INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(846, 'Q923J6', 'Dynein heavy chain 12; axonemal', 'GO:0003777', 357248, '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}.', 'MSDPNKTAITAEKEALNLKLPPIVHPPKNIGVDTPKQSELLNYRRSKEQQKKINQLVISAAKKSLDKTLDKRIPPLPEPDFPPTMTSEIKKKGLNYIFMKQCVESSPIVPIQPQWLDHMLMLIPEHLKEGKKREELLGSLINEVSMDFEKSMKRYLVQSVLVKPPVKWLEDEWGPLPESPEGLDYSNPWHSNFVQARSQILANLHIVHPTMKLLLELGYTTFSDIILLDLTGIRDRGPIDCEALRNDLSIQARKAEERIMNTWYPKVINLFTKKEALEGIKPEKVDSFYNCVSILMSNQLKDLLWRTVEEFVRLFDSRYILRLPIFKMELTFDDDKMEFYPTFQDLEDVVLGLIERISETLQTVQTVPSWLSGTTAPVNLDTELPEHVMYWALSTLRIAVHQNLEGVRAHYKTYVTNYNWLLDGTATKMIERFQSENHTFDEYTEFIERFFSLASEIMLLPQWAHYPMVRLDCEDLKTGLTNKAKAFANILLNDIASKHRKENESICSEFETIKEHALRVPETTEEMMELIAFIEKARTTGIQNLAQRIQESKRQMGYFLDTFLLSQEDLNLNASVLLWPSKINPVFDENDELIENSKRTKENELIAKREKLILEIEKESRRMEEFTEFAELDRMQQYVADVRHLQKRIQDSEEAVQFINKEEELFKWELTKYPELEKLKVTIEPYQKFFNFVLKWQRTEKRWMDGGFLDLNGESMEADIDEFSREVFKTLKFFQTKQKKELQEKRKAARKRSLMEEKPEEEPKESPTITMMRARHWKQMSEIVGYDLTPDSGTTLRKVLKLNLTPYLESFEVISAGASKEFSLERAMNAMIATWDDISFHISLYRDTGVYILSSVDEIQAILDDQIIKTQTMRGSPFIKPFENEIKAWEDRLIRIQETIDEWLKVQAQWLYLEPIFCSEDIMQQMPEEGRQFQTVDRHWKDIMKFCAKDPKVLAATSLTGLLEKLQNCNDLLDKIMKGLNAYLEKKRLFFPRFFFLSNDEMLEILSETKDPLRVQPHLKKCFEGIAKLEFLTNLDIKAMYSSEGERVELISVISTSAARGAVEKWLIQVEDLMLRSIHDVIAASRLAYPESARKDWVREWPGQVVLCVSQMFWTSETQEVISGGNEGLKKYYKELQYQLNDIVELVRGKLSKQTRITLGALVTIDVHARDVVMDMIDMGVSHDTDFQWLAQLRYYWEYENARVRIVNCNVKYAYEYLGNSPRLVITPLTDRCYRTLIGAFYLNLGGAPEGPAGTGKTETTKDLAKALAVQCVVFNCSDGLDYLAMGKFFKGLASSGAWACFDEFNRIELEVLSVVAQQILCIQRAIQQKLEVFVFEGTELRLNPNCFVAITMNPGYAGRSELPDNLKVLFRTVAMMVPNYALIAEISLYSYGFLNAKPLSVKIVMTYRLCSEQLSSQFHYDYGMRAVKAVLVAAGNLKLKYPNENEDILLLRSIKDVNEPKFLSHDIPLFNGITSDLFPGIKLPEADYQEFLECAYEACETQNLQPVKFFLEKIIQTYEMMIVRHGFMLVGEPFAAKTEVLHILADTLTLMNERNYGDEEKVMYRTVNPKSITMGQLFGQFDPVSHEWTDGIVANTFREFALAESPDRKWVVFDGPIDTLWIESMNTVLDDNKKLCLMSGEIIQMSPQMSLIFETMDLSQASPATVSRCGMIYLEPSQLGWEPIVASWLNSLKEPLNELEHQNLLKELFNWLVQPSLEFRRKKCKVTAHRVWLFPTVYSSWVCLILFVLEVSAVSPKCSLKSNCYNLFHQQATFVFSLIWSVGASCDTDGRLAFDNFLRSLVTGKNDKAPMPVFINKWECPFDEKGLVYDYMYELRNRGRWIHWNDLIKSSDIEDRRTKIQDIIVPTMDTIRYTFLMDLCISHAKPLLFVGPTGTGKSVYVKDKLMNHLEKGKYFPFYVNFSARTSANQVQNIIMARLDKRRKGVFGPPMGKKCVVFIDDMNMPSLEKYGAQPPIELLRQFFDCGHWYDLKDTTKITLVDIELIAAMGPPGGGRNAVTPRFIRHFNICTINSFSDETMVRIFSSIMMFYLRTHDFSPEYFVLGHQIVSATMEIYKQSMGNLLPTPAKSHYTFNLRDFSRVIRGCLLIDKEAIESKHTMIRLFVHEVLRVFYDRLINDEDRNWLFLLIKNVIKDHFKESLENVFSHLRRGNSSINEEDLRNLMFGDYMNPDLEGDDRVYIEILNIHQFNEVVDQCLDEYNQTHKRRMNLVVFRYVLEHLSRICRILKQSGGNALLIGLGGSGRQSLTSLATSMAKMQIFQPEISKSYGMNEWREDIKPNLMSVFYATSIRDNLSKILEKRLRYLNDHFTYNLYCNICRSLFEKDKLLFSFLLCANLLLAKKEIEYQELMFLLTGGVSLKSAEKNPDPNWLQDKSWEEICRASELPVFHGLREHFCNHIREWEDIYNSKEPHNMKLPESMDKTLNELQKIIILRCLRPDKITPAITNYVTDKLGKKFVEPPPFDLTKSYLDSNCTIPLIFVLSPGADPMASLLKFANDKSMSGNKFQAISLGQGQGPVATKMITAAIEEGTWVCLQNCHLAVSWMPTLEKICEDFSPEICNPTFRLWLTSYPSPKFPVTILQNGVKMTNEPPTGLRLNLLQSYLSDPISDPEFFNGCPGKELAWEKLLFGVCFFHALVQERKKFGPLGWNIPYGFNESDLRISIRQLQLFINEYDTIPFEAISYLTGECNYGGRVTDDWDRRLLLTMLADFYNSLIIENPHYKFSPSGNYFAPPKGTYDEYIEFIKKLPFTQEPEIFGLHENVDISKDLQQTKLLFESLLLTQGGVKQTGSSGSTDQILLEITEDILTQLPNDFDIEAALRSYPVRYEESMNTVLVQEMERFNNLIITIRNTLRDLKKAIKGVVVMDSALEALSGSLLIGKVPEMWAQRSYPSLKPLGSYITDFLTRLKFLEDWFTMGKPNVFWISGFFFTQAFLTGAMQNYARKYTIPIDLLGYEFEVIPSDNATNPPEDGVYIHGLYLDGARWNRTSGLLAEQHPKLLFDLMPIIWIKPNVKTEIVKTDAYVCPLYKTSERKGTLSTTGHSTNFVIAMLLRTELPAQHWIKRGVALLCQLD', 3092, 'Q923J6;', 'KD00846', 'Rattus norvegicus (Rat)', 'Dnah12', '#Dynein heavy chain 12; axonemal#Bm259', '-', '-', '-'),
(847, 'Q6NW76', 'Aurora kinase B', 'GO:0034501===GO:0032133===GO:0000780', 36947, 'Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint; a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Phosphorylates ''Ser-10'' of histone H3 during mitosis (By similarity). Plays an essential role in early embryonic development. {ECO:0000250; ECO:0000269|PubMed:12006978}.', 'MQNKENREPRVQQTPSAGVGPLRVEMNPDTHAVSGPGRVPVKSNSKVLSIDDFDIGRPLGKGKFGNVYLARERKLKVVIALKVLFKSQMVKEGVEHQLRREIEIQSHLRHPNILRFYNYFHDDTRVFLILEYAPRGEMYKELQRYGRFDDQRTATYMEEVSDALQYCHEKKVIHRDIKPENLLLGYRGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGHSHDEKVDLWSIGVLCYECLVGNPPFETASHAETYKRITKVDLQFPKLVSEGARDLISKLLRHSPSMRLPLRSVMEHPWVKANSRRVLPPVCSSEPH', 320, 'Q6NW76; Q8JGS8;', 'KD00847', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'aurkb', '#Aurora kinase B#2.7.11.1#Serine/threonine kinase A#Serine/threonine-protein kinase 12#Serine/threonine-protein kinase aurora-B', '-', '-', '791894'),
(848, 'Q10426', 'Chromatin modification-related protein rik1', 'k', 118124, 'Component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin; telomeric regions and at the silent mating-type loci. Rik1 has also a function in meiotic telomere clustering. {ECO:0000269|PubMed:10766735; ECO:0000269|PubMed:15197176; ECO:0000269|PubMed:15372076; ECO:0000269|PubMed:16024659; ECO:0000269|PubMed:7851795; ECO:0000269|PubMed:8138176}.', 'MALCVHSFWATAVDTATSCHFISSENCLVLLQALKINIYLCSEVHGLQFFTSIPLFSTVKHIRPYRPPGLDRDYLFVVLNDDTYFSIYWDEDYQKVIVDHPPVRYRVTFPWNRNAKSYCLVDLRMRAIFLSIDEISMICIRILSAEERLKTGRSIDSGFPFSFPVHLIYDMCILNDSSTPTLVVLHSDGLDCYVTAFLLDLSSKSLGKGIRLFERVKPSMIMPFGKRGLLVFESLFIHCMYRGNFVTINGPCTTYMHWTPLKGQKMHYIVCDTNGYLFGVYSSILGKNKWSLVMERLPIPPFDFITSLNSIHEGLLFIGSKNSESKLINLSTLKDVDSIPNLGPIHDLLVLKNDIEKSFLVCAGTPRNASLIYFQHALKLDILGQTKISGILRAMVLPSYPEHKLFLGFPSETVAFNIKEDFQLELDPSLSTKERTIALSGTNGEFVQVTSTFLCIYDSAKRSRLVYIEKITNAACYQEYSAIVINGTALAIFKKDTEVARKVFESEISCLDFSAQFQIGVGFWSKQVMILTFSDNSSISCAFQTNVPSLPRNIILEGVGVDRNLLLVSSGSGEFKSYVLFKNNLVFSETKHFGTTPVSFRRFTMNIGTYIICNNDCPHMVYGFNGALCYMPLSMPQSYDVCQFRDNSGKDFLISVSLGGLKFLQLNPLPELTPRKVLLEHVPLQAIIFQNKLLLRTLENRYEDYESYKENYHLELVDSYDDNSFRVFSFTENERCEKVLKINESSLLVGTSIIEQDKLVPVNGRLILLEFEKELQSLKVVSSMVLSAAVIDLGVYNDRYIVAFGQQVAIVKLTEERLMIDSRISLGSIVLQLIVEGNEIAIADSIGRFTIMYFDGQKFIVVARYLFGENIVKAALYEGTVYIIATNSGLLKLLRYNKDAKNFNDRFICESVYHLHDKVSKFQNFPITNTNSFLEPKMLFATEIGAIGSIVSLKDKELELEELTRKIRKLKFSYLSSMDYESIEADLISPVPFIDGDLVIDVKRWASSELFRLCRSVEHRESLNSYQKVQALLEEIQSLC', 1040, 'Q10426; Q9USN9; Q9UUL7;', 'KD00848', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rik1', '#Chromatin modification-related protein rik1#Silencing protein rik1', '-', '-', '2539050'),
(849, 'Q2UF95', 'Probable kinetochore protein spc24', 'GO:0000778===GO:0051455===GO:0031617', 22876, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MLLDENPGTLIHHTIGNFNIQPDKQAVTRINDSLSTLQQSRELRMREAESSLRKLSRHLHSLNAQHEEAVAAHDSSKHAADMVELDTKKFRIAKAATELEIESERLESELEMLKERLADLEAQGLEGDEATRRERELDDATILRLKIYRSLGVDIEADDAGNFNKAVIRNSRKGDVHVVNIDPKFSRFFYSNYFWSTMQG', 200, 'Q2UF95;', 'KD00849', 'Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)', 'spc24', '#Probable kinetochore protein spc24', '-', '-', '5993800'),
(850, 'Q59QH6', 'DASH complex subunit SPC19', 'GO:0008608===GO:0042729', 20424, '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}.', 'MAQQDLPQNQRFNNLDNCTDSLRQSIKILQQSNKILDETLQDSTRLTKILSTNKVFDLIPELDLNDAKSNFTKNITPQLNQQLNKLEDELIQLQTKKTTLTNKLKLINVRLKNYEKKGNKEEGGKNFNSNGLSDIDIDNLLTNRHKNGYDVNKLHQLRFLRDKKTRLQYSLNRLN', 175, 'Q59QH6;', 'KD00850', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'SPC19', '#DASH complex subunit SPC19#Outer kinetochore protein SPC19', '-', '-', '3646423'),
(851, 'Q10428', 'Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 1 isoform', 'c;k', 63346, '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. Has a role in cell shape control and septum formation. {ECO:0000269|PubMed:10757751; ECO:0000269|PubMed:11380623}.', 'MKGIKSKMLSRGKSQDTQKSSKKKESKKSNSHDSSKAPKESPSTDPNGSVIGAQNDFLTVPKHSGKKVPIDTTPTPRDEILLENVRTVRKQRSSLYHISENRNLVRLPSFTDVPVNKWHSLALEKLEQCCVVFDFNDPSTDLYGKEVKREALQDLIDLISVRKEAIDESLYPSIVHMFAVNVFRPLPPPSNPPGEIMDLEEDEPALEVAWPHLHLVYDFFLRFFESPSLNTSVAKVYINQKFIRKLLVLFDSEDPRERDFLKTTLHRIYGKFLSLRAFIRRSINNLFLQFVYENEQFNGIAELLEILGSIINGFALPLKEEHKIFLSRVLIPLHKAKSLPLYYPQIAYGIVQFVEKDSSVTEEVVLGLLRYWPKVNSSKEVLFLNEIEDIIEVMEPSEFLKIQVPLFHKLATSISSQNFQVAERALYFFNNDYFVHLVEENVDIILPIIYPALFEISKSHWNRVIHSMVCNVLKLFMDINPSLFDEVDAEYSESRRKKEDEEIIREERWTILENIAKENAMKLKSQNPTTVHSTTERLKKLSLDYTNG', 548, 'Q10428;', 'KD00851', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'par1', '#Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 1 isoform#PP2A; B subunit; B'' delta 1 isoform', '-', '-', '2539379'),
(852, 'Q19020', 'Dynein heavy chain; cytoplasmic', 'GO:0003777', 521579, 'Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.', 'MDSGNESSIIQPPNLKTAAEGDVKEYIVQVVTSHFGLSPRDQTTLDVELTAATTFITDFINEADKNVIVVDRVVAREQGDQPAGAESGGEESAPATFQVHDGLFMTDRGQAMMFVKQSNVIEAEKKIATQVSAFPLNGGSAWEQLHFLMSRLLNPYCKSFIGQSGRGERDGDKLAPTVQKCFTEAEAALLHLQQNIDIPEINLVVNQHILDAIEQAGKENRRAKIEDLGDLVEDANFLNALQSGCNRWVKEIRKVTQLERDPSSGTSLQEMTFWLNLERALLKISQKRDGEEVTLTLEALKCGKRFHATVGFDSDNGLKQKLAVVQDYNTLMKEFPLSELVSATDVPKLMHAVVGIFLHLRKLRSTKYPLQRALRLVEAISRDLNSQLLKVLSSYNLMRTPIAEFNEIMSQCQALFSKWDDEYDKFIALLRDINKKKRDDPSKLSWKVTAVHKRLETRLMQILQFRKQHEQFRTVIERVLRPVGNGSREREQLMIDSSEGEKSPDEQVDIAYEFLKNVDFLDVDSPAWENAFKRYEDQIGVVETAITTRLKSQLESSRNSNEMFSIFSRYNALFIRPRIRGAIYEYQTRLINRVKEDINELQARFTKARGEQGVKIMQTVGLPPFSAKIMWIRNYERQLQRYMKRVEDVLGKQWENHVDGRQLKADGDNFKVKLNTQPMFDEWVESVQSQNWTLPNKILTVDRVQVDGRMQLQLKINYHSDSSVLYKEVSHLKSMGFRVPLKIVNWAHQANQMRPSATSLIEAARTFASVNAALASVQGVDSLLASYKKDIQNQLIEGATLGWDSYKVDQYQLKLAETVNTYQERCEELLNVVRIVNADLNVLKSCRYDKETIENLLTSIQKGVDQLSLGNYSNLAQWVNTLDRQIETILARRVEDAIRVWTLVFSQSEEVEELRERQVVLPTVKNVVVDLCMTAQTLYISPSTRETREKILEQLYEWHSVCTAQMRISGKRFQMVMNEEIEPETYHNILNVMPEGQACLEKAYDCVNGIMSDLEEYLSEWLSYQSLWVLQAEQLFEMLGTSLSKWMKTLMEIRKGRLVFDTQDTRKVIFPVSVEYGKAQQKILFKYDYWHKEMLVKFGAVVGDEMQKFFNSVSKWRNVLETQSVDGGSTSDTIGLISFVQSLKKQTKSGQDAVDLYRSSQRLLNQQRYQFPAQWLYSENVEGEWSAFTEILSLRDASIQTQMMNLQTKFAQEDELVEKRTVETLTEWNKSKPVEGAQRPQEALNVITAFEAKLNKLTEERNKMRKARVALDLSDSAHAPSEGDKLTVATEELAAMKDVWKALQPVYTGIDEAKEKTWLSVQPRKIRQSLDELMNQLKQLPVKCRTYKSYEHVKQMLHTYGKMNMLVAELKSEALKERHWHQMMKEMRVNWNLSDLTLGQVWDADILRHEHTIKKILLVAQGEMALEEFLREMREYWQNYEVELVNYQNKTRLIKGWDDLFNKLKEHQNSLSAMKLSPYYKQFEESAQSWDEKLNKINAMFDVWIDVQRRWVYLEGLFSGSAEISTLLPFESSRFATITTDVLALMKKVAASPRILDVVNMQGAQRLLERLADMLAKIQKALGEYLERERSSFPRFYFVGDEDLLEIMGNSKDITRIQKHLKKMFAGITAIDINEEDRSITAFHSREGEKVDLVKIVSTKDVRINDWLQALEAEMKHTLARQLAASLTHFSKMNIQTMTTDDYVEWLDKFPAQVITLTAEIWWCDEMEKTLADGKGAENVEQAVVKTLELLADSVLKEQPPIRRKKMEALITELVHKRDTCRKLVSMKIRAANDFGWLQCMRFYFDPKQVDPVRCCVVKMANSQFFYGFEYLGIQERLVRTPLTDRCYLTMTQALHSRLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRILVGLCQVGAWGCFDEFNRLEERMLSAVSQQIQTIQEAVRAGGDMSVDLVGKRLNVNSNIGIFITMNPGYSGRSNLPDNLKQLFRSLAMTQPDRQLIAQVMLFSQGFRTAETLANKIVPLFILCKEQLSDQCHYDFGLRALKYVLVSAGNIKRDKLDKMGSAALEDVAEQQMLIQSVCETLVPKLVNEDIALLFSLLSDVFPGIHYTANQMRELRQQLSTVCDEHLLIYSDVQGEMGSMWLDKVLQLYQITNLNHGLMLVGSSGSGKTMAWKVLLKALERWENVEGVAHVIDAKAMSKDSLYGVMDPNTREWTDGLFTSVIRKIIDNVRGEADRRQWIIFDGDVDPEWVENLNSVLDDNKLLTLPNGERLSIPPNVRIIFEVADLKYATLATVSRCGMVWFSEEVVTSEMLFERYLSIIRRVPLDSDSAISFSSSSAPVNLIGEDAKPTRSIEIQRTAALALQTHFSPDGIVPGSLKYAVSELEHIMPPTPQRLLSSFFSMMSYSIRKIVSHDEGLIDDSVEIDQIQSFVLRSMLTNLVWAFSGDGKWKSREMMSDFIRQATTISLPPNQQACLIDYEVQLSGDWQPWLSKVPTMEIESHRVAAADLVVPTIDTVRHEMLLAAWLAEHKPLVLCGPPGSGKTMTLLAALRSQQEMEVVNVNFSSSTTPELLLRTFDHYCEYRRTPNGVVLAPVQLSQWLVIFCDEINLPAPDKYGTQRVISFLRQLVELNGFYRTSDHSWVSLERIQFVGACNPPTDPGRHPMTSRFLRHVPIVYVDYPGQTSLQQIYGTFNRAMLKMTPAVRGLADQLTNAMVDVYLASQEHFTQDDQPHYVYSPRELTRWVRGISEAITPLESLSAEQLVRLWAHEAIRLFQDRLVTEEEREWTDKLVDTTAERYFGNACRLDEALKRPLLYSCWLSRNYVPVTREELQDYVSARLKGFYEEELDVKLVLFDQMLDHVLRIDRIYRQSQGHLLLIGTAGAGKTTLSRFVAWLNGLSVFQLKVHSKYTAADFDEDMRTVLRRAGCRNEKLCFIMDESNMLDTGFLERLNTLLANGEVPGLFEGDEHTTLMTQIKEGAQRQGLILDSHDELYKWFTQQVMRNLHVVFTMNPSGSGLRERASTSPALFNRCVLNWFGDWSENALYQVGSELTRTMDLDRTDYEGSVRLTPSCELVPSQPTYRDAVVNTLCLVHKTVQKFNEMETKKGHRVMACTPRHFLDFIKQFMSLFHEKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELAEQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKSQLVEVKSMSSPPVTVKLTLEAICILLGENVGTDWKAIRQVMMKDDFMTRILQFDTELLTPEILKQMEKYIQNPDWEFDKVNRASVACGPMVKWARAQLLYSTMLHKVEPLRNELKRLEQEAAKKTQEGKVVDVRITELEESIGKYKEEYAQLIGQAENIKQDLLSVQEKVNRSTELLSSLRSERDRWSSGSAGFSQQMDSLVGDALLSSAFLAYAGYYDQMLRDEIFHKWFNHVVNAGLHFRHDLARIEYLSTVDDRLQWQLNSLPVDDLCTENAIMLHRFNRYPLIIDPSGQAVEYIMKQFAGKNIQKTSFLDESFRKNLESALRFGNSLLVQDVEAYDPILNPVLNREVKRAGGRVLITIGDQDIDLSPSFQIFMITRDSTVEFSPDICSRVTFVNFTVTSSSLASQCLNQVLRSERPDVDKKRNDLLKLQGEFAVRLRHLEKALLAALNESKGKILDDNSVIETLEKLKNEAAEVAQKSAETDKVMAEVDAVSAQYQRLSTACSHIYHTLQQLNEIHFLYHYSLDFLVEIFTHVLKTPELSSTTDYAKRLRIITTSLFQTVFRRVSRGMLHTDKVLLALLLMRIHIRSNPSAPAYEQHFDLLLGRSDFVAKNDEADSTIPGGLDFLTVENKKSIAKARKVVGFENVFAHLQHNSAAVTSWLTNDNPESNVPVVWDDADGKLSPLCIAMNSLIVVHALRPDRLMASAHRVVSTAFDDHFMQQDKVVDILSIVDNEVSPSEPVLLCSATGYDASGKIEDLAVETNRQLTSIAIGSAEGFNQADSALGTATKSGRWVLLKNVHLAPSWLAQLEKRLHSMKPHAQFRLFLTAEIHPKLPSSILRASRVVVFEPATGLKANLLRSLSSIPPQRLTKAPTERSRLYLLVCWLHALVQERLRYTPLGWSTAYEFSDADLRVACDTLDAAVDAVAQGRPNVEPERLPWTTLRTLLSQCIYGGKIDNQFDQVLLDCVLENLFTAKSFEQDHVLIPKYDGDDSLFTPNMSKKDQMIGWVEELKNEQLPAWLGLPNNAEKVLLTKRGESMLRNMLKVTDEELAFNEDGKEEVKPQWMAQLGELAKQWLQLLPKEIVKMRRTVENIKDPLFRFFEREVNLGSQLLKDIRRDLNEISAVCRAEKKQNNETRALAASLQKGEVPTGWKRYTVPREVTVMDWMTDLNERLKQLIRIGGADNLKRETFWLGGTFSPEAYITATRQQVAQANTWSLEQLNLHIHIGRTDSTDVFRISGIDIRGAKSVGGNKLELCELVKSECDIVEFSWKQDVADGTRLPLYLYGDRRQLISPLAFHLSSATVFYQRGVALVANSTL', 4568, 'Q19020;', 'KD00852', 'Caenorhabditis elegans', 'dhc-1', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC', '-', '-', '172041'),
(853, 'Q9N3R7', 'MIS-12; isoform a', 'k', 20198, '', 'MESELSGISNENQISFFGFSAGSFSDSIFNIYVDAWEEVCSNEFKNSLKKLTDKDRLCLLSFPFSDKTNEKAFKMMKRFCVTNIFRIPASVTLPECKKMLIASAKEHKSLKQVEKEFDEKLEKIRQLRIKLAKRHDELEAVNNAIEVLHVMEKSQEQLISQKRIVPDSPTRMSPV', 175, 'Q9N3R7;', 'KD00853', 'Caenorhabditis elegans', 'mis-12', '#MIS-12; isoform a {ECO:0000313|EMBL:CCD72569.1}', '-', '-', '171927'),
(854, 'O35066', 'Kinesin-like protein KIF3C', 'GO:0003777', 89973, 'Microtubule-based anterograde translocator for membranous organelles. {ECO:0000250}.', 'MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQARAVGSTHMNEVSSRSHAIFVITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNAAGGPATQPTAGGGSGSGSASGSASSGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKKGMLGKRPRRKSSRRKKAVSAPAGYPEGSVIEAWVAEEEDDNNNNHHPPQPILEAALEKNMENYLQDQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEDLRREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMLLRDEETMELRGTYSSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHEEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWRFQPLVPAGVNNSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAIFEMEFSHDQEQDPRVLHMERLMRLDSFLERPSTTKVRKSRSWCQSPQRMPPPSTAHASMTSVPLHPATVVDHD', 796, 'O35066; O35229; Q3UH55;', 'KD00854', 'Mus musculus (Mouse)', 'Kif3c', '#Kinesin-like protein KIF3C', '-', '-', '16570'),
(855, 'P35203', 'Centromere DNA-binding protein complex CBF3 subunit C', 'GO:0051382===GO:0000778===GO:0031518===k', 56336, 'Acts as central component of the centromere DNA-binding protein complex CBF3; which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII; found in centromers and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly.', 'MPSFNPVRFLELPIDIRKEVYFHLDGNFCGAHPYPIDILYKSNDVELPGKPSYKRSKRSKKLLRYMYPVFATYLNIFEYSPQLIEKWLEYAFWLRYDCLVLDCFKVNHLYDGTLIDALEWTYLDNELRLAYFNKASMLEVWYTFKEYKKWVIDSVAFDELDLLNVSNIQFNIDNLTPQLVDKCLSILEQKDLFATIGEVQFGQDEEVGEEKDVDVSGANSDENSSPSSTIKNKKRSASKRSHSDNGNVGATHNQLTSISVIRTIRSMESMKSLRKITVRGEKLYELLINFHGFRDNPGKTISYIVKRRINEIRLSRMNQISRTGLADFTRWDNLQKLVLSRVAYIDLNSIVFPKNFKSLTMKRVSKIKWWNIEENILKELKVDKRTFKSLYIKEDDSKFTKFFNLRHTRIKELDKSEINQITYLRCQAIVWLSFRTLNHIKLQNVSEVFNNIIVPRALFDSKRVEIYRCEKISQVLVI', 478, 'P35203; D6VZR7;', 'KD00855', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CTF13', '#Centromere DNA-binding protein complex CBF3 subunit C#Chromosome transmission fidelity protein 13#Kinetochore protein CTF13', '-', '-', '855119'),
(856, 'P35201', 'Protein MIF2', 'GO:0000776===GO:0051382===GO:0000780===k', 62473, 'Required for mitotic spindle integrity during anaphase spindle elongation. Probably binds at tracts in DNA. Interacts with CEP1.', 'MDYMKLGLKSRKTGIDVKQDIPKDEYSMENIDDFFKDDETSLISMRRKSRRKSSLFLPSTLNGDTKNVLPPFLQSYKSQDDEVVQSPSGKGDGSRRSSLLSHQSNFLSPANDFEPIEEEPEQEENDIRGNDFATPITQKLSKPTYKRKYSTRYSLDTSESPSVRLTPDRITNKNVYSDVPDLVADEDDDDRVNTSLNTSDNALLEDELEDDGFIPESEEDGDYIESDSSLDSGSDSASDSDGDNTYQEVEEEAEVNTNDNEDDYIRRQASDVVRTDSIIDRNGLRKSTRVKVAPLQYWRNEKIVYKRKSNKPVLDIDKIVTYDESEDEEEILAAQRRKKQKKKPTPTRPYNYVPTGRPRGRPKKDPNAKENLIPEDPNEDIIERIESGGIENGEWLKHGILEANVKISDTKEETKDEIIAFAPNLSQTEQVKDTKDENFALEIMFDKHKEYFASGILKLPAISGQKKLSNSFRTYITFHVIQGIVEVTVCKNKFLSVKGSTFQIPAFNEYAIANRGNDEAKMFFVQVTVSEDANDDNDKELDSTFDTFG', 549, 'P35201; D6VXJ9;', 'KD00856', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MIF2', '#Protein MIF2', '-', '-', '853773'),
(857, 'Q5BIX7', 'Protein Spindly-A', 'GO:0043515===GO:0034501===GO:0000940', 70573, 'Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. {ECO:0000255|HAMAP-Rule:MF_03041}.', 'MEESETVLKLRRQLKEAEEERVKAAHYGLELLESQSDLQNQLEEQRNEMTGTIENLEQEKYSLQREVELKNRMLESVTSECENIRQQQKLILEQLQEQLERNHHRELGEIKDKLEKLKAELDEARLSEKQLKHKLEYQTEVLANKSEELRMMSERVHETMSSEMLTLQLEKTELESAKANLEQEVNELQYREQQLLLTNGTQSRKLEHLQTEKEEREKESVGYFSALEKAREANQDLQAQLDIALQQAQDPNSKGNSLFSEVEDRRAEMERQLISMKVQFQSLQKQHAFSRQQMHRMKVQIATLLQMKGSQSDPEQLERLQAMVAQKNSEIEALVMKVRQLEKSQQVSENGPAVGSSDNLGQGDETYYVDLLKMKLLNSSKENEKIKDELSLQRMKALAESQRVLELERKLFANDRHLKLSQGENMKLRVSLDEIKMKYEPDEMGKIHTQKRRKEQLPLDFPMDNTSAAVTSGTEAQGLYDATAGETCTAESTDGRIHSKEDLSLSTKEQDPSSVAVKPKELPNGPPPKERKRVRIMEDENNAQDLNKRNTHNCSVTSASPRSTSEDATSESKRFDEEQEKRKQERKSRLRAPPVLHVPSKPNATTQCPQQ', 611, 'Q5BIX7;', 'KD00857', 'Xenopus laevis (African clawed frog)', 'spdl1-a', '#Protein Spindly-A {ECO:0000255|HAMAP-Rule:MF_03041}#Coiled-coil domain-containing protein 99-A {ECO:0000255|HAMAP-Rule:MF_03041}#Spindle apparatus coiled-coil domain-containing protein 1-A {ECO:0000255|HAMAP-Rule:MF_03041}', '-', '-', '734358'),
(858, 'Q9XZ57', 'Eb1; isoform ELD08743p', 'k', 32489, '', 'MAVNVYSTNVTSENLSRHDMLAWVNDCLQSQFSKIEELCTGAAYCQFMDMLFPNSVPVKRVKFRTNLEHEYIQNFKILQAGFKKMSVDKIIPIDKLVKGRFQDNFEFLQWFKKFFDANYDGRDYDASAVREGAPMGFGSGAVKSLPGTAASGVSSSYRRGPSATTRPAMTSAVKPISKVLPRTNNAAPASRINACANSTGTVKKNDVSNSVNNQQIEEMSNQVMDMRINLEGLEKERDFYFSKLRDIEILCQEADDAEAHPIIQKILDILYATEDGFAPPDDAPPEDEEY', 290, 'Q9XZ57;', 'KD00858', 'Drosophila melanogaster (Fruit fly)', 'Eb1', '#Eb1; isoform E {ECO:0000313|EMBL:AAS64780.1}#LD08743p {ECO:0000313|EMBL:AAD27859.1}', '-', '-', '35584'),
(859, 'Q0P426', 'Spindle and kinetochore-associated protein 2', 'GO:0000940', 25296, '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}.', 'METVDKLEAMFQKAEADIEYVEKRLKFDFMASAREAGTFEGNPVELLEDLSAIKARHAALCAQVEEIAAEQKRSMDSIRAHLDTTVQLVQQLQNTADVQVPPLTEEEQEARDALCSSVAALNVEAMPTSEPQSQAQSEAQNVHEDVSEKTFETVPRSVRGNLKLKDLNALYKQLFEHFSDKSRGPISTQRMKKLNMKVNDSALKTLQHLKLIELDKKGLVSLLAND', 226, 'Q0P426;', 'KD00859', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'ska2', '#Spindle and kinetochore-associated protein 2#Protein FAM33A', '-', '-', '-'),
(860, 'Q8BW94', 'Dynein heavy chain 3; axonemal', 'GO:0003777', 467777, '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}.', 'MSDTNCSAQKLDKSDSVHHMSHSQARPELPPLPVSANEEPSELYKTVMSHSFYPPLMQRTSWTLAVPFKEQDHHRGPSDSIGNNYSLTARDMKLKDLLKVYQPVTISIPRDKTSQGLPLGTSSKTSTEPSKKKMKFNLKAKDDVTGMPFVCKFSSSLSIKNTTDSSVTHPESRPMSPEQQMDVMLQQEMEIESKEQKPSELDLERYYYYLTNGIRKDMIAPENEEVMMRIYKLIPKTLLTTPALEPLQVSLRSEKESDYYYSLMKSIVDYILMDPMEKKRLFIKSIPRLFPHRVIRAPVPWHNIYQSTKKWNEEHLHTVNPMMYKLKELWFAEFQNLRFVRTADLLAGKLPLLPHEYKEVVQKHCREARHILLTKWIPTCAQLFVTQKEHWVHFAPKNDYDSSRNIEEYFASVASFMSLQLRDLVIKSLRDLVSFFMIHKDGNDFKEPYQEMDFFIPQLIMIKLEVRDPIIVFNPTFDDCWQLIKNSFLEIIKNSDGIPKVYLCWKPLASYICVSPHLRMTSVLQVESILFPDLKGYNMILGTVNPEESLVSDFLDQTLEVFKKNQVGPYKYLNVYKKYDDLLDNMAEKGISEFLKEKHEIEDFVTSINSIKKRKNEIASMHITVPLAMFCLDAVFLNYDLCERAQNLKDNLILYQVDVNRETNTSICNQYSTIADKVSEIPANTAELVALIEYLKKSSDVTVFKLRRQLRDASERLEFLMDYADLPSESIEDVFESSRNLLMSKRDQAEMDLIKRCSEFESRLEGYSKELEMFRKREVMTTEEMKNNVEKLHDLSKNLDLALTEFELINKEEELLEKEKSSFPLLQTLMINKIPYEQLWVTAYEFSTKSEEWMNGPLYLMNAEQIAEEIGNMWRTTYKLTKTLIDVPAPKRLAENVKLKIEKFKQHIPILNIACNPGMKDRHWQQISDIVGYEIKPTETTCLANMLEYGFGKFVDKLEPIGAAASKEYSLEKNLEKMKADWVNMCFSFVKYRDTDTSILCAVDDIQLILDDHVIKTQTMCGSVFIKPIEAECRKWEEKLVRVQENLDAWLKCQVTWLYLEPIFSSEDIIAQMPEEGKKFTTVDTYWKSLMAQAVNDTRVMVAADQPRMTEKLQEANVLLEDIQRGLNDYLEKKRLFFPRFFFLSNDELLEILSETKDPLRVQPHLKKCFEGIAKLEFTDNLEIKGMISSEKETVPFIQTIYPVKAKGMVEKWLQQVEQVMLASMRQVIENGIEAYVQVPRNAWVLEWPGQVVICVSSIFWTREVSEALVEDTLTDFLKKSNDQIAQIVELVRGKLSSGARLTLGALTVIDVHARDVVAKLRHDHINSLNDFQWISQLRYYWTEKNVHVQMITTEALYGYEYLGNSPRLVITPLTDRCYRTLMGALKLNLGGAPEGPAGTGKTETTKDLAKALAKQCVVFNCSDGLDYKAMGKFFKGLAQAGAWACFDEFNRIEVEVLSVVAQQILSIQQAIIRKLKRFIFEGTELSLNPTCAVFITMNPGYAGRAELPDNLKALFRTVAMMVPDYALIGEISLYSMGFLDSRSLAQKIVATYRLCSEQLSSQHHYDYGMRAVKSVLTAAGNLKLKYPEENESVLLLRALLDVNLAKFLAQDVPLFQGIISDLFPGVVLPKPDYEVFLEALNNNIRKMKLQPVPWFIGKIIQIYEMMLVRHGYMIVGDPMGGKTSAYKVLAAALGDLHAANQMEEFAVEFKIINPKAITMGQLYGCFDAVSHEWTDGVLANAFREQASSITDDRKWIIFDGPVDAVWIENMNTVLDDNKKLCLMSGEIIQMSSKMSLIFEPADLEQASPATVSRCGMIYMEAHQLGWKPLKDSYMDTLPRCLTKEHTELVEDMFTWLVQPCLDFSRLHCKFVVQTSPIHLAFSMMRLYSSLLDEIRDIQEEEMEIYEGLSSQQIFLWLQGLFLFSLVWTLAGTINAESRKKFDVFFRNLIMGMDDRNPRPKSVKLTKNNIFPERGSIYDFYFLKQGGGHWNAWTEYITKEEETIPANAKVSDLIIPTMETARQSFFLKTYLDHEIPILFVGPTGTGKSAITNDFLLHLPKNVYQPNFINFSARTSANQTQDIIMSKLDRRRKGLFGPPIGKKAVVFVDDLNMPAKEVYGAQPPIELLRQWIDHGYWFDKKDTNRLDIVDVLLVTAMGPPGGGRNDITGRFTRHLNIISINAFEDEILTKIFSSIADWHFGKGFDVMFLRYGKMLVQATQTIYRAAVENFLPTPSKSHYVFNLRDFSRVIQGVLLCPHTHLQDLEKFIRLWIHEVYRVFYDRLIDNDDRQTFFNLVKETTSNCFKQTMEKVLIHLSPTGKITDDNIRSLFFGDYLKPESDQKIYDEIIDLRGLTVVMEYYLDEFNSVSKAPMSLVMFKFAIEHISRICRVLKQKKGHLLLVGIGGSGRQSATKLSTFMNSYELYQIEITKNYTNSDWREDLKKIMLQSGVATKSTVFLFSDNQIKHESFVEDINMLLNTGDVPNIFPADEKADLVEKMQTAARTEGEKVEATPLSMYNFFIERGTNRAYFSLAMSPIGDAFRTRLRMFPSLINCCTIDWFQSWPTDALELVANKFLEDVELDDNIRAEVVSMCKYFQESVKKLSVDYYNTLLRHNYVTPTSYLELILTFKTLLNSKRQEVDTIRNRYLAGLQKLEFASSQVAVMQVELTALQPQLIQTSEDTAMMMVKIELETKEADAKKLLVQADEKEANAAAAISQAIKNECEGDLAEAMPALEAALAALDTLNPSDITLVKSMQNPPGPVKLVMESICVMKGLKPERKPDPSGSGKMIEDYWGVSRKILGDLKFLESLKTYDKDNIPSVIMKRIRERFIDHPDFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLREAEGKLEIQMQKLNQKRAELKLVEDRLQDLNDEFELMNRKKNSLEKNIEICSQKLVRAEKLISGLGGEKDRWTEAARQLGIRYDNLTGDVLLASGTVAYLGAFTVDYRAQCQNEWLVSCKDKVIPGSVDFSLSNTLGDPIKIRAWQIAGLPVDSFSVDNGIIVSNSRRWPLMIDPQGQANKWVKNMEKTNKLSVIKFSDTNYVRTLENALQFGTPVLLENVGEELDAFIEPILLKATFKQQGVEYMRLGENIIEYSREFKFYITTRLRNPHYLPEVAVKVCLLNFMITPLGLQDQLLGIVAAKEKPELEEKKNKLILESAQNKKQLKEIEDKILEVLSLCEGNILEDETAIKILSSSKVLSEEISEKQEIASVTETQIDETRMGYKPVAVHSAAIFFCISDLAHIEPMYQYSLTWFINLYVQSLANSNKSDELDLRIEYIIEHFTLSIYNNVCRSLFEKDKLLFSLLLTVGLLKERKAIDEEVWYFLLTGGVALDNPFPNPAPEWLSEKSWGEIVRASSLQKLKGLMEDVMQNIKVWKDIYDSAWPHEESLPSPWFFLQTLEKIAILRCLRPDKIVPAIQNFICETMGKIFIEAPTFDLQGSYGDSSCCVPLIFILSPGADPMAGLLKFADDVSMGGTKTQTISLGQGQGPIAANMINKAIHEGTWVVLQNCHLATSWMPALEKICEEVIVPENTNSEFRLWLTSYPSEKFPVSILQNGIKMTNEPPKGLRANLLRSYLNDPISDPLFFQSCTKPVIWQKLLFGLCFFHAIVQERRNYGALGWNIPYEFNESDLRISMRQIQMFLNDYEEVPFEALTYLTGECNYGGRVTDDKDRRLLLSLLSMFYCKEIETDNYHIAPGDAYVIPPYGSYQSYIEYLRTLPITAHPEVFGLHENADITKDNQETNQLFQGVLLTLPRQSGGSGKSPQEVVEELAQDILSKLPNDFNLEEVMKKYPVVYKESMNTVLRQELIRFNRLTKVVRRSLIDLGRAIKGQVLMSSELEEVFNSMLVGKVPAMWAAKSYPSLKPLGGYVADLLARLTFFQEWIDKGPPVVFWISGFYFTQSFLTGVSQNYARKYTIPIDHIGFEFEVTPKETTMENIPEDGAYIKGLFLEGARWDRSTSQIGESLPKILYDPLPIIWLKPGESASFLHQDIYVCPVYKTSARRGILSTTGHSTNYVLSIELPTDMPQKHWINRGVASLCQLDN', 4083, 'Q8BW94; O08829; Q7TT83;', 'KD00860', 'Mus musculus (Mouse)', 'Dnah3', '#Dynein heavy chain 3; axonemal#Axonemal beta dynein heavy chain 3#Ciliary dynein heavy chain 3', '-', '-', '-'),
(861, 'E3RPB1', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 33978, '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}.', 'MNVQYQAFTPPHLLNNTRRSPTRNISSLSSAMSGRKRKAEDDGSAGDDDRMSASPSASPAVLPRPAPRGMKRMRTNISGRPLPLPRLLETLSPDEMRNLLQSICQRHPDISNEIVTTAPRPSIQSTLEVLAKYEASFQAAFPFGGRASSDYAYNRVRQQLDELLDSLKDFTPHFLPPNEQQPATSLAFLDGATDIIHRLPNWDTFQHNRHKQEAYEEMAKAWAIVIREAAKKAGGIQLQYGGWDEKIAKHNEISGGKMQEAVNELRGGLGWMGAETSNSAAGAPADAMSIRQQLLSGNYGAGSPASIGAW', 310, 'E3RPB1;', 'KD00861', 'Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus(Drechslera teres f. teres)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '10519386'),
(862, 'Q06162', 'Central kinetochore subunit NKP2', 'GO:0000776===GO:0000777===k', 17862, '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.', 'MNSEQLLHNYVSDSLLTTLISFQEFKQQLQSYTSDEQQLQHWYELLQARDARVTSELEARIKQFFITLRSRLLRFLESEQLSHSLSLETLIDALYKINDLLQQRLQILDDAIQEKTSELAEFENMVRSPSAGDNAIPGLLQIIQSYINLLEEN', 153, 'Q06162; D6VYV9;', 'KD00862', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'NKP2', '#Central kinetochore subunit NKP2#Non-essential kinetochore protein 2', '-', '-', '851025'),
(863, 'Q4R834', 'NAD-dependent protein deacetylase sirtuin-2', 'GO:0051987', 43222, '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}.', 'MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMILGLGGGMDFDSKKAYRDVAWLGDCDQGCLALAELLGWKKELEDLVRREHASIDAQSGAEAPNPSTSASPRKSPPPAQDEARTTEREKPQ', 389, 'Q4R834;', 'KD00863', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'SIRT2', '#NAD-dependent protein deacetylase sirtuin-2#3.5.1.-#Regulatory protein SIR2 homolog 2#SIR2-like protein 2', '-', '-', '-'),
(864, 'Q05090', 'Kinesin light chain', 'GO:0003777', 76517, '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.', 'MSGSKLSTPNNSGGGQGNLSQEQIITGTREVIKGLEQLKNEHNDILNSLYQSLKMLKKDTPGDSNLVEEKTDIIEKSLESLELGLGEAKVMMALGHHLNMVEAEKQKLRAQVRRLVQENTWLRDELAATQQKLQTSEQNLADLEVKYKHLEYMNSIKKYDEDRTPDEEASSSDPLDLGFPEDDDGGQADESYPQPQTGSGSVSAAAGGYEIPARLRTLHNLVIQYASQSRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAGNLLHDALAIREKTLGPDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEWYYQRALEIYEKKLGPDDPNVAKTKNNLAAAYLKQGKYKAAETLYKQVLTRAHEREFGLSADDKDNKPIWMQAEEREEKGKFKDNAPYGDYGGWHKAAKVDSRSRSSPTVTTTLKNLGALYRRQGKYDAAEILEECAMKSRRNALDMVRETKVRELLGQDLSTDVPRSEAMAKERHHRRSSGTPRHGSTESVSYEKTDGSEEVSIGVAWKAKRKAKDRSRSIPAGYVEIPRSPPHVLVENGDGKLRRSGSLSKLRASVRRSSTKLLNKLKGRESDDDGGMKRASSMSVLPSRGNDESTPAPIQLSQRGRVGSHDNLSSRRQSGNF', 686, 'Q05090; Q04801; Q05088; Q05089;', 'KD00864', 'Strongylocentrotus purpuratus (Purple sea urchin)', '', '#Kinesin light chain#KLC', '-', '-', '373373'),
(865, 'Q8CFN2', 'Cell division control protein 42 homolog', 'GO:0051988', 21259, 'Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin; actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration (By similarity). {ECO:0000250}.', 'MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL', 191, 'Q8CFN2; Q6P9Y3; Q71TW5;', 'KD00865', 'Rattus norvegicus (Rat)', 'Cdc42', '#Cell division control protein 42 homolog', '-', '-', '64465'),
