLRPLDKLPGLNTATILLVGTEDALLQQLADSMLKEDCASELKVHLAKSLPLPSSVNRPRIDLIVFVVNLHSKYSLQNTEESLRHVDASFFLGKVCFLATGAGRESHCSIHRHTVVKLAHTYQSPLLYCDLEVEGFRATMAQRLVRVLQICAGHVPGVSALNLLSLLRSSEGPSLEDL', 180, 'Q9NSP4; A7LM22; B1AHQ9; Q6I9W3;', 'KD00697', 'Homo sapiens (Human)', 'CENPM', '#Centromere protein M#CENP-M#Interphase centromere complex protein 39#Proliferation-associated nuclear element protein 1', '-', 'ENSG00000100162', '-'),
(698, 'B4K8J8', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 23968, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MRKRLMAMLQNDISLQQQENALAKQSAKFHSKIAAKHQLIKRQQRKLEKLNQVANERKEDQENRSAFEQSMRDKLLREQQNLSEMQTELATKKQRRDELMGFVRTMSEATNTYINLKALPARVKGVALRPEQGEWIPFNCDAYDLKGLNALWSRLNEPSASTDKWQQLFSAEPTAKEKENANASLSSIIEIDLTSPTAHRSLAKMLEK', 208, 'B4K8J8;', 'KD00698', 'Drosophila mojavensis (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6572830'),
(699, 'Q9GZR1', 'Sentrin-specific protease 6', 'GO:0090234', 126146, 'Protease that deconjugates SUMO1; SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly- SUMO3 chains; but does not efficiently process SUMO1; SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA; leading to transcriptional activation. Involved in chromosome alignment and spindle assembly; by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI; protecting them from degradation by the ubiquitin ligase RNF4; which targets polysumoylated proteins for proteasomal degradation. Desumoylates also RPA1; thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. {ECO:0000269|PubMed:16912044; ECO:0000269|PubMed:17000875; ECO:0000269|PubMed:18799455; ECO:0000269|PubMed:20212317; ECO:0000269|PubMed:20705237; ECO:0000269|PubMed:21148299}.', 'MAAGKSGGSAGEITFLEALARSESKRDGGFKNNWSFDHEEESEGDTDKDGTNLLSVDEDEDSETSKGKKLNRRSEIVANSSGEFILKTYVRRNKSESFKTLKGNPIGLNMLSNNKKLSENTQNTSLCSGTVVHGRRFHHAHAQIPVVKTAAQSSLDRKERKEYPPHVQKVEINPVRLSRLQGVERIMKKTEESESQVEPEIKRKVQQKRHCSTYQPTPPLSPASKKCLTHLEDLQRNCRQAITLNESTGPLLRTSIHQNSGGQKSQNTGLTTKKFYGNNVEKVPIDIIVNCDDSKHTYLQTNGKVILPGAKIPKITNLKERKTSLSDLNDPIILSSDDDDDNDRTNRRESISPQPADSACSSPAPSTGKVEAALNENTCRAERELRSIPEDSELNTVTLPRKARMKDQFGNSIINTPLKRRKVFSQEPPDALALSCQSSFDSVILNCRSIRVGTLFRLLIEPVIFCLDFIKIQLDEPDHDPVEIILNTSDLTKCEWCNVRKLPVVFLQAIPAVYQKLSIQLQMNKEDKVWNDCKGVNKLTNLEEQYIILIFQNGLDPPANMVFESIINEIGIKNNISNFFAKIPFEEANGRLVACTRTYEESIKGSCGQKENKIKTVSFESKIQLRSKQEFQFFDEEEETGENHTIFIGPVEKLIVYPPPPAKGGISVTNEDLHCLNEGEFLNDVIIDFYLKYLVLEKLKKEDADRIHIFSSFFYKRLNQRERRNHETTNLSIQQKRHGRVKTWTRHVDIFEKDFIFVPLNEAAHWFLAVVCFPGLEKPKYEPNPHYHENAVIQKCSTVEDSCISSSASEMESCSQNSSAKPVIKKMLNKKHCIAVIDSNPGQEESDPRYKRNICSVKYSVKKINHTASENEEFNKGESTSQKVADRTKSENGLQNESLSSTHHTDGLSKIRLNYSDESPEAGKMLEDELVDFSEDQDNQDDSSDDGFLADDNCSSEIGQWHLKPTICKQPCILLMDSLRGPSRSNVVKILREYLEVEWEVKKGSKRSFSKDVMKGSNPKVPQQNNFSDCGVYVLQYVESFFENPILSFELPMNLANWFPPPRMRTKREEIRNIILKLQEDQSKEKRKHKDTYSTEAPLGEGTEQYVNSISD', 1112, 'Q9GZR1; A6NNY9; O94891; Q5VUL3; Q5VUL4; Q8TBY4; Q9UJV5;', 'KD00699', 'Homo sapiens (Human)', 'SENP6', '#Sentrin-specific protease 6#3.4.22.68#SUMO-1-specific protease 1#Sentrin/SUMO-specific protease SENP6', '-', 'ENSG00000112701', '-'),
(700, 'Q9VPB2', 'Spc105-related; isoform A', 'k', 223105, '', 'MVDLLFLQLRKVPTKEDEATTTTSAIKQQIKRRISFSGKKSVREFVNTKETNNWDDSYEVSEHHAEDSSGSKCCSTGSASVARVSEHADKENIPLPSHCEREHVDLSVNLQASVDFTLLPCEMMDKSRKTSSISAVSFCMTSEERKLLQSSLSDRQLVDKTMDLISGSLVNRHQIASSVCEESSIKVATNKLEKVVFTPAVKAVSDSFMDITPLGFTDPNPAAPAPAPVATLYPPTQQSLMELEEDSIVREMRESTKNQTKTPAQKSLFMDVGETKNKTQQGAGGASFSLNVSNNRDRSPSNSFESLNSTMNFTRDESMLIPFDMISGKNISKKLNFRQLNEDLETGKIQIFPNGPKTPTTDRKAKKNRFWCGLEEESAGDNSPKKDIRSIVPRGMLNFSENMTLTPTKTSPVGKNKEKLKAADEKQKYRLSQADEMMLDNTNFLAHARLGDETQSRNTSKNSTRRETTCETSELNLEYPTLSQDFQPIPSSKTRKTDFMAEEMQLSQTNYPAIPALKTATSRRTLHLNESMDHETTKSTYVRKEISVTTQETIYEKSTTNEQNSNQNRNTWACTKTKRRATLLMQESMEEDIISPLKNLQLKPNAAPMNTGQSKVNHTLYLAEPLEEVDINQSNMLPTKNVAPREQLKARKTLLLEEPMEEEMSSNIGYNSKRKTLHLAEPLVVEGEDFILEKHIPIKVVAHQENKSKGRQTLLFEEPVEEEIFHNAKDLPECALKGNKTGPQKYSQLNQGKSFTSQSRSKARQTLLIEEPMEEDTEFNNKYNIAKPGENHIRKIAKSRQTLLLSEPLEEEMCLPPPKNKSIVSQKTIDKSTEQQRSKSRHTLLLSEPIEEEHIQQDLPAEKEDSLARQQRFKPRQTLIMAEPIEEDVGETERRVQTNITGSSTSRPRHTLLMSEPIEEELTNEDKSTNASTNRTLRSRRTILMAEPIEEEGNKSIAEKIGQFTKESSEEAVFQTSKSRQTLLMAEPIEEDVFNQSNDQPKPLPISKDKITRKTSRRHTLITAEPIEEDLSVRKPLENSKESSLTARIIQSFAEPIENALFSITDQIAKQQFSESVQTPPKEPLNYLHQKPRNTLISHETIQEDLEPVNENSSVGPLRSRYRKTLIMAEPIEEDVNNHNMTKQNGICDSLNVPQSGGYMAAKTRQSVHIPVPIEEDHIPGQQQRESEPAVKGRTTLLTESIEEDVPAQHTRISKNKSMGSKVSAEPIIEDLDSNRPEISQSVEETLPQRSQVPDVPSSRRHTLLLSEPMEEDEGIFGHNYPIRTKHQISEKLEKPEGPIHSSKNSVENEEIGTPPSAKTQQSIAMSESMDFQSPQFRPRGPDFNAITPGMSLTEFVDQEEMCKTPIHKRVLLTSHRKKLSMYQPVPIDLEANASGFGTPKNLVQLKRLPTHLTPNLPESKKRNTHLFPNSNMDIELEEDQEGSWGTKSIQMHTGTSKSRRTYTVDQLDASVQPVRDYNPVVTEMNKQGGLNMLELPRKSTYNMDLEEKPITISDVNNYFHEQKEQQRQSSERESGSSNDRTFKSYAATISKFINLTGNTTIFAAAEDLGGEGKDQPHQIDNEHLSLVSTLAEETDDDGDEKEEEEEQKQKQHLLQPEICEAQLNSMVKAGSEGSCKKCRNCNHTLSETRLSSESFVLPPRKLWDFSRLQQRLRNIRQRPSWKEVNTYWEIEEEARLSRNQDSDDSMEQTRVEEEATKWNKAALLEMCKLRTEEKDIAMPPESFFTRLKRLLTEQQPNWIFDYQRKVSQQMIFYNRQLTTIRIVVNYQIEDLVEESTISVCSIQLDNDVPTPKDQWSSREHFLNFHLSLRLPMNPSDEIEGSDETAFLKFLNGIDRRIAEVKQKLHKVLDLLAQKRARLTREANRTIVRKIVRKCIDQEPIVRLEKITFLIEIGNIEDVSFTDILRPELHLFNENIQYLPKGIPFLEAFLTDPEQYLRK', 1959, 'Q9VPB2;', 'KD00700', 'Drosophila melanogaster (Fruit fly)', 'Spc105R', '#Spc105-related; isoform A {ECO:0000313|EMBL:AAF51643.2}', '-', '-', '40300'),
(701, 'P14699', 'Membrane antigen containing repeating peptides', 'GO:0003777', 23706, '', 'QETSAKLADTEETLQETSAKLADTEETLQETSAKLADTEETLQETSAKLADTEETLSAEIASLAEQHGVAQTLCEQQGAYMNQLLTYVRAAYNVTLDGMTEVQATAVADILRQCDYALRSVAQAASDEVEHVKEMYNMVDGNYKETAARFDILRRILGKIDQDVKEASVEIDAPERRQTCSLHPTPRRLGDVSNRENSIENKTRSASRLSGRLF', 214, 'P14699;', 'KD00701', 'Leishmania major', '', '#Membrane antigen containing repeating peptides#Clone 20', '-', '-', '-'),
(702, 'P97329', 'Kinesin-like protein KIF20A', 'GO:0003777', 99876, 'Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1; involved in recruitment of PLK1 to the central spindle (By similarity). Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. {ECO:0000250; ECO:0000269|PubMed:9438855}.', 'MSHRILSPPAGLLSDEDVVDSPILESTAADLRSVVRKDLLSDCSVISASLEDKQALLEDTSEKVKVYLRIRPFLTSELDRQEDQGCVCIENTETLVLQAPKDSFALKSNERGVGQATHKFTFSQIFGPEVGQVAFFNLTMKEMVKDVLKGQNWLIYTYGVTNSGKTYTIQGTSKDAGILPQSLALIFNSLQGQLHPTPDLKPLLSNEVIWLDSKQIRQEEMKKLSLLIGGLQEEELSTSVKKRVHTESRIGASNSFDSGVAGLSSTSQFTSSSQLDETSQLWAQPDTVPVSVPADIRFSVWISFFEIYNELLYDLLEPPSHQHKRQTLRLCEDQNGNPYVKDLNWIHVRDVEEAWKLLKVGRKNQSFASTHMNQQSSRSHSIFSIRILHLQGEGDIVPKISELSLCDLAGSERCKHQKSGERLKEAGNINTSLHTLGRCIAALRQNQQNRSKQNLIPFRDSKLTRVFQGFFTGRGRSCMIVNVNPCASTYDETLHAAKFSALASQLVHAPPVHLGIPSLHSFIKKHSPQVGPGLEKEDKADSDLEDSPEDEADVSVYGKEELLQVVEAMKALLLKERQEKLQLEIQLREEICNEMVEQMQQREQWCSERLDNQKELMEELYEEKLKILKESLTTFYQEQIQERDEKIEELETLLQEAKQQPAAQQSGGLSLLRRSQRLAASASTQQFQEVKAELEQCKTELSSTTAELHKYQQVLKPPPPAKPFTIDVDKKLEEGQKNIRLLRTELQKLGQSLQSAERACCHSTGAGKLRQALTNCDDILIKQNQTLAELQNNMVLVKLDLQKKAACIAEQYHTVLKLQGQASAKKRLGANQENQQPNHQPPGKKPFLRNLLPRTPTCQSSTDSSPYARILRSRHSPLLKSPFGKKY', 887, 'P97329; Q542M4;', 'KD00702', 'Mus musculus (Mouse)', 'Kif20a', '#Kinesin-like protein KIF20A#Kinesin-like protein 174#Rab6-interacting kinesin-like protein#Rabkinesin-6', '-', '-', '19348'),
(703, 'Q9WV60', 'Glycogen synthase kinase-3 beta', 'c;k', 46710, 'Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis; Wnt signaling and regulation of transcription factors and microtubules; by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2); EIF2B; CTNNB1/beta-catenin; APC; AXIN1; DPYSL2/CRMP2; JUN; NFATC1/NFATC; MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle; contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling; GSK3B forms a multimeric complex with APC; AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain; thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export; shutting off NFATC1/NFATC gene regulation; and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on ''Thr-548''; decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1; inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF- kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regulates replication in pancreatic beta-cells; resulting in apoptosis; loss of beta-cells. Through phosphorylation of the anti-apoptotic protein MCL1; may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells; decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2; leading to inhibit its activity. Phosphorylates SIK1 at ''Thr-182''; leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SFPQ at ''Thr-679'' upon T-cell activation. Phosphorylates SNAI1; leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates NR1D1 st ''Ser-55'' and ''Ser-59'' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1; CLOCK and PER2. Phosphorylates CLOCK AT ''Ser-427'' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at ''Ser-17'' and ''Ser-21'' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at ''Ser-3'' or ''Ser-4'' which positively regulates its activity. {ECO:0000269|PubMed:10894547; ECO:0000269|PubMed:15791206; ECO:0000269|PubMed:16543145; ECO:0000269|PubMed:17391670; ECO:0000269|PubMed:18288891; ECO:0000269|PubMed:20049328; ECO:0000269|PubMed:20123978; ECO:0000269|PubMed:21295697; ECO:0000269|PubMed:22057101; ECO:0000269|PubMed:23395175}.', 'MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASPPANATAASDTNAGDRGQTNNAASASASNST', 420, 'Q9WV60;', 'KD00703', 'Mus musculus (Mouse)', 'Gsk3b', '#Glycogen synthase kinase-3 beta#GSK-3 beta#2.7.11.26#Serine/threonine-protein kinase GSK3B#2.7.11.1', '-', '-', '56637'),
(704, 'Q9WV63', 'Kinesin-like protein KIF2A', 'GO:0003777', 79792, '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}.', 'MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEDIEPSPEIPPPSSSSKVNKIVKNRRTVASIKNDPPPRDNRVVGSARARPSQLPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDCSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTVDPTAAGDVRPIMHHPPSQIDDLETQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWIEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL', 705, 'Q9WV63; Q5BJW1;', 'KD00704', 'Rattus norvegicus (Rat)', 'Kif2a', '#Kinesin-like protein KIF2A#Kinesin-2', '-', '-', '-'),
(705, 'Q6FV07', 'Spindle assembly checkpoint kinase', 'GO:0000777', 40992, '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}.', 'MENKATLARNIGEKRVSPRSKVNGTGKSWRISYSPQRMDGVSSGRNVSKIPSPVRERLFLKNQERKPLGVSPLSNLSPNSLGRNSLEKSTYNNKLSLKDFEVGRKLGKGKFGKVYCVRHKKSGFICALKAIEKNEILQFNLLKQLKREVDIQLGMDHPNIIKLYAHFHDEKRVYLLMEHSINGELYKSLKNNGPFNDVLASHYIYQIADALHYMHKKRIIHRDVKPENVLIGFDNVVKLADFGWSILNPEGSKRKTLCGTIDYLSPEMITPREYDEQVDVWALGVLAYELVVGVPPFEENSKELTYKRILKCDLNFPESISKDAKDLISKLLVTDTTQRLSLTGVKTHPWILKNKPFW', 358, 'Q6FV07;', 'KD00705', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'IPL1', '#Spindle assembly checkpoint kinase#2.7.11.1#Aurora kinase', '-', '-', '2887534'),
(706, 'Q9V877', 'Kinesin-like protein subito', 'GO:0003777', 71387, 'Required during female meiosis for bipolar spindle formation in the absence of the centrosomes and chromosome homolog segregation. Also has roles in male meiosis and mitotic divisions of the early embryo. {ECO:0000269|PubMed:11973304}.', 'MDSKEVSEVPRREVRSFLMARDPSIDRRFRPRPNKKMRLFDNIQESEEESFSEYSDTESEYKYQSSEATEGASCATSAADSSNVETGPQVFLRLRPVKDASKAYIVSEEANVLITSCKVDSTSNNVNRMEKHFGFTSIFDSTVGQRDIYDTCVGPKIMEEECVTIMTYGTSGSGKTYTLLGDDVRAGIIPRALENIFTIYQDTVFRSPKLKLINGSIVFLQDDASLKELQIRKKLLDLCPDISAHHQRLKQVIDGDHMFETKASTDVSVLVWVSFVEIYNELVYDLLAIPPKQDKLGEVPRKNLKIVGNKGHVFIKGLTSVFVTSSEEALRLLRLGQQRSTYASTSVNANSSRSHCVFTVDILKYNRSGITTQSSYKFCDLAGSERVNNTGTSGLRLKEAKNINTSLMVLGRCLDAASTVQKKKNADIIPYRDSKLTMLLQAALLGKEKLAMIVTVTPLDKYYEENLNVLNFASIAKNIIFKEPVIKQHRVSYCGFMEFSKMSTCEGGDYTKELEDENVRLQLEIEQLKYDHVLQMQLLEEKLRRELTATYQEIIQNNKKQYEDECEKKLLIAQRESEFMLSSQRRRYEEQIEDLKDEIEELKNPASDTDISDDPNESKSPIEILDDD', 628, 'Q9V877;', 'KD00706', 'Drosophila melanogaster (Fruit fly)', 'sub', '#Kinesin-like protein subito#Protein double or nothing', '-', '-', '44870');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(707, 'Q9BW27', 'Nuclear pore complex protein Nup85', 'GO:0000777===c;k', 75019, 'Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP98/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2- activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl- inositol 3-kinase-Rac-lammellipodium protrusion cascade. {ECO:0000269|PubMed:12718872; ECO:0000269|PubMed:15995708; ECO:0000269|PubMed:16807356}.', 'MEELDGEPTVTLIPGVNSKKNQMYFDWGPGEMLVCETSFNKKEKSEMVPSCPFIYIIRKDVDVYSQILRKLFNESHGIFLGLQRIDEELTGKSRKSQLVRVSKNYRSVIRACMEEMHQVAIAAKDPANGRQFSSQVSILSAMELIWNLCEILFIEVAPAGPLLLHLLDWVRLHVCEVDSLSADVLGSENPSKHDSFWNLVTILVLQGRLDEARQMLSKEADASPASAGICRIMGDLMRTMPILSPGNTQTLTELELKWQHWHEECERYLQDSTFATSPHLESLLKIMLGDEAALLEQKELLSNWYHFLVTRLLYSNPTVKPIDLHYYAQSSLDLFLGGESSPEPLDNILLAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCKLLQSHNLYFGSNMREFLLLEYASGLFAHPSLWQLGVDYFDYCPELGRVSLELHIERIPLNTEQKALKVLRICEQRQMTEQVRSICKILAMKAVRNNRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRMYGEKRFADAASLLLSLMTSRIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELMRCLEDLTSRRPVHGESDTEQLQDDDIETTKVEMLRLSLARNLARAIIREGSLEGS', 656, 'Q9BW27; B4DMQ3; B4DPW1; Q8NDI4; Q9H9U1;', 'KD00707', 'Homo sapiens (Human)', 'NUP85', '#Nuclear pore complex protein Nup85#85 kDa nucleoporin#FROUNT#Nucleoporin Nup75#Nucleoporin Nup85#Pericentrin-1', '-', 'ENSG00000125450', '-'),
(708, 'Q5RBF1', 'NAD-dependent protein deacetylase sirtuin-2', 'GO:0051987', 39515, 'NAD-dependent protein deacetylase; which deacetylates internal lysines on histone and non-histone proteins such as ACLY; PCK1 and RELA. Deacetylates ''Lys-40'' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle; probably via its role in the regulation of cytoskeleton. Deacetylates PCK1; opposing proteasomal degradation. Deacetylates ''Lys-310'' of RELA (By similarity). {ECO:0000250}.', 'MDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQSGAGVPNPSTSASPKKSPPPAKDEARTTEREKPQ', 352, 'Q5RBF1;', 'KD00708', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'SIRT2', '#NAD-dependent protein deacetylase sirtuin-2#3.5.1.-#Regulatory protein SIR2 homolog 2#SIR2-like protein 2', '-', '-', '100172430'),
(709, 'Q6CVK1', 'DASH complex subunit DAM1', 'GO:0008608===GO:0042729', 34528, '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}.', 'MSQRPNTPQRDRPTEYRLSLSSNASSRRSSLGNNGRDQHASNQTMIEKYVLPQLQELSDSMVTLDGNMTHMNFIHESIADLNEALSALLYGLMCNSWCVDFPNISHDTPHELKLIQRLEELKQERQALQAKLKPKELTKGSILPLSRQPLSRGSQMLYRDENVPGSTASSNVNIDINDDEDNTAASFVSNPTTFKPQMISSVGASTDFMGKQTVGSASSKLRRRSILHQIRNNAAIGTIPNTLTGITPGERKRSLAVSAKRIPILAGSSTTAGSASSANRESTNTEPALPNRVVRTRQRTYNPKNLASRPPFR', 313, 'Q6CVK1;', 'KD00709', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'DAM1', '#DASH complex subunit DAM1#Outer kinetochore protein DAM1', '-', '-', '2896917'),
(710, 'Q9GZS0', 'Dynein intermediate chain 2; axonemal', 'GO:0003777', 68821, 'Part of the dynein complex of respiratory cilia.', 'MEIVYVYVKKRSEFGKQCNFSDRQAELNIDIMPNPELAEQFVERNPVDTGIQCSISMSEHEANSERFEMETRGVNHVEGGWPKDVNPLELEQTIRFRKKVEKDENYVNAIMQLGSIMEHCIKQNNAIDIYEEYFNDEEAMEVMEEDPSAKTINVFRDPQEIKRAATHLSWHPDGNRKLAVAYSCLDFQRAPVGMSSDSYIWDLENPNKPELALKPSSPLVTLEFNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIESSHRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKMSEPTEVVILDITKKEQLENALGAISLEFESTLPTKFMVGTEQGIVISCNRKAKTSAEKIVCTFPGHHGPIYALQRNPFYPKNFLTVGDWTARIWSEDSRESSIMWTKYHMAYLTDAAWSPVRPTVFFTTRMDGTLDIWDFMFEQCDPTLSLKVCDEALFCLRVQDNGCLIACGSQLGTTTLLEVSPGLSTLQRNEKNVASSMFERETRREKILEARHREMRLKEKGKAEGRDEEQTDEELAVDLEALVSKAEEEFFDIIFAELKKKEADAIKLTPVPQQPSPEEDQVVEEGEEAAGEEGDEEVEEDLA', 605, 'Q9GZS0; C9J0S6; Q8IUW4; Q9H179; Q9NT53;', 'KD00710', 'Homo sapiens (Human)', 'DNAI2', '#Dynein intermediate chain 2; axonemal#Axonemal dynein intermediate chain 2', '-', 'ENSG00000171595', '-'),
(711, 'Q6GQ71', 'Kinetochore protein Nuf2-B', 'GO:0000777===GO:0031262', 54631, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MDKLTFPIFPAADLVNFFRQNILTGTEAKNFNKNDLYPNPKPEMVQKLYMRILQQVFSYGVEQFYMVPMDLDIQYPHLVEGFAPVANILKLMARLLPMCRVYDFHPSDVLNPKGKRTLHLLSGIFNFLQFRTTQREVYMEYCSGYKSALENVRQLQKTNHEAEIKIEKLTTVPPEQQAEFKALSSEIHDLQQIISQEYRAKDVMFQEKIAQRKAEFAEKNKRLNEQKLTIATMKEEQERMKSQIVESPEQRKSKTERMKETVHRLKQARQETSDKCDHYRDRVALAFMWQSDVQGYLKKLQNIDANLEIHRKIHEEIRHIEEQLMNLNLELKSLSNEDAQLKRIILVKKEKLAKVDIKNKKKQEDFNQQKQEILEVCSHIQEKRQVIHGRVAQVLQEIQQTISKKEQLLETTEAGKNKCQEVITDFRAALEKYHDSLQKASERSADRRREKIAELNRRLSRQ', 462, 'Q6GQ71; Q498I2;', 'KD00711', 'Xenopus laevis (African clawed frog)', 'nuf2-b', '#Kinetochore protein Nuf2-B#Cell division cycle-associated protein 1-B', '-', '-', '-'),
(712, 'Q28HU3', 'Centromere protein O', 'GO:0000776===GO:0034508', 34192, 'Probable component of a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. {ECO:0000250}.', 'MEQAQSLFREGVLSHLEQLEALSYNLAVKQEKQRQEWAALRKNQELVLELRKKRDELKAKIERHKAEIQAFRGREEAGEDHGSAAGTSQQAMLELCVEELKGMLEMHWLTGISGKRTKKGVCVCISTAFEGAYLDSFHLDIALKPSVGISRHSVPPFIPLEQIAKEHLQTDLKKFLSVLFEHLNAYAGRKYQFQQLQSFPGGFVRDAQQGNSLHTVLTFGYNVRVEKQPFCLRAKLLYGGVTRSLPTEAVITCEDNRPSVQEKISSHSSLFCQNPLHRALECISSEDETLNHSSASLLGTHMF', 303, 'Q28HU3; Q501R3;', 'KD00712', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'cenpo', '#Centromere protein O#CENP-O', '-', '-', '733516'),
(713, 'O59790', 'Serine/threonine-protein kinase ark1', 'GO:0034501===GO:0000778===GO:0031134===GO:0032133===k', 40597, 'Required for the spindle checkpoint attachment response during spindle formation; kinetochore microtubule interactions and chromosome segregation during anaphase. Ark1 activity depends upon cut17 function and phosphorylation. Ark1 with bir1 is required for full-scale association with kinetochores and formation of a complex with mad3. Ark1 is also required for phosphorylation of histone H3 that accompanies chromosome condensation and condensin recruitment to mitotic chromatin. Ark1 with pic1 is required for the execution of cytokinesis. {ECO:0000269|PubMed:11792803; ECO:0000269|PubMed:11950927; ECO:0000269|PubMed:12676091}.', 'MSDSKLADSLNCLSVSTPSTTANPGRQQLLRLAVSNQRQVNNVSLANGKENKRTSNSKFNSSLRKIEEPIAGVPSSAGPQWREFHIGMFEIGKPLGKGKFGRVYLAKEKKTGFIVALKTLHKSELVQSKIEKQVRREIEIQSNLRHKNILRLYGHFHDEKRIYLILEFAGRGELYQHLRRAKRFSEEVASKYIFQMANALSYLHKKHVIHRDIKPENILLGIDGEIKLSDFGWSVHAPSNRRTTLCGTLDYLPPEMVEGKEHTEKVDLWSLGVLTYEFLVGAPPFEDMSGHSATYKRIAKVDLKIPSFVPPDARDLISRLLQHNPEKRMSLEQVMRHPWIVKYKDSWTRKSSESS', 355, 'O59790;', 'KD00713', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ark1', '#Serine/threonine-protein kinase ark1#2.7.11.1#Aurora-related kinase 1', '-', '-', '3361036'),
(714, 'Q9H410', 'Kinetochore-associated protein DSN1 homolog', 'GO:0000444===SCL===k', 40067, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. {ECO:0000269|PubMed:15502821; ECO:0000269|PubMed:16585270}.', 'MTSVTRSEIIDEKGPVMSKTHDHQLESSLSPVEVFAKTSASLEMNQGVSEERIHLGSSPKKGGNCDLSHQERLQSKSLHLSPQEQSASYQDRRQSWRRASMKETNRRKSLHPIHQGITELSRSISVDLAESKRLGCLLLSSFQFSIQKLEPFLRDTKGFSLESFRAKASSLSEELKHFADGLETDGTLQKCFEDSNGKASDFSLEASVAEMKEYITKFSLERQTWDQLLLHYQQEAKEILSRGSTEAKITEVKVEPMTYLGSSQNEVLNTKPDYQKILQNQSKVFDCMELVMDELQGSVKQLQAFMDESTQCFQKVSVQLGKRSMQQLDPSPARKLLKLQLQNPPAIHGSGSGSCQ', 356, 'Q9H410; B4DWT2; E1P5U9; Q5JW55; Q5JW56; Q9H8P4;', 'KD00714', 'Homo sapiens (Human)', 'DSN1', '#Kinetochore-associated protein DSN1 homolog', '-', 'ENSG00000149636', '-'),
(715, 'Q86Z98', 'Kinesin heavy chain', 'GO:0003777', 103243, '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.', 'MSSANSIKVVARFRPQNKVELESGGKPIVSFDGEDTCTVASKEAQGSFTFDRVFDMGCKQQDIFDFSIRSTVDDILNGYNGTVFAYGQTGAGKSYTMMGTNIDDDEGRGIIPRIVEQIFASIMSSPGTIEYTVRVSYMEIYMERIRDLLAPQNDNLPVHEEKNRGVYVKGLLEIYVSSVQEVYEVMRRGGNARAVAATNMNQESSRSHSIFVITITQKNVETGSAKSGQLFLVDLAGSEKVGKTGASGQTLEEAKKINKSLSALGMVINALTDGKSSHIPYRDSKLTRILQESLGGNSRTTLIINCSPSSYNDAETLGTLRFGMRAKSIKNKAKVNAELSPAELKSLLKKAQGQVTNFESYISSLEGEIQMWRAGEAVPKERWATPLTTDAVARTKADARTSTRPSTPSLISDSRSETPAISDRAGTPSLPLDKDEREEFLRRENELQDQISEKESQAASAEKQLRETKEELAYLKDHDSKVGKENEKLTTEVNEFKMQLERLTFESKEAQITMDALKEANSELTTELDEVKQQLLDVKMSAKESGAALDEKEKRKAEKMAKMMAGFDLGGEVFSENERHIAETIEKVDSLHELSATGDNIAPDEFKALKARLVETQGIVRQAELSMYSTSSSESDSRRRQELEARLEAVQAEYEEILTRNLGPEDIEEVKARLENAFANRQTAQSQFVEELKEDIAQKAAENTRMKTLIEDLQQRVKAGATAPMANGKTIQQQIAEFDVMKKSLMRDLQNRCERVVELEISLDETREQYNNVLRSSNNRAQQKKMAFLERNLEQLTQVQRQLVEQNSALKKEVAIAERKLIARNERIQSLESLLQDSQEKMAAANHKYVQLAAVKERLELAKAGSTRGLNSPGGFSFANAGSRIAKPLRGGGGGNDAPSIPTIQNLQGQNEGNTSSGSSSKRASWFFTKS', 931, 'Q86Z98;', 'KD00715', 'Gibberella moniliformis (Maize ear and stalk rot fungus) (Fusariuverticillioides)', 'KLP1', '#Kinesin heavy chain', '-', '-', '-'),