(866, 'Q06168', 'Chromatin structure-remodeling complex subunit SFH1', 'k', 48777, 'Component of the chromatin structure-remodeling complex (RSC); which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation; DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes; RSC complex is required both for proper kinetochore function in chromosome segregation and; via a PKC1-dependent signaling pathway; for organization of the cellular cytoskeleton. This subunit is essential for mitotic growth and required for cell cycle progression. {ECO:0000269|PubMed:10025404; ECO:0000269|PubMed:10329629; ECO:0000269|PubMed:12072455; ECO:0000269|PubMed:12183366; ECO:0000269|PubMed:12697820; ECO:0000269|PubMed:8980231; ECO:0000269|PubMed:9154831}.', 'MSHQNQLIPQAYISNFHNRLTNEDDGIPIFTMAQQTRQHKRAKVVNYAEYDNDLFDEFNMNGSNFNNADTHYKDNAVSHENTPALTNGVTMDGSEYNVLENMNGADSIISNNKYDAGSNMVVESLSGLNSNNNASNGPSNKAQAQDIGNAVLPDLQDQHHNPFNILRYPKIRDTFINGKVVSPYRLNTDQETKANANSGEAIMIPITLDIEHMGHTIKDQFLWNYNDDSISPEEFASIYCKDLDMTSATLQTQIANIIKEQLKDLENIAATEIMSDLHVIINLTCNLQDRFFEDNFQWNLNDKSLTPERFATSIVQDLGLTREFIPLISQSLHETILKIKKDWVDGHLIQDHVPNDAAFGYLSGIRLDIDELGSNWCPRVEILTKEEIQKREIEKERNLRRLKRETDRLSRRGRRRLDDLETTMRM', 426, 'Q06168; D6VYW4;', 'KD00866', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SFH1', '#Chromatin structure-remodeling complex subunit SFH1#RSC complex subunit SFH1#SNF5 homolog 1', '-', '-', '851032'),
(867, 'Q3U8K7', 'Histone-lysine N-methyltransferase SUV420H1', 'GO:0000780', 98580, 'Histone methyltransferase that specifically trimethylates ''Lys-20'' of histone H4. H4 ''Lys-20'' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1; RBL1 and RBL2). Plays a role in myogenesis by regulating the expression of target genes; such as EID3. {ECO:0000269|PubMed:15145825; ECO:0000269|PubMed:23720823}.', 'MKWLGDSKNMVVNGRRNGGKLSNDHQQNQSKLQQHSGKDTLKTGRNAVERRSSRCHGNSGFEGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHISKADSFSHNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKEHVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNRLKKLGDSSKNSDSQSVSSNTDADTTQEKDNATSNRKSSVGVKKSSKSRALTRPSMPRVPAASNSTSPKLVHTNNPRVPKKLRKPAKPLLSKIRLRNHCKRLDQKSASRKLEMGSLVLKEPKVVLYKNLPIKKEREPEGPAHAAVGSGCLTRHAAREHRQNHGRGAHSQGDSLPCTYTTRRSLRTRTGLKETTDIKLEPSPLDGYKNGILEPCPDSGQQPTPEVLEELAPETAHREEASQECPKNDSCLSRKKFRQVKPVKHLAKTEDCSPEHSFPGKDGLPDLPGSHPDQGEPSGTVRVPVSHTDSAPSPVGCSVVAPDSFTKDSFRTAQSKKKRRVTRYDAQLILENSSGIPKLTLRRRHDSSSKTNDHESDGVNSSKISIKLSKDHDSDSNLYVAKLSNGVSAGPGSSSTKLKIQLKRDEESRGPCAEGLHENGVCCSDPLSLLESQMEVDDYSQYEEDSTDESSSSEGEEEEEDCEDDFDDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA', 883, 'Q3U8K7; Q3UTP6; Q6DI74; Q6Q784; Q8BU67; Q8BUN0; Q8BUT7; Q8BW73;Q8BZ24; Q91X81;', 'KD00867', 'Mus musculus (Mouse)', 'Suv420h1', '#Histone-lysine N-methyltransferase SUV420H1#2.1.1.43#Suppressor of variegation 4-20 homolog 1#Su(var)4-20 homolog 1#Suv4-20h1', '-', '-', '225888'),
(868, 'Q9UEE9', 'Craniofacial development protein 1', 'GO:0000777===SCL===k', 33593, 'May play a role during embryogenesis. {ECO:0000250}.', 'MEEFDSEDFSTSEEDEDYVPSGGEYSEDDVNELVKEDEVDGEEQTQKTQGKKRKAQSIPARKRRQGGLSLEEEEEEDANSESEGSSSEEEDDAAEQEKGIGSEDARKKKEDELWASFLNDVGPKSKVPPSTQVKKGEETEETSSSKLLVKAEELEKPKETEKVKITKVFDFAGEEVRVTKEVDATSKEAKSFFKQNEKEKPQANVPSALPSLPAGSGLKRSSGMSSLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP', 299, 'Q9UEE9; O00393; O00404; Q9UEF0; Q9UEF1; Q9UEF8;', 'KD00868', 'Homo sapiens (Human)', 'CFDP1', '#Craniofacial development protein 1#Bucentaur', '-', 'ENSG00000153774', '-'),
(869, 'O74309', 'Histone transcription regulator slm9', 'k', 90433, 'Probably required for replication-independent chromatin assembly (By similarity). Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. May play an indirect role in the regulation of cdc2 and/or wee1 at the G2/M stage of mitosis. {ECO:0000250; ECO:0000269|PubMed:10835386; ECO:0000269|PubMed:15121850; ECO:0000269|PubMed:16428807}.', 'MHIFVPKLLENHQFSSISSSKDFVAVSAETNVYILSKDFFYPKSSEKRIIQSLNGHKTTHLSFDSPISCIRFTYDGSCLAVATEAGTFLYHSEKWDKAFQVLSGPAYEVCWSQQGHILATSWKQISIYVKDEGLRTETIVKKTEHADSNHQPAVSIEESKEAVESTSQSSEISFKLIKVIEGHHTFVGGLAFDPMGQFLASQSFDHTLKVWKLSTFGVEKSIAKPFEQMPTGNRFLRLSWSPDGAHIASVNAVNEGAYVIAIVQRDTWTYDINLVGHQGPLECATFNPYLYEDPFQKSIIASAAHDGCVSIWNTACARPMAVIHELSCSSFVDLQWSTSGFELYGVSLDGNLMLLQFEESEFGEKMDTIHYPDDLSYFNSSRSKAHVNKNAAADRTTSPTQGQPESPSKSILLRPPPSIASSPESKRRKCPKKFVARPPVPHPTSLYSQIRIGCPYLKPKLVISKSFGTLIVKNHNQLSLLKCTFSNLDGNDCSWFSYLPNAIVLANGTSVFWAVATEDSSIYIYSPAGRLLLPPVVVAATPCFLECCGDFLCCIVSTGLLYIWNIKNFEAIHSPVSTLPLFHSNFSVSKIARGPSIEQFFVTKQGHPVAIMSDGNAFAFIRDSSSWLRVSEGWWMIGSQYWGPLASESNEESPLGFLERCTDEEIIKAGRGRFLQRLVKALMLRQGYDNYEMLVSIRHLENRLMSSAKLDLEYDFRENLILYAKKIAEEGMKDKMDELCKELLGPLRIPHNGIDTVKVGNRLWSPTIAGNNKRNLLKDIIIHTAKYRDMQRITSQYSDLLRRSALL', 807, 'O74309;', 'KD00869', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'slm9', '#Histone transcription regulator slm9', '-', '-', '2540128'),
(870, 'Q80WE4', 'Kinesin-like protein KIF20B', 'GO:0003777', 203514, 'Plus-end-directed motor enzyme that is required for completion of cytokinesis. {ECO:0000250}.', 'MESHLNPDGVPRPSYVFSADPIARPLEINFDGVKLDLSHEFSLVASNPAANSLGSKNYLQVCLRIRPFTQSEKEHEAEGCVQVLDSQSVLLKDPQSILGHLSEKSSGQVAQKFSFSKVFGPETSQKEFFLGCIMQPVKDLLEGHSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKMSFKPHRCREYLKLSSDQEKEESANKNTLLRQIKEVTIHNDSYDVLCGHLTNSLTIPEFEESVNSCDQSSLNVDNIKYSVWVSFFEIYNESIYDLFVPVSSKFQKRKMLRLSQDIKGYSFIKDLQWVQVSDSKEAYRLLKLGVKHQSVAFTKLNNASSRSHSIFTIRILQIEDSEIPRVTRVSELSLCDLAGSERSMKTQNEGERLREAGNINTSLLTLGKCINVLKNSEKSKVQHVPFRESKLTHYFQSFFTGKGKICMIINISQSCSAYDETLNVLKFSTTAQRVYVPDTLSSSQEKSFASNKSLQDVSLDSNLDNKILNVKRKTVSWENSLEDVLENEDLVEDLEENEETQNMETELTDEDSDKSLEECRVSTCHKKNKELLDLIEKLNKRLINENKEKLTLELKIREEVTQEFTQYWSQREADFKETLLHEREILEENAERRLAIFKDLVGKCDSQDEPTNRICDIELETEEAHNYVGVEDIFHSLQDDVTDIKKQAELAHLYITSLVDPQEAIACLQLKFNQVKAELAETKEELIKAQEELKNRESNSLVQALKTSSKVDTSLTSNKSTCNETSEMPKNSRAQTHSERKRLNEDGLQLGEPPAKKGLILVSPPITEEQNKMGEMQQSVSEVVEGNRVLKEKNEELKRLLTIGENELRNEKEEKAELNKQVVSLQQQLRFFEEKNSSLRADVEQIQASYNSAVAELQTQKAVNQEQRDRILKLSQEMETAARSIESNVSQIKQMQTKIDELRSLDSPSHISKIDLLNLQDLSSGAKGDNCLNTSQQLPGGDFSSTWVKEYHTQEISRENSFHASIEAIWEECKEIVKASSKKSHQIQGLEEQIEKLQVEVKGYREENSDLRAQESQGKNRDHQLKEKESLIQQLREELQEKSVSLRVQVQLVAEREQALSELSQDVTCYKAKIKDLEVIVETQKDECKRLVELEQSILEKESAILKLEANLKECEAKHQDHIRTNDLSAKEVKFREEVTRLANNLHDTKQLLQSKEEENEISRQETEKLKEELAANSILTQNLKADLQKKEEDCAELKEKFIDAKKQIEQVQREVSVMRDEEKLLRIKINELEKKKNQYSQDLDMKQRTIQQLKEQLSNQKMEEAVQQYEKVCKDLSVKEKLVEDMRLTLVEQEQTQAEQDRVLEAKSEEADWLATELDKWKEKFKDLETRSNQRLNTGTMDDLDVLTRKFSKLQDELQESEEKYKADRKKWLEEKAVLTTQAKEAENVRNREMRKYADDRERCLKLQNEVETLTAQLAEKNSELQKWREERDQLVTAVETQMKALLSSCKHKDEEIQELRKAAAKSTGTENQTMNPKPEYNDSVDLGGVETEPQSTSLEISRNTAEDGSVVLDSCEVSTENVQSTRFPKPELEIQFTPLQPNKMAVKHPGCPTPVTIKIPKARKRKSGEVEEDLVKCENKKNSTPRSNVKFPVSEHRNSPVKKEQKVSVGPSSKKTYSLRSQASTVSANIASKKREGTLQKFGDFLQHSPTILQSKAKKIIETMSSPKLSTVEVSKENVSQPKKAKRKLYRNEISSPINISGQVILMEQKVKETDHQILKRRLRTRTAK', 1774, 'Q80WE4; E9QPW5; Q3V347; Q80VC0; Q8BLI2; Q99PT5;', 'KD00870', 'Mus musculus (Mouse)', 'Kif20b', '#Kinesin-like protein KIF20B#Kinesin family member 20B#Kinesin-related motor interacting with PIN1#M-phase phosphoprotein 1#MPP1', '-', '-', '240641'),
(871, 'B0Y5Q9', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 34278, '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}.', 'MNSLVATPPVPPHFYEYSRLSSPHPMSTPTHTPINRKRKADDDGNDHDGRMSASPTNSPAFTPRSLPAPRSFKRSRPNVSGRPLSLPRLLETLDTDALRGILRSMCERHPALADEVIHTSPRPSVSSALQVLRNYQSTLQNSFPLGGNPESDYAYNRVRQPLGNLLDALSDFTPHFLPPHETQASVSLSYLDGATDIIHALPRWHSPQNNIERDSAYDEICKAWILVIREAAKRGGGIQLQYGGWDQKLAKHNQNAGGRLQAAVNELGNSLGWMHGPDSQGYGSSTGGDLVSVREQLLSGTYGLGTPVKVGPW', 313, 'B0Y5Q9;', 'KD00871', 'Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163(Aspergillus fumigatus)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '-'),
(872, 'Q39610', 'Dynein alpha chain; flagellar outer arm', 'GO:0003777', 503617, '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.', 'MSIFWEVPNAQGEAPCPRSGHSFTVLGERFVLFGGCGRKDGKAAAFNDLYELDTSDPDEYKWKELVVANAPPPRARHAAIALDDKRLLVFGGLNKRIRYNDVWLFNYDDKSWTCMEVEGAAPEPRAHFTATRFGSRVFIFGGYGGSGQVYNEMWVLHFGEDGFRWQNITESIEGTGPAPRFDHSAFIYPVTPNSDTYDKLLIMGGRDLSQMYQDSHMLDLNKMAWENETQPPTLPYEICNNVCDGIESVPYHKVFSFGGRKGMMQYLNTVEVMDCGTQMWSTPPVDHGVAPVGREDTAWVFDVKTCSLLIFGGWANRWLGDLHKLNVSPIIGPPYACTAIQPEMGPVFGSTELVIRGLRFRDGKVQVKFGLSEKNEVVVEGTYVDQETIRVQTPNYEQFGALTVDVRVSINGEGWTVNKIKYAYFANTAARNCIAYGPGLLAETISGVEVPFIIQAKDTLNDKRTSGGDVFKVTVVSADGKNEGVSRVRDLQNGQYEVQYAAPTAGPYLIHVAFNELGTSDFVPIRGSPFTVKCTDSWTKHRVMGAAPAKRKGATICTMGNELVLYGGDKSGVTVLNTEGAEWRWSPATVSGSTPPDRTAHSTVVLSDGELVVFGGINLADQNDLNDIYYLRKQGEGWVWSCPSESRPYIRHPKGAAAVSAEPSAEPAAEPAAEPAAEPDADAPAAEPAAEGEEGAVPAEGEEGAEGATGSRPVSAKPAPAAAAPAAEALPELPVSARNSHVAVAIDKDLYVMMGDHDGDLMTELAMVDTSDRTCAHWLEPILKGDVPVPRKACAAAATGNTIVLFGGQTQNADGEATVTGDLVIMEVTGPNSIQCAVNPAAPGASGSPAARYGAVMQEFSNGKLFLHGGMDAASKPLNDGWLFDVPSKTWQCVYVGSSDVVLPTGQLATLSGNRIVLVSAAVGSPKLDSVQSLDFQELRDQAGVHAKMRASTETLLKGLEDWVDTQAHGMELARSPEKLSKDFENGLRKVMDALFQVKSQRSQTDLLIDQLHEAFAQLAEEKVPGINKMEKRLEAAAHKWDEIKKAQPQVKTDVEPIQAAKGEDIKKEIETFAAKVRNYRADFRRRGFFKYATGFDGAYPLLDAAAHELAELKKECDRLSELASVFEFPQAIEPVTVAIKETVEDLVMVKDVWDTAVLCELQFQDWRQTLWSDIRTDIMEEGAKQFVKEVKSLHKKVRDEDVFRGVDQVVKNFLVSVPLVADLRSPAMRDRHWEQLMATTKMTFNVKDPNFKLDDLLALELHKFEEEVGEIVDRAQKEEKMEIAIRKLNDTWTRVEFQFHRHKDYDVHTVKMAEEDFEALEDNQVQVQGMIANRYMATFKDEILGWQKKLNDVADVNQIMAEIQRTWAYLESLFIHSEEVKKELPQATERFAAIDTEVKKVLREFQQLKNCVSCCNREGLYANLETQERELEICKKALNDYMESKRRAFPRFYFVSSADLLDILSNGNNPMRVQIHMNKCFQAIDNVRLDSEEVVPGRRPKALGMESCVGIEYVPFSSLPLENKVEQYMNDIIAKMRNDVRMVLKASVEDYPSKPRDKWLFDWPSQIILVVNQIYWCLEVEQAFTEMARGDKGAMSKYNEFQVKQLTKLIEVTRTDLSKPDRQKIMNMITIDAHSRDMVLAGADQPDSFQWVSQLRSYWDRDISDCRIRICDASFPYGYEYLGNGPRLVITPLTDRIYITATQACWLSLGTAPAGPAGTGKTETTKDLSAQLGKSVYVFNCSPEMDYRTMGDIFKGLAASGSWGCFDEFNRLVPEVLSVCSVQYKCVTDSQKKKTMLPGRGLEYIKDGVKHPAVEHWSFIAADGVEMPLEEGTSAFITMNPGYIGRAELPESLKALFRPITVMVPDRQLIMENMLMAEGFVEAKMLAKKFASLYYLLEDLLSPQKHYDWGLRAIKSVLVVAGSLLRAEAGQVEADVLFRALRDFNIPKILAQDMVIFMGLLNDLFPGIDPPRKRDMEFEDVIVSTIKDLGLTPEDDFVLRVVQFSELLAIRHCVFLMGPTGTGRTECYRVLAKAITKGCNNPVNDYLKMTNKKKVVIRDINPKSISTYELYGQVNQATREWKDGLLSYYMRDVANMPGDDPKWLLLDGDLDANWIESMNSVMDDNRLLTLPSNERIRVLPHMKLIFEIRDLKFATPATATRAGILYISEGQQWHNMAMSWINRVVKPYAERAKWKDPQLPCTWLREMFDKYIPPTLLEMKKSYSHITPLAQMNFISTLVNIMEGVLKPENLSNKADQAMFEMYFVFAMIWAFGGGLVEKDGIPYRRNFDKWFKQTWTTVKIPGKGTVYDYFVNPKTQKFQPWAELVTDIDYDGSRPMSTVFVPTAETSSLRFFLDMMVDLRKPIMFVGGAGVGKTQLVKGKLGSLNEEQISLSISFNYFTDVVSFQKVLESPLEKQPAGINYGPPGTKQLIYFVDDLNMPKLDLYETAMPISLIRQHLGWGHWFDRAKLTPKNINNTQYVACMNPTAGSFIINPRLQRLFMTLAVDFPGQDSLMKIYGTFLQGHLKKFSESIQDMGTKILQAALALHDRVSQTFRKTAINFHYEFTVRHLANVFQGLLMSTPEAFNSPTKWGKLWLHESERVYADRLVSLYDLDAYNKAATAIAKKYFSVADIDDYYKKKDPKPLIFCHFARGLADKAYDEVADYTSLYKTLTEALNEYNETNAAMDLVLFEDAMKHVCRISRIVSNPSGHALLVGVGGSGKQSLARLAAHICGYATQMIVISGSYSMNNFKEDIQKMYKRTGVKGEGVMFLFTDSQIVDERMLVYINDLLSSGEIPDLFPQEDRDEIVNALRSETKSLGLLDTAENCWATFIQKVKTNLHMVFTASPVGENFRVRSQRFLATVTSTVIDWFQPWPESSLFSVAKRFLDEVDLGEDAVANAVVEFMPYSFQLVNKVSIKFREQERRYNYTTPKTFLELIKLYKNVLAAKRKANQDNTERLENGLHKLHKVQADVDILVEEAKVKAVEVEHKVASANIFAEQVGVEKEKVNAENAAAQVEAEKCAVIAKEVSEKQASCEKDLAAAEPLVAEAMAALETVTKKDLGEAKSLKKPPPGVDDITAVVIILLENNPKDKSWQAAQKLMNNVDKFLERVKSFKSVIDAGQVARKTVDACRPYLALEWFNREAIGKKSAAAAGLCEWAVNIIKYYDVVQEVEPKRQELAAANAKLEEANVTLAAVEEKVALLNAKVQELEQQYKEANDDKEAAIRESERCQRKLELANRLINALASEGERWALTVEQLRKSYEVLTGDMLLAAAFVSYAGPFTAKFRAHVIDDWILFLRERHMPMTEGITDPLKVLVDDALVAGWIREGLPSDPTSVQNGTILTNSERWSLMMDPQLQGILWIKERESKNNLQVTRMGASNMLQVMERAIEAGHSVLVENMGETIDAVLNPIITRSTFKKGRSLYVKLGDKECEYNKNFRLFLHTKLSNPHYPPEIQAETTLINFTVTEAGLEDQLLALVVNKERPDLEETKTQLIIQNTEFTIKLKELEDGLLLKLSTAEGDITEDVALIESLEDAKRVSTEISEKVKESRETEAAINENRNKYRTVAARGAMLFFLLNSLNKIHAFYQFSLNAFVTVFSRGLDLAPGGRKKGKGLKKTPSLRDQPMDHQSLMEKARRSSGVGDRRPSQEGLPGPEASQASLAESQGGRGSQVGDAEDEDDESFAMAPEALEQRLVNLLETCTFTVYNYTRRGLFDRDKLIVLSLLTFTILLRSQAVDASEYEALCRGMRNPTPPPITDDLSRWMAESQWAALDVLTTLPCFAHLAKDMEKNSDDWFNWCNNEAAERAPMPGEWGKLTEFRQLLIIRALRPDRITNALQNFCEHMMGSDYVNQDAFSPAAMMDESSSATPIFFILFPGYSPSKEIEVYANKCGYSVANGRLCLISMGQGQEAPAEAVLDKYTREGGWVFLDNVHLMQGWIPKLERKLEIAAESAHPDFRCFFSAEPINGAPHANIIPESILQTCIKISNEPPSDMKSNMRRAFAAFTPEQCDRPSTPAKRVAFRAILFGLCFYHSLLLGRKKFGVGIGTGSGSGLGFCRGYSFNIGDLTTCGDVLYNYLEAYEQIPWRDLQYMFGEVFYGGHITDSMDRRCCTTYLEVLIRNEILPKGNPDEVEAWEAPTLELAPGFFAPKPVDYPTLKEYIETSLPAESPVVYGMHPNAELSLLTSLGETLFKTVVEVAGGGGGGGGGGGGGENAVRQALETFKERLPEPFNMVEVELRVKEKTPFVVVALQEATRMNALLSEMKRSMEELQLGLDGALNMSDNMEKLAKGIASNTVPELWMSCMSTRVQEVYTLTAWYQDVVKRHDQLSAWTAGDIITPHSVWLPGLFNPKAFLTAVMQTFARANKLPLDVMKFMTEVTRMTSPEQVTEAAPLGVYVHGLVLEGARWDREDGCLRDSKPNELHPAMPVLQVKPVTADQFNLEGYYECPVYTNMQRANVYSPVVSTFTLRTQDMPAKWVLASVALLLQDDLAG', 4499, 'Q39610;', 'KD00872', 'Chlamydomonas reinhardtii (Chlamydomonas smithii)', 'ODA11', '#Dynein alpha chain; flagellar outer arm#DHC alpha', '-', '-', '-'),
(873, 'O64629', 'Serine/threonine-protein kinase Aurora-3', 'GO:0032133===GO:0000780', 33119, 'Phosphorylates in vitro histone H3 at ''Ser-10'' and ''Ser- 28''; but not at ''Thr-3'' or ''Thr-11''. Colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. {ECO:0000269|PubMed:16028112; ECO:0000269|PubMed:17087760}.', 'MSKKSTESDAGNTEKQWSLADFEIGRPLGKGKFGRVYLAREAKSKYIVALKVIFKEQIEKYKIHHQLRREMEIQTSLRHPNILRLFGWFHDNERIFLILEYAHGGELYGVLKQNGHLTEQQAATYIASLSQALAYCHGKCVIHRDIKPENLLLDHEGRLKIADFGWSVQSSNKRKTMCGTLDYLAPEMVENRDHDYAVDNWTLGILCYEFLYGNPPFEAESQKDTFKRILKIDLSFPLTPNVSEEAKNLISQLLVKDPSKRLSIEKIMQHPWIVKNADPKGVCASIDI', 288, 'O64629;', 'KD00873', 'Arabidopsis thaliana (Mouse-ear cress)', 'AUR3', '#Serine/threonine-protein kinase Aurora-3#AtAur3#2.7.11.1#Aurora-like kinase 3', '-', '-', '819157'),
(874, 'Q6CTI2', 'Histone H3-like centromeric protein CSE4', 'GO:0000777', 21410, '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}.', 'MEQSIRSIDGSRSLSNVGASLIDRESINQRALQLLQRNRRRRLLLNRSEDKARYIQPERSASSQQIHPPEHHISAHERITKARGTRYKPTDLALAEIRKYQRSTDLLISRMPFARLVKEVTDQFTTESEPLRWQSMAIMALQEASEAYLVGLLEHTNLLALHAKRITIMRKDMQLARRIRGQFI', 184, 'Q6CTI2;', 'KD00874', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog#Chromosome segregation protein 4', '-', '-', '2891972'),
(875, 'Q9Y6D9', 'Mitotic spindle assembly checkpoint protein MAD1', 'GO:0000776===GO:0000777===c;k;m', 83067, 'Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression; possibly by interfering with MYC binding. {ECO:0000269|PubMed:10049595; ECO:0000269|PubMed:12837246; ECO:0000269|PubMed:20133940}.', 'MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA', 718, 'Q9Y6D9; B3KR41; Q13312; Q75MI0; Q86UM4; Q9UNH0;', 'KD00875', 'Homo sapiens (Human)', 'MAD1L1', '#Mitotic spindle assembly checkpoint protein MAD1#Mitotic arrest deficient 1-like protein 1#MAD1-like protein 1#Mitotic checkpoint MAD1 protein homolog#HsMAD1#hMAD1#Tax-binding protein 181', '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;', 'ENSG00000002822', '-'),
(876, 'C7YRR5', 'Tethering factor for nuclear proteasome STS1', 'GO:0061638', 32729, '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}.', 'MNVLLSPQPPVFPHQHENHHLSPQRSLSPFHNMATRKRKADEDGDETMSPRSSPTISSRPLARPSKKIRANEVIGRPLALPRLLETLDTAQLRTVLERICERHPDIGHEVETGAPRPSVSSVVVVLQGYMEKLSNAVPYGETSPEYTYYRVKEPLVALIDALSDFTPQFLPPNETQPTKSLEFLNEATNIIHKLPDWEPQTYRHHKENAYEEISKAWALVINEAGKRAGGINLHSGGWDQILSRHNEQSGGRLAYAISAMTTSVGWLDPSTSSGPAGASDPNSILNQLMSGIMGLA', 296, 'C7YRR5;', 'KD00876', 'Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596MPVI) (Fusarium solani subsp. pisi)', 'STS1', '#Tethering factor for nuclear proteasome STS1', '-', '-', '9667992');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(877, 'P51955', 'Serine/threonine-protein kinase Nek2', 'GO:0000776===GO:0000777===GO:0051988===c;k;m', 51763, 'Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC; CEP250 and NINL; resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGOL1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Isoform 1 phosphorylates and activates NEK11 in G1/S- arrested cells. Isoform 2; which is not present in the nucleolus; does not. {ECO:0000269|PubMed:11742531; ECO:0000269|PubMed:12857871; ECO:0000269|PubMed:14978040; ECO:0000269|PubMed:15161910; ECO:0000269|PubMed:15358203; ECO:0000269|PubMed:15388344; ECO:0000269|PubMed:17283141; ECO:0000269|PubMed:17621308; ECO:0000269|PubMed:17626005; ECO:0000269|PubMed:18086858; ECO:0000269|PubMed:18297113; ECO:0000269|PubMed:20034488; ECO:0000269|PubMed:21076410}.', 'MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR', 445, 'P51955; Q53FD6; Q5I1Z9; Q5VXZ1; Q6NZX8; Q7Z634; Q86XH2; Q96QN9;', 'KD00877', 'Homo sapiens (Human)', 'NEK2', '#Serine/threonine-protein kinase Nek2#2.7.11.1#HSPK 21#Never in mitosis A-related kinase 2#NimA-related protein kinase 2#NimA-like protein kinase 1', '-', 'ENSG00000230450', '-'),
(878, 'Q5RBU1', 'Centromere protein X', 'GO:0000777===GO:0051382', 8985, '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}.', 'MEGPGAGSGFRKELVSRLLHLHFKDDKTKVSGDALQLMVELLKVFVVEAAVRGVRQAQAEDALRVDVDQLEKVLPQLLLDF', 81, 'Q5RBU1;', 'KD00878', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'STRA13', '#Centromere protein X#CENP-X#FANCM-interacting histone fold protein 2#Fanconi anemia-associated polypeptide of 10 kDa#Stimulated by retinoic acid gene 13 protein homolog', '-', '-', '100172339'),
(879, 'Q8VHE6', 'Dynein heavy chain 5; axonemal', 'GO:0003777', 527558, 'Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles. {ECO:0000269|PubMed:15269178}.', 'MFRIGRRQLWKQSVTRVLTQRLKEEKEAKRARLDGRHDYLFAIVASCLDLNKPEVEDALLEGNQIERMDQLFAVGGLRHLMFYYQDVEGAEAGHCGSSGGVNPASGKMKKPKVFVTEGKDVALMGACVFFIRSDPSKAITPENIHREVSFNTLDTADGGLLNSVRRLLSDIFIPALRASSHGWGELEGLQDASSIRQEFLSSLEGFVGILSGAQNSLKEKVNLQKCDIIELKSLKEPTDYLALASNPETVEKVECCMRVWIKQMEQILAENSQLRKEADDVGPRAELEHWKQRLSRFNYLLDQLKSPDVKAALALLAAAKSKLLKVWRDTDIRITDAANEAKDNVKYLYTLEKCCDPLYSSDPVTMIDAIPTLINAIKMVYSISHYYNTSEKITSLFVKVTNQMISACKAHITNNGTATIWSQPQEIVMQKIAAVIKLKQGYQSCFQETKQKLKQNPSEKQFDFSEMYIFGKFETFHRRLAKIMDIFTTFKTYSVLQDSKIEGLEDMATKYQDIVAAIKKKEYNFLDQREMDFDQDYEEFCKRINELHNDLQRFMDITFEKIPSTRQALSTLKKFERLNIPNLGIEEKYQIIFQNFATDIDTISKLYTKQKYDPPLARNQPPIAGKILWARQLFHRLEQPMQLFQQHPFVLRTAEAKPVIRSYNRIAKVLLEFEVLYHRAWLQQIEEIHAGLEASLLVKAPGTGELFVNFDPQILVLFRETQCMSQLGLPVSPFAAALFQKRDMFKKNFSDMKMMLSEYERVKLKMPPAIEQLMFPHLARVDEALQPGLAVLTWTSLNIGGYLENAFAKIKDLELLLDRVNDLIEFRIHAILEEMSSMALCQLPQDDPLTCEEFLQMTKDLCVSGAQLLHFKSSLVEEAVNELINMLLDVDVPPEEAAENVCHENASPSGNTSGRREGHSEALASSFNAGASSLPLTATARKKKETEVLEEARELLSHFNHQNTDALLKVTRNTLEAIRRRIHFSHMINFRDSNDASKAKQNHLPIFRASVTLAIPNIAMTPALEDIQQTLNKAVECIISVPKGVRQWSSELLSKRKMHERKMAAVKNNEDSDSDAEVEENELQETLEIASINLPIPVQTQNYYKNISDNKEIVKLVSVLSTVISSTKKEVITSMDRFKRYNHIWQKEKEDTIMTFIAQNPLLPEFESRILYFQSLEQEINAEPEYIRVGSIALYTADLKLSLTAETKAWMAVIGRHCNRKYRAEMENILTVVEESQKKLSRPIKDLDDIRIAMAALKEIREQQISTDFQVGPIEESYALLNKYGLLVAKEEMDKVDTLRYAWEKLLARASDVQNELGALQPSFRKELISTVEVFLQDCQQFYLDYDLNGPMASGLKPQEASGRLIIFQNQFDNIYRKYITYTGGEELFGLPVTPYPQLLEIKRQLNLLQKIYSLYNNVIETVNSYQDTLWSDVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKTIDDFSECCPLLEYMASNAMVERHWQRITALTGHSLDVGNETFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLRQVINEWDNKTLTFSGFKTRGELLLRGDSTSEVIASMEDSLMLLGSLLSNRYNMPFKAQIQKWVQCLSNSTDIIENWMTVQNLWIYLEAVFVGGDIAKQLPKEAKRFSNIDKSWVKIMTRAHEIPNVVQCCVGDETMGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVSDPALLEILGQASDSHTIQAHLLNVFDNIKTVKFHDKIYDRILSISSREGETIELDKPVMAEGNVEVWLNSLLEESQSSLHLVIRQAAANIQEPGFQLIEFLSSFPAQVGLLGIQMLWTRDSEEALRNAKFDKKIMQKTNQAFLELLNMLIEITTKDLSSMERVKYETLITIHVHQRDIFDDLCHMHVKSPTDFEWLKQCRFYFKEDSDKTMIHITDVAFIYQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFTDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINFRSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYQLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRASPTDTESTIVMRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELETAISKQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTLGPSGSGKTTCIHTLMKAMTDCGKPHREMRMNPKAITAPQMFGRLDVATNDWTDGIFSTLWRKTLKAKKGEHIWIVLDGPVDAIWIENLNSVLDDNKTLTLANGDRIPMAPNCKIVFEPHNIDNASPATVSRNGMVFMSSSVLDWSPILEGFLKRRSPQEAEILRQLYAETFPDLYRFSIQNLEFKMEVLEAFVITQSTHMLQGLIPPKEQAGEVDPEHLGRLFVFAMMWSVGAVLELEGRRRMELWLRSREGPTLHLPQLTDAGDTMFDYYVAPNGTWRHWSLCTPEYVYPPDTTPEYGSILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKGFMSKFDPESHMVKNLNFSSATTPVMFQRTIESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQSGFYNLEKPGEFTSIVDIQFLAAMIHPGGGRNDIPQRLKRQFSIFNCTLPSDASMDKIFGVIGAGYYCAQRGFSEEVQDALIKLVPLTRRLWQMTKLKMLPTPAKFHYVFNLRDLSRIWQGMLNITSEVIKDTDELLRLWKHECKRVIADRFSMSSDVTWFDKAVVSLVEEEFGEEKAPVVDCGVDAYFVDFLRDAPEATGETPEEADAEMPKLYEPIASLNHLRERLSVFLQLYNESIRGTGMDMVFFIDAMVHLVKISRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKEESFLEYMNNVLSSGEVSNLFARDEIDEINSDLTPIMKKEHPRRPPTNDNLYEYFMSRVRGNLHIVLCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLSSYTIDCTAEIKKELVQCMGSFQDGVAEKCADYFQRFRRSTHVTPKSYLSFIQGYKFIYEEKHMEVQSLANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMDCVLLLFQRRVNAVKIDVDKGCTMPSWQESLKLMTAGNFLQNLQQFPKDTINEEVIEFLNPYFEMSDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPLKANLIVQENRHILAMQDLQKAQAELDAKQAELDVVQAEYEQAMAEKQTLLEDADRCRHKMQTASTLISGLAGEKERWTEQSKEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLHDWKKEMKARKIPFGNGLNLNEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESQNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVGEELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTSIIDFTVTVKGLEDQLLGRVILTEKQELEKERTHLLEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIIVLSNTKKTAEEVTQKLEISGETEIQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDLSLARSVKSPITSKRIANIIEHMTYEVFKYAARGLYEEHKFLFTLLLTLKIDIQRNLVKHEEFLTLIKGGASLDLKACPPKPSKWILDMTWLNLVELSKLKQFSDILDQISRNEKMWRVWFDKENPEEEPLPNAYDKSLDCFRRLLLIRSWCPDRTIAQARKYIMDSMGENYAEGVILDLEKTWEESDPRTPLICLLSMGSDPTDSIIALGKRLKIETRYVSMGQGQEVHARKLLHQTMANGGWVLLQNCHLGLDFLDELMDVVTETETVHDTFRLWITTEVHKQFPITLLQMSIKFANEPPQGLRAGLRRTYGGVSQDLLDVSVGAQWKPMLYAVAFLHSTVQERRKFGPLGWNIPYEFNQADFNATVQFIQNHLDDMDVKKGVSWTTVRYMIGEIQYGGRVTDDYDKRLLNTFAKVWFSENMFGPDFTFYQGYNIPKCSTVDGYLQYIQSLPAYDSPEVFGLHPNADITYQSKLAKDVLDTILGIQPKDSSGGGDETREAVVARLADDMLEKLPEDYSPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSLVRSTLTELKLAVDGTIIMSENLRDALDCMFDARIPARWKKASWVSSTLGFWFTELLERNCQFTSWVSNGRPHCFWMTGFFNPQGFLTAMRQEITRANKGWALDNMVLCNEVTKFMKDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFELMPVIRIFAENNTARDPRLYCCPIYKKPVRTDLNYIAAVDLKTAQAPEHWVLRGVALLCDVK', 4621, 'Q8VHE6; E9QKD7; Q8BWG1;', 'KD00879', 'Mus musculus (Mouse)', 'Dnah5', '#Dynein heavy chain 5; axonemal#Axonemal beta dynein heavy chain 5#mDNAH5#Ciliary dynein heavy chain 5', '-', '-', '110082'),
(880, 'P20480', 'Protein claret segregational', 'GO:0003777', 77474, 'NCD is required for normal chromosomal segregation in meiosis; in females; and in early mitotic divisions of the embryo. The NCD motor activity is directed toward the microtubule''s minus end. {ECO:0000269|PubMed:2146510}.', 'MESRLPKPSGLKKPQMPIKTVLPTDRIRAGLGGGAAGAGAFNVNANQTYCGNLLPPLSRDLNNLPQVLERRGGGARAASPEPMKLGHRAKLRRSRSACDINELRGNKRTAAAPSLPSIPSKVSRLGGALTVSSQRLVRPAAPSSITATAVKRPPVTRPAPRAAGGAAAKKPAGTGAAASSGAAAAAPKRIAPYDFKARFHDLLEKHKVLKTKYEKQTEDMGELESMPQQLEETQNKLIETESSLKNTQSDNECLQRQVKQHTAKIETITSTLGRTKEELSELQAIHEKVKTEHAALSTEVVHLRQRTEELLRCNEQQAAELETCKEQLFQSNMERKELHNTVMDLRGNIRVFCRIRPPLESEENRMCCTWTYHDESTVELQSIDAQAKSKMGQQIFSFDQVFHPLSSQSDIFEMVSPLIQSALDGYNICIFAYGQTGSGKTYTMDGVPESVGVIPRTVDLLFDSIRGYRNLGWEYEIKATFLEIYNEVLYDLLSNEQKDMEIRMAKNNKNDIYVSNITEETVLDPNHLRHLMHTAKMNRATASTAGNERSSRSHAVTKLELIGRHAEKQEISVGSINLVDLAGSESPKTSTRMTETKNINRSLSELTNVILALLQKQDHIPYRNSKLTHLLMPSLGGNSKTLMFINVSPFQDCFQESVKSLRFAASVNSCKMTKAKRNRYLNNSVANSSTQSNNSGSFDK', 700, 'P20480; Q9VAG8;', 'KD00880', 'Drosophila melanogaster (Fruit fly)', 'ncd', '#Protein claret segregational', '-', '-', '43517'),
(881, 'O76406', 'KNL-3', 'k', 38407, '', 'MSQKSNDTTFSVRAALFASPVGSSSAVPKKKVAREVPRAGPPVFALEHDVSEVTDRNKDGTFLAADACASGPTLKVPDETQGCPETFSVSEHEDDDDVEPMEVDGTIVPSPQRATPTRGVTPCEKSTTPRRRSSRKSMPTPGKRLFFTSKDTTNEDRKADDSTQLELLMAKIPQEMSGYMKKLATDIKEMSQYDAQLARNIDDMEAVFKSRETKLKSAIEIAKDSFISSALPLRLETLDMTLRKEESPNDIVARLHGSFLDKTQDAGNVNTAQKENQQLEDERGMLEEKLESLNKIKREKDEFLAKMRKEEEEALARREEIKQGFERIDALMSKIKPIPIFEF', 343, 'O76406;', 'KD00881', 'Caenorhabditis elegans', 'knl-3', '#KNL-3 {ECO:0000313|EMBL:CCD74226.1}', '-', '-', '178669'),
(882, 'P53061', 'Protein ZIP2', 'k', 82816, 'Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation; a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis. Required for the normal localization of MSH4 to chromosomes. {ECO:0000269|PubMed:10319812; ECO:0000269|PubMed:10848609; ECO:0000269|PubMed:10943844; ECO:0000269|PubMed:11454751; ECO:0000269|PubMed:15805472; ECO:0000269|PubMed:16740482; ECO:0000269|PubMed:9590170}.', 'MIIERWEVKLSKCNQNVGGYSVLSGNLKENIKLGRRAQKYLKELRNLQLKPLKIGGYENCGTINGEEYFLEVIHITSGRQKIDVAVGKTWNVTNIENDNKEELQYELFKEKLKVGKQDMLFFSWMKSLSVQLNAPLHQKMTEHGLADDNTRLEWFNIPLLRRSQYRKKVPYPSLRQMSSVLEVQCSTLTEEKLNFCVGFSDKPLSEWKPQIFEQTYNRYRLQRISPEKSFKYKSRCSKYNFKTSSQSWVVKVPEHDQQLNTFEKRYDELFDAQFNKLEFFKIRMKKLKKNKPIEKKNYKIWCLEKEDLKDLVWDPLKRICNHSRYAIFEHVTINREAYSIKPLRLTFQKLDSGSLDLIDNQKKTFGSIKLAMSMPDVKKTENQSIEESERHDETAIETQEFDENDCLSSKADINTSLAPQKRSFIDNELMSMLVTKKKIKKDKDVSDTGISSTSYLINSGTYANSHIEIPTSNSVYNGKEDCSFNNYSVKHSILEEDIENKCIAVNENKVIENQKVIQSLCKNSHLDLIEQSYFGECDFIINHSTCVYKIQASRFMQLRNNGSLHYDKAVNDLLTEFQRVIIIVEFSEIIQDVDPDLFWKIKLYLLNSRVDVFFIHETTDFFIDWMKYFIARWAFSYNDEKEKNIANADILLDLGFNILLVRKIFQTYSLEEFFMAIIKEESKAVKMLTVSQMTRLKKLLTLEW', 704, 'P53061; D6VV86;', 'KD00882', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'ZIP2', '#Protein ZIP2#Zipping up meiotic chromosomes protein 2', '-', '-', '852643'),
(883, 'O15392', 'Baculoviral IAP repeat-containing protein 5', 'GO:0000777===GO:0032133===c;k;m;s', 16389, '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. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform. {ECO:0000269|PubMed:10626797; ECO:0000269|PubMed:12773388; ECO:0000269|PubMed:16291752; ECO:0000269|PubMed:16322459; ECO:0000269|PubMed:18591255; ECO:0000269|PubMed:20826784; ECO:0000269|PubMed:21536684; ECO:0000269|PubMed:9859993}.', 'MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD', 142, 'O15392; A2SUH6; B2R4R1; Q2I3N8; Q4VGX0; Q53F61; Q5MGC6; Q6FHL2;Q75SP2; Q9P2W8;', 'KD00883', 'Homo sapiens (Human)', 'BIRC5', '#Baculoviral IAP repeat-containing protein 5#Apoptosis inhibitor 4#Apoptosis inhibitor survivin', '-', 'ENSG00000089685', '-'),
(884, 'P02829', 'ATP-dependent molecular chaperone HSP82', 'k', 81406, 'Molecular chaperone that promotes the maturation; structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes; resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other; stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally; ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins; thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition; ATPase cycle and chaperone function. Required for growth at high temperatures. {ECO:0000269|PubMed:17114002}.', 'MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEVD', 709, 'P02829; D6W3D1;', 'KD00884', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'HSP82', '#ATP-dependent molecular chaperone HSP82#82 kDa heat shock protein#Heat shock protein Hsp90 heat-inducible isoform', '-', '-', '855836'),
(885, 'P34223', 'UBX domain-containing protein 1', 'GO:0031134', 46987, 'Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway. Direct or indirect positive regulator of GLC7 activity. {ECO:0000269|PubMed:15258615}.', 'MAEIPDETIQQFMALTNVSHNIAVQYLSEFGDLNEALNSYYASQTDDQKDRREEAHWNRQQEKALKQEAFSTNSSNKAINTEHVGGLCPKPGSSQGSNEYLKRKGSTSPEPTKGSSRSGSGNNSRFMSFSDMVRGQADDDDEDQPRNTFAGGETSGLEVTDPSDPNSLLKDLLEKARRGGQMGAENGFRDDEDHEMGANRFTGRGFRLGSTIDAADEVVEDNTSQSQRRPEKVTREITFWKEGFQVADGPLYRYDDPANSFYLSELNQGRAPLKLLDVQFGQEVEVNVYKKLDESYKAPTRKLGGFSGQGQRLGSPIPGESSPAEVPKNETPAAQEQPMPDNEPKQGDTSIQIRYANGKREVLHCNSTDTVKFLYEHVTSNANTDPSRNFTLNYAFPIKPISNDETTLKDADLLNSVVVQRWA', 423, 'P34223; D6VPU2; E9P8S9;', 'KD00885', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SHP1', '#UBX domain-containing protein 1#Suppressor of high-copy PP1 protein', '-', '-', '852222'),
(886, 'Q4QQS8', 'Nuclear pore complex protein Nup85', 'GO:0000777', 74881, '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 (By similarity). {ECO:0000250}.', 'MEELDCEPAVTWIPGVNSKKKQMCFDWGPGEMLLCETSFNKTDKSEKVPSCPFIYIIRKDVDVYSQILRKLFNESHGIFVGLQRLEEELSGKSRKAQLVRVSKNYRSVIRACMEEMHQVAIAAKDPASGRQFSSQVSILSAMELIWNLCEILFIEVAPAGPLLLHLLDWVRLHVCEVDSLSADVLGSDHPSKHESFWNLVTVLVLQGRLDEARQMLSKEADASPSSAGMCRVLGDLMRTMPILSPGNTQTLTELELKWQHWREECERHLQDNTFAANPHLESLCKIMLGDEATLLEQKELMSNWYHFLVTRLLYSNPTVKPTDLHLYAQSSLDMFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCRLLQSHNLYFGSNMREFLLLEYASGLFAHHSLWQLGVDYFDYCPELGRVSLELHIERIPLNTEQKALKVLRICEQRQMTEQVGSICKILAMKAVRNNRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRLYGEKRFGDAASLLLSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELMRCLEDLASRRPECGEPDAQRLQDDDIETTKVEMLRLALARNLARAIIREGSLEGS', 656, 'Q4QQS8;', 'KD00886', 'Rattus norvegicus (Rat)', 'Nup85', '#Nuclear pore complex protein Nup85#85 kDa nucleoporin#Nucleoporin Nup85#Pericentrin-1', '-', '-', '287830'),
(887, 'Q90640', 'Chromosome-associated kinesin KIF4', 'GO:0003777', 138924, 'Required for mitotic chromosomal positioning and bipolar spindle stabilization. {ECO:0000269|PubMed:7876303}.', 'MVREEEKGIPVRVVRCRPLVPKETSEGCQMCLSFVPGEPQVIVGSDKAFTYDYVFDPSVEQEEVFNTAVAPLIRGIFKGYNATVLAYGQTGSGKTYSMGGTYTASQEHDPSMGVIPRVIKLLFKEKEQRQDWEFVLKVSYLEIYNEDILDLLCSSRERSSQISIREDPKEGIKIVGLTERNVASARDTVSCLEQGNNCRTVASTAMNSQSSRSHAIFTICIDQKKKNDKNSSFHSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGEENKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVNVDPQAAELNHLKQQVQQLQVLLLQAHGGTLPVSINSMAPSENLQSLMEKNQSLMEENEKLSRGLSEAAGQTAQMLERIIVTEQENEKMNAKLEQLQQHAVCKLDLQKLLETVEDEELKENVEVIRNLQQVLAQFQSESAAAAEAATEMANAEQDAAGEAETGQVTKRSSDDFTTQHALRQAQMSKELVELNKALALKEALAKKMIQNDSQLEPIQSQYQTNIKDLELEVSNLQKEKEELILALSMAKKDVNQAKLSERRRKRLQELEGQINELKKKLNEQAKLLKLKESTERTVSKLNQEIREMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERDFQKQASVLRRKTEEAAAANKRLKDALQKQREAADKRKESQNRGMEGVAARVKSWLANEVEVLVSTEEARRHLADLLEDRKILAQELLQLKEKKESGENPPSKLRRRTYSITDLQASEMDLSLSKQIESLETEMELRSAQIADLQQKLLDADNGDRVKQRWDNIATILEAKCALKYLLGELVSSKVQESKLESSLQQSKTNCSDIQKMLIEERNHATEMEAEFQNQLLLQEQQHQQEVLYLLSQFQQKEAPGKGVEDSLSEQEKQMQERLKFQEKELEKMREICEKNQELLQENDVLKQKMLLVQVASGQKLRRDQQVSPESPDSPFDYIPPKPKTRRQTVAKPRAPTPEMNVEELFSDSEESGEEEDAEWVPVKAAKGTKKSATGCFCKGRCGNRQCGCRKQKVGCTAGCSCDSTKCRNRDPGFQDATVCEDQTKDSEGSFKLEDLRDVTAGETFFQPVYSPPTMKVLKDITDQGVFMKKPSTAASLLVRDEESQENQLPFVKKKKRMLSSNTSFFSGCTPIKEEID', 1225, 'Q90640; Q90608;', 'KD00887', 'Gallus gallus (Chicken)', 'KIF4', '#Chromosome-associated kinesin KIF4#Chromokinesin', '-', '-', '395823'),
(888, 'Q5T280', 'Putative methyltransferase C9orf114', 'GO:0000777===SCL', 42009, 'Required both for chromosome alignment and for association of the centrosomes with the poles of the bipolar spindle during metaphase. {ECO:0000269|PubMed:20813266}.', 'MAERGRKRPCGPGEHGQRIEWRKWKQQKKEEKKKWKDLKLMKKLERQRAQEEQAKRLEEEEAAAEKEDRGRPYTLSVALPGSILDNAQSPELRTYLAGQIARACAIFCVDEIVVFDEEGQDAKTVEGEFTGVGKKGQACVQLARILQYLECPQYLRKAFFPKHQDLQFAGLLNPLDSPHHMRQDEESEFREGIVVDRPTRPGHGSFVNCGMKKEVKIDKNLEPGLRVTVRLNQQQHPDCKTYHGKVVSSQDPRTKAGLYWGYTVRLASCLSAVFAEAPFQDGYDLTIGTSERGSDVASAQLPNFRHALVVFGGLQGLEAGADADPNLEVAEPSVLFDLYVNTCPGQGSRTIRTEEAILISLAALQPGLIQAGARHT', 376, 'Q5T280; Q0D2P6; Q6P469; Q6PGP9; Q6PIJ1; Q6PJV9;', 'KD00888', 'Homo sapiens (Human)', 'C9orf114', '#Putative methyltransferase C9orf114 {ECO:0000305}#2.1.1.- {ECO:0000305}', '-', 'ENSG00000198917', '-'),
(889, 'Q6CTH8', 'DASH complex subunit ASK1', 'GO:0008608===GO:0042729', 24223, '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}.', 'MDAVNIEQIDQEITLNLQSIDSDLSYCFNKITKDIIPYVTRYGQTCEDITNSSSWLKEMFQQSANVQLVTDQAVESAGQVLEPRTSLFPEVENETDEFHTVDQYPALSQTGVSSAGAPTTKTGGSVKQDQFQDQDTDELTQDSAMEKQRKKRKVSLQIHQHFNSSSSSNSSMENDISANSSPIKTIPPETETGTETHNKIQGELAKPGTVIHFNSKRD', 218, 'Q6CTH8;', 'KD00889', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'ASK1', '#DASH complex subunit ASK1#Associated with spindles and kinetochores protein 1#Outer kinetochore protein ASK1', '-', '-', '2892639'),
(890, 'Q9ESN5', 'Centromere protein K', 'GO:0000777', 31686, '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. Acts in coordination with CASC5/KNL1 to recruit the NDC80 complex to the outer kinetochore (By similarity). {ECO:0000250}.', 'MSENKQEVHPDTITDVEAVIDTEEELIKECEEMWKDMEDCQNKLSLIGTETLTNADAQLSLLIMQMKCLTAELGQWKKRKPEIIPLNEDVLLTLGKEEFQKLRCDLEMVLSTIQSKNEKLKEDLEREQQWLDEQQQILDTLNVLNSDVENQVVTLTESRIFNELTTKIRGIKEFKEKLLLTLGAFLDNHFPLPEASTPKKRKNIQDSNAQLITLNEILEMLINRMFDVPHDPYVKIRDSFWPPYIELLLRYGIALRHPEDPSQIRLEAFHQ', 271, 'Q9ESN5; Q3UXA9; Q569Q3; Q8C469;', 'KD00890', 'Mus musculus (Mouse)', 'Cenpk', '#Centromere protein K#CENP-K#SoxLZ/Sox6 leucine zipper-binding protein in testis', '-', '-', '60411'),
(891, 'P11440', 'Cyclin-dependent kinase 1', 'GO:0034501', 34107, 'Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition; and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin; APC; AMPH; APC; BARD1; Bcl- xL/BCL2L1; BRCA2; CALD1; CASP8; CDC7; CDC20; CDC25A; CDC25C; CC2D1A; CSNK2 proteins/CKII; FZR1/CDH1; CDK7; CEBPB; CHAMP1; DMD/dystrophin; EEF1 proteins/EF-1; EZH2; KIF11/EG5; EGFR; FANCG; FOS; GFAP; GOLGA2/GM130; GRASP1; UBE2A/hHR6A; HIST1H1 proteins/histone H1; HMGA1; HIVEP3/KRC; LMNA; LMNB; LMNC; LBR; LATS1; MAP1B; MAP4; MARCKS; MCM2; MCM4; MKLP1; MYB; NEFH; NFIC; NPC/nuclear pore complex; PITPNM1/NIR2; NPM1; NCL; NUCKS1; NPM1/numatrin; ORC1; PRKAR2A; EEF1E1/p18; EIF3F/p47; p53/TP53; NONO/p54NRB; PAPOLA; PLEC/plectin; RB1; UL40/R2; RAB4A; RAP1GAP; RCC1; RPS6KB1/S6K1; KHDRBS1/SAM68; ESPL1; SKI; BIRC5/survivin; STIP1; TEX14; beta-tubulins; MAPT/TAU; NEDD1; VIM/vimentin; TK1; FOXO1; RUNX1/AML1; SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis; CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation; Golgi dynamics; nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate; CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation; chromosome decondensation; reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C- mediated dephosphorylation and restoring cell cycle progression. In proliferating cells; CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity; leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome; an important step for spindle formation. In addition; CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl- xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast; CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines; as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. {ECO:0000269|PubMed:16007079; ECO:0000269|PubMed:17700700; ECO:0000269|PubMed:17942597; ECO:0000269|PubMed:22405274}.', 'MEDYIKIEKIGEGTYGVVYKGRHRVTGQIVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQFMDSSLVKSYLHQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLVYDPAKRISGKMALKHPYFDDLDNQIKKM', 297, 'P11440; P70337; Q3TI12;', 'KD00891', 'Mus musculus (Mouse)', 'Cdk1', '#Cyclin-dependent kinase 1#CDK1#2.7.11.22#2.7.11.23#Cell division control protein 2 homolog#Cell division protein kinase 1#p34 protein kinase', '-', '-', '12534'),
(892, 'Q63170', 'Dynein heavy chain 7; axonemal', 'GO:0003777', 464557, '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}.', 'MSSEQVRAGSPGSRVPGARRTGAVWTAPSENLDSSTIPALCVSLLFPSQPLDVVVTMGHNTLGMRQLWKLALQRPQLLSGSTGVKPQWQQTAPSFHLNVKQENPIEPYNVKNEQSYAEYMEHFGKKGKLLDQIDDTRSAPSTSRSKVKSPHKERENFRSTLVNVIMQQDSSLEPDVTDESGIPKATTSAIEKDILRYYYYIHHGIDTDNVAPMEDSWLEHVLQLVPQHLKVLTNSITVLSDEMREDYLLSVKKSIVDFVLKDPREKEDDTKITELPPHRAEMEVLPKPWRRSFLSACSYIRDHLNAMNPTMLAVLDLWHSTFKKLRLVDIEEFHNRQDALELSGFQNIVIKHMESAKETLLKTWFPEVQNIYYQGNKKKQLPTGDSSAKLESFFNCAATLMTLQLQDLILVSMQDFTDLIAQPPESIRAFEHPGFIMRLVLDKKAVKFEPEFTDYIDILVNVYEIMIKAVSFVPRVETKLYSKWESKSKPTTLKPIILDEIIDAHKEKIREVVLRESVAPTEHLKMYDKYQFLITRQAEQDIEEFLTQSQNYERLIEEIRKYQKLGEEIQYTSRKTVRLGMFEMHCEELIRSLVKRADIICGKLIAKMFRDHQEVNTMLCEEFEKIAEKALSTPPNTAELMEMKAHIQKVETTDMLDLGQRLVDSKNCLAFLIECVNFSPADIRLNNSVFQWYGRMGEIFDEHRKIIKDKTEQYQEGLKLRCERFVEELESYAKQAEEFYTFGDLQDVQRYLKKAQVLNSKLDAAADKIEQFNAEEEAFGWIPSVYPQRKKIQDGLNPYLRLYETAVEFSTKHRAWTEGPYHKVNPDQVEADVGNYWRGLYKLEKAFHDSPNALAMTKKVRARVEDFKQYIPLVQVICNPGLRPRHWEAMSAIVGYPLQPSDDSTVFSFIDMNLEPFLDRFEGISEAASKEYSLEKSMDKMMTEWEAMEFVIHPYRESGTFILSAVDDIQMLLDDHIIKTQTMRGSPFIKPYEKQMREWEGKLLLLQEILDEWLKVQATWLYLEPIFSSPDIMSQMPEEGRRFTAVDKTWRDVMKMVVQNKHVLAVVTIERMLERMKKSNELLELILKGLNEYLEKKRLFFPRFFFLSNDELLEILSETKDPTRVQPHLKKCFEGIARVEFTETLDITHMKSSEGEVVELVDTISTTKARGQVEKWLVELERIMIKSIHKVIGDAITAYTKNARINWVRDWPGQTVLCVSQTFWTVEVQVAIPMGHKALEDYLGKCNHQIDDIVTLVRGKLSKQNRVTLGALVVLDVHARDVLANLVKKRISDDTDFEWLSQLRYYWHENNLETKMINAGLRYGYEYLGNSPRMVLAPFCDYCFLTLFGALHLHLGGAPEGPAGTGKTETTKDLAKAVAKQCVVFNCSDGLDYLALGKFFKGLLSCGAWACFDEFNRIDLEVLSVVAQQILTIQIGINSGTELLVFEGTELKLDPTCAVFITMNPGYAGRSELPDNLKALFRTVAMMVPDYAMIAEIVLYSCGFVTARPLSIKIVATYRLCSEQLSSQHHYDYGMRAVKSVLTAAGNLKLKYPNENEEILLLRSIIDVNLPKFLSHDLPLFEGITSDLFPGVKLPKPDYNDLLAAIRENCHSMNLQMTNFFSEKILQIYEMMIVRHGFMIVGEPFGGKTSAYRVLAGALGDICEKGLMEENKVQITVLNPKSVTMGQLYGQFDLVSHEWSDGILAVSFRAFAASSTPDRKWLIFDGPVDAVWIENMNTVLDDNKKLCLMSGEIIQMSPQMNLIFEPMDLEVASPATVSRCGMIYMEPQMLGWRPLMVSWINTLPQSVSIIQKEFIEGLFDRMVPLSVEFIRRHTKELSPTSDTNLVRSLMNLIDCFMDDFADENKQKERNDRENFSLLEGIFLFSLIWSVGASCTADDRIKYNKILRELMEGPISDLTRNKFKLLSGTEQTSSKALTVPFPEKGTIYDYQFIPEGLGRWDQWIKKLADTPPIPKDVQFNEIIVPTLDTVRYSALMSLLTTHQKPSIFVGPTGTGKSVYIINFLLNQLNKDIYKPLIVNFSAQTTAAQTQNIIMSKLDKRRKGVFGPPLGKRMIVFVDDVNMPAREVYGAQPPIELLRQWLDHWNWYDLKDCSMIKLVDIQIMCAMGPPGGGRNPITPRYMRHFNIITINEFSDKSMFTIFSRILTWHLRTCYKFPDDFLDLTTQIVNGTMTLYKDAMKNLLPTPAKSHYLFNLRDFSRVIQGVCLSRPETAENKEAIKRLWVHEVLRVYYDRLLDNADRSWLVNYIQEILRNYMQEDFHDLFKNLDFDNDGIVEEDDLRSLMFCDFHDPKREDFGYREIPNVDALRVIVEGHLDEYNNMSKKPMNLVLFRFAIEHISRISRILKQPRSHALLVGVGGSGRQSVTRLAAHMADYSLFQVEISKGYGSHEWHEDLKVILRKCAEGDMQGVFLFTDTQIKRESFLEDVNNLLNAGEVPNLFALDEKQEICEKMRQLDRQRDKTKQTDGSPIALFNMFIDRCRNQLHVVLAMSPIGDAFRIRLRKFPALVNCCTIDWFQSWPEDALEAVASRFLEDIEMSEEIREGCIDMCKSFHTSTINLSTTFHNELQRYNYVTPTSYLELISTFKLLLEKKRNEVMKMKRRYEVGLDKLDSASSQVATMQGELEALHPQLKVASRQVDDMMIMIEKESIEVAKTEKIVKADETVANDQAMAAKAIKDECDADLAEALPILESALAALDTLTAQDITVVKSMKSPPAGVKLVMEAICILKGIKADKIPDPTGSGKKIEDFWGPAKRLLGDIRFLQSLHEYDKDNIPPAYMNIIRKSYIPNPDFVPEKIRNASTAAEGLCKWVIAMDSYDKVAKIVAPKKIKLAAAEGELRIAMEGLRKKQAALREVQDKLAKLQDTLELNKQKKADLENQVDLCSKKLERAEQLIGGLGGEKTRWSNSALELGHLYVNLTGDILISSGVVAYLGAFTSNYRQHQTKEWSHSCKERDIPCSDDYSLMGTLGEAVTIRAWNIAGLPSDLFSIDNGIIIMNARRWPLMIDPQGQANKWIKNMEKTNSLQLIKLSDPDYVRTLENCIQFGTPVLLENVGEELDPILEPLLLKQTFKQGGSTCIRLGDSTIEYAPDFRFYITTKLRNPHYLPETSVKVTLLNFMITPEGMQDQLLGIVVARERPDLEEEKQALILQGAENKRQLKEIEDKILEVLSSSEGNILEDETAIKILSSSKALANEISQKQEVAEETEKKIDNTRMGYRPIAVHSSILFFSIADLANIEPMYQYSLTWFINLFILSIENSEKSDILSQRLHILRDHFTYSLYVNICRSLFEKDKMLFSFCLTVNLLIHENAINKAEWRFLLTGGIGLDNPYTNPCTWLPQKSWDEICRLDELHAFKTIRREFMRLKEGWKKVYDSMEPHHEIFPEEWENKANDFQRMLIIRCLRPDKVIPMLQEFIIKKLGRSFIEPPPFDLAKAFGDSNCCAPLIFVLSPGADPMNALLKFADDQGYGGSKLSSLSLGQGQGPIAMKMLEKAVKDGTWVVLQNCHLATSWMPTLEKVCEELSPESTHPDFRIWLTSYPSPNFPVSVLQNGVKMTNEAPKGLRANIIRSYLMDPISDPEFFGSCRKPEEFKKLLYGLCFFHALVQERRKFGPLGWNIPYEFNETDLRISVQQLHMFLNQYEELPYDALRYMTGECNYGGRVTDDWDRRTLRSILNKFFCTELVENPQYKFDSSGIYFVPPSGDHKSYIEYTKTLPLIPDPEIFGMNANADITKDQSETQLLFDNILLTQSRSSGSGAKSSDEVVNEVAGDILGKLPNNFDIESAMRRYPTTYTQSMNTVLVQEMGRFNKLLITIRESCINIQKAIKGLVVMSTELEEVVSSILNVKIPGMWMGKSYPSLKPLGSYVNDFLARLKFLQQWYEVGPPPVFWLSGFFFTQAFLTGAQQNYARKFTIPIDLLGFDYEVMDDKEYKNAPEDGVYIHGLFLDGASWNRKTKKLAESHPKVLYDTVPVMWLKPCKKSDIPKRPSYVAPLYKTSERRGTLSTTGHSTNFVIAMILPSDQPKEHWIGRGVALLCQLNS', 4057, 'Q63170; Q62821;', 'KD00892', 'Rattus norvegicus (Rat)', 'Dnah7', '#Dynein heavy chain 7; axonemal#Axonemal beta dynein heavy chain 7#Axonemal dynein heavy chain b#Ciliary dynein heavy chain 7#Dynein-like protein 7', '-', '-', '-'),
(893, 'P49810', 'Presenilin-2', 'GO:0000776===c;k', 50140, 'Probable catalytic subunit of the gamma-secretase complex; an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. {ECO:0000269|PubMed:10497236; ECO:0000269|PubMed:10652302}.', 'MLTFMASDSEEEVCDERTSLMSAESPTPRSCQEGRQGPEDGENTAQWRSQENEEDGEEDPDRYVCSGVPGRPPGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLLLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEVFEPPLTGYPGEELEEEEERGVKLGLGDFIFYSVLVGKAAATGSGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI', 448, 'P49810; A8K8D4; B1AP21; Q96P32;', 'KD00893', 'Homo sapiens (Human)', 'PSEN2', '#Presenilin-2#PS-2#3.4.23.-#AD3LP#AD5#E5-1#STM-2#Presenilin-2 NTF subunit#Presenilin-2 CTF subunit', '-', 'ENSG00000143801', '-'),
(894, 'Q5R559', 'Dynactin subunit 5', 'GO:0000777', 20169, '', 'MELGELLYNKSEYIETASGNKVSRQSVLCGSQNIVLNGKTIVMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQKFLPLTRI', 182, 'Q5R559;', 'KD00894', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'DCTN5', '#Dynactin subunit 5#Dynactin subunit p25', '-', '-', '100173847'),
(895, 'P51532', 'Transcription activator BRG1', 'k', 184646, 'Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Component of the CREST-BRG1 complex; a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons; transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx; RB1 is dephosphorylated by calcineurin; which leads to release of the repressor complex. At the same time; there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism; which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter; and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons; npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A; are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self- renewal/proliferation by enhancing Notch-dependent proliferative signals; while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. {ECO:0000250; ECO:0000269|PubMed:19571879; ECO:0000269|PubMed:20418909}.', 'MSTPDPPLGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSMMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED', 1647, 'P51532; B1A8Z4; B1A8Z5; B1A8Z6; B1A8Z7; E9PBR8; O95052; Q9HBD3;', 'KD00895', 'Homo sapiens (Human)', 'SMARCA4', '#Transcription activator BRG1#3.6.4.-#ATP-dependent helicase SMARCA4#BRG1-associated factor 190A#BAF190A#Mitotic growth and transcription activator#Protein BRG-1#Protein brahma homolog 1#SNF2-beta#SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4', '-', 'ENSG00000127616', '-'),
(896, 'Q4R7H3', 'Protein Spindly', 'GO:0043515===GO:0034501===GO:0000940', 70138, 'Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. {ECO:0000255|HAMAP-Rule:MF_03041}.', 'METDIVINLRCKLKEAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKSKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRNLEKFKNLYESMESKPSVDSGALEDNTYYTDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENMKLRAKLDELKLKYEPEETVEVPVLKKRREVLPVDITTSKDTCVNNSAVGGEVYRLPPQKEETQCCPNSLEDNNLQLEKSVSIHTPIVSLSPHKNLPVDMQLKKEKKCVKLVGVPADAEALSERSGNTLNSPRLAAESKLQTEVKEGKETASKLEKETCKKSHPILYVSSKSTPETQCPQQ', 605, 'Q4R7H3;', 'KD00896', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'SPDL1', '#Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041}#Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041}#Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041}', '-', '-', '101926343'),
(897, 'P12270', 'Nucleoprotein TPR', 'GO:0000776===GO:0005868', 267293, '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. According to some authors; plays a limited role in the regulation of nuclear protein export (PubMed:22253824 and PubMed:11952838). 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. {ECO:0000269|PubMed:11952838; ECO:0000269|PubMed:15654337; ECO:0000269|PubMed:17897941; ECO:0000269|PubMed:18794356; ECO:0000269|PubMed:18981471; ECO:0000269|PubMed:19273613; ECO:0000269|PubMed:20133940; ECO:0000269|PubMed:20407419; ECO:0000269|PubMed:21613532; ECO:0000269|PubMed:22253824; ECO:0000269|PubMed:9864356}.', 'MAAVLQQVLERTELNKLPKSVQNKLEKFLADQQSEIDGLKGRHEKFKVESEQQYFEIEKRLSHSQERLVNETRECQSLRLELEKLNNQLKALTEKNKELEIAQDRNIAIQSQFTRTKEELEAEKRDLIRTNERLSQELEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVSVKYREKRLEQEKELLHSQNTWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVSRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVEELHKLLKEAGEANKAIQDHLLEVEQSKDQMEKEMLEKIGRLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKLENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSVKLEQAMKEIQRLQEDTDKANKQSSVLERDNRRMEIQVKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLVALRELGETREREEQETTSSKITELQLKLESALTELEQLRKSRQHQMQLVDSIVRQRDMYRILLSQTTGVAIPLHASSLDDVSLASTPKRPSTSQTVSTPAPVPVIESTEAIEAKAALKQLQEIFENYKKEKAENEKIQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLHERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLSSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTETNLHLNTKELLKNAQKEIATLKQHLSNMEVQVASQSSQRTGKGQPSNKEDVDDLVSQLRQTEEQVNDLKERLKTSTSNVEQYQAMVTSLEESLNKEKQVTEEVRKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRRAIESMEQQLSELKKTLSSVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMASVRQHLEETTQKAESQLLECKASWEERERMLKDEVSKCVCRCEDLEKQNRLLHDQIEKLSDKVVASVKEGVQGPLNVSLSEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNAEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQDLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQHLVSQQKDPDTEEYRKLLSEKEVHTKRIQQLTEEIGRLKAEIARSNASLTNNQNLIQSLKEDLNKVRTEKETIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQYEELKAQQDKVMETSAQSSGDHQEQHVSVQEMQELKETLNQAETKSKSLESQVENLQKTLSEKETEARNLQEQTVQLQSELSRLRQDLQDRTTQEEQLRQQITEKEEKTRKAIVAAKSKIAHLAGVKDQLTKENEELKQRNGALDQQKDELDVRITALKSQYEGRISRLERELREHQERHLEQRDEPQEPSNKVPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGSTSGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPANQELSSNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTIEASDQVSDDTVEMPLPKKLKSVTPVGTEEEVMAEESTDGEVETQVYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTTSSQDGQGKGDDVIVIDSDDEEEDDDENDGEHEDYEEDEEDDDDDEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGGEGNHRAADSQNSGEGNTGAAESSFSQEVSREQQPSSASERQAPRAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETATGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGVSHAMGGRGGINRGNIN', 2363, 'P12270; Q15624; Q15655; Q5SWY0; Q99968;', 'KD00897', 'Homo sapiens (Human)', 'TPR', '#Nucleoprotein TPR#Megator#NPC-associated intranuclear protein#Translocated promoter region protein', '-', 'ENSG00000047410', '-'),
(898, 'Q63164', 'Dynein heavy chain 1; axonemal', 'GO:0003777', 515021, '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}.', 'MVTLSISDTLHTPAFVENRHLAITGMPTRKANNGFPSPDDNNVWGQFWKDLQTPLLVVVYVHGAQCQLLLPIENRRVSSGSDKSLKNGMEECDKEEASTSSQGPGYCPANVPENHDLEKMLKESSRNPEKTSPNPELKTPPLPLSDLGQPRKSPLAGTDKKYPIMKQRGFYSDILSPGTLDQLGDVCCGPYLSQNLIRQADLDKFTPKGQCHEHWAAESFVIPEDFQERVEQQSIGTTTRLLTQTDFPLQSYEPKVQVPFQVLPGRCPRKIEIERRKQQYLRLDIEQLLANEGIDSNKLMPRHPDLQQPQTIEQGRDPLFPIYLPLKVFDNEEFDCRTPTEWLNMGLEPDAQYRKPVPGKALLPTDDALGHVHRAGCKQVSFSKCINTGISLPEAGKKQSVSFTLDSNDRNNLTKLSPVLQCLAIKPWEQGHVKCTEFQLPRFTGALALSRNTRAKRGSQEASTRDHLDFEDPKSQELDYRWCEVGVLDYDEEKKLYLVQKTDKRGLVRDEMGMPIVNGGVTPEGRPPLLDTQYWVPRIQLLFCAEDPRVFTQRVVQANALRKNTEALLLYNLYVDCMPTEGQRVINEQSLSKIKQWALSTPRMRKGPSVLEHLSSLAREVNLDYERSMNKINFDQIVSSKPETFSFVTLPEKEEEKVPNQGLVSVPEYPFREQKEDFTFVSLLTRSEVITALSKVRAECNKVTSMSLFHSNLSKYSRLEEFEQIQSQTFSQVQMFLKDSWISTLKVAMRSSLRDMSKGWYNLYETNWEVYLMSKLRKLMELIKYMLQDTLRFLVQDSLGSFAQFIGDACCSVLECIDDMDWGEDLINSPYKPRKNPLFIVDLVLDNTGVHYSTPLEQFEVILLNLFDKGILATHAVPQLEKLVMEDIFISGDPLLESVGLHEPLVEELRANITNAMHKAMIPLQAYAKEYRKTYQTQCPSAEEVREVVITHLKEKEILDNSLPSSIIIGPFYINVDNVKQSLSKKRKALATSMLDILAKNLHNEVDSICEEFRSISRKIYEKPNSIEELAELRDWMKGIPEKLVILEVRQALALAARSLVEPEVGPALEIPFNNPLPSMTRHFLLMQERIVKVMSDYEVMDEFFYNLTTDDFNDKWAANNWPTKILGQIDMVRQQHVEDEEKFRKIQLMDQNNFQEKLEGLQLVVAGFSTHVEIARAHEIANEVRRVKKQLKDCQQLAMLYNNRERIFGLPITNYDKLSRMVKEFQPYLDLWTTASDWLRWSESWMNDPLSAIDAEQLEKNVIESFKTMHKCVKQFKDIPACQDVALDIRARIDEFKPYIPLIQGLRNPGMRNRHWEVLSNEININVRPKANLTFARCLEMNLQDYIESISKVAEVAGKEYAIEQALDKMEKEWASILFNVLPYKETDTYILKSPDEASQLLDDHIVMTQSMSFSPYKKPFEQRINSWETKLKLTQEVLEEWLNCQRSWLYLEPIFSSEDITRQLPVESKRYQTMERIWRKIMKNAYENREVINVCSDQRLLDSLRDCNKLLDLVQKGLSEYLETKRTAFPRFYFLSDDELLEILSQTKDPTAVQPHLRKCFENIARLLFQEDLEITHMYSAEGEEVKLSFSIYPSSNVEDWLLEVERSMKASVHDIIEMAIKAYPTMLRTEWVLSWPGQVTIAGCQTYWTLEVAQALEASSISSSLFPQLSKQLSDLVALVRGKLSRMQRMVLSALIVIEVHAKDVVSKLIDENVVSVHDFEWISQLRYYWTNNDLYIRAVNAEFIYGYEYLGNSGRLVITPLTDRCYLTLTGALHLKFGGAPAGPAGTGKTETTKDLGKALAIQTVVFNCSDQLDFMAMGKFFKGLASAGAWACFDEFNRIDIEVLSVVAQQITTIQKAQQQRSREYIKSLGGAVMCLPFLCVLYVQALFRPVAMMVPDYAMIAEISLYSFGFNEANVLAKKITTTFKLSSEQLSSQDHYDFGMRAVKTVISAAGNLKRENPTMNEELICLRAIRDVNVPKFLQEDLKLFSGIVSDLFPTTKEEETDYGILDQAIRKACEKNNLKDVEGFLIKCIQLYETTVVRHGLMLVGPTGSGKSNCYRILAAAMTSLKGKPSISGGVYEAVNYYVLNPKSITMGQLYGEFDLLTHEWTDGIFPSLIRAGAIASDTNKKWYMFDGPVDAVWIENMNTVLDDNKKLCLSSGEIIKLTEAMTMMFEVQDLAVASPATVSRCGMVYLEPSILGLMPFVECWLKHLPSIIKPYEEQFKTLFVKFLESSIAFVRTTVKEVVASTNSNLTMSLLKLLDCFFKPFLPREGLKKIPSEKLSHIPELIEPWFIFSLVWSVGATGDHSSRLNFSQWLKIKMVFEQIKLAFPEEGLVYDYRLDDAGISSTEDDDEDDEESKQVATALPAQEGGMVKPPGLWDLPPRDSGHLEKATLTASRSEAVAWVKWMDYSVPFTMMPDTNYCNIIVPTMDTMQMSYLLGMLITNHKPVLCIGPTGTGKTLTVSNKLLKNLPLEYISHFLTFSARTSANQTQDLIDSKLDKRRKGVFGPPLGRNFIFFIDDLNMPALETYGAQPPIELLRQWMDHGGWYDRKIIGAFKNLVDINFVCAMGPPGGGRNAITPRLTRHFNYLSFIEMDEVSKKRIFSIILGCWMDGLLGEKSYREPVPGAPNIVHMTEPLVNATISIYAIITSQLLPTPAKSHYTFNLRDLSKVFQGILMAEPAKVEDKVQLLRLWYHENCRVFRDRLVNEEDRGWFDGLLEMKMEDLGVAFNKVCPFQPILYGDFMSPGSDVKSYELITSENKMMQVIEEYMEDYNQINTAKLKLVLFVDAMSHICRISRTLRQALGNALLLGVGGSGRSSLTRLASHMAEYECFQVELSKNYGMSEWREDVKKILLKAGMQNLPITFLFSDTQIKNESFLEDINNILNSGDIPNLYSADEQDQIVNTMRPYIQEQGLQPTKANLMAAYTGRVRNNIHMVLCMSPIGEVFRARLRQFPSLVNCCTIDWFNEWPAEALQSVATRFLHEIPELECSSEVIEGLIHVCVYIHQSVAKKCVEYLAELARHNYVTPKSYLELLNIFSILIGQKKMELKTAKHRMKSGLDKLLRTSEDVAKMQEELEIMRPLLEEAAKDTLLTMDQIKVDTAIAEETRKSVQAEEIKANEKASKAQAIADDAQKDLDEALPALDAALASLRNLNKNDVTEVRAMQRPPPGVKLVIEAVCIMKGIKPKKVPGEKPGSKVDDYWEPGKGLLQDPGRFLESLFKFDKDNIGEAVIKAIQPYIDNEEFQPAAIAKVSKACTSICQWVRAMHKYHFVAKAVEPKRQALREAQDDLEVTQRILEEAKHHLREVEDGISTLQAKYRECVTKKEELEMKCEQCEQRLGRADKSQSPGQPPGAHPTRLLLQLINGLADEKVRWQDTVENLENMLDNIFGDVLVAAGFVAYLGPFTGQYRAALYEYWVNQLTVYGVPHTSKPTLISTLGNPVKIRSWQIAGLPNDTLSVENGVINQFSQRWTHFIDPQGQANKWIKNMEKESGLDVFKLSDRDFLRSMENAIRFGKPCLLENVGEELDPALEPVLLKQTYKQQGNTVLKLGDTVIPYHEDFRMYITTKLPNPHYSPEVSTKLTLINFTLSPSGLEDQLLGQVVAEERPDLEEAKNQLIISNAKMRQELKDIEDQILYRLSSSEGNPVDDVELIKVLEASKMKAAEIQAKVRIAEQTEKDIDLTRMEYIPVAVRTQILFFCVSDLANVDPMYQYSLEWFLNIFLSGIANSERADNLKKRIVNINRYLTFSLYSNVCRSLFEKHKLMFAFLLCVRIMMNEGKINQGEWRYLLSGGSIQTMSENPAPHWLSDRAWRDILALSNLPAFSTFSTDFVQHLPKFQAIFDSAEPHREPLPGIWNTYLDEFQKLLILRCLRGDKVTNAMQDFVANHLEPRFIEPQTANLSAVFKESNSTTPLIFVLSPGTDPAADLYKFAEEMKFSKKLSAISLGQGQGPRAEAMMRNSIERGKWVFFQNCHLAPSWMPALERLIEHINPDKVHRDFRLWLTSLPSNKFPVSILQNGSKMTIEPPRGVKANLLKSYNSLSDDFLHSCQKVVEFKSLLLSLCLFHGNALERRKFGPLGFNIPYEFTDGDLRICISQLKMFLDEYEDIPYKVLKYTAGEINYGGRVTDDWDRRCVMNILEDFYNPAVLSPEHRYSKSGIYHQIPPTYDLNGYLSYIKSLPLNDMPEIFGLHDNANITFAQNETFALFGAILQLQPKSSSMGGQSREELVEDVAEDILVQVPKPVDLEEVVNKYPVLYEESMNTVLVQEVIRYNKLLMVITQTLSDMLKAIKGLVVMSLELELMSTSLYNNAVPELWKSKAYPSLKPLASWIMDLLQRLNFLHSWIKNGIPSVFWISGFFFPQAFLTGTLQNFARKFVISIDTITFDFKVLSYASSEIAERPSTGCYIYGLFLEGARWDPFDFQLAESRPKELYTEMAVIWLLPVANRKVQNQDFYLCPIYKTLTRAGTLSTTGHSTNYVIAVEIPSNQPQRHWIKRGVALICALDY', 4516, 'Q63164;', 'KD00898', 'Rattus norvegicus (Rat)', 'Dnah1', '#Dynein heavy chain 1; axonemal#Axonemal beta dynein heavy chain 1#Ciliary dynein heavy chain 1', '-', '-', '171339');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(899, 'H6X1M8', 'Shugoshin-like protein 2', 'k', 115737, '', 'MALQTSASLATLQTVKDRMREKIHGSLKTVKLNTTLAAKIKTKTLNNSSILKISLKHNNKVLACALTAEREKARRLENDKMFLQKEVKMLHFQNALLRQNLSLLNKMLKDIDIFMNINLPAAIEISNIENSTDLSTLESRKSERFSNHSVFSLDDDQGFRMTGMALRVPSSSIGDRRTIIPADPVVEAPTENSILPNSNSLRERSLHKPIPDNLNVPSKESLGTSNEIKNDIPNIQNMELVPCEEFRVSDVLNSDICGFVTKRKKRSTASHSSTQSIKSDLNQYKYSRQESSNRVHCEQTTDSSIATNANYETPAVSEYDSQTDGYERQAIKRATMSFESPSNPKINSGQSEGSSDFVIEQHGEAIDPLAADPIHSAIVTEHTAEDKNVRQEKTLYDADMELTCSDSATIITVSSVSKTEKKSKSCIPIKQDGSSLRKVKHARREKTHKSKIKEVSSIDNKPFKGKQNETFDLEHNHQDSEHISNNIQQDDDLLSKISKNFALIPQSTVDFRKTYVLTQPIKQEEAEIKCDTEIKGKQVLKHPYEEKRATSTNNCILDQEPSNNMQILHVEHTEVPLPKENEQFKEIKCESAHAFIKPGQVKSSGTTAKISEISKKKHTKTGKIKTKQQEICLEMKKTEINTNADEKVNLKKTVDVSSSFLNMACSQAHIRRETYFVNTSEATGLTSAVEFVPKDVAHYRRGTYVINKPEDMANFQTGASVQPLGSLESPTTMDLFQSNKSNSFDNVHKTKPKNPNLEIALDAPNIKGHKRMLDNVTCKPVIEDNTLYSLSSISPADKRKTHILPAKEDVGHKQGTLVQESLIDLPVTQPCKKTRFFSGILRNDQDSFMLDMVSESILDSVVESNSFFEFPSASNTEDATFTIEKTLNNNPDLELPTFEECNPKWMAQPPGNFSVYNEKQQQNCEEQHSELQCEDQDQSIEEQETAVKPLQDLTNSTLGSLKQSPKFCSGEDDDSRASSRRKRNPVNYKEPSLGTKLRRGDTNTSTEFLHSPVHKEKKRPRKIKVKSEK', 1029, 'H6X1M8;', 'KD00899', 'Xenopus laevis (African clawed frog)', 'sgol2', '#Shugoshin-like protein 2 {ECO:0000313|EMBL:AEZ57108.1}', '-', '-', '100861581'),
(900, 'Q8X225', 'Histone-lysine N-methyltransferase; H3 lysine-9 specific dim-5', 'GO:0051315', 37572, 'Histone methyltransferase that specifically trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA methylation. {ECO:0000269|PubMed:11713521; ECO:0000269|PubMed:12372305; ECO:0000269|PubMed:12679815; ECO:0000269|PubMed:12887903}.', 'MEKAFRPHFFNHGKPDANPKEKKNCHWCQIRSFATHAQLPISIVNREDDAFLNPNFRFIDHSIIGKNVPVADQSFRVGCSCASDEECMYSTCQCLDEMAPDSDEEADPYTRKKRFAYYSQGAKKGLLRDRVLQSQEPIYECHQGCACSKDCPNRVVERGRTVPLQIFRTKDRGWGVKCPVNIKRGQFVDRYLGEIITSEEADRRRAESTIARRKDVYLFALDKFSDPDSLDPLLAGQPLEVDGEYMSGPTRFINHSCDPNMAIFARVGDHADKHIHDLALFAIKDIPKGTELTFDYVNGLTGLESDAHDPSKISEMTKCLCGTAKCRGYLW', 331, 'Q8X225; Q1K5Y7;', 'KD00900', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'dim-5', '#Histone-lysine N-methyltransferase; H3 lysine-9 specific dim-5#2.1.1.43#Histone H3-K9 methyltransferase dim-5#H3-K9-HMTase dim-5#HKMT', '-', '-', '3873656'),