(716, 'O42263', 'Kinesin-like protein', 'k', 339968, '', 'MSEGDAVKVCVRVRPLIQREQGDQANLQWKAGNNTISQVDGTKSFNFDRVFNSHESTSQIYQEIAVPIIRSALQGYNGTIFAYGQTSSGKTYTMMGTPNSLGIIPQAIQEVFKIIQEIPNREFLLRVSYMEIYNETVKDLLCDDRRKKPLEIREDFNRNVYVADLTEELVMVPEHVIQWIKKGEKNRHYGETKMNDHSSRSHTIFRMIVESRDRNDPTNSENCDGAVMVSHLNLVDLAGSERASQTGAEGVRLKEGCNINRSLFILGQVIKKLSDGQAGGFINYRDSKLTRILQNSLGGNAKTVIICTITPVSFDETLSTLQFASTAKHVRNTPHVNEVLDDEALLKRYRKEILDLKKQLENLESSSETKAQAMAKEEHTQLLAEIKQLHKEREDRIWHLTNIVVASSQESQQDQRVKRKRRVTWAPGKIQNSLHASGVSDFDMLSRLPGNFSKKAKFSDMPSFPEIDDSVCTEFSDFDDALSMMDSNGIDAEWNLASKVTHREKTSLHQSMIDFGQISDSVQFHDSSKENQLQYLPKDSGDMAECRKASFEKEITSLQQQLQSKEEEKKELVQSFELKIAELEEQLSVKAKNLEMVTNSREHSINAEVQTDVEKEVVRKEMSVLGDSGYNASNSDLQDSSVDGKRLSSSHDECIEHRKMLEQKIVDLEEFIENLNKKSENDKQKSSEQDFMESIQLCEAIMAEKANALEELALMRDNFDNIILENETLKREIADLERSLKENQETNEFEILEKETQKEHEAQLIHEIGSLKKLVENAEMYNQNLEEDLETKTKLLKEQEIQLAELRKRADNLQKKVRNFDLSVSMGDSEKLCEEIFQLKQSLSDAEAVTRDAQKECSFLRSENLELKEKMEDTSNWYNQKEKAASLFEKQLETEKSNYKKMEADLQKELQSAFNEINYLNGLLAGKVPRDLLSRVELEKKVSEFSKQLEKALEEKNALENEVTCLSEYKFLPNEVECLKNQISKASEEIMLLKQEGEHSASIISKQEIIMQEQSEQILQLTDEVTHTQSKVQQTEEQYLEMKKMHDDLFEKYIRNKSEAEDLLREMENLKGTMESVEVKIADTKHELEETIRDKEQLLHEKKYFFQAMQTIFPITPLSDSLPPSKLVEGNSQDPIEINDYHNLIALATERNNIMVCLETERNSLKEQVIDLNTQLQSLQAQSIEKSDLQKPKQDLEEGEVKLLLEMELLKGHLTDSQLSIEKLQLENLEVTEKLQTLQEEMKNITIERNELQTNFEDLKAEHDSLKQDLSENIEQSIETQDELRAAQEELREQKQLVDSFRQQLLDCSVGISSPNHDAVANQEKVSLGEVNSLQSEMLRGERDELQTSCKALVSELELLRAHVKSVEGENLEITKKLNGLEKEILGKSEESEVLKSMLENLKEDNNKLKEQAEEYSSKENQFSLEEVFSGSQKLVDEIEVLKAQLKAAEERLEIKDRDYFELVQTANTNLVEGKLETPLQADHEEDSIDRRSEEMEIKVLGEKLERNQYLLERLQEEKLELSNKLEILQKEMETSVLLKDDLQQKLESLLSENIILKENIDTTLKHHSDTQAQLQKTQQELQLAKNLAIAASDNCPITQEKETSADCVHPLEEKILLLTEELHQKTNEQEKLLHEKNELEQAQVELKCEVEHLMKSMIESKSSLESLQHEKHDTEQQLLALKQQMQVVTQEKKELQQTHEHLTAEVDHLKENIELGLNFKNEAQQKTTKEQCLLNENKELEQSQHRLQCEIEELMKSLKDKESALETLKESEQKVINLNQEMEMVMLEMEELKNSQRTVIAERDQLQDDLRESVEMSIETQDDLRKAQEALQQQKDKVQELTSQISVLQEKISLLENQMLYNVATVKETLSERDDLNQSKQHLFSEIETLSLSLKEKEFALEQAEKDKADAARKTIDITEKISNIEEQLLQQATNLKETLYERESLIQCKEQLALNTEHLRETLKSKDLALGKMEQERDEAANKVIALTEKMSSLEEQINENVTTLKEGEGEKETFYLQRPSKQQSSSQMEELRESLKTKDLQLEEAEKEISEATNEIKNLTAKISSLEEEILQNASILNEAVSERENLRHSKQQLVSELEQLSLTLKSRDHAFAQSKREKDEAVNKIASLAEEIKILTKEMDEFRDSKESLQEQSSHLSEELCTYKTELQMLKQQKEDINNKLAEKVKEVDELLQHLSSLKEQLDQIQMELRNEKLRNYELCEKMDIMEKEISVLRLMQNEPQQEEDDVAERMDILESRNQEIQELMEKISAVYSEQHTLLSSLSSELQKETEAHKHCMLNIKESLSSTLSRSFGSLQTEHVKLNTQLQTLLNKFKVVYRTAAVKEDHSLIKDYEKDLAAEQKRHDELRLQLQCLEQHGRKWSDSASEELKFCEIEFLNELLFKKANIIQSVQDDFSEVQVFLNQVGSTLQEELEHKKGFMQWLEEFGDLHVDAKKLSEGMQQENRRIASTIQLLTKRLKAVVQSKIQREITVYLNQFEAKLQEKKEQNKELMRRMEHHGPSASVMEEENARLLGILKTVQDESKKLQSRIKMLENELNLVKDDAMHKGEKVAILQDKLLSRNAEAELNAMQVKLTKKQDNLQAAMKEIENLQKMVAKGAVPYKEEIDNLKTKVVKIEMEKIKYSKATDQEIAYLKSCLEDKEEGLRRLKEELRRAQADNDTTVCVPKDYQKASTFPVTCGGGSGIVQSTAMLVLQSEKAALERELSHYKKKYHHLSRTMSSSEDRKKTKAKSDAHSSHTGSSHRGSPHKTETYRHGPVTPERSEMPSLHLGSPKKSESSTKRVVSPNRSEIYSQLVMSPGKTGMHKHILSPSKVGLHKKRALSPNRSEMPTQHVISPGKTGLHKNLTESTLFDNLSSPCKQQKVQENLNSPKGKLFDVKSKSMPYCPSQFFDNSKLGDFSELNTAESNDKSQAENWWYEAKKETAPECKTS', 2954, 'O42263;', 'KD00716', 'Xenopus laevis (African clawed frog)', 'cenpe', '#Kinesin-like protein {ECO:0000256|RuleBase:RU000394}', '-', '-', '394299'),
(717, 'A7YY75', 'Nucleoporin SEH1', 'GO:0000777===GO:0051315', 39641, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (By similarity). As a component of the GATOR2 complex; inhibits GATOR1 complex; an inhibitor of the amino acid-sensing branch of the TORC1 pathway (By similarity). {ECO:0000250}.', 'MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGEWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHAPMIAVGSDDSSPNAMAKVQIFEYNENTRKYAKAETLLTVTDPVHDIAFAPNLGRSFHILAIATKDVRIFTLKPVRKELTSSGGPTKFEIHIVAQFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILKGNGSPVNGSSQQGNSNPSVGSNIPSLQNSLNGSSAGRKHS', 360, 'A7YY75;', 'KD00717', 'Bos taurus (Bovine)', 'SEH1L', '#Nucleoporin SEH1#Nup107-160 subcomplex subunit SEH1', '-', '-', '506509'),
(718, 'Q9UW86', 'Serine/threonine-protein phosphatase PP1', 'GO:0034501===GO:0000778', 35568, '', 'MADHTEVDLDSIIDRLLEVRGSRPGKQVQLLEAEIRYLCTKAREIFISQPILLELEAPIKICGDIHGQYYDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFILRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIIDEKIFTMHGGLSPDLNSMEQIRRVMRPTDIPDCGLLCDLLWSDPDKDITGWSENDRGVSFTFGPDVVSRFLQKHDMDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGAMMSVDESLLCSFQILKPAEKKQKFGRR', 308, 'Q9UW86; O59927; Q7RV51;', 'KD00718', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'pph-3', '#Serine/threonine-protein phosphatase PP1#3.1.3.16#Phosphoprotein phosphatase 1', '-', '-', '3872306'),
(719, 'Q9BW19', 'Kinesin-like protein KIFC1', 'GO:0003777', 73748, 'Minus end-directed microtubule-dependent motor required for bipolar spindle formation. May contribute to movement of early endocytic vesicles. {ECO:0000269|PubMed:15843429}.', 'MDPQRSPLLEVKGNIELKRPLIKAPSQLPLSGSRLKRRPDQMEDGLEPEKKRTRGLGATTKITTSHPRVPSLTTVPQTQGQTTAQKVSKKTGPRCSTAIATGLKNQKPVPAVPVQKSGTSGVPPMAGGKKPSKRPAWDLKGQLCDLNAELKRCRERTQTLDQENQQLQDQLRDAQQQVKALGTERTTLEGHLAKVQAQAEQGQQELKNLRACVLELEERLSTQEGLVQELQKKQVELQEERRGLMSQLEEKERRLQTSEAALSSSQAEVASLRQETVAQAALLTEREERLHGLEMERRRLHNQLQELKGNIRVFCRVRPVLPGEPTPPPGLLLFPSGPGGPSDPPTRLSLSRSDERRGTLSGAPAPPTRHDFSFDRVFPPGSGQDEVFEEIAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPGGDPQLEGLIPRALRHLFSVAQELSGQGWTYSFVASYVEIYNETVRDLLATGTRKGQGGECEIRRAGPGSEELTVTNARYVPVSCEKEVDALLHLARQNRAVARTAQNERSSRSHSVFQLQISGEHSSRGLQCGAPLSLVDLAGSERLDPGLALGPGERERLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIGTAQANRK', 673, 'Q9BW19; O60887; Q14834; Q4KMP0; Q5SU09; Q6GMS7; Q6P4A5; Q9UQP7;', 'KD00719', 'Homo sapiens (Human)', 'KIFC1', '#Kinesin-like protein KIFC1#Kinesin-like protein 2#Kinesin-related protein HSET', '-', 'ENSG00000237649', '-'),
(720, 'Q751Z6', 'Probable kinetochore protein SPC25', 'GO:0000778===GO:0051455===GO:0031617', 26094, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSLEGFAELRAQMEAFQGRVHGHLGQQRHAMEQLLAAHRQEVEKLRLRTGAVQQQLARLAGEEQELRQNISSLQERTQHTTAQRDAYAAQRQKLAAERTQLEHDRAELHAMLARKQAELQRQREAIKRQHMRDNPEVRVYEQLLGLYVRASRPDSLEFAFRNVSEADARAECSFTLDLGADGYRVAAAQPPLPLERLRDLERDLGSSGDLPAFLKAIRAALVTAMAGQADA', 231, 'Q751Z6;', 'KD00720', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '4622516'),
(721, 'O13684', 'Monopolin complex subunit pcs1', 'GO:0000776===GO:0000778===GO:0051315===GO:0051456===GO:0033551===k', 30418, 'The monopolin-like pcs1/mde4 complex is essential for accurate chromosome segregation during mitosis and meiosis II. May clamp together microtubule binding sites on the same kinetochore; preventing merotelic attachment of microtubules. In contrast to its S.cerevisiae ortholog CSM1; is not required ofr mono- orientation during meiosis I. {ECO:0000269|PubMed:12689592; ECO:0000269|PubMed:17627824}.', 'MRKNNMQTSKDSELKEQAKGKSSKLIHKLPKQRTRISQGQMHSTQDFVNNEDQDAYSVRENENELHINNSGMSELNKKLQLPNVELSTLSHTQEQEFNELNKLIRKINELQEFYLLEDLAKPVTNAGADADDTIVKDLKKELENEKKANHSLKNELLKTREQIKNYSKINILIKELFGLEVADCIEDEDGYRFNCKNTGRRGTLEYQLLLDDQNFTFTPRLNVQTDEELMKHLPDYLLEEIIFTKEQGKLFSARLMKALQD', 261, 'O13684; Q870L5; Q9UTP7;', 'KD00721', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'pcs1', '#Monopolin complex subunit pcs1#Chromosome segregation protein 1', '-', '-', '3361562'),
(722, 'Q96DT5', 'Dynein heavy chain 11; axonemal', 'GO:0003777', 520369, '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.', 'MAAQVAAREARDFREAPTLRLTSGAGLEAVGAVELEEEEENEEEAAARRARSFAQDARVRFLGGRLAMMLGFTEEKWSQYLESEDNRQVLGEFLESTSPACLVFSFAASGRLAASQEIPRDANHKLVFISKKITESIGVNDFSQVVLFGELPALSLGHVSAFLDEILVPVLSNKNNHKSWSCFTSQDMEYHIEVMKKKMYIFRGKMSRRTLLPIPTVAGKMDLDQNCSENKPPSNERIILHAIESVVIEWSHQIQEIIERDSVQRLLNGLHLSPQAELDFWMMRRENLSCIYDQLQAPVVLKMVKILTTKQSSYFPTLKDIFLAVENALLEAQDVELYLRPLRRHIQCLQETEFPQTRILIAPLFHTICLIWSHSKFYNTPARVIVLLQEFCNLFINQATAYLSPEDLLRGEIEESLEKVQVAVNILKTFKNSFFNYRKKLASYFMGRKLRPWDFQSHLVFCRFDKFLDRLIKIEDIFATTLEFEKLERLEFGGTKGAILNGQVHEMSEELMELCKLFKQSTYDPSDCTNMEFESDYVAFKSKTLEFDRRLGTIICEAFFNCNGLEAAFKLLTIFGNFLEKPVVMEIFSLHYSTLVHMFNTELDVCKQLYNEHMKQIECGHVVLNKNMPFTSGNMKWAQQVLQRLQMFWSNFASLRYLFLGNPDHALVYQKYVEMTTLLDQFESRIYNEWKSNVDEICEFNLNQPLVKFSAINGLLCVNFDPKLVAVLREVKYLLMLKKQDIPDSALAIFKKRNTILKYIGNLDLLVQGYNKLKQTLLEVEYPLIEDELRAIDEQLTAATTWLTWQDDCWGYIERVRAATSELEHRVERTQKNVKVIQQTMRGWARCVLPPRREHRREAAFTLEDKGDLFTKKYKLIQGDGCKIHNLVEENRKLFKANPSLDTWKIYVEFIDDIVVEGFFQAIMHDLDFFLKNTEKQLKPAPFFQAQMILLPPEIVFKPSLDREAGDGFYDLVEEMLCNSFRMSAQMNRIATHLEIKNYQNDMDNMLGLAEVRQEIMNRVVNVINKVLDFRNTLETHTYLWVDDRAEFMKHFLLYGHAVSSDEMDAHANEEIPEQPPTLEQFKEQIDIYEALYVQMSKFEDFRVFDSWFKVDMKPFKVSLLTIIKKWSWMFQEHLLRFVIDSLNELQEFIKETDSGLQRELNEGDHDGLVDIMVHLLAVRSRQRATDELFEPLKETITLLESYGQKMPEQVYIQLEELPERWETTKKIAATVRHEVSPLHNAEVTLIRKKCILFDAKQAEFRERFRHYAPLGFNAENPYTALDKANEELEALEEEMLQMQESTRLFEVALPEYKQMKQCRKEIKLLKGLWDVIIYVRRSIDNWTKTQWRQIHVEQMDVELRRFAKEIWSLNKEVRVWDAYTGLEGTVKDMTASLRAITELQSPALRDRHWHQLMKAIGVKFLINEATTLADLLALRLHRVEDDVRRIVDKAVKELGTEKVITEISQTWATMKFSYEVHYRTGIPLLKSDEQLFETLEHNQVQLQTLLQSKYVEYFIEQVLSWQNKLNIADLVIFTWMEVQRTWSHLESIFVCSEDIRIQLVKDARRFDGVDAEFKELMFKTAKVENVLEATCRPNLYEKLKDLQSRLSLCEKALAEYLETKRIAFPRFYFVSSADLLDILSKGAQPKQVTCHLAKLFDSIADLQFEDNQDVSAHRAVGMYSKEKEYVPFQAECECVGHVETWLLQLEQTMQETVRHSITEAIVAYEEKPRELWIFDFPAQVALTSSQIWWTTDVGIAFSRLEEGYETALKDFHKKQISQLNTLITLLLGELPPGDRQKIMTICTIDVHARDVVAKLISQKVVSPQAFTWLSQLRHRWEDTQKHCFVNICDAQFQYFYEYLGNSPRLVITPLTDRCYITLTQSLHLTMSGAPAGPAGTGKTETTKDLGRALGMMVYVFNCSEQMDYKSIGNIYKGLVQTGAWGCFDEFNRISVEVLSVVAVQVKMIHDAIRNRKKRFVFLGEAITLKPSVGIFITMNPGYAGRTELPENLKALFRPCAMVAPDIELICEILLVAEGFVDARALARKFITLYTLCKELLSKQDHYDWGLRAIKSVLVVAGSLKRGDKNRPEDQVLMRALRDFNMPKIVTDDIPVFLGLVGDLFPALDVPRRRKLHFEQMVRQSTLELRLQPEESFILKVVQLEELLAVRHSVFVVGNAGTGKSKILRTLNRTYVNMKQKPVWNDLNPKAVTTDELFGFIHHATREWKDGKIVYSYFIGLFSSILREQANLKHDGPKWIVLDGDIDPMWIESLNTVMDDNKVLTLASNERIALTPFMRLLFEIHHLRSATPATVSRAGILYVNPQDLGWNPYVASWIDRRRHQSEKANLTILFDKYVPACLDKLRTSFKTITSIPESSLVQTLCVLLECLLTPENVPSDSPKEVYEVYFVFACIWAFGGTLLQDQISDYQADFSRWWQKEMKAVKFPSQGTIFDYYVDHKTKKLLPWADKIAQFTMDPDVPLQTVLVHTTETARLRYFMELLLEKGKPLMLVGNAGVGKTVFVGDTLASLSEDYIVSRVPFNYYTTSTALQKILEKPLEKKAGHNYGPGGNKKLIYFIDDMNMPEVDLYGTVQPHTLIRQHIDYGHWYDRQKVMLKEIHNCQYVACMNPMVGSFTINPRLQRHFTVFAFNFPSLDALNTIYGQIFSFHFQQQAFAPSILRSGPTLIQATIAFHQTMMCNFLPTAIKFHYIFNLRDLSNVFQGILFASPECLKGPLDLIHLWLHESARVYGDKLIDKKDCDLFQRRMLETAYKYFEGIDSHMLLQQPLIYCHFADRGKDPHYMPVKDWEVLKTILTETLDNYNELNAAMHLVLFEDAMQHVCRISRILRTPQGCALLVGVGGSGKQSLSRLAAYLRGLEVFQITLTEGYGIQELRVDLANLYIRTGAKNMPTVFLLTDAQVLDESFLVLINDLLASGEIPDLFSDEDVDKIISGIHNEVHALGMVDSRENCWKFFMARVRLQLKIILCFSPVGRTLRVRARKFPAIVNCTAIDWFHAWPQEALVSVSRRFIEETKGIEPVHKDSISLFMAHVHTTVNEMSTRYYQNERRHNYTTPKSFLEQISLFKNLLKKKQNEVSEKKERLVNGIQKLKTTASQVGDLKARLASQEAELQLRNHDAEALITKIGLQTEKVSREKTIADAEERKVTAIQTEVFQKQRECEADLLKAEPALVAATAALNTLNRVNLSELKAFPNPPIAVTNVTAAVMVLLAPRGRVPKDRSWKAAKVFMGKVDDFLQALINYDKEHIPENCLKVVNEHYLKDPEFNPNLIRTKSFAAAGLCAWVINIIKFYEVYCDVEPKRQALAQANLELAAATEKLEAIRKKLVDLDRNLSRLTASFEKATAEKVRCQEEVNQTNKTIKLANRLVKELEAKKIRWGQSIKSFEAQEKTLCGDVLLTAAFVSYVGPFTRQYRQELVHCKWVPFLQQKVSIPLTEGLDLISMLTDDATIAAWNNEGLPSDRMSTENAAILTHCERWPLVIDPQQQGIKWIKNKYGMDLKVTHLGQKGFLNAIETALAFGDVILIENLEETIDPVLDPLLGRNTIKKGKYIRIGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEAQLLAEVVSIERPDLEKLKLVLTKHQNDFKIELKYLEDDLLLRLSAAEGSFLDDTKLVERLEATKTTVAEIEHKVIEAKENERKINEARECYRPVAARASLLYFVINDLQKINPLYQFSLKAFNVLFHRAIEQADKVEDMQGRISILMESITHAVFLYTSQALFEKDKLTFLSQMAFQILLRKKEIDPLELDFLLRFTVEHTHLSPVDFLTSQSWSAIKAIAVMEEFRGIDRDVEGSAKQWRKWVESECPEKEKLPQEWKKKSLIQKLILLRAMRPDRMTYALRNFVEEKLGAKYVERTRLDLVKAFEESSPATPIFFILSPGVDALKDLEILGKRLGFTIDSGKFHNVSLGQGQETVAEVALEKASKGGHWVILQNVHLVAKWLGTLEKLLERFSQGSHRDYRVFMSAESAPTPDEHIIPQGLLENSIKITNEPPTGMLANLHAALYNFDQDTLEICSKEQEFKSILFSLCYFHACVAGRLRFGPQGWSRSYPFNPGDLTICASVLYNYLEANSKVPWEDLRYLFGEIMYGGHITDDWDRKLCRVYLEEFMNPSLTEDELMLAPGFAAPPYLDYAGYHQYIEEMLPPESPALYGLHPNAEIEFLTVTSNTLFRTLLEMQPRNALSGDELGQSTEEKVKNVLDDILEKLPEEFNMAEIMQKNSNRSPYVLVCFQECERMNILIREIRISLEQLDLSLKGELALSPAVEAQQFALSYDTVPDTWSKLAYPSTYGLAQWFNDLLLRCRELDTWTQDLTLPAVVWLSGFFNPQSFLTAIMQTMARKNEWPLDKTRLTADVTKKTKEDYGHPPREGAYLHGLFMEGARWDTQAGTIVEARLKELACPMPVIFAKATPVDRQETKQTYECPVYRTKLRGPSYIWTFRLKSEEKTAKWVLAGVALLLEA', 4516, 'Q96DT5; Q9UJ82;', 'KD00722', 'Homo sapiens (Human)', 'DNAH11', '#Dynein heavy chain 11; axonemal#Axonemal beta dynein heavy chain 11#Ciliary dynein heavy chain 11', '-', 'ENSG00000105877', '-'),
(723, 'Q0USL4', 'Tethering factor for nuclear proteasome STS1', 'GO:0061638', 33892, '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}.', 'MNAIHGSFTPPHLLNNRHSPTRNIYPSSAMTGRKRKADDDGSSDDRMSASPSISSAELPRQQPRHMKRMRTNLSGRPLPLPRLLETLSADEMRNLLQSICQRHPDIGNEVVSTAPRPSIQSTLEVLSKYESAFQSAFPFGGRASSDYAYNRVRQQLIELLESLKDFTPHYLPPNEQQSATSLAFLDGATEIIHRLPNWDTYQHNRHKEEAYEEMAKAWAIVFREAAKKAGGIQLQYGGWDQKIAKHNEHSGGKMQEAVNELRGGLGWMGADAPAPAASGPEDAMSIRQQLLSGNYGMGSSASIGAW', 306, 'Q0USL4;', 'KD00723', 'Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173(Glume blotch fungus) (Septoria nodorum)', 'STS1', '#Tethering factor for nuclear proteasome STS1', '-', '-', '5972533'),
(724, 'P04909', 'Histone H2A-alpha', 'GO:0034501', 13878, 'Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin; limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation; DNA repair; DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones; also called histone code; and nucleosome remodeling. {ECO:0000269|PubMed:15226425}.', 'MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKTSGRTGKPSQEL', 132, 'P04909;', 'KD00724', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hta1', '#Histone H2A-alpha#H2A.1', '-', '-', '2539499'),
(725, 'Q6PDL0', 'Cytoplasmic dynein 1 light intermediate chain 2', 'GO:0003777===GO:0005868', 54218, '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 (By similarity). {ECO:0000250}.', 'MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLRETLVIFVADMSRPWTIMESLQKWASVLREHIDKMKIPPEEMRDLERKFMKEFQDYIEPEEGCQGSPQRRGPLTSGSDEDSVALPLGDNVLTHNLGIPVLVVCTKCDAMSVLEKEHDYRDEHLDFIQAHLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTIPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQSLLAKQPATPTRTSESPARGPSGSPRTQGRGGPASVPSASPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPSAGGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA', 492, 'Q6PDL0; Q3UGJ3;', 'KD00725', 'Mus musculus (Mouse)', 'Dync1li2', '#Cytoplasmic dynein 1 light intermediate chain 2#Dynein light intermediate chain 2; cytosolic', '-', '-', '234663'),
(726, 'P24339', 'Kinesin-like protein cut7', 'c;k', 122133, 'Could be a spindle pole body motor. On transition from G2 to M phase of the cell cycle; the spindle pole body duplicates; the daughter pole bodies seed microtubules which interdigitate to form a short spindle that elongates to span the nucleus at metaphase. Mutations at cut7 block spindle formation.', 'MAPRVAPGGSQQFLGKQGLKAKNPVSTPNSHFRSASNPRKRREPPTIDTGYPDRSDTNSPTDHALHDENETNINVVVRVRGRTDQEVRDNSSLAVSTSGAMGAELAIQSDPSSMLVTKTYAFDKVFGPEADQLMLFENSVAPMLEQVLNGYNCTIFAYGQTGTGKTYTMSGDLSDSDGILSEGAGLIPRALYQLFSSLDNSNQEYAVKCSYYELYNEEIRDLLVSEELRKPARVFEDTSRRGNVVITGIEESYIKNAGDGLRLLREGSHRRQVAATKCNDLSSRSHSIFTITLHRKVSSGMTDETNSLTINNNSDDLLRASKLHMVDLAGSENIGRSGAENKRARETGMINQSLLTLGRVINALVEKAHHIPYRESKLTRLLQDSLGGKTKTSMIVTVSSTNTNLEETISTLEYAARAKSIRNKPQNNQLVFRKVLIKDLVLDIERLKNDLNATRKKNGVYLAESTYKELMDRVQNKDLLCQEQARKLEVLDLNVKSSREQLQYVSKSNQEHKKEVEALQLQLVNSSTELESVKSENEKLKNELVLEIEKRKKYETNEAKITTVATDLSQYYRESKEYIASLYEKLDRTERNNKENENNFWNLKFNLLTMLRSFHGSFTDETNGYFTLLNDFNASMEELLNTHSNQLLISMTKITEHFQSLDEALQSARSSCAVPNSSLDLIVSELKDSKNSLLDALEHSLQDISMSSQKLGNGISSELIELQKDMKESYRQLVQELRSLYNLQHTHEESQKELMYGVRNDIDALVKTCTTSLNDADIILSDYISDQKSKFESKQQDLIANIGKIVSNFLQEQNESLYTKADILHSHLNDTNSNIRKANEIMNNRSEEFLRNAASQAEIVGANKERIQKTVENGSQLLDSKSKAIHSNSRSMYDHCLALAESQKQGVNLEVQTLDRLLQKVKEHSEDNTKEKHQQLLDLLESLVGNNDNLIDSIKTPHTELQKITDHVLKGTTSLANHTNELLGLGDESLCNLETTIEDTSLVKLETTGDTPSKRELPATPSWTRDSSLIKETTNLNLDSDKKFVRETYTSSNQTNEPDVYDKPSNSSRTSLLRSSRSAYSKMKR', 1085, 'P24339;', 'KD00726', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cut7', '#Kinesin-like protein cut7#Cell untimely torn protein 7', '-', '-', '2542732'),
(727, 'Q9NGQ2', 'Kinesin-related protein 1', 'GO:0003777', 248003, 'Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule''s plus end. Transports cytoplasmic vesicles and particularly phosphatidylinositol 4;5-bisphosphate- containing liposomes along microtubules. {ECO:0000269|PubMed:10545495; ECO:0000269|PubMed:12015984}.', 'MNVQVAVRVRPFNSREKERNAELIVQMNNKSTILTRPSALRANPLAAPTADDEKSFSFDYSYWSYDSNDPHFASQSTVYNDLGKEVLKNAWDGFNCSIFAYGQTGSGKSYSMMGYGEEKGIIPLICEELFQRIQSTPSNSNEQTIYKTTVSYMEIYNEKVKDLLNPNNNKTGGLKVRNNPSTGPYVEDLSKLAVKSFSEIDMLMDEGSKARTVASTNMNATSSRSHAVFTIVFTQSKIDKTRGTAIDRVSKISLVDLAGSERANSTGATGVRLKEGANINKSLSTLGKVISALAENSTSKKAVFVPYRDSVLTYLLKETLGGNSKTIMIAAISPADINYEESLSTLRYADSAKKIKTVAVVNEDAQSKLIRELQGEVERLRAMMDQGGQYHANDSKLMNSDYDETVSTLNEKIEQYEKLMAELNKSWEEKLSEAEAIREDRMAALKDMGVAIKVVSSIPHLINLNEDPLMSESLIYYVKEGKTRIGRSDSEIPQDIILNGLNIHKEHCIFENINGKVIISPSNNFMNNNNNKENSSSTTPTSSKSPSKPKSEKEKENNNDDDDGEKKLDRSYIYVNGVEINKPTILTTGNRVILGNNHIFRFNNPEEAIKIARERNQTTGGIVSSTKSPVDQIMDYDFALNELASIQGTLAMSKHINDKQEYKKQMRALYDQIRLQLENDCDPEVKEQREKLALLAFRRWRSKVHRSKLLNKISFIILSLNEANAISSTLNKKINLSLKLYSVFPEPDQISDNIEPEIDWRKTQILIKATDSSTGESTLVTDQDFVDRIYLMRELYQNDGRLDTELPEDPFQFTFTKDSLIGVSHVYLKNTLYLVESNRPVPILDENGNQKGYLNLLVSSSSTDITESERGLYLENPSNNKSLLLGKNLEITIGFEGFSEFIDENKFSDVFIKFNFPNQNGTIVDTFLTEPQPISAFIDQKRIVITSLTESLINLLQTQYVSFEIRGHKKSKQQPKLTSSSSSASTTSSSSKNQPMLENFEFLATLNILESEKNTGTDDQYKPVHILEDPDVYNTHLPSVTFRLKKDKTNRQILFKVIKNESNSIIKECKSARISDIKIFGKRDNPLLSSSATPNTPNTPNNSRIAGIQNTPGTPMTPYSNQTNNQQSSSSQPPLPQQQGTPYNPQSNNPNVISNAPPTPNSNLLKDLSLAANVQTSSSSSSSSLNVLLNNQQQQQQSQQSQQQQQQQSQQSSETSSTTNSITNSASNSSLSLLVNNQTTNSNNSGGNIFEIPVLSCTDDSVLLLWKTNDPSFIFNQKTRKGDKILFKLTFDLLIQGFPDVVSISKDIAIKILSSESMPSATMPDGTSSSSMSNLLDKFKTHFKGESILSEPSIHAGSVFSINLTKSRQQEHQNRIGEMIDAHQENILKLGYAMKMEKLRQELDLREKLTNLKEKTIDSTNTDDVNAANGVAESSNSSTIDVEEIVKKMLLMNSTHQQQQQNFSSPSSTSPTLVNGESSPKSGRSSNTTSSSSGGGGGGGRKRSSTIVEVKVKEVPSSALLKEDETSGYLKKKSAFKEEWKPRWFVFKKPYLYYSHNQKDTHKLKKIDLTNSSVAITQDEVPFGFAIIQLRRVWLLQANSVEDRDKWVQTLDPLRKVTELKDEELRTAKQQIEKSSSQLDQIKSQLQTGQQIVLAKQKEIEELTNTISQLQLEKEINTQQFDGLRDEIQNRDEELEQYKSQQSQKINQLSGQVNKLENVTQEKELTIGSLSSTLNNTNQIIELINEQSKSYKNVAEMEIESLRDETTQLRETSQLLANRLKECRSSIQSAESLLSERDLEITQLKALLTQQEESSGITSLNLKNLQSDQTMKQGQIDILSKTVQQSTATIQNISSQLDSTTKASDSKDEQITSINSAYKDESDRLKDQTTQLNSLTTNLRQQMRSLEQTHLQQKETSASDQKTLLLLLHDMEQGLTRASQTITDQSAQVTVLKKQLEDSKKSNEQLPTVEKQLSLMKDRLIQSENQLIDRECENTILSDKLKLWEEEIKIKDSKLSLLENNVKEVRAEYANGMAFSREFSQHHTDSGSISGKFNRRSKQISAEEQMETLRESSIAHQSHNAFLNSQIQRLETEMRTQEKVYSDTIQRIKKDLQQRNQQNIAFMKHQVGDEIVKKMEDVTASMEILKKKYFVSLVVAAKLQNAMMGNICNVDAYELYEQSVVEHILDQDQWPNWIAQTISTQNKHL', 2205, 'Q9NGQ2; Q54F81;', 'KD00727', 'Dictyostelium discoideum (Slime mold)', 'kif1', '#Kinesin-related protein 1#Kinesin family member 1#Kinesin-3', '-', '-', '8627956'),
(728, 'Q9MBF8', 'Dynein-1-beta heavy chain; flagellar inner arm I1 complex', 'GO:0003777', 510667, 'Force generating protein of eukaryotic cilia and flagella. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for assembly of the I1 inner arm complex and its targeting to the appropriate axoneme location. Also required for phototaxis.', 'MEPGDEGKGHQLTADATCIAWVRSKLQLLKPESLGDSDGAEWLSSVWHNDVHTPVVSTFLMSVKATRMFAALDGGHEGGSSPKLVLALEVPKQFEQMVYFVRDPSKFVTRENVGSVIFFGVMRGGDPLHSLLNIMHGLYVPVVVANTTWPETVKSDFTAQMHKFMANLTETVYEVKGKTILYIPQEDLRDPKAAAKQKDLVQRLESTIIHWTRQVKELLNQQDSVDASEQAGPLAEIEFWRERSVDLSGIRAQLDDGAVSSIVSVLEYAKSSYLAPFLSLRNLIHREAVAAEDNLKFLLCLEEPCQQLASAHPQTIPSLLPPILNCIRMVWNLSRFYNTPERLSVLLRKLSNEIINRCCSVISLPDVWSGDVDNVMVALRQSMEAGERWKELYKRTAAAVAVRSPKPWDFDISSIFAHIDAFLQRCNDLLEVCEAQLQFAPRTPLPVFGGTYGPEVKKSILDIQESFQGLVQGLQALKYDILDVKATRWHDDFNGFKGGVKDLEVMMANVIQRAFDTQPCLAARGELLEGFQTMAKRDYIRRFVEKKTVEFFALFNAEINTVKKLFDAVKRSQPKSPILPRYAGLAKYAMNLMRRLEQSHKVVDSVRYTLPQVSEAADVMQQYELAHQAIEQYISNTHNDWFSTIESSIAKELQACLLTQDKASGGLLSMNFHKDLLSMGQEVHFWERMRLAVPLVAMEINAQREKYRVLRDNILMVVRDYNKILTALDKEERKLFHDRIRYLDRRIMPGVTKLQWTADKHALEFYYREARKFCRDADMAVGDYKTANSRLDAICRSISELVLVDVEKKKIYQHAEFANLQESHHAKIKDRLVSAVDEIRDIMASIHRVFEQDSEEVQREWVRFTQKVDRKLEDALRHVIKKSLQELSRLLNGDNKTEVMPIFHVTMVLERTNRVELRPTIQALFDTINSVARNLILVLQSVPRVALQLTDKQRRDMEDAGLPLPKPLPTLYETISADEDAVLRTIMQITSGITSIIDKVQAFLTYWEKKYRQVWEADRDAYIRRYEKAQKPLSSFEADISRYLQCIDEIRGEDGATNMRFLRIDCGPLKLTLVGHCEAWVSKFTGLLGQLAATELRTLHTYFRENKDSLMLAPSTLEQLAELVGLHRRLADERRRTEARFEPLRDKYKLLERYEVGAKEEEAALLEGLEPAWTQFQALLDETAGKLERYKDNFREKVKSLLDTFLKDVAQLCEDFSRDAPYSSEVPTPDALDFIQASKQADEDTRKRAAEIKNGMDIFNIPQPQYKDLAAMEKDLDFLDRIWGLKDEWEQLYYGWKDGSFTDIKVEEMEEAAVRIGKNVAKLGRDIRQWTVWSSLKDTLDAFKRTMPLITDLRNPAMRPRHWQNLQDHIGVRFDPHSRDFTLDSLVALRLDQHVEFVAELSVNATKELAIENNIKAIAATWSALGLDMAEYKSTFKLRSTEEIFTSLEENIVTLSTMKASKYFIVFEKDIAYWEKTLSHISETIEIILQVQRNWMYLENIFIGSEDIRKQLPQESQMFDAVHNNFMRLMKQLYSTANCLKACTAQGLLESFQDMNNKLERIQKSLDNYLENKRQQFPRFYFLSSDDLLEILGQAKDPLNVQPHLKKCFEGIKKLDMHLPGEDRKQTISVGITSPDGEYLPFANPVITEGRPEEWLNRVEDAMFLTTKKHLYKVLEESKAQKKEKWVKENQGQMIITAGQIVWTHECEKALADADSARKNLKLLKKKWISYLNKLTAVTRSKLNKIERNKVVALITIEVHARDVIEKLGKSNCSSTNDFEWVSQLRFYWDREKNDCIVKQVLSVFYYGYEYQGNNGRLVITPLTDRCYMTLGAAMFTRRGGNPLGPAGTGKTETVKDFGKALARYVIVFNCSDGVDYKMTGKMFSGLAQTGAWACLDEFNRIEVEVLSVVATQIAAVMQAIKESKKRFLFLGQEIRLNPSCGIFVTMNPGYAGRSELPDNLKAMLRPVSMMVPDFTLIAEIMMFSEGFSSAKVLAKKMIAIMELSQQQLSKQDHYDYGLRSFVIPIARAAGSLKRLDPEGSEEVILYRTMLDLIKPKLVYLDLPLFMALLSDLFPGVELPPADGGSLRRAIEAELRESNLQIVPEFVTKIIQVFDCKVARHGNMIVGRTGSGKSEAWKCLQRALGRLRKEEPDDDRFQKVHVHTINPLALSNDELYGCFEAATHEWQDGVLARIMRTVCKDETHEQKWILFDGPVDTLWIESMNTTLDDNKLLTLLSGERIAMTPAVSLLFEVEDLSQASPATVSRAGMIYLNVEDLGWRPFITSWLAAKQAAPGADAAIIDQVSKLVDKYMEAALEHKRLHCRELVPTDRLSCVRAFTRLWDALAVPENGVGTMPVDESAGPPGSKAAAAAAAAAAAAAPPEETSGGTGGNLVEMWFLFCLIWGIGGPLDEEGRKKFDAFMREMDTRYPSSDTVFEYFVEPKAKSWLAWETKLTGAFKPAMDQPFFKILVPTVDTVRNRFVGSALVRVSQHTLIVGNVGVGKTMIVGSLLEGLPGDRMSSMTINFSAQTSSNSLQDTIEGKLEKRTKGVFAPAGGKRLVCFIDDLNMPQKSKFGFIPPLELLKLWVDNGFWYDRAKCEVKHIKDMQLLAAMAPPGGGRNAFSQRVQACFATLNVTAPNDNQLKRIFGTILNAKLADFDDEVKPLSEPITMATIGIYRAVSKELLPTPSKSHYLFNTRDLAKIIQGMMQATKAFYNSKEEVLQLWCHECMRIIADRMWDHADKEWLVRQLDEKLGTTFSTSFGTLFEAYNETVPPFVTFMRQNVDVPVYEAVRDMVALKDLLTERLEDYALEPGHSAMDLVLFRDALSHVCRIHRILGQPRGNALLVGVGGSGRKSLARLAAFVAELKCFTIEITKNYRQTEFREDLKGLYRQAGVANKPTVFLFDETQIVYETFLEDVNNILTSGEVPNLFPKDELGSVLDELRPAAKAAGAGETADALYGFLLERVRTNLHVVLCLSPVGEAFRERCRMFPGLVNCTTIDWFTEWPADALFEVAQKQLMDVDLGSTEVKTAVCKVFVTAHQSVENTSAKMFAALKRRNYVTPTNYLETVRGYKGLLAEKRTELGEKAAKLQGGLHKLDETSVQVAAMKKVAEEKKVVVAQAKADCEELLVEIVQDKRVADEQEKQVNAEAQKIGKEAEEANIIAAQVQQELDKALPALREAEAALDVLTKKDMSELKAYAKPPEKVEMTLNAVLTVLRRPPNWDEAKKRLSDANFMQSLKEFDKDKLDDSLLKKIGKFTANPDFTYEKINTVSAAASGMCKWVHAMETYGYVAKDVAPKRAKLKSAQDTLARKQAALALAQEQLAVVLAKVQALKDKYDTSIARKQALEEELADLEGKLERAEKLVTGLAGERVRWEASISEYNIALGCLPGDVVVAAAFMSYAGPFPSEYRDELVKHTWLPQVKALNIPASEHFDFALFLANPAMVRDWNIQGLPSDSFSTENGVMVTRGRRWPLMIDPQGQANKWIKNMEGRGGRLKVLNLQMSDMARQIENAIQFGQPVLMQDILQEIDPILEPVLAKSFIKRGNQTLIKLGDKEVDYNFDFRLYLTTKLANPLYTPEISTKVMIVNFAVKEQGLEAQLLATVVKNERPDLDKQKNDLVVKVAAGKRTQAELEDTILHLLSTATGSLLDNVTLINTLDQSKTTWEEVNASLAVAEETQKKIEAASQLYRPCSVRASVLYFVLNDLSTIDPMYQFSLDAYNDLFLLSIKNSPKNDNLAERIKSLNDFHTYAVYKYTSRGLFERHKLLLSLQMCVRILQTANQVNTEEWQFFLRGGTVLDRSSQPNNPSQEWISEEAWDNITELDALPNFKGVVSSFESNLGEWEAWYRKGDPEASELPAEWESKCNELQRLILVRCLRPDRVIFAATTYVSNALGRKYVEPPVLDLAETLKDSTALSPLIFVLSAGVDPTDNLRKLATEKGMTSRFFTVALGQGQAPTATRLIEDGLREGNWVFLANCHLMTSWLPTLDKIIEGFETKQPHENFRLWLSSNPSPSFPIAILQRGIKMTTEPPKGLRANLLRLYNSVSDASYAQCKTQIKYQKLLFALTYFHSVLLERRKFRTLGFNIPYDFNDTDFSVSDDLLKSYLDSYEQTPWDALKYLIAEANYGGRVTDELDRRVLASYLNKFYCEDALAVPGYLLSPLSTYYVPENGPLQSFKDYILTLPAGDRPEAFGQHPNAEISYLIEDSKVLLDSLLSLQPRTEGAAGGAGTRREDVVMAIATDLLDQVPQPFNLEEVMKAKADDPSALHVVLFQEVERYNALLVAVRRSCVELQRGIKGLVVMSADLDLIFESLYAAKVPAAWLKTYPSLKPLGPWTRDLLQRIEQLATWVEETYPRVYWLSGFTYPTGFLTAVLQTTARKASVPIDTLSFEFSIINLDEREINAPPKEGVYIKGLFLEGAGWDFENGCLCEPNPMELIVPMPILLFRPVENKKRTAKGIYTCPLYLYPLRTGTRERPSFMINVDLRSGSADPDHWIMRGTALLLSLAT', 4513, 'Q9MBF8; Q9ZPC2;', 'KD00728', 'Chlamydomonas reinhardtii (Chlamydomonas smithii)', 'DHC10', '#Dynein-1-beta heavy chain; flagellar inner arm I1 complex#1-beta DHC#Dynein-1; subspecies f', '-', '-', '-'),