(901, 'Q9P7H1', 'Tyrosine-protein phosphatase CDC14 homolog', 'GO:0034501===GO:0000778===GO:1902425===c;k;m', 60253, 'Protein phosphatase which antagonizes mitotic cyclin- dependent kinase cdc2; the inactivation of which is essential for exit from mitosis. To access its substrates; is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation; where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Dephosphorylates the mitotic inducer cdc25 for its rapid degradation. Down-regulation of cdc25 activity ensures a prompt inactivation of mitotic cdc2 complexes to trigger cell division. Dephosphorylates also cdc2-phosphorylated nsk1; allowing nsk1-binding to kinetochores and spindle. Dephosphorylates ase1; which is essential for spindle midzone assembly and for continuous extension of the anaphase spindle. Tethered to the contractile ring by mid1; where it dephosphorylates cdc15. {ECO:0000269|PubMed:11448769; ECO:0000269|PubMed:11683392; ECO:0000269|PubMed:15128870; ECO:0000269|PubMed:15265986; ECO:0000269|PubMed:15525536; ECO:0000269|PubMed:16085490; ECO:0000269|PubMed:17562791; ECO:0000269|PubMed:18378776; ECO:0000269|PubMed:19570910; ECO:0000269|PubMed:22065639; ECO:0000269|PubMed:22624651}.', 'MDYQDDGLGEMIEFLEDKLYYTSLSQPPKAELYPHMHFFTIDDELIYNPFYHDFGPLNVSHLIRFAVIVHGIMGKHRQAKKSKAIVLYSSTDTRLRANAACLLACYMVLVQNWPPHLALAPLAQAEPPFLGFRDAGYAVSDYYITIQDCVYGLWRARESSILNIRNIDVHDYETYERVENGDFNWISPKFIAFASPIQAGWNHASTRPKKLPQPFAIVLDYFVANKVKLIVRLNGPLYDKKTFENVGIRHKEMYFEDGTVPELSLVKEFIDLTEEVEEDGVIAVHCKAGLGRTGCLIGAYLIYKHCFTANEVIAYMRIMRPGMVVGPQQHWLHINQVHFRAYFYEKAMGRAIQQATAAEPLATPPRHPLNATNGTSQSNISTPLPEPTPGQPRKVSGHNPPSARRLPSASSVKFNEKLKNASKQSIQNENKASYSSYEDSEIQNDDETRTVGTPTETISVVRLRRSSSQSNIEPNGVRSPTSSPTGSPIRRTSGNRWSSGSSHSKKSAQRSVSMSSLNNTSNGRVAKPKPSKSRLIS', 537, 'Q9P7H1;', 'KD00901', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'clp1', '#Tyrosine-protein phosphatase CDC14 homolog#3.1.3.48#CDC fourteen-like phosphatase 1', '-', '-', '2542358'),
(902, 'P09734', 'Tubulin alpha-3 chain', 'GO:0005828', 49694, '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.', 'MREVISINVGQAGCQIGNACWELYSLEHGIKEDGHLEDGLSKPKGGEEGFSTFFHETGYGKFVPRAIYVDLEPNVIDEVRTGRFKELFHPEQLINGKEDAANNYARGHYTVGREIVDEVEERIRKMADQCDGLQGFLFTHSLGGGTGSGLGSLLLENLSYEYGKKSKLEFAVYPAPQLSTSVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDICKRNLGISRPSFSNLNGLIAQVISSVTASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYAPILSKKRATHESNSVSEITNACFEPGNQMVKCDPTKGKYMANCLLYRGDVVTRDVQRAVEQVKNKKTVQMVDWCPTGFKIGICYEPPSVIPSSELANVDRAVCMLSNTTAIADAWKRIDQKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALERDYIEVGADSYAEEF', 445, 'P09734; D6W0G1;', 'KD00902', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'TUB3', '#Tubulin alpha-3 chain', '-', '-', '854915'),
(903, 'P09733', 'Tubulin alpha-1 chain', 'GO:0005828', 49800, '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.', 'MREVISINVGQAGCQIGNACWELYSLEHGIKPDGHLEDGLSKPKGGEEGFSTFFHETGYGKFVPRAIYVDLEPNVIDEVRNGPYKDLFHPEQLISGKEDAANNYARGHYTVGREILGDVLDRIRKLADQCDGLQGFLFTHSLGGGTGSGLGSLLLEELSAEYGKKSKLEFAVYPAPQVSTSVVEPYNTVLTTHTTLEHADCTFMVDNEAIYDMCKRNLDIPRPSFANLNNLIAQVVSSVTASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYSPVLSKSKAFHESNSVSEITNACFEPGNQMVKCDPRDGKYMATCLLYRGDVVTRDVQRAVEQVKNKKTVQLVDWCPTGFKIGICYEPPTATPNSQLATVDRAVCMLSNTTSIAEAWKRIDRKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALERDYIEVGADSYAEEEEF', 447, 'P09733; D6W0J8;', 'KD00903', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'TUB1', '#Tubulin alpha-1 chain', '-', '-', '854889'),
(904, 'Q9D084', 'Centromere protein S', 'GO:0000777', 16335, 'DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Required for optimal chromatin association of the FA core complex. Required for efficient damage-induced monoubiquitination and focus formation of FANCD2. Stabilizes FAAD24; FANCM and APITD1/CENPS in the FA core complex. Plays a role in DNA interstrand cross-linking (ICL) repair and in recovery of replication forks stalled by topoisomerase I-DNA cleavage intermediates induced by camptothecin. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation. Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). {ECO:0000250}.', 'MEEVEAEEPQEFSHRQRLKAAVHYTVGCLCQEVTLNKQVNFSKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKLLARRNNSLLKYITEKNEEIAQLNLKGKAKKKRKPEDESRSSRESMAEELDGAEELQSES', 142, 'Q9D084; A2AH77; Q80ZS2; Q8BH28;', 'KD00904', 'Mus musculus (Mouse)', 'Apitd1', '#Centromere protein S#CENP-S#Apoptosis-inducing TAF9-like domain-containing protein 1 homolog#FANCM-interacting histone fold protein 1', '-', '-', '69928'),
(905, 'Q9Y738', 'Centromere protein mis12', 'GO:0000941===GO:0031617===GO:0000779===k', 30195, 'Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Required for correct segregation of chromosomes and for maintaining the inner centromere structure. {ECO:0000269|PubMed:12773390}.', 'MLVELLEFTPLSFIDDVINITNQLLYKGVNGVDKAFSQTRFAKKAPQEIEEGLHKFEVLFESVVDRYYDGFEVYTLRNIFSYPPELKGYMRTFGKDVDYSITTEQDAAMDQAIQEAAEKLVVKMQLRRDLRMRLSRKREKKTEIEKHLERISFLNKVPENWQVTLPETTDFLLDQLGNLQHAVKRVVEASPTVHSREVDERITYLEKGYERLSNPIDQQKDFWSHHLSKLESTANTETANNIHKLLLSSEKDVGHTDEP', 259, 'Q9Y738;', 'KD00905', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis12', '#Centromere protein mis12#NMS complex subunit mis12', '-', '-', '2540494'),
(906, 'Q62673', 'Serine/threonine-protein kinase PLK1', 'GO:0000776===GO:0000942', 68291, '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}.', 'MNAAAKAGKLARAPADLGKGGVPGDAAPGAPGAAPLAKEIPEVLMDPRSRRQYVRGRFLGKGGFAKCFEISDSDTKEVFPGKIVPKSLLLKPHQKEKMSMEISIHRSLAHQHVVGFHGFFEDSDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNQVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYEGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIHELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGVENPLPDRPREKEEPVVRETNEAIECHLSDLLQQLTSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLNYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGTVQINFFQDHTKLILCPLMAAVTYINEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSACNRLKAS', 603, 'Q62673; F1LNH6; Q5XHX4;', 'KD00906', 'Rattus norvegicus (Rat)', 'Plk1', '#Serine/threonine-protein kinase PLK1#2.7.11.21#Polo-like kinase 1#PLK-1', '-', '-', '25515'),
(907, 'Q9N0X0', 'Aurora kinase B', 'GO:0034501===GO:0032133', 39222, 'Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint; a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C; leading to retain abscission- competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin; CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA; DES/desmin; GPAF; KIF2C; NSUN2; RACGAP1; SEPT1; VIM/vimentin; GSG2/Haspin and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process; whereas histone H3 is phosphorylated at ''Ser-10'' and ''Ser-28'' during mitosis (H3S10ph and H3S28ph; respectively). AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells; inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (By similarity). {ECO:0000250}.', 'MAQKENTYPWPYGRQTAQSGLNILPQRVLRKEAVTPSALVLMSRSNTQPTAAPGQKVVENSSGTPNFSTRSFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLQHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKCRTFDEQRTATIMEELADALIYCHGKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRTHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIGKVDLKFPPSVPAGAQDLISKLLKHNPSDRLPLAQVSAHPWVRAHSRRVLPPSAPQSVP', 344, 'Q9N0X0; Q7YRC7;', 'KD00907', 'Sus scrofa (Pig)', 'AURKB', '#Aurora kinase B#2.7.11.1#Aurora 1#Aurora- and IPL1-like midbody-associated protein 1#AIM-1#Aurora/IPL1-related kinase 2#ARK-2#Aurora-related kinase 2#STK-1#Serine/threonine-protein kinase 12#Serine/threonine-protein kinase 5#Serine/threonine-protein kinase aurora-B', '-', '-', '396955'),
(908, 'Q9D083', 'Kinetochore protein Spc24', 'GO:0000777===GO:0031262', 23416, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (By similarity). {ECO:0000250}.', 'MAAFRDMVEVSNWLLSLLGANRAEAQQRRLLGSYEQMMERLLEMQDGAYRQLRETLAVEEEVAQSLLELKECTRQGDTELQQLEVELQRTSKEDTCVQARLRQLITELQELREMEEELQRQERDVDEDNTVTIPSAVYVAHLYHQISKIQWDYECEPGMIKGIHHGPTVAQPIHLDSAQLSPKFISDYLWSLVDTTWEPEP', 201, 'Q9D083; Q3TIF5; Q8CD13;', 'KD00908', 'Mus musculus (Mouse)', 'Spc24', '#Kinetochore protein Spc24', '-', '-', '67629'),
(909, 'P52304', 'Serine/threonine-protein kinase polo', 'GO:0000776===GO:0005828===GO:0000940===c;k;m', 66974, 'May play a role in regulating both nuclear and cytoplasmic aspects of the mitotic cycle. {ECO:0000269|PubMed:1660828}.', 'MAAKPEDKSTDIPDRLVDINQRKTYKRMRFFGKGGFAKCYEIIDVETDDVFAGKIVSKKLMIKHNQKEKTAQEITIHRSLNHPNIVKFHNYFEDSQNIYIVLELCKKRSMMELHKRRKSITEFECRYYIYQIIQGVKYLHDNRIIHRDLKLGNLFLNDLLHVKIGDFGLATRIEYEGERKKTLCGTPNYIAPEILTKKGHSFEVDIWSIGCVMYTLLVGQPPFETKTLKDTYSKIKKCEYRVPSYLRKPAADMVIAMLQPNPESRPAIGQLLNFEFLKGSKVPMFLPSSCLTMAPRIGSNDTIEDSMHRKPLMEMNGIRPDDTRLESTFLKANLHDAITASAQVCRHSEDYRSDIESLYQQLTNLINGKPRILQGNLGDENTDPAAQPLFWISKWVDYSDKYGFGYQLCDEGIGVMFNDTTKLILLPNQINVHFIDKDGKETYMTTTDYCKSLDKKMKLLSYFKRYMIEHLVKAGANNVNIESDQISRMPHLHSWFRTTCAVVMHLTNGSVQLNFSDHMKLILCPRMSAITYMDQEKNFRTYRFSTIVENGVSKDLYQKIRYAQEKLRKMLEKMFT', 576, 'P52304; A4V258; Q9VWB2;', 'KD00909', 'Drosophila melanogaster (Fruit fly)', 'polo', '#Serine/threonine-protein kinase polo#2.7.11.21', '-', '-', '40232'),
(910, 'O74372', 'DASH complex subunit duo1', 'GO:0042729===GO:0031134', 31909, '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}.', 'MTSELQQELQILRSFNYTIEKLTDGLSASKEKIKSFETSINNSNRLIQLWSSVLSQTEHTQNLILNSDWKGLSFDNEELERLQHQKMLQIQAEEQRKIELQQEQERLEQERRQKEEAIALQKQQQQRLLRSKDPKVRPARRAASSYVPSRPSHVPRSSSMNVRSRVSMATTSNPNSLRTPSSSFASHRQSAIPKSATSSAPTIPTSNLPSVASSIPNNGLNSSNRKSIISKTSSRLRPPSRVSNVPSVPQHPSTRSRTSTRETTQPPFTTNPSNRSKRTTLR', 282, 'O74372;', 'KD00910', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'duo1', '#DASH complex subunit duo1#Outer kinetochore protein duo1', '-', '-', '-'),
(911, 'B5X5N3', 'Spindle and kinetochore-associated protein 2', 'GO:0000940', 25785, '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}.', 'METAVDKLEAMFQKAEADMEYMEKRLRLDFLTNVPENSAAEENPMKLLENLSAIKTRHAALCTQVQEIAAEQKQSMDAIRVHLDTTVQLVQQLQQTADVELPTVTETEQESAEFLGLSVNQNTIEVPMSMELPAQELPQSSREGEFEEVSEATLEAVPCSMRANVKLANLNAFYKQLHEYFSFRKNSGALSLPKMKQMNMKVSDAKLKTLQHLSLIELDMKGHVRLLL', 228, 'B5X5N3; B5XA91;', 'KD00911', 'Salmo salar (Atlantic salmon)', 'ska2', '#Spindle and kinetochore-associated protein 2#Protein FAM33A', '-', '-', '100195579'),
(912, 'Q12018', 'Cell division control protein 53', 'k', 93944, 'Core component of multiple cullin-RING-based SCF (SKP1- CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The SCF complex associates with CDC34 as the E2 ubiquitin- conjugating enzyme. The functional specificity of the SCF complex depends on the type of F-box protein. SCF(CDC4) controls the G1- to-S phase transition; it directs ubiquitination of the phosphorylated CDK inhibitor SIC1 and of CDC6. SCF(CDC4) directs ubiquitination of GCN4. SCF(GRR1) directs ubiquitination of phosphorylated CLN1; CLN2 and GIC2. SCF(MET30) directs ubiquitination of MET4. SCF(DIA2) is specifically involved in the pheromone induced degradation of phosphorylated TEC1. SCF(MDM30) seems to direct ubiquitination of FZ01. Involved in the regulation of methionine biosynthesis genes. {ECO:0000269|PubMed:10213692; ECO:0000269|PubMed:16421250; ECO:0000269|PubMed:7813440; ECO:0000269|PubMed:9312054; ECO:0000269|PubMed:9346238; ECO:0000269|PubMed:9346239; ECO:0000269|PubMed:9499404; ECO:0000269|PubMed:9736614}.', 'MSETLPRSDDLEATWNFIEPGINQILGNEKNQASTSKRVYKILSPTMYMEVYTAIYNYCVNKSRSSGHFSTDSRTGQSTILVGSEIYEKLKNYLKNYILNFKQSNSETFLQFYVKRWKRFTIGAIFLNHAFDYMNRYWVQKERSDGKRHIFDVNTLCLMTWKEVMFDPSKDVLINELLDQVTLGREGQIIQRSNISTAIKSLVALGIDPQDLKKLNLNVYIQVFEKPFLKKTQEYYTQYTNDYLEKHSVTEYIFEAHEIIKREEKAMTIYWDDHTKKPLSMALNKVLITDHIEKLENEFVVLLDARDIEKITSLYALIRRDFTLIPRMASVFENYVKKTGENEISSLLAMHKHNIMKNENANPKKLALMTAHSLSPKDYIKKLLEVHDIFSKIFNESFPDDIPLAKALDNACGAFININEFALPAGSPKSATSKTSEMLAKYSDILLKKATKPEVASDMSDEDIITIFKYLTDKDAFETHYRRLFAKRLIHGTSTSAEDEENIIQRLQAANSMEYTGKITKMFQDIRLSKILEDDFAVALKNEPDYSKAKYPDLQPFVLAENMWPFSYQEVEFKLPKELVPSHEKLKESYSQKHNGRILKWLWPLCRGELKADIGKPGRMPFNFTVTLFQMAILLLYNDADVLTLENIQEGTSLTIQHIAAAMVPFIKFKLIQQVPPGLDALVKPETQFKLSRPYKALKTNINFASGVKNDILQSLSGGGHDNHGNKLGNKRLTEDERIEKELNTERQIFLEACIVRIMKAKRNLPHTTLVNECIAQSHQRFNAKVSMVKRAIDSLIQKGYLQRGDDGESYAYLA', 815, 'Q12018; D6VRL7;', 'KD00912', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CDC53', '#Cell division control protein 53#Cullin-A#E3 ubiquitin ligase complex SCF subunit CDC53', '-', '-', '851424'),
(913, 'Q4WXP0', 'Probable kinetochore protein ndc80', 'GO:0034501===GO:0000778===GO:0051315===GO:0051455===GO:0031617===GO:0031262', 83995, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MRSDGLRLTNIFLIQTLGSVQNYSALPQPSSALKRTSSIGYQNPPFTSQHTRSMSLLNSASRPQQPNFQRSSSGGAFGADAGLSSVRRSVSSNIFHGASVGRPSYAPGSLSASSASQSLQRRSSVFSRPSVGGPMGHQSFFTQVPNAAGVPRDPRPLRDRSFQARIGQELLEYLTHNNFELEMKHSLGQNTLRSPTQKDFNYIFQFLYHRIDPGYRFQKSMDAEVPPILKQLRYPFEKGITKSQIAAVGGQNWPTFLGMLHWLMQLAQMMDRFVLGEYDEACAEMGVDVSGDRIIFRFLTGAYHDWLQGGEDEDDETAEKRLVPHIESMAQEFERGNEKYMQEMQVLEAENRALRDQIEELEKNAPDMAKLDKHFRILEDDKRKFEDYNQNVQGKIEKYENRIKFLEEEIQKVEAELQAAEEERSSLQSSVDQQGITIQDIDRMNTERDRLQKSLEDTTARLEETHARVMEKEAEASRKLEDLEEIVKVYNTLGYQTSLIPSTAVNAKGQDYELSLNINDNSFSASQIGGLPNRISSEADRLLAEPFTGYHPAHLLNLDLRGMVRSSLQALRKEINERRKRAIDDDLERRNLLDNIKEAMDEKRSEVEALEHKRRAAEEEFERLKEITTTQKLASDAQIEKMEKELAKMRATLSESVQLMEQREMNTNIEYEQLTLRANALREELHTNVESMLNDVIRFKVHIQKGLEDYESFVVDEVEQELGGDLPATKDVTSQT', 736, 'Q4WXP0;', 'KD00913', 'Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSA1100) (Aspergillus fumigatus)', 'ndc80', '#Probable kinetochore protein ndc80', '-', '-', '3511788'),
(914, 'Q8R1Q8', 'Cytoplasmic dynein 1 light intermediate chain 1', 'GO:0000776===GO:0000777===GO:0003777===GO:0005868', 56614, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress throuh the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores (By similarity). {ECO:0000250}.', 'MAAVGRVGSFGSSPPGLASTYASGPLANELASGSGGPAAGDDEDGQNLWSCILSEVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGEDFPASPQRRTTGAQEDRGDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKVEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVGGSPGGGAAGASPSLPPSAKKSGQKPVLSDVHAELDRITRKPASVSPTTPTSPTEGEAS', 523, 'Q8R1Q8;', 'KD00914', 'Mus musculus (Mouse)', 'Dync1li1', '#Cytoplasmic dynein 1 light intermediate chain 1#Dynein light chain A#DLC-A#Dynein light intermediate chain 1; cytosolic', '-', '-', '235661'),
(915, 'Q5U2W4', 'Centromere protein N', 'GO:0000777===GO:0034508', 39459, '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. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate (By similarity). {ECO:0000250}.', 'MDENVAEFLRRIILKIPLCEMKTILEAWDFLSEDQLQSINLKQRKEFLAQEVILLCEDKCASLDDMALLDLMYTQFHRHQKLWNVFQMSKEPGGNDVDLFDMEQFQSSFKRILQRALKNVTVSFRVYEKNSVWIRVAWGTQYSQPNQYKPTFVVYYPQTPYVFISSCYLKSTVPLLHQALKVASKHHQMAQLDLRSRHLDSLTAIVFNEYDQTFENYNSTASWREGSLGLKTDLDSKIIHENTEEKVRIHRATQEAFGAYPQPQLEFAQYKLETKFKSDVGGGILADRKEPLRCLVKFSSPHLLEALKSLAPAGIADTPLSPLLTCIPSKKMNYFKIRDK', 340, 'Q5U2W4;', 'KD00915', 'Rattus norvegicus (Rat)', 'Cenpn', '#Centromere protein N#CENP-N', '-', '-', '361416'),
(916, 'Q96GM5', 'SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1', 'k', 58233, 'Involved in chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons; npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A; are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Has a strong influence on vitamin D-mediated transcriptional activity from an enhancer vitamin D receptor element (VDRE). May be a link between mammalian SWI-SNF-like chromatin remodeling complexes and the vitamin D receptor (VDR) heterodimer. Mediates critical interactions between nuclear receptors and the BRG1/SMARCA4 chromatin-remodeling complex for transactivation. {ECO:0000250; ECO:0000269|PubMed:12917342; ECO:0000269|PubMed:14698202; ECO:0000269|PubMed:8804307}.', 'MAARAGFQSVAPSGGAGASGGAGAAAALGPGGTPGPPVRMGPAPGQGLYRSPMPGAAYPRPGMLPGSRMTPQGPSMGPPGYGGNPSVRPGLAQSGMDQSRKRPAPQQIQQVQQQAVQNRNHNAKKKKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRLDIQEALKRPIKQKRKLRIFISNTFNPAKSDAEDGEGTVASWELRVEGRLLEDSALSKYDATKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTATTQETDGFQVKRPGDVNVRCTVLLMLDYQPPQFKLDPRLARLLGIHTQTRPVIIQALWQYIKTHKLQDPHEREFVICDKYLQQIFESQRMKFSEIPQRLHALLMPPEPIIINHVISVDPNDQKKTACYDIDVEVDDTLKTQMNSFLLSTASQQEIATLDNKIHETIETINQLKTQREFMLSFARDPQGFINDWLQSQCRDLKTMTDVVGNPEEERRAEFYFQPWAQEAVCRYFYSKVQQRRQELEQALGIRNT', 515, 'Q96GM5; A6NN27; Q92924; Q9Y635;', 'KD00916', 'Homo sapiens (Human)', 'SMARCD1', '#SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1#60 kDa BRG-1/Brm-associated factor subunit A#BRG1-associated factor 60A#BAF60A#SWI/SNF complex 60 kDa subunit', '-', 'ENSG00000066117', '-'),
(917, 'Q9GLN5', '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}.', 'MSAPSLPPAWQLYLKDHRISTFKNWPFLEGCACTPERMAAAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLSEFLKLDKERAKNKIAKETNNKQKEFEETAKKVRCAIEQLAASE', 142, 'Q9GLN5;', 'KD00917', 'Sus scrofa (Pig)', 'BIRC5', '#Baculoviral IAP repeat-containing protein 5#Apoptosis inhibitor survivin', '-', '-', '397266'),
(918, 'Q75QI0', 'Craniofacial development protein 1', 'GO:0000777', 32780, 'May play a role during embryogenesis. {ECO:0000250}.', 'MSGCEEEAGDGYSSAEDEDYVPSGAEYSEEDESELLREEEEEAAGPRPTRSRNSPRQATRRKKKKRRGLVLEVDEKEEGKAQENEDEEDDLKQSEKDREEEEKKKEDALWASFLSDVGQKPKAAATQATHADKAGEVKSVNKLQGKPKESEKPKDSGRVTITKVFDFAGEEVRVTKEVDSSSKEAKSFLKQQEKWQSSAPGSLPTVSGVKRPSGISSLLGKIGSKKQKMSTLEKSKLDWENFKEEEGIVEELAIHNRGKDGYIERKAFLERVDHRQFEIERDIRLSRMKP', 290, 'Q75QI0; Q8JIM2;', 'KD00918', 'Gallus gallus (Chicken)', 'CFDP1', '#Craniofacial development protein 1#Bucentaur', '-', '-', '374073'),
(919, 'Q6BL27', 'DASH complex subunit DAD1', 'GO:0042729', 11865, '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}.', 'MSESSTYFEKQRDMLIQEIGVSIESVVYNLDILNRSLNGSISVGKEFDNVGRLWSHFYDGLNQLKERNNQEETNKNDQGDANDDDSSSDEHGSSDEEIDQDQEN', 104, 'Q6BL27;', 'KD00919', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'DAD1', '#DASH complex subunit DAD1#Outer kinetochore protein DAD1', '-', '-', '2903110'),
(920, 'O01427', 'Aurora/IPL1-related protein kinase 2', 'GO:0032133===GO:0000780===k;m', 34749, 'Serine/threonine-protein kinase which mediates both meiotic and mitotic chromosome segregation. Required for histone H3 ''Ser-10'' phosphorylation. Phosphorylates tlk-1 at ''Ser-634''; which enhances its activity. Phosphorylates zen-4 at ''Ser-680''. {ECO:0000269|PubMed:10354474; ECO:0000269|PubMed:10975519; ECO:0000269|PubMed:10983970; ECO:0000269|PubMed:11050384; ECO:0000269|PubMed:11050385; ECO:0000269|PubMed:11940606; ECO:0000269|PubMed:12015116; ECO:0000269|PubMed:15854913; ECO:0000269|PubMed:15916946; ECO:0000269|PubMed:9852156}.', 'MENKPPVINLPEKETVNTPQKGGKFTINDFEIGRPLGKGKFGSVYLARTKTGHFHVAIKVLFKSQLISGGVEHQLEREIEIQSHLNHPNIIKLYTYFWDAKKIYLVLEYAPGGEMYKQLTVSKRFSEPTAAKYMYEIADALSYCHRKNVIHRDIKPENLLIGSQGELKIGDFGWSVHAPSNKRQTMCGTMDYLPPEMVNGADHSDAVDLWAIGVLCYEFLVGKPPFEHEDQSKTYAAIKAARFTYPDSVKKGARDLIGRLLVVDPKARCTLEQVKEHYWIQGMMEAKIRAEKQQKIEKEASLRNH', 305, 'O01427;', 'KD00920', 'Caenorhabditis elegans', 'air-2', '#Aurora/IPL1-related protein kinase 2#2.7.11.1#Serine/threonine-protein kinase aurora-B', '-', '-', '172268'),
(921, 'P61956', 'Small ubiquitin-related modifier 2', 'k', 10871, 'Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I; and can be promoted by an E3 ligase such as PIAS1-4; RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport; DNA replication and repair; mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (PubMed:18408734; PubMed:18538659; PubMed:21965678; PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269|PubMed:18408734; ECO:0000269|PubMed:18538659; ECO:0000269|PubMed:21965678; ECO:0000269|PubMed:24105744; ECO:0000269|PubMed:9556629}.', 'MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVY', 95, 'P61956; B2R4I2; P55855; Q32Q42; Q6IPZ6; Q96HK1;', 'KD00921', 'Homo sapiens (Human)', 'SUMO2', '#Small ubiquitin-related modifier 2 {ECO:0000305}#SUMO-2 {ECO:0000305}#HSMT3 {ECO:0000303|PubMed:8630065}#SMT3 homolog 2 {ECO:0000312|HGNC:HGNC:11125}#SUMO-3 {ECO:0000303|PubMed:10692421}#Sentrin-2 {ECO:0000303|PubMed:9556629}#Ubiquitin-like protein SMT3B {ECO:0000305}#Smt3B {ECO:0000303|PubMed:10692421}', '-', 'ENSG00000271236', '-'),
(922, 'Q54UL8', 'Probable serine/threonine-protein kinase mps1', 'GO:0000778', 113573, '', 'MDTHQSFNENQHPNFNSGNHGGINMNRFQRFSKPTISPIQQQQQPQPQQPSSIIQRQSIIMTQPQPQPQPQMIPIFREPNEWYKLIDMEMNKFNNESRPSPEYIKYLTQLFQQALDSLEHKNTPEFYLFLLNRATFQSKIGENEDAKGTLKYMKVLKMESFEVFVLLSEIESKSFRFSKARSIINRGIQKIPSRSKEFEGFLMVIDIQEDEFSRNGCIISNNNNISFNNGDVNNNSIIMNENDQPMVINLNPQQQQQQQQQPYEISSSSSLMSTPASSRHLSNRSSIVPTPNSSTKLSESIKTIGLRSVQPRRVIHKQTTTNFNTTTTTIPENSYDDDADQPMDHDGNNNNNFRIHSNNNNNSSANSSYNKSENDEDDQDEEDEEEEDEDEDDDEEDEEEYEDNNNNNNNNNNNNNNNNNNNNNNNNNNYFKYNRQQYILNNDSDTSTNPNSPASSNSSVNDIINSISITDDSKLDYENNVKLQQQQQQQQQQQQQQQQQQQQQQQQQYIQQQQQQQPKIHPQRFSLQNNTPTTTTTTTAATNVQNPSSSSSYISPPLSSQSSELQHQRRHSIQAQRANKPPVIPPPSKLHQNNLQQQQQQQQQQQQQQQQQQQQQLLLQQQALLQQQQQQQILLQQQQQQQQQQQQQQQQQKQQEQQLKKTNMQPPPPKQPQPQTQTQQQQKNINNSEIVDKEKSFEVAKSWSEVAMVNGKPYLRIEFIGKGGSGKVYKVLSGDLKIYALKYVCLSDPNEIEAQLNEIEMLKRLRKQVNIIQLIDYEVNMAKNYILLVLEFGEIDLSKLLQRLQTPNGTNVNFIRIYWQQMLQAVHTIHEEKIIHGDLKPANFVSVQGSLKLIDFGIAKAIQSDDTTNIVRESQIGTINYISPEALIDTSQGGPKQCMKLGRASDIWSLGCILYEMAFGYPPFKSFSNIISKYQAIINPHHKIEFPVHPNENLLKVLKLCLIRNPHERPTIPTLLNHDFLKI', 983, 'Q54UL8;', 'KD00922', 'Dictyostelium discoideum (Slime mold)', 'mps1', '#Probable serine/threonine-protein kinase mps1#2.7.11.1#Monopolar spindle protein 1', '-', '-', '8622811'),
(923, 'O44081', 'H/ACA ribonucleoprotein complex subunit 4', 'k', 56831, 'Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex; which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5; instead of the normal N1. Pseudouridine (''psi'') residues may serve to stabilize the conformation of rRNAs. Required for maintenance of the germline stem cell lineage during spermatogenesis. {ECO:0000269|PubMed:10087258; ECO:0000269|PubMed:12645924; ECO:0000269|PubMed:9829824}.', 'MADVEVRKEKKKKKIKEEPLDGDDIGTLQKQGNFQIKPSSKIAELDTSQWPLLLKNFDKLNIRSNHYTPLAHGSSPLNRDIKEYMKTGFINLDKPSNPSSHEVVAWIKKILKVEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQSAGKEYVAIFKLHGAVESVAKVRQGLEKLRGALFQRPPLISAVKRQLRVRTVYDSKLLDYDETRNMGVFWVSCEAGSYIRTMCVHLGLVLGVGGQMLELRRVRSGIQSERDGMVTMHDVLDAMWLYENHKDESMLRRVIKPLEGLLVNHKRIIMKDSSVNAVCYGAKITLPGVLRYEDGIEIDQEIVICTTKGEAICLAIALMTTATMASCDHGVVAKIKRVIMERDTYPRKWGLGPKASAKKALIAAGKLDKFGRPNENTPKEWLTGYVDYNAKKPAAQEVSPTNGSSEPSKRKLSTSSVEETAAAAVSEETPSKDKKKKKKKHKGDEEAPEAAEEEAEPVEKEKKKKKKKDKDRDRDEAQE', 508, 'O44081; A8E745; Q0GLB4; Q0MVP1; Q8T408; Q9UAN8; Q9V3Z5;', 'KD00923', 'Drosophila melanogaster (Fruit fly)', 'Nop60B', '#H/ACA ribonucleoprotein complex subunit 4#5.4.99.-#Nucleolar protein AT band 60B#Protein minifly', '-', '-', '37873'),
(924, 'Q5R581', 'Kinesin light chain 1', 'GO:0003777', 63888, '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}.', 'MYDNMSTMVYIKEDKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSNMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDTDSTKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGDYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGTSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPENMEKRRSRESLNVDVVKYESGPDGGEEVSMSVEWNGMRKMKLGLVK', 560, 'Q5R581;', 'KD00924', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'KLC1', '#Kinesin light chain 1#KLC 1', '-', '-', '100173833'),
(925, 'Q9SMH3', 'Dynein-1-alpha heavy chain; flagellar inner arm I1 complex', 'GO:0003777', 522843, '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.', 'MDRRLEWVKEKACLGLGVEPNLFEAAIANPESRARVTAFLDGTVTSSALLFALEEATIYVEEYQEVLAEEQAPEAEDGEGEEHDGQEPGEAGGEGAEGSTAPGDSGDGQPEDAPAAAAEANGANPEDEAAAPADGAADGAAGEGGEEGDGAEGDEPPAPPAPKYVRRVISVPKVVSKLNVALGSLPEELSVFPVFYFILNRSGHVAAEELDSAVEFGLLSEGPSLRILEQMLSSVFVPILVQMSGGDVASGGVLMQSMTDNSHRELLGNMQKFHSQVTQALQQLTGDVTLQLPDFPLEDMDRAAADTDLVMQLEQYMAEWSQVLASVLQRESQKHPTGKGPLAEIEFWRERNAVLSSLYEQLNLPQVKRMILVVEKGSDDRNLMAGFKSQLGELTKLATEARDNVKFLTTLERHFKNIATGPLGGILDTLPPMMNALRMVWIISRHYSDDQRMGSLFQRIAREIGDRVEAAVDLRHIFRMTSADAVELLKVCKSVLEHWLQTYMAMREKIELSGRDARWEFPKQLLFARTNYMAEICTDLIEMVEIVDDFFRFLGPELKTVTGDTAGIDRVVHRVVAMYEPIESISFNVFDYGNQHEWKAAKQQFYADNEDIKEATRELIDTSFRKLRSAEGACELLQSFKSIKSKGAIQKQVMNKFNDILEQFAREIEQTADIFERNKDAPPVTKNQPPVAGAIKWVRSLLERLKRTMAKLLSTEEEIIRTTELGQAVESKFKSFARSVMLTEKKWFSSWSDSINGVAMQHLKQTIFRRSAATNRVEVNFHPDLVRLIRETRYLDRMGFPIPEIALNVALQEDKFLQWLEGLNSMLFKYYESIDQLTPVERELMERKLEELESCLQPGFTILNWNSLGITEFIGTCDKAIATFQQLVKQVQKNSGIIEQVVYAIAGAQLVTEPEEGAEVMDLQEFYEDIERQRLAALESLVKKYRTISPLLGKIEEVVAGTNSGKSPALSSYYSFWERAIFNALNTMVLCAMTKLQDMIEQRSKHAEGGRKPPLFKVTVSLQSVDVVVQPPMTEVNKALGRLVRSLVESTKAFVRWMDGTCVETPEQRGATDDDEPIVFTFYWDVAANPQVIKTMLNLNQSIQRAITSVNKYAESWRRHQALWKTDKNSVLDKFKARDPSAAQFEDKLSKYAKMATEISAQAKDFDQDFIRVSCHALASSVCDEAQAWVRAIAQTMRELDAVTESQLRDKIAKYQTALHRPPDTLEELKQVLNTVNTIRGESMVMELRYADLEERYRTRLLYATNPEEESQCAHELASASQVRALWTELLNEAEAVDWSLEETKKKFSETTRSQVSDFAAITAELWEKFRTTGPGLPTVELASGLDELHKYESNLADALRQREQLVLAEKLFGMEITAYPELAQLESEIRKLAQVYGVYAEHAEAVRQYGGQLWSELDVGKMMAGTEAILTKLRKLKSLKLLPVYELVEKEIQGFYNSLPLMKELKSEALRKRHWTRLMEVTGQEFDMDPKTFTLGNMFAMQLHKYAEEIGKITNAAVKELTIESEIRKLADVWREQRFELGKYMKGPEDRGWVLRSTEDILVLLEDMGLNLQSMMASPFVRPFLTEVRAWEQKLSLIGECIEVWMHVQRKWMYLESIFVGSDDIRHQLPAEAKRFDNIDRQWQKIMNDTAKNTVVLDACMADGRLDLLKSLSEQLEVCQKSLSEYLDTKRCAFPRFYFISDDELLSILGTSDPTSVQEHMLKLFDNCAALVFGRGNKTITGMVSSEKEGFEFRNVVPIEGAVELWMTNVEAEMRKTLYQITKEGIFFYAKTPRTKWISENLGMVTLVGSQIWWTWETEDVFRRVRDGNKHSMKEFAAKLTGQLSELTSMVRSDLSNEVRKKVNTLIIIDVHARDIIDTYVRDSIVDAREFAWESQLRFYWDRQQDDILIRQCTGLFKYGYEYMGLNGRLVITALTDRCYMTLTTALTYRLGGAPAGPAGTGKTETTKDLAKSMALLCVVFNCGEGLDYKAMGSIFSGLVQCGAWGCFDEFNRIEAEVLSVVSSQIKNIQEALKNDLTRFQFEGKEISIDPRTGIFITMNPGYAGRTELPDNLKALFRPVTMVVPDLEQICEIMLFSEGFDSAKVLAKKMTVLYKLSREQLSKQHHYDFGLRALKSVLVMAGSLKRGAPDMSEQLVLMRALRDMNLPKFIFDDVPLFLGLINDLFPGMDCPRVRYPQFNDVVEADLADQGFKVLTEPSEQVDKVVQLYEVMMTRHTTMVVGQTGGGKTVILNTLARAQTKLGKKTHLYTINPKAISVAELYGVLDKDTRDWTDGLLSNIFREMNKPLPAERDEARYLVFDGDVDAVWVENMNSVMDDNKLLTLPNGERIRLQNHCKLLFEVFDLQYASPATISRCGMVYVDSRNLGYKPYIYTWLNSRAKQAEVDILRGLFEKYAVPSVDWILEGIDGEELVRRPKQAVPVTNLNMITQLCNLLNATITDHPRMSDPQILEAIFIFCTIWSLGAAIVQRPESPDRDRFDAFVKHIASMGLVDGERVAATQLPARSLYEYCFDTNEGVWKSWRSYLQPYEPPADGAFAKILVPTVDVVRSTWLLNTVVAAGKPCLFVGESGTAKSVTIANYLAHLDSTINIVLNVNFSSRTSSLDVQRAIEDSTEKRTKDTYGPPMGKRLLMFIDDLNMPRVDTYGTQQPIALLKLFIERKGLYDRGKELSWKNMKDVQVVGAMGPPGGARNPVDPRFISLFSVFEIQFPSNENLRTIYQAILSRHLAKLPTDEIRDQLGERLTDVTLELYNFIIDKLPPTPSRFHYIFNLRDLSRIYEGLLLTVGDVFKTPEQFLRLWRNECLRVLHDRLISTDDKRVMTERLEALVQQKFPNLAAHTLASPVLFGDFKNVINELQGEGEVAPRMYDDLGDYNSIKPLFEDVMTNFYNRKRKPMNLVFFEDALEHLTRIHRTLRLPQGNCLLVGVGGSGKQSLSKLAAFTAGCEVFEITLTRGYDELAFREDLKRLYAMLGSDNKRVMFLFTDAHVADEGFLELINNMLTSGMVPALYDGAEKDGLIGSVRAEVEKKGLLATKESCWSYYVDKCRNNLHVVLAMSPVGETLRSRCRNFPGMVNNTVIDWFEPWPEQALTSVASVFLAEEALPEALRPQIVEHMVTVHQSVRTFSTRFLEELRRYNYVTPKNYLDFINNYKRALATNRRTIEDTVTRLSGGLEKLIQAAVEVDAMQKELSQAQVVVAQATKECNELLEVISTNTVDVETKAKAAAIKEAQLKVDSEQIAIEKAEAEAALEEAIPALEEAAAALQDLSKDHITEIRSYAKPPEQVQKVCECVVILRNIKDVSWLGAKSMMADGNFLRSLVEFDKDSLTDKQVKKVKEYFKDPKAPLTYDSLRAISTAGAGLLKWVLAMVNYNNVARTVEPKRKKVAESEKNLRIAQKDLASTKLELQSLNDQLGKLRTQFEEKTAEQQDLKAKADLMERRLIAASKLIAGLGSERERWTRDIADLESRRDRLIGDCLLTSSFLSYTGAFTATYRHAMVYEMWQDDVKARGVPVTQPFRLEALLTSDVETTGWASEGLPSDELSIQNGILTVRANRWPLCIDPQMQAVNWIKSREGKMLEGKVKTFNDSDFLKQLELSIQYGFPFLFENLDEYIDPVIDPVLEKNLVPGDGKFVIKLGDKEVEWDSNFRLYMTSKLSNPHYGPEISGKTMIINYGVTQQGLTEQLLNVTLRHERSDLEEAREALIKQMSENKATLQALEDTLLRELSNAQGNILDNSELIATLESAKLKAVEIAEKLEASKVTAAEIEETRVRYSPAAKRGAILFFVIAGLSAITNMYEYSLASFLVVFNGSLHSSRRDASIEGRLRNIIDTLTYDVYAYTCLGLFERHKLMFSFQMTCKILEGDTPLDPQLLDFFLKGNLSLEKAARRKPFDWFPDAGWQDLMRLVELGQKKIGADGRMHALGSLANDVESDEAAWRTWYDLEAPEEAELPCGYQSFLSDFEKLCLMRCLRMDRVTVGITRFVIGVMGEKYVQPPVLEYRSIYKQSTETTPIVFVLSPGADPAFDVFKLGEEMGFRPGAKLKYMALGQGMGPKAQELIETGATRGLWIMLQNCHLLPTWLKTLEKILEKITKPHADFRLWLTTELTDRFPLGVLQRSLKVVTEPPNGLKLNMRQSYSKITEEVLADCPHQAFRPLVYVLGFFHAVVQERRKYGKLGWNVPYDFNETDFRISMALISTYLTKAWDAQDDLIPWGTLRYLIGEAMYGGRVSDSYDRRILTTYLDEYLGDFLFDTFQPFRFYACKDYEIAIPQTGSRDTYLKAVEALPLVQSPEAFGLNANADISYYTSATKAIWTDLVDLQPRTGGGGGGVAREEFIGGVARDIAAKIPEPFDLPQLRKELGTPSPTQVVLLQELERWNSVLGVMVSSLRDLQRALSGEIGFSSRLEELASSLYNGKLPAMWARLNPATEKALGAWMLWFGRRYRQYKDWTEHGEPKVIWLSGLHIPETYIAALVQAACRDKGWPLDKSTLYTKVTKFTDPYQVSERPKYGCYMSGLYLEGAAWDLEASQLRKQDPKVLVNELPILQVIPIEANKLKLANTFRAPVYVTQARRNAMGVGLVFDADLASAEHSSHWVLQGVALVLNIDQ', 4625, 'Q9SMH3; Q96388;', 'KD00925', 'Chlamydomonas reinhardtii (Chlamydomonas smithii)', 'DHC1', '#Dynein-1-alpha heavy chain; flagellar inner arm I1 complex#1-alpha DHC#Dynein-1; subspecies f', '-', '-', '-'),