(729, 'Q9WV04', 'Kinesin-like protein KIF9', 'GO:0003777', 89898, '', 'MGTRKKVQAFVRVRPTDDFAHEMIKYGEDNKSIDIHLKKDTRRGVVNNQQTDWSFKLDGVLHNASQDLVYETVAKDAVSQALDGYNGTIMCYGQTGAGKTYTMTGATENYKHRGILPRALQQVFRMIEERPTHAITVRVSYLEIYNENLFDLLSTLPYVGPSVTPMTIVENPQGIFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYMEAHSRTLSDEKYITSKINLVDLAGSERLSKTGSEGRVLKEATYINKSLSFLEQAIIALGDQNRDHVPFRQSKLTHALKDSLGGNCNMVLVTNIYGEAAQLDETLSSLRFASRMKLVTTEPAINEKYDAERMVKNLEKELALLKQELAIHDSLSNRTLVNYDPMDEIQIAEINSQVRRYLEGTLDEIDIINLRQIQEVFNQFRVVLSQQEQEVESALRRKYTLIDKNDFAAISAVQKVGLMDIEGNLVGEPDGQSFGLGVAPFSVKPGKKPKTKKTPKDQFSSSARKEGASSPVSGKDFDVASISKTQLIPSSKDGDLKDMLARERETSSIEPLISDSPKEELRAPRPSTPPSRTVAFEEFKNERGSEINRIFKENKSILNERKKRASETTQRINAIKQEIDETKDALNFQKSLREKQGEYENKGLMIIDEEEFLLILKLKDLKKQYRNEYQELRDLRAEIQYCQRLVDQCRHRLLMEFDIWYNESFMIPEDVQVALKLGSSIRPGMVPISRIVCLGEDDQDRFSHLQQTVLPEGLDSITFYNAKVKTDQKHNYMKTMVGLQQSHRK', 790, 'Q9WV04; E9QMT7; O35070;', 'KD00729', 'Mus musculus (Mouse)', 'Kif9', '#Kinesin-like protein KIF9', '-', '-', '16578'),
(730, 'Q9YHY6', 'Condensin complex subunit 1', 'k', 154191, '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 topoisomerases. May target the condensin complex to DNA via its C-terminal domain. {ECO:0000269|PubMed:10428035; ECO:0000269|PubMed:9774278; ECO:0000269|PubMed:9852142}.', 'MTFHFHIPLAFRDLLKSGGIGQYVVQEVLPVRHVDAQFAAFQTSFRTEAPLCILQHFDTLYSILHHFRSLDIAIKEDVLEVMVKVASRHANELPAILEDLNLSVPQRAAHLNALKMNCFILTQLIEAFEAETYKASLGSVEPSGKGKKAKSKPEGFSWESERESILQALTHLLQLDIRRLWSMSVVEEEFVSMMTSCCYKMMENPNIVMAKNKSTREALGHLLGVTVKRYNHMLSASVKVIQLLQHFEHLASVLVHTVSLWATEYGMKPVIGEIMREIGQKCSQDLSRESSGFKAFATFLTELAERIPAIMMPSISVLLDYLDGENYMMRNSVLTVMGEMVVRVLSGDQLEEAEKSSRDQFLDTLQEHLHDVNTYVRSCVIQIYNRIVQEKALPLSRFQSVVTLVVGRLFDKSVNVCKNAIQLLASFLANNPFTCKLSSVDLKVPLEKETKKLKEMREKYQGPKPVVVISPEEEWEAMLPEVLEAFKILQQESKEEEDIETEEIESSQHLREQILILLRKTSYKNSIRLTQKGIERFQEDPLFSEGDSEAKSELGILEKIFTEKKADLEQPTTKDQDDAQVNPTSEELPSQEVQNSDMDKQEMLVQYLSDAHHFALKIEEAIDVISKMMYETAVSVVQEVIEFFVTVSQFGVSQALLGVRRMLPLVWSKEPGVREAVLSAYRRLYLSSNGESERVKAQALVRSLSLLMVDSSAGILQCLEEIVSEFVQKGDIHPSVIQLLWEKFTQKSPCSEFERRAAVMLLGMMTRGQPEIVMSNLDTLVSVGLGEQVQKDYQLAREVCNCILKITDSQKQTLGKSTEPFRLPKDHSLFVCLTEAVAGGIGLSGLHWLPFKETAVRLVYELGEEPEEICSEILLRCSQNVLDGHQTQDEVPNVPAFLLTHLLSLAGDVALQQVVHLERAVSAELRRRRVLKEEQEAEKVGKQRKSKANESTMEEELGLVGASADDIEAELIRKICDTELLGGQQYLSAFLPLILRICNNPGRYSDPDLCTVATLALAKYMMISSDFCDTHLRLLFTLLEKSPLPSVRSNIMIALGDLSIRFPNLIEPWTPNLYARLRDPSREVRKTAGMVMTHLILKDMVKVKGQVSEMAVLLIESDQEISALARNFFNELSNKGNAVYNLLPDIISRLSDPDCGVEEEAFRTIMKQLLSYITKDKQTESLVEKMCHRFRTARTERQWRDLAHCLSLLPFSEKGLRKMQDCFDCYGDKLSDEAVYNSFLTTVAKMRRGAKPELKALIDEFEQKLSRCHNKGLENMDVPEEPSAESDAQPPKAKRPPLASVNVKKGKSEDDFQTPKPPASRKSRRKVAVNFSSDEESDLEAELSEAETPKNPTPIRRTARSRAK', 1364, 'Q9YHY6; Q9YGS5;', 'KD00730', 'Xenopus laevis (African clawed frog)', 'ncapd2', '#Condensin complex subunit 1#Chromosome assembly protein XCAP-D2#Chromosome condensation-related SMC-associated protein 1#Chromosome-associated protein D2#Eg7#Non-SMC condensin I complex subunit D2', '-', '-', '398080'),
(731, 'Q9Y266', 'Nuclear migration protein nudC', 'k;m', 38243, 'Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation. {ECO:0000250; ECO:0000269|PubMed:12679384; ECO:0000269|PubMed:12852857}.', 'MGGEQEEERFDGMLLAMAQQHEGGVQELVNTFFSFLRRKTDFFIGGEEGMAEKLITQTFSHHNQLAQKTRREKRARQEAERREKAERAARLAKEAKSETSGPQIKELTDEEAERLQLEIDQKKDAENHEAQLKNGSLDSPGKQDTEEDEEEDEKDKGKLKPNLGNGADLPNYRWTQTLSELDLAVPFCVNFRLKGKDMVVDIQRRHLRVGLKGQPAIIDGELYNEVKVEESSWLIEDGKVVTVHLEKINKMEWWSRLVSSDPEINTKKINPENSKLSDLDSETRSMVEKMMYDQRQKSMGLPTSDEQKKQEILKKFMDQHPEMDFSKAKFN', 331, 'Q9Y266; Q5QP31; Q5QP35; Q9H0N2; Q9Y2B6;', 'KD00731', 'Homo sapiens (Human)', 'NUDC', '#Nuclear migration protein nudC#Nuclear distribution protein C homolog', '-', 'ENSG00000170584', '-'),
(732, 'Q10103', 'Chromo domain-containing protein 1', 'k', 108726, 'Component of the kinetochore which plays a role in stabilizing microtubules and so allowing accurate chromosome segregation. Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA- directed RNA polymerase (RDRC) complex. {ECO:0000269|PubMed:10835380; ECO:0000269|PubMed:14704433; ECO:0000269|PubMed:15607976; ECO:0000269|PubMed:9722643}.', 'MVSVKPLPDIDSNEGETDADVYEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKKRKKLIAKGLLEPFDAEDNEAKKMKREKEILRQQRQKRKSELTQLSQKVKEKFKKMRKKPARRIVTIANDEEEEDDQTMDEDAFERKSMQGELKERNLTDKTSTLSTSFGETSPDVNPFYLSEWPTVTDSILLSKSLSSDAIPLKNGEIKSTMLMPSDSDNSVPGIQNSNNLENTGAFVENANSPQSNTPLSTFRHSSPLSLSPVITSDNDVANSLFFSNSTPLPSSLKIKKEAPKLETHTILVSDNSGSLTKQDILSYFAFIKGNIEVFFLKSPKKDKVCNMAYIQFDSIEQAKLAYDKGHPSWHVTLVKGKISTDMEECKVSKSILKTTPSKKANARSVSFTQTTTDTLSESEKFASNVDLDENFDFNVNVTNEDAKQLKKSVIGSSWTTVNNDWNSVSKSDQTFENDGASKVVPAGNITLNSDNSLHHSISESEDLSSASTLSDYFRFVLRVGKSLYYAGELSFDISKLKAETEHQQLLRSLVSCKQVDVLRFVTSQYLEVFGTCLTKVLSGSLCIRSDVDMTHFKNILNRGNGAGIVLGSNYTLLLFTEDNNALMNLYDCQGQSNSPFWMVIFEPLESILVEWSAKNLRPKKPYHKSQSYLSYLLQLGHIDLHKIGAFQATQILIVSKQPSPEAEELEDTFREAAIPTFRGLEIPESLFLSQNVFVFLNVSLEDDFDQLQFLTLAKRKSCKFFLFGLSLPLKSPNDSHVGTDFKKNNEPLDKLTYSQYLRPMFPKGGVVSVTLSALIKTPRLLELISPFLEIKKDSWILILPPSIVDMVKSYFVTNNPDKSLLEIQNLLNTLQRYLTNPALKNVTLYQDWDIVIDDSADVSLASTLQLYQKKNYDKYRRFVLIHELKNELTPVNGLDIVDYDEFKETFMRAIGLK', 960, 'Q10103;', 'KD00732', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'chp1', '#Chromo domain-containing protein 1', '-', '-', '2542239'),
(733, 'Q8N954', 'G patch domain-containing protein 11', 'k', 30199, '', 'MAEEEDYMSDSFINVQEDIRPGLPMLRQIREARRKEEKQQEANLKNRQKSLKEEEQERRDIGLKNALGCENKGFALLQKMGYKSGQALGKSGGGIVEPIPLNIKTGKSGIGHEASLKRKAEEKLESYRKKIHMKNQAEEKAAEQFRMRLKNKQDEMKLEGDLRRSQRACQQLDVQKNIQVPREAWYWLRLEEETEEDEEEKEQDEDEYKSEDLSVLEKLQILTSYLREEHLYCIWCGTAYEDKEDLSSNCPGPTSADHD', 259, 'Q8N954; A8K0D9; B7Z2G4; B8ZZ44;', 'KD00733', 'Homo sapiens (Human)', 'GPATCH11', '#G patch domain-containing protein 11#Coiled-coil domain-containing protein 75', '-', 'ENSG00000152133', '-'),
(734, 'Q9CR46', 'Spindle and kinetochore-associated protein 2', 'GO:0000940', 13725, '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}.', 'MEAEVDKLELMFQKADSDLDYLQYRLEYEVKTNHPHSAGEKNAVTVLKELSAIKSRYQALCARFKAVSVEQKETKSCICATLNKTMTMIQELQKQTNLELTLLTEEEKAATEPLKSHMPD', 120, 'Q9CR46; B2KGY1;', 'KD00734', 'Mus musculus (Mouse)', 'Ska2', '#Spindle and kinetochore-associated protein 2#Protein FAM33A', '-', '-', '66140'),
(735, 'Q92376', 'Kinesin-like protein 1', 'GO:0000778===GO:0031134===c;k', 96337, 'Microtubule-dependent motor that is involved in microtubule organization in the mitotic spindle. {ECO:0000269|PubMed:8898367}.', 'MVIENTKDISINTGYKRQEDALNTDSEDLIYRPKKIIKTNQEDAVHDLKYENFVSKNHVLQSDINGKKRDSNRDKAAVVTAPIASTHESNYEESVSKFKESWLPQLKDLIESHKTICESTLAYESDQAMASSNTLKRIKDLKSKPKNIIQLERLHMLSNGEHRLLSKDETDDIESAYLNLRSHLQVQEQVYAEKDHEYSLQLQSYREAAEKAKQDILETKENLSSELSISNIQLKEAKERLEAANASYQKLRREHKELALYHEKKTHSLVCNLNGERKSFGDFVENEVKSYKHEYANICESLRRALVLIQGSCTEKILRFKEKILDLLEMKQQEENDRISHIEYENDLTVKKLKRRISELEMAVKEYESEKSYSEKEYEEKISSLRIELEDKLAEIDMLRNKLLKEEHKHHSTSEKLEELSKYVASIQDKERNNGQNALELQARIQQLERRNEDMYNKLLAEEIIRRKLHNDIQELKGNIRVFCRVRPLLPSEESEYCIADVLQFPDKDALEPQKLILKGPNVESSLGHTYDRNYEFSFDRVFAPESDNSSVFEEISQLIQSAIDGYNVSIFAYGQTGSGKTYTMSSQDGMIAMSIKHIFNYLSTLREKGWVYKLRGQFLEIYNETIYDLLNKAEMLKNPKHDIHHDEKERRTTVDNVSIIDFNEEDTVYKMLNRAGENRFIAATKANERSSRSHTVFMLYIDGENSRTKQICKGTLNLVDLAGSERLSYSQAVGDRLRETQAINKSLSCLGDVIHALGNASNSTTKEKSHIPYRNSKLTYLLKYSLGKGAKTLMFVNVSPLKSQFMDTLNSLRFATKVNDTKVGSIKHYKR', 832, 'Q92376; O42669;', 'KD00735', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'klp1', '#Kinesin-like protein 1', '-', '-', '2542655'),
(736, 'P46824', 'Kinesin light chain', 'GO:0003777', 58044, '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.', 'MTQMSQDEIITNTKTVLQGLEALRVEHVSIMNGIAEVQKDNEKSDMLRKNIENIELGLSEAQVMMALTSHLQNIEAEKHKLKTQVRRLHQENAWLRDELANTQQKFQASEQLVAQLEEEKKHLEFMASVKKYDENQEQDDACDKSRTDPVVELFPDEENEDRHNMSPTPPSQFANQTSGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLERTSGHDHPDVATMLNILALVYRDQNKYKEAANLLNDALSIRGKTLGENHPAVAATLNNLAVLYGKRGKYKDAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYDEVEKYYQRALDIYESKLGPDDPNVAKTKNNLAGCYLKQGRYTEAEILYKQVLTRAHEREFGAIDSKNKPIWQVAEEREEHKFDNRENTPYGEYGGWHKAAKVDSPTVTTTLKNLGALYRRQGMFEAAETLEDCAMRSKKEAYDLAKQTKLSQLLTSNEKRRSKAIKEDLDFSEEKNAKP', 508, 'P46824; Q9VU05;', 'KD00736', 'Drosophila melanogaster (Fruit fly)', 'Klc', '#Kinesin light chain#KLC', '-', '-', '39445'),
(737, 'Q9BZD4', 'Kinetochore protein Nuf2', 'GO:0000777===GO:0031262===c;k', 54304, '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. {ECO:0000269|PubMed:12438418; ECO:0000269|PubMed:14654001; ECO:0000269|PubMed:15062103; ECO:0000269|PubMed:15235793; ECO:0000269|PubMed:15239953; ECO:0000269|PubMed:15548592; ECO:0000269|PubMed:17535814}.', 'METLSFPRYNVAEIVIHIRNKILTGADGKNLTKNDLYPNPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVMYPHLMEGFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEGNSQKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRKMFKMST', 464, 'Q9BZD4; Q8WU69; Q96HJ4; Q96Q78;', 'KD00737', 'Homo sapiens (Human)', 'NUF2', '#Kinetochore protein Nuf2#hNuf2#hNuf2R#hsNuf2#Cell division cycle-associated protein 1', '-', 'ENSG00000143228', '-'),
(738, 'P38903', 'Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform', 'GO:0000776===GO:0031134===GO:0000780===c;k;m', 85335, '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. {ECO:0000269|PubMed:9154823}.', 'MMRGFKQRLIKKTTGSSSSSSSKKKDKEKEKEKSSTTSSTSKKPASASSSSHGTTHSSASSTGSKSTTEKGKQSGSVPSQGKHHSSSTSKTKTATTPSSSSSSSRSSSVSRSGSSSTKKTSSRKGQEQSKQSQQPSQSQKQGSSSSSAAIMNPTPVLTVTKDDKSTSGEDHAHPTLLGAVSAVPSSPISNASGTAVSSDVENGNSNNNNMNINTSNTQDANHASSQSIDIPRSSHSFERLPTPTKLNPDTDLELIKTPQRHSSSRFEPSRYTPLTKLPNFNEVSPEERIPLFIAKVDQCNTMFDFNDPSFDIQGKEIKRSTLDELIEFLVTNRFTYTNEMYAHVVNMFKINLFRPIPPPVNPVGDIYDPDEDEPVNELAWPHMQAVYEFFLRFVESPDFNHQIAKQYIDQDFILKLLELFDSEDIRERDCLKTTLHRIYGKFLSLRSFIRRSMNNIFLQFIYETEKFNGVAELLEILGSIINGFALPLKEEHKVFLVRILIPLHKVRCLSLYHPQLAYCIVQFLEKDPLLTEEVVMGLLRYWPKINSTKEIMFLNEIEDIFEVIEPLEFIKVEVPLFVQLAKCISSPHFQVAEKVLSYWNNEYFLNLCIENAEVILPIIFPALYELTSQLELDTANGEDSISDPYMLVEQAINSGSWNRAIHAMAFKALKIFLETNPVLYENCNALYLSSVKETQQRKVQREENWSKLEEYVKNLRINNDKDQYTIKNPELRNSFNTASENNTLNEENENDCDSEIQ', 757, 'P38903; D6W281;', 'KD00738', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'RTS1', '#Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform#PP2A; B subunit; B'' delta isoform#Protein RTS1#Protein SCS1', '-', '-', '854179'),
(739, 'C5DK07', 'Spindle pole body component KRE28', 'GO:0000777', 41242, '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}.', 'MADDPTINGLELQLNAAEEHATALTEEALQNQDLHYKEVVEQLKRSVEQLVEDNESLFTAVDLPPEVDPTCISGRILDLAQLTQQLKSTHLQQETLDNFLRYTISSTDILQLESESDERYASVSRAVSQLQDNDIIQLDSEVDQIKQDIRKAGQTIADQREALNELCLETGNLADECHTLLSELEEATRTREMVEKQAAVEVTNDHPVEEMYASWQSLKEELQQESHLRRHLNQLKQSKASLEAILGTKNGNEHKDTNVMQEYASYDAFIRFWISKFTNKEMENLEVFPRSNKFQFTHRGTDVVISLGPRGISRVELYGKGIPLEKIAAARKDVNEEASRGEELYMSINRIIDKIKEHTTVS', 362, 'C5DK07;', 'KD00739', 'Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284(Yeast) (Kluyveromyces thermotolerans)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '8292436'),
(740, 'P46825', 'Kinesin light chain', 'GO:0003777', 64452, '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.', 'MEVTQTVKSYRIKKIEEIGKMTALSQEEIISNTKTVIQGLDTLKNEHNQILNSLLTSMKTIRKENGDTNLVEEKANILKKSVDSIELGLGEAQVMMALANHLQHTEAEKQKLRAQVRRLCQENAWLRDELANTQQKLQMSEQKVATIEEEKKHLEFMNEMKKYDTNEAQVNEEKESEQSSLDLGFPDDDDDGGQPEVLSPTQPSAMAQAASGGCEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQGKYKEAANLLNDALGIREKTLGPDHPAVAATLNNLAVLYGKRGKYKDAEPLCKRALVIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVERYYQRALEIYQKELGPDDPNVAKTKNNLASAYLKQGKYKQAEILYKEVLTRAHEKEFGKVDDDNKPIWMQAEEREENKAKYKDGAPQPDYGSWLKAVKVDSPTVTTTLKNLGALYRRQGKYEAAETLEECALRSRKSALEVVRQTKISDVLGSDFSKGQSPKDRKRSNSRDRNRRDSMDSVSYEKSGDGDEHEKSKLHVGTSHKQ', 571, 'P46825;', 'KD00740', 'Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii)', '', '#Kinesin light chain#KLC', '-', '-', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(741, 'Q6C7C3', 'Probable kinetochore protein SPC24', 'GO:0000778===GO:0051455===GO:0031617', 21475, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MDPIDLLRDVAKSFSTNEEIASTERVSVDITRLSLFREAKLAEARDKLQDQIRQRDLCQESVAGDSTTSERTQHVHELEREKMRLARAINDLEETLNATQAATSKLNAELELVEKESQQPIESAVENDSSAALQLKLFRTLGVTFDAEKPEKYTKCMIRSNTTSNVATLDLNVKEYSGFFITNYIWDKL', 189, 'Q6C7C3;', 'KD00741', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'SPC24', '#Probable kinetochore protein SPC24', '-', '-', '2912075'),
(742, 'Q8TD57', 'Dynein heavy chain 3; axonemal', 'GO:0003777', 470771, '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}.', 'MGATGRLELTLAAPPHPGPAFQRSKARETQGEEEGSEMQIAKSDSIHHMSHSQGQPELPPLPASANEEPSGLYQTVMSHSFYPPLMQRTSWTLAAPFKEQHHHRGPSDSIANNYSLMAQDLKLKDLLKVYQPATISVPRDRTGQGLPSSGNRSSSEPMRKKTKFSSRNKEDSTRIKLAFKTSIFSPMKKEVKTSLTFPGSRPMSPEQQLDVMLQQEMEMESKEKKPSESDLERYYYYLTNGIRKDMIAPEEGEVMVRISKLISNTLLTSPFLEPLMVVLVQEKENDYYCSLMKSIVDYILMDPMERKRLFIESIPRLFPQRVIRAPVPWHSVYRSAKKWNEEHLHTVNPMMLRLKELWFAEFRDLRFVRTAEILAGKLPLQPQEFWDVIQKHCLEAHQTLLNKWIPTCAQLFTSRKEHWIHFAPKSNYDSSRNIEEYFASVASFMSLQLRELVIKSLEDLVSLFMIHKDGNDFKEPYQEMKFFIPQLIMIKLEVSEPIIVFNPSFDGCWELIRDSFLEIIKNSNGIPKLKYIPLKFSFTAAAADRQCVKAAEPGEPSMHAAATAMAELKGYNLLLGTVNAEEKLVSDFLIQTFKVFQKNQVGPCKYLNVYKKYVDLLDNTAEQNIAAFLKENHDIDDFVTKINAIKKRRNEIASMNITVPLAMFCLDATALNHDLCERAQNLKDHLIQFQVDVNRDTNTSICNQYSHIADKVSEVPANTKELVSLIEFLKKSSAVTVFKLRRQLRDASERLEFLMDYADLPYQIEDIFDNSRNLLLHKRDQAEMDLIKRCSEFELRLEGYHRELESFRKREVMTTEEMKHNVEKLNELSKNLNRAFAEFELINKEEELLEKEKSTYPLLQAMLKNKVPYEQLWSTAYEFSIKSEEWMNGPLFLLNAEQIAEEIGNMWRTTYKLIKTLSDVPAPRRLAENVKIKIDKFKQYIPILSISCNPGMKDRHWQQISEIVGYEIKPTETTCLSNMLEFGFGKFVEKLEPIGAAASKEYSLEKNLDRMKLDWVNVTFSFVKYRDTDTNILCAIDDIQMLLDDHVIKTQTMCGSPFIKPIEAECRKWEEKLIRIQDNLDAWLKCQATWLYLEPIFSSEDIIAQMPEEGRKFGIVDSYWKSLMSQAVKDNRILVAADQPRMAEKLQEANFLLEDIQKGLNDYLEKKRLFFPRFFFLSNDELLEILSETKDPLRVQPHLKKCFEGIAKLEFTDNLEIVGMISSEKETVPFIQKIYPANAKGMVEKWLQQVEQMMLASMREVIGLGIEAYVKVPRNHWVLQWPGQVVICVSSIFWTQEVSQALAENTLLDFLKKSNDQIAQIVQLVRGKLSSGARLTLGALTVIDVHARDVVAKLSEDRVSDLNDFQWISQLRYYWVAKDVQVQIITTEALYGYEYLGNSPRLVITPLTDRCYRTLMGALKLNLGGAPEGPAGTGKTETTKDLAKALAKQCVVFNCSDGLDYKAMGKFFKGLAQAGAWACFDEFNRIEVEVLSVVAQQILSIQQAIIRKLKTFIFEGTELSLNPTCAVFITMNPGYAGRAELPDNLKALFRTVAMMVPDYALIGEISLYSMGFLDSRSLAQKIVATYRLCSEQLSSQHHYDYGMRAVKSVLTAAGNLKLKYPEENESVLLLRALLDVNLAKFLAQDVPLFQGIISDLFPGVVLPKPDYEVFLKVLNDNIKKMKLQPVPWFIGKIIQIYEMMLVRHGYMIVGDPMGGKTSAYKVLAAALGDLHAANQMEEFAVEYKIINPKAITMGQLYGCFDQVSHEWMDGVLANAFREQASSLSDDRKWIIFDGPVDAIWIENMNTVLDDNKKLCLMSGEIIQMNSKMSLIFEPADLEQASPATVSRCGMIYMEPHQLGWKPLKDSYMDTLPSSLTKEHKELVNDMFMWLVQPCLEFGRLHCKFVVQTSPIHLAFSMMRLYSSLLDEIRAVEEEEMELGEGLSSQQIFLWLQGLFLFSLVWTVAGTINADSRKKFDVFFRNLIMGMDDNHPRPKSVKLTKNNIFPERGSIYDFYFIKQASGHWETWTQYITKEEEKVPAGAKVSELIIPTMETARQSFFLKTYLDHEIPMLFVGPTGTGKSAITNNFLLHLPKNTYLPNCINFSARTSANQTQDIIMSKLDRRRKGLFGPPIGKKAVVFVDDLNMPAKEVYGAQPPIELLRQWIDHGYWFDKKDTTRLDIVDMLLVTAMGPPGGGRNDITGRFTRHLNIISINAFEDDILTKIFSSIVDWHFGKGFDVMFLRYGKMLVQATKTIYRDAVENFLPTPSKSHYVFNLRDFSRVIQGVLLCPHTHLQDVEKCIRLWIHEVYRVFYDRLIDKEDRQVFFNMVKETTSNCFKQTIEKVLIHLSPTGKIVDDNIRSLFFGDYFKPESDQKIYDEITDLKQLTVVMEHYLEEFNNISKAPMSLVMFRFAIEHISRICRVLKQDKGHLLLVGIGGSGRQSAAKLSTFMNAYELYQIEITKNYAGNDWREDLKKIILQVGVATKSTVFLFADNQIKDESFVEDINMLLNTGDVPNIFPADEKADIVEKMQTAARTQGEKVEVTPLSMYNFFIERVINKISFSLAMSPIGDAFRNRLRMFPSLINCCTIDWFQSWPTDALELVANKFLEDVELDDNIRVEVVSMCKYFQESVKKLSLDYYNKLRRHNYVTPTSYLELILTFKTLLNSKRQEVAMMRNRYLTGLQKLDFAASQVAVMQRELTALQPQLILTSEETAKMMVKIEAETREADGKKLLVQADEKEANVAAAIAQGIKNECEGDLAEAMPALEAALAALDTLNPADISLVKSMQNPPGPVKLVMESICIMKGMKPERKPDPSGSGKMIEDYWGVSKKILGDLKFLESLKTYDKDNIPPLTMKRIRERFINHPEFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLREAEGKLAAQMQKLNQKRAELKLVVDRLQALNDDFEEMNTKKKDLEENIEICSQKLVRAEKLISGLGGEKDRWTEAARQLGIRYTNLTGDVLLSSGTVAYLGAFTVDYRVQCQNQWLAECKDKVIPGFSDFSLSHTLGDPIKIRAWQIAGLPVDSFSIDNGIIVSNSRRWALMIDPHGQANKWIKNMEKANKLAVIKFSDSNYMRMLENALQLGTPVLIENIGEELDASIEPILLKATFKQQGVEYMRLGENIIEYSRDFKLYITTRLRNPHYLPEVAVKVCLLNFMITPLGLQDQLLGIVAAKEKPELEEKKNQLIVESAKNKKHLKEIEDKILEVLSMSKGNILEDETAIKVLSSSKVLSEEISEKQKVASMTETQIDETRMGYKPVAVHSATIFFCISDLANIEPMYQYSLTWFINLYMHSLTHSTKSEELNLRIKYIIDHFTLSIYNNVCRSLFEKDKLLFSLLLTIGIMKQKKEITEEVWYFLLTGGIALDNPYPNPAPQWLSEKAWAEIVRASALPKLHGLMEHLEQNLGEWKLIYDSAWPHEEQLPGSWKFSQGLEKMVILRCLRPDKMVPAVREFIAEHMGKLYIEAPTFDLQGSYNDSSCCAPLIFVLSPSADPMAGLLKFADDLGMGGTRTQTISLGQGQGPIAAKMINNAIKDGTWVVLQNCHLAASWMPTLEKICEEVIVPESTNARFRLWLTSYPSEKFPVSILQNGIKMTNEPPKGLRANLLRSYLNDPISDPVFFQSCAKAVMWQKMLFGLCFFHAVVQERRNFGPLGWNIPYEFNESDLRISMWQIQMFLNDYKEVPFDALTYLTGECNYGGRVTDDKDRRLLLSLLSMFYCKEIEEDYYSLAPGDTYYIPPHGSYQSYIDYLRNLPITAHPEVFGLHENADITKDNQETNQLFEGVLLTLPRQSGGSGKSPQEVVEELAQDILSKLPRDFDLEEVMKLYPVVYEESMNTVLRQELIRFNRLTKVVRRSLINLGRAIKGQVLMSSELEEVFNSMLVGKVPAMWAAKSYPSLKPLGGYVADLLARLTFFQEWIDKGPPVVFWISGFYFTQSFLTGVSQNYARKYTIPIDHIGFEFEVTPQETVMENNPEDGAYIKGLFLEGARWDRKTMQIGESLPKILYDPLPIIWLKPGESAMFLHQDIYVCPVYKTSARRGTLSTTGHSTNYVLSIELPTDMPQKHWINRGVASLCQLDN', 4116, 'Q8TD57; O00437; O15437; O43326; Q3C0H2; Q8WUP9; Q9UEM3; Q9UEM5;Q9UG35;', 'KD00742', 'Homo sapiens (Human)', 'DNAH3', '#Dynein heavy chain 3; axonemal#Axonemal beta dynein heavy chain 3#HsADHC3#Ciliary dynein heavy chain 3#Dnahc3-b', '-', 'ENSG00000158486', '-'),
(743, 'Q10113', 'Microtubule integrity protein mal3', 'GO:0051315===k', 35094, 'May play a role in regulating the integrity of microtubules possibly by influencing their stability. Involved in an anchoring mechanism to maintain tea2 and tip1 at growing microtubule ends. Strongly stimulates the ATPase activity of tea2. {ECO:0000269|PubMed:15177031; ECO:0000269|PubMed:15665379}.', 'MSESRQELLAWINQVTSLGLTRIEDCGKGYAMIQIFDSIYQDIPLKKVNFECNNEYQYINNWKVLQQVFLKKGIDKVVDPERLSRCKMQDNLEFVQWAKRFWDQYYPGGDYDALARRGNRGPANTRVMNSSAGATGPSRRRQVSSGSSTPSMTKSSANNNNVSSTANTAAVLRAKQAQQQITSLETQLYEVNETMFGLERERDFYFNKLREIEILVQTHLTTSPMSMENMLERIQAILYSTEDGFELPPDQPADLTTALTDHDTNNVAEEAQMTDLKDSETQRVPSAPDFVHARLQSLEVDDDENITF', 308, 'Q10113;', 'KD00743', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mal3', '#Microtubule integrity protein mal3', '-', '-', '2542123'),
(744, 'P21691', 'Regulatory protein SIR1', 'k', 76933, 'Involved in the establishment; but not the maintenance; of heterochromatic silencing at the cryptic mating-type loci HMR and HML. Is recruited by interacting with the ORC1 subunit of the origin recognition complex (ORC); which binds to HML-I or HMR-E silencers; DNA elements that direct the formation of silent chromatin at the mating-type loci. Establishes transcriptional silencing by recruiting the three other SIR proteins; SIR2; SIR3; and SIR4; that function directly in silenced chromatin and establish repression. Also found in centromeric chromatin. Binds to and helps retain CAC1; a subunit of chromatin assembly factor I (CAF-I) at centromeric loci independent on the other SIR proteins. {ECO:0000269|PubMed:12134062; ECO:0000269|PubMed:8221892; ECO:0000269|PubMed:8622770}.', 'MLQINSRLAVIDGWLVDTVKRKPINFRSPEVRLLLPNDDDYKKLSQQNLVDWTRLKKDSNSVLVGVKSMELFKHIKLVLREFFLLEDGRIILKRIRSKLRYKVVKKLTCKCCRLYLPKWGTVYIHPMLKDKEKPLAGVCEFSLDVNPDREYPLIEINVSHQYIIIEGFLLYLNERRLYRWNDNNLRSQVGLTKWAHLRKTYNPVSLDILYSLNSNFYFVKDDLLFQLLGKRVFVKFCKVMENGKCGKAPLWYRVKRTTTAKATHIAYAISNSTAPDSFKSKNNDYRFIVREKPIVENTISNLDYSDIKKQQFTEAEVVKRKISADISQIENVHTQFNSQKEKNNIRVNKVSSEVLDQISKFPVSRVTLLLMSAGQDKNYIELVEELARRLEKICIEKTTQSLEEIRDTFQANPEMQASFDKEYYQSIEEYKITLELIKEDLLITLIKQMENMWAAEKKFSTEEEYVSPRFLVADGFLIDLAEEKPINPKDPRLLTLLKDHQRAMIDQMNLVKWNDFKKYQDPIPLKAKTLFKFCKQIKKKFLRGADFKLHTLPTEANLKYEPERMTVLCSCVPILLDDQTVQYLYDDSIIPEFEATSSYATKQSKCGRKMSLQMEPDLLFQEAIRRMRHLTAYDVLRRNYIAAFEELYMGNCND', 654, 'P21691; D6VXG2;', 'KD00744', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SIR1', '#Regulatory protein SIR1#Heterochromatin protein SIR1#Silent information regulator 1', '-', '-', '853976'),
(745, 'Q9VLD6', 'Borealin', 'GO:0032133===k;m', 34681, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of embryonic mitosis. The CPC complex has essential functions at the centromere for ensuring sister chromatid cohesion; recruitment of the CPC to kinetochores; and chromosome alignment and segregation. There is no function in meiotic histone phosphorylation or spindle formation. {ECO:0000269|PubMed:16224046}.', 'MPRTKIPKNSKRNREVANREEKVRLYELKMDSRLISIDSLETKFLSAVDHQVKTLLGQVQKELANLKMPEVLRLFEELDRFSDFKASDQTQLLASMSMSGSAIEGHAPSATGSRNDEEDSSIGASGGSILAAHTGSLLRSTKAMRTPGPLHSARARRARRSRSACGDLNILHSAKPPSISSSSSSSRNSRSKLRTPMASRAKAFSADRTPLKQKQMRSGSPTTPPMAFLRYPKPGEVALSKYGSPMVAQVMPDKFANVNIPIRNGVLSLRPKKLDADEVESNLLENLDEDTLNQIKTLHENLQMIVNKASQAVFK', 315, 'Q9VLD6; Q8I0R3;', 'KD00745', 'Drosophila melanogaster (Fruit fly)', 'borr', '#Borealin#Aurora borealis protein#Borealin-related', '-', '-', '34245'),
(746, 'P38907', 'Central kinetochore subunit CHL4', 'GO:0051382===GO:0000942===SCL===k', 52672, 'Component of the central kinetochore; which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle- microtubule attachments and proper chromosome segregation. {ECO:0000269|PubMed:9339342}.', 'MSNELRLEDNYVPTSDTLVVFKQLMKLPVTVLYDLTLSWFAKFGGSFDGDIYLLTETLDLLIEKGVRRNVIVNRILYVYWPDGLNVFQLAEIDCHLMISKPEKFKWLPSKALRGDGKPYVVKLQPAKFIENLQTDLAKIYHCHVYMFKHPSLPVLITRIQLFDSNNLFLSTPNIGSINKESLYNKLDKFQGKPLISRRPYYVAFPLNSPIIFHSVDKDIYARLVLQSISRTISERETIIFKPVQKIPVKSIHNIMTLLGPSRFAESMGPWECYASANFERSPLHDYKKHQGLTGKKVMVREFDDSFLNDDENFYGKEEPEIRRLRLEKNMIKFKGSANGVMDQKYNDLKEFNEHVHNIRNGKKNEDSGEPVYISRYSSLVPIEKVGFTLKNEINSRIITIKLKFNGNDIFGGLHELCDKNLINIDKVPGWLAGENGSFSGTIMNGDFQREQVAKGGLL', 458, 'P38907; D6VSN4;', 'KD00746', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CHL4', '#Central kinetochore subunit CHL4#Chromosome loss protein 4#Chromosome transmission fidelity protein 17#Minichromosome maintenance protein 17', '-', '-', '851841'),
(747, 'Q39493', 'Diatom spindle kinesin-1', 'GO:0003777', 70308, 'Involved in anaphase spindle elongation.', 'MNAANRRKSTSTVGITGRKDATRMKIEQMEKERKERRKTMMQRKEARKQEHMKNIEAGNPGDVDFIGLVEEWRREQENKIGDKSPPSLFASTNSNICIAVRKRPISDKERQKLDHDSVSCFQNKVWIHSAKLKVDGITKYLTHNSFQLDHTFGEDSTTEQIYLATTLPLVDHVVSTQGRATVFCYGQTGSGKTYTMNGIQQILAYDLYGQLAEHTDDLEITVAFFELYSGNVLDLLHGCQRCKLLEDGNGEVNITGLREVPAPTPEAFLQVIEEGHSLRTTQKTEANDASSRSHAICQVFLRDYGGNLRGKLGLVDLAGSERGSDTKQHNSQRRTESADINTSLLALKECIRALGQKSAHVPYRGSKLTLILKDCFSPDSKTTMVATVSPGASAADHSLNTLRYADRIKEQRVSSNGQRGKAAKASNREIMPSKERLMRIAAATEQADDQHSAFVQKMLAEHDQVQADANDYAFTEQVDEEEADDEEGDYEEESEDLDYEDSEGQDYEEAVESQYDHSQEAQEGEEELRRTVQAVFELEEALLNQHMSNIQANAEMLTQEGKLLQSVQAGGLSEDEMHNYAIQLAEFLDKKESLIYKLQSKLDEFQEQLAREQELARQVQLTQY', 624, 'Q39493;', 'KD00747', 'Cylindrotheca fusiformis (Marine diatom)', 'DSK1', '#Diatom spindle kinesin-1', '-', '-', '-'),
(748, 'Q4WNW3', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 34181, '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}.', 'MNSLVATPVPPHFYEYSRLSSPHPMSTPTHTPINRKRKADDDGNDHDGRMSASPTNSPAFTPRSLPAPRSFKRSRPNVSGRPLSLPRLLETLDTDALRGILRSMCERHPALADEVIHTSPRPSVSSALQVLRNYQSTLQNSFPLGGNPESDYAYNRVRQPLGNLLDALSDFTPHFLPPHETQASVSLSYLDGATDIIHALPRWHSPQNNIERDSAYDEICKAWILVIREAAKRGGGIQLQYGGWDQKLAKHNQNAGGRLQAAVNELGNSLGWMHGPDSQGYGSSTGGDLVSVREQLLSGTYGLGTPVKVGPW', 312, 'Q4WNW3;', 'KD00748', 'Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSA1100) (Aspergillus fumigatus)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '3509576'),
(749, 'Q9VLD7', 'Australin; isoform BCG17009-PAIP08034p1', 'k;m', 24564, '', 'MPRTKITARRQAQRQKADREEKVRLSQIKMDSALEKIDEMSKRYKQEVDNQIKVIRGRTDKQLLQMKMPEFLALGFKTFAEFQRAAIKPPTTRSLSISRGRTRTPQNALPPRLQAHSVDRALSGDTMSFVRWPRAGEMVLSKAGSPLAVQMRPDRYADVHIPTRGGVITVKPHKINTVKREVLMQLDENTLNQVKTLNANLGLIVDMANKLGKLKP', 216, 'Q9VLD7;', 'KD00749', 'Drosophila melanogaster (Fruit fly)', 'aust', '#Australin; isoform B {ECO:0000313|EMBL:AHN54289.1}#CG17009-PA {ECO:0000313|EMBL:AAF52756.1}#IP08034p1 {ECO:0000313|EMBL:AEN86882.1}', '-', '-', '34244'),
(750, 'P46822', 'Kinesin light chain', 'GO:0003777', 60225, '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.', 'MSNMSQDDVTTGLRTVQQGLEALREEHSTISNTLETSVKGVKEDEAPLPKQKLSQINDNLDKLVCGVDETSLMLMVFQLTQGMDAQHQKYQAQRRRLCQENAWLRDELSSTQIKLQQSEQMVAQLEEENKHLKYMASIKQFDDGTQSDTKTSVDVGPQPVTNETLQELGFGPEDEEDMNASQFNQPTPANQMAASANVGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAANLLNEALSIREKCLGESHPAVAATLNNLAVLFGKRGKFKDAEPLCKRALEIREKVLGDDHPDVAKQLNNLALLCQNQGKYEEVEKYYKRALEIYESKLGPDDPNVAKTKNNLSSAYLKQGKYKEAEELYKQILTRAHEREFGQISGENKPIWQIAEEREENKHKGEGATANEQAGWAKAAKVDSPTVTTTLKNLGALYRRQGKYEAAETLEDVALRAKKQHEPLRSGAMGGIDEMSQSMMASTIGGSRNSMTTSTSQTGLKNKLMNALGFNS', 540, 'P46822; Q18088; Q6BEW4; Q8I7M2; Q8TA80; Q95QV1;', 'KD00750', 'Caenorhabditis elegans', 'klc-2', '#Kinesin light chain#KLC', '-', '-', '178942'),
(751, 'Q9H0B6', 'Kinesin light chain 2', 'GO:0003777', 68935, '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}.', 'MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEDASPNEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGDNKPIWMHAEEREESKDKRRDSAPYGEYGSWYKACKVDSPTVNTTLRSLGALYRRQGKLEAAHTLEDCASRNRKQGLDPASQTKVVELLKDGSGRRGDRRSSRDMAGGAGPRSESDLEDVGPTAEWNGDGSGSLRRSGSFGKLRDALRRSSEMLVKKLQGGTPQEPPNPRMKRASSLNFLNKSVEEPTQPGGTGLSDSRTLSSSSMDLSRRSSLVG', 622, 'Q9H0B6; A8MXL7; B2RDY4; Q9H9C8; Q9HA20;', 'KD00751', 'Homo sapiens (Human)', 'KLC2', '#Kinesin light chain 2#KLC 2', '-', 'ENSG00000174996', '-'),
(752, 'Q7JNE1', 'Non-histone chromosomal protein ProdProliferation disrupterSD02315p', 'k;t', 39428, '', 'MNGKMDRRKKRTSSEQYQMYIDMMESDPIFATGRVPRDYDLNYLTKKWKELSDRLNKCSSGPTLTPEEWRKRLNDWKNTTRCKYRRSLLSTEKDISMTSVETRALDLFGKVPTTGGETMLNLKSEKDEHDDEMEELGQRTSVAFQKELQAAVEEAINDEVDEEEMVEEHVDHEDMMEENLAETGITASTTAVNTGGGTYRTIVVDNTSFEHVEEDPQTVQPHAVEYVTSRRPAAPVINPGTASSGNKLINGELPVKRMRTQPREQIIYEVKNAPRCISNMQAVPPLHSTKLEREPSSLTSALSSSDAQQIAHQLKRLADIKFETLQFEIARFKFNNPGFQYDPPSL', 346, 'Q7JNE1;', 'KD00752', 'Drosophila melanogaster (Fruit fly)', 'prod', '#Non-histone chromosomal protein Prod {ECO:0000313|EMBL:AAC32727.1}#Proliferation disrupter {ECO:0000313|EMBL:AAF57616.1}#SD02315p {ECO:0000313|EMBL:AAL13986.1}', '-', '-', '37187'),
(753, 'Q5B3B1', 'Probable kinetochore protein ndc80', 'GO:0000778===GO:0051315===GO:0031262', 84067, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSQDTGLFSIKRPRETLGSVQNFSSLPQPSSALKRTSSIGYQNPPFTSQHTRSMSLLNSVGRPQQPNFQRSSSGGFGADPGLSSVRRSVSSNVFHGTSAGRPSFAPGSMSSNPASQSLQRRSSVFSRPSTGGAMGHQSFFTQVPSAAGVPRDPRPLRDRSFQARIAQELLEYLTHNNFELEMKHSLGQNTLRSPTQKDFNYIFQWLYHRIDPGYRFQKAMDAEVPPILKQLRYPYEKGITKSQIAAVGGQNWPTFLGMLHWLMELAQMMDRFAMGEYDEACAEMGVDVSGDRIIFRFLTGAYHDWLQGGEEEDDDAAAQRLIPHIELMAQEFEKGNEKYVQEMQVLDAENRALRDQIEELEKNAPDMAKLDKQFRILEDDKRKFEDYIQNVQGKIEKYESRIAFLEDEIRKTESELQAAEEERAGLQASVDQQGLTIQDIDRMNTERDRLQRSLDDAVSRLEETHARVMAKESEASAKLEDLEELVKTYNTLGYQNSLIPSTAVNANGQEYELGLNVNERSFSTSQIGGIPSRISPEADRLLAEPFTGYHPAHLLNLDLRGIVRSNLQALRKEINERRKRGIDADLERRNLLDNIKEAMDEKRSEVEALEHKRRTAEEEFERLKEVTTTQKLASDAQIEKMEKELAKMRATMSESVQLMEQREMNTNIEYEQLTLRANALREELHTNVESMLNDVIRFKVHIQKGLEDYENFVVDEVEQELGGDTQLDEDAPMSTEEL', 738, 'Q5B3B1; C8V902;', 'KD00753', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'ndc80', '#Probable kinetochore protein ndc80', '-', '-', '2872769'),
(754, 'Q3V0Q1', 'Dynein heavy chain 12; axonemal', 'GO:0003777', 356231, '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}.', 'MSDPNKTAIAAEKEALNLKLPPIVQPPKNIGVDTPKQSELLKYRRSKEQQKKINQLVISGAKKSLDKTLDKRIPPLPEPDFPPTMTSEIKKRGLNYIFMKQCVENSPIVPIQSQWLDNMLMLVPEHLKEGEKSEELLGSLIDEVSMDYEKSMKRYLVQSVLVKPPVKWLEDEGGPLPESPEGLDYSNPWHSNFVQARSQILANLHIVHPTMKMLLELGYTAFAKIILLDLTGIRARGPIDCEALRNDLSIQARKSEEKIMNTWYPKVINLFTKKEALEGIKTEKLDSFYNCVSILMSNQLKDLLWRTVEEFIKLFDPRYLNRLPIFKMELTFDDDKMEFYPTFQDLEDVVLGLIERISETLQTVQTVPSWLSGTSSPVNLDTEIPEHVLQWALCTLRTAIQHNLEGAKAHHKTYVTKYNWLLDGTATKMIQRFQAENHTFDEYTEFIEKFFNLASEIMLLPQWAHYPMVRLDCEDLKIGLTNKARAFANILLNDIASKHRKENESICSEFEAIRDHALRVPETTEEMMELIAFVERARTVGILDLALRIQESKRQMSYFLDALLMSQEDLNLNATVLLWPTKITPVFDENDELIENAKHAKENELIAKREKLILEIEKESRRMEEFTEFAELDRMHQYVADVRQLQKRIQESEEAVQFINKEEELFKWELTKYPELEKLKVTIEPYQKFFNFVLKWQRTEKRWMDGGFLDLNGESMEADIDDFSREVFRTLKFFHAKQKKELQERRKAARKRSLMEEKPEEEPKENPTITMMRARHWKQMSEIVGYDLTPDSGTTLRKVLKLNLSPYLESFEVISAGASKEFSLERSMNAMIATWDDISFHISLYRDTGIGILSSVDEIQAILDDQIIKTQTMRGSPFIKPFENEIKAWEDRLIRIQETIDEWLKVQAQWLYLEPIFCSEDIMQQMPEEGRQFQTVDRHWKDIMKFCAKDPKVLAATSLTGLLEKLQNCNDLLEKIMKGLNAYLEKKRLFFPRFFFLSNDEMLEILSETKDPLRVQPHLKKCFEGIAKLEFLANLDIKAMYSSEGERVELIALISTTAARGAVEKWLIQVEDLMLRSIRDVIAASRLAYPESARKDWVREWPGQVVLCVSQMFWTSETQEIISGGTEGLKKYYKELQYQLNDIVELVRGKLSKQTRITLGALVTIDVHARDVVMDMIEMGVSHDTDFQWLAQLRYYWEYENARVRIINCNVKYAYEYLGNSPRLVITPLTDRCYRTLIGAFYLNLGGAPEGPAGTGKTETTKDLAKALAVQCVVFNCSDGLDYLAMGKFFKGLASSGAWACFDEFNRIELEVLSVVAQQILCIQRAIQQKLEAFVFEGTELRLNPNCFVAITMNPGYAGRSELPDNLKVLFRTVAMMVPNYALIAEISLYSYGFLNAKPLSVKIVMTYRLCSEQLSSQFHYDYGMRAVKAVLVAAGNLKLKYPNENEDILLLRSIKDVNEPKFLSHDIPLFNGITSDLFPGIKLPEADYKEFLECAHETCQTHNLQPVKFFLEKIIQTYEMMIVRHGFMLVGEPFAAKTEVLHVLADTLTLMNERNYGDEEKVMYRTVNPKSITMGQLFGQFDPVSHEWTDGIVANTFREFALAESPDRKWVVFDGPIDTLWIESMNTVLDDNKKLCLMSGEIIQMSPQMSLIFETMDLSQASPATVSRCGMIYLEPSQLGWEPLVASWLNSLKEPLSELEHQNLLKELFDWLVPPSLVFRRKKCKFLSLHDLSKYFKQVLIYYILVVSPKFSLKSNHYKIFFHQQASFIFSLIWSIGASCDTDGRLAFDAFLRTAVSGRNEEAPMPVSISKWECPFDEKGLVYDYMYELRNRGRWIHWNELIKSSDLEDKRAKIQDIIVPTMDTIRYTFLMDLSITSAKPLLFVGPTGTGKSVYVKDKLMNHLEKEKYFPFYVNFSARTSANQVQNIIMARLDKRRKGVFGPPMGKKCVIFIDDMNMPSLEKYGAQPPIELLRQFFDCGHWYDLKDTSKITLIDIELIAAMGPPGGGRNAVTPRFIRHFNICTINTFSDETMVRIFSSIMAFYLRTHAFSPEYFVLGNQIVSGTMEVYKQSMGNLLPTPAKSHYTFNLRDFSRVIRGCLLIEKDAIESKHTMIRLFVHEVLRVFYDRLINDEDRNWLFLLIKNVIKDHFKESFDTVFHHLRNGNAPVTEEDLRNLMFGDYMNPDLEGDDRVYIEIPDIHHFNEVVDQCLDEYNQTHKRRMNLVVFRYVLEHLSRICRILKQSGGNALLIGLGGSGRQSLTKLATSMAKMQIFQPEISKSYGMNEWREDIKGFLLLIIIWAVVESLSKILEKRLRYLNDHFTYNLYCNICRSLFEKDKLLFSFLLCANLLLAKKEIEYQELMFLLTGGVSLKSAEKNPDPDWLQDKSWEEICRASELPVFHGLREHFCNYIYLWEEIYDSKEPHNMKFPEPMDKTLNELQKIIILRCLRPDKITPAITNYVTDKLGKKFVEPPPFDLTKSYLDSNCTIPLVFVLSPGADPMASLLKFANDKSMSGNKFQAISLGQGQGPVASKMITAAIEEGTWVCLQNCHLAVSWMPTLEKICEDFSPETCNPTFRLWLTSYPSPKFPVTILQNGVKMTNEPPTGLRLNLLQSYLSDPISDTQFFKGCPGKELAWEKLLFGVCFFHALVQERKKFGPLGWNIPYGFNESDLRISVRQLQLFINEYDTIPFEAISYLTGECNYGGRVTDDWDRRLLLTMLADFYNSFIIENPHYKFSPSGNYYAPPKGTYDDYIEFIKKLPFTQEPEIFGLHENVDISKDLQQTKVLFESLLLTQGGAKQTGSSGSTDQVLLEITEDILTQLPNDFDIEAALKNYPVRYEESMNTVLVQEMERFNNLIRTIRNTLRDLKKAIKGLVVMDSALEALSGSLLIGKVPEMWAKRSYPSLKPLGSYITDFLARLKFLEDWFSSGKPSVFWISGFFFTQAFLTGAMQNFARKYTIPIDLLGYEFEVIPFDYSDTPPEDGVYIHGLYLDGARWDRFSGLLAEQYPKLLFDLMPIIWIKPNLKIEIVKIEAYICPLYKTSERKGTLSTTGHSTNFVIAMLLKTDQPTQHWIKRGVALLCQLDN', 3086, 'Q3V0Q1; Q8BVT4; Q8VHS7;', 'KD00754', 'Mus musculus (Mouse)', 'Dnah12', '#Dynein heavy chain 12; axonemal#Axonemal beta dynein heavy chain 12#Axonemal dynein heavy chain 12-like protein#Axonemal dynein heavy chain 7-like protein#Ciliary dynein heavy chain 12', '-', '-', '-'),
(755, 'A7TFD7', 'Spindle pole body component KRE28', 'GO:0000777', 43331, '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}.', 'METQAVKTIRDELRELENTVAQASDMVLSEQDHRNASAIREMTQSVIAMSKENSLISVSNEIDYNEEIGNLAIDPSLIDEKIKQSNNFVELLKLTHLEQEALDYFLRYTISSTNTLELESTSDPKFVSLENEVTELENKTLTEHRDKIQEAKKDISDKSKDLANKQDQINELCLGAANSVDECWKMLNELEDIHSQRDNDVKETLSQDTTTTSDLIEETYKEWSSLQTSLTELNNSKDELDQLIAFKNEKHKDNDSTKIRNANIKNKTITENVKMLKLLINFWESNFIVPGSKKSKLSNLEVYPQTKKFQFKCAEQYTVIIQLNQNGGSIKSIEIFENDGKSVQENKNLSSLILNKYKNPLSSYPIFQVINDIVEELK', 378, 'A7TFD7;', 'KD00755', 'Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294(Kluyveromyces polysporus)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '5547274'),
(756, 'Q922S8', 'Kinesin-like protein KIF2C', 'GO:0000777===GO:0003777===k', 81085, '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}.', 'MESLHARLFPGLSINIQRSNGLIHPANISTVNVEKSCVSVEWIEGGTTKGKEIDIDDVAAINPELLQLLPLRPKDSLPLQENVTVPKQKRKSVNSKIPALKEGLRSRSTRMSTVSEVRIPAQENEMEVELPVPTNSRKQFAIPSHPRASCSTVTELPLLMVSEEAEEQAHSTRSTSSANPGNSVRRKSCIVKEMEKMKNKREEKRAQNSELRIKRAQEYDSSFPNWEFARMIKEFRVTMECSPLTVTDPIEEHRICVCVRKRPLNKQELAKKEIDVISVPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNASKGIYAMASRDVFLLKNQPRYRNLNLEVYVTFFEIYNGKVFDLLNKKAKLRVLEDSRQQVQVVGLQEYLVTCADDVIKMINMGSACRTSGQTFANSNSSRSHACFQILLRTKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQPVQMETEVMEASSNGTSLTGNEEEELSSQMSSFNEAMTQIRELEERALEELREIIQQGPNWLELSEMTDQPDYDLETFVNKAESALTQQAKQAKHFSALREVIKALRLAMQLEEQASKQINSKKRHQ', 721, 'Q922S8; A2AE71;', 'KD00756', 'Mus musculus (Mouse)', 'Kif2c', '#Kinesin-like protein KIF2C#Mitotic centromere-associated kinesin#MCAK', '-', '-', '73804'),
(757, 'Q8NFH3', 'Nucleoporin Nup43', 'GO:0000777===k', 42151, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. {ECO:0000269|PubMed:17363900}.', 'MEEIYAKFVSQKISKTRWRPLPPGSLQTAETFATGSWDNEENYISLWSIGDFGNLDSDGGFEGDHQLLCDIRHHGDVMDLQFFDQERIVAASSTGCVTVFLHHPNNQTLSVNQQWTTAHYHTGPGSPSYSSAPCTGVVCNNPEIVTVGEDGRINLFRADHKEAVRTIDNADSSTLHAVTFLRTPEILTVNSIGQLKIWDFRQQGNEPSQILSLTGDRVPLHCVDRHPNQQHVVATGGQDGMLSIWDVRQGTMPVSLLKAHEAEMWEVHFHPSNPEHLFTCSEDGSLWHWDASTDVPEKSSLFHQGGRSSTFLSHSISNQANVHQSVISSWLSTDPAKDRIEITSLLPSRSLSVNTLDVLGPCLVCGTDAEAIYVTRHLFS', 380, 'Q8NFH3; B4E2F0; Q9H8S0;', 'KD00757', 'Homo sapiens (Human)', 'NUP43', '#Nucleoporin Nup43#Nup107-160 subcomplex subunit Nup43#p42', '-', 'ENSG00000120253', '-'),
(758, 'B4R1Z3', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25643, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAIIMAESSYERRVKALYEKQIRMEALEAKFIKKVYKFNSNLLDVKEAACRHQRKVGKLQKVLMERREELDKRVSFIEELDRELEATKLRDLAMKDRIKQQKMLARQRKNEIMESIHTLSKTTETYINQDALPARVKGVTVLRGDKRNQLIPFDLKSTDVEGLDSLCQHLESLNVDIAQWQQLISLAMDVAMESRAPTTPPKEAANCNSIIEIDLTSPTCHI', 222, 'B4R1Z3; Q64EW7;', 'KD00758', 'Drosophila simulans (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6728293'),
(759, 'Q6AXW0', 'Borealin', 'GO:0032133', 32099, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex; it may be required to direct the CPC to centromeric DNA (By similarity). {ECO:0000250}.', 'MAPKKRSSRGTRTNTLRSRKLASFLKDFDREVQVRTKQIESDRQTLLKEVENLYNIEVLRLPKALQVMKWLDYFALGGNRQALEEAATADRDITEINNLTAEAIQTPLKSVKKRKVIEVDEAIKEEEEDEEEEGGGGGGRKSHKNLRSARVKRCPPSKKRTQSIQGRSRSKRLSHDFVTPAMSRLEPSLVKPTPGMTPRFDSRVFKTPGLRTPAAKEQVYNISINGSPLADSKEISLSVPIGGGASLRLLASDLQRVDIAQLNPEALGNIKKLSSRLAQICSSIRTGR', 288, 'Q6AXW0;', 'KD00759', 'Rattus norvegicus (Rat)', 'Cdca8', '#Borealin#Cell division cycle-associated protein 8', '-', '-', '500545'),
(760, 'Q8NFH4', 'Nucleoporin Nup37', 'GO:0000777===k', 36708, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. {ECO:0000269|PubMed:17363900}.', 'MKQDASRNAAYTVDCEDYVHVVEFNPFENGDSGNLIAYGGNNYVVIGTCTFQEEEADVEGIQYKTLRTFHHGVRVDGIAWSPETRLDSLPPVIKFCTSAADMKIRLFTSDLQDKNEYKVLEGHTDFINGLVFDPKEGQEIASVSDDHTCRIWNLEGVQTAHFVLHSPGMSVCWHPEETFKLMVAEKNGTIRFYDLLAQQAILSLESEQVPLMSAHWCLKNTFKVGAVAGNDWLIWDITRSSYPQNKRPVHMDRACLFRWSTISENLFATTGYPGKMASQFQIHHLGHPQPILMGSVAVGSGLSWHRTLPLCVIGGDHKLLFWVTEV', 326, 'Q8NFH4; Q9H644;', 'KD00760', 'Homo sapiens (Human)', 'NUP37', '#Nucleoporin Nup37#p37#Nup107-160 subcomplex subunit Nup37', '-', 'ENSG00000075188', '-'),
(761, 'Q6ING5', 'Zw10 protein', 'k', 87796, '', 'FVTEVLANSGRLEKEDLGTKISRLSRRVDELKGEVCDMINKKYDEFLPSMQSAEDLVTQVHGLVSDVDVLKSRIETEVKSDLKVAVNEFTELKQQLEKNTLILGVLKQLQEFDSAIEKYNCALTGKNYISAARHLQKAHSCLKVLKSRKGCELKLLKSLGIELTVQKQNLLYHLGEEWQQLAVWKLPPSKENSSMEMILKTELHLCTLPSNDESATVPLLASVLQAFAILGELNTKLKFFSQLLLNYILKPLVSYPSLHAQMETQQQGVILRFESIETQLEHPPPAEVFIKLRLVFELLHKHLLDVPVEDSSQSGEKGMVVLAEVLGEMIWEEISEAIIKDCLVYSIPNNSSKLVQYEEVINATEEFENALKDMNYFKGDATDLLKYAQNVNAHFASKKCQDVIVMARNLMTSEIHNTVKITPDCKITVPVLPKSEGSEKMIKKENHLSQEAPGLENNVKLSQHTFALPTCRISESVQKLMELAYQTLSEATTSSKPCSIQLFYTVRNIFHLFYDVVPTYHKENLQKLPQLSAIHHNNCMYIAHHLLTLGHQFRYHLPSPLSDGAATFVDMVPGFRRLGTESFLAQMRSQKGDLLERLSNARNFSNIEDEDNYTAAHKTIRQVMHQLSRLGKVWQDVLPVAIYCKAMGTLLNTAIVEMISKITALEDISTEDGERLYSLCRTMIEEGPLLFTPMPEETKNKKYQEEVTLYVQKWMKFKEQMIILQASLQEIVDRWADGKGPLAVEFSPSEVKNLIRALFQNTERRAAALAKIK', 773, 'Q6ING5;', 'KD00761', 'Xenopus laevis (African clawed frog)', 'zw10', '#Zw10 protein {ECO:0000313|EMBL:AAH72316.1}', '-', '-', '-'),
(762, 'O14064', 'Protein bir1', 'GO:0034501===GO:0000778===GO:0032133===k;m', 112580, 'Seems to act in the pleiotropic control of cell division. Has a role in chromosome segregation by recruiting condensin and ark1 kinase to appropriate sites as the cell progresses through mitosis. Ark1 activity depends upon bir1 function and phosphorylation. Ark1 with bir1 function is required for full-scale association with kinetochores and formation of a complex with mad3. {ECO:0000269|PubMed:10571085; ECO:0000269|PubMed:11554922; ECO:0000269|PubMed:16199877}.', 'MKPITSSSKRRWNRFRREMCNYSKRLDTFQKKKWPRAKPTPETLATVGFYYNPISESNSEERLDNVTCYMCTKSFYDWEDDDDPLKEHITHSPSCPWAYILSSKNNPNQNPQAAALTKCREQTFVDKVWPYTNRPDYHCEPSVMAASGFVYNPTADAKDAAHCLYCDINLHDWEPDDDPYTEHKRRRADCVFFTWKDPNSLSPTKLSFLSTSNIDPEDLTEDNSILPVSPTRDSTKSHKTLNFSPSRKNNLNARPLTMSLYTNTSEEKDSQPTRAPQSPTKPVLLTAPRRKNKSPKKSKPAVFKPVKPIFSDEDEDDDDLTASQPFSKGICNDSMQVAKKNFTEEIPLKEDEKDNELEHLVSPATSVHTTVSDITGHQSVTDESDEQNNCMSTPPKIEIESKIEEEISVVSKSKEISSSVSSVGKEQNHTEKQVAIETPEQQKVEKEDEHLNLQGSFIEESTKQPISSKPSTSSPDMTDAATGGRVSSSSFRDKILQTNFSPRSTIDSFSNISKKRNSEEANDENDETNLKIPIPEKKRKFQEVLQSKNILVSSTEDSHEPVKVTEDSQTAIHVSKFEDLENKSMESEQSLQLLSESENDDKPLIDLIPLLAIKRKDNLVSGVLEKGKSTSTSKTKFDTSIVDFIEKPKTEISEVLPEEKRKAICDESQTVRVSIDRGVTKTRDVSSPVSDEKSENVNHEEANSGHTVMNVHSSLDPQPIVQPNELESGSYLKDLPDRNVGNSEKVTFQEDDINSPKLQSKNNQTVEAVNTETSDKLQEKEANHELENIEKIEEKLTEVDKVSLSDAFPDQEIKNSRTSVQNGTRSVSKNTPEKETKVDKIDNVSKKDVETSPGSCETSSAFAKTYAEKEVTSINLPSVRKPLDESYYDHSISPFDPLCQSSFLAPQTPVKSKHALPLVEANAPPWEPIDFSSLLESPVPNPVEPNKLSEKELDMTVEQWIKFMYAKCAKEFEEACEEKIEWLLEEGKRAEEYIQNL', 997, 'O14064; Q9USG4; Q9UTZ0;', 'KD00762', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'bir1', '#Protein bir1#Chromosome segregation protein cut17', '-', '-', '2538875'),
(763, 'Q8MJ46', 'Serine/threonine-protein phosphatase PP1-gamma catalytic subunit', 'GO:0000777', 37015, '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. Dephosphorylates RPS6KB1. 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 (By similarity). {ECO:0000250}.', 'MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECVSINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGETDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPLRGMITKQAKK', 323, 'Q8MJ46;', 'KD00763', 'Canis familiaris (Dog) (Canis lupus familiaris)', 'PPP1CC', '#Serine/threonine-protein phosphatase PP1-gamma catalytic subunit#PP-1G#3.1.3.16#Protein phosphatase 1C catalytic subunit', '-', '-', '403557'),
(764, 'Q2V2P8', 'Uncharacterized protein YDR374W-A', 'GO:0000776', 10244, '', 'MDTEALANYLLRQLSLDAEENKLEDLLQRQNEDQESSQEYNKKLLLACGFQAILRKILLDARTRATAEGLREVYPYHIEAATQAFLDSQ', 89, 'Q2V2P8; D6VT06;', 'KD00764', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'YDR374W-A', '#Uncharacterized protein YDR374W-A', '-', '-', '3799971'),
(765, 'Q8C0X4', 'Putative uncharacterized protein', 'k', 110038, '', 'MSWALEEWKEGLPSRALQKIQELEGQLEKLKKEKQQRQFQLDSLEAALQKQKQKVEDGKTEGADLKRENQRLMEICEHLEKSRQKLSHELQVKESQVNLQESQLSSCKKQIEKLEQELKRCKSEFERSQQVAQSADVSLNPCSTPQKLFATPLTPSSTYEDLKEKYNKEVEERKRLEEEVKALHAKKVSLPFSQATMNHRDIARHQASSSVFPWQQENTPSRLSSDALKTPLRRDGSAAHFLGEEVSPNKSSMKTGRGDCSSLPDLKSKMTELELRLQGQEKEMRSQVNKCQDLQVQLEKTKVELIEKERILNKTRDEVVRSTAQYDQAAAKCTTLEQKLKTLTEELSCHRQNAESAKRSLEQRIKEKEKELQEELSRQHQSFQALDSEYTQMKTRLTQELQQVKHLHSTLQLELEKVTSVKQQLERNLEEIRLKLSRAEQALQASQVAENELRRSSEEMKKENSLIRSQSEQRTREVCHLEEELGKVKVSLSKSQNFAEEMKAKNTSQEIMLRDLQEKLNQQENSLTLEKLKLALADLERQRNCSQVLLKKREHHIDQLNNKLNKIEKEFETLLSALELKKKECEELKEEKNQISFWKIDSEKLINQIESEKEILLGKINHLETSLKTQQVSPDSNERIRTLEMERENFTVEIKNLQSMLDSKMVEIKTQKQAYLELQQKSESSDQKHQKEIENMCLKANKLTGQVESLECKLQLLSSEVVTKDQQYQDLRMEYETLRDLLKSRGSSLVTNEDNQRSSEDNQRSSEDNQRGSLAFEQQPAVSDSFANVMGRKGSINSERSDCSVDGGRSPEHIAILQNRVTSLESSLESQNQMNSDLQMRCEELLQIKGEVEENLSKAEQIHQNFVAETNQCISKLQEDAAVHQNIVAETLATLESKEKELQLLKEKLEAQQTEVQKLNKNNCLLEGTLKELQLLSDTLSSEKKEMNSIIS', 952, 'Q8C0X4;', 'KD00765', 'Mus musculus (Mouse)', 'Cenpf', '#Putative uncharacterized protein {ECO:0000313|EMBL:BAC26488.1}', '-', '-', '-'),
(766, 'O22806', 'Mitotic spindle checkpoint protein BUBR1', 'GO:0000777===GO:0005828===SCL', 45374, 'Essential component of the mitotic checkpoint. Required for normal mitosis progression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions may be to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C (By similarity). {ECO:0000250}.', 'MAAETKVQVSDPEAEFLNSKQETGYEWELFKENVRPLKRGRNVGILNHALKSHSDHQLRKNLIEKRRNLIEAIDEYEGDDPLSPWIECIKWVQEAFPPGGECSGLLVIYEQCVRKFWHSERYKDDLRYLKVWLEYAEHCADAEVIYKFLEVNEIGKTHAVYYIAYALHIEFKNKVKTANEIFNLGISRDAKPVEKLNDAYKKFMVRTMRRSNTADEEPKENNDLPSRSFGTLLSRGDNNARRQALGSSNPQAKKLKPNQSSKTPFAIYADAVSDTTSGNQPESDKSRPEFGSWLMLGGRAERNKENNSLPRKWASFKVPQKPIVRTVAAASASTFEVFVDEEECTEEEEEKKKNDETISSSSNVLPLNGGREIKKETELLRQNPLRHFPPNSFLR', 395, 'O22806; F4IFV2; Q8L9V1;', 'KD00766', 'Arabidopsis thaliana (Mouse-ear cress)', 'BUBR1', '#Mitotic spindle checkpoint protein BUBR1#BUB1-related protein 1', '-', '-', '817921'),
(767, 'O75935', 'Dynactin subunit 3', 'GO:0000777===SCL===c;k;m', 21119, 'Together with dynein may be involved in spindle assembly and cytokinesis. {ECO:0000269|PubMed:9722614}.', 'MAGLTDLQRLQARVEELERWVYGPGGARGSRKVADGLVKVQVALGNISSKRERVKILYKKIEDLIKYLDPEYIDRIAIPDASKLQFILAEEQFILSQVALLEQVNALVPMLDSAHIKAVPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAATQVKPAEE', 186, 'O75935; A6NII7; B2RBM5; Q5T1I5; Q5T1I7; Q5T8G3; Q9BPU8;', 'KD00767', 'Homo sapiens (Human)', 'DCTN3', '#Dynactin subunit 3#Dynactin complex subunit 22 kDa subunit#p22', '-', 'ENSG00000137100', '-'),