(926, 'Q9SMH5', 'Cytoplasmic dynein 2 heavy chain 1', 'GO:0003777', 481652, 'May function as a motor for intraflagellar retrograde transport. Functions in flagellar biogenesis. {ECO:0000269|PubMed:10069812; ECO:0000269|PubMed:12802074; ECO:0000269|PubMed:9971742}.', 'MSSDSRKTFVVTTIACAIAPAGQQDQYAAYLGQDENGAIASFLDSTQNTLQAGVSGLGTGQLQLKLSNAAEFPEGCEFSVVLSKLRAGPIRTEDVPAGVAVATVAHSPLSSLYHTLKDVYSPLIKSQTAEGVPVLDKRLSELLAQVQAGLGTAVRKGVPASAQEVADPNQAPLQEVVTPLDEINFWAELTNSPNAGPIKSSALQVSSALEPLRQSFEQLSSDAPEGEGGSIGWEGAKELVDLTTNALRAAWPVKLPIGGWAMGQKRADNFLRVVGAALATYVQRRVDRLAAAGRGDLWSAPFGEVRAVLVGASGLMTRWVQESTALVEDWRLGVDTGGHDWEGAAFADAYVRSFQERLEEIYNMREMVDELAKLVGREEAGSLGVQQVFAPFQGLQALQVSDFNTHVWKAAHEDFERRMGPIEQRISQKLKELFASVIIPSLTSAIGPGRGGDRAAAGGSLIQPQQVFAEIKRYSSLMGRKNIASALQSEKETLAKQVDRHLDSVQAEFDAHRDSATGGAKVAPVGRVTASIVERIMWCMQTLQKLGKVSEVLKHMLRGGVAGDEGSGGAALRNTLGVVSELQKEVEIFRKEQYSAWEEWMSEELGEMANWKNSKLMTFDSQNSHVKTHFNDQLVLLLREVRQLQSLGFGVRKDILNEVEIANKFYRYGMVLKQRANFYNNIATEMVQCQKPMMLKDALDFEKVLMNPKDAQGKEITWRNAAALDGYVRRLNEVADRLAEKNRTLRKWHSVLSDKVVTLAGTDLVRHKDKWAAGVKEMREIFGRLEAEGYSRESQQVWRQHWDFQLYKALEVQYLSGLEMINKTLPEVEVKMVFRQHRLQYDPPLEELRIRHVKDLLNTFLGLPLRMKGVSDLSERPGFFRPIVDANPTGIARVYAAAESLFTQLADELKKYQDWMVLGTLDLDEFADANLLEVSDWELNFRMLKAASRDAEKLPNEIRIECYKVSLAPVKGSIDEHMKKLQDTLVASLRRKTVAEKDQIEDFMKNGRELFTRQANTVEDIGLAGQEAKGLTAKLAEVQAARRRIDEKNKLLRQMAGGGRDAAFAVVDLTEVNNSWDAFTNQLQQFDAHLEEQKGNLAVQISRQLEEFKGKVAGMNSRWQELKPKSGPSGNPAVVLAKIQEYANAIKELREESAKLYKEAEAFKIDVPDFELMTEMETDVMATKAHWDRYADFLRERDEMANRDWLSMRDQVWKIEDFLAKWTKATAGKSDDPIAVILTQEIDNYTLCLPHLKSCLRGAGWEDTHWNQLFGLLGMKTSGPAAVSKETVTLTHFLEKADLVVKHADVIKSLDAQAQGEAVIRKALTELKMWGMAREFTFTESTQSVAGRQRRTPLIKEWRDAMTEVGDNQSLVASLKQSSYYNMFKDEVSSWENKLSFLQEGLTLLNQIQRKWVYLEPIFGRGALPSQQQRFRNVDEEFRRTMTSLESTKKVVTFADIPGIRDKLPQMAQQLDVCQRALADFLEEKRSQFPRFYFLGDDDLLEILGQARNPAVIQSHLKKLFAGIQKVKFSQDQSTIQAMQSMEGEVVDLAPTVRITEQIETWLGDLTRSMKNTLQQQNEVLCAGRMNDEFRAAASQCLQLKEAVAFTEKAEVALKAGSSGLAKLVTEMRAQLMKLTGSDFTGHHLLQLKKQALVLDFIHYCDVAEYLAKDKIGGTTEWGWTRQLRYYHRAEGSVKVAMAEATFDYTWEYQGNAAKLVYTPLTDKCYLTLTQGMALGYGGNPYGPAGTGKTESVKALGQALARQVLVFNCDEEFDFKSMGRIFVGLVKCGAWGCFDEFNRLDEEVLSAVSQQIQTIQLALKEGAKTMMFMDKTVEVDKNAGIFVTLNPAGKGYGGRSKLPDNLKQLFRSIAMTVPNNELIAEVLLLSEGFNHAKDLARKLVSLFSLSRELLSPQQHYDWGLRALKTVLGIAGRELRDARKAGQNVDAEIEAEIIIRSVAATKLPTLTFDDNSRFKALINDLFPGAKLTDARNEALEKALAEAAAACKMELTQQQIDRMLQLHLACEQRIGVIIVGPSGSGKSTLWELLEKAYERLGRKPIVYKMNPKAMPRQQLLGSMNMDTREWSDGVLTAAARKVVKEPLEQRSWIICDGDVDPEWIESLNSVLDDNRLLTMPNGERIQFANNVNFIFECHSLEFASPATVSRCGMLFMSDEAMEVERMLQRWLKVQATDNGDPGQMQSWMNDFFDKAFQWALSHPRAVETTKGGILDSGLSHLKLGPGSKQEFMAGLCRGLGSNMNPDIRNQFYNDMARMSGEGGIMDVGVATDPLIVLGDELRERGMDEADGGLVVTPEVTQNLLMMAPWFKNRDPFLVVGPEGCGKGALLDYCFKRIMGVQVAVVNCSAQTSAANVVQKLVQVCGKPVTTTSGKALRPPDNTRVILYLKDLNLPRPDKYNTCQLISFLQQLIAHHGYYDENLDFIRVERVQIVGSMTPPGSVGRHALSTRFTALVRIVTMGYPDRENLATIYTNMAQRVLANSKTASSVSPAALSKAMLEVYSSVRERFTPNDYPHYEFNARELSDWINGIQRYSLEGGLTLVQAIAHEGLRVFRDRLVGDHQEQFTSMLYGTLTSLLGYKPDATPWYTSTLGASAEERISGDLTKIKMLRWEQDTFAELVAEKLKGYEREHKELNLLLFPEVLERVSRFDRVLSQQGGSLLLCGNSGVGRRSLMLLLAYMHNMDFITPKMTKNYDLKSFRNDLKEVLRRAGVEAKPVMLFLEDHQLVNNAFLELVNSLLSGGEVPGLFTPEELAKELAPLDKARDEDPLYTGPSNSYAFFSYRIRRNLHIVVSMDPSNEMFRSRCEANPALFTRCSVQWLEGWSVKGLQQIAAARLTELVESSPELMKLGRDKLINHMIHIHASSGSQTTREYLALVSLYGQIYNRKRTQVLEQQNFLKGGLGKLAEAAVTVDTLSAEAEKQRVVLKAKQAEADEALVHIQDSMLKAADRRKEVEVLKKRTAIEEVEMKERRVKVEEELSEVQPLIDAARKAVGNIKKDNIAEIRSLKMPPDAIRDVLEGVLMVLGQQDTSWNNMKTFLGKGSVKDDIINYDAHKITPEIRARCAKLLAAKGNSFEDAVIRRVSVAAAPMAQWFKANLEFSKVLERVSPLESELHRLQSSLEESQRLIKQYEEELVQLDAAVASLKAEFSKKTSEAETLKISVDKAESVLSSARQLLDGLRGEKVRWEITVGTLGEQLKELPLSSLLAAAFITYLPSHPEEHRLKVTKDWCAYLGAAEFDVTRFLSSESEMLKWKAEGLPADGLSAQNAVVILNSTSRSPLIIDPSTQASEWLKSHLRVTGQNVEVTTMADQRFTTTLELAVRFGKTLVVAEVDKVEPILYPLLRMDLDRQGPRFVVQIGDKATDYNDTFRLFLVTRNPDPYLPPDARSLLAVTNFTVTRSGLEGQLLGLTLQKERPELEEQKSTMLRQEDECKVALAELERNLLQTLATSTGNILENKDLLDKLNETKTRSATVEKALTESKTLQASLDQQREVYRPIAARGSVMYFLLADLQALNQMYTFSLSVFLNLFKKALDRDTPPGGDVTARIALLAESLLELVFAYVSRSLFNADRLTFGMHMARHLQPSLFPEAQWAFFLGKPVPDSASPPPKPSWVREEQAGAFSALAAAFPQLVAAAELADSALWAQWASGATDALPGKIAGGKVNPFQQLLLVKAFRPDRLQSAMSSFICGTLNIKSVSPPPFSLKALIEGETRPDEPVLFITTPGADPSQELSEYAAQTMGKERWYFEVAMGQGQAEKAVTLLRECAKNGDWLVLKNVHLAVSWLPSLEKELLMLQKHDNFRIFLTSEPHPKFPSTLLEMSLKVTFEAPPGMKKNLQRTYEAWSAEYLASGPPIRAQLLFVLAWFHAVVQERRTYIPQGWTKFYEFSFADLRSGMDVITLATRAGTAPQWPLLLGLLDDAIYGGRLDNPFDSQVLLTFLRRLFSAETVGAAGGKVRPLPGSKVVVPTTNHRADYVSIISALPDVDTPGLFCMPDNIDRTAQQVNSARVISQLKAMSLRADAAGGFNRAQWQAQLGPLLRLWDQLMSGASALKAAMKDIRARGTTDKGGAPIENFVALERYKGASLVALIDRTLGAIARVLKGTDTLSSGVQSSGAALLADVIPGSWDAAWEGPEAPMDYCRAVVAKALAIEGHWARCQQPGGGGLLDGSGGAGPLELSSVFHPGTFLNALRQQSARTLGCSMDMLKAVTSWETAKLKAAAGGAPVALLGGLIMQGATFDGSRLSPVAAEAPAFRAVPAMSMAWLHKDSPMAYASYMEAPLYMTSDRSKLLARVQLPVSGPEEMDGWVLAGLSLFLSV', 4334, 'Q9SMH5; A8HYT6; Q9ZSS7;', 'KD00926', 'Chlamydomonas reinhardtii (Chlamydomonas smithii)', 'DHC1B', '#Cytoplasmic dynein 2 heavy chain 1#Cytoplasmic dynein heavy chain 1b#cDHC1b', '-', '-', '5722214'),
(927, 'O17915', 'GTP-binding nuclear protein ran-1', 'GO:0000777===SCL===k', 24254, 'Ran GTPase system comprises ran-1; ran-2 and ran-3 and is essential in nucleocytoplasmic transport. Ran-1 is a GTP- binding protein that mediates the interaction between mitotic chromosomes and kinetochore microtubules. Plays a crucial role in nuclear envelope assembly at the end of each cell division. Required for the import of protein into the nucleus and also for RNA export. RCC1 (ran-3)/Ran (ran-1) complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA. {ECO:0000269|PubMed:11909538}.', 'MSGGDGIPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGQIRFNVWDTAGQEKFGGLRDGYYIQGQCAIIMFDVTARVTYKNVPNWHRDLARVCENIPIVLCGNKVDVKDRKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLLGDPNLEFVAMPALAPPEVQMDPAMIAEYEKDLDNAAKADLPDDDDDL', 215, 'O17915;', 'KD00927', 'Caenorhabditis elegans', 'ran-1', '#GTP-binding nuclear protein ran-1#Ras-related nuclear protein 1', '-', '-', '176503');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(928, 'Q96Q89', 'Kinesin-like protein KIF20B', 'GO:0003777', 210629, 'Plus-end-directed motor enzyme that is required for completion of cytokinesis. {ECO:0000269|PubMed:12740395}.', 'MESNFNQEGVPRPSYVFSADPIARPSEINFDGIKLDLSHEFSLVAPNTEANSFESKDYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKMNLKPHRSREYLRLSSEQEKEEIASKSALLRQIKEVTVHNDSDDTLYGSLTNSLNISEFEESIKDYEQANLNMANSIKFSVWVSFFEIYNEYIYDLFVPVSSKFQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKVCVPDTLNSSQEKLFGPVKSSQDVSLDSNSNSKILNVKRATISWENSLEDLMEDEDLVEELENAEETQNVETKLLDEDLDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEKLTLEFKIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEETHNYVGFEDIIDSLQDNVADIKKQAEIAHLYIASLPDPQEATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKSHMENTFKCNDKADTSSLIINNKLICNETVEVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVSTENDQSTRFPKPELEIQFTPLQPNKMAVKHPGCTTPVTVKIPKARKRKSNEMEEDLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSSKKTYSLRSQASIIGVNLATKKKEGTLQKFGDFLQHSPSILQSKAKKIIETMSSSKLSNVEASKENVSQPKRAKRKLYTSEISSPIDISGQVILMDQKMKESDHQIIKRRLRTKTAK', 1820, 'Q96Q89; A8MXM7; O43277; Q09471; Q2KQ73; Q32NE1; Q561V3; Q58EX8;Q5T9M8; Q5T9M9; Q5T9N0; Q5T9N1; Q7KZ68; Q7Z5E0; Q7Z5E1; Q7Z6M9;Q86X82; Q9H3R8; Q9H6Q9; Q9H755; Q9NTC1; Q9UFR5;', 'KD00928', 'Homo sapiens (Human)', 'KIF20B', '#Kinesin-like protein KIF20B#Cancer/testis antigen 90#CT90#Kinesin-related motor interacting with PIN1#M-phase phosphoprotein 1#MPP1', '-', 'ENSG00000138182', '-'),
(929, 'Q62698', 'Cytoplasmic dynein 1 light intermediate chain 2', 'GO:0003777===GO:0005868', 54745, '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.', 'MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLRETLVIFVADMSRPWTIMESLQKWASVLREHIDKMKIPPEEMRDLERKFMKDFQDYIEPEEGCQGSPQRRGPLTSGSDEDNVALPLGDNVLTHNLGIPVLVVCTKCDAVSILEKEHDYRDEHLDFIQAHLRGFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTIPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQESPARGPSGSPRTQGRGGPASVPSASPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPSAGGVQSTAKKSGTEGEPQSFRSLTEQCCQTGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA', 497, 'Q62698;', 'KD00929', 'Rattus norvegicus (Rat)', 'Dync1li2', '#Cytoplasmic dynein 1 light intermediate chain 2#Dynein light intermediate chain 2; cytosolic#LIC-2#LIC53/55', '-', '-', '81655'),
(930, 'O97593', 'Structural maintenance of chromosomes protein 1A', 'GO:0000776', 143248, 'Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM; and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint (By similarity). Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase; the complex is cleaved and dissociates from chromatin; allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM; or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000250}.', 'MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRTSNIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ', 1233, 'O97593;', 'KD00930', 'Bos taurus (Bovine)', 'SMC1A', '#Structural maintenance of chromosomes protein 1A#SMC protein 1A#SMC-1A', '-', '-', '282370'),
(931, 'P54198', 'Protein HIRA', 'k', 111835, 'Cooperates with ASF1A to promote replication-independent chromatin assembly. Required for the periodic repression of histone gene transcription during the cell cycle. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {ECO:0000269|PubMed:12370293; ECO:0000269|PubMed:14718166; ECO:0000269|PubMed:15621527}.', 'MKLLKPTWVNHNGKPIFSVDIHPDGTKFATGGQGQDSGKVVIWNMSPVLQEDDEKDENIPKMLCQMDNHLACVNCVRWSNSGMYLASGGDDKLIMVWKRATYIGPSTVFGSSGKLANVEQWRCVSILRNHSGDVMDVAWSPHDAWLASCSVDNTVVIWNAVKFPEILATLRGHSGLVKGLTWDPVGKYIASQADDRSLKVWRTLDWQLETSITKPFDECGGTTHVLRLSWSPDGHYLVSAHAMNNSGPTAQIIEREGWKTNMDFVGHRKAVTVVKFNPKIFKKKQKNGSSAKPSCPYCCCAVGSKDRSLSVWLTCLKRPLVVIHELFDKSIMDISWTLNGLGILVCSMDGSVAFLDFSQDELGDPLSEEEKSRIHQSTYGKSLAIMTEAQLSTAVIENPEMLKYQRRQQQQQLDQKSAATREMGSATSVAGVVNGESLEDIRKNLLKKQVETRTADGRRRITPLCIAQLDTGDFSTAFFNSIPLSGSLAGTMLSSHSSPQLLPLDSSTPNSFGASKPCTEPVVAASARPAGDSVNKDSMNATSTPAALSPSVLTTPSKIEPMKAFDSRFTERSKATPGAPALTSMTPTAVERLKEQNLVKELRPRDLLESSSDSDEKVPLAKASSLSKRKLELEVETVEKKKKGRPRKDSRLMPVSLSVQSPAALTAEKEAMCLSAPALALKLPIPSPQRAFTLQVSSDPSMYIEVENEVTVVGGVKLSRLKCNREGKEWETVLTSRILTAAGSCDVVCVACEKRMLSVFSTCGRRLLSPILLPSPISTLHCTGSYVMALTAAATLSVWDVHRQVVVVKEESLHSILAGSDMTVSQILLTQHGIPVMNLSDGKAYCFNPSLSTWNLVSDKQDSLAQCADFRSSLPSQDAMLCSGPLAIIQGRTSNSGRQAARLFSVPHVVQQETTLAYLENQVAAALTLQSSHEYRHWLLVYARYLVNEGFEYRLREICKDLLGPVHYSTGSQWESTVVGLRKRELLKELLPVIGQNLRFQRLFTECQEQLDILRDK', 1017, 'P54198; Q05BU9; Q8IXN2;', 'KD00931', 'Homo sapiens (Human)', 'HIRA', '#Protein HIRA#TUP1-like enhancer of split protein 1', '-', 'ENSG00000149929', '-'),
(932, 'P54199', 'Serine/threonine-protein kinase MPS1', 'GO:0034501===GO:0000778===GO:0051988===GO:0031134===c;k', 86772, 'Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. Implicated in spindle pole body (SPD) duplication. Dual specificity kinase that can phosphorylate serine; threonine and tyrosine residues. Phosphorylates the SPC29 and SPC110 spindle pole body components. {ECO:0000269|PubMed:11278681; ECO:0000269|PubMed:19269975}.', 'MSTNSFHDYVDLKSRTNTRQFSDDEEFTTPPKLSNFGSALLSHTEKTSASEILSSHNNDKIANRLEEMDRSSSRSHPPPSMGNLTSGHTSTSSHSTLFGRYLRNNHQTSMTTMNTSDIEINVGNSLDKSFERIRNLRQNMKEDITAKYAERRSKRFLISNRTTKLGPAKRAMTLTNIFDEDVPNSPNQPINARETVELPLEDSHQTNFKETKRNTDYDSIDFGDLNPIQYIKKHNLPTSDLPLISQIYFDKQREENRQAALRKHSSRELLYKSRSSSSSLSSNNLLANKDNSITSNNGSQPRRKVSTGSSSSKSSIEIRRALKENIDTSNNSNFNSPIHKIYKGISRNKDSDSEKREVLRNISINANHADNLLQQENKRLKRSLDDAITNENINSKNLEVFYHRPAPKPPVTKKVEIVEPAKSASLSNNRNIITVNDSQYEKIELLGRGGSSRVYKVKGSGNRVYALKRVSFDAFDDSSIDGFKGEIELLEKLKDQKRVIQLLDYEMGDGLLYLIMECGDHDLSQILNQRSGMPLDFNFVRFYTKEMLLCIKVVHDAGIVHSDLKPANFVLVKGILKIIDFGIANAVPEHTVNIYRETQIGTPNYMAPEALVAMNYTQNSENQHEGNKWKVGRPSDMWSCGCIIYQMIYGKPPYGSFQGQNRLLAIMNPDVKIPFPEHTSNNEKIPKSAIELMKACLYRNPDKRWTVDKVLSSTFLQPFMISGSIMEDLIRNAVRYGSEKPHISQDDLNDVVDTVLRKFADYKI', 764, 'P54199; D6VRW4;', 'KD00932', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MPS1', '#Serine/threonine-protein kinase MPS1#2.7.12.2#Monopolar spindle protein 1#Regulatory cell proliferation kinase 1', '-', '-', '851533'),
(933, 'Q13185', 'Chromobox protein homolog 3', 'GO:0000779===k', 20811, 'Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at ''Lys-9''; leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 ''Lys-9'' trimethylation; mediates the recruitment of the mehtyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1.', 'MASNKTTLQKMGKKQNGKSKKVEEAEPEEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEAFLNSQKAGKEKDGTKRKSLSDSESDDSKSKKKRDAADKPRGFARGLDPERIIGATDSSGELMFLMKWKDSDEADLVLAKEANMKCPQIVIAFYEERLTWHSCPEDEAQ', 183, 'Q13185; Q96CD7; Q99409; Q9BVS3; Q9P0Z6;', 'KD00933', 'Homo sapiens (Human)', 'CBX3', '#Chromobox protein homolog 3#HECH#Heterochromatin protein 1 homolog gamma#HP1 gamma#Modifier 2 protein', '-', 'ENSG00000122565', '-'),
(934, 'Q7ZXV8', 'BUB3-interacting and GLEBS motif-containing protein ZNF207', 'GO:0000776===GO:0000777===GO:0008608', 48549, 'Kinetochore-binding protein involved in spindle-assembly checkpoint signaling by regulating mitotic chromosome alignment and mediating the stability and kinetochore loading of bub3. {ECO:0000250}.', 'MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMEERRRILEQKTQVDGQKKKTNQDDSDYDDDDDTAPSTSFQQMQTQQAFMPTMGQPGIPGLPGAPGMPPGITSLMPAVPPLISGIPHVMAGMHPHGMMSMGGMMHPHRPGIPPMMAGLPPGVPPPGLRPGIPPVTQAQPALSQAVVSRLPVPSTSAPALQSVPKPLFPSAGQAQAHISGPVGTDFKPLNNIPATTAEHPKPTFPAYTQSTMSTTSTTNSTASKPSTSITSKPATLTTTSATSKLVHPDEDISLEEKRAQLPKYQRNLPRPGQAPISNMGSTAVGPLGAMMAPRPGLPPQQHGMRHPLPPHGQYGAPLQGMAGYHPGTMPPFGQGPPMVPPFQGGPPRPLMGIRPPVMSQGGRY', 452, 'Q7ZXV8;', 'KD00934', 'Xenopus laevis (African clawed frog)', 'znf207', '#BUB3-interacting and GLEBS motif-containing protein ZNF207#BuGZ#Zinc finger protein 207', '-', '-', '380016'),
(935, 'P0C2N6', 'Histone-lysine N-methyltransferase SUV420H2', 'GO:0000780', 53607, 'Histone methyltransferase that specifically trimethylates ''Lys-20'' of histone H4. H4 ''Lys-20'' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1; RBL1 and RBL2).', 'MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPTLRRQHHLRSALEAFLRQRDLEAAFRALTLGGWMAHYFQNRAPRQEAALKNHIFCYLRAFLPESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEYLLRAGENDFSVMYSTRKRSAQLWLGPAAFINHDCKPNCKFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGEGAFRLQPREPELRPRPLDKYELRETKRRLQQCLDSSQQNLLSLRACSHLSPLRPDPFCAACQPSCLLPVSPHMDYLPLWLQWVPQPQPRVRPRKRRRRRRRRPRIPQASLSPDLHTACVSLHRWGGCGPHCQLRAEAMVTLHLLPQTRWTPKQDWYWARRYGLPSVVRVELSPLAPALPAAPAPAGNLGPTPTPDLIPKQALAFAPFCPPKRLRLVVSHGSIDLDINSGEP', 470, 'P0C2N6;', 'KD00935', 'Rattus norvegicus (Rat)', 'Suv420h2', '#Histone-lysine N-methyltransferase SUV420H2#2.1.1.43#Suppressor of variegation 4-20 homolog 2#Su(var)4-20 homolog 2#Suv4-20h2', '-', '-', '308345'),
(936, 'O55099', 'Aurora kinase B', 'GO:0034501===GO:0032133===GO:0000780', 39234, 'Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint; a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C; leading to retain abscission- competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin; CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA; DES/desmin; GPAF; KIF2C; NSUN2; RACGAP1; SEPT1; VIM/vimentin; GSG2/Haspin and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process; whereas histone H3 is phosphorylated at ''Ser-10'' and ''Ser-28'' during mitosis (H3S10ph and H3S28ph; respectively). AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells; inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (By similarity). {ECO:0000250}.', 'MAQKENVYPWPYGSKTSQSGLNTLPQRVLRKEPAVTPAQALMNRSNSQSTAVPGQKLTENKGATALQGSQSRQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSGTFDEQRTATIMEELSDALMYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSMPLGAKDLISKLLKHNPSQRLPLEQVSAHPWVRANSRRVLPPSAL', 343, 'O55099; Q4V8N1;', 'KD00936', 'Rattus norvegicus (Rat)', 'Aurkb', '#Aurora kinase B#2.7.11.1#Aurora 1#Aurora- and IPL1-like midbody-associated protein 1#Aurora/IPL1-related kinase 2#ARK-2#Aurora-related kinase 2#STK-1#Serine/threonine-protein kinase 12#Serine/threonine-protein kinase 5#Serine/threonine-protein kinase aurora-B', '-', '-', '114592'),
(937, 'P0C2N5', 'Histone-lysine N-methyltransferase SUV420H1', 'GO:0000780', 98668, 'Histone methyltransferase that specifically trimethylates ''Lys-20'' of histone H4. H4 ''Lys-20'' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1; RBL1 and RBL2). Plays a role in myogenesis by regulating the expression of target genes; such as EID3 (By similarity). {ECO:0000250}.', 'MKWLGDSKNMVVNGRRNGSKLSNDHQQNQSKLQHAGKDALKTGRNAVERRPNRCHGNSGFEGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHISKADSFSHNNPMRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKEHVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNRLKKLGDSSKSSDSQSVSSNTDADTTQEKDNATSNRKSSVGVKKNSKSRALTRQSMPRVPAASNSTSPKLVHMNNSRVPKKLRKPAKPLLSKIKLRNHCKRLDQKSTSRKLEMGNLVLKEPKVVLYKNLPIKKEREAEGPVHAAVGSGCLTRHAAREHRQNPGRGAHSQGDSLPCTYTTRRSLRTRTGLKETTDIKLAPSPLDGYKNGILEPYPDSGQQPTPEVLEELAPETALREEASQECPKSDSCPSRKKFRQGKPVKHLAKTEDCSPEHSFPGKDGLPDLPGPHPDQGEPSGTVRVPVSYTDSAPSPVGCSIVTPDSFTTKDSFRTAQSKKKRRVTRYDAQLILENSSGIPKLTLRRRHDSSSKTNDHESDSVNSSKISIKLSKDHESDSNLYVAKLSNGVSSGPGSSSTKLKIQLKRDEESRGPCAEGLHENGVCCSDPLSLLESQMEVDDYSQYEEDSTDDSSSSEGEEEEEDCEDDFDDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA', 883, 'P0C2N5;', 'KD00937', 'Rattus norvegicus (Rat)', 'Suv420h1', '#Histone-lysine N-methyltransferase SUV420H1#2.1.1.43#Suppressor of variegation 4-20 homolog 1#Su(var)4-20 homolog 1#Suv4-20h1', '-', '-', '361688'),
(938, 'O54864', 'Histone-lysine N-methyltransferase SUV39H1', 'k', 47754, 'Histone methyltransferase that specifically trimethylates ''Lys-9'' of histone H3 using monomethylated H3 ''Lys- 9'' as substrate. H3 ''Lys-9'' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1; CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 ''Lys-9'' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes; such as repression of MYOD1- stimulated differentiation; regulation of the control switch for exiting the cell cycle and entering differentiation; repression by the PML-RARA fusion protein; BMP-induced repression; repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex; a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone- modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation; elevation of NAD(+)/NADP(+) ratio activates SIRT1; leading to histone H3 deacetylation followed by dimethylation of H3 at ''Lys-9'' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1; contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 ''Lys-9'' trimethylation. {ECO:0000269|PubMed:11701123; ECO:0000269|PubMed:12867029; ECO:0000269|PubMed:14690609; ECO:0000269|PubMed:14690610; ECO:0000269|PubMed:14702045; ECO:0000269|PubMed:18004385; ECO:0000269|PubMed:24413057}.', 'MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF', 412, 'O54864; Q3TEW2; Q3UT51; Q8C2L3; Q9JLC7; Q9JLP8;', 'KD00938', 'Mus musculus (Mouse)', 'Suv39h1', '#Histone-lysine N-methyltransferase SUV39H1#2.1.1.43#Histone H3-K9 methyltransferase 1#H3-K9-HMTase 1#Position-effect variegation 3-9 homolog#Suppressor of variegation 3-9 homolog 1#Su(var)3-9 homolog 1', '-', '-', '20937'),
(939, 'Q9CZA6', 'Nuclear distribution protein nudE homolog 1', 'GO:0000776===GO:0000777', 38523, 'Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post- mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. {ECO:0000269|PubMed:15473967}.', 'MEDSGKTFESEEEETNYWRDLAMTYKQRAENTQEELREFQEGSREYEAELEAQLQQIETRNRDLLSENNRLRMELESVKEKFEMQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQDKPRTPMPGSGQAKRTDMAVQATGSVPSTPVAHRGPSSGLNTPGMFRRGLDSSTSGTPLTPAARISALNIVGDLLRKVGALESKLASCRNFMYDQSPSRTSGPASGRGTKNRDGVDRRPGSTSVGDKGSGKRLEFGKPASEPASPALPSAQGVVKLLL', 344, 'Q9CZA6; Q3UBS6; Q3UIC1; Q9ERR0;', 'KD00939', 'Mus musculus (Mouse)', 'Nde1', '#Nuclear distribution protein nudE homolog 1#NudE#mNudE', '-', '-', '67203'),
(940, 'Q24246', 'Cytoplasmic dynein 1 intermediate chain', 'GO:0034501===GO:0005868', 73917, '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 help dynein bind to dynactin 150 kDa component (By similarity). {ECO:0000250}.', 'MDRKAELERKKAKLAALREEKDRRRREKEIKDMEEAAGRIGGGAGIDKDQRKDLDEMLSSLGVAPVSEVLSSLSSVNSMTSDNSNTQTPDASLQATVNGQSGGKKQPLNLSVYNVQATNIPPKETLVYTKQTQTTSTGGGNGDVLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFTDDEESSLQNLGNGFTSKLPPGYLTHGLPTVKDVAPAITPLEIKKETEVKKEVNELSEEQKQMIILSENFQRFVVRAGRVIERALSENVDIYTDYIGGGDSEEANDERSHARLSLNRVFYDERWSKNRCITSMDWSTHFPELVVGSYHNNEESPNEPDGVVMVWNTKFKKSTPEDVFHCQSAVMSTCFAKFNPNLILGGTYSGQIVLWDNRVQKRTPIQRTPLSAAAHTHPVYCLQMVGTQNAHNVISISSDGKLCSWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEINSLVMGSEDGYVYSASRHGLRSGVNEVYERHLGPITGISTHYNQLSPDFGHLFLTSSIDWTIKLWSLKDTKPLYSFEDNSDYVMDVAWSPVHPALFAAVDGSGRLDLWNLNQDTEVPTASIVVAGAPALNRVSWTPSGLHVCIGDEAGKLYVYDVAENLAQPSRDEWSRFNTHLSEIKMNQSDEV', 663, 'Q24246; O96508; O96510; O96511; O96512; O96513; O96514; O96515;O96516; Q5U0Z1; Q86BQ5; Q9NG49; Q9TZR7; Q9TZR8; Q9TZR9; Q9TZS0;Q9VR78;', 'KD00940', 'Drosophila melanogaster (Fruit fly)', 'sw', '#Cytoplasmic dynein 1 intermediate chain#DH IC#Dynein intermediate chain; cytosolic#Protein short wing', '-', '-', '44160'),
(941, 'Q9V3V7', 'Kinetochore protein Spc25', 'GO:0000776===GO:0000777===GO:0031262===SCL===k', 25742, '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. {ECO:0000269|PubMed:17333235; ECO:0000269|PubMed:17895365}.', 'MAIIMTESSYERRVKALYEKQIHMEALEAKFIKKVFKFNSNLLDVKEAASRHQRKVGKLQKVLMERREELDKRVSFIEELDRELEATKLHNLAMKDWFKQQKMLAKQRKNEIMESIHTLSKTTRTYINQEALPARVKGVTVLRGDKRDQLIPFDLKATDVEGLDSLCQHLESLNVDVAQWQQLISLAMDMAMESRAPTTPPKEADNCKSIIEIDLTSPMSHT', 222, 'Q9V3V7;', 'KD00941', 'Drosophila melanogaster (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000303|PubMed:17895365; ECO:0000312|EMBL:AAF54875.1}#Chromosome alignment defect 2 {ECO:0000303|PubMed:17412918}#Mitotic chaos {ECO:0000303|PubMed:17895365}', '-', '-', '41585'),
(942, 'P61287', 'Serine/threonine-protein phosphatase PP1-gamma catalytic subunit', 'GO:0000777', 36984, '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. In balance with CSNK1D and CSNK1E; determines the circadian period length; through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E (By similarity). {ECO:0000250}.', 'MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK', 323, 'P61287; Q08DZ0;', 'KD00942', 'Bos taurus (Bovine)', 'PPP1CC', '#Serine/threonine-protein phosphatase PP1-gamma catalytic subunit#PP-1G#3.1.3.16#Protein phosphatase 1C catalytic subunit', '-', '-', '282318'),
(943, 'P61285', 'Dynein light chain 1; cytoplasmic', 'GO:0000776===GO:0005868', 10366, 'Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity). {ECO:0000250}.', 'MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG', 89, 'P61285; Q6B859;', 'KD00943', 'Bos taurus (Bovine)', 'DYNLL1', '#Dynein light chain 1; cytoplasmic#Dynein light chain LC8-type 1', '-', '-', '101905447'),
(944, 'Q8IZT6', 'Abnormal spindle-like microcephaly-associated protein', 'c;k;m;s', 409800, 'Probable role in mitotic spindle regulation and coordination of mitotic processes. May have a preferential role in regulating neurogenesis. {ECO:0000269|PubMed:12355089; ECO:0000269|PubMed:15972725}.', 'MANRRVGRGCWEVSPTERRPPAGLRGPAAEEEASSPPVLSLSHFCRSPFLCFGDVLLGASRTLSLALDNPNEEVAEVKISHFPAADLGFSVSQRCFVLQPKEKIVISVNWTPLKEGRVREIMTFLVNDVLKHQAILLGNAEEQKKKKRSLWDTIKKKKISASTSHNRRVSNIQNVNKTFSVSQKVDRVRSPLQACENLAMNEGGPPTENNSLILEENKIPISPISPAFNECHGATCLPLSVRRSTTYSSLHASENRELLNVHSANVSKVSFNEKAVTETSFNSVNVNGQRGENSKLSLTPNCSSTLNITQSQIHFLSPDSFVNNSHGANNELELVTCLSSDMFMKDNSQPVHLESTIAHEIYQKILSPDSFIKDNYGLNQDLESESVNPILSPNQFLKDNMAYMCTSQQTCKVPLSNENSQVPQSPEDWRKSEVSPRIPECQGSKSPKAIFEELVEMKSNYYSFIKQNNPKFSAVQDISSHSHNKQPKRRPILSATVTKRKATCTRENQTEINKPKAKRCLNSAVGEHEKVINNQKEKEDFHSYLPIIDPILSKSKSYKNEVTPSSTTASVARKRKSDGSMEDANVRVAITEHTEVREIKRIHFSPSEPKTSAVKKTKNVTTPISKRISNREKLNLKKKTDLSIFRTPISKTNKRTKPIIAVAQSSLTFIKPLKTDIPRHPMPFAAKNMFYDERWKEKQEQGFTWWLNFILTPDDFTVKTNISEVNAATLLLGIENQHKISVPRAPTKEEMSLRAYTARCRLNRLRRAACRLFTSEKMVKAIKKLEIEIEARRLIVRKDRHLWKDVGERQKVLNWLLSYNPLWLRIGLETTYGELISLEDNSDVTGLAMFILNRLLWNPDIAAEYRHPTVPHLYRDGHEEALSKFTLKKLLLLVCFLDYAKISRLIDHDPCLFCKDAEFKASKEILLAFSRDFLSGEGDLSRHLGLLGLPVNHVQTPFDEFDFAVTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIPAISRLQKMHNVDIVLQVLKSRGIELSDEHGNTILSKDIVDRHREKTLRLLWKIAFAFQVDISLNLDQLKEEIAFLKHTKSIKKTISLLSCHSDDLINKKKGKRDSGSFEQYSENIKLLMDWVNAVCAFYNKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVECTQTGSVVLNSSSESDDSSLDMSLKAFDHENTSELYKELLENEKKNFHLVRSAVRDLGGIPAMINHSDMSNTIPDEKVVITYLSFLCARLLDLRKEIRAARLIQTTWRKYKLKTDLKRHQEREKAARIIQLAVINFLAKQRLRKRVNAALVIQKYWRRVLAQRKLLMLKKEKLEKVQNKAASLIQGYWRRYSTRQRFLKLKYYSIILQSRIRMIIAVTSYKRYLWATVTIQRHWRAYLRRKQDQQRYEMLKSSTLIIQSMFRKWKQRKMQSQVKATVILQRAFREWHLRKQAKEENSAIIIQSWYRMHKELRKYIYIRSCVVIIQKRFRCFQAQKLYKRRKESILTIQKYYKAYLKGKIERTNYLQKRAAAIQLQAAFRRLKAHNLCRQIRAACVIQSYWRMRQDRVRFLNLKKTIIKFQAHVRKHQQRQKYKKMKKAAVIIQTHFRAYIFAMKVLASYQKTRSAVIVLQSAYRGMQARKMYIHILTSVIKIQSYYRAYVSKKEFLSLKNATIKLQSTVKMKQTRKQYLHLRAAALFIQQCYRSKKIAAQKREEYMQMRESCIKLQAFVRGYLVRKQMRLQRKAVISLQSYFRMRKARQYYLKMYKAIIVIQNYYHAYKAQVNQRKNFLQVKKAATCLQAAYRGYKVRQLIKQQSIAALKIQSAFRGYNKRVKYQSVLQSIIKIQRWYRAYKTLHDTRTHFLKTKAAVISLQSAYRGWKVRKQIRREHQAALKIQSAFRMAKAQKQFRLFKTAALVIQQNFRAWTAGRKQCMEYIELRHAVLVLQSMWKGKTLRRQLQRQHKCAIIIQSYYRMHVQQKKWKIMKKAALLIQKYYRAYSIGREQNHLYLKTKAAVVTLQSAYRGMKVRKRIKDCNKAAVTIQSKYRAYKTKKKYATYRASAIIIQRWYRGIKITNHQHKEYLNLKKTAIKIQSVYRGIRVRRHIQHMHRAATFIKAMFKMHQSRISYHTMRKAAIVIQVRCRAYYQGKMQREKYLTILKAVKVLQASFRGVRVRRTLRKMQTAATLIQSNYRRYRQQTYFNKLKKITKTVQQRYWAMKERNIQFQRYNKLRHSVIYIQAIFRGKKARRHLKMMHIAATLIQRRFRTLMMRRRFLSLKKTAILIQRKYRAHLCTKHHLQFLQVQNAVIKIQSSYRRWMIRKRMREMHRAATFIQSTFRMHRLHMRYQALKQASVVIQQQYQANRAAKLQRQHYLRQRHSAVILQAAFRGMKTRRHLKSMHSSATLIQSRFRSLLVRRRFISLKKATIFVQRKYRATICAKHKLYQFLHLRKAAITIQSSYRRLMVKKKLQEMQRAAVLIQATFRMYRTYITFQTWKHASILIQQHYRTYRAAKLQRENYIRQWHSAVVIQAAYKGMKARQLLREKHKASIVIQSTYRMYRQYCFYQKLQWATKIIQEKYRANKKKQKVFQHNELKKETCVQAGFQDMNIKKQIQEQHQAAIIIQKHCKAFKIRKHYLHLRATVVSIQRRYRKLTAVRTQAVICIQSYYRGFKVRKDIQNMHRAATLIQSFYRMHRAKVDYETKKTAIVVIQNYYRLYVRVKTERKNFLAVQKSVRTIQAAFRGMKVRQKLKNVSEEKMAAIVNQSALCCYRSKTQYEAVQSEGVMIQEWYKASGLACSQEAEYHSQSRAAVTIQKAFCRMVTRKLETQKCAALRIQFFLQMAVYRRRFVQQKRAAITLQHYFRTWQTRKQFLLYRKAAVVLQNHYRAFLSAKHQRQVYLQIRSSVIIIQARSKGFIQKRKFQEIKNSTIKIQAMWRRYRAKKYLCKVKAACKIQAWYRCWRAHKEYLAILKAVKIIQGCFYTKLERTRFLNVRASAIIIQRKWRAILPAKIAHEHFLMIKRHRAACLIQAHYRGYKGRQVFLRQKSAALIIQKYIRAREAGKHERIKYIEFKKSTVILQALVRGWLVRKRFLEQRAKIRLLHFTAAAYYHLNAVRIQRAYKLYLAVKNANKQVNSVICIQRWFRARLQEKRFIQKYHSIKKIEHEGQECLSQRNRAASVIQKAVRHFLLRKKQEKFTSGIIKIQALWRGYSWRKKNDCTKIKAIRLSLQVVNREIREENKLYKRTALALHYLLTYKHLSAILEALKHLEVVTRLSPLCCENMAQSGAISKIFVLIRSCNRSIPCMEVIRYAVQVLLNVSKYEKTTSAVYDVENCIDILLELLQIYREKPGNKVADKGGSIFTKTCCLLAILLKTTNRASDVRSRSKVVDRIYSLYKLTAHKHKMNTERILYKQKKNSSISIPFIPETPVRTRIVSRLKPDWVLRRDNMEEITNPLQAIQMVMDTLGIPY', 3477, 'Q8IZT6; Q4G1H1; Q5VYL3; Q86UX4; Q8IUL2; Q8IZJ7; Q8IZJ8; Q8IZJ9;Q8N4D1; Q9NVS1; Q9NVT6;', 'KD00944', 'Homo sapiens (Human)', 'ASPM', '#Abnormal spindle-like microcephaly-associated protein#Abnormal spindle protein homolog#Asp homolog', '-', 'ENSG00000066279', '-'),
(945, 'Q923A2', 'Protein Spindly', 'GO:0043515===GO:0034501===GO:0000940', 70237, 'Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. {ECO:0000255|HAMAP-Rule:MF_03041}.', 'MEADITNLRNKLKECEDERLKAAHYGLQLLERQTELQSQLDKCHEEMMITAEKYNQEKHALQREVELKSRMLDSLSCECEALKQQQKAQLEQLEVQLHRSHRQEVSDLKNKLENLKVELDEARLGEKQLKQKLDLQGELLAHKSEELRLLSEQRVLSSMSSELLALETELTAAEGVKNALKEEVNELQYKQEQLECLNTSLLHQVDRLKEEKEEREREAVSYYNALEKARVENQDLQVQLGHALQQAADPNSKGNSLFAEVEDRRVAMERQLNLMKDKYQSLKKQNAFTRDQMNKMKLQISTLLRMRGSQTEFEQQERLFAMIEQKNGEIKHLLGEINKLEKFKNLYESMESRPSTSDTACVLEDSTYYSDLLQLKLDKLNKENESTKDELSIQRMKALFESQRALDIERKLFTNERHLQLSESENMKLRAKLDELKLKYEPEERIEVPVLKRRREVLPLNITTPEETEETAAASATEDGVSRLPPHREEESCLNSLKDNTVQWKQPASSCVQPASLSPHKNLHLDTQPKKEKKCVKLVDSPANIEVLHEQSGNTPNSPRLTAESKLPTEVKERIETTSKLGKGACKKSHNIIYVSSKSAPETQCSQQ', 608, 'Q923A2; Q5DY45;', 'KD00945', 'Mus musculus (Mouse)', 'Spdl1', '#Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041}#Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041}#Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041}', '-', '-', '70385'),
(946, 'Q9BU64', 'Centromere protein O', 'GO:0000777===k', 33786, 'Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Modulates the kinetochore-bound levels of NDC80 complex. {ECO:0000269|PubMed:16622420; ECO:0000269|PubMed:16716197; ECO:0000269|PubMed:16932742; ECO:0000269|PubMed:18007590}.', 'MEQANPLRPDGESKGGVLAHLERLETQVSRSRKQSEELQSVQAQEGALGTKIHKLRRLRDELRAVVRHRRASVKACIANVEPNQTVEINEQEALEEKLENVKAILQAYHFTGLSGKLTSRGVCVCISTAFEGNLLDSYFVDLVIQKPLRIHHHSVPVFIPLEEIAAKYLQTNIQHFLFSLCEYLNAYSGRKYQADRLQSDFAALLTGPLQRNPLCNLLSFTYKLDPGGQSFPFCARLLYKDLTATLPTDVTVTCQGVEVLSTSWEEQRASHETLFCTKPLHQVFASFTRKGEKLDMSLVS', 300, 'Q9BU64; B2RDC0; D6W536; Q53T55; Q96JV3;', 'KD00946', 'Homo sapiens (Human)', 'CENPO', '#Centromere protein O#CENP-O#Interphase centromere complex protein 36', '-', 'ENSG00000138092', '-'),
(947, 'P52732', 'Kinesin-like protein KIF11', 'GO:0003777', 119159, 'Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays. {ECO:0000269|PubMed:19001501}.', 'MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL', 1056, 'P52732; A0AV49; B2RMV3; Q15716; Q5VWX0;', 'KD00947', 'Homo sapiens (Human)', 'KIF11', '#Kinesin-like protein KIF11#Kinesin-like protein 1#Kinesin-like spindle protein HKSP#Kinesin-related motor protein Eg5#Thyroid receptor-interacting protein 5#TR-interacting protein 5#TRIP-5', '-', 'ENSG00000138160', '-'),
(948, 'Q6YUL8', 'Kinesin-like protein BC2', 'GO:0003777', 116386, 'Microtubule-dependent motor protein involved in the control of the oriented deposition of cellulose microfibrils (PubMed:20444225; PubMed:21325138). Involved in wall biogenesis and modification; and contributes to cell-cycle progression and cell division (PubMed:20444225). Acts as a transcriptional activator in gibberellic acid (GA) biosynthesis pathway. Binds specifically to the DNA sequence 5''-ACCAACTTGAA-3'' of the ent- kaurene oxidase 2 (CYP701A6 or OsKO2) promoter. May regulate CYP701A6 gene expression and mediates cell elongation by regulating the GA biosynthesis pathway (PubMed:21325138). {ECO:0000269|PubMed:20444225; ECO:0000269|PubMed:21325138}.', 'MTMEHGEDCCVKVAVHVRPLIGDEKLQGCKDCVSVVSGKPQVQIGSHSFTFDHVYGSSGTPSAAMFEECVAPLVDGLFQGYNATVLAYGQTGSGKTYTMGTACKEGSHIGIIPRAMATLFDKIDKLKNQVEFQLRVSFIEILKEEVRDLLDPATAAVGKLENGNGHATKLSVPGKPPVQIREASNGVITLAGSTEVHVTTQKEMTACLEQGSLSRATGSTNMNNQSSRSHAIFTITLEQMRKADPIMTLDGMPIEEMNEDYLCAKLHLVDLAGSERAKRTGSDGLRFKEGVHINRGLLALGNVISALGDEKKRKEGAHVPYRDSKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQNKPIVNRNPVADEMKRMRQQIEYLQAELVSARGGVVLDDVQGLRERISMLEQKNEDLCRELYDLRNHGYTDPCEPELQKIGTGYTKGEGLKRSLQSTEPFDVPMTDSVRAGSPKDIDDEVAKEWEHTMLQDSMGKELNELNRQLEQKESEMKMYGSDTVALKQHFGKKLLELEEEKRAVQQERDRLLAEVESLNADGQTHKLRDAQLQKLKTLEAQILDLKKKQENQVQLLKEKQKSDEAAKKLQEEIHSIKAQKVQLQHKIKQEAEQFRQWKATREKELLQLRKEGRRNEYERHKLQALNQRQKLVLQRKTEEAAMATKRLKELLEARKSSGRDNSGMNGTSPGSHMTEKSLQKWLEQDLEVMVHVHEVRNEYEKQSQLRAALGEELAILKQEDVMSGAASPPRGKNGNSRANTLSPNARQARIASLESMVTISSNTLVAMASQLSEAEERERAFSGRGRWNQLRSMAEAKSLLQYIFNVAADARCQVREKEMEIKEMKEQMTELVTILRHSESRRRETEKQLKQREQAAVTATTSPGNGNGSVKHSADDSNTPLSPVAVPAQKQLKYSAGIVNSPSKGVPAFNKQHLKMVPMAQLPVGKKVSIAGQSGKLWRWKRSHHQWLLQFKWKWQKPWKLSEMIRHSDETMTRTRPRPQLLPHRPQRVM', 1035, 'Q6YUL8; B9G250; Q6YUL7;', 'KD00948', 'Oryza sativa subsp. japonica (Rice)', 'BC2', '#Kinesin-like protein BC2 {ECO:0000305}#Protein BRITTLE CULM 2#Protein GIBBERELLIN-DEFICIENT DWARF 1', '-', '-', '4346402'),
(949, 'Q960Z0', 'Kinesin-like protein Klp10A', 'GO:0005828===GO:0003777===c;k', 88672, 'Required during anaphase to drive sister chromatid separation to promote flux by actively depolymerizing kinetochore microtubules at their pole-associated minus ends; thereby moving chromatids through a "poleward flux". {ECO:0000269|PubMed:14681690; ECO:0000269|PubMed:20946984; ECO:0000269|PubMed:24100293}.', 'MDMITVGQSVKIKRTDGRVHMAVVAVINQSGKCITVEWYERGETKGKEVELDAILTLNPELMQDTVEQHAAPEPKKQATAPMNLSRNPTQSAIGGNLTSRMTMAGNMLNKIQESQSIPNPIVSSNSVNTNSNSNTTAGGGGGTTTSTTTGLQRPRYSQAATGQQQTRIASAVPNNTLPNPSAAASAGPAAQGVATAATTQGAGGASTRRSHALKEVERLKENREKRRARQAEMKEEKVALMNQDPGNPNWETAQMIREYQSTLEFVPLLDGQAVDDHQITVCVRKRPISRKEVNRKEIDVISVPRKDMLIVHEPRSKVDLTKFLENHKFRFDYAFNDTCDNAMVYKYTAKPLVKTIFEGGMATCFAYGQTGSGKTHTMGGEFNGKVQDCKNGIYAMAAKDVFVTLNMPRYRAMNLVVSASFFEIYSGKVFDLLSDKQKLRVLEDGKQQVQVVGLTEKVVDGVEEVLKLIQHGNAARTSGQTSANSNSSRSHAVFQIVLRPQGSTKIHGKFSFIDLAGNERGVDTSSADRQTRMEGAEINKSLLALKECIRALGKQSAHLPFRVSKLTQVLRDSFIGEKSKTCMIAMISPGLSSCEHTLNTLRYADRVKELVVKDIVEVCPGGDTEPIEITDDEEEEELNMVHPHSHQLHPNSHAPASQSNNQRAPASHHSGAVIHNNNNNNNKNGNAGNMDLAMLSSLSEHEMSDELIVQHQAIDDLQQTEEMVVEYHRTVNATLETFLAESKALYNLTNYVDYDQDSYCKRGESMFSQLLDIAIQCRDMMAEYRAKLAKEEMLSCSFNSPNGKR', 805, 'Q960Z0;', 'KD00949', 'Drosophila melanogaster (Fruit fly)', 'Klp10A', '#Kinesin-like protein Klp10A#Kinesin-like protein at cytological position 10A', '-', '-', '32049'),
(950, 'Q09933', 'Phosphoprotein p93', 'GO:0000778===GO:0051315===c;k', 97546, 'Has a role in sister chromatid separation. {ECO:0000269|PubMed:7628693}.', 'MELDDFNSRILSQIFDKSWKVRFEAYESLLHALNRALDDSDVCFQPWIHDPALWKQGLCDSNVPTQEHAVKSLRCFLDKSRQKGVNSAKSFVVAPLLEKCLPSPRQSIRDASHQALLILAKSDALDYVLEGLFSAARVKHPKQAVASIKELNSLLENFGIPALSPIPFYKLIPTLFAQSDKNIRQEASNLSITLYAWVGNAFKTHVFPQLKQIQVSDLEASFQNVTSRTTTGGHISNSLNTQEVVLPSFSSNAKPKPHLSSKSSSQGNTLQRSTSSFSTPNRKVSQPSDFSASPSRSIVSPAKNIVGSTPVDVLSKLTPEFHTALSSPKWKDRKEALESMVPVCSNPVYQEGDYSELLRVIAKSLKDANVVVVGVAALLLTHIAKALRKGFLPYTGIVLPSLFDRFKERKSSLVHSLLDAANAIFESCGLNDIMDETLEFLKHKNPQVKTETLRWLNRCLQLTDVCPPRASLETLCSLCVTLINDTFEPVRMATTNVLATLVQIFSQPVLSKYIVGLDPKKLPKILELSKDITVNAHPNQPSRPRLPRVASPLKTSPVKLAVTPQAPSPLPSSNPSQASLTEESLSTRSSPTKPSTTSLRSQSLVNRFASSTLKAPSSSSKGVSNAASSKQSFPSSPSISKKLETSRLSTKKLPGSTMKAASALKEYPQQQSMKSGGEKQDNLVTITMSEKVELDLLREEKAIRQVQEAEDALERERLFREINDLQIQNAEMKEQVYEKESTISQKEVEITSLRNEKDRLSTRLQQVLLELEKQHETNEEAMDIDLKVPESGAIGRVTTRATATTAMDESGNAGMVSSGIHSVSTKPSSYGTRRSLAGSMLQKPTQFSRPSFMFSPEARDNWRESHDLSSHLWEQIQRMKKA', 882, 'Q09933;', 'KD00950', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dis1', '#Phosphoprotein p93', '-', '-', '2539505'),
(951, 'Q92831', 'Histone acetyltransferase KAT2B', 'GO:0000776===k', 93013, '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. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection; it is recruited by the viral protein Tat. Regulates Tat''s transactivating activity and may help inducing chromatin remodeling of proviral genes. 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:10675335; ECO:0000269|PubMed:14645221; ECO:0000269|PubMed:23932781; ECO:0000269|PubMed:8684459; ECO:0000269|PubMed:9707565}.', 'MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK', 832, 'Q92831; Q6NSK1;', 'KD00951', 'Homo sapiens (Human)', 'KAT2B', '#Histone acetyltransferase KAT2B#2.3.1.48#Histone acetyltransferase PCAF#Histone acetylase PCAF#Lysine acetyltransferase 2B#P300/CBP-associated factor#P/CAF', '-', 'ENSG00000114166', '-'),
(952, 'Q7Z4S6', 'Kinesin-like protein KIF21A', 'GO:0003777', 187179, 'Microtubule-binding motor protein probably involved in neuronal axonal transport. In vitro; has a plus-end directed motor activity (By similarity). {ECO:0000250}.', 'MLGAPDESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHIAIKNGLPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADNATDNKIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDRASQQINALRSEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLVSDQANHVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARAPYFSGSSTFSPTILSSDKETIEIIDLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINACTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQDLDSVPLENVEDSTDEDAPLNSPGSEGSTLSSDLMKLCGEVKPKNKARRRTTTQMELLYADSSELASDTSTGDASLPGPLTPVAEGQEIGMNTETSGTSAREKELSPPPGLPSKIGSISRQSSLSEKKIPEPSPVTRRKAYEKAEKSKAKEQKHSDSGTSEASLSPPSSPPSRPRNELNVFNRLTVSQGNTSVQQDKSDESDSSLSEVHRSSRRGIINPFPASKGIRAFPLQCIHIAEGHTKAVLCVDSTDDLLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVSTSYIKVWDIRDSAKCIRTLTSSGQVTLGDACSASTSRTVAIPSGENQINQIALNPTGTFLYAASGNAVRMWDLKRFQSTGKLTGHLGPVMCLTVDQISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNFEPPHYDGIEALTIQGDNLFSGSRDNGIKKWDLTQKDLLQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICVNSTHIFTAADDRTVRIWKARNLQDGQISDTGDLGEDIASN', 1674, 'Q7Z4S6; A8MX28; B0I1R9; B9EGE4; F5H0C3; F5H219; Q2UVF1; Q6UKL9;Q7Z668; Q86WZ5; Q8IVZ8; Q9C0F5; Q9NXU4; Q9Y590;', 'KD00952', 'Homo sapiens (Human)', 'KIF21A', '#Kinesin-like protein KIF21A#Kinesin-like protein KIF2#Renal carcinoma antigen NY-REN-62', '-', 'ENSG00000139116', '-'),
(953, 'Q9D4J7', 'PHD finger protein 6', 'GO:0000777', 41139, 'Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000250}.', 'MSSSIEQKKGSTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMVYCRKHKKTAHNSEADLEESFNEHELEPSSPKTKKKSRKGRPRKTNLKGLPEDSRSTSSHGTDEMESSSYRDRSPHRSSPNDTRPKCGFCHVGEEENEARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMKCTLCSQPGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNHSGNDERDEEDEERESKSRGRVAIDQQLTQQQLNGN', 364, 'Q9D4J7; Q80T86; Q8BYT8; Q8C1B5;', 'KD00953', 'Mus musculus (Mouse)', 'Phf6', '#PHD finger protein 6', '-', '-', '70998'),
(954, 'Q9P802', 'Kinetochore protein mis18', 'GO:0051382===GO:0000778===GO:0061638===k', 22542, 'Required for correct chromosome segregation where it has a role in the formation and/or maintenance of specialized chromatin at the centromere. Has a role in kinetochore assembly and CENP-A loading. Maintains the deacetylated state of histones specifically in the central core of the centromeres. {ECO:0000269|PubMed:15369671}.', 'MSQTETSHSGYIDFKKESQPSVFQCKKCFQIVGDSNAWVISHREYLSFTLSDAVENSVRVEDTFKRSDDGLCVYSELSCTRCNEVIGKVYNSTPIYLDDIRDMYTFSMDKLQAYQLGNKTVNPEGLTRYQVDLEMREDIIKLKSFCLSLYEKFELHDETLRSVKETISSLKKPKIEGKEGKKEKARTYSKRTRK', 194, 'Q9P802;', 'KD00954', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis18', '#Kinetochore protein mis18', '-', '-', '2538763'),
(955, 'H2L0I2', 'LFI-1; isoform a', 'k', 273876, '', 'MFFSCGVNSSSPGRQLVVSESVSEDNLHNPSSHALRTLSPVSPPTANSSSSTSRSCSPVVRAETIVAGKWTHISGKVSVRPLTPSETESVLDRQRQKNRRSSRKDKLKMSTHDDTRSSGGGDGTIHIPSADAKEPTPESPGSRSNYGEFYWDTSGENNYHHTSSFDDDLLLEIDSSRGAAVARLDRTQDDLNKFRQRIDNNVEQQREYSEMMAALQNKVHEYRKHIAELEGRMVGARNRMLDDPTSNVMIFDNYDPGNTYITNHNVELWSPARGKRETILGGGGAPGLTTVNVHAGAGYSGSGVAGYGGGVQAMVGDPNANYEMIARLDEERRRSDEYRMQWENERQKSLSLEDENDRLRREFERYANDSKDKEKTFINRERNLAQYLSDEQRKMLDLWTELQRVRKQFSDLKTHTEEDLDKQKAEFTRAIRNVNNISRNAAFSAGAGDGLGLYGLEDGGDVNRTTNNYEKVFIETIKRMNGTGGAGSASSADLLEELRKIRGGGSSEGDAELHKELMTKYEESIERNIELESRGDDSQRKIAELEAELRRNREKLNEAQGALKKLHEMAQDSEKNVDGTVSIKRTRSLSPGKTPLPPSEALRAVRNTFRNKDNDIQQLERKLKIAESQVKEFLNKFENADEARRRLDKQFADAKREISNLQKSVDEAERNSRRTDDKLRASEAERVAAEKARKFLEDELAKLQASFQKSSTDDARKLRDEMDEHTNSIQEEFKTRIDELNRRVENLLRENNRLKSEVNPLKDKYRDLENEYNSTQRRIEEKETQIRYSDDIRRNIQKDLDDLREKYDRVHTDNEKILGELEHAQKAAHLAEQQLKEIKIQRDDYQKQKDEHARHLFDIRHKLETEIKGRQDLEKNGARNNDELDKLRQTISDYESQINLLRRHNDELDTTIKGHQGKITHLENELHSRSGEIEKLNDLNQRLQKEKQDILNQKLKLDGDVQALKETIRKLENELEKLRNENKELVGKEARARDAANQQLSRANLLNKELEDTKQDLKHSTDVNKQLEQDIRDLKERLANIGKGGRISRDSTTGTDGGAFGDRSSVADPSRTRGAAGSTVFVPAAEDIESRGGGEIDIPSSGDVIHGRDGRDGRDAGNRGTHTITNTKERIERIEKNILDRYHDDELVEHKIREVNDRWKRELERLENEKDDLERRIRELEDELSQIGRGNDKTENDITELKRKHAAEIDKLKSDISALHDKHLSDLDDEKEQYGKAVENLKSVEDDLRDKLNNLEKQLADSLNRENELEREKRDYDEKINSLYGQNQKIKDEWDDFRNDADKEIQKWKTDAYTVRSEAKALETTNTALKAQLQAANDRIDHLTKTVNDHTSKVRDLTSQVRHLEDELADTKGNLVQKEMDLESTQNRLRSLEDQHSTLQSDANKWRGELDAALRENDILKSNNTNMETDLTRLKNRLKSAEDALKELKNSLSHAKTEKERLQNAFREKTKQADHLNQLASQFDTKLTKLRNELQDTNDKLITSDTERNALRNELQKLSQELKFGNEQIQRKSDEYQTTIDDLAHSHRVSEDSRLNALQELEARKYEINDLTSRLDSTEQRLATLQQDYIKADSERDILSDALRRFQSSANRVINFHTFVDGGAGYVDGVPGGTSVIGGGPSAQRSGAYDPSSGGVIGSGISGGPGGSDFGREIEIGRGDSDQSDVAYPRSVPFPPSADFSSGRPGAASAGGRVINNLDGTTTVNMNGGFDIANLEGTLQSLLNKIEKLEMERNELRDTLARMKKKTTETHTTINQKETRYRNIEDNLQDAEEERRALESRLQSAKTLLRSQEEALKQRDEERRQMKSKMVAAELQARGKEAQLRHLNEQLKNLRTDLDNAHTDIRSLRDKEEQWDSSRFQLETKMRESDSDTNKYQLQIASFESERQILTEKIKELDGALRLSDSKVQDMKDDTDKLRRDLTKAESVENELRKTIDIQSKTSHEYQLLKDQLLNTQNELNGANNRKQQLENELLNVRSEVRDYKQRVHDVNNRVSELQRQLQDANTEKNRVEDRFLSVEKVVNTMRTTETDLRQQLETAKNEKRVATKELEDLKRRLAQLENERRNSSQLSDGWKKEKITLLKKIELLENEKRRTDAAIRETALQREAIEKSLNAMERENKELYKNCAQLQQQIAQLEMENGNRILELTNKQREEQERQLIRMRQEKGQIEKVIENRERTHRNRIKQLEDQIAILRDQLDGERRRRREYVDRSMVNDIGRLGSNVLGIRNSYGDNSIDAIINGGSRSVGFYPRSTFASNPLTPPLGSSTPTHRPHVTDFRSAVDAGSSYRRPISTIEDSGSVYGGSIRDRDSVYGGGGRDSSFGTRAGDSISRAGVEPRDPSLVEIPSNEPPMTTSTHSQGGSRYDTLAPNRDDL', 2396, 'H2L0I2;', 'KD00955', 'Caenorhabditis elegans', 'lfi-1', '#LFI-1; isoform a {ECO:0000313|EMBL:CCD73129.1}', '-', '-', '180771'),
(956, 'Q9URY2', 'Microtubule protein alp7', 'GO:0000778===c;k', 53175, 'Required for bipolar spindle formation and proper chromosome segregation. Has an indirect role in connecting the kinetochores and the plus end of pole to chromosome microtubules by targeting alp14 to the spindle pole body. Involved in the emergence of large microtubule organizing centers (MTOC) in interphase cells. Attaches to the minus ends of microtubules and associates with the sites of microtubule attachment on the nuclear envelope. This leads to the stabilzation of the microtubule bundles. {ECO:0000269|PubMed:14742702; ECO:0000269|PubMed:16481403}.', 'MSDIVSSSTDYSRRSPSSSSIGTNETDHTGFHEKRQGASSESLIPPAQRSSEESMPAPKLFPKLTSKPNPQLNLKDTLNKRVSDRLQALELNKSFDFSGTPRPMHPISHPLSQHKTPEFKHRKRNVESILTPKNPSLFSSSNAASQRGSLNTAPSNFAYSHSSSLQTSASSRPPVLSNGSFPRQTNTAPLNPPVHLKDNIRNSATPSTSQADIPTQYPINSTQKQQAKYEAEIEGYKAKLAGTYHEISVLQNTIVNVSGQLIAVNDQLQQLRSGKASTSPSTKDTNMRLVEGHNEETLALQRGKYTQEEVDKLIQERMEKVAEDLHAQYSAKHTQKINAFKANYARKYEATIQELQNQIGTAPNAPKISNSNWEEERRALKADNQTLQKQLEKAIQERQDMSDFLNNFKADMAKSDKLLMQQQSQQTGDLETLRLQLQALQEELRVEREERQQLIQMSEDLVIAMDQLNLEQKS', 474, 'Q9URY2; Q9UU56;', 'KD00956', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'alp7', '#Microtubule protein alp7#Altered polarity protein 7#Transforming acidic coiled-coil protein mia1#TACC protein mia1', '-', '-', '2543382');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(957, 'Q91783', 'Kinesin-like protein KIF11-A', 'GO:0003777', 119885, 'Plus end-directed motor protein required for establishing a bipolar spindle. Associates with both interphase and spindle microtubules. May be involved in nuclear divisions taking place during the development of unfertilized eggs. {ECO:0000269|PubMed:15583027}.', 'MSSQNSFMSSKKDDKGKNIQVVVRCRPFNQLERKASSHSVLECESQRKEVCVRTGEVNDKLGKKTYTFDMVFGPAAKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSSDEEFTWEQDPLAGIIPRTLHQIFEKLSEIGTEFSVKVSLLEIYNEELFDLLSPSPDVGERLQMFDDPRNKRGVIIKGLEEISVHNKDEVYQILERGAAKRKTASTLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHIPYRESKLTRILQDSLGGRTKTSIIATVSPASINLEETMSTLDYASRAKNIMNKPEVNQKLTKKALIKEYTEEIERLKRELATAREKNGVYLSNENYEQLQGKVLSQEEMITEYSEKIAAMEEEIKRIGELFADNKKELEECTTILQCKEKELEATQNNLQESKEQLAQEAFVVSAMETTEKKLHGTANKLLSTVRETTRDVSGLHEKLDRKRAVEQHNSQVHENFAEQINRRFSVIQQTVDEYSVKQQGMLDFYTNSIDDLLGASSSALSATATAVAKSFASVQETVSKQVSHSVEEILKQETLSSQAKDDLQKLMTAHRTGLEQALRTDLLPVVTAVLDLNSHLSHCLQSFLGVADKIDSHKEDMNSFFTEHSRSLHKLRLDSSSALSSIQSEYESLKEEIATAQSTHSEGVNNLISSLQNQLNLLAMETRQQFSGFLSKGGKLQESVGCLQQDLDLVSSDAIECISSHHSKFTEQSQAVTVEIRQLAGSNMSTLEESSKQCEKLTNSINTICQESQQWCESAGQKMDSLLEEQVCYLHSSKKQIQTLHKDVEDGCGSSVVEITDRVNVQCQAQEKALTSLVEQVKDDKEMLGEQRLELNEQVQSGLNKVHVYLKEELRNDVPTGTTPQRRDYVYPSLLIKTKPRDVLLEQFRQQQQEYLESICSVISEAVEPPVEQDSLEDEPPVAVNDSVISEKSCIDLSMTCQEKGGVPFFQQKKALRKEKENRGNATLLERSKIMDEVEQSLPKSKLPLRMQN', 1067, 'Q91783;', 'KD00957', 'Xenopus laevis (African clawed frog)', 'kif11-a', '#Kinesin-like protein KIF11-A#Kinesin-5#Kinesin-related motor protein Eg5-2#XLEg5K2', '-', '-', '-'),
(958, 'Q007T2', 'Cell division control protein 42 homolog', 'GO:0051988', 21259, 'Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin; actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration (By similarity). {ECO:0000250}.', 'MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL', 191, 'Q007T2; D1YSL6;', 'KD00958', 'Sus scrofa (Pig)', 'CDC42', '#Cell division control protein 42 homolog', '-', '-', '780428'),
(959, 'Q91784', 'Chromosome-associated kinesin KIF4', 'GO:0003777', 138924, 'Required for mitotic chromosomal positioning and bipolar spindle stabilization. {ECO:0000269|PubMed:7720067}.', 'MGKDEGIPVRVALRCRPLVPKENNEGCKMCLTFVPGEQQVIVGTEKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNATVLAYGQTGSGKTYSMGGAYTHNQENEPTVGVIPRTVIALFREIHQRPEWEFNLKVSYLEIYNEEILDLLYAARDKTNTISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEGDKNNSFRSKLHLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNMEETLNTLRYADRARKIKNKPIVNTDPQAAELQRLKLQVQELQVLLLQAHGGTLPVLNSMEPSENLQSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEELKQHAACKVNLQRLVETLEDQELKDNVEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAASFPVPEEDSGEKRSSDGFTTNHALRQAQLSKELIELNKALVMKEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAKKDNNQAKLSERRRKRLQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEVEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTDAGERIPTKIRRRTYTVAELENLEEEASVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISNIMEAKCALKYLITELVSSKVAGSKLESSVKQNRAHVADLQKNIFEERNQMAEMETEHQSQLMQLEQHHQEKILYLLSQLQQKQASVPVTIEELPAEEITEREKQLMERLKFQDEEIEKMKALCEKNQQLLQENDMYKQKLALLHVASGKKLHNILPAAEICSPDSPFDFIPPKPRGKRRTNAKSAAVILEDLLSESESEEESDDKNWEPGNNSKQSKKLTSKCSCKARCGNKMCGCRKTKQNCSDDCFCDPSKCRNRDNHMDEGKHEDQSLESENSKIDYPDVTAGGSFFTPPCVTPTKKVLREISDIGQVLSIKLQRKPSTASASASVMESQENQTSILTKKKKVLCNSNTSFFSGCSAITEDE', 1226, 'Q91784; Q9PSI0;', 'KD00959', 'Xenopus laevis (African clawed frog)', 'kif4', '#Chromosome-associated kinesin KIF4#Chromokinesin#Chromosome-associated kinesin KLP1', '-', '-', '394332'),
(960, 'Q91785', 'Kinesin-like protein KIF15-A', 'GO:0003777', 159141, 'Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. Required for centrosome separation and maintenance of spindle bipolarity during mitosis. {ECO:0000269|PubMed:8548825}.', 'MPPGTKGDPSNVTQPLPCLPSAEEDAIKVFVRIRPPVEGTLTGVDGEQGLCLTALSSTTIRLHSKPEPKMFTFDHVANVDTNQESVFSSVAKNIVESCMNGYNGTIFAYGQTGSGKTFTMLGPSESDNFTHNLRGVIPRSFEYLFFLINREKEKAGEGKSFLCKCSFIEIYNEQIFDLLDSASAGLFLREHIKKGVFVVGAVEQVVTSAAEAYQVLSMGWRNRRVASTSMNRESSRSHAVFTVTIESMEKTNDLVNIRSSQLNLVDLAGSERQKDTQTEGVRLKEAGSINRSLSCLGQVITALVDVANGRQRHICYRDSKLTFLLRDSLGGNAKTFYIANVHPGSKCFGETLSTLQFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKKLKEQLSQLLSGQMPGDISVARVPSVGDNNMDYMNNFIEAMMILEKSDREKKVLLQKVVQLEDLCNKKEKFIQSNKMIVKFREDHISRLEKAHKEGRISLSNNEQDDFIAELKEEIRTLKEQVEHHPRVAKYALENHSLREENKRLHSLQSVKRAQEVTAQMIAELEKAFLEVSVSEKDRQVAPMHSTPIQLDNNSLMSAARMRERMLQLESELATSKQEYEEFKELTKKKQVEQESELQSLIKSNQHLENILEAIKANKRHEVSQLNRMHAAETIKNMTTPTKSYNLRSRLVPRLSPDAMPNGLMDTPKSGDVMDDIINEPIPPEMSEQAYEAIAEELRIVQEQVTALQAKLDEEEGKNIRLQQQVNKLELCSTQIQELFNSERSNWNKEQQDLIAQIKSLEKQKQENKSQEDVLKSEVHDLRVVLQSADRELGAVKGEYSLYREKQEKELSQLSARHMDVQLQLDNVRLEHETLLEEKRSLQDAFDNLEEVMKFEIDQLKQEISDSKHENETLRAEFSNLLELLETEKERRQKLTSQLEEDKENKTKELLQVVDENMHLRKQCSELMTKCEQQVTELHGLEHSLTSSKEMIADLEKKNTADKEVVADLMNQIQVHRTTIIHKTESIDLLTRELEDIHSKYSIVLLAKEESKTVIEEQEKQIEELRECLERKQSADNIEKELLCDDLAHATEELEKLTEAFNKQEALLHTHEKELVEKEQQISELTNQVKLMTDLEISREQEKIRPASSNSSSPVVLPETPRTPEGNPYDSEIANLQKRNTNLEILVSELNEERTSKNEEIIRLKMQLCETENMRLEIQNLQGMCKELKSQLENCNNVMKDSNDQKPSDMQDLKREIEKEVSERMEKGKATEHILKLQAELEETRNILCTKDHSLNELSKEIERTRSLEAKAFTEKEEIRSILEGKYEETEKLSHELDMLRKQVLFLAEENGKILGHQNPNQKIQYLVKLKKENNKLLEEAEKLRIENLFLKESKKCEHCN', 1388, 'Q91785;', 'KD00960', 'Xenopus laevis (African clawed frog)', 'kif15-a', '#Kinesin-like protein KIF15-A#Kinesin-like protein 2-A#Xklp2-A', '-', '-', '397909'),
(961, 'Q91W40', 'Kinesin light chain 3', 'GO:0003777', 56006, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.', 'MSVQVAAPGSTGLGPERLNPEELVRQTRQVVQGLEALRAEHHSLAGHLAEALAGPGPVAGVELLEEKQQVVNHSLEAIELGLGEAQVLLALSAHVSVLEAEKQRLRAQARRLAQENTWLREELEETQRRLRASEEAVAQLEEEKSHLQFLGQLRQYDPPEESQRPESPPRRDSLASLFPSEEEEKKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFQDVERHYARALSIYEALGGPQDPNVAKTKNNLASAYLKQNKYQQAEELYKEILSQEALPAPLGAPQGGTAGDTQQQVLRRSSSFSKLRESIRRGSEKLVSRLRGEGMAGAAGMKRAMSLNMLNVDGPRAARTQLSQLSTRHLSEAPRTLSISTQDLSPR', 508, 'Q91W40; Q3TZ56;', 'KD00961', 'Mus musculus (Mouse)', 'Klc3', '#Kinesin light chain 3', '-', '-', '232943'),
(962, 'B5VH51', '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, 'B5VH51;', 'KD00962', 'Saccharomyces cerevisiae (strain AWRI1631) (Baker''s yeast)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '-'),
(963, 'Q8WQ86', 'Microtubule-associated protein RP/EB family member 1', 'GO:0000776===GO:0000777===SCL', 56983, 'Involved in microtubule polymerization; and spindle function by stabilizing microtubules and anchoring them at centrosomes.', 'MEGFGRNEILNWINDLLQLDYKKIEQLGSGAALCQLVDIIHPGKINLKMVNFNAKYDYEYIKNFSYLQESFAKLGVEKYVEVSELVKSRPQANLEFAQWMKKYFDQYYTGEPYNAIERRIALKIPTDKDRSSLKGKTAATGAPPTSKPSPSSTLKPATTAASKPAPVSKPTTTTAKPTPSSVSKPVSKPTPSSISKPVSKPTPSISKPVTKPTPTTTSTSTTTTVSTPPSTPKPTNTPIPSTTGKPTLTQPTFKPTPKSVSPTPPVVAGSTVTTKTVIVSEPPTELLEELEQQKRELEQQRKELEEQKSVIQEMTEKIANFEITIQDIEKDRDFYFERLREAEIFCQDHSDVPLLGEVLKILYNSNGEEEGEEGEGEEQGGEEEEEEEEQGENNIEQEEEEQIEQQQQQQEEEEEHERETLSEPEPDQDNSAIPLEQLEINDEEEEFNQHQEQEEEDEHFEDEEKVNGLNEEEIMNSVLQNASDEDDILESTFDGNEDDSLLQDEY', 506, 'Q8WQ86; Q54QT3;', 'KD00963', 'Dictyostelium discoideum (Slime mold)', 'eb1', '#Microtubule-associated protein RP/EB family member 1#DdEB1', '-', '-', '8624179'),
(964, 'A8XA80', 'Histone H3-like centromeric protein cpar-1', 'GO:0000777', 41344, '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. Not required for chromosome segregation during meiosis (By similarity). {ECO:0000250|UniProtKB:P34440}.', 'MYHHDSGPHIEEVFDPPSRRTMMQEIETHPDVIAFGKKLRKIKNQPESTFLSSADRMEEIIDAFRDQIAKWEEEEELNEPCEYRQLKIEIFTQKKIEYQRKNNLAVDEFYKKRNLKNHSNRKPLEESRRREEPRDRVHESNIDITHRGDSTSLNHYSRHHYSQRQSQSSRFERERESDEEEENSQPIQRYRSRSPKPSYSYNQSTMQQSQRDDTNVYHRSHQSTSQPPQVRMRSGKSRVTKTHNRKFRPGQKALAEIRKYQKSTDMLIQKAPFVRLVHEIIREQTYKSQDYRIRADALMALQEAAEAFMVEMFEGSVLICNHAKRVTLMPTDIQLYRRLCLRNLS', 345, 'A8XA80;', 'KD00964', 'Caenorhabditis briggsae', 'cpar-1', '#Histone H3-like centromeric protein cpar-1#CENP-A-related protein 1#Centromeric protein A related {ECO:0000250|UniProtKB:P34440}', '-', '-', '8583693'),
(965, 'P70399', 'Tumor suppressor p53-binding protein 1', 'GO:0000776===GO:0000777===SCL', 211340, 'Plays a key role in the response to DNA damage. May have a role in checkpoint signaling during mitosis. Enhances TP53- mediated transcriptional activation (By similarity). {ECO:0000250}.', 'MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEEDAGSHFSVLSRHLPNLQMHKENPVLDIVSNPEQSAVEQGDSNSSFNEHLKEKKASDPVESSHLGTSGSISQVIERLPQPNRTSSALAVTVEAASLPEEEKEEEELEEKEGVGANAPGADSLAAEDSASSQLGFGVLELSQSQDVEEHTVPYDVNQEHLQLVTTNSGSSPLSDVDASTAIKCEEQPTEDIAMIEQPSKDIPVTVQPGKGIHVVEEQNLPLVRSEDRPSSPQVSVAAVETKEQVPARELLEEGPQVQPSSEPEVSSTQEDLFDQSSKTASDGCSTPSREEGGCSPVSTPATTLQLLQLSGQKPLVQESLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQGGRKDEPMDMSVIPAGGEPFQKLHDDEAMETEKPLLPSQPTVSPQASTPVSRSTPVFTPGSLPIPSQPEFSHDIFIPSPSLEEPSDDVKKGGGLHSSSLTVECSKTSESEPKNFTDDLGLSMTGDSCKLMLSTSEYSQSSKMESLGSPRTEEDRENTQIDDTEPLSPVSNSKLPADSENVLVTPSQDDQVEMSQNVDKAKEDETEDRGDCKGREDAVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMDTKEHHPEEGFSGSEVEEVPETPCGSHREEPKEEAMESIPLHLSLTETQSEALCLQKEAPKEECPEAMEVETSVISIDSPQKLQVLDQELEHKDPDTWEEATSEDSSVVIVDVKEPSPRADVSCEPLEEVEKCSDSQSWEGVAPEEEPCAENRLDTPEEKRIECDGDSKAETTEKDAVTEDSPQPPLPSVRDEPVRPDQETQQPQVQEKESPVTVDAEVADDKQLGPEGACQQLEKAPACASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVTSESMVEINDPLLGNEKGDSESAPEMDGKLSLKMKLVSPETEASEESLQFSLEKPTTAERKNGSTAIAEPVASLQKPVPVFGCIYEAQQEKEAQSEAPPSAPDRANLLHFPSAQEEDKERPDVTPKLRQSEQPVKPVGPVMDDAAPEDSASPVSQQRASQEPFSPAEDVMETDLLEGLAANQDRPSKMLMDRPTQSNIGIQTVDHSLCAPETVSAATQTVKSVCEQGTSTAEQNSGKQDATVQTERGSGEKPASAPVDDTESLHSQGEEEFEMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSSHHTSSGTSLSAIHSSGSSGRGAGPLKGKASGTEAADFALPSSRGGPGKLSPRKGISQTGAPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETVVSGPLGVEDISPSMSPDDKSFTRIMPRVPDSTKRTDASSSTLRRSDSPEIPFQAATGSSDGLDSSSSGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNISSPVTPTAASSSSTTPTRKATESPRASTGVPSGKRKLPTSEEERSPAKRGRKSATVKPGTVGAAEFVSPCETGDNIGEPSVLEEPRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLLDGPTGSSEEEEEFLEIPPFNKQYTECQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH', 1957, 'P70399; Q68FD0; Q8CI97; Q91YC9;', 'KD00965', 'Mus musculus (Mouse)', 'Tp53bp1', '#Tumor suppressor p53-binding protein 1#53BP1#p53-binding protein 1#p53BP1', '-', '-', '27223'),