(768, 'Q8WXX0', 'Dynein heavy chain 7; axonemal', 'GO:0003777', 461159, '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}.', 'MSSEQDKSASKEKSKKPVRFLPQLSMEKLASKEKFKAPARALPQLSMVSTKPHWQQAAPSFHLSVKQDDESPEPFSVKNEQSHAEYMERFGKKGKLPHQVDDSYVGPSTSKSKGKSPHKERENFRSTLVNVIMQQDADLDSAVPDGSTIPKPTASAIEKDILRYYYYIHHGIDTDHVAPMEDSWLEHVLDLVPQHLKVFTDSIVTLSDEMREDYLLSVRKSIVDFVLKDPREKGDDKKTDELPAHRAEMEILPKPWRKSFLAASSYIRDHLNAMNPTMLAVLDLWHTNFKKLRLVDIKEFHNCQDALELSSFQNIIMRHMDSAKETLLKMWFPEVQNIYYQGNKKKQLPTGDSSAKLESFFNCAAALMTLQLQDLTLVSMQDFTDLIAQPPDSVRAFEHPGFIMRLILDNDTIKFEPELSDYIDIFLNVYDVMIKAVSFVPRVETKLYSKWESKSKPTTLKPIILNEIVDAHKEKIKEVIMKESVAPTEHLRLYDKYDFLITRKAERDVDNFLAENHSYEKIIDEICKYQKLIEEIQYTSIKTIRLGMFEMHCEELIRALVKRADIICGKLLAKMFRDHQEVNTRLCDEFERIAEKALSTPPNTAELMEMKAYIQKVEVTDMIELEQRLVDSKNCLAFLIEYVNFSPADMRLNNSVFQWYGRMGEIFEEHRKIIKEKIEQYQEGLKLRCERFVEELESYAKQSEEFYSFGDLQDVQRYLKKAQILNGKLDLAADKIEQFNAEEEAFGWLPSVYPQRKKIQDGLNPYLRLYETAVEFSSNYRAWTEGPYHKVNPDQVEADIGNYWRGLYKLEKTFHDSPYALAMTKKVRSKVEDFKQHIPLIQVICNPGLRPRHWEAMSAIVGYPLQPSDDSTVSSFLDMNLEPYIDRFEGISEAASKEYSLEKAMEKMITEWDAVEFVIHSYRETGTFILASVDEIQMLLDDHIIKTQTMRGSPFIKPYEKQMREWEGKLLLLQEILDEWLKVQATWLYLEPIFSSPDIMSQMPEEGRRFTAVDKTWRDIMRSVMQDKHVLTVVTIDRMLERLKKSNELLELILKGLNEYLEKKRLFFPRFFFLSNDELLEILSETKDPTRVQPHLKKCFEGIAKVEFTETLDITHMKSSEGEVVELIEIISTAKARGQVEKWLVELERVMINSIHKVTGDATFAYTKYERINWVRDWPGQTVLCVSQIFWTKEVQTAIPMGIKALEQYLKTCNRQIDDIVTLVRGKLSMQNRVTLGALVVLDVHARDVLSSLVKKNISDDSDFEWLSQLRYYWQENHLETKMINAGLRYGYEYLGNSPRLVITPLTDRCYRTLFGALHLHLGGAPEGPAGTGKTETTKDLAKAVAKQCVVFNCSDGLDYLALGKFFKGLLSCGAWACFDEFNRIDLEVLSVVAQQILTIQRGINAGADILMFEGTELKLDPTCAVFITMNPGYAGRSELPDNLKALFRTVAMMVPDYAMIAEIVLYSCGFVTARPLSVKIVATYRLCSEQLSSQHHYDYGMRAVKSVLTAAGNLKLKYPNENEEILLLRSIIDVNLPKFLSHDLPLFEGITSDLFPGVKLPKPDYNDLLAAIKDNCASMNLQMTAFFSEKILQVYEMMIVRHGFMIVGEPFGGKTSAYRVLAGALNDICEKGLMEENKVQITVLNPKSVTMGQLYGQFDSVSHEWSDGVLAVSFRAFASSVTPDRKWLIFDGPVDAVWIENMNTVLDDNKKLCLMSGEIIQMSPQMNLIFEPMDLEVASPATVSRCGMIYMEPHMLGWRPLMLSWVNLLPASVSVIQKEFIMGLFDRMVPVSVEFIRKHTKELSPTSDTNLVRSLMNLIDCFMDDFADEVKLKERNDRETYSLLEGIFLFSLIWSVGASCTDDDRLKFNKILRELMESPISDRTRNTFKLQSGTEQTSSKALTVPFPEKGTIYDYQFVTEGIGKWEPWIKKLKEAPPIPKDVMFNEIIVPTLDTIRYSALMELLTTHQKPSIFVGPTGTGKSVYITNFLLNQLNKEIYKPLLINFSAQTTAAQTQNIVMSKLDKRRKGVFGPPLGKRMVVFVDDVNMPAREVYGAQPPIELLRQWLDHWNWYDLKDCSMIKLVDIQIMCAMGPPGGGRNPVTPRYMRHFNIITINEFSDKSMYTIFSRILTWHLEICYKFPDEFLDLTTQIVNGTMTLYKEAMKNLLPTPAKSHYLFNLRDFSRVIQGVCLSRPETTETTEVIKRLWVHEVLRVYYDRLLDNTDRSWLINYIQEILRNYMYEDFHELFQRLDFDNDGMVEADDLRSLMFCDFHDPKREDTNYREIADVDNLRMIVEIHLEEYNNISKKPMNLVLFRFAIEHISRISRILKQPRSHALLVGVGGSGRQSVTRLAAHMADYSVFQVEISKGYDTTEWHEDLKVILRKCAEGEMQGVFLFTDTQIKEESFLEDVSNLLNAGEIPNLFALDEKQEICDKMRQLDRQRDKTKQTDGSPIALFNMFIDHCRSQLHVVLAMSPIGDAFRNRLRKFPALVNCCTIDWFQSWPEDALQAVASRFLEEIEMSEEIRDGCIDMCKSFHTSTIDLSKSFFVELQRYNYVTPTSYLELISTFKLLLEKKRSEVMKMKKRYEVGLEKLDSASSQVATMQMELEALHPQLKVASKEVDEMMIMIEKESVEVAKTEKIVKADETIANEQAMASKAIKDECDADLAGALPILESALAALDTLTAQDITVVKSMKSPPAGVKLVMEAICILKGIKADKIPDPTGSGKKIEDFWGPAKRLLGDMRFLQSLHEYDKDNIPPAYMNIIRKNYIPNPDFVPEKIRNASTAAEGLCKWVIAMDSYDKVAKIVAPKKIKLAAAEGELKIAMDGLRKKQAALKEVQDKLARLQDTLELNKQKKADLENQVDLCSKKLERAEQLIGGLGGEKTRWSHTALELGQLYINLTGDILISSGVVAYLGAFTSTYRQNQTKEWTTLCKGRDIPCSDDCSLMGTLGEAVTIRTWNIAGLPSDSFSIDNGIIIMNARRWPLMIDPQSQANKWIKNMEKANSLYVIKLSEPDYVRTLENCIQFGTPVLLENVGEELDPILEPLLLKQTFKQGGSTCIRLGDSTIEYAPDFRFYITTKLRNPHYLPETSVKVTLLNFMITPEGMQDQLLGIVVAQERPDLEEEKQALILQGAENKRQLKEIEDKILEVLSSSEGNILEDETAIKILSSSKALANEISQKQEVAEETEKKIDTTRMGYRPIAIHSSILFFSLADLANIEPMYQYSLTWFINLFILSIENSEKSEILAKRLQILKDHFTYSLYVNVCRSLFEKDKLLFSFCLTINLLLHERAINKAEWRFLLTGGIGLDNPYANLCTWLPQKSWDEICRLDDLPAFKTIRREFMRLKDGWKKVYDSLEPHHEVFPEEWEDKANEFQRMLIIRCLRPDKVIPMLQEFIINRLGRAFIEPPPFDLAKAFGDSNCCAPLIFVLSPGADPMAALLKFADDQGYGGSKLSSLSLGQGQGPIAMKMLEKAVKEGTWVVLQNCHLATSWMPTLEKVCEELSPESTHPDFRMWLTSYPSPNFPVSVLQNGVKMTNEAPKGLRANIIRSYLMDPISDPEFFGSCKKPEEFKKLLYGLCFFHALVQERRKFGPLGWNIPYEFNETDLRISVQQLHMFLNQYEELPYEALRYMTGECNYGGRVTDDWDRRTLRSILNKFFNPELVENSDYKFDSSGIYFVPPSGDHKSYIEYTKTLPLTPAPEIFGMNANADITKDQSETQLLFDNILLTQSRSAGAGAKSSDEVVNEVASDILGKLPNNFDIEAAMRRYPTTYTQSMNTVLVQEMGRFNKLLKTIRDSCVNIQKAIKGLAVMSTDLEEVVSSILNVKIPEMWMGKSYPSLKPLGSYVNDFLARLKFLQQWYEVGPPPVFWLSGFFFTQAFLTGAQQNYARKYTIPIDLLGFDYEVMEDKEYKHPPEDGVFIHGLFLDGASWNRKIKKLAESHPKILYDTVPVMWLKPCKRADIPKRPSYVAPLYKTSERRGVLSTTGHSTNFVIAMTLPSDQPKEHWIGRGVALLCQLNS', 4024, 'Q8WXX0; B8ZZX8; O00433; O95492; Q4G152; Q53QX7; Q53S64; Q53T02;Q68CY5; Q8N1Z2; Q9UMS3; Q9Y2F3;', 'KD00768', 'Homo sapiens (Human)', 'DNAH7', '#Dynein heavy chain 7; axonemal#Axonemal beta dynein heavy chain 7#Ciliary dynein heavy chain 7#Dynein heavy chain-like protein 2#hDHC2', '-', 'ENSG00000118997', '-'),
(769, 'Q759T0', 'Dynein light chain 1; cytoplasmic', 'GO:0005868', 10048, '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 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}.', 'MSKPAILKASDITDELRDEIFGISVQAVEQFQLEREVAAYIKKELDSKHGQTWHVIVGKNFGSYVTHEKGHFIYFYIGPLAFLVFKTA', 88, 'Q759T0;', 'KD00769', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DYN2', '#Dynein light chain 1; cytoplasmic', '-', '-', '4620451'),
(770, 'Q08446', 'Protein SGT1', 'GO:0051382===k', 44860, 'Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Required for both entry into S phase and kinetochore function. Also involved in cyclic AMP (cAMP) pathway; possibly by participating in the assembly or the conformational activation of specific multiprotein complexes. {ECO:0000269|PubMed:10445024; ECO:0000269|PubMed:12456005}.', 'MPVEKDLKTAYKALYDEKEPLKALHLYDEILKGSPTNLTALIFKAACLEKLYFGFSDWHSDATMENAKELLDKALMTAEGRGDRSKIGLVNFRYFVHFFNIKDYELAQSYFKKAKNLGYVDDTLPLWEDRLETKLNKKNKKQKDSTNKHTIKPVESIENRGDNNSSHSPISPLKIETAPQESPKFKIDWYQSSTSVTISLFTVNLPESKEQVNIYISPNDRRTLSISYQVPKSGSEFQYNAKLSHEVDPKAVSLKIFPKKLEITLSKIDSTQWKKLEEDILTESSRLSDEGKNSDSATRLLSAETASKERLSYPSSSKKKIDWSKLDIDEEADEEAGSADSFFQKLYAGADPDTKRAMMKSFIESNGTALSTDWEDVSKGTVKTSPPEGMEPKHW', 395, 'Q08446; D6W2C0; E9P8U7;', 'KD00770', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SGT1', '#Protein SGT1#Suppressor of G2 allele of SKP1', '-', '-', '854222'),
(771, 'Q9CQU5', 'ZW10 interactor', 'GO:0000776===GO:0000777', 28713, 'Part of the MIS12 complex; which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase (By similarity). {ECO:0000250}.', 'MADAEKNAVAEKNNAVATKEVLAEAAAILEPVGLQEEAELPAKIMEEFMRNSRKKDKLLCSQLQVVNFLQTFLAQEDTEQSPDALASEDASRQKATETKEQWKDMKATYMDHVDVIKCALSEALPQVKEAHRKYTELQKAFEQLEAKKRVLEEKLQLAQKQWVLQQKRLQNLTKISAEVKRRRKRALEKLDGSHQELETLKQQAGQEQEKLQRNQSYLQLLCSLQNKLVISEGKAEDKDVKGRALTAKSKSP', 252, 'Q9CQU5; Q3UYT8; Q91VI4; Q9D0W9;', 'KD00771', 'Mus musculus (Mouse)', 'Zwint', '#ZW10 interactor#ZW10-interacting protein 1#Zwint-1', '-', '-', '52696'),
(772, 'Q9Y2Z0', 'Suppressor of G2 allele of SKP1 homolog', 'GO:0000776===k', 41024, 'May play a role in ubiquitination and subsequent proteasomal degradation of target proteins.', 'MAAAAAGTATSQRFFQSFSDALIDEDPQAALEELTKALEQKPDDAQYYCQRAYCHILLGNYCVAVADAKKSLELNPNNSTAMLRKGICEYHEKNYAAALETFTEGQKLDIETGFHRVGQAGLQLLTSSDPPALDSQSAGITGADANFSVWIKRCQEAQNGSESEVWTHQSKIKYDWYQTESQVVITLMIKNVQKNDVNVEFSEKELSALVKLPSGEDYNLKLELLHPIIPEQSTFKVLSTKIEIKLKKPEAVRWEKLEGQGDVPTPKQFVADVKNLYPSSSPYTRNWDKLVGEIKEEEKNEKLEGDAALNRLFQQIYSDGSDEVKRAMNKSFMESGGTVLSTNWSDVGKRKVEINPPDDMEWKKY', 365, 'Q9Y2Z0; A2A303; Q5JAK5; Q5TAM6; Q6VXY6;', 'KD00772', 'Homo sapiens (Human)', 'SUGT1', '#Suppressor of G2 allele of SKP1 homolog#Protein 40-6-3#Sgt1', '-', 'ENSG00000239827', '-'),
(773, 'Q12495', 'Chromatin assembly factor 1 subunit p90', 'k', 70210, 'Acts as a component of chromatin assembly factor 1 (CAF- 1); which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process; bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p90 may facilitate the efficient and timely assembly of histones into telomeric chromatin.', 'MEQHLKSIPLQDDTKKKGILSFFQNTTTVKSNKFLTKEKDVITLDDPKEDVSGPMIETVKQETMKSINKECADEMKTTPKKANAEDKLLCYKNSPIQSTKYDRNTNKQVPNGNIIAIETKSRSSSPCSKRELSSSKKEEAKREKELKKQQRAEEKHRKELLRQEEKKKKELKVEEERQRRAELKKQKEEEKRRKEEARLEAKRRKEEERLKKEEEIRLKEEAKERAQSRIGNFFKKLSDSNTPVVEKSDYEKFFLPFYAKDGVRVSNKWKLTKVELEGSKRKIDDELLNSKDKTSSDDLLNWLQSRRLPRGHKIKRKAVDVLQQMPLKEKTDDELQSLLAQVPHKYIKFYENVRPPFIGTYSMDFTLPPNDPFSTKGTGFNYDYDSDVEWVNEEEEGEVDNLESGEEEEEEEDDEDVPSEGEFDGFLDSEENSDLDGLPCAKRKFVGPLIPTICLKSNFENLSEENKRYLQQLKAEVIIETDGPIDPFKEPKTSSLPSKRSNSDLQAQTASQSQSPEKKQKAMITDPMDLLRLFDGVQDSTFSLGTVTEIAQKNLPQYNKQTIKNTIKEYAIRSSGKGDLPRKWVIKDAQNWENLRANANMPTPSL', 606, 'Q12495; D6W428;', 'KD00773', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'RLF2', '#Chromatin assembly factor 1 subunit p90#CAF-1 90 kDa subunit#RAP1 localization factor 2', '-', '-', '856129'),
(774, 'Q751U7', 'Spindle pole body component KRE28', 'GO:0000778', 41228, '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}.', 'MSTKDTSGQSGYANDIRKLGEQTAHVSEQVLVQQERQRLGALEELHQSIIQIAEENSFVTPIKKDAANVHIDPRGIAVSVQQFKQLAEVLKVTHLEQETLDNFLRYTISDNDQLLDIKSVADSRYARLAEEVCQLEQEELRHLENEIISLNGNITEQTTKVIDANEKVKEECLEVSNGIERCWGLLNELETLRSTTDEGNVELGPLEETYQKWKSVDHFLQQKLHLKEQLRVLEDTRKSLSEVTKSSGNRAPDLDASEKFVTYRLLDSMWKKQFVDTTKIRDLELYPRTGKIQFQVADTIYVLAISGDQISNIQLFNDKLPAADLENNTQDLNKRFLGTSDVRRVVDFITHQQAVPQAQVH', 361, 'Q751U7;', 'KD00774', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '4622567'),
(775, 'Q21441', 'Kinesin-like protein vab-8', 'GO:0003777', 118211, 'Required for posterior migration of cells and axon growth cones during nervous system assembly. Isoform a is required for posterior migration of the axon growth cone and the ALM cell body. Isoform a may enhance posterior migration by regulating the subcellular location or stability of guidance cue receptors such as sax-3 and unc-40; promoting their localization to the cell surface. Isoform b is specifically required for CAN cell migration. {ECO:0000269|PubMed:15539493; ECO:0000269|PubMed:17237777; ECO:0000269|PubMed:17237778; ECO:0000269|PubMed:8625818; ECO:0000269|PubMed:9581759}.', 'MEACSSKTSLLLHSPLRTIPKLRLCASISSEDVAHGRCSLTDQHLQIEGKNYSKTTFDHIFRTDATQDDMYTAFLSDTINSVFAGNDATVLAMGAKTNGKDERLYGNSVSRNGLVQMAITQLMNALDDNKDSEERIQVRMSAIMVSQNESSIVDLLSPFNPDPRHRVVKIVDDARTGVFIDNESEIRVETIDQALFYLNTAVDHRMIQDEHTHRTSHVFISLSLYSYKMGDKMQGGRRRLCFLDMGIGERNSTNGGMTMPALGSILLAMVQRNKHIPSRDSSVCQLIRCALSTSRFTTFVFSFGAKSDDNENIAHLACKIARTRAKSMVGHGRKSSGTMSTGTMESNSSSCGTTTITPGGTPRTQRRFELESGSELSAAETVIFLGPNSSRTASPASTTMPFTPTSIRPLHRTTRNHSGVEALSKPLSVETKSSPTHNCHDGCIHSIPPMLRGHTPFLSASLKLYDELCSPPSSSRASPAPPAAFGGKTSEKREDFGIMIAQPSIPLMKAKSKYNLDDGKMKQIMQWMETSEAPPILFSSPCYENSATSVEELRECVGILSHPLEDIIEQEEESMRTSTATTGGSKKDHPLRILSKQDLNVEPEIKDKQEENELELVMAASLSSMRSHDILAKLEAMRNAQNGNSVQNIGNSQSNTDMDVSEMDVYRRASHLEEYAMQRVREIEENKLKNKKKIKLGLNCCQQQSMISSGSTVVDWSQIERKKEKEREVHEEEMRKEMLRERRAKLKITELEIKRERNLIDKELDDKKGIANSIARQLQHFSLSPCRGGRTHRSVSTHRIDPPNASLPSTPTMSHKKVIGGSLAKLSASGASGSTGAPPSPALGYHQSLPRHSKLPTSVNGRRASAERERKSNKASRNSCSKERKISGSKEELQWRSPYAQMTSPKSYGGPGTSSSGRGSSAPGSDFETPVVSTTEKSANGTIPRSKRQSYSASSGYESANDYHIYSTTNKKPHILDKKRNEEKLSLVRQADEIRHRQWQLKKELEEAKRAIGQEDDAKMIANSSDQRLNGLSRTTMIDAMLQENRILEKRLVACRNHSMLVTTFI', 1066, 'Q21441; Q9TVW0; Q9U541;', 'KD00775', 'Caenorhabditis elegans', 'vab-8', '#Kinesin-like protein vab-8#Variable abnormal morphology protein 8', '-', '-', '179675'),
(776, 'Q12493', 'Central kinetochore subunit NKP1', 'GO:0000776===GO:0000777===SCL===k', 26976, 'Component of the central kinetochore; which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle- microtubule attachments and proper chromosome segregation.', 'MTDTYNSISNFIENELTALLSSDDYLMDDLAGELPNEVCRLLKAQVIEKRKDAMSRGKQDLLSKEIYDNESELRASQSQQIMELVGDIPKYSLGSELRNRVEGEPQSTSIERLIEDVLKLPQMEVADEEEVEVENDLKVLSEYSNLRKDLILKCQALQIGESKLSDILSQTNSINSLTTSIKEASEDDDISEYFATYNGKLVVALEEMKLLLEEAVKTFGNSPEKREKIKKILSELKK', 238, 'Q12493; D6VT17;', 'KD00776', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'NKP1', '#Central kinetochore subunit NKP1#Non-essential kinetochore protein 1', '-', '-', '851991'),
(777, 'P04910', 'Histone H2A-beta', 'GO:0034501', 13776, 'Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin; limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation; DNA repair; DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones; also called histone code; and nucleosome remodeling. {ECO:0000269|PubMed:15226425}.', 'MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKQSGKGKPSQEL', 131, 'P04910;', 'KD00777', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hta2', '#Histone H2A-beta#H2A.2', '-', '-', '2542226'),
(778, 'Q64EW0', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25327, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAITTAESSYEKRIKALFDKQVQMEAREASVIKKVFKFNSNLLDVKEAVVHHHRDVEKLQKVVIQRREEMEKRVSFMEELAQEVEATKQRNLVMREQIKQQKMLVRQRKNEIMESIHTLSKATGTYINREALPARVKGVTVLHGDNRDELIPFDLKATDVEGLDSLCQHLHSLNIDVSQWQQLVSLATEMSMKSHPATPPKDAAKCKSIIEIDLTSPTIQA', 221, 'Q64EW0;', 'KD00778', 'Drosophila eugracilis (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '-'),
(779, 'Q5U1Z7', 'Centromere protein R', 'GO:0000777', 19917, 'Transcription coregulator that can have both coactivator and corepressor functions. Involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast; it does not coactivate nuclear receptors for retinoic acid; vitamin D; progesterone receptor; nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit; possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells; but not in other cancer cells; via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A-associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex (By similarity). {ECO:0000250}.', 'MPVKRSLKLDDQFEENSFGPSKIMRKKSITAFSPTTGTYQLSPFSSPRTPKEQEHRDGPSNGTRKWSVLSSPARQDSTVKGSDGFMMLLSKIERSSEKTMEIMKNLSSLQALEGNRQLEDLLGVSLVPCSLKSEAKKTKELMTKVMKQKLFEKKNSRIPPKEHHPNSFEFLKAILN', 176, 'Q5U1Z7;', 'KD00779', 'Rattus norvegicus (Rat)', 'Itgb3bp', '#Centromere protein R#CENP-R#Nuclear receptor-interacting factor 3', '-', '-', '362548');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(780, 'Q5ZMC9', 'Nuclear distribution protein nudE homolog 1', 'GO:0000776', 39564, 'Required for centrosome duplication and formation and function of the mitotic spindle. {ECO:0000250}.', 'MEDSEEHHFSSVEEETRYWKELAMKYKQCAENIQEELCEFQEGSREYEAELETQLQQTESRNRDLLSENNRLRIELESVKEKFEMQHSEWYRQVSALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRAAIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPKTPMRTSLETERTDTAVQASLSLPSTPSLHRAPNINIPTPATFRRGFEDSYCATPLTPAARISALNIMGDLLRKVGALESKLASCRNFVYDQSPDRTTVSMYMNRDALETRMSPHQPLCDTGLVKRLEFGTRPSSTPGPMSHPSQSVVKMLL', 342, 'Q5ZMC9;', 'KD00780', 'Gallus gallus (Chicken)', 'NDE1', '#Nuclear distribution protein nudE homolog 1', '-', '-', '416597'),
(781, 'Q64EW1', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25243, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAIIMAESSYERRVKALYEKQIRMETLEGKFIKKVFKFNSILLDVKEAAARHQRKVEKMQKVVIERREELEKRVSFMGQLAQEVEATKLRNLAMKDRIKQQKMLARERNNEIMERIHTLSKTTGTYVNQEALPARVKGVTVLRGDKRDQLIPFDLNATDAEGLNSLCQHLESLNVDVSQWQQLVSLVMDVTMEARAPTTPPKEAANCKSIIEIDLTSPTS', 220, 'Q64EW1;', 'KD00781', 'Drosophila erecta (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6553662'),
(782, 'Q64EW2', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25060, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAIIMAESSYERRIKALYEKQIRMEALEGKFIKKVFKFNSVLLDIKETSARHQRKVGKMQKVVTERREELGRRVTFMGHLTQEVEAIKLRNLAMKDQIKQQKMLNNQRKNEIMERIHTLSKTTGTYVNQEALPARVKGVTVIPGDRRNQLIPFDLNATDDEGLNSLCQHLESLNVDVSQWQQLVSLAMDVALGARAPTTPPKEAANCKSIIEIDLTSPTS', 220, 'Q64EW2;', 'KD00782', 'Drosophila orena (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '-'),
(783, 'Q9NGT3', 'MDF-2MDF-2; isoform a', 'k', 23529, '', 'MTDVKTQNAISLKGSAQLVKEFFHFGLNSILYQRALYPSDSFKREKKYGLTLWVAHEKKLQAFMDPLLQQVEYWLAKRQLKRLVMVISEVKTKEVVERWQFDIHTENLAEEGENAHRVKEEKKIRQEISDVIRQITASVSFLPLLEEPVSFDVLIYTGKDTQAPEDWTESGACLIQNSETVQLRSFSTSVHSVNTNVQYKADF', 203, 'Q9NGT3;', 'KD00783', 'Caenorhabditis elegans', 'mdf-2', '#MDF-2 {ECO:0000313|EMBL:AAF63495.1}#MDF-2; isoform a {ECO:0000313|EMBL:CCD74132.1}', '-', '-', '177046'),
(784, 'Q8VIL3', 'ZW10 interactor', 'GO:0000777', 30142, 'Part of the MIS12 complex; which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase (By similarity). {ECO:0000250}.', 'MADAEKNAVAEKNAVAEENAVAEENAVADKNATKEVLAEAASVLEPVGLPEEAELPAKIMEEFMRNSRKKDKLLCSQLQVVNFLQTFLAQEDNTDQNPDALASEDTSRQKATETKEQWKELKATYMDHVDVIKCALSEALPQVKEAHRKYTELQKAFEQLEAKKRVLEEKLQLAQKQWVLQQKRLQNLTKISAEVKRRRKRALEKLDGSHQELETLKQQAGQEQEKLQRNQSYLQLLCSLQNKLVISESKADDKDVKGPALPPKSP', 266, 'Q8VIL3; Q546Y5;', 'KD00784', 'Rattus norvegicus (Rat)', 'Zwint', '#ZW10 interactor#SNAP25-interacting protein 30#Scoilin#ZW10-interacting protein 1#Zwint-1', '-', '-', '257644'),
(785, 'Q64EW3', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25648, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAIIIPESSYERRVKALYEKQIRMEALEGKFIKKVYKFNSNLLDVKEAVLRHQRKVGKLQKVVMERREELEKRVSFMEELAQELEATKLRNLAMKEQIKQRKMIARQRKNEIMERIQTLSKTTGTYVNQEALPARVKGVTVLRGDKRDQLIPFDLNATDAEGLNSLCQHLESLNVDVSQWQQLVSLAMDVAMEARAPTTPPKEVANCKSIIEIDLTSPTSHQA', 223, 'Q64EW3;', 'KD00785', 'Drosophila teissieri (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '-'),
(786, 'Q6C3J2', 'Spindle assembly checkpoint kinase', 'GO:0005828===GO:0034501===GO:0000778===GO:0008608===GO:0032133', 42751, '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 (By similarity). {ECO:0000250}.', 'MSMKQLETSMSSVSLQEKKPTRIKIALHPQSKSEQNETDRASKIPTGRISTTQPQTYYRPTNLTKTPASQVSRRSSYTTDPPSPLTGITGFRNYSLDDFEIGKALGKGKFGKVYLVKDKKTGFVSALKCMEKKELVEGNVEKQFRREVEIQSNLRHTNVLRLFGHFHDKDRVYLILEYVVHGELYKLLRNQKRFTESTASSYIYQMSEALLYLHGKNIIHRDIKPENILLHFNDTIKISDFGWSVHAPSNRRSTLCGTMDYLPPEIVQSRPYDKNVDVWSLGILMYEFLCGAPPFEEPGGAQATYRRIVKLDLRIPPYVSADAADLIKRMLTLDPAKRFKLKDMHKHPWIVRLRPTWKYKVPKTASHERSA', 371, 'Q6C3J2;', 'KD00786', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'IPL1', '#Spindle assembly checkpoint kinase#2.7.11.1#Aurora kinase', '-', '-', '2912237'),
(787, 'Q64EW6', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 25619, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MAIIMAESSYERRVKALYEKQIRMEALEAKFIKKVYKFNSNLLDVKEAACRHQRKVGKLQKVLMERREELDKRVSFIEELDRELEATKLRDLAMKDRIKQQKMLARQRKNEIMESIHTLSKTTGTYINQDALPARVKGVTVLRGDKRNQLIPFDLKSTDVEGLDSLCQHLESLNVDMAQWQQLISLAMDVAMESRAPTTPPKEATNCNSIIEIDLTSPTCHI', 222, 'Q64EW6;', 'KD00787', 'Drosophila mauritiana (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '-'),
(788, 'Q0MXD1', 'Histone H3-like centromeric protein CSE4', 'GO:0000777', 17938, '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}.', 'MARISTSSNRPVPTSSALRRQRERDDGGRSTRAPGHNTGLYGNQPGDPPTIRSTNTTVKRRYRPGTKALREIRRYQRSSELLIRKLPFARLVKEVAENYIGADYGIRWQSNAVLALQEACEAFLVHLLEDTNLCAIHAKRVTIMQKDIQLARRIRGNI', 158, 'Q0MXD1;', 'KD00788', 'Millerozyma farinosa (Yeast) (Pichia farinosa)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog', '-', '-', '-'),
(789, 'Q0MXD0', 'Histone H3-like centromeric protein CSE4', 'GO:0000777', 34129, '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}.', 'MQSQQYSTPNLSLFNDGSAIIGEIRPIHGANQDVINDRALQLLQRTREHRNFLHRAHDDIRRYEPPTTQIDALENDEDENFYLNDMNTNEEYQSDRESVKSGLNSIANRYKNAVQSSPSDLDDIDFVGEEEQDLSYDESDYSDPLQEIDSNYRESPRRTTDKILKSSSKNYRRRENLGGEIRKIRQEKANKTATRYRPSDLALYEIRKYQQSTDLLISKIPFARLVKEVTDNFILENQHLQWHSMAILALQEASEAYLVGLLEHANLLALHAKRITLMKKDVQLARRIRGQFI', 293, 'Q0MXD0;', 'KD00789', 'Kazachstania servazzii (Yeast) (Saccharomyces servazzii)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog', '-', '-', '-'),
(790, 'O00139', 'Kinesin-like protein KIF2A', 'GO:0003777', 79955, '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. {ECO:0000269|PubMed:15843429; ECO:0000269|PubMed:17538014; ECO:0000269|PubMed:18411309}.', 'MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEEIEPSPETPPPPASSAKVNKIVKNRRTVASIKNDPPSRDNRVVGSARARPSQFPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTVDPTAAGDVRPIMHHPPNQIDDLETQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWLEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL', 706, 'O00139; A5YM42; A5YM54; B4DY54; D3DW97; E9PB70; Q7Z5I3; Q8N5Q7;', 'KD00790', 'Homo sapiens (Human)', 'KIF2A', '#Kinesin-like protein KIF2A#Kinesin-2#hK2', '-', 'ENSG00000068796', '-'),
(791, 'O94679', 'Condensin complex subunit 1', 'GO:0000939===k', 131324, '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 topoisomerases. The condensin complex probably also plays a role during interphase.', 'MSLDLLSRLKKYIHDEENSDLDSIYAECENAGLTAVVNDVIDTLLLGTSSCFDEDCLEKLFAICSHFADLSSSVRNKVYDLLTSNISSESAILEDMISANATDFTVPQTNLETTGIAFQLTVNSLSSSNQLSVIRSSTNTVKGRKKNPTTNSNWNGISHVNALLDAIITLFQKKLSRVWTTSSERDMFLSLFLKPIYTLMESEINIKNASFRSRLFNIIGLAVQFHNHTTAAETNIIQNLQYFEHLSEYAADLVHIVTVQFNSVTLAEGIIRTLCSLEFNDNDVKGPKQVALFLVRLSSLIPNLCLKQLTQLVKLLDSESYTLRCAIIEVLANVVIDQIHDEAQNEMSESVPATVQSLMDLLSERLLDISPYCRTKVLHVFIKIFDLPIKYPRKRQEIAELVIRCLQDRSSHVRRNAIKLFSKLLTTHPFSVMHNGLLTRNIWEKGLSIIEEQLNSLQPKQQEKVVDSELEVDENLLEDATMIQDDESHEGESHLENSLSEYVDSVPAEEIVKVNLTKRFYLEALQYIDIVEAGAKIISQLLFAKNKSEVIESMDFFVFCNSFGISSSKLYIKKMIHLIWVKGTSDEGNNIQNHVLSCYKTLFFEPPPNSGTNEAANYIARNLISLTYDASLAELTSLEQMLCILMKDGYFSHLVITKLWQVYSYQKKDISRTQRRGSIIVIGMLALGNTDVVMQGLDHLIQIGLGPPGLEDLVLARYTCIAIKRIGKDASGSSNINFPNSHTLCQKLCMLLLRPSFSEEWFGLEEQAIEAIYAVAKHPDELCTNIILLLTKQLFKPSNHENTTSNDDHAMDEDLDDSPEEETLKDEEEIGIRLAHLIFLVGHVAIKQLVYIEYCEAEFKRRKADAERLAVQNSNNPINGQETSEYDLITGTSEDDFSEAMTFIRERELLYGENSLLSRFAPLVVELCSNHKSHNNQSLLLAASLTLSKFMCLSNNFCMEHLPLLITILEKCDNPIIRNNLVIGLADLTVCFNHFIDEISEYLYRRLMDEESSVKKTCFMTLAFLILAGQIKVKGQLGIMARSLEDEDARISDLARMFFTDFAAKDNSVYNNFIDIFSVLSRSAEEQDEDDAKFKRIIRFLTSFIEKERHTKQLAERLAARLDRCKTQRQWDHVVYALSLLPHKADNIQKLIDDGYHE', 1158, 'O94679;', 'KD00791', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cnd1', '#Condensin complex subunit 1#XCAP-D2 homolog#p128', '-', '-', '2541201'),
(792, 'P55735', 'Protein SEC13 homolog', 'k', 35541, 'Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum; SEC13 is involved in the biogenesis of COPII-coated vesicles. As a component of the GATOR2 complex; inhibits GATOR1 complex; an inhibitor of the amino acid-sensing branch of the TORC1 pathway. {ECO:0000269|PubMed:23723238; ECO:0000269|PubMed:8972206}.', 'MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDHPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASVTEGQQNEQ', 322, 'P55735; A8MV37; B4DXJ1; Q5BJF0; Q9BRM6; Q9BUG7;', 'KD00792', 'Homo sapiens (Human)', 'SEC13', '#Protein SEC13 homolog#SEC13-like protein 1#SEC13-related protein', '-', 'ENSG00000223899', '-'),