(966, 'Q9UJW0', 'Dynactin subunit 4', 'GO:0005868', 52337, 'Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton.', 'MASLLQSDRVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSDKYGLGTRLQRPRAGASISTLAGLSLKEGEDQKEIKIEPAQAVDEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDFQPVCASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLFECEEGDPDDINSTAKVVVPPKELVLAGKDAAAEYDELAEPQDFQDDPDIIAFRKANKVGIFIKVTPQREEGEVTVCFKMKHDFKNLAAPIRPIEESDQGTEVIWLTQHVELSLGPLLP', 460, 'Q9UJW0; B3KWW0; D3DQH0; E5RGT5; Q8TAN8;', 'KD00966', 'Homo sapiens (Human)', 'DCTN4', '#Dynactin subunit 4#Dyn4#Dynactin subunit p62', '-', 'ENSG00000132912', '-'),
(967, 'O13952', 'Centromere-localized protein 2', 'GO:0000776', 21922, 'Kinetochore-associated protein which may be involved in the reorganization of chromosomes during the transition from mitosis to meiosis. {ECO:0000269|PubMed:17035632}.', 'MNMEEQILNDYLLSQGRLQSIISLEQWRQLFPQRYREDPLIERLYEYCTQQRQKRLAKLRANIHLESQVIGKSRIDRMLATNVEKLQTVSHASTLHDVEEFYTSHSAKPLDISEINERLSEAVQSAYTKLNEEKERCTQLTLKMNSQIASLSDFQWSKEPNVDESIHLVESLIESLEKAAPSAIEELD', 188, 'O13952;', 'KD00967', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cnl2', '#Centromere-localized protein 2', '-', '-', '2541788'),
(968, 'Q5R706', 'Kinesin-like protein KIF3C', 'GO:0003777', 89515, 'Microtubule-based anterograde translocator for membranous organelles. {ECO:0000250}.', 'MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQTRAVGSTHMNEVSSRSHAIFIITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNTAGGASTPSSGGSGGGGGSGGGAGGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKRGMLGKRPRRKSSRGKKAVSAPPGYPESPVIEAWVAEEEDDNNNNHRPPQPILESALEKNMENYLQEQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEKDLRREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMMLRDEETMELRGTYTSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHDEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWKFQPLVPAGVNSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAVFEMEFSHDQEQDPRALHMERLMRLDSFLERLSTSKVRKSRSWCQSPQRPPPSTTHASLASASLRPATVADHE', 793, 'Q5R706;', 'KD00968', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'KIF3C', '#Kinesin-like protein KIF3C', '-', '-', '100169734'),
(969, 'Q96H22', 'Centromere protein N', 'GO:0000777===k', 39555, '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. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate. {ECO:0000269|PubMed:16622419; ECO:0000269|PubMed:16716197; ECO:0000269|PubMed:18007590; ECO:0000269|PubMed:19543270}.', 'MDETVAEFIKRTILKIPMNELTTILKAWDFLSENQLQTVNFRQRKESVVQHLIHLCEEKRASISDAALLDIIYMQFHQHQKVWEVFQMSKGPGEDVDLFDMKQFKNSFKKILQRALKNVTVSFRETEENAVWIRIAWGTQYTKPNQYKPTYVVYYSQTPYAFTSSSMLRRNTPLLGQALTIASKHHQIVKMDLRSRYLDSLKAIVFKQYNQTFETHNSTTPLQERSLGLDINMDSRIIHENIVEKERVQRITQETFGDYPQPQLEFAQYKLETKFKSGLNGSILAEREEPLRCLIKFSSPHLLEALKSLAPAGIADAPLSPLLTCIPNKRMNYFKIRDK', 339, 'Q96H22; A8MZE6; B3KN53; B4DJD1; B4DPY7; C9JJM5; D3DUK8; E7ES30;E7ETS3; Q9NZ83;', 'KD00969', 'Homo sapiens (Human)', 'CENPN', '#Centromere protein N#CENP-N#Interphase centromere complex protein 32', '-', 'ENSG00000166451', '-'),
(970, 'P40460', 'Kinetochore protein NDC80', 'GO:0034501===GO:0000778===GO:0031262===GO:0000780===k', 80487, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is involved in chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:10409732; ECO:0000269|PubMed:11266451; ECO:0000269|PubMed:12514103; ECO:0000269|PubMed:9585415}.', 'MQSSTSTDQHVLHHMDPHRFTSQIPTATSSQLRRRNSTNQGLTDMINKSIARNTISGTGIPTGGINKNKRTRSTVAGGTNGTALALNDKSNSRNSVSRLSINQLGSLQQHLSNRDPRPLRDKNFQSAIQEEIYDYLKKNKFDIETNHPISIKFLKQPTQKGFIIIFKWLYLRLDPGYGFTKSIENEIYQILKNLRYPFLESINKSQISAVGGSNWHKFLGMLHWMVRTNIKLDMCLNKVDRSLINQNTQEITILSQPLKTLDEQDQRQERYELMVEKLLIDYFTESYKSFLKLEDNYEPSMQELKLGFEKFVHIINTDIANLQTQNDNLYEKYQEVMKISQKIKTTREKWKALKSDSNKYENYVNAMKQKSQEWPGKLEKMKSECELKEEEIKALQSNISELHKILRKKGISTEQFELQNQEREKLTRELDKINIQSDKLTSSIKSRKLEAEGIFKSLLDTLRQYDSSIQNLTRSRSQLGHNVNDSSLKINISENLLDRDFHEGISYEQLFPKGSGINESIKKSILKLNDEIQERIKTIEKDNITLEKDIKNLKHDINEKTQINEKLELELSEANSKFELSKQENERLLVAQRIEIEKMEKKINDSNLLMKTKISDAEELVTSTELKLEELKVDLNRKRYKLHQQVIHVIDITSKFKINIQSSLENSENELGNVIEELRNLEFETEHNVTN', 691, 'P40460; D6VVE3;', 'KD00970', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'NDC80', '#Kinetochore protein NDC80 {ECO:0000303|PubMed:11179222}#80 kDa spindle component protein {ECO:0000303|PubMed:2229181}#Nuclear division cycle protein 80 {ECO:0000303|PubMed:9585415}#Two-hybrid interaction with DMC1 protein 3 {ECO:0000303|PubMed:9335591}', '-', '-', '854662'),
(971, 'P31269', 'Homeobox protein Hox-A9', 'k', 30172, 'Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1; on the endothelial cells surface at sites of inflammation. {ECO:0000269|PubMed:22269951}.', 'MATTGALGNYYVDSFLLGADAADELSVGRYAPGTLGQPPRQAATLAEHPDFSPCSFQSKATVFGASWNPVHAAGANAVPAAVYHHHHHHPYVHPQAPVAAAAPDGRYMRSWLEPTPGALSFAGLPSSRPYGIKPEPLSARRGDCPTLDTHTLSLTDYACGSPPVDREKQPSEGAFSENNAENESGGDKPPIDPNNPAANWLHARSTRKKRCPYTKHQTLELEKEFLFNMYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKINKDRAKDE', 272, 'P31269; O43369; O43429; Q99820;', 'KD00971', 'Homo sapiens (Human)', 'HOXA9', '#Homeobox protein Hox-A9#Homeobox protein Hox-1G', '-', 'ENSG00000078399', '-'),
(972, 'Q9VC45', 'Protein abnormal spindle', 'GO:0051383', 230180, 'Required to maintain the structure of the centrosomal microtubule organizing center (MTOC) during mitosis. May have a preferential role in regulating neurogenesis. Required for germ cell mitosis and oocyte differentiation. {ECO:0000269|PubMed:10073938; ECO:0000269|PubMed:15242765; ECO:0000269|PubMed:9151690}.', 'MSAFEITVTPSRLKQKKRAEGREPAVVVMAPFSAKAIVQFEDVPITKTARRQVRVLNPSDDDIEVKVMKAIREEHNLSLEWMEHTVPARDEVSMELVWSPVLEVACKETLQLIDNRNFRKEVMIILKSKSNQPVKNPRKFPTVGKTLQLKSPTGAGKTMKSVVSAAVQQKKRMSAAAAPPSKQTWRVTAPSRPAAWAHPPPQAPLVEKNVYKTPQEEPVYISPQPRSLKENLSPMTPGNLLDVIDNLRFTPLTETRGKGQATIFPDNLAAWPTPTLKGNVKSCANDMRPRRITPDDLEDQPATNKTFDVKHSETINISLDTLDCSRIDGQPHTPLNKTTTIVHATHTRALACIHEEEGPSPPRTPTKSAIHDLKRDIKLVGSPLRKYSESMKDLSLLSPQTKYAIQGSMPNLNEMKIRSIEQNRYYQEQQIQIKAKDLNSSSSSEASLAGQQEFLFNHSEILAQSSRFNLHEVGRKSVKGSPVKNPHKRRSHELSFSDAPSNESLYRNETVAISPPKKQRVEDTTLPRSAAPANASARSSSAHAWPHAQSKKFKLAQTMSLMKKPATPRKVRDTSIQPSVKLYDSELYMQTCINPDPFAATTTIDPFLASTMYLDEQAVDRHQADFKKWLNALVSIPADLDADLNNKIDVGKLFNEVRNKELVVAPTKEEQSMNYLTKYRLETLRKAAVELFFSEQMRLPCSKVAVYVNKQALRIRSDRNLHLDVVMQRTILELLLCFNPLWLRLGLEVVFGEKIQMQSNRDIVGLSTFILNRLFRNKCEEQRYSKAYTLTEEYAETIKKHSLQKILFLLLFLDQAKQKRIVKHNPCLFVKKSPHKETKDILLRFSSELLANIGDITRELRRLGYVLQHRQTFLDEFDYAFNNLAVDLRDGVRLTRVMEVILLRDDLTRQLRVPAISRLQRIFNVKLALGALGEANFQLGGDIAAQDIVDGHREKTLSLLWQLIYKFRSPKFHAAATVLQKWWRRHWLHVVIQRRIRHKELMRRHRAATVIQAVFRGHQMRKYVKLFKTERTQAAIILQKFTRRYLAQKQLYQSYHSIITIQRWWRAQQLGRQHRQRFVELREAAIFLQRIWRRRLFAKKLLAAAETARLQRSQKQQAAASYIQMQWRSYQLGRIQRQQFLRQRDLIMFVQRRMRSKWSMLEQRKEFQQLKRAAINIQQRWRAKLSMRKCNADYLALRSSVLKVQAYRKATIQMRIDRNHYYSLRKNVICLQQRLRAIMKMREQRENYLRLRNASILVQKRYRMRQQMIQDRNAYLRTRKCIINVQRRWRATLQMRRERKNYLHLQTTTKRIQIKFRAKREMKKQRAEFLQLKKVTLVVQKRRRALLQMRKERQEYLHLREVTIKLQRRFHAQKSMRFMRAKYRGTQAAVSCLQMHWRNHLLRKRERNSFLQLRQAAITLQRRYRARLNMIKQLKSYAQLKQAAITIQTRYRAKKAMQKQVVLYQKQREAIIKVQRRYRGNLEMRKQIEVYQKQRQAVIRLQKWWRSIRDMRLCKAGYRRIRLSSLSIQRKWRATVQARRQREIFLSTIRKVRLMQAFIRATLLMRQQRREFEMKRRAAVVIQRRFRARCAMLKARQDYQLIQSSVILVQRKFRANRSMKQARQEFVQLRTIAVHLQQKFRGKRLMIEQRNCFQLLRCSMPGFQARARGFMARKRFQALMTPEMMDLIRQKRAAKVIQRYWRGYLIRRRQKHQGLLDIRKRIAQLRQEAKAVNSVRCKVQEAVRFLRGRFIASDALAVLSRLDRLSRTVPHLLMWCSEFMSTFCYGIMAQAIRSEVDKQLIERCSRIILNLARYNSTTVNTFQEGGLVTIAQMLLRWCDKDSEIFNTLCTLIWVFAHCPKKRKIIHDYMTNPEAIYMVRETKKLVARKEKMKQNARKPPPMTSGRYKSQKINFTPCSLPSLEPDFGIIRYSPYTFISSVYAFDTILCKLQIDMF', 1954, 'Q9VC45; O01401; Q8SX66;', 'KD00972', 'Drosophila melanogaster (Fruit fly)', 'asp', '#Protein abnormal spindle', '-', '-', '42946'),
(973, 'P61273', 'Dynein light chain 1; cytoplasmic', 'GO:0000776===GO:0005868', 10366, 'Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1. {ECO:0000250}.', 'MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG', 89, 'P61273; Q4R7J2;', 'KD00973', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'DYNLL1', '#Dynein light chain 1; cytoplasmic#Dynein light chain LC8-type 1', '-', '-', '101866391'),
(974, 'C8Z692', '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, 'C8Z692;', 'KD00974', 'Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse(Baker''s yeast)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '-'),
(975, 'P23198', 'Chromobox protein homolog 3', 'GO:0000779===k', 20855, 'Component of heterochromatin. Recognizes and binds histone H3 tails methylated at ''Lys-9''; leading to epigenetic repression. Probably involved in the repression of many genes located in euchromatin; such as E2F1; MYC and CDC25A. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 ''Lys-9'' trimethylation; mediates the recruitment of the mehtyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1. {ECO:0000269|PubMed:24413057}.', 'MASNKTTLQKMGKKQNGKSKKVEEAEPEEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEDFLNSQKAGKEKDGTKRKSLSDSESDDSKSKKKRDAADKPRGFARGLDPERIIGATDSSGELMFLMKWKDSDEADLVLAKEANMKCPQIVIAFYEERLTWHSCPEDEAQ', 183, 'P23198; Q921C4;', 'KD00975', 'Mus musculus (Mouse)', 'Cbx3', '#Chromobox protein homolog 3#Heterochromatin protein 1 homolog gamma#HP1 gamma#M32#Modifier 2 protein', '-', '-', '-'),
(976, 'Q9CZW2', 'Centromere protein N', 'GO:0000777===GO:0034508', 39240, '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. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate (By similarity). {ECO:0000250}.', 'MKENVAEFLRRTILKIPLSEMKSILEAWDFLSEDQLQTINLKQRKDYLAQEVILLCEDKRASLDDVVLLDIVYTQFHRHQKLWNVFQMSKEPGEDVDLFDMEQFQSSFKRILQRALKNVTVSFRVYEKDSVWIRVAWGTQYSQPNQYKPTFVVYYPQTPYAFISSCHLKNTVPLLHQALKVASKHHQIVHLDLRSRHLDSLKAIVFREYNQTCENYSSTTSLQEASLSMCLDSKITHENTEEKVRVHRVTQETFGTYPQPQLEFAQYKLETKFKSNIGGGLLADRKEPFRCLVKFSSPHLLEALKSLAPAGIADAPLSPLLTCIPSKKMNYFKIRDK', 337, 'Q9CZW2; Q6PE73; Q8R2W7;', 'KD00976', 'Mus musculus (Mouse)', 'Cenpn', '#Centromere protein N#CENP-N', '-', '-', '72155'),
(977, 'O94261', 'Kinetochore protein fta3', 'GO:0051382===GO:0000778', 24997, '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}.', 'MDNNDQISNLCLGALQLLADQPISVISNEPSEEQRNEHVLKKWENNVLRHWKILFSLFMQTCGDSVQGNAAFSILNFMTTNSLVGQLYQRLYDESNSLGFISSPLNETEHLSEENLKIESSITFTSEEIEKEKENIKSVLLPSVQSISSSLELYASKESDYRSSIEGVLADLKLARARWEIVRNVTQILLLESGISFLENKKLAYIMDLCGDREDNYSSY', 220, 'O94261;', 'KD00977', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'fta3', '#Kinetochore protein fta3#Sim4 complex subunit fta3#Sim4-mal2-associated protein 3', '-', '-', '2541342'),
(978, 'Q0IJ01', 'Protein zwilch homolog', 'GO:0000777', 67494, '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}.', 'MWAERHRAAVELQQFLSSIYEQVKKGESLGPFQYKDDVQVHVVCDGHCKPLENFCSGSEVLYIMEKKPLTLEDNALDETENNEGISFYMSLQESPQPQAIPTMSARQFLTSYTLTHNPNMIQLNSGVPVKVLPPLWVRCDSSDAEGTCWLGAEPIKSNRNEITGMSFRTVTCAGPTADKSTFPSLDSLRQAHKERHYSSAMQTRGFAQYDLFGSNTVENSVIESQSSVTVDFVWNGVERILQLPPLTSAATLNIKVESGDLRSPVYSVYKELDFLLVLAEGLKTGVTEWPETSETKSAVDLVQHLLNDLKNKVDGLSTSVSKKDNEKIKSDTAAVDCSIQSFITERGDLDFAEMLWCKMRKSVSSYQDVVNCFSLVIQSLKHGEMHPWIHRGSSSTLSKLIQESYHGDMQSLSLTGLTPMRMLLEIGLDKMKKDYINCFIGQDLATFNYLDYFICTSVDLQEQVQRVKKLHHMLEVVVVCNAFLSLGHENLFPLTQSCLKYYKENPWNEQHVFQLPIRPSVISTFYQNSHPQTWRVEIISGHGQKEVKTTWQLTSRRPVDHVSFAVPDVPIDMTISGDNEELVYYPTQVSCSQVHFC', 597, 'Q0IJ01;', 'KD00978', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'zwilch', '#Protein zwilch homolog', '-', '-', '548970'),
(979, 'Q03790', 'Nucleoporin NUP53', 'GO:0034501===k', 52619, 'Functions as a component of the nuclear pore complex (NPC). NPC components; collectively referred to as nucleoporins (NUPs); can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both; a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus; with GDP in the cytoplasm). NUP53 may play an important role in cell cycle regulation by inhibiting PSE1 transport functions during mitosis and sequestration of MAD1-MAD2 in a cell cycle-dependent manner. It also seems to play an important role in de novo NPC assembly by associating with nuclear membranes and driving their proliferation. {ECO:0000269|PubMed:11352933; ECO:0000269|PubMed:12403813; ECO:0000269|PubMed:12473689; ECO:0000269|PubMed:12604785; ECO:0000269|PubMed:14697200; ECO:0000269|PubMed:9864357}.', 'MADLQKQENSSRFTNVSVIAPESQGQHEQQKQQEQLEQQKQPTGLLKGLNGFPSAPQPLFMEDPPSTVSGELNDNPAWFNNPRKRAIPNSIIKRSNGQSLSPVRSDSADVPAFSNSNGFNNVTFGSKKDPRILKNVSPNDNNSANNNAHSSDLGTVVFDSNEAPPKTSLADWQKEDGIFSSKTDNIEDPNLSSNITFDGKPTATPSPFRPLEKTSRILNFFDKNTKTTPNTASSEASAGSKEGASTNWDDHAIIIFGYPETIANSIILHFANFGEILEDFRVIKDFKKLNSKNMSKSPSLTAQKYPIYTGDGWVKLTYKSELSKSRALQENGIIMNGTLIGCVSYSPAALKQLASLKKSEEIINNKTSSQTSLSSKDLSNYRKTEGIFEKAKAKAVTSKVRNAEFKVSKNSTSFKNPRRLEIKDGRSLFLRNRGKIHSGVLSSIESDLKKREQASKSKKSWLNRLNNWLFGWNDL', 475, 'Q03790; D6VZX4;', 'KD00979', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'NUP53', '#Nucleoporin NUP53#Nuclear pore protein NUP53', '-', '-', '855184'),
(980, 'O43482', 'Protein Mis18-beta', 'k', 24691, 'Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038}.', 'MAAQPLRHRSRCATPPRGDFCGGTERAIDQASFTTSMEWDTQVVKGSSPLGPAGLGAEEPAAGPQLPSWLQPERCAVFQCAQCHAVLADSVHLAWDLSRSLGAVVFSRVTNNVVLEAPFLVGIEGSLKGSTYNLLFCGSCGIPVGFHLYSTHAALAALRGHFCLSSDKMVCYLLKTKAIVNASEMDIQNVPLSEKIAELKEKIVLTHNRLKSLMKILSEVTPDQSKPEN', 229, 'O43482; Q96BX7;', 'KD00980', 'Homo sapiens (Human)', 'OIP5', '#Protein Mis18-beta#Cancer/testis antigen 86#CT86#Opa-interacting protein 5#OIP-5', '-', 'ENSG00000247556', '-'),
(981, 'Q8IID4', 'Dynein heavy chain-like protein PF11_0240', 'GO:0003777', 617381, 'Acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (By similarity). {ECO:0000250|UniProtKB:Q14204}.', 'MTKFSEGHYDILNLIEVKSNIQEKNILGYSIDYTVGGLFLFGGFKIDIEENNGIICNDAYLIHIKNDKAEYETLSIKIKPSIRCYHNSCTLLENYVIIFGGLNSEVPFVALNDLWVFNSLNKTFVEIKLKCKEKNKEKNLQNGINGTNEKGYISQTDDENCSDNKYGENQDYGSNDSDSKDGEDIDKDDSILDNSYVKNLRKYLKSNKSDELHSSDIPCPRYFSSLDLYIIRKNNIEEEKGFKKDEIKIIKNNIIVSNSLNYEYFSLILFGGYGGYDRSSYNDLYEFNILNNEWILRGCKGNVPSTRYGHISFIHGNNLFILGGTNAEISFNDMYSCDLKNNEWSEVDFSYSFNISKVFCRSVLVESIDRNIIFIFGGYNIISDEKGNRKIEYNNIELNMLKLYDTFKLEELKYNIIQNNEENIIKNNNMEEINNMNSNNVKNEIISTKHDIYEDSNISNNITFCSITYDFMDSNLIITDNKKKIYIMNISNIIGPKYAIFNIWPKQCDINGNKKLLFRGKGFTNEGKILVKYKSDDINLYSEGIYINENNIYTIVPNAKNKIKNNICQVQLSINDKCYTTNSCFLEYYYNIDPKNTLIFGSGLLEPVCLQKDNIFFLIAKNSLNEHKKIGGDKFQISIIYEQKSEQYDIKYFVYDLNNGFYIVKYFSFLNDKQMKVKMQNVGKNNNIEQRNNNNDNNDNNNNDNNNNNNNDNNNNNNNNNNNNNNNNDNLNEQLNCNVVQRKNQNDLETLEGPQNISNKNSMNNEDIKSNTNNHMEILDLNGTLKITVKLKDENIQNSPFFLKVDNNLKDKIIYVKQFINDRLENLLRKGECLFDLIKNKNMNTNNLIQLNINIDHFLNTFPKAIHDINIIEQYILYGLIDIDKIKNVITNLHEEDNLVNASQEEEIYIDKEIHELINNEKFKNDQTDEMGEYTATTTNNVKHTNNTNNNDTHITDTLTHINENNDTRNNFLKVKDNHKIVDFINENKLKFLDYIDPNIMKKLRNYINLLNTEELNLKNKKDNKKIDDSNKKDLLGIKKKRSEDKFHLDNNLEKDEKKIEVIKNLLIFYHKLKTVCLSKKEKELKDEFIKEEKESIKKLKLNYNKFVNIKKNLEVSNVYLHNNGYDSSLKELETTKKYLIEIKDEVTKIKQISDNIIKIDNVEELNKDIENLNNEIHEIEKMWLFIKKKEEILNEFFFCPFKDLDVEDFDIQIKKLQNDFKKIKVDRKHNICKEETLKLKEIIKFISVLCEIKKPFIKDRHIKEMENNINEEKEKNKEEDKINIIIDDSTLTIYFYKLNIMKYHDTIEEVIIKAYNEKIIEETINKFEDYWDKIYFKKKEYKNNILLTYIDDICIDTIEEHQVTLQNCFSSKYFLFFSDELNLWQKKISNIYEVIQLLKDIEKLWIYLQNMYIYSEEVKKELPLYSKFFLTINDEYLEMLKQIIDNNIKVVDFSNEGGIIEKLEELKVKLCKSEKPLNEYLDSKRKSFPRFFFISSTDLIDILSNGNNFKLVNTHVQKIFLSIRKFVTKNEQLTDNEIQNEVKLNNQETITEEKNKNANENSNEIETNKYNKKEELTNNRDGDGDDDDNIKNDKDEKDEKEETIIKLISSYGEEICNFHEGLVLKGKVECYLNDIIDHIKYTLKYYITNLFRLKDLFNNEKEKWIDENYLAQVFILCNTIFFVNDVENILIKKDINIYEELNKYYKNHILQLENVIKKVQKKLTIKNRIKIMCIITLDTFYRDVLEVILKNKSSISINMFDWQSQIRMYPFFKNQKIYEQNENQTEESNLKLDNKNLDNEHQEGKQEYNNKNNDNDNNNNNNNNNILNNELSKYTCLTHFKDLYIKIKIMDCSFNYSYDYIGNYQRLVITPLTSRIYITATQALSLYMGCAPAGPAGTGKTETTKDLSSFFGKNCYVFNCSDQLDYKSMGNIFKGIGSTGCWCCFDEFNRLIPEVLSVCSIQFKSILDCKRNNNNVCIIGSDEIIVKKNCAVFITMNPDYLGRSKLPESLKILFRPITVIIPDFNKICENMLMAEGYVNAKYLSIKFTTFFELAKSLLKDKHCDWGLRSIKSVLTKAGDLKRNYPDVDENKLLYSAIHDINIAKISSSNCPIFSGLLNDIFFSNQNDITDINDINDINENKKEKDNIEELKSDNVKEEKKTKKKHLEDNNNNKKKELFNLNNIEKELMDICKKNHLFGLNYFVKKIIQLNDIMNIRHCVFIMGEAGCGKTTLFNMLMEYQKKQNLKTVSIRINPKSINIDDLYGNVHIKTREWKDGVFSKYMRNYSKKDDCDKAYIIFDGNLDSHWIENMNSVMDDNKVLTLSSNERILLKNHMNLVFEFSDLMFATPATISRAGLVYFSVDPNDLWKNYFLSWIDKHDNFNSNIKKLFEKLMYKYVEPTFSYLSTLQTSIKISPMSHIQSLSALLDILLIDNNYESVEHYFIYSVIWCFGGFLGEKDNVNYKKSFDKYWKNTFKSIKVNRKISVFDFYVENNKFKEWDEAEITNELKQNYVLQDDIFIETIESYSYKYICKLFLKSDMPILFIGKTGVGKTQLCKKILNEEKEEFKSFYMIFNYYTTSKNVQTLMQSCLEKKSGKQFSPPYQQKLIYFIDDINMPKCDDYNTQSAIELLCQYIDTNSWFDLEKLNLIKILNTKLISCMNYNRGNFTINPRLIRHFFILNINFPENNTVNSIFSVLLKNHFNNFKQDVSDLIPSILKSTISLFYNIEKTFKRTATYFYYEFNLRDIHSIVKGLLTTTPVTFQDCDKLLFLWLHECERVYSDKLNKKDKNKYKKIITDIIKKMYNKYEINKFVMKYDSTLLFSNFHKGSHDKTYDICKNMEELTLFLNEELNEYNNSYNVNIVLFSDAIKHICKLIRIVDNLKAHALLLGIGGCGKTTISKFSSYISSKTFFEMDFSAHCTDNDIKKYLQNIFHKCAMKNEDIVLFLKESKIHDTFFIYVNEYMCSNNIIDLYTKEERDYIIHNIRNIAKADGIEQSDNNIFDYYIKKVNDNLHFILCFSPTSNNFRDKSNNFQCILNNTMIDIYDNWEADSLMCVGKNYVSNIYMNINTGDILLDQEYINLKNKNIEKDITLGNKQIEKNYIPTISTNDGDDHYKDMDKTNMKNGDITTTINNIPIDNNNNNNNNRDNIDGNNFFKNREGNDENMKRKVYSNNFTNQNDLNTNITNNNNNNSNNNNNNIYDKNDSILKEEEYVNLKDIITEYLKECYEDLLDISSFYYSHERSHIYITPKLYLESIKTYHIMLLKNITNINNKMNMLKNGITKMNETSSNVENIKNCLKDKKKISEEKMEAAEKYAIDIGNEKMVVKKESDLADIEEQNCLEIQKKVLKQQEECENDIRLGIPLIEQAEEALNTLNKKNIQELKTLNKPPPGVEDITAAVMQLLATIDTTISIDKFGKIKDRSWKSAQKMMINPEKFISLLKDYKNKIDENLVPDCNFKYVENLINLPHFNKNAIQKKSKAAAGLAEWVLNITSFYKIIQNILPKRILLDNTKKGLEEANEKLQIVREKVQSLKAKLSELISQYDHAIYERDLVILEEKKLKTKLELSIRLIDALSSEEISWSKQYESLKKKKKTILTDILLSSTFVTFCGGFTKKYRNKIMTNCVDTLKRKNEIQNNIFNNMLKKINNNDQNFINNNNNNNSSNNNSTNFGYNEDPQKKDNHNNFDISNKLNIKNEKKDNELGNDNLKKEEMIYDIFLVNNFNLDLLINEEVLSKLSKQGLTLNSVCIENNIILENSDKFPIIIDPQMESLKWLINSHKEKSEKLIITDINDKILLKKIEECISFGYSIIVENADEYIDNTLYNVISKNIIKRKNNYYININDKELMFHPSFYIILHTQLSNPHYQPEIQSACSLINFTVTPDDLEEHLLSITLENEFNHLSKKKKKLSLLKYDYMCQLSFLQSSILQKLTDAKGDILEDVSLIENLEKTKLLSENIAKKTEIVKNTEVHINTIINLYRPLSKRGVMYFFILQKLKNLHSFYFYSLEIFLKIFIKCLNDSSPNRSPSKVNQEQEYYLKSEDNDFNDDYLGSTKEEEKMEDEEKMEEEKVDEEKMEEEKVDEEKMEDEKVEEKMEEEKVVEENTEDEKAIEINTEDEKAVEKNTEDEKAVEKNTEDEKAIEKNTEDEKAVEKNTEDEKAVEKNTEDEKAIEKNTEDEKAVEKNTEDEKAVEQNTEDEKVVEENTEDEKAVEKNTEDEKAVEKNTEDEKVVEEKIEDEKGEEQKAEEENVGIEEVEKVQIDDYKVSEKKGENKNCTYEENGKIDKDKEDDLEEEEDFENDDFTNEETKIDKNEVEKRVNMLTDLLNIKMWMYMDKGLLERDKLIVKCLIMLHLEKLNDKISEEEEEIFINPKYKLSNNNITSIRNKKENESMEKKLMNKSFINEELYEDCKNLENLKDFENITESFESESMSWKQWFLSEKVENEELPRKYNNIKDFSKLLLIRVLRKDRFLIALKNYITKNIKMTNDEKNNTYALENILDEYIDNKTPVLFLLTTGYDPSKEIEDYINKMKNNAIKKNDSNKKESNKNNIAYVNISMGQGQENIALKYLKEISKCGGYIFLQNIHLMTKWLKEFEEILDKIFLDAHVNFRLFLSAAIPNEKDTKLLPEKLLKKCFRINNEKSYSLKDNIKCCLDKFENGQYDDKLKTVILGLSYYHSLLLGRFLYGKIGFSQSYSFNDNDLEISFNIIKRYLKTYESFPLADVLFLIGEIIYGGHITDIWDRRINKTYVKNILKEIYRNIISINEKNKNINMDFHHPNDSNNNYNDDDNNNSHKNNKNNNNNNNKDDDDESNNSNDNEEENEEKLILKNTKHNILFDVFKFPDCSKYNINQLKKYIDEKLNKEQTYLLGLHINAEIEYMKNECSRILQTLQELSNKEIASTESYKKNTKIIKKEKPGDNKDNKYTHDQKKETIHKEEDDEDEKHSGSNKSTKIIYDIINHLLNELPDKIDTNDLKIEDSQTNTFMVIALKEAEKFNKLIECINDTLIEIKLVLDGILNMNDKIQNTIKSLMLHNIPHIWINYSYPSKKKLMPWFENFKLRIIFIKEWISKIRNNIFLPNSVWLSALFNPISFLTAIKQKFAQENKVPIDKLKLKWQVTNITKLEDLNNKNNALYIHGLYLQGASWFINSKNDTFTFDKDNINDNVSYGNIIESVPKHIYYSMPLIYVYCISNEQDELLKENMEYRSLDTPLYVTSDRGNTFVCSIDLNLEMEDIEDKWILAGVALFLSDD', 5251, 'Q8IID4;', 'KD00981', 'Plasmodium falciparum (isolate 3D7)', 'PF11_0240', '#Dynein heavy chain-like protein PF11_0240 {ECO:0000250|UniProtKB:Q14204; ECO:0000303|PubMed:17653272}', '-', '-', '810787'),
(982, 'Q750S2', 'Sister chromatid cohesion protein 2', 'GO:0051315', 170017, 'Plays a structural role in chromatin. Probably involved in sister chromatid cohesion; possibly by interacting with the cohesin complex (By similarity). {ECO:0000250}.', 'MSTFPGEDTRIPKRISEALSHQPLNHLVPKRELSRLLSKPVQISVQLESEDAFEEVPEELWQYPHPIDLDPLRLEESQPLRFRRPRGARLDYREDSSEIADLPGMGQLARACLSGTQLVDSAAIVESIESNAKKRKQTLAIGDVEMVSPDKKTKVMASVSPVSLNRVALGSQHLKTLERLMQYIGADESSAEFGDFEYWITLEDRATHILSEQCIDKLHIVFRNILSIPAVWTELDVSLLQRIMDVCVSTITICLEKIELKEYSHDYTLIAFGSSMVVFFIFLLDQNDRRLQLEQYMMVPLQFLTFTADNLEEEFDRGGNGVERSLAMLHSTLDVFYMYISNKPKLDDGLVVKLVYMFTELIMSTWSHNVSSVSLQNHIGNVKTIGMKSIEVLFEKLPEQRLFIIDELLSHLDNLPNTRSQKRMKNIGKNLHITHFSYIMLSILQVWNNYDYCSNLVSPDTEQLHDLIAHHAATQSDLEFAADHIIDTILKKCFSNISKYRFVFDQFVTDMTTVVTLPDWPVSDLILARLLKKLLSIFNPQSQKHINIESVALQGIGLIGSTILDIRLSSNSNPTANLIHLFNYPEDIDGLFKAYRTCLAYCTNSVQHHTPYKFLWCKQLDVLTKLKEMDKESQGWGSKLQQKFLSLIESIHLPLEQAANLGAVEILPTYCSTLLTSELINMYEPYLKLVLSLLERHKVKLRSGAIRCLALLISKDKNMLYTPIVKETIENRLTDSSPLVKDAILELIELGSSYIDFYQHININYNDDSMLVRKHVLRMNQIIYDDTEDIIIKAYVASRILRRIEDEEDVIIETARSELLKRWILSIQCPNAKPELQIKNCRVSIRVIAQLLVGGDKICDLFEHFLIFYVLNKNAHTEDQNKLISSSLCLLTDQVIEMVIENEAADVDNQREEEGRNIMKFLSVLSSCQDSFITKDHITALYPYLHSDTKSDFQLHILKVYRNTFEQLSHFKPKFLYDLETTILSRLPRMNVRELDEAIPLSWSLSRHRKDDTRICKACASCLGQLSPYIANATTDPSAVRPDGKLQRLLYLATGFARFCSFENTEGKFPNLKTRENIFEYVTKCLLMFTKENIHHVIRRIATKNLVKIASRYPKLFNSRHVLTVLDTQFEKGILDIQLVVLESLYDFFLAEERRSLIQVGVDGTISSNNELRKVVANHTKSDSINDGICSALVSRYLDKILKICLIADLNNAMVAIRFLKQILTYGYTNPSLCVPTVIALTASPNSYMRDLSSEMFSELLQGYESMAFNCLNQGIRLGTEYAVKIRPKQFHEDSMFLRRLQQLMSTNKRNRSKFLKVVKKTVFSNYLSTSVNYEESCYHIIYLLHNLSKISYDNMLELYEMLRSVISVSEYFSDRISERLDGFQSNQNTAAEVSAIIVTRLSIEEFKRFMFEQHHLSEAKLTLLDATDDENLRNKSVAALDDQVGSLHMENIFLGYENPINNKDYCWKYISTLHRDEI', 1479, 'Q750S2;', 'KD00982', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'SCC2', '#Sister chromatid cohesion protein 2', '-', '-', '4622833'),
(983, 'Q5VQ09', 'Armadillo repeat-containing kinesin-like protein 2', 'GO:0003777', 97845, '', 'MSGKVANATPKAAAGKPRLSAAGGGAYRRTSSGPLPSAGGGGGRASSESGVSSRVRVAVRLRPRNADELAADADFGDCVELQPELKRLKLRKNNWESETYEFDEVLTEFASQKRVYEVVAKPVVESVLEGYNGTVMAYGQTGTGKTFTLGRLGEEDTAARGIMVRAMEDILADITPETDTVSVSYLQLYMEMIQDLLDPVNDNIAIVEDPRTGDVSLPGATVVEVRDQKSFVDLLRIGEAHRVAANTKLNTESSRSHALLMVNVRRAVKGKHEMDVSISGENGHSSSMVGSLRPPIVRKSKLVVVDLAGSERIDKSGSEGHTLEEAKSINLSLSALGKCINALAENSPHVPVRDSKLTRLLKDSFGGTARTSLVVTIGPSPRHRGETTSTIMFGQRAMKVENMVKLKEEFDYKSLCRRLDIELDKLIAENERQRKYFDDEIERITAEAQLRVTEAEREYKISLENEKAKYHQEYLDSIKILEEKWKIHQQSPKKLIKETEPTSSEVGEVQNLLQNEKVLRQSAEDEANDLKNQVLHWKKMEAAATAEVVKLRKMLDTEASQKEKLDEEIAVLKSQLLQLSLDADETRRSLDRGDGSGKIFPGFDSLMSHSRNSQPREQSNGPKPPIAKLFEQVGLQKILSLLESEEPDVRVHAVKVVANLAAEEANQEKIVEAGGLTSLLMLLRSSEDETIRRVAAGAIANLAMNETNQDLIMAQGGVSLLSMTASDAEDPQTLRMVAGAIANLCGNDKLQTRLRGEGGIKALLGMVKCGHPDVLAQVARGIANFAKCESRAATQGNKVGKSLLIDDGALPWIVKNANNEAAPIRRHIELALCHLAQHEVNSKDIISEGALWELVRISRDCSREDIRMLAYRTLTSSPTLQSEMRRLRIEC', 891, 'Q5VQ09;', 'KD00983', 'Oryza sativa subsp. japonica (Rice)', 'Os06g0137100', '#Armadillo repeat-containing kinesin-like protein 2', '-', '-', '-'),
(984, 'Q8AWF5', 'Kinetochore protein NDC80 homolog', 'GO:0000776===GO:0000777===GO:0031262===SCL===k', 74477, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:12514103; ECO:0000269|PubMed:14738735}.', 'MRRSSVTNRQSLLPLRVQDANRMGLTTPQNKDRQGFGKLSMSKPHSGTSEKKTSFFGKRASNGTARTSQYGAFGGTEKIKDPRPLHDKAFIQQCIRQLCEFLNENGYSQALTVKSLQGPSTKDFLKIFAFIYTFICPNYENPESKFEEEIPRIFKELGYPFALSKSSMYTVGAPHTWPQIVAALVWLIDCVKLCCVLRSENPVFEDPPMGEQSENGIDFNQLFLDYTVRCYDQFMEGRDTFEEYDTDVCIRLKEAYHVDESNLEALQQESRRLMEEIERLEKEKENEPDRLASMRKLKASLQADIQKYQNYLTEIESHSTLLDQRVSSISEELEATELESRAIQQENLRLKNILDNQKYSVADIERIKYEETELQQTIAKLTKDLDEDKQQLWHEELKYAKMKESVETQLSEFHKIGRKVRLIPPTAEFANGYDFQIQCNLDSEQSSLMHYRNKINVPLVEILSQSEGHIASSTNKKMGVEDMVEQLNTLIGEKKNEVKVQKDEAQKLEEIYQQKVEESEEHEKRWISEIESLEKHRQLLESGVNKSLDEAMKDLQKEQQELQLVEHRTEEEMRQVENKLVRVVHAVANHVAVIEKHLEEKRLKVEREYEEFMKEDLLLDLRELLEKYKEKARVLDSL', 638, 'Q8AWF5; Q6NRM2;', 'KD00984', 'Xenopus laevis (African clawed frog)', 'ndc80', '#Kinetochore protein NDC80 homolog#Kinetochore protein Hec1#Kinetochore-associated protein 2#xNdc80', '-', '-', '398429'),
(985, 'Q9I869', 'Kinesin-like protein KIF22-A', 'GO:0003777', 73066, 'Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA. {ECO:0000269|PubMed:10966104; ECO:0000269|PubMed:10966105; ECO:0000269|PubMed:12360284}.', 'MVLTGPLQRESVSMAKRVSMLDQHKKSSCARVRVAVRLRPYMDEKDEAKATTVCVRGLDSQSLEIVNWRNQLETMQYQFDAFYGDSASQREIYMGSVCHILPHLLIGQNASVFAYGPTGAGKTHTMLGNPNQPGVIPRAVRDLLQMSRTAASAPENENWTYTINMSYVEIYQEKVMDLLEPKNKDLPIREDKDHNILIPGVTQKMINSFADFDEHFIPASQNRTVASTKLNDRSSRSHAVLLIKVQKSQQVVPFRQLTGKLYLIDLAGSEDNRRTGNQGIRLKESGAINSSLFTLSKVVDALNQGLPRIPYRDSKLTRLLQDSLGGSAHSVMITNIAPEQTYYFDTLTALNFAAKSKQIINKPFSQETTQTVVQPAMKRPREETGHIAGSQKRKKSKNDSTESSPNSSMDTAGKQKLNLATLDPAVVERLLKLDKILTEKGKKKAQLLSTPKRERMALLKKWEESQMEIERLKEKQKELEQKAMEAEARLEKSNNSDLSDSSVSENTFRAPLRGRNTSTAKVKKVLRVLPMQGNSQLQSTVEEGIPVFEKKKKKKQVTCEGLENQPTWEMNMRTDLLESGKERILKLLNTGSVKELKSLQRIGDKKAKLIIGWREVNGPFKNVEELACLEGISAKQVSSFIKANIMSSIAS', 651, 'Q9I869; Q9I8K0;', 'KD00985', 'Xenopus laevis (African clawed frog)', 'kif22-a', '#Kinesin-like protein KIF22-A#Chromokinesin kid-A#Xkid-A', '-', '-', '100337510'),
(986, 'O16844', 'Kinesin-like protein costa', 'GO:0003777', 133148, 'Regulates cubitus interruptus (ci) processing by recruiting multiple kinases to promote its efficient phosphorylation. Scaffolds multiple kinases and ci into proximity to promote its hyperphosphorylation; which then targets it for SCFSlimb/proteasome-mediated processing to generate its repressor form. Hh signaling inhibits ci phosphorylation by interfering with the cos-ci-kinases complex formation. {ECO:0000269|PubMed:15691767; ECO:0000269|PubMed:9244298}.', 'MEIPIQVAVRIFPHRELKDLLRSFGPTEPKKDAQAVDEGADSKDSEAQVPAAEKDNPSISETDPNGNAEQDSAADSKTIPDANGNDSGQKDYPDSAYCVQAIPISASALGLPSALPGGDPMDSIAAGLIQVGPHTVPVTHALPSSSSQEQVYHQTVFPLITLFLEGFDASVVTYGQRGQGKSYTLYGNVQDPTLTDSTEGVVQLCVRDIFSHISLHPERTYAINVGFVEICGGDVCDLLGMGNIHCTNVDAVFHWLQVGLSARQSLPAHTLFTLTLEQQWVSKEGLLQHRLSTASFSDLCGTERCGDQPPGRPLDAGLCMLEQVISTLTDPGLMYGVNGNIPYGQTTLTTLLKDSFGGRAQTLVILCVSPLEEHLPETLGNLQFAFKVQCVRNFVIMNTYSDDNTMIVQPAEPVPESNSSAGPLSQAGPGDNFGLQFAASQWSKLVTNAEGLFSKLIDSKLITEVEKEQIEEWLFLKQECEECLSSTEAMRQQKQLVPILEAEEPEDVNSEAANSESPNSDNENDTDNESHRPDLDDKIESLMEEFRDKTDALILEKHAEYLSKHPKAVMQSQDREIEAQPPEENGDDRKVSIGSRRRSVQPGASLSTAELAMLNRVASQQPPPPIDPESVVDPLESSSGEGIRQAALAAAAATAPIEQLQKKLRKLVAEIEGKQRQLREIEETIQVKQNIIAELVKNSDTRSHAKQRFHKKRAKLEAECDKAKKQLGKALVQGRDQSEIERWTTIIGHLERRLEDLSSMKHIAGESGQKVKKLQQSVGESRKQADDLQKKLRKECKLRCQMEAELAKLRESRETGKELVKAQGSPEQQGRQLKAVQARITHLNHILREKSDNLEEQPGPEQQETLRHEIRNLRGTRDLLLEERCHLDRKLKRDKVLTQKEERKLLECDEAIEAIDAAIEFKNEMITGHRSIDTSDRIQREKGEQMLMARLNRLSTEEMRTLLYKYFTKVIDLRDSSRKLELQLVQLERERDAWEWKERVLSNAVRQARLEGERNAVLLQRQHEMKLTLMLRHMAEETSASSASYGERALAPACVAPPVQASSDFDYDHFYKGGGNPSKALIKAPKPMPTGSALDKYKDKEQRSGRNIFAKFHVLTRYASAAAAGSSGSTAEESTALIESTTTATATTTSTTTTGAVGKVKDKALVSFRPEQLKRLMPAPTATKVTRQKNKIIIQDASRRN', 1201, 'O16844; A1Z6X4; B5RIP3; Q6AWI9; Q8IH04;', 'KD00986', 'Drosophila melanogaster (Fruit fly)', 'cos', '#Kinesin-like protein costa#Kinesin-like protein costal2', '-', '-', '35653'),