(793, 'Q2TA25', 'Serine/threonine-protein kinase PLK1', 'GO:0000776===GO:0000942', 68000, '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 (By similarity). 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:P53350; ECO:0000250|UniProtKB:Q07832}.', 'MSAAATAGKLGRAPADPGKAPGVAAPGASTAAPPAKEIPEVLVDPRSRRRYLRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQKEKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHGNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKNNEYSIPKHINPVASSLIKKMLQPDPTARPTIHELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGMENPMPERPREKEEPVVREASEPVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYSDGDSLQYIERDGSESYLTVSSHPNSLIKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGCVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCSKELASRLRYARAMVDKLLSSRSAANRLKASS', 602, 'Q2TA25; F1N225;', 'KD00793', 'Bos taurus (Bovine)', 'PLK1', '#Serine/threonine-protein kinase PLK1#2.7.11.21#Polo-like kinase 1#PLK-1', '-', '-', '538238'),
(794, 'A6QM04', 'Protein zwilch homolog', 'GO:0000777', 66385, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores (By similarity). {ECO:0000250}.', 'MWSGANRAAEEFYAGLLQEFDENKKGIRKDPFIYEADIQVQLISKGQPNPLKNILHENETIFIVEKVPLEKEEPSPIEELQSEDTAISDLSTGENVGLLALPIGRARQLIGFYTMAHNPNMTHLKINRPVTALPPLWVRCDGSDPEGISWLGAELISTSSNITGIVLYMVTCKVDKNYSVNLEDLKKSHKKRHHLSTLTASGFARYELFKSTALDDTVAASQTTITLDISWSPVDEILQTPPLSSTATLNIKVESGEPRGPLSQLHRELKFLLVLADGLRTGVTEWPEPLEAKSAVELVQEFLNELSKLNEFGDSTKKDTEIVKHDAAAVDGSIECLLTVRGDLDFAEQLWCKMSSSVISYQDLVKCFSLVIQSLQRGAIQPWLHSGSNSLLSKLIHQSYYGTMDTVSLSGTVPVQMLLEIGLDKLKKDYICFFIGQELASLNHLEYFISPSVDTQEQVHRVQKLHHILEIVVSCMLFIKPQHELLFSLTQSCIKYYEQNPLDEQHIFQLPVRPTAVKDLYQNEKPQKWRVEINSGQKKVKTVWQLSDSPPIDHLNFHRPDFSELTLSGSLEERISFTNMVTCSQVHFK', 589, 'A6QM04;', 'KD00794', 'Bos taurus (Bovine)', 'ZWILCH', '#Protein zwilch homolog', '-', '-', '534811'),
(795, 'Q9CUU3', 'Synaptonemal complex protein 2', 'k', 172123, 'Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase. May be involved in the organization of chromatin by temporarily binding to DNA scaffold attachment regions. Requires SYCP3; but not SYCP1; in order to be incorporated into the axial/lateral elements. {ECO:0000269|PubMed:11463847; ECO:0000269|PubMed:16717126}.', 'MPVRPDLQQLEKCIDDALRKNDFKPLLALLQIDICEDVKIKCSKQFLRKLDDLICRELNKKDIQTVSSILISIGRCSKNIFILGQAGLQTMIKQGLVQKMVSWFENSKEIILNQQQSKDEAVMNMIEDLFDLLMVIYDISDEGKNQVLESFIPQICALVIDSRVNFCIQQEALKKMNLMLDRIPQDANKILSNQEMLTLMSNMGERILDVGDYELQVGIVEALCRMTTEKRRQELAYEWFSMDFIANAFKEIKDCEFETDCRIFLNLVNGILGDKRRVYTFPCLSAFLGKYELQIPSDEKLEEFWIDFNLGSHTLSFYIAGDEEDHQWEAVTVPEEKVQMYNIEVRESKKLLTLTLKNIVKISKKEGKELLFYFDESLEITNVTKKVFGGNKYKEFTRKQGISVAKTSIHVLFDASGSQILVPESQPSPVKENLIHLKEKSDIQKKLVNPLELGNSSSQDEITTPSRKKMSEASMIVPDTDRYTVRSPILLINTSTPRRSREPLQAINSVEKAVSKTSESGMDYAASPKSRQSDGRKRWNNRANHNKTTAVIQNKQYEDNESPDQNFNEIEDTLSNVSSAVGKVDKPVLPGVLDISKNTTHSRWACWTPVTTIKLCNNQRSRALPGDTCTQDTGVNKKCTKQKSVSDDDSEETQKGKYSKDVIKCNKSDEAEFCERNIQEQNHPKYSQKKNTANAKKSDWHIESETTYKSVLLNKTTEESLIYKKTCVLSKDVNTTICDKSPSRKSKRNHTKSRKELMSELTSCELEEIPVRENSKGKRFTGASESLINQISRRYNPSDSMMSTRKLKEPQDGSGFSKKPDLQFNKVQRKSYRKLKATVVNVTSECPLDDVYNFSLNGADEPVIKLGIQEFQATTREASMDNSLKLVKNHDEHDPFLKTKDKRMLSYEKKTLLSDTETECGCDDSKTDISWLKEPKTKRLMDYSRNKNTTKYKSRKSRSSMEKGQPRPTMVLNKNSMKNDYEVVVDGRTRLPRRATKTKKNYKDLSTSESESESEKECSYLFKDKLPTKEETIHSRAQTKKLPEKQQKVFNSEALKGQPSEEQKNSSRLREGREDSLCLSSASVSRSSSSVEVMRCTEKITERDFTQDYDYITKSLSPYPKAPSPEFLNGNNSVVGRGQSPRISETSAMCVRKSYSPASGPPFSPRHTPTKNNSVVNMKKANSVINNQRTQHCNSYSDVSSNSSEKLYMEPESPESCDNHMQNKREGNHAASPLSLSSEKIEKMWFDMPSENTHVSGPSQRGSKRRMYLEDDELSNSNEAEVEEAEEREHLLSKKRCQWENSDQHTFKTSLSTPDFSVPKDWQQELQGAGMFYDNISSDYKRKTDSQHKIMDDFTTKTLKLTQQHLMAMTSQAQGRRDENVEKFQVTLLDELEKVEKDSQTLRDLEKELVDIEEKLVQKMRAYHRCERERFRVLKTSLDKSFLVYNSVYEESVFTSEMCLMKANMKMLQDKLLKEMHEEEVLNIRRGLQSLFKAHEGNDA', 1500, 'Q9CUU3; A2AJW2; Q1G7B6;', 'KD00795', 'Mus musculus (Mouse)', 'Sycp2', '#Synaptonemal complex protein 2#SCP-2#Synaptonemal complex lateral element protein', '-', '-', '320558'),
(796, 'Q9P7A0', 'Shugoshin-1', 'GO:0000778===k', 37135, 'Plays a central role in chromosome cohesion during meiosis by preventing premature dissociation of cohesin complex from centromeres after prophase; when most of cohesin complex dissociates from chromosomes arms. May act by protecting centromeric rec8 from separase degradation during anaphase I. {ECO:0000269|PubMed:14730319; ECO:0000269|PubMed:14972679; ECO:0000269|PubMed:16303567}.', 'MNFQFINSNINNEDKLPMESLKKKFLKQNREIIKINTQLSIKIRESENEIQDLIQENFTLKSYLVKLEARFRNQSQTEDLLKNFFPEIQTIHKKISQVQSLLKIIEKKCSSDFLEANVKSQFTTCENKDSKEDYQILHNKRLEYVSFNDELKSLETGQPLYCFQDFQKKVHGPPALSEKPGKCILKDKTNAHVNKIPQDEVNYSLPQKNITIFSKELKENEFESINEGETEEEKAKTSNVCVCIPCKSAEQITDLKGQATGDSSPCDFEESQPRINGREKLRRSVKVINYAIPSLRTKLRRDFDLPSDRKRKRHPRGKA', 319, 'Q9P7A0;', 'KD00796', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'sgo1', '#Shugoshin-1', '-', '-', '2541326'),
(797, 'P17106', 'Centromere-binding protein 1', 'GO:0000776===k', 39388, 'Required for chromosome stability and methionine prototrophy. It is involved in chromosomal segregation. Binds to a highly conserved DNA sequence (5''-RTCACRTG-3''); called CDEI; found in centromeres and in several promoters. DNA-binding activity is enhanced by MET28. Required as an auxiliary factor for transcriptional activation of sulfur metabolism together with MET4 and MET28. {ECO:0000269|PubMed:1549123; ECO:0000269|PubMed:8665859}.', 'MNSLANNNKLSTEDEEIHSARKRGYNEEQNYSEARKKQRDQGLLSQESNDGNIDSALLSEGATLKGTQSQYESGLTSNKDEKGSDDEDASVAEAAVAATVNYTDLIQGQEDSSDAHTSNQTNANGEHKDSLNGERAITPSNEGVKPNTSLEGMTSSPMESTQQSKNDMLIPLAEHDRGPEHQQDDEDNDDADIDLKKDISMQPGRRGRKPTTLATTDEWKKQRKDSHKEVERRRRENINTAINVLSDLLPVRESSKAAILACAAEYIQKLKETDEANIEKWTLQKLLSEQNASQLASANEKLQEELGNAYKEIEYMKRVLRKEGIEYEDMHTHKKQENERKSTRSDNPHEA', 351, 'P17106; D6VWN1; P17623; Q6Q5N1;', 'KD00797', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CBF1', '#Centromere-binding protein 1#CBP-1#Centromere promoter factor 1#Centromere-binding factor 1', '-', '-', '853523'),
(798, 'P57740', 'Nuclear pore complex protein Nup107', 'GO:0000777===k', 106374, 'Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC. {ECO:0000269|PubMed:12552102; ECO:0000269|PubMed:15229283}.', 'MDRSGFGEISSPVIREAEVTRTARKQSAQKRVLLQASQDENFGNTTPRNQVIPRTPSSFRQPFTPTSRSLLRQPDISCILGTGGKSPRLTQSSGFFGNLSMVTNLDDSNWAAAFSSQRSGLFTNTEPHSITEDVTISAVMLREDDPGEAASMSMFSDFLQSFLKHSSSTVFDLVEEYENICGSQVNILSKIVSRATPGLQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSALEEESVFAVTAVNASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGEFSDNIEFYAKSVYWENTLHTLKQRQLTSYVGSVRPLVTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLYHDPNVNGGTELEPVEGNPYRRIWKISCWRMAEDELFNRYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIQTSVATLDETEELPREYLGANWTLEKVFEELQATDKKRVLEENQEHYHIVQKFLILGDIDGLMDEFSKWLSKSRNNLPGHLLRFMTHLILFFRTLGLQTKEEVSIEVLKTYIQLLIREKHTNLIAFYTCHLPQDLAVAQYALFLESVTEFEQRHHCLELAKEADLDVATITKTVVENIRKKDNGEFSHHDLAPALDTGTTEEDRLKIDVIDWLVFDPAQRAEALKQGNAIMRKFLASKKHEAAKEVFVKIPQDSIAEIYNQCEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNEWFKHMNSVPQKPALIPQPTFTEKVAHEHKEKKYEMDFGIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAKEDHERTHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQL', 925, 'P57740; B4DZ67; Q6PJE1;', 'KD00798', 'Homo sapiens (Human)', 'NUP107', '#Nuclear pore complex protein Nup107#107 kDa nucleoporin#Nucleoporin Nup107', '-', 'ENSG00000111581', '-'),
(799, 'Q6GNF1', 'Nucleoporin seh1-B', 'GO:0000777===GO:0051315', 39746, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (By similarity). {ECO:0000250}.', 'MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSENVNWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGVVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNIMGKVQIYEYNENTRKYAKAETLMSVSDPVHDIAFAPNLGRSFHILAVATKDVRIFTMKPLRKELSSSGGVTKFENHTVAQFDNHNSQVWRVSWNITGTVLASSGDDGTVRLWKANYMDNWKCIGVLKGDGNPVGNSFQGIFGSSIGSASHGLQNSVNGTSTSGRKHS', 360, 'Q6GNF1;', 'KD00799', 'Xenopus laevis (African clawed frog)', 'seh1l-b', '#Nucleoporin seh1-B#Nup107-160 subcomplex subunit seh1-B', '-', '-', '444365'),
(800, 'Q00839', 'Heterogeneous nuclear ribonucleoprotein U', 'k', 90584, 'Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Binds to pre-mRNA. Has high affinity for scaffold-attached region (SAR) DNA. Binds to double- and single- stranded DNA and RNA. Plays a role in the circadian regulation of the core clock component ARNTL/BMAL1 transcription (By similarity). {ECO:0000250|UniProtKB:Q8VEK3; ECO:0000269|PubMed:19029303}.', 'MSSSPVNVKKLKVSELKEELKKRRLSDKGLKAELMERLQAALDDEEAGGRPAMEPGNGSLDLGGDSAGRSGAGLEQEAAAGGDEEEEEEEEEEEGISALDGDQMELGEENGAAGAADSGPMEEEEAASEDENGDDQGFQEGEDELGDEEEGAGDENGHGEQQPQPPATQQQQPQQQRGAAKEAAGKSSGPTSLFAVTVAPPGARQGQQQAGGKKKAEGGGGGGRPGAPAAGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLWAGGRASYGVSKGKVCFEMKVTEKIPVRHLYTKDIDIHEVRIGWSLTTSGMLLGEEEFSYGYSLKGIKTCNCETEDYGEKFDENDVITCFANFESDEVELSYAKNGQDLGVAFKISKEVLAGRPLFPHVLCHNCAVEFNFGQKEKPYFPIPEEYTFIQNVPLEDRVRGPKGPEEKKDCEVVMMIGLPGAGKTTWVTKHAAENPGKYNILGTNTIMDKMMVAGFKKQMADTGKLNTLLQRAPQCLGKFIEIAARKKRNFILDQTNVSAAAQRRKMCLFAGFQRKAVVVCPKDEDYKQRTQKKAEVEGKDLPEHAVLKMKGNFTLPEVAECFDEITYVELQKEEAQKLLEQYKEESKKALPPEKKQNTGSKKSNKNKSGKNQFNRGGGHRGRGGFNMRGGNFRGGAPGNRGGYNRRGNMPQRGGGGGGSGGIGYPYPRAPVFPGRGSYSNRGNYNRGGMPNRGNYNQNFRGRGNNRGYKNQSQGYNQWQQGQFWGQKPWSQHYHQGYY', 825, 'Q00839; O75507; Q8N174; Q96HY9; Q9BQ09;', 'KD00800', 'Homo sapiens (Human)', 'HNRNPU', '#Heterogeneous nuclear ribonucleoprotein U#hnRNP U#Scaffold attachment factor A#SAF-A#p120#pp120', '-', 'ENSG00000188206', '-'),
(801, 'Q96BT3', 'Centromere protein T', 'GO:0000776===GO:0000777===GO:0051382===k', 60423, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome- associated complex that binds specifically to histone H3- containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000269|PubMed:16716197; ECO:0000269|PubMed:21529714; ECO:0000269|PubMed:21695110}.', 'MADHNPDSDSTPRTLLRRVLDTADPRTPRRPRSARAGARRALLETASPRKLSGQTRTIARGRSHGARSVGRSAHIQASGHLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQAVQPSRQESSCGSLELQLPELEPPTTLAPGLLAPGRRKQRLRLSVFQQGVDQGLSLSQEPQGNADASSLTRSLNLTFATPLQPQSVQRPGLARRPPARRAVDVGAFLRDLRDTSLAPPNIVLEDTQPFSQPMVGSPNVYHSLPCTPHTGAEDAEQAAGRKTQSSGPGLQKNSPGKPAQFLAGEAEEVNAFALGFLSTSSGVSGEDEVEPLHDGVEEAEKKMEEEGVSVSEMEATGAQGPSRVEEAEGHTEVTEAEGSQGTAEADGPGASSGDEDASGRAASPESASSTPESLQARRHHQFLEPAPAPGAAVLSSEPAEPLLVRHPPRPRTTGPRPRQDPHKAGLSHYVKLFSFYAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVLVERHLPLEYRQLLIPCAYSGNSVFPAQ', 561, 'Q96BT3; Q96I29; Q96IC6; Q96NK9; Q9H901;', 'KD00801', 'Homo sapiens (Human)', 'CENPT', '#Centromere protein T#CENP-T#Interphase centromere complex protein 22', '-', 'ENSG00000102901', '-'),
(802, 'Q5RBS5', 'Borealin', 'GO:0032133', 31323, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex; it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment (By similarity). {ECO:0000250}.', 'MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK', 280, 'Q5RBS5;', 'KD00802', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'CDCA8', '#Borealin#Cell division cycle-associated protein 8', '-', '-', '100174395'),
(803, 'Q54UC9', 'Kinesin-related protein 3', 'GO:0003777', 130532, 'Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule''s plus end. The maximal velocity in an inverted motility assay (moving microtubules on fixed motors) was 1.96 um/s. {ECO:0000269|PubMed:10545495; ECO:0000269|PubMed:18160177}.', 'MSSIRVVCRFRPQNKLELAQGGDSIVSIAPENDSVTINGSESNHSFSFDYVFPSNTTQRDVYDHAAKPVIEDIMAGYNGTLFVYGQTGSGKTFSMTGINDPNGDQELRGIVPRMIETVFEFISNADENIEFIVKASYIEIYMERIRDLLDTRKDNLKVREEKGKGVWVEGTSEVYIYREEDILDVINTGISNRAIAETRMNAESSRSHSIFILTIQQKNLKVGSIKTGKLYLVDLAGSEKISKTGAQGTTLDEAKMINKSLSSLGNVINALTDGKSTHIPYRDSKLTRVLQESLGGNSRTTLIINCSPSSYNEAETISTLRFGSRAKNIKNKAKINQERSAAELKILLSKAENEIENLKGYIKELETVSGVTVSNLKSSGSGSGSGSGSSSSSSGSSGGSGSGGSSNLSNSVNSTSNLNTSSNTSSSNVNANANVITTSVSAPTSPKDTELIKVLQEKCIQLEKQLFKKEEEKKEILEQLEQQQEQIQDKDQEIEGLNSMIESSNNINSLYQNSTNENSVLNVQLSELKLALEKSRFEATEQSLTIEGLNEENQSIKSQLEILKDRIAQSGDSSIASLVPSTPKSSAEMDPLATASKHADEWNEKAEQLKLLQRTPSKAVGSSKSNTATSSPIISLNISESDNIGSGATTTTNNNNATITPATSSNNNVEQQQQQVEELLPSVNEQLLESENQKLQKRIQEIELEFETYKIAKENLTMQKDLEIEQLLESQRISSSFVVDPRNLDDELPAEMMLQAEQIRKLIAENSEQKVHFEATKNENSKLKNRIEMIEEETRQRMEEELNVLREQTNQKLSEFGSLKESLIRDLENRCQKVIDLELVLDELQDRIVTLNERLKRVNKPGGGDQEAAFVQSKLDEITAVKHQLVIENNKHKTEVERLKKLLSHRGEHILILEKTMAINQESLFKLALNHNALTIEHDRAKNELEKLNNLLSQVGVDAQNTGGARVARVIRGGGGNNQLKKFNHSSSSSTSSSSALNHSSINNNHTTPTPLSANLYSNTKRSTKELNTGVKAEPLSLSGSPFNTSIPSSPNHTSSNNINNNSNNNNNNNNNNNIGNSGNIGGVGNNNSSISNSNNNSSSNLNANLNGNTPVKITSENSSSSLWNIFKKKSPSSTPPSSTNNLSPQSPQTPSHLSADGSGNISPNLSPPIPVNFSYTPAVVTSSTINKDQQKD', 1193, 'Q54UC9; O15720; Q6S005; Q8I825;', 'KD00803', 'Dictyostelium discoideum (Slime mold)', 'kif3', '#Kinesin-related protein 3#Kinesin family member 3#Kinesin-1', '-', '-', '8622903'),
(804, 'P17123', 'Sporulation-specific protein 12', 'k', 19912, 'It is required for meiosis I chromosome division during sporulation. A component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. {ECO:0000269|PubMed:11832211}.', 'MSNKASDQSARTASILKTDITRENTITRSSSSNNDNYHHHNNINNYNESAKTGEDANKENIPNLEEEIAAFRIFRKKSTSNLKSSHTTSNLVKKTMFKRDLLKQDPKRKLQLQQRFASPTDRLVSPCSLKLNEHKVKMFGKKKKVNPMKLNFKGNLAADSEDVEIDEDEEYFY', 173, 'P17123; D3DLA1;', 'KD00804', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SPO12', '#Sporulation-specific protein 12', '-', '-', '856557'),
(805, 'P17120', 'Kinesin-like protein bimC', 'GO:0003777', 131576, 'Important role in mitotic dividing cells. Microtubule motor required for spindle body separation.', 'MAGPQRATSGLPTRRTTTRQPTRRAGSAIPERQTSTASPAVSTKTAAISRTRTLKSPGEPASVLAKRKERDIEREINEDTSIHVVVRCRGRNEREVKENSGVVLQTEGVKGKTVELSMGPNAVSNKTYTFDKVFSAAADQITVYEDVVLPIVTEMLAGYNCTIFAYGQTGTGKTYTMSGDMTDTLGILSDNAGIIPRVLYSLFAKLADTESTVKCSFIELYNEELRDLLSAEENPKLKIYDNEQKKGHMSTLVQGMEETYIDSATAGIKLLQQGSHKRQVAATKCNDLSSRSHTVFTITVNIKRTTESGEEYVCPGKLNLVDLAGSENIGRSGAENKRATEAGLINKSLLTLGRVINALVDKSQHIPYRESKLTRLLQDSLGGRTKTCIIATISPARSNLEETISTLDYAFRAKNIRNKPQINSTMPKMTLLREFTAEIEKLKAELIATRHRNGVYMSVESYEEMKMENESRRIISEEQRAKIESMESSLRHKVQELLTLTSKFNDLKKDNDDTLAALCSTNDVLQQTDIVLQNTRAQLEEEEMLRCAHEETEHQLQDVGKGLISTLGQTVEDINSLQSKLDRKAELDATNAELWRASSTEVSDVTKRIDQRVEAFQTRHAKLLETTSVKVNEFIATEISNIERTRSDLSEYNRSLDAACNNAKAETSSAHEDMNNVLEEIKDLREEVKSKVGEGLNGLSAAAARISEEVIGEFTQLHSQLHTSFNNLGKDLKSIFETMATHLSEQKNEINRLRAELQSSNRQNIETTHKASAHLAQAIEEEHVAAEAEREILMSQIKALVEESRQKQFARLRAKIDGVRTEISASGDMLEQATTQHDRQIDEWVFKSEQFAKDVNASKDEIRTKLQNDWEAFDQRNSTIRKATESVHKETVRIVDVQVDDMGRQMEALDDFVAKARSQNGRYRDAHIATLDTIATGVRDSYSSIEGRVENLTGRMNQFQQEATHHHATLEESIAPLSNDVRKPLTDLSSSFQNRSLEEYVATGVTPKKRKYDYISVLPSTESHEVLKSRLRTTKEMEVLPFNSDDQLSGPSSSPGGSPSKGFVYNDVEDEVGTHAPTVTNVNPSNTGLREVDANVAARPLVYSTGEKSTDQDGSPVVSPDSATEAEGMNGPPSKRRRSNSVVADTKLPNKMLARRMAGMMEGRENVPPPGISNGRRLRGRPSP', 1184, 'P17120; C8VHR3; Q5B7W7;', 'KD00805', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'bimC', '#Kinesin-like protein bimC', '-', '-', '2874347'),
(806, 'Q6FTI5', 'DASH complex subunit DAD2', 'GO:0042729', 14320, '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}.', 'MDGLEQQKLAKQQELAALKRITALTDQMRTELDEMSIEVSKINKNAESVANVMANWDSIRKYISEASLGLLRYAEGDYQVGAWDGKENKSDKSNADKSYQSDDEHKTEPLPEALVRISVANNEESRK', 127, 'Q6FTI5;', 'KD00806', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'DAD2', '#DASH complex subunit DAD2#Outer kinetochore protein DAD2', '-', '-', '2888276'),
(807, 'Q960V3', 'Trafficking kinesin-binding protein milt', 'GO:0003777', 120649, 'Required for kinesin-mediated axonal transport of mitochondria to nerve terminals. The oocyte acquires the majority of its mitochondria by competitive bidirectional transport along microtubules mediated by the Milton adapter. Mitochondria enter the young oocyte en mass from interconnected germ cells to generate the large aggregate known as the Balbiani body. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent; anterograde transport of mitochondria. {ECO:0000269|PubMed:12495622; ECO:0000269|PubMed:16717129; ECO:0000269|PubMed:16887820}.', 'MTHVNNGEVMEKEMEPTGERERDRETAAGSGVHHRFLASASERDANSGNALEAAATKTKTGTTITNLEDLAFEACQNWSDLHQDFFITDDELEYEDELSLGSSIGGNIATTTTADAAVEGLITGEHQNEQLLMEVLCGNRVSQMTRAYDDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDADDGTDTDTPTMSKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADISAQLNDANSQYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQARSSFLGGLGTSGAGMGGSLFPPDSLHCELMESSLYSENSLDSGISGDSQRSADRISRMMMHMPSGGMSSSTMGGSVYAGAGNVPPYKRVFDTVRCAGKSGNYMDSGNVSMTQLGAMSMSSSSGPRMASMAYPAGSYYRGGSNQSLGVKTLSSESLNSQSDDGYPAQPSGVPGAPGAKELEAALKRLTPAEVLARRAMLSYAPAGTYNYDEPMGHGTGNVRNSDLPLGVRTPDSIMSTGSSGMSGSTNHMSASMTHQWRLPEKLQIIKPMEGSQTLHHWSRLATPTLSGLLDERPGVTIRGGRGLDDLGMQIYTLSDVEEDVSDDLPGKQFEAPGCTFTYTNSMVMHPDDGFVNDLSFLSQSQMSSRMASTSTSRQPSCPATPRAGLSRKNSCSTFSVNLGLAGMLNERGIKAVTPSALNTPAGPNFSPTVTPCNSPEGSPPRAQSPEPLFGLLSCGADLIRRKIVGDQHQQQQQKQRSSLSKQQQQKIMLSHLERRALRSLNLIEKVESIGLENIISAQRGLGSGIANRSSSPLSSGSLQSLHTSSNSIVDDIHFDRAQIKGVLHRGLKSPTPATASTSAAAAASGPGISTSSSTSAYNSDDSDDQGLVMKIKPSKSATPTTTGAAQSQPSSATTSNGTASETRLKQMQRQKSRRQLKNGMANQRPDLGTISGAGGGGRVRPDLGKVADSGSSSKLSTKRSEAKPAEEEEATPQTITQAFVGSVSSLLFGRKGGWL', 1122, 'Q960V3; Q0E8S6; Q8SWX2; Q95NI8;', 'KD00807', 'Drosophila melanogaster (Fruit fly)', 'milt', '#Trafficking kinesin-binding protein milt {ECO:0000303|PubMed:12495622}#Protein milton {ECO:0000303|PubMed:12495622}', '-', '-', '45683'),
(808, 'P17119', 'Kinesin-like protein KAR3', 'c;k', 84004, 'Essential for yeast nuclear fusion during mating. KAR3 is a bifunctional protein having a kinesin-like motor domain joined to a distinct microtubule binding domain. It may mediate microtubule sliding during nuclear fusion and possibly mitosis. May interact with spindle microtubules to produce an inwardly directed force acting upon the poles. KAR3 function antagonizes CIP8 and KIP1 outward force action. KAR3 motor activity is directed toward the microtubule''s minus end. {ECO:0000269|PubMed:11729143; ECO:0000269|PubMed:2138512}.', 'MESLPRTPTKGRSTQHLSTPSPKNDILAMNGHKRRNTTTPPPKHTLLKPQRTDIHRHSLASQSRISMSPNRELLKNYKGTANLIYGNQKSNSGVTSFYKENVNELNRTQAILFEKKATLDLLKDELTETKEKINAVNLKFETLREEKIKIEQQLNLKNNELISIKEEFLSKKQFMNEGHEIHLKQLAASNKKELKQMENEYKTKIEKLKFMKIKQFENERASLLDKIEEVRNKITMNPSTLQEMLNDVEQKHMLEKEEWLTEYQSQWKKDIELNNKHMQEIESIKKEIENTLKPELAEKKKLLTEKRNAYEAIKVKVKEKEEETTRLRDEVALKQKTNLETLEKIKELEEYIKDTELGMKELNEILIKEETVRRTLHNELQELRGNIRVYCRIRPALKNLENSDTSLINVNEFDDNSGVQSMEVTKIQNTAQVHEFKFDKIFDQQDTNVDVFKEVGQLVQSSLDGYNVCIFAYGQTGSGKTFTMLNPGDGIIPSTISHIFNWINKLKTKGWDYKVNCEFIEIYNENIVDLLRSDNNNKEDTSIGLKHEIRHDQETKTTTITNVTSCKLESEEMVEIILKKANKLRSTASTASNEHSSRSHSIFIIHLSGSNAKTGAHSYGTLNLVDLAGSERINVSQVVGDRLRETQNINKSLSCLGDVIHALGQPDSTKRHIPFRNSKLTYLLQYSLTGDSKTLMFVNISPSSSHINETLNSLRFASKVNSTRLVSRK', 729, 'P17119; D6W4D9;', 'KD00808', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'KAR3', '#Kinesin-like protein KAR3#Nuclear fusion protein', '-', '-', '856263'),
(809, 'Q9VJE5', 'Restin homolog', 'GO:0000776===c;k', 189065, 'Together CLIP-190 and jar may coordinate the interaction between the actin and microtubule cytoskeleton. May link endocytic vesicles to microtubules. May play a role in formation of furrows during cellularization. {ECO:0000269|PubMed:11076973; ECO:0000269|PubMed:9472041}.', 'MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSINSAYTDNSSAVLTANTEQFIIGQRVWLGGTRPGQIAFIGDTHFAAGEWAGVVLDEPNGKNDGCVSGKRYFQCEPKRGIFSRLTRLTTYPLAGAQTPTSPLAKSSPDRSRTVSPTASIRSSMLRSPGIGGKNGMAVGDRVIVSSGFGSRPGILRYLGETQFAPGNWCGVELDEPSGKNDGTVDDIRYFECKPKYGVFVPIAKVSLSPSSKKTRLSRTGSRESLTSIGTMNSIATTATSRMRMNAQQRKSSTPVKPILATPKSQFSMQDLLREKQQHVEKLMVERDLDREDAQNQALQLQKNINELKARIVELESALDNERKKTEELQCSIDEAQFCGDELNAQSQVYKEKIHDLESKITKLVSATPSLQSILPPDLPSDDGALQEEIAKLQEKMTIQQKEVESRIAEQLEEEQRLRENVKYLNEQIATLQSELVSKDEALEKFSLSECGIENLRRELELLKEENEKQAQEAQAEFTRKLAEKSVEVLRLSSELQNLKATSDSLESERVNKTDECEILQTEVRMRDEQIRELNQQLDEVTTQLNVQKADSSALDDMLRLQKEGTEEKSTLLEKTEKELVQSKEQAAKTLNDKEQLEKQISDLKQLAEQEKLVREMTENAINQIQLEKESIEQQLALKQNELEDFQKKQSESEVHLQEIKAQNTQKDFELVESGESLKKLQQQLEQKTLGHEKLQAALEELKKEKETIIKEKEQELQQLQSKSAESESALKVVQVQLEQLQQQAAASGEEGSKTVAKLHDEISQLKSQAEETQSELKSTQSNLEAKSKQLEAANGSLEEEAKKSGHLLEQITKLKSEVGETQAALSSCHTDVESKTKQLEAANAALEKVNKEYAESRAEASDLQDKVKEITDTLHAELQAERSSSSALHTKLSKFSDEIATGHKELTSKADAWSQEMLQKEKELQELRQQLQDSQDSQTKLKAEGERKEKSFEESIKNLQEEVTKAKTENLELSTGTQTTIKDLQERLEITNAELQHKEKMASEDAQKIADLKTLVEAIQVANANISATNAELSTVLEVLQAEKSETNHIFELFEMEADMNSERLIEKVTGIKEELKETHLQLDERQKKFEELEEKLKQAQQSEQKLQQESQTSKEKLTEIQQSLQELQDSVKQKEELVQNLEEKVRESSSIIEAQNTKLNESNVQLENKTSCLKETQDQLLESQKKEKQLQEEAAKLSGELQQVQEANGDIKDSLVKVEELVKVLEEKLQAATSQLDAQQATNKELQELLVKSQENEGNLQGESLAVTEKLQQLEQANGELKEALCQKENGLKELQGKLDESNTVLESQKKSHNEIQDKLEQAQQKERTLQEETSKLAEQLSQLKQANEELQKSLQQKQLLLEKGNEFDTQLAEYQKVIDEMDDAASVKSALLEQLQNRVAELETALRQANDAQKTAYLETKELRRQLESLELEKSREVLSLKAQMNGASSRSGKGDEVESLDIETSLAKINFLNSIIADMQQKNDALKAKVQTLETLPMDFTKPHAFDALTKRKPAPRLFCDICDEFDQHDTEDCPIQGSEDQDYSTPSSESNNNEKERKLPAPRKYCDSCEVFGHDTSECADDETY', 1690, 'Q9VJE5; O44929; Q8INY8; Q8MSD0;', 'KD00809', 'Drosophila melanogaster (Fruit fly)', 'CLIP-190', '#Restin homolog#Cytoplasmic linker protein 190#Microtubule-binding protein 190#d-CLIP-190', '-', '-', '35042'),
(810, 'Q29DY1', 'Kinesin-like protein Klp68D', 'GO:0003777', 89225, 'Plus-end directed microtubule motor that may be used for anterograde axonal transport and could conceivably move cargos in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors. {ECO:0000250|UniProtKB:P46867}.', 'MSAKSRRPGTASSQTPNECVQVVVRCRPMSNRERSEGSPEVVNVYPNRGVVELQNVVDANKEQRKVFTYDAAYDASASQTTLYHEVVFPLVSSVLEGFNGCIFAYGQTGTGKTFTMEGVRGNDDLMGIIPRTFEQIWLHINRTENFQFLVDVSYLEIYMEELRDLLKPNSKHLEVRERGSGVYVPNLHAINCKSVDDMIRVMKVGNKNRTVGFTNMNEHSSRSHAIFMIKIEMCDTETNTIKVGKLNLIDLAGSERQSKTGASAERLKEASKINLALSSLGNVISALAESSPHVPYRDSKLTRLLQDSLGGNSKTIMIANIGPSNYNYNETLTTLRYASRAKSIQNQPIKNEDPQDAKLKEYQEEIERLKRLIAPQQQQRSEKQGTIKKQRVKKPKKEPISQELIGSALQASSADLQVDEDRDSDGDGAESESDKENEAEVAKSNEELERERVENAKLAAKLAELEGQLVRGGKNLLDTYSERQIELEKKLVEIAERKKREIEIQQQLELQEETTLEIRERNVSLEQEVELKKRKLSKCYAKYLALQQELNDCKHDHNQDLRELEMAQNELVKELKRQLLIIDNFVPIEVKQRLYTQAKYDEEQEEWKFSSFPLPLPPSGGDGRQGYRRPVSHPQRRRPTSEHALQEAKSNAPSSLRFKSENIVSYELEMPCRTTQEYRTPKVSASLQAVLAQAMQTGGDDIDIVDSHTNSLRSRLENIINANSSSNGGPGSGAGPLAANTAGSGVGSMPNVRNIKSSRGLPSAGTALDSNRRPPTGRIPAKKPASAYPKARGLVNK', 797, 'Q29DY1;', 'KD00810', 'Drosophila pseudoobscura pseudoobscura (Fruit fly)', 'Klp68D', '#Kinesin-like protein Klp68D', '-', '-', '4812180'),
(811, 'Q2UMQ5', 'Histone acetyltransferase ESA1', 'GO:0034508', 58335, '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}.', 'MGVRDSHGEATATPDPVEKGFATLNTIRIGVKAMVQKDGELRKAEILSIRQRKDGPSFYVHYVDFNKRLDEWIDSTRIDLSHEVEWPQPEKPEKKKAGPGNKAPSKNAQKRARAGSREVSATPDLLTGKNTNIGKAQRPSKAGGKENRDETPANLSVLDSEAISADVTPKPEMEDVDMIGVSFTDTKEEHEQGKMSREEEIERLRTSGSMTQNPTEIHRVRNLNRLQMGKFDIEPWYFSPYPASFSDVDMVYIDEFCLSYFDNKRAFERHRSKCTLVHPPGNEIYRDDRISFFEVDGRRQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMATRDETGCHLVGYFSKEKDSAEGYNLACILTLPQYQRLGYGRLLIAFSYELSKREGKLGSPEKPLSDLGLLSYRQYWRETLVELLIEPGRESMSENELAVLTSMTEKDVHETLVVFNMLRYHKGNWVIVLTDQVVEQHNKRLEKEKIKGSRKIDPARLQWKPPVFTASSRTWNW', 506, 'Q2UMQ5;', 'KD00811', 'Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)', 'esa1', '#Histone acetyltransferase ESA1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}', '-', '-', '5991133'),
(812, 'Q9GZM8', 'Nuclear distribution protein nudE-like 1', 'GO:0000776===GO:0000777===c;k', 38375, '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:12556484; ECO:0000269|PubMed:14970193; ECO:0000269|PubMed:16291865; ECO:0000269|PubMed:17600710}.', 'MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV', 345, 'Q9GZM8; B3KP93; D3DTS0; J3QT32; Q86T80; Q8TAR7; Q9UH50;', 'KD00812', 'Homo sapiens (Human)', 'NDEL1', '#Nuclear distribution protein nudE-like 1#Protein Nudel#Mitosin-associated protein 1', '-', 'ENSG00000166579', '-'),
(813, 'Q9QWT9', 'Kinesin-like protein KIFC1', 'GO:0003777', 74153, 'Minus end-directed microtubule-dependent motor required for bipolar spindle formation. May contribute to movement of early endocytic vesicles. {ECO:0000269|PubMed:16638812; ECO:0000269|PubMed:17360972}.', 'MDVQAQRPPLLEVKRNVELKAALVKSSSRVPLSASRLKRGPDQMEDALEPAKKRTRVMGAVTKVDTSRPRGPLLSTVSQTQGHTAAQKGPKKTGPRGCSAIGTVLRSQKPVPAAPAQKPGTSTAPVVVGKRAGKRPAWDLKGQLCDLNEELKRYREKTQTLELENRGLREQLREVQEQATTLGTERNTLEGELASVRSRAEQDQQRLETLSARVLELEECLGTRERLLQELQGERLQLQEERSTLSTQLEEQERRFQATEAALSSSQEEVVCLRQKTEAQVTLLAEQGDRLYGLEMERRRLHNQLQELKGNIRVFCRVRPVLEGESTPSPGFLVFPPGPAGPSDPPTGLSLSRSDDRRSTLTGAPAPTVRHDFSFDRVFPPGSKQEEVFEEIAMLVQSALDGYPVCIFAYGQTGSGKTFTMEGGPRGDPQLEGLIPRAMRHLFSVAQEMSGQGWTYSFVASYVEIYNETVRDLLATGPRKGQGGECEIRRASPGSEELTVTNARYVPVSCEKEVEALLHLAHQNRAVAHTAQNKRSSRSHSVFQLQISGEHAARGLQCGAPLNLVDLAGSERLDPGLHLGPGERDRLRETQAINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIGTAQANKK', 674, 'Q9QWT9; O08671; O35230; Q497Y3; Q4A1N2; Q6PG90; Q8BV06; Q99L84;Q9JKZ0;', 'KD00813', 'Mus musculus (Mouse)', 'Kifc1', '#Kinesin-like protein KIFC1', '-', '-', '100502766'),
(814, 'Q8BJS8', 'Mdm2-binding protein', 'GO:0000776===GO:0034501', 100314, 'May play a role in MDM2-dependent p53/TP53 homeostasis in unstressed cells. Inhibits autoubiquitination of MDM2; thereby enhancing MDM2 stability. This promotes MDM2-mediated ubiquitination of p53/TP53 and its subsequent degradation. Inhibits cell migration in vitro and suppresses the invasive behavior of tumor cells. {ECO:0000269|PubMed:10906133; ECO:0000269|PubMed:15632057}.', 'MDRYLLLVTWREGKFRSVAGGEIEPGTEATSLESTDKQPDLTATNIYHLLKRSISDSIHPDDSTFPACSVGGTPHSRKWFFAVQAICGFYQFCSSDWQEIHFDAEKDKIEDVLQANIEECQSAVECFEEDDSNSRESLPLADLYEESAENLHQLSDKLPAPGRAMIDIILLPSDKDPPKLKECLPIVGALKHLKEWHSAKVIIAGSYCEINCQKIAEYLSASVVPLEEFRNAIDPRELWRGEIQMRERKFGFEISFPEFCLKGVTPTNVSAYNLNTCFLAKKIASSKVFHYYGPALEFVQMIKLSDLPSCYMSDIEFELEVTGHCTRQNSMLLLEQISSLCGKVGALFVLPCTVSNVLIPPPSQLASRKWKEYMAKKPKTISVPDVAVKGEFSGYHLLLQGMGKRKCRATLLHSASQINGSFALSVIHGKMKTKAGEARPSFPFDFSSLPRFSEEQVLQREKQLASFQVLALKECLKRRKAANQPEAFSADELKSLLALTRERFLGHFDVLPTEAALAQTDTVKAAGVVNDDGTVEPYSSSLMETNPLEWPERHVLQNLETSEKAKQKMRTGSLPRSSEQLLGHKEGPRDSLTLLDAKELLKYFTSDGLPVGDLQPLHIQRGEKPFVLTPELSPGKLQVLPFEKASECHYHGIEYCLDDQKALERDGGFSELQSRLIRYETQTTCTRDSFPVPTVLSPLPSPAVLSEPQSVPEGEALQGELRTEVSGLKRRSKDPSCLYPQKRLTRSESSDCLPSQASCNSNHHHHTGKPRKPQAERCVSGLPLPGREASKDTSKTSSGQKRAHESKSSKQMKESRSQKHTRMLKEVVKDTLKRHHITEAHESFTACSQRLFDISKFYLKDLKTSRGLFEEMKKTANNNVVQVIEWVVEKMSKK', 894, 'Q8BJS8; Q80VU3; Q8BTU9; Q8BTW0; Q99K25; Q9ER61;', 'KD00814', 'Mus musculus (Mouse)', 'Mtbp', '#Mdm2-binding protein#mMTBP', '-', '-', '105837'),
(815, 'O70201', 'Baculoviral IAP repeat-containing protein 5', 'GO:0000777===GO:0032133', 16298, '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}.', 'MGAPALPQIWQLYLKNYRIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQMEELTVSEFLKLDRQRAKNKIAKETNNKQKEFEETAKTTRQSIEQLAA', 140, 'O70201; Q923F7; Q9WU53; Q9WU54;', 'KD00815', 'Mus musculus (Mouse)', 'Birc5', '#Baculoviral IAP repeat-containing protein 5#Apoptosis inhibitor 4#Apoptosis inhibitor survivin#TIAP', '-', '-', '11799');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(816, 'P32383', '1-phosphatidylinositol 4;5-bisphosphate phosphodiesterase 1', 'GO:0034501===GO:0000778===k', 100548, 'The production of the second messenger molecules diacylglycerol (DAG) and inositol 1;4;5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Required for cell growth; osmoresistance and expression of GPD1. {ECO:0000269|PubMed:12073033}.', 'MTESAIDDQRFNLTKELQRHSCRDQGKITQKDDALDFISYSSFQSSFNTDQKSANNGSTVRRSIRSIFRRAAELPRVHMGPLTYSHGINELVNKKLRKDCDLSTLCRVLQRGIRMIRMTRRRRKFYEFKLINNNGQIIWKDGSKYLELDSVKDIRIGDTASTYQEEVDPKRLRSDSKLWIAIIYKVSNKLKALHVVALNELDFNTFLSCICGLVKLRRELMESILLPDNSQFARIHWQITVSEKEEDEKKDTLSFADVKKLCDKFHIYVSTGQLLEFFQLADINHNGLLNYFEFEKFIKILKNRKEVNMIWSKFTKPPHSHLSFENFFQFLITEQHEQVDRQTAWSYFIKYREPTQLTMGQDGFTKFLKEQPYLVEVKEELYSKPLNHYFIASSHNTYLLGKQIAETPSVEGYIQVLQQGCRCVEIDIWDGENGPVVCHGFLTSAIPLKTVIRVIKKYAFITSPYPLIISLEINCNKDNQKLASLIMREVLAEQLYFVGTRTDKLPSPRELKHKILLKSKKTSEATRGLSVNEPFPSSFSSSYESANEQELRMKDDSTNSSSATNSSSMQRIKRIGLKKHADIINDVSNISGIHGIKFRNFSLPESKTIAHCFSLNERKVEYMIKDKHLKLSLDKHNRRYLMRVYPHVLRYKSSNFNPIPFWKAGVQMVATNWQTNDIGQQLNLAMFQILDHQPDGSFKSGYVLKPKKLLPVVTKAKMIPLIYEHFENGSDPVTVKIRILSTQLLPRLNDTSPSRNNTNSFVKVEFHTDDEPTMPISIDKGTRISATEASTKSSQGNGFNPIWDAEVSITLKDTDLTFIKFMVISEETQIASVCLKLNYLRMGYRHIPLFNMEGEQYIFCTLFIHTQIL', 869, 'P32383; D6W3A2;', 'KD00816', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'PLC1', '#1-phosphatidylinositol 4;5-bisphosphate phosphodiesterase 1#3.1.4.11#Phosphoinositide phospholipase C#Phospholipase C-1#PLC-1', '-', '-', '855860'),
(817, 'Q4JIM4', 'Presenilin-1', 'GO:0000776', 52831, 'Probable catalytic subunit of the gamma-secretase complex; an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx; cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin; thus negatively regulating Wnt signaling. May also play a role in hematopoiesis (By similarity). {ECO:0000250}.', 'MTELSAHLPQFQHGQMTENFPDNHLSNTNDNSERRRHDNSERRRNDNPGSETNGQPQNNIQQVVDQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEETDTIGQRALNSILNAAIMISVIIVMTILLVVLYKYRCYKVIHGWLIISSLLLLFFFSFIYLGEVFKTYNVAMDYITVALIIWNFGVVGMICIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEEDPEGQRKASKNSTYDKQAPANQSQNEDAEADDGGFSQEWQQQRDNRIGPIESTPESRAAVQALPSNSQTSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTLACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDNLVQPFMDQLAFHQFYI', 468, 'Q4JIM4; Q90X08;', 'KD00817', 'Gallus gallus (Chicken)', 'PSEN1', '#Presenilin-1#PS-1#3.4.23.-#Presenilin-1 NTF subunit#Presenilin-1 CTF subunit', '-', '-', '373977'),
(818, 'Q9Y6G9', 'Cytoplasmic dynein 1 light intermediate chain 1', 'GO:0000776===GO:0000777===GO:0003777===GO:0005868===SCL', 56579, '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. {ECO:0000269|PubMed:19229290}.', 'MAAVGRVGSFGSSPPGLSSTYTGGPLGNEIASGNGGAAAGDDEDGQNLWSCILSEVSTRSRSKLPAGKNVLLLGEDGAGKTSLIRKIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDAVSLKDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKQMEQKLIRDFQEYVEPGEDFPASPQRRNTASQEDKDDSVVLPLGADTLTHNLGIPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKAEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVSGGSPAGGAGGGSSGLPPSTKKSGQKPVLDVHAELDRITRKPVTVSPTTPTSPTEGEAS', 523, 'Q9Y6G9; A2RRG7; Q53HC8; Q53HK7;', 'KD00818', 'Homo sapiens (Human)', 'DYNC1LI1', '#Cytoplasmic dynein 1 light intermediate chain 1#LIC1#Dynein light chain A#DLC-A#Dynein light intermediate chain 1; cytosolic', '-', 'ENSG00000144635', '-'),
(819, 'Q63100', 'Cytoplasmic dynein 1 intermediate chain 1', 'GO:0000776===GO:0000777===GO:0003777===GO:0005868', 72754, '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.', 'MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVPDDSDLDRKRRETEALLQSIGISPEPPLVQPLHFLTWDTCYFHYLVPTPMSPSSKSVSTPSEAGSQDDLGPLTRTLQWDTDPSVLQLQSDSELGRRLNKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSEEDEEDEEMVEPKVGHDSELENQDKKQETKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYSNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNSDTEVPTASVAIEGAYALNRVRWAQGGKEVAVGDSEGRIWIYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGAVELAA', 643, 'Q63100;', 'KD00819', 'Rattus norvegicus (Rat)', 'Dync1i1', '#Cytoplasmic dynein 1 intermediate chain 1#Cytoplasmic dynein intermediate chain 1#Dynein intermediate chain 1; cytosolic#DH IC-1', '-', '-', '29564'),
(820, 'P32364', 'Kinesin-related protein SMY1', 'GO:0003777', 73799, 'Possible microtubule-based motor that can interact or substitute with myosin 2 (MYO2).', 'MHWNIISKEQSSSSVSLPTLDSSEPCHIEVILRAIPEKGLQNNESTFKIDPYENTVLFRTNNPLHETTKETHSTFQFDKVFDANATQEDVQKFLVHPIINDVLNGYNGTVITYGPSFSGKSYSLIGSKESEGILPNICKTLFDTLEKNEETKGDSFSVSVLAFEIYMEKTYDLLVPLPERKPLKLHRSSSKMDLEIKDICPAHVGSYEDLRSYIQAVQNVGNRMACGDKTERSRSHLVFQLHVEQRNRKDDILKNSSLYLVDLHGAEKFDKRTESTLSQDALKKLNQSIEALKNTVRSLSMKERDSAYSAKGSHSSAYRESQLTEVLKDSLGGNRKTKVILTCFLSNVPTTLSTLEFGDSIRQINNKVTDNTTGLNLKKKMDLFIQDMKIKDDNYVAQINILKAEIDSLKSLHNKSLPEDDEKKMLENTKKENIKLKLQLDSITQLLSSSTNEDPNNRIDEEVSEILTKRCEQIAQLELSFDRQMNSNSKLQQELEYKKSKEEALESMNVRLLEQIQLQEREIQELLTTNAILKGELETHTKLTETRSERIKSLESSVKELSLNKSAIPSPRRGSMSSSSGNTMLHIEEGSEISNSPWSANTSSKPLVWGARKVSSSSIATTGSQESFVARPFKKGLNLHSIKVTSSTPKSPSSGS', 656, 'P32364; D6VXK8;', 'KD00820', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SMY1', '#Kinesin-related protein SMY1#Suppressor protein SMY1', '-', '-', '853783'),
(821, 'Q2TA06', 'Aurora kinase A', 'GO:0032133===GO:0000780', 45462, 'Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle; centrosome duplication; centrosome separation as well as maturation; chromosomal alignment; spindle assembly checkpoint; and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins; including ARHGEF2; BORA; BRCA1; CDC25B; DLGP5; HDAC6; KIF2A; LATS2; NDEL1; PARD3; PPP1R2; PLK1; RASSF1; TACC3; p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway; and particularly the checkpoint-response pathways critical for oncogenic transformation of cells; by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors; the protein phosphatase type 1 (PP1) isoforms; to inhibit their activity (By similarity). Necessary for proper cilia disassembly prior to mitosis (By similarity). Interacts with SIRT2 (By similarity). {ECO:0000250}.', 'MDRCKENCISGPKTAVPLSDGPKRVPVAQQFPSQNPVSVNSGQAQRVLCPTNSSQRVPSQAQKLVSIQKPVQTLKQKPPQAASAPRPVTRPPSNTQKSKQPQPPAPGNNPEKEVASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGAVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEADTYQETYRRISRVEFTFPDCVPEGARDLISRLLKHNPSQRPTLKEVLEHPWIIANSKPSSCQKKESTSKQS', 402, 'Q2TA06;', 'KD00821', 'Bos taurus (Bovine)', 'AURKA', '#Aurora kinase A#2.7.11.1#Aurora 2#Aurora/IPL1-related kinase 1#ARK-1#Aurora-related kinase 1#Serine/threonine-protein kinase 15#Serine/threonine-protein kinase 6#Serine/threonine-protein kinase aurora-A', '-', '-', '504437'),
(822, 'Q90694', 'Cell division control protein 42 homolog', 'GO:0051988', 21273, '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 (By similarity). {ECO:0000250}.', 'MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKTRRCVLL', 191, 'Q90694;', 'KD00822', 'Gallus gallus (Chicken)', 'CDC42', '#Cell division control protein 42 homolog#G25K GTP-binding protein', '-', '-', '395917'),
(823, 'B4JEY0', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 23900, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MTEQFDTRRRLMAMFRNEMRMEKLENTIAKKSTKFHTNSAALMTTIDLQQRKFEKLNALITRRCEDINTRTAFTRAVREKLAEERQKNAEMQAQLEKANDERIEQMDCVRTLSDASNTFINPSALPARLKGVTVLREEGRWISLDYDGDDLKGLSTFWAQAHSGSASQKWQQLLSMDKAIMPTLNDKGNVNVSVSSIIEIDLTASPSHK', 209, 'B4JEY0;', 'KD00823', 'Drosophila grimshawi (Fruit fly) (Idiomyia grimshawi)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6563035'),
(824, 'P53086', 'Kinesin-like protein KIP3', 'k', 91090, '', 'MNVPETRQSSIVVAIRVRPFTSMEKTRLVNEASGAEANFPGLGDSSLILPMSNNSDSDIDIDAEEGSTRSKRNSLLRRKVIRPEGIRKIVDCVDDRMLIFDPADRNPLNKVSDQVLNSMRARATKATASSINNSNATNKFSSQRRRHGGEIKFVFDKLFDETSSQARVYKETTSPLLDSVLDGFNSTVFAYGATGCGKTYTVSGTPSQPGIIFLAMEELFNKITDLKDEKDFEISLSYLEIYNERIRDLLKPETPSKRLVIREDTQNHIKVANLSYHHPNTVEDVMDLVVQGNINRTTSPTEANEVSSRSHAVLQIHIMQTNKLVDLTSQHTFATLSIIDLAGSERAAATRNRGIRLHEGANINRSLLALGNCINALCLNDGSRSCHIPYRDSKLTRLLKFSLGGNCKTVMIVCISPSSSHYDETLNTLKYANRAKEIKTKIIRNQQSLSRHVGSYLKMITEQKRQIEELREREEKMISLKLTKYKLNKEKIQLAINECVNRVQQTYAGVETYQVAKTLKSLILCKRRFLQMVKLEVDNLILLFEREESTAAEMQPVISNCRMISGQLYNKIHELEMKFDETDTLSSVIHQVHSIDLNKLREMEDWDETYDLVYLESCLNQISELQRNEILVNSSIMTEKLMSDPGLNSRFKFLSKWLMNRTPNIESIIQDLVHIDEEFESFARTFIANPDSNFTNTNINIINTTAADLAVPAETLQRQNFSQKKVKWTSPDLSPSPMIEPQPELEPELHQDQDAIASEVDVSMQDTTFNEQGPSTPSAPTTAVPRRKMRSSLLTHQSLLATARK', 805, 'P53086; D6VTU0;', 'KD00824', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'KIP3', '#Kinesin-like protein KIP3', '-', '-', '852655'),
(825, 'Q5ZKV8', 'Kinesin-like protein KIF2A', 'GO:0003777', 79864, '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}.', 'MAAANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLAPDEDIEPSPETQPLPAPSAKVNKIVKGRRTVAPVKNDTPARDNRVASSARARPTQLPEQSSSSQQNGTVSGISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGNLDYRPLTTADPIDEHRICVCVRKRPLNRKETLMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDETAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIEIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTIDPSAAGDIRPIIHHTPSQIDDLDTQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRTVFQESIRWLEDEKALLEMTEEVDYDVDSYATQLEAILDQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAV', 706, 'Q5ZKV8;', 'KD00825', 'Gallus gallus (Chicken)', 'KIF2A', '#Kinesin-like protein KIF2A', '-', '-', '427156'),
(826, 'Q8BK63', '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. 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:21930935}.', 'MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKTKSNMKGF', 337, 'Q8BK63; Q3UIL0; Q64506; Q80XI2; Q99LY3;', 'KD00826', 'Mus musculus (Mouse)', 'Csnk1a1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', '-', '93687'),
(827, 'Q75UQ2', 'Craniofacial development protein 1', 'GO:0000777', 32969, 'May play a role during embryogenesis. {ECO:0000250}.', 'MEEFDSEDFSTSDEDEDYVPSGGEYSEDDVNELVKEDEVDGEEQAEKTKGKRRKAQSIPARKRKQSGLLLDEEEDGEEDSGGSSREEDEEEQEGGLGSETSRKKKEDELWASFLNDVGTKSKAASSSQVKVAEETEETSSSKPLVKADELEKPKESEKVKITKVFDFAGEEVRVTKEVDATSKEAKSFLKQTEKEKPQALVTSAATPPPAGSGIKRTSGMSSLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLERVDHRQFEIERDLRLSKMKP', 295, 'Q75UQ2;', 'KD00827', 'Rattus norvegicus (Rat)', 'Cfdp1', '#Craniofacial development protein 1#Bucentaur', '-', '-', '292027'),
(828, 'O76447', 'HCP-1', 'k', 166763, '', 'MDESPIFDNENKRSAGNKRQQTESPFSAATPKSRLGREPKRIFGTSSGNMADSNLEETCLEHDSRPSSASSITPADNTSLLDLSTVTALATDDASFVGTNDASITPGSNVDVNLEQSELYDTSNCTSNLSMVQESDETDADATLSNDFDNQLALDGETTPTASRTPMSQILSRECTPTVSNPQLLTEIAKGVDQPTKPVRDVPQSPVLPVKGHIDFSLHEFEMLEQNSEHEESIKLLQSQIELLRQSHSQQLSEIQEARIFEEKMLTQQVDSAMKKAKSDREAAKAREQVLEKQVQELRLKLEEPDEEKNQLVHNLAALNAQIEELTQKALKVDSMQQGATASEDRIRELIGGHQEAIKQLENTKQMNESLQRDLVEKEARFSEEMERIRTESQTTSESLKYEHELVRKMMIEDMEKLEAEVLALKSQQANLEIQEFHDKIKQLELEVQLSSENKEKLQAELMVVQEKASENIKNAEEKVNGLEAEVEKLRFEATNNSRVVELEQQLEEFRSLMIKEISDLENQLEAAKLESGSTSEPNAQLEASQATIQELTSEMKMQLEEVKRQSDENNSLNVHLTSSNEKIAELTSSLEMVAAQLLSSQQETDVAVTKVENLELKMEEAHRMYLLDIELSRVKIDELQSSIEVLSKLEREVQSSNLQNEELKLSLRNFEELQADLAMSKAKNEELEQQIEDSSREFSVITEASKEMKLKWDSSEAQMSEMIASLAAFQEEMQSTQADAVASEDKVKQVESLLENLKEPLEELNNLRANLKDSNDKILDLQSQLELAQQSSDLADRLQEDLRTSDARVQELNIQVSELEQQIEVSSREFSVITEANKEMQLKLDSSEAQISEMTASLTAFQEEMQSTRADAVASEDKVKELESLLENLKEPLEELNNLRANLKDSNGKVLELQSQLDLAQQFSDLTDRLQEDLRTSDARVQELNVQVSDLQSELETARQDTNAVQVVMEALKSEQGESYEALRAELDAAVQEKGRSSDLVTSLEGKIQELETAIESSTAENVQKSKTIQDFTDKVSLLESQICELKSQNEQMEIDTNLNMDQLSEMSSQLESANAELIELTRTSAETIDKLRGEVEKSTKAMMDQEEHLAELVAKIESRDVENADQAAKHKEEQERLQSVIDTLRTSQSTIEESQAKSEELNSRIKELQASIEFAQKALADTENAKQEKVEELEKVQEQMLNLVQAFEVEKASIRLEWNSSLSNANEKLEAAEEALSQKENTIVTLESRIETISQQFEARLEEANVWKSQAMQLGTLTQSLSQMQRQLGEMHEKMEASDRRVIEVEEQAQHDITLIQVENKEQSEALEQAHSRILELEEKLVRAEIEIQRLEKVCDAFDDDEREYKDKIMTLQSEIKQLKGVKTPPRVMGLIEQARLGVKQLSRESSLVEPQNSAHEDAFEDAQNSFQDRLQTMSNTTARQIDASNHHPEDHVLEKSARETPSKKNRSNCQHQ', 1475, 'O76447;', 'KD00828', 'Caenorhabditis elegans', 'hcp-1', '#HCP-1 {ECO:0000313|EMBL:CCD68844.1}', '-', '-', '179049'),
(829, 'O08901', 'Mitotic checkpoint serine/threonine-protein kinase BUB1', 'GO:0000776===GO:0000777===GO:0000780===k', 119563, '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. Essential during early and later stages of embryonic development. Necessary for postimplantation embryogenesis and proliferation of primary embryonic fibroblasts and plays an important role in spermatogenesis and fertility. {ECO:0000269|PubMed:17925231; ECO:0000269|PubMed:17938250; ECO:0000269|PubMed:19772675}.', 'MDNLENVFRMFEAHMQSYTGNDPLGEWESFIKWVEENFPDNKEYLMTLLEHLMKEFLHKKNYHNDSRFINYCLKFAEYNSDRHQFFEFLYNQGIGTKSSYIYMSWAGHLEAQGELQHASAIFQTGIHNEAEPKELLQQQYRLFQARLTGIHLPAQATTSEPLHSAQILNQVMMTNSSPEKNSACVPKSQGSECSGVASSTCDEKSNMEQRVIMISKSECSVSSSVAPKPEAQQVMYCKEKLIRGDSEFSFEELRAQKYNQRKKHEQWVSEDRNYMKRKEANAFEEQLLKQKMDELHKKLHQVVELSHKDLPASENRPDVSLVCVGQNTCSQQELRGPSLSSISHQTSESSGEKPQEEPSVPLMVNAVNSTLLFPAANLPALPVPVSGQSLTDSRCVNQSVHEFMPQCGPETKEVCETNKVASINDFHTTPNTSLGMVQGTPCKVQPSPTVHTKEALGFIMDMFQAPTLPDISDDKDEWPSLDQNEDAFEAQFQKNAVSSGDWGVKKIMTLSSAFPIFEDGNKENYGLPQPKNKPLGARTFGERSLSKYSSRSNEMPHTDEFMDDSTVCGIRCNKTLAPSPKSIGDFTSAAQLSSTPFHKFPADLVQIPEDKENVVATQYTHMALDSCKENIVDLSKGRKLGPIQEKISASLPCPSQPATGGLFTQEAVFGLEAFKCTGIDHATVEDLSDANAGLQVECVQTLGNVNAPSFTVENPWDDELILKLLSGLSKPVTSYSNTFEWQSKLPAIKTKTEYQLGSLLVYVNHLLGEGAFAQVFEAIHGDVRNAKSEQKCILKVQRPANSWEFYIGMQLMERLKPEVHHMFIKFYSAHLFKNGSILVGELYSYGTLLNVINLYKNTSEKVMPQALVLTFAIRMLYMVEQVHSCEIIHGDIKPDNFILGHRFLEQADEDLATGLALIDLGQSIDMKLFPKGTVFTGKCETSGFQCPEMLSNKPWNYQIDYFGVAATIYCMLFGSYMKVKNEGGVWKPEGLFRRLPHLDMWEEFFHIMLNIPDCHNLPSLDFLRQNMKKLLEQQYSNKIKTLRNRLIVMLSEYKRSRK', 1058, 'O08901; O09007;', 'KD00829', 'Mus musculus (Mouse)', 'Bub1', '#Mitotic checkpoint serine/threonine-protein kinase BUB1#mBUB1#2.7.11.1#BUB1A', '-', '-', '12235'),
(830, 'Q8NI77', 'Kinesin-like protein KIF18A', 'GO:0005828===c;k;s', 102281, '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. {ECO:0000269|PubMed:17346968; ECO:0000269|PubMed:18267093; ECO:0000269|PubMed:18513970; ECO:0000269|PubMed:19625775}.', 'MSVTEEDLCHHMKVVVRVRPENTKEKAAGFHKVVHVVDKHILVFDPKQEEVSFFHGKKTTNQNVIKKQNKDLKFVFDAVFDETSTQSEVFEHTTKPILRSFLNGYNCTVLAYGATGAGKTHTMLGSADEPGVMYLTMLHLYKCMDEIKEEKICSTAVSYLEVYNEQIRDLLVNSGPLAVREDTQKGVVVHGLTLHQPKSSEEILHLLDNGNKNRTQHPTDMNATSSRSHAVFQIYLRQQDKTASINQNVRIAKMSLIDLAGSERASTSGAKGTRFVEGTNINRSLLALGNVINALADSKRKNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSVFYDDTYNTLKYANRAKDIKSSLKSNVLNVNNHITQYVKICNEQKAEILLLKEKLKAYEEQKAFTNENDQAKLMISNPQEKEIERFQEILNCLFQNREEIRQEYLKLEMLLKENELKSFYQQQCHKQIEMMCSEDKVEKATGKRDHRLAMLKTRRSYLEKRREEELKQFDENTNWLHRVEKEMGLLSQNGHIPKELKKDLHCHHLHLQNKDLKAQIRHMMDLACLQEQQHRQTEAVLNALLPTLRKQYCTLKEAGLSNAAFESDFKEIEHLVERKKVVVWADQTAEQPKQNDLPGISVLMTFPQLGPVQPIPCCSSSGGTNLVKIPTEKRTRRKLMPSPLKGQHTLKSPPSQSVQLNDSLSKELQPIVYTPEDCRKAFQNPSTVTLMKPSSFTTSFQAISSNINSDNCLKMLCEVAIPHNRRKECGQEDLDSTFTICEDIKSSKCKLPEQESLPNDNKDILQRLDPSSFSTKHSMPVPSMVPSYMAMTTAAKRKRKLTSSTSNSSLTADVNSGFAKRVRQDNSSEKHLQENKPTMEHKRNICKINPSMVRKFGRNISKGNLR', 898, 'Q8NI77; Q4VPE3; Q86VS5; Q9H0F3;', 'KD00830', 'Homo sapiens (Human)', 'KIF18A', '#Kinesin-like protein KIF18A#Marrow stromal KIF18A#MS-KIF18A', '-', 'ENSG00000121621', '-'),
(831, 'P13681', 'Serine/threonine-protein phosphatase PP1-1', 'k', 37636, 'Essential role in cell cycle control. PP1 is perhaps required for exit from mitosis.', 'MSNPDVDLDSIIDRLLEVRGSRPGRQVQLSEDEIRFLCNKAREIFISQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLEVICLLLAYKIKYPENFFILRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIIDEKIFTMHGGLSPDLNSMDQIQRIMRPTDVPDTGLLCDLLWSDPDKDLTGWGDNDRGVSFTFGPDVVSRFLHKHDMDLVCRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGAMMSVDESLLCSFQILKPAEKKQRYGYQGSSQNWHMTPPRKNKTGNSK', 327, 'P13681;', 'KD00831', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dis2', '#Serine/threonine-protein phosphatase PP1-1#3.1.3.16', '-', '-', '2541193'),
(832, 'P20439', 'G2/mitotic-specific cyclin-B', 'GO:0008608', 59256, 'Essential for the control of the cell cycle at the G2/M (mitosis) transition.', 'MVGTTLKMRGDENASENFKQVQLKKLTVPSMEATTKRAALGDLQNRGISRPIAAKDAAQKDSKDLKLTDALRNAKARVDSHWKKQPLGSTNGNGNGAVPPKVNEGGVSAFLRSNSVRNRVPTKTTVEPTKVTVKSSSSENVNEPTLKREDSNLSKKSLTKLRAALAKPVMGVSGIRREPVAVSRKEAETKKELPETKKDSLEVKKDATRMPLIRGNSAVTTTTSTMPTTMSLSSKRLAGIEDIDANDKENLVLVSEYVNDIYDYLYQVELEQPIHKDHLAGQKEVSHKMRAVLIDWINEVHLQFHLAAETFQLAVAIIDRYLQVVKDTKRTYLQLVGVTALFIATKYEELFPPAIGDFVFITDDTYTARQIRQMELQIFKAIDCNLSRPLPIHFLRRYSKAAGAEDEHHTMSKYFIELASVDYEMATYRPSEIAAASLFLSLHLLNGNHRAGTGFNDRHWTPTLTFYSRYSAAHLRPITRLIAKLARDAPQAKLKAIYNKYQGSKFQKIALRTELTGALMDSIVGQSQRK', 530, 'P20439; Q0E8Y2; Q8MME2; Q9I7V2; Q9TYH6; Q9TYH7; Q9V3F4;', 'KD00832', 'Drosophila melanogaster (Fruit fly)', 'CycB', '#G2/mitotic-specific cyclin-B', 'BIOMD0000000144,Calzone2007_CellCycle;', '-', '37618'),
(833, 'Q8IVF4', 'Dynein heavy chain 10; axonemal', 'GO:0003777', 514841, '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). Probable inner arm dynein heavy chain. {ECO:0000250}.', 'MVPEEVEVEIDEIPVLSEEGEEEEETYSQKVESVDKVRAKRVSLRTESLGQPLNREDEEMDKEISEKLPSKRTAKHIMEKMHLHMLCTPLPEEFLDQNVVFFLRNTKEAISEATDMKEAMEIMPETLEYGIINANVLHFLKNIICQVFLPALSFNQHRTSTTVGVTSGEVSNSSEHESDLPPMPGEAVEYHSIQLIRDEFLMNVQKFASNIQRTMQQLEGEIKLEMPIISVEGEVSDLAADPETVDILEQCVINWLNQISTAVEAQLKKTPQGKGPLAEIEFWRERNATLSALHEQTKLPIVRKVLDVIKESDSMLVANLQPVFTELFKFHTEASDNVRFLSTVERYFKNITHGSGFHVVLDTIPAMMSALRMVWIISRHYNKDERMIPLMERIAWEIAERVCRVVNLRTLFKENRASAQSKTLEARNTLRLWKKAYFDTRAKIEASGREDRWEFDRKRLFERTDYMATICQDLSDVLQILEEFYNIFGPELKAVTGDPKRIDDVLCRVDGLVTPMENLTFDPFSIKSSQFWKYVMDEFKIEVLIDIINKIFVQNLENPPLYKNHPPVAGAIYWERSLFFRIKHTILRFQEVQEILDSDRGQEVKQKYLEVGRTMKEYEDRKYEQWMEVTEQVLPALMKKSLLTKSSIATEEPSTLERGAVFAINFSPALREIINETKYLEQLGFTVPELARNVALQEDKFLRYTAGIQRMLDHYHMLIGTLNDAESVLLKDHSQELLRVFRSGYKRLNWNSLGIGDYITGCKQAIGKFESLVHQIHKNADDISSRLTLIEAINLFKYPAAKSEEELPGVKEFFEHIERERASDVDHMVRWYLAIGPLLTKVEGLVVHTNTGKAPKLASYYKYWEKKIYEVLTKLILKNLQSFNSLILGNVPLFHTETILTAPEIILHPNTNEIDKMCFHCVRNCVEITKHFVRWMNGSCIECPPQKGEEEEVVIINFYNDISLNPQIIEQAVMIPQNVHRILINLMKYLQKWKRYRPLWKLDKAIVMEKFAAKKPPCVAYDEKLQFYSKIAYEVMRHPLIKDEHCIRLQLRHLANTVQENAKSWVISLGKLLNESAKEELYNLHEEMEHLAKNLRKIPNTLEDLKFVLATIAEIRSKSLVMELRYRDVQERYRTMAMYNLFPPDAEKELVDKIESIWSNLFNDSVNVEHALGDIKRTFTELTRGEIMNYRVQIEEFAKRFYSEGPGSVGDDLDKGVELLGVYERELARHEKSRQELANAEKLFDLPITMYPELLKVQKEMSGLRMIYELYEGLKVAKEEWSQTLWINLNVQILQEGIEGFLRALRKLPRPVRGLSVTYYLEAKMKAFKDSIPLLLDLKNEALRDRHWKELMEKTSVFFEMTETFTLENMFAMELHKHTDVLNEIVTAAIKEVAIEKAVKEILDTWENMKFTVVKYCKGTQERGYILGSVDEIIQSLDDNTFNLQSISGSRFVGPFLQTVHKWEKTLSLIGEVIEIWMLVQRKWMYLESIFIGGDIRSQLPEEAKKFDNIDKVFKRIMGETLKDPVIKRCCEAPNRLSDLQNVSEGLEKCQKSLNDYLDSKRNAFPRFFFISDDELLSILGSSDPLCVQEHMIKMYDNIASLRFNDGDSGEKLVSAMISAEGEVMEFRKILRAEGRVEDWMTAVLNEMRRTNRLITKEAIFRYCEDRSRVDWMLLYQGMVVLAASQVWWTWEVEDVFHKAQKGEKQAMKNYGRKMHRQIDELVTRITMPLSKNDRKKYNTVLIIDVHARDIVDSFIRGSILEAREFDWESQLRFYWDREPDELNIRQCTGTFGYGYEYMGLNGRLVITPLTDRIYLTLTQALSMYLGGAPAGPAGTGKTETTKDLAKALGLLCVVTNCGEGMDYRAVGKIFSGLAQCGAWGCFDEFNRIDASVLSVISSQIQTIRNALIHQLTTFQFEGQEISLDSRMGIFITMNPGYAGRTELPESVKALFRPVVVIVPDLQQICEIMLFSEGFLEAKTLAKKMTVLYKLAREQLSKQYHYDFGLRALKSVLVMAGELKRGSSDLREDVVLMRALRDMNLPKFVFEDVPLFLGLISDLFPGLDCPRVRYPDFNDAVEQVLEENGYAVLPIQVDKVVQMFETMLTRHTTMVVGPTRGGKSVVINTLCQAQTKLGLTTKLYILNPKAVSVIELYGILDPTTRDWTDGVLSNIFREINKPTDKKERKYILFDGDVDALWVENMNSVMDDNRLLTLANGERIRLQAHCALLFEVGDLQYASPATVSRCGMVYVDPKNLKYRPYWKKWVNQIPNKVEQYNLNSLFEKYVPYLMDVIVEGIVDGRQAEKLKTIVPQTDLNMVTQLAKMLDALLEGEIEDLDLLECYFLEALYCSLGASLLEDGRMKFDEYIKRLASLSTVDTEGVWANPGELPGQLPTLYDFHFDNKRNQWVPWSKLVPEYIHAPERKFINILVHTVDTTRTTWILEQMVKIKQPVIFVGESGTSKTATTQNFLKNLSEETNIVLMVNFSSRTTSMDIQRNLEANVEKRTKDTYGPPMGKRLLVFMDDMNMPRVDEYGTQQPIALLKLLLEKGYLYDRGKELNCKSIRDLGFIAAMGKAGGGRNEVDPRFISLFSVFNVPFPSEESLHLIYSSILKGHTSTFHESIVAVSGKLTFCTLALYKNIVQDLPPTPSKFHYIFNLRDLSRVFNGLVLTNPERFQTVAQMVRVWRNECLRVFHDRLISETDKQLVQQHIGSLVVEHFKDDVEVVMRDPILFGDFQMALHEGEPRIYEDIQDYEAAKALFQEILEEYNESNTKMNLVLFDDALEHLTRVHRIIRMDRGHALLVGVGGSGKQSLSRLAAFTASCEVFEILLSRGYSENSFREDLKSLYLKLGIENKAMIFLFTDAHVAEEGFLELINNMLTSGIVPALFSEEEKESILSQIGQEALKQGMGPAKESVWQYFVNKSANNLHIVLGMSPVGDTLRTWCRNFPGMVNNTGIDWFMPWPPQALHAVAKSFLGYNPMIPAENIENVVKHVVLVHQSVDHYSQQFLQKLRRSNYVTPKNYLDFINTYSKLLDEKTQCNIAQCKRLDGGLDKLKEATIQLDELNQKLAEQKIVLAEKSAACEALLEEIAVNTAVAEEKKKLAEEKAMEIEEQNKVIAMEKAEAETTLAEVMPILEAAKLELQKLDKSDVTEIRSFAKPPKQVQTVCECILIMKGYKELNWKTAKGVMSDPNFLRSLMEIDFDSITQSQVKNIKGLLKTLNTTTEEMEAVSKAGLGMLKFVEAVMGYCDVFREIKPKREKVARLERNFYLTKRELERIQNELAAIQKELETLGAKYEAAILEKQKLQEEAEIMERRLIAADKLISGLGSENIRWLNDLDELMHRRVKLLGDCLLCAAFLSYEGAFTWEFRDEMVNRIWQNDILEREIPLSQPFRLESLLTDDVEISRWGSQGLPPDELSVQNGILTTRASRFPLCIDPQQQALNWIKRKEEKNNLRVASFNDPDFLKQLEMSIKYGTPFLFRDVDEYIDPVIDNVLEKNIKVSQGRQFIILGDKEVDYDSNFRLYLNTKLANPRYSPSVFGKAMVINYTVTLKGLEDQLLSVLVAYERRELEEQREHLIQETSENKNLLKDLEDSLLRELATSTGNMLDNVDLVHTLEETKSKATEVSEKLKLAEKTALDIDRLRDGYRPAARRGAILFFVLSEMALVNSMYQYSLIAFLEVFRLSLKKSLPDSILMKRLRNIMDTLTFSIYNHGCTGLFERHKLLFSFNMTIKIEQAEGRVPQEELDFFLKGNISLEKSKRKKPCAWLSDQGWEDIILLSEMFSDNFGQLPDDVENNQTVWQEWYDLDSLEQFPVPLGYDNNITPFQKLLILRCFRVDRVYRAVTDYVTVTMGEKYVQPPMISFEAIFEQSTPHSPIVFILSPGSDPATDLMKLAERSGFGGNRLKFLAMGQGQEKVALQLLETAVARGQWLMLQNCHLLVKWLKDLEKSLERITKPHPDFRLWLTTDPTKGFPIGILQKSLKVVTEPPNGLKLNMRATYFKISHEMLDQCPHPAFKPLVYVLAFFHAVVQERRKFGKIGWNVYYDFNESDFQVCMEILNTYLTKAFQQRDPRIPWGSLKYLIGEVMYGGRAIDSFDRRILTIYMDEYLGDFIFDTFQPFHFFRNKEVDYKIPVGDEKEKFVEAIEALPLANTPEVFGLHPNAEIGYYTQAARDMWAHLLELQPQTGESSSGISRDDYIGQVAKEIENKMPKVFDLDQVRKRLGTGLSPTSVVLLQELERFNKLVVRMTKSLAELQRALAGEVGMSNELDDVARSLFIGHIPNIWRRLAPDTLKSLGNWMVYFLRRFSQYMLWVTESEPSVMWLSGLHIPESYLTALVQATCRKNGWPLDRSTLFTQVTKFQDADEVNERAGQGCFVSGLYLEGADWDIEKGCLIKSKPKVLVVDLPILKIIPIEAHRLKLQNTFRTPVYTTSMRRNAMGVGLVFEADLFTTRHISHWVLQGVCLTLNSD', 4471, 'Q8IVF4; C9JMF5; O95495; Q6ZUC9; Q6ZUP6; Q8N761;', 'KD00833', 'Homo sapiens (Human)', 'DNAH10', '#Dynein heavy chain 10; axonemal#Axonemal beta dynein heavy chain 10#Ciliary dynein heavy chain 10', '-', 'ENSG00000197653', '-'),
(834, 'Q7SZL5', 'Microtubule-associated tumor suppressor 1 homolog', 'k', 147067, 'Regulates microtubule dynamics during mitosis by stimulating kif2c. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. {ECO:0000269|PubMed:12919681}.', 'MSVQTATTENRFQSTLDDNNGNNSESKNIARCPKYEWNANVNDQGPGVIDHSILDQQSDNEINKHYLLQSPNALELDSTLDYIGNAAGHCDTFNLKADKGCKTVNSSLLHENPGEEDETVDYINNELCNKMQDTLCPPSIPIQTSASDEIHKGLGAITDRGSAYNKIAEQSLCVQESTDYLCKMEPKWTVQAFFGDADKLCRNEANNLVDISTTDHKYDHNSSFGIFTLSLDFSDEKCMREDSLVLSGSEKPLSASILEGSALPNSSIDVFTGSVKKTDNIDGFCQGAELSLRDLDYLEVPHQKDSTETPQSKLSLTSEHSVFTSETSEVMLEVDARRVMDKTVESHLPNLRLSSNVGKEDSAPGASLEEFVSGSVPAVAPEELASNLIKDKNTIKNKESHGEAHSLESPARPDSSSSELKDLLSNLSGQNCEDTFIISSPNSGIGSKAFTSTPLPESKNMTFSVPVLESITENNELQQNLDAIKYDLEGLRHSSDSNIVTKPTNKKPAVGSVVGKAKKNEVISFPKPSFKNVKAKVLTRPSLQAKDSNPYASKTSPRSPPSLSNASSPAQSPRPLSSAVKTVQKRSVINQDMKTEAAIAKSQKQPITKQLFPTHSAHVPTHSKHALGKVPRAAALKHTQNETERASSSNSTRSSGSAAAALTCTAGSRVTENKSEKAKTSAKPSAPNVRLMGPNKIEQKGIIQPHFDKAQSLKEAKEGTVSADMDILANIVPLPTKLAIPSSRNLHKELILGIKNVASQPAKGRVQTTVQRRGSLGKNILTIRVSSPPREKPQVTVEGGLNSPKGRPISVKASAANGTGSLPRTRLPCRGTTLQRTASVSSVCSTQSELSNLSTRSTTTTSSIKTEDIPTAKCIRPNSASGALTAKSSIPRGRSQSLKVTQTVTGTKKSPSIIPTLPRSSGPALSLTKKLEARSLQNVEKNKQKTSPRGPVTQAQTPPVDPKSIELTKCKAACEQQRGVIENLKNLLSSSNQRFEALTVVVQQLINQREETLKKRKALSQELLNLRGDLVCASSTCERLEKEKNELLKAYEGILQKVKEEHHAELSDLEEKLKQFYTGECEKLQSIFIEEAEKYKNELQEKVDDLNTTHEAYRLQAETSQIETIHTLKEDYEKSLTELKDAKDKENKILEDSFKEKQAEVEKKILELKDVNESLKEKLKYEEEQRKLTKEKSVQKNPQVMYLEQELESLKAVLEIKNEKLHQQDKKLMQVEKLVETNTTLVERLNKCQQENEDLKARMVNHVALSRQLSTEQEVLQRSLEKESKANKRLSMENEELLWKLHNGDLCSPKKLSPSSPGIPFHPSRNSGSFSSPTVSPR', 1338, 'Q7SZL5; Q9PTL6;', 'KD00834', 'Xenopus laevis (African clawed frog)', 'mtus1', '#Microtubule-associated tumor suppressor 1 homolog#F-box protein 27#Inner centromere KinI stimulator#Mitochondrial tumor suppressor 1 homolog', '-', '-', '398697'),
(835, 'D3YXS5', 'Kinesin-like protein KIF28P', 'GO:0003777', 114827, 'Microtubule-dependent motor protein required for mitochondrion morhology and transport of mitochondria in neuronal cells. {ECO:0000250}.', 'MGRVPVPRSDSVRVAVRVRPFSQREKNSGSQCVISMHSGNISIRDPKNEERVKTFTFDLTYWSHDGFQKDEDGVLIPSDPASKFAGQSDVFHDIGRGILDSAWRGYNATLLAYGQTGSGKSYSMIGFGTNKGLIPRVCEELFQAIEKQKENLEPQVMFSMLEIYNEQIRDLLSRTKAPGGLRVREDQQLGFFVEGLKWVPCENYAQIEKLVEQGSKIRMTASTNMNASSSRSHMLIAIQFKQVFLDTALTKRSSINMVDLAGSERQRSSGSEGDRLREGSRVNLSLTSLGNVISALADLAMGKKVLHIPYRDSVLTKLLQSALGGNSRTTLIAALSPADICYEETLSTLRYAERAKKVRNRAVINTCPLARASRAENALLLGFRGAGAAEHPACFWAEQQLGNQGTWAQLLEQARREWEEQYEALTQEQKMVRILPHLLNVNEDPQLTGVLKFFIHNGSCDVGRAASNAICLQGLGISDKHASFVNLDGKVTVAPHSKCKVIVNGVPVTGRTKLQHLDRIILGSNSAFLYVGFPSERGAEDLSRFDYDFFQLERAAAEGVSVATLGCVSPGDDQADPSILAVFQDYVKLMPLVVEANQMSEELKKGLTMELKVKNLASSDSRGYDLQKEVMVKVTKQGTHEVWIWSKAKFINRKFLMEELYQRFLESRDSHVAQEDDPFWDPLEVVHLGSAHVWLQPLAHCMMLEEQVEFLNCDGLEEAVLHIRITPCSPEGWAHGEEDMVIDPLELLGKRIDFQTHIVRCLGVKWLKEDGSRGIQMGYGIYDLPNTLYTKPVWKSVNPRIEETVHFAALGASREFLDYLLTNALIVDLWGLQEGCAPLGVSQLDVLLTGEGHIMVDTKTFSSVKDVSQITSNQVPELYQKLLKLEQETELLRDVNRALRGENVFLKASLENAGSAPQAQKLDNPEGATRTAAREAKQVCAQQASSDAQLARALKVFYQGMGVARGQLLRLRRCRPPEDDQMLRPFVHQQSQMLKDLEDLLESSLHKLKADVAFIVKKRKEYLLPSQQ', 1028, 'D3YXS5;', 'KD00835', 'Mus musculus (Mouse)', 'Kif28p', '#Kinesin-like protein KIF28P#Kinesin-like protein 6', '-', '-', '-'),
(836, 'Q4IMM0', 'Probable kinetochore protein SPC25', 'GO:0000778===GO:0051455===GO:0031617', 30146, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MATDFRSSFSASMRQSMPPVGPSVANQLPNINFGFDDLRDRMAKFTARFDAFIEEGRKRVLDERNQFRMNVAELQEDQRMKKRDIEIVQTKTATHQQTIEKEKAETREMETAINSLASQRDNHLSTRDSLKAEIAQTQAEIETRLAAQREYAQHQQSQSRFNVPELDFWITNLCLKIEGAGHDDRLKFVYTHVDEKDWEREAWFELVTSSRDYDVKHCRPKVEREKVEKVLDKLNESRELVVLLKGMRELFVEAMKS', 257, 'Q4IMM0; I1RD49; V6QWZ0;', 'KD00836', 'Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084(Wheat head blight fungus) (Fusarium graminearum)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '-'),
(837, 'Q8BRT1', 'CLIP-associating protein 2', 'GO:0000777', 140739, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). {ECO:0000250}.', 'MRRLICKRICDYKSFDDEESVDGNRPSSAASAFKVPAPKTPGNPVSSARKPGSAGGPKVGGPSKEGGAGAVDEDDFIKAFTDVPSVQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSTVAGRVSVGGSKANPLPGSLQRSRSDIDVNAAAGAKAHHAAGQAVRSGRLGAGALNPGSYASLEDTSDKMDGTASDDGRVRAKLSTPLVAVGNAKTDSRGRSRTKMVSQSQPGSRSGSPGRVLTTTALSTVSSGAQRVLVNSASAQKRSKIPRSQGCSREASPSRLSVARSSRIPRPSVSQGCSREASRESSRDTSPVRSFQPLGPGYGISQSSRLSSSVSAMRVLNTGSDVEEAVADALLLGDIRTKKKPARRRYESYGMHSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASSNWSERKEGLLGLQNLLKNQRTLSRIELKRLCEIFTRMFADPHGKVFSMFLETLVDFIQVHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDITRESFPNDLQFNILMRFTVDQTQTPSLKVKVAILKYIETLAKQMDPRDFTNSSETRLAVSRVITWTTEPKSSDVRKAAQSVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLRNTGNGTQSSMGSPLTRPTPRSPANWSSPLTSPTNTSQNTLSPSAFDYDTENMNSEDIYSSLRGVTEAIQNFSFRSQEDMSEPVRRDPKKEDGDTICSGPGMSDPRAGGDAADGSQPALDNKASLLHSMPLHSSPRSRDYNPYNYSDSISPFNKSALKEAMFDDDADQFPDDLSLDHSDLVAELLKELSNHNERIEERKIALYELMKLTQEESFSVWDEHFKTILLLLLETLGDKEPTIRALALKVLKEILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEAASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNMLLPEIMPGLIQGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGSAGADPTADVSGQS', 1286, 'Q8BRT1; Q8CHE3; Q99JI3; Q9DB80;', 'KD00837', 'Mus musculus (Mouse)', 'Clasp2', '#CLIP-associating protein 2#Cytoplasmic linker-associated protein 2', '-', '-', '76499'),
(838, 'Q8BK67', 'Protein RCC2', 'GO:0072356===GO:0051987', 55983, 'Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1 (By similarity). {ECO:0000250}.', 'MPRKKGAAWEEPSSGNGTARAGPRRRGGPAGRKRERPERCSSSSGGGSSGDEDGPELDGAPGGGKRTARPATAGKAAGAAAIITEPEHTKERVKLEGSKCKGQLLIFGATNWDLIGRKEVPKQQAAYRNLGQNLWGPHRYGCLSGVRVRTVVSGSCAAHSLLITTEGKLWSWGRNEKGQLGHGDTKRVEAPRLIEALSHEAIVLAACGRNHTLALTDTGSVFAFGENKMGQLGLGNQTDAVPSPAQIMYNGQPITKMACGAEFSMLMDCKGNLYSFGCPEYGQLGHNSDGKFIARAQRIEYDCELVPRRVAIFIEKTKDGQILPVPNVVVRDVACGANHTLVLDSQKRVFSWGFGGYGRLGHAEQKDEMVPRLVKLFDFPGRGATQIYAGYTCSFAVSEVGGLFFWGATNTSRESTMYPKAVQDLCGWRIRSLACGKSSIIVAADESTISWGPSPTFGELGYGDHKPKSSTAAQEVKTLDGIFSEQVAMGYSHSLVIARDESEAEKEKLQRLPEYTPRTL', 520, 'Q8BK67; A2AWQ3; Q6ZPQ0;', 'KD00838', 'Mus musculus (Mouse)', 'Rcc2', '#Protein RCC2', '-', '-', '108911'),
(839, 'A5WWB6', 'Protein zwilch homolog', 'GO:0000777', 66078, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and mad1-mad2 complexes onto kinetochores (By similarity). {ECO:0000250}.', 'MGSKIVSDANAFVKFLKLCQDESKDNCTYMDDVSVLLVKKEQLLHDIIGEKNQPIFICEKAQTKYEPEATETSADTSDVEDVLFKVEQDPGPQPLSIMKARQLLSWYTMAHNPNMSRLKAPENLHPLWVRCDKSDPCATAWLGVEITYSGNKTSGVKLYTVCCKGPTGDETAFTTLDELKQEHQNRHHTSAVSTKGYAQYNLFCSLTEESLMFESQSSVIASLTWNHVEKMLECPPLSSKATLNIKVAVGDIRSPLYQTYREMEFLLALAGGLRTGEIEWLEPVETQSAVDLTRALIEELENLAHGVPGHSAKASEKQKAKPDAAFSSMVIERGDLDFTEQLWEKMRKSVTSYQDITECMKIVVKAVKLGKIKPWIHKDSNSTLSKLILQSYQQQIDSVPLTGLAPANMLLELGLDKIRKDFINYLVGKELTTLNYLSYYLDTEVDLQEQVVRVRKLHHLLEILGTCSTFLSLPHERLFLFTQSCLQYYKTSNYDEDHIFQLQIKPALISYFYEKEQPFSWAVEVSSGQGSKEVKTSLYLSDKPLVDHIHLDLDVSLNESVNGDSEKMFYYRTMVSCSLINFI', 583, 'A5WWB6; Q1JQ30; Q501W8;', 'KD00839', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'zwilch', '#Protein zwilch homolog', '-', '-', '336439'),
(840, 'Q6NVU2', 'Serine/threonine-protein phosphatase PP1-gamma catalytic subunit', 'GO:0000777', 36956, 'Protein phosphatase 1 (PP1) is essential for cell division; and participates in the regulation of glycogen metabolism; muscle contractility and protein synthesis. 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}.', 'MADVDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNASRPVTPPRGMITKQAKK', 323, 'Q6NVU2;', 'KD00840', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'ppp1cc', '#Serine/threonine-protein phosphatase PP1-gamma catalytic subunit {ECO:0000250|UniProtKB:P36873}#PP-1G {ECO:0000250|UniProtKB:P36873}#3.1.3.16', '-', '-', '407879'),
(841, 'Q10430', 'Kinetochore protein spc25', 'GO:0000778===GO:0051455===GO:0031617===c;k', 28811, 'Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Acts as a component of the essential kinetochore-associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:15728720}.', 'MSLANFPTIELDYDSLKSKISNFNSIFDRFLQEERKKLLNNKNEYLRQLSEINEAQKKAEKSLEQTEARKQNFTELLEKEHEEQAITEQEIFSFQEKLDAMLKRKQKLSEELDHYRAIISSKRELRAQEMEAKRKQDSYNNPELKFWEDYLGLKMEGVHDEVIRFIFTNIDEKDWNKQFSFQINLAERDYKVVHCHPPLPHVDDLVNKVNRTRDFYQFLKDMRKGFRELHRKDLSQLI', 238, 'Q10430;', 'KD00841', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'spc25', '#Kinetochore protein spc25', '-', '-', '2539200'),
(842, 'Q71F23', 'Centromere protein U', 'GO:0000777===k', 47522, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression. {ECO:0000269|PubMed:12941884; ECO:0000269|PubMed:16716197; ECO:0000269|PubMed:17081991}.', 'MAPRGRRRPRPHRSEGARRSKNTLERTHSMKDKAGQKCKPIDVFDFPDNSDVSSIGRLGENEKDEETYETFDPPLHSTAIYADEEEFSKHCGLSLSSTPPGKEAKRSSDTSGNEASEIESVKISAKKPGRKLRPISDDSESIEESDTRRKVKSAEKISTQRHEVIRTTASSELSEKPAESVTSKKTGPLSAQPSVEKENLAIESQSKTQKKGKISHDKRKKSRSKAIGSDTSDIVHIWCPEGMKTSDIKELNIVLPEFEKTHLEHQQRIESKVCKAAIATFYVNVKEQFIKMLKESQMLTNLKRKNAKMISDIEKKRQRMIEVQDELLRLEPQLKQLQTKYDELKERKSSLRNAAYFLSNLKQLYQDYSDVQAQEPNVKETYDSSSLPALLFKARTLLGAESHLRNINHQLEKLLDQG', 418, 'Q71F23; A2RRD9; Q09GN2; Q32Q71; Q9H5G1;', 'KD00842', 'Homo sapiens (Human)', 'CENPU', '#Centromere protein U#CENP-U#Centromere protein of 50 kDa#CENP-50#Interphase centromere complex protein 24#KSHV latent nuclear antigen-interacting protein 1#MLF1-interacting protein#Polo-box-interacting protein 1', '-', 'ENSG00000151725', '-'),
(843, 'Q8C3Y4', 'Kinetochore-associated protein 1', 'GO:0000777===GO:0005828', 250358, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores (By similarity). {ECO:0000250}.', 'MWNNIELLTSDDTGSGCLSVGSRKENVTALYQADLLGKISSEKTSLSPKIQAFSLSHGFIIVADQSVILLDSICRSLQLFLIFDTDVDVVGLCQEGKFLFVGERSGNFHLIYVTSKQTLFTKAFVEKALDESQRTYRNLIIEKDGSNEGTYYMLLLTNNGFFYITNLQLSQIEQAIENTDLDSAKKLQGQFKCSFISTENYHSCLSLVASQSGTFASKTSVIIGGTGSCAFSKWEPDSTKKEMSLKNFVGTDIIKGAKSFQLIDNLLFVLDTDNVLSLWDAYTLTPVWNWPSLPVEQFVLTTEADSPSSVTWQGITNLKLVTLTATAKEKMRSLIIYSLPSMETLYSLEVSSVSSLVQTGISTDTIYLLEGIHKNDPNLCEDSVSDLVLRYLTEVLPENRLSRLLHKHRFAEAESFAIQFGLDVELVYKVKSNDMLEKLALISSDKSEQSKWQQLVDEAKENLCKIQDDDFVVNFCLKAQWVTYETTQEMLSYAKTRLMKKEDRALPASSDAFMEVLKAHAKLTTFYGAFGPEKFSGSSWIEFLNNEDDLRDVFLQLSEGNFACAQYLWLRHRADFESKFDVKMLENLLNSISTQFPLENLCSWFKNEVIPFVRRIVPEGQNILAKWLEQASRNLELTDKANWPENGLQLAEVFFTAEKTDRFGFASSWHWISLDYQNTEEVRQLRTLVSKLRELIILHRKYNCKLALSDFEKENATTVVFRMFDRVSAPELIPSVLEKSVRVYIREQNLQEEELLLLYIEDLLKRCSSKSMTLFDTAWEAKAMAVIRCLSDTDLIFDAVLKIMYKAVVPWSAAVEQLVKQHLEMDHPKVKLLQESYKLMEMKKLLRGYGIREVNLLNKEIMRVIRYILKQDIPSSLEDALKVAQGYRLSDDEIYSLRIIDLIDREQGGDCLLLLKSLPAAEAEKTAERVIIWARLALQEEPDGSEEDKAWRISVAKTSVDILKILCDIRKDNLQKKDESEEFLKRFQMVASLQENFEVFLPFEDYSNTALVAGLREQYIKAQEAAQAEHKHRGPPGPTPARGTHLSIKSKLHRQALALQVSEQELEAELTLRALKDGKVVAALSKCRDLLKHYCNADTGRLLFVVCQKLCQMLADDVPMVAPGGLSLPSEIHDLACHAVTICSPDYLLDVLELSKYTLTAVELCRQCQMDDCGMLMKAALGTHKDPYEEWSFSDFFSEDGIVLESQVVLPVIYELISSVMPPAESKRHPLDSISLPYCSTSEGENRILPLVSSISALLRSLQECSQWELALRFVVGSFGTCLQHSMSNVMSISLSKQLLGKNTLANSRHIIMELKEKSITFIRENATTLLHKVFNCRVVDLDLALAYCTLLPQKDVFDNLWKFIDKAWQNYDKILALSLVGSQLANLYQDIETGLWFHELSIDAKWGIRLGKLGISFQPAFRQNFLTKKDLIKALVNNIDMDTSLILEYCSTFQLDSDAALRLFIETLLRNTSSQSQGDAAPESTKHQHSKLLAKATELVPLLKNTKDLVISLSEILYKLDPYDYEMIDVVLKVLEQANEKITSVNINQALNLLRHLKSYRRISPPVDHEYQYALEHMITLPPAAHTRLPFHLILFGTAQNFWKILSSELSEESLPTLLLIAKLMKFSLDTLYVSTAKHLFEKNLKPKLLKSAQARSSTLMSKEVDKLMQTLESYLLSIVNPEWAVAIAISLTQEVPEGPFKMSSLKFCLYLAERWLQNIPPQDETCEKAKALQKKLCLQVRLSGTEAVLIAHKLNDQEYLRVIGKPAHLIVSLYEHPSISERLCTTSGKDYPDIHTAAKEIAEVNEVNLEKIWDMLLEKWLCPSTVPSEKASEFFELEEDEVLHRVVYLLQARPVDYCSRMLFVFATSATSTLGMRQLTFAHKARALQCLLYLADKETIESLFKKPIKEMKSYLKCITFLASFETLNIPITYELFCNSPKEGMIKGLWKNHSHEPMAVRLVAELCLEYKIYDLQLWNGLLQKLLGFNMIPYLRKVLSCISSIHSLWQVPYFSKAWQRVIQIPLLSASCPLRPSQLADCCDSLVAILECPVSDDLDMMGVAKQYVQLDLPAFALTCLTLMPHSEKRHQQIKNFLNSCDARIILQQIEEHMNTGQLAGFSHQIGSLVLNHVVNKKEFGILAKTKYFQLLKCHVINTGNVTELVNYLANDFSVDEASALINEYSKHCGKPVPADAAPCEILQTFLGGS', 2207, 'Q8C3Y4; Q6A0B3;', 'KD00843', 'Mus musculus (Mouse)', 'Kntc1', '#Kinetochore-associated protein 1', '-', '-', '208628'),
(844, 'Q60862', 'Origin recognition complex subunit 2', 'GO:0000939', 65893, '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}.', 'MSTLQLKETKVPSVQFVGDDDVLSHILDREGGTKLKKEKAQLLVNPQKVIKKADCELEKSDLEVLEDQNYVKVLGRNIQESLGNGSAKDGRNKVYSFQQRKHPEEMTKLALELAKTSGKKDPLDSNDPEITKNIAQKSKGHSTSEKAPLVNNNKTEFLSTQPHNLRKRIIASRSHYDSESEYSASSSEDDEEATKDEEEDTNVARLSQKSQGQNRLLPAPVSKETLPKKKKRDKASDLVEEYFEAHSSSKVLTSDRTLQRLRRARVDQKTLHNLLRKFVPSFSAEIERLNQQHEKLFHKWMLQLHLGFNIVLYGLGSKRDLLEKFRTTMLQDSIHVVINGYFPGVSVKSILNSITEDVLSHVGTFQSVLDQRDWIINRFKEDSSLELFLLIHNLDSQMLRGDNSQQILGQLSSLHNVYLIASIDHLNAPLMWDHAKQSLYNWLWYETTTYSPYTEETSYENSLLVKQSGSLPLSSLIHVLRSLTPNARGIFRLLMKFQLDNQDSPSYIGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGTDGVEYLLIPVDSGILADFLEKEEEEA', 576, 'Q60862;', 'KD00844', 'Mus musculus (Mouse)', 'Orc2', '#Origin recognition complex subunit 2', '-', '-', '18393'),
(845, 'F1MA98', 'Nucleoprotein TPR', 'GO:0000776===GO:0005868', 267306, 'Component of the nuclear pore complex (NPC); a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs; plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase; and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153; regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Plays also a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally; acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). Plays a role in the regulation of nuclear protein export. {ECO:0000250; ECO:0000269|PubMed:11839768}.', 'MAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVNETRECQNLRLELEKLNNQVKVLTEKNKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVTVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCTLENKKEEVLRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQDHLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDNQRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETREREEQETTSSKIAELQNKLENSLTELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLVSTPKRSSTSQTVSTPAPEPIIESTETIEAKAALKQLQEIFENYKKEKMDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINLHLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSASNVEQYRAMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLTELKKTLSSVQSEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKAESQLLECKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKEVVQSPLNISLNEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLINQQKDPDTEEYRKLLSEKEIHTKRIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLKEDLSKVRTEKESIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFEELKAQQKAMETSTQSSGDHQEQHISVQEMQELKDNLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTAQLQSELSRLRQELQDKTTKEEQLRQQMNEKDEKTWKAITVARSKIAHLSGVKDQLTKENEELKQRNGALDQQKDELDVRMTALKSQYEGRISRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSISQPLLTVQQQTQATAFVQPTQQSHPQIEPANQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRAREEEEDSTIEAGDQVSDDTVEMPLPKKLKTVTPVGTEEEVMAEESTDGEAETQTYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTSSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDEDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGAESNQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETPAGDDGDEVFVETESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGISHAMGGRGGINRGNIN', 2360, 'F1MA98; Q3T1J7;', 'KD00845', 'Rattus norvegicus (Rat)', 'Tpr', '#Nucleoprotein TPR#Megator#NPC-associated intranuclear protein#Translocated promoter region protein', '-', '-', '-');