(987, 'Q8AWF4', 'Kinetochore protein Nuf2-A', 'GO:0000777===GO:0031262===k', 54453, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:12514103}.', 'MDKLTFPIFPAADLVNFFRQNILTGTEAKNFNKNDIFPNPKPEMVQKLYMRILQQVFNYGVEQFYMVPMDLDIQYPHLVEGFAPVANILKLMARFLPMCRVYDFHPSDVLNPKGKRTLHSLSGIVNFLHFSATRKEVYFEYCSSYKSALENVRQLQKANQEAEIKIEKLTTVPPEQQAEFKALSSEIHDLQQIISQEYRAKDVAFQEKIAQRKTEFAEKNKRLNEQKLAIATMKEEQERMKSQIVESPEQRKSKTERMKETVHRLKQARQETNDKCDYYRDRVAFACMWQTDVQGYLKKLQGIDTNLEIHRKIREEIRHSEEQVVNLNLELKSLSNEDAQLKRIILVKKEKLAKVDIKNKKKQEDFNQQKQEILEVCSRIQEKRQVVHGRVAQVLQEIQQTIGKKEQLLETTEAGKKKCQEVITDFRAALEKYHDSLQKASERSADRRREKIAELNRRLSRR', 462, 'Q8AWF4;', 'KD00987', 'Xenopus laevis (African clawed frog)', 'nuf2-a', '#Kinetochore protein Nuf2-A#xNuf2#Cell division cycle-associated protein 1-A', '-', '-', '398428'),
(988, 'Q8K015', 'Centromere protein O', 'GO:0000777===GO:0034508', 34154, 'Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Modulates the kinetochore-bound levels of NDC80 complex (By similarity). {ECO:0000250}.', 'MESANTLCPGRKCKGGVLAHLERLEAQTNISNRKSEEPAVRKKESSLRTKIRELRQQRDKLRAEVKQWGARVKEPPAKEDPSRTVISEQEVLEREWRNVDAILEAYRFTGLSGKLTSRGVCMCISTAFEGNLLDSYFVDLVIEKPLRIHHHSVPVFIPLEKIAAAHLQTDVQRFLFRLWEYLNAYAGRKYQADQLESDFCDVLTGPLQRNALCNLLSFTYKVEQRCQTFSFSARLLYEDPTAALPTNVTVTRPGVEASSPPWEEHRASHQMLFRTKPLHKVFASFSKETEKLHLNLVS', 298, 'Q8K015; Q8R587; Q9CYY6;', 'KD00988', 'Mus musculus (Mouse)', 'Cenpo', '#Centromere protein O#CENP-O', '-', '-', '52504'),
(989, 'G5EFA2', 'BIR-1Inhibitor of apoptosis homolog', 'k', 17720, '', 'MAPGTKKKSDMAKFTFYKDRLMTFKNFEYDRDPDAKCTSQAVAQAGFYCTGPQSGKCAFCNKELDFDPEDDPWYEHTKRDEPCEFVRIGKLDDSELTINDTVRLSQTAMIMTKLFEHEMMINNLSNHSSSDALFDQLKKVPNTASTTKSNSRRGK', 155, 'G5EFA2;', 'KD00989', 'Caenorhabditis elegans', 'bir-1', '#BIR-1 {ECO:0000313|EMBL:CAA98553.1}#Inhibitor of apoptosis homolog {ECO:0000313|EMBL:AAB94330.1}', '-', '-', '179597'),
(990, 'Q75BY2', 'Histone acetyltransferase ESA1', 'GO:0034508', 51121, '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; histone H2A to form H2AK4ac and H2AK7ac; and histone variant H2A.Z to form H2A.ZK14ac. 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}.', 'MAQEEEKDAGISKYISTTDEIIIGCKCWVEKDGEQRLAEILSINNRRQPPKFYVHYEDFNKRLDEWILASRINIEREVTFPKPRDPDEKKKKKQKKSATPQATDGETLESADIMDLENLNVQGLRDEGISRDDEIKKLRTSGSMTQNPHEVSRVRNLSKIIMGKHEIEPWYFSPYPIELTDEDVVYIDDFSLQYFGSKKQYARYRQKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTQRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGRLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLIKLLVENGTEITIDEISSMTSLTTTDILHTAKALNILRYYKGQHILYLNEDVLLRYEKLIAKKRRSIDPEKLIWKPPIFTASQLRFAW', 435, 'Q75BY2;', 'KD00990', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'ESA1', '#Histone acetyltransferase ESA1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}', '-', '-', '4619672'),
(991, 'Q9UST6', 'Kinetochore protein spc24', 'GO:0000778===GO:0051455===GO:0031617===c;k', 23039, '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}.', 'MSDSPIELMRSTLAGFQIAPDVKTISNIQDIRAQIQSFREKELEGSQTKFKVLSRKLEISTQAMESLKQTAESSQHAEEILSREKEKFRIAKLLNITENEIMSLESQLQKMKEQLLQLEERENTSEDICQSEENANMLKLNFYHSLGFDLETAENTGNKRVIIHTENDLQTVQISNKYSPYFYSNYFWDLLDDSKDKK', 198, 'Q9UST6;', 'KD00991', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'spc24', '#Kinetochore protein spc24', '-', '-', '2540238'),
(992, 'Q6CGR3', 'DASH complex subunit DAD2', 'GO:0042729', 12881, '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}.', 'MVRPRVSLAPNRLNHAGSELDEKIAAKKRELQQLVQLRQYSSDLADELEGLVQHVSCLAEETDVVAEVMGNWAAVIRAINLASTALARYTEEDYREPVLPEQLIRVPLEDEQEE', 114, 'Q6CGR3;', 'KD00992', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'DAD2', '#DASH complex subunit DAD2#Outer kinetochore protein DAD2', '-', '-', '2906184'),
(993, 'P35734', 'DASH complex subunit ASK1', 'GO:0008608===GO:0051315===GO:0051987===GO:0042729===SCL===k', 32072, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A; and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally; thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids. {ECO:0000269|PubMed:15664196; ECO:0000269|PubMed:16415853; ECO:0000269|PubMed:16777964}.', 'MDSASKEETLEKLDQEITVNLQKIDSNLSFCFHKITQDIIPHVATYSEICERIMDSTEWLGTMFQETGLVNLQANAAAPVGNAPVKSLVSNNVGIFPTSAEEASRQSQTDNGPNEADSAVHVNRDVHSMFNNDSIDDFHTANITSTGQILKLPDSSDEDTGSEAVPSREQTDLTGEGHGGADDEQDESTIQRQSRKRKISLLLQQQYGSSSSMVPSPIVPNKMRKQLAHEEHINNDGDNDDENSNNIESSPLKQGHHHPKGQADDNNEGPDEEESTKEVPKPGTIIHFSTNR', 292, 'P35734; D6VXN5; Q68EC3; Q6B290;', 'KD00993', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'ASK1', '#DASH complex subunit ASK1#Associated with spindles and kinetochores protein 1#Outer kinetochore protein ASK1', '-', '-', '853814'),
(994, 'Q8WQ99', 'Casein kinase I gamma', 'GO:0005818', 46369, 'Involved in the asymmetric cell division of the embryo downstream of par-2 and par-3 by regulating the asymmetric cortical distribution of pkk-1; a phosphatidylinositol 4;5- bisphosphate-producing enzyme; which in turn regulates the asymmetrical distribution of grp-1; grp-2 and lin-5. {ECO:0000269|PubMed:18694560}.', 'MTNTRGSNSATSASTTNSQGVLMVGPNFKVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSKAPQLHLEYRFYKLLGQAEGLPQVHYFGPCGKYNALVMELLGHSLEDLFDLCDRHFSLKTVAMVAMQLIRRIEYVHTKHLIYRDVKPENFLIGRYSTRKQHVLHIIDFGLAKEYIDCDTGKHIAYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRQTAVEVLCEGFPDEFAQYLRYARRLDFFETPDYDFCYNLFKSVLDRLGATYDYEFDWTPKLNNVSTPSGSLHTSESKDVKRTDRGELKVSQAAAHAQFGSTQVINSNAGEVVEESRNTEGRTAAGDNSSGEVKCCCFRRRRRKHNNATPATQK', 407, 'Q8WQ99;', 'KD00994', 'Caenorhabditis elegans', 'csnk-1', '#Casein kinase I gamma {ECO:0000303|PubMed:18694560}#CKI-gamma {ECO:0000250|UniProtKB:P78368}#2.7.11.1 {ECO:0000250|UniProtKB:P78368}', '-', '-', '172891');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(995, 'O43093', 'Kinesin heavy chain', 'GO:0003777', 105041, '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. The speed of this motor is 4-5 times faster than its animal counterparts.', 'MSGNNIKVVCRFRPQNSLEIREGGTPIIDIDPEGTQLELKGKEFKGNFNFDKVFGMNTAQKDVFDYSIKTIVDDVTAGYNGTVFAYGQTGSGKTFTMMGADIDDEKTKGIIPRIVEQIFDSIMASPSNLEFTVKVSYMEIYMEKVRDLLNPSSENLPIHEDKTKGVYVKGLLEVYVGSTDEVYEVMRRGSNNRVVAYTNMNAESSRSHSIVMFTITQKNVDTGAAKSGKLYLVDLAGSEKVGKTGASGQTLEEAKKINKSLTALGMVINALTDGKSSHVPYRDSKLTRILQESLGGNSRTTLIINCSPSSYNEAETLSTLRFGARAKSIKNKAKVNADLSPAELKALLKKVKSEAVTYQTYIAALEGEVNVWRTGGTVPEGKWVTMDKVSKGDFAGLPPAPGFKSPVSDEGSRPATPVPTLEKDEREEFIKRENELMDQISEKETELTNREKLLESLREEMGYYKEQEQSVTKENQQMTSELSELRLQLQKVSYESKENAITVDSLKEANQDLMAELEELKKNLSEMRQAHKDATDSDKEKRKAEKMAQMMSGFDPSGILNDKERQIRNALSKLDGEQQQTLTVEDLVSLRRELAESKMLVEQHTKTISDLSADKDAMEAKKIELEGRLGALEKEYEELLDKTIAEEEANMQNADVDNLSALKTKLEAQYAEKKEVQQKEIDDLKRELDRKQSGHEKLSAAMTDLRAANDQLQAALSEQPFQAPQDNSDMTEKEKDIERTRKSMAQQLADFEVMKKALMRDLQNRCEKVVELEMSLDETREQYNNVLRASNNKAQQKKMAFLERNLEQLTNVQKQLVEQNASLKKEVALAERKLIARNERIQSLETLLHNAQDKLLNQNKKFEQQLATVRERLEQARSQKSQNSLAALNFSRIAKPLRGNGAAIDNGSDDGSLPTSPTDKRDKRSSWMPGFMNSR', 935, 'O43093;', 'KD00995', 'Syncephalastrum racemosum (Filamentous fungus)', '', '#Kinesin heavy chain#Synkin', '-', '-', '-'),
(996, 'Q6CH63', 'Tethering factor for nuclear proteasome STS1', 'GO:0061638', 32841, '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}.', 'MMGSVVPLSSPAWDLNLSAGQNLLGHGSPTPSHSRKRRLSVTPEAGDSHMEHESPSKPRQQSPFVHKRARVTRQLQSRPLPMSRLLSSLDQKTLVSLLEGICAQDDRVARQVMEVTPKPTVSSAMDVLSRALDQAFALFPYKGDHQNDYAFFRVRPALEEFLAELSDYLSHFLPPNETQVSNSFAFLDQATSLVHRMPQWSSPANNRLKEETYEHIDVAWTLVCEEAAKRQRGSLAMSGVGNWLIRLEKHNELSGDRLKTSLHLLRDMLDDQGYRPPNPFASFNGAQQLFTV', 292, 'Q6CH63;', 'KD00996', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'STS1', '#Tethering factor for nuclear proteasome STS1', '-', '-', '2906519'),
(997, 'Q9UT81', 'UBX domain-containing protein 3', 'k', 44897, 'Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway. Involved in delivery of substrates to the 26S proteasome. Also required for membrane fusion and sporulation. {ECO:0000269|PubMed:15120077; ECO:0000269|PubMed:16303567}.', 'MDREDILKEFCNRNNIDVSQGRFFLESTNWNYELATALLHEVIPPEEDHGLQPSSDVSKVPEVTGSSSGISGGDQQPPRPLQRQQNTQGQGMKSGTASKKFATLRDLEGNDESAEEKSHLFTGGEKSGLSVEDGDPDPKKQLVRDILEKARQHTISPLDEQDSGPSSLASSWASVGQRLGTENEASGSTTPVTQSGPPRENPPTESQPEKPLRRTLYFWRNGFSVDDGPIYTYDDPANQEMLRYINSGRAPLHLLGVSMNQPIDVVVQHRMDEDYVAPFKPFSGKGQRLGSTYMQPRMSQMPGGLYTDTSTSSSVPINVKPNSTTPHASLQIDENKPTTRIQVRLSNGGRTVLTVNLSHTLHDIYEAVRAVSPGNFILSVPFPAKTLEDDPSVTVEAASLKNASLVQKSL', 410, 'Q9UT81;', 'KD00997', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ubx3', '#UBX domain-containing protein 3#Meiotically up-regulated gene 39 protein', '-', '-', '2543170'),
(998, 'Q2UEA0', 'Probable kinetochore protein nuf2', 'GO:0000778===GO:0051455===GO:0031617===GO:0031262', 54522, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MAYNHRMSQQFRGSQQHHGRGRKKEDENDALMRLPDKEIAGCINDIGIPFTAADLIKPNPQQIQMVFEWFAELLMNITHEAVEPAMRAAADDVGGDFPDIVPTDTRNLMGFFVSLRKLMMECGVNDFTFTDLTKPTHDRLVKIFSYLINFVRFRESQTPVIDEHFNKSEKTKARIDTLYAENQEMEQRLEEMRRNLRANEAQVKEKVRRNDELKARLLELRRNQERVAETLERVKADKTRRQTQLEEKTEKVVRTRQEVEKLRPYAMESPVSLQASLTELSENLLREKAQIDAMEKRARALQTSSDTFTVVSNDVQACVKLLEDISVELQKEEDEESRASRNKEAISERGNSVREVEQTEKLLQRQLARWNERIETLRKNAQEKAEAAQARMEELREVQKQLREERAEKQRDMERRRIRIEQTEKKMVDLKENIESEIQSAHDEYLRLESHIKLYITEMEKCI', 463, 'Q2UEA0;', 'KD00998', 'Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)', 'nuf2', '#Probable kinetochore protein nuf2', '-', '-', '5994145'),
(999, 'P40381', 'Chromatin-associated protein swi6', 'GO:0072356===k', 37293, 'Recognizes and binds histone H3 tails methylated at ''Lys-9''; leading to epigenetic repression. Involved in the repression of the silent mating-type loci MAT2 and MAT3. May compact MAT2/3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes.', 'MKKGGVRSYRRSSTSKRSVIDDDSEPELPSMTKEAIASHKADSGSSDNEVESDHESKSSSKKLKENAKEEEGGEEEEEDEYVVEKVLKHRMARKGGGYEYLLKWEGYDDPSDNTWSSEADCSGCKQLIEAYWNEHGGRPEPSKRKRTARPKKPEAKEPSPKSRKTDEDKHDKDSNEKIEDVNEKTIKFADKSQEEFNENGPPSGQPNGHIESDNESKSPSQKESNESEDIQIAETPSNVTPKKKPSPEVPKLPDNRELTVKQVENYDSWEDLVSSIDTIERKDDGTLEIYLTWKNGAISHHPSTITNKKCPQKMLQFYESHLTFRENE', 328, 'P40381;', 'KD00999', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'swi6', '#Chromatin-associated protein swi6', '-', '-', '2541633'),
(1000, 'Q9NDC9', 'Lissencephaly-1 homolog', 'GO:0000776===GO:0000777===GO:0005818===c;k', 45777, '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. Required for neuronal cell differentiation. {ECO:0000255|HAMAP-Rule:MF_03141; ECO:0000269|PubMed:11685578; ECO:0000269|PubMed:15254012; ECO:0000269|PubMed:15331665}.', 'MSLSERQKEEINRAIAEYMQNNGYSESFSVFLKESSLSENDIKPLGGILEKKWTTVLRLQRKVNDLESKLQESQREINHGAPTRDKRQAADWIPRPPETQKLTGHRLPITRVIFHPLWTIMASCSEDATIKVWDYETGQLERTLKGHTDAVNDIAIDAAGKQLVSCSSDLSIKLWDFGQTYDCLKSLKGHEHTVSSVTFLPTGDFVLSASRDHTIKQWDISTGYCVYTFRGHNDWVRMIRISNDGTLFASASLDQTVTVWSFATKSAKLVLRDHEHAVECVEWAPDTAYTNVTGQQPEGNSTHILFSGSRDRSIKAWNINTGDVLFTLLAHENWVRGLAFHPKGKYLISVADDKTLRVWELSAQRCMKAIEAHEHFVSTVAFHQTSPFVITGSVDMSCKVWECR', 404, 'Q9NDC9; O45742;', 'KD01000', 'Caenorhabditis elegans', 'lis-1', '#Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141}#Pronuclear migration abnormal protein 1', '-', '-', '176758'),
(1001, 'O60108', 'CENP-B homolog protein 2', 'GO:0000780===k', 59691, 'Binds to the central core and core-associated repeat regions of centromeric heterochromatin. {ECO:0000269|PubMed:11238404}.', 'MPPLRRQALTLAEKKAIRKHYFESATKPSQQELISWFEEHFHKKLAQSTVSSILSSKNEFLDNLDAENSQIRRNRQGKYPILENALIDWQTRLQKQDGAITGNAIKKSAAELWRRIPEYSELPIPEFSNGWLEKFKKRCLKHGLKLQGESTSVNQGTYEENMVQIQELISLFDPKDIFNMDETGLCWKLIPNQSPASERVKGITRDKARVTVTICCNATGSEKAPLWVIGYAKSPRAFRQANAHPDSMDFHWRYNGTARMTTSIMEEWLRWFDDLMKGRKVLLILDKFVAHECALENIRNSERKLVNTTVVFLPVNSTEIYHPCGQEIVYAFKSYYRKYWLNYMLEEIRLGKNPSKTMNVLKAVRWMIRSWNVDFEPSIIYNCFLRSGLFQNQQPLTGPSPETIRIAVNLQELIGKYLGDKDIFQIENFINPIEENSADTNDDIVNQVAAQFLDEREFETDEEEEESQYLLSTKDAINAINTLLNFQEQSEDGNVLFTRTLLQFQKVLESRSIV', 514, 'O60108;', 'KD01001', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cbh2', '#CENP-B homolog protein 2#CBHP-2', '-', '-', '2539728'),
(1002, 'Q09825', 'Spindle pole body-associated protein sad1', 'GO:0072766===GO:0000780', 58077, 'Associates with the spindle pole body and maintains a functional interface between the nuclear membrane and the microtubule motor proteins. Involved in chromosome segregation during meiosis where it associates with the telomeres. {ECO:0000269|PubMed:16615890}.', 'MFTNTPVGGKRERQNGAHPAWSTLGANSAQIHQNTADLASKMHKLRYTKIRSPPTRVSIESITPKQRFPAPNFEQAYHSNIRYEQEESDNEEFENVVKNGHEASTNVFYESDGDDEEFVNEEYENSIDEESDDEGYSLNEDTTATNASFRYPMNQRSTRKSQFYSSKFKPLLWFGITLFSTLLIITLLHKGQEFYSRSFSSDNSQPSNSPVPNIPPASNDTKTSLKPDIIKDFTDSPSKVGGNEEFDYSTGDLITKKEFDKILQQKVEQLKQSLKEEMSNYKSSVPFEVELNDDWKFFIESTVRKYLTDPVSMPNFALLSTGAEVLPALTSKRYVRRPSAFIPRFTSYFFDSLVVRGHEPSIALTPNNAVAMCWSFQGSEGQLGISLSRPVYVTNVTIEHVQHKIAHDLSSAPKDFELWVQGMSSKMFVLLGKARYSLTEDSIQTFSFESSNYIVAEPIQNVILKIKSNWGNPNYTCLYQVRVHGTVPNADEQPIPSLGEKAESTAENTGQDSS', 514, 'Q09825; Q9UU40;', 'KD01002', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'sad1', '#Spindle pole body-associated protein sad1', '-', '-', '2539914'),
(1003, 'Q9GYZ0', 'Kinesin-like protein KIF15', 'GO:0003777', 166590, 'Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. Plays a role in positioning spindle poles during mitosis; specifically at prometaphase. {ECO:0000269|PubMed:10931863}.', 'MSKKLKEQAANDASEGDAIKVFVRVRPSESHDADAAFGQCLEVRLPDTIIMHSKPEPKVFTYDHVTAANTTQESVFTAVGKRIIESCVGGFNGTIFAYGQTGSGKTFTMLGPCEDGDNFHHEMRGVIPRSFEYLFSLVNREREKHGDRYEFLCRCSFLEIYNEQIYDLLDPASLGLHLRENMKKGVFVDGLIERAVASASEAYGVLQAGWHNRRVAATSMNRESSRSHAVFTVSIESKEKKAGVSNIRVSQLHLVDLAGSERQKDTKAIGVRLKEAGSINKSLSILGNVIMALVDIAHGKQRHVPYRDSKLSFLLRDSLGGNAKTYIIANVHPDAKCFGETLSTLKFARRAKMIKNRAVVNEDTQGNVMHLQAEIRRLREALCMKGAEGSIPRGPSESGDSQMSNSSTESNGPVSGQQSGSSSSSKWKKYFLEAMSLRDIVEVEKREMREKVSSLEELCSKRDQVISSNKMIIKFRNSTIDMLQKTKNKALLKEDRDLLNENLKKEIEQLQEQLEHNPFVMRYVVENQSLRAQNKKLKMMEAVRSGEAMAATKAEELETLFLELREGLSKNRRYSSTPVDGEKVPTSTLVILKSQIKKLQDELENAKQEHAEQEEMTRTTRLDLESELAAYKKANLDMEKTLQGMKIKNRMDRDAMNDIHMQTIKSITTPKKVTYQLRSRTVLRTAGEETPGGPGFAGLSDNGSPLRSHSTNSLPPSGDILVTNSSPAMSEEGIIDEEMPEHVIEQCNEALTIELQKLQDKNANLQQQLEEHESQKHKMLQNSSKLDHQLQQITELYSTESQAWQEHEKDLTTRLAEATIQISTLQRDYEMTRGEAEDFKVMLQAADKEIGQEKKQKSKVTQDWDRVRAALDAQVVRLENEMCGQSRELENLTEDREQLQDAYNTLQAEHEFQQQREADLENRLKGKKAEITQLQEEIQKHLEKLDSERDKSMRLTAELRQGDNTKKDLLDAQELIDQFREERDDLLHRLDTEALKLSSSKEDLETVNSALTAIKKTDVEQKEALSSLMAALQGQKGMVKDKEEQLASMQMQLEDTRGQVSLLEAALEEGKASGAGLQSQIAALEDRMHAQAGEYQEQIEQMRADAMDANQHQKELLKELEKQSEELTQLHKQMKEKEEEYETKESEHKDTIESLEEQLEEVKTNLSTVVVELDEPESKKRKMADAQAMEIESLRDSEKRFKELSSVYDNMRDQMNEEIRSLKMKADELEDVRISKEILQAQHTALTYEIEQVRNEMAEKESSLKDEVNHLKRDMERQKTVLASMLRDKDEAVEKLYTVQTTLDQVKANEEILQENMDQVMEELDRTSALESTHFKEKEDIKSKLEEEREEKSKLTKDLTRLKEVYEEAEKKITELGGHQNPKQKIHHLQAVKSENYFLKEEVESLEKQLGKAQSDSEQMKRDYEALQKRLTSSSAEPPEEAGATTCIRCLPHSKRIMQTQTA', 1463, 'Q9GYZ0;', 'KD01003', 'Strongylocentrotus purpuratus (Purple sea urchin)', 'KIF15', '#Kinesin-like protein KIF15#Kinesin-related protein KRP180', '-', '-', '373236'),
(1004, 'Q8W1Y3', 'Kinesin KP1', 'GO:0003777', 121149, 'Required for keeping the ATP levels stable and balancing the aerobic respiration pathways during seed germination at low temperature. {ECO:0000269|PubMed:21406623}.', 'MDQGAMETLPEKPSEDEFSLALRNGLILCNVLNKVNPGSVLKVVENPITPAIQYADGAAQSAIQYFENMRNFLKAVEDMQLLTFGASDLEKGGSSNKVVDCILCLKGFYEWKQAGGVGVWRYGGTVRIVSFNRKGSSPPQYGIGSESTTDESVSLDESESSQYDQLLDFLHLSNEISAEESETAISLAFLFDHFALQLLHGYLKESDGINDMPLNEMVIDTLLNRVVKDFSAILVSQGAQLGSFLRKILKCDNGDLSRSEFLAAVFRYLQHRKDLVSKEFSKFCKCGGKLEFSRLNAREFSPGHVEAIGLQQKELEEVKSNFVETRSQVKQMQSEWQKELQRIVHHVKAMEVTSSSYHKVLEENRLLYNEVQDLKGTIRVYCRVRPFFQEQKDMQSTVDYIGENGNIIINNPFKQEKDARKIFSFNKVFGQTVSQEQIYIDTQPVIRSVLDGFNVCIFAYGQTGSGKTYTMSGPDLMTETTWGVNYRALRDLFQLSNARTHVVTYEIGVQMIEIYNEQVRDLLVSDGSSRRLDIRNNSQLNGLNVPDANLIPVSNTRDVLDLMRIGQKNRAVGATALNERSSRSHSVLTVHVQGKELASGSILRGCLHLVDLAGSERVEKSEAVGERLKEAQHINKSLSALGDVIYALAQKSSHVPYRNSKLTQVLQDSLGGQAKTLMFVHINPEVNAVGETISTLKFAQRVASIELGAARSNKETGEIRDLKDEISSLKSAMEKKEAELEQLRSGSIRNTTECQRARAVSPFHLPRTGNGAGTKAEASPQPNDGTRSYETRSCSTGKQRKSGFPSALRNREASPRMPNLAEERLNPSPSRRSLSTDRASTIKSRNKPDVTQNLPVSRTPFPARVPVVKSFSTVPLNPSAENNHRLHTDNSSEAFQNHQKLSARKLFPEIEEEHIRHALHIRQGGVKKTRAESSKAKAKQPSPARFQKLDVGISLRSDADSEAKVGNYQTQKGNNNHNVIHSRFQNFDVGISLFSDLCAGDKSDSTLKSDSSETDNEPPSKSKNAQRNSSKNSLNHKLRTIYAHEDTSLVDDKPSNGTAHIKEGNNNISMPEFRRSRSTHHARFMVP', 1087, 'Q8W1Y3; F4J373; O22240;', 'KD01004', 'Arabidopsis thaliana (Mouse-ear cress)', 'KP1', '#Kinesin KP1#Kinesin-like protein 1#AtKP1', '-', '-', '823602'),
(1005, 'Q96GD4', 'Aurora kinase B', 'GO:0034501===GO:0008608===GO:0032133===GO:0000779===GO:0000780===k;m;s', 39311, 'Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint; a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C; leading to retain abscission- competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (PubMed:22422861; PubMed:24814515). AURKB phosphorylates the CPC complex subunits BIRC5/survivin; CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA; DES/desmin; GPAF; KIF2C; NSUN2; RACGAP1; SEPT1; VIM/vimentin; GSG2/Haspin; and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process; whereas histone H3 is phosphorylated at ''Ser-10'' and ''Ser-28'' during mitosis (H3S10ph and H3S28ph; respectively). A positive feedback between GSG2 and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells; inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. {ECO:0000269|PubMed:11516652; ECO:0000269|PubMed:11756469; ECO:0000269|PubMed:11784863; ECO:0000269|PubMed:11856369; ECO:0000269|PubMed:12458200; ECO:0000269|PubMed:12686604; ECO:0000269|PubMed:12689593; ECO:0000269|PubMed:12925766; ECO:0000269|PubMed:14602875; ECO:0000269|PubMed:14610074; ECO:0000269|PubMed:14722118; ECO:0000269|PubMed:15020684; ECO:0000269|PubMed:15249581; ECO:0000269|PubMed:16103226; ECO:0000269|PubMed:17617734; ECO:0000269|PubMed:20959462; ECO:0000269|PubMed:21658950; ECO:0000269|PubMed:22422861; ECO:0000269|PubMed:24814515}.', 'MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA', 344, 'Q96GD4; B4DNM4; C7G533; C7G534; C7G535; D3DTR4; J9JID1; O14630;O60446; O95083; Q96DV5; Q9UQ46;', 'KD01005', 'Homo sapiens (Human)', 'AURKB', '#Aurora kinase B#2.7.11.1#Aurora 1#Aurora- and IPL1-like midbody-associated protein 1#AIM-1#Aurora/IPL1-related kinase 2#ARK-2#Aurora-related kinase 2#STK-1#Serine/threonine-protein kinase 12#Serine/threonine-protein kinase 5#Serine/threonine-protein kinase aurora-B', '-', 'ENSG00000178999', '-'),
(1006, 'O43463', 'Histone-lysine N-methyltransferase SUV39H1', 'k', 47907, 'Histone methyltransferase that specifically trimethylates ''Lys-9'' of histone H3 using monomethylated H3 ''Lys- 9'' as substrate. Also weakly methylates histone H1 (in vitro). H3 ''Lys-9'' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1; CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 ''Lys-9'' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes; such as repression of MYOD1-stimulated differentiation; regulation of the control switch for exiting the cell cycle and entering differentiation; repression by the PML-RARA fusion protein; BMP-induced repression; repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex; a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone- modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation; elevation of NAD(+)/NADP(+) ratio activates SIRT1; leading to histone H3 deacetylation followed by dimethylation of H3 at ''Lys-9'' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1; contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 ''Lys-9'' trimethylation. {ECO:0000269|PubMed:14765126; ECO:0000269|PubMed:16449642; ECO:0000269|PubMed:16818776; ECO:0000269|PubMed:16858404; ECO:0000269|PubMed:18004385; ECO:0000269|PubMed:18485871}.', 'MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKGIRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF', 412, 'O43463; B2R6E8; B4DST0; Q53G60; Q6FHK6;', 'KD01006', 'Homo sapiens (Human)', 'SUV39H1', '#Histone-lysine N-methyltransferase SUV39H1#2.1.1.43#Histone H3-K9 methyltransferase 1#H3-K9-HMTase 1#Lysine N-methyltransferase 1A#Position-effect variegation 3-9 homolog#Suppressor of variegation 3-9 homolog 1#Su(var)3-9 homolog 1', '-', 'ENSG00000101945', '-'),
(1007, 'F4IVI0', 'Mitotic checkpoint serine/threonine-protein kinase BUB1', 'GO:0000777', 61123, '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. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C). Necessary for ensuring proper chromosome segregation. Can regulate chromosome segregation in a kinetochore- independent manner. 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. 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 (By similarity). {ECO:0000250}.', 'MTIGYRDAAGDPLFPWLMEIKNSMEDLYAGKNSGYDLDKLLFDCISTYKKDSRYRNDLRFLKIWFLYLEGREDFERVYREIEETEICKGHSLLYEWYAIFLEVKGLWRRANSVYQTGLSRKAEPFDRLKEAHSLFLQRISKRTKASSLEKVGDDAQATDLETGFVNPWETSTVNGLIHKIKPQLVKYDGYHVSNKVFPGKANLSSLQNYSRNKIIEIGGRKYQMKGCAGQGGFAQVFKAFIDSNPDEVVALKVQKPPFPWEFHMYRQLDCRIPDSQRSSFGLAQRVHVYSDYSILVCDYLSHGTLQDVINSYVVVGKSMEEVLCMYYTIEMLNMLETLHSVGIIHGDFKPDNLLIRYPPENLTETGFHEKTGSWSKKGLCLVDWGRGIDLSLFPRTTEFTGDCRTSGFRCVEMKEDKPWKFQVDTYGLCVIVHMMLHNVYMEIEKKQSLDGGYINMPRTSFKRYWKVDLWKELFTKLLNRETCEDDTETLRNLRKSMEEYICSDPKLMKKLNELLAKQRISLCSS', 525, 'F4IVI0; Q8S8D9;', 'KD01007', 'Arabidopsis thaliana (Mouse-ear cress)', 'BUB1', '#Mitotic checkpoint serine/threonine-protein kinase BUB1#AtBUB1#2.7.11.1#Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 1', '-', '-', '816591'),
(1008, 'Q8S905', 'Kinesin-like protein NACK1', 'GO:0003777', 110174, 'Probable plus end-directed motor protein that functions in a MAP kinase signaling pathway (ANP1-MKK6-MPK4); which is essential for somatic cell cytokinesis; especially for the cell- plate formation and its expansion. Regulates the activity and the localization of ANP1; probably by association through the non- catalytic region of the kinase. Functionally redundant with NACK2 and essential to promote the progression of cytokinesis and for cellularization (formation of the cell plate) during microgametogenesis and megagametogenesis. {ECO:0000269|PubMed:11818068; ECO:0000269|PubMed:11955449; ECO:0000269|PubMed:15569152; ECO:0000269|PubMed:19825582; ECO:0000269|PubMed:20802223; ECO:0000269|PubMed:22006334}.', 'MTIKTPGTPVSKMDRTPAVTPGGSSRSREEKIVVTVRLRPMNKRELLAKDQVAWECVNDHTIVSKPQVQERLHHQSSFTFDKVFGPESLTENVYEDGVKNVALSALMGINATIFAYGQTSSGKTYTMRGVTEKAVNDIYNHIIKTPERDFTIKISGLEIYNENVRDLLNSDSGRALKLLDDPEKGTVVEKLVEETANNDNHLRHLISICEAQRQVGETALNDTSSRSHQIIRLTIQSTHRENSDCVRSYMASLNFVDLAGSERASQSQADGTRLREGCHINLSLMTLTTVIRKLSVGKRSGHIPYRDSKLTRILQHSLGGNARTAIICTLSPALAHVEQSRNTLYFANRAKEVTNNAHVNMVVSDKQLVKHLQKEVARLEAERRTPGPSTEKDFKIQQMEMEIGELRRQRDDAQIQLEELRQKLQGDQQQNKGLNPFESPDPPVRKCLSYSVAVTPSSENKTLNRNERARKTTMRQSMIRQSSTAPFTLMHEIRKLEHLQEQLGEEATKALEVLQKEVACHRLGNQDAAQTIAKLQAEIREMRTVKPSAMLKEVGDVIAPNKSVSANLKEEITRLHSQGSTIANLEEQLESVQKSIDKLVMSLPSNISAGDETPKTKNHHHQSKKKKLLPLTPSSASNRQNFLKSPCSPLSASRQVLDCDAENKAPQENNSSAARGATTPQGSEKETPQKGEESGDVSSREGTPGYRRSSSVNMKKMQQMFQNAAEENVRSIRAYVTELKERVAKLQYQKQLLVCQVLELEANDGAGYSVENEENTIMEDEEQNQVAWHITFIEERQQIIELWHVCHVSIIHRTQFYLLFKGDQADQIYMEVELRRLTWLEQHLAEVGNATPARNCDESVVSLSSSIKALRREREFLAKRVNSRLTPEEREELYMKWDVPLEGKQRKLQFVNKLWTDPYDSRHVQESAEIVAKLVGFCESGNISKEMFELNFAVPSDKRQWNIGWDNISNLLHL', 974, 'Q8S905; Q9LPQ5;', 'KD01008', 'Arabidopsis thaliana (Mouse-ear cress)', 'NACK1', '#Kinesin-like protein NACK1#AtNACK1#NPK1-activating kinesin-1#Protein HINKEL', '-', '-', '838418'),
(1009, 'Q6FU86', 'DASH complex subunit SPC19', 'GO:0008608===GO:0042729', 17278, '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}.', 'MQSLEQCVNSLEAIVHQLDGSVSRLARNGEASNELCEGILKIKRVFELVPEYDVESARLALFEEVDPMVKTLGDKIEKALIRKRRELENLRQTSELNSLRLSGDLYFSETGIDNQDMDVSTDAIAIASATDAELDELRALKARRAELQELLDGR', 154, 'Q6FU86;', 'KD01009', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'SPC19', '#DASH complex subunit SPC19#Outer kinetochore protein SPC19', '-', '-', '2887932'),
(1010, 'O44956', 'KBP-5', 'k', 15744, '', 'MNPNHNEGLLELYTQAISLEALKDAEQFLENSLLGKDAQVERLLAQVLIEEQQIETNRKKIAQLRIEKEELEFDCANSDLKSLEQMQAERDELQRKCQPGQHTKSNHKSSEQLLRMKKETDALRAYMKKISQFED', 135, 'O44956;', 'KD01010', 'Caenorhabditis elegans', 'kbp-5', '#KBP-5 {ECO:0000313|EMBL:CCD62120.1}', '-', '-', '172970'),
(1011, 'Q754U2', 'DASH complex subunit DAD3', 'GO:0008608===GO:0051987===GO:0042729', 9359, '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}.', 'MSDALSTLQRSVLEKYRTLADCLHELNDTLVELNTDSDTNPEQVLAQMREIEVKIALVGTLLKGSVYSLVLQRNMGKQAPGGKAK', 85, 'Q754U2;', 'KD01011', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DAD3', '#DASH complex subunit DAD3#Outer kinetochore protein DAD3', '-', '-', '4621760'),
(1012, 'Q7JZC9', 'Nnf1aRE42502p', 'k', 22485, '', 'MEDSEAAFKRHEGVGPKVKQAYEEAIKQIFADLSCADLQAWDAIYQEHEQSALDTESIVDRTRSLMTKVVLEMNRCFFASNDVPNKLQTLEMLKEHFAAYEGKKWNVNTAAPDKLTRPLRMRFLDFSVEFMEQQLASQAKELEIAMAKSNANRERLQHVHDKRLKLTVQMEQQLSQYEKVKTELIKLGEALNDF', 194, 'Q7JZC9;', 'KD01012', 'Drosophila melanogaster (Fruit fly)', 'Nnf1a', '#Nnf1a {ECO:0000313|EMBL:AAF57451.1}#RE42502p {ECO:0000313|EMBL:AAL49009.1}', '-', '-', '37325'),
(1013, 'Q6SKR5', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262===SCL===k', 26704, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:14738735}.', 'MSALKMDDEQSLNVYMQEFRTRFINKSSDEMTSQALKESYKESAATDAWFKKYRDGELMIEKVLEFRNEITLQNKRIEEKQKNILQEAAKQDDHEQLKGELTERIQRLREELNQKREVALANRKANKERIKELQKSATLFKERLGLEIRKLRGDKLQFVFRCINPKDLDQPYSCIISLNAEGDYEVAGCDPPLECIAEFQEKIRETRNFSALLANLRKSFTALGSQVK', 228, 'Q6SKR5; Q6DDZ6;', 'KD01013', 'Xenopus laevis (African clawed frog)', 'spc25', '#Kinetochore protein Spc25#xSpc25', '-', '-', '100101271'),
(1014, 'O43068', 'Monopolin complex subunit mde4', 'GO:0051315===GO:0051456===GO:0033551===k', 47664, '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. {ECO:0000269|PubMed:17627824}.', 'MSTISTSTDSKLDNLGLSVTSRRNQILFYLSKALNLAHLLRSDSLQKSFLDALKQSATDSELLHKNLDEIKFLQNEKLNNEKLLEQEQNEANDYRLKVERLEHKISDYVQEINSLNSQLQIQKSNPEKHEDAVSQNRLRGSLDTVSSPSKTHKANKDEKATRLHLIIANLKKALKEKDAEVLNLQSHVSSKESELDRFKIKLETEESNWKVRLQVLESKLATQDRKLRMQKKSTERKSLLVSPRVSSPKLFSPSKQAIMGTRQPNATSGSPLSVTPFLQKTSTSIGLSSSPPQSSPSAQSSQPFSRDKYPHSMTVSPSNARYLKKHLDDTIPSNVSDINHNDHLKIPQSPSSLSPSKIPIRKKRKLKDTVSNCEFTEEDSESSFLLETIQPTKSTLRRSISPLKKRNDEINELKKGFTMKK', 421, 'O43068;', 'KD01014', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mde4', '#Monopolin complex subunit mde4#Mei4-dependent protein 4', '-', '-', '2541155'),
(1015, 'Q54DM1', 'Mitotic checkpoint protein bub3', 'GO:0000776', 37420, 'Involved in cell cycle checkpoint enforcement. {ECO:0000250}.', 'MSNEPTSSFYELRLPPSDGISSVNFCPNSVNLLVTSWDSTVRCYDTQNNVQKWQYNHKGPVMDGCFPEKNKVFSGDVFGSVKHYDPVAGVEKEVGSHEDGVRSVVYNSDTQQLFTGGWDQQLKLWDIRSDKMEISNHDLQSKIFTMDVSPISNMLVIGTADKYVTIYDTRQMETHLQKRESSIKYQTRCIRTFTDGKGYALASVEGRIAMEYFDPSPAVQSKKYAFKCHRLTESGVDVVYPVNCIAFNPHYGTFATGGCDKNVFFWDGANRKRLHALKTYPTSISSMSFNTDGNILAVASSYTFEEGEKDHPPDQIFIHNILSEKIIKPIK', 331, 'Q54DM1;', 'KD01015', 'Dictyostelium discoideum (Slime mold)', 'bub3', '#Mitotic checkpoint protein bub3', '-', '-', '8628531'),
(1016, 'A1Z8E9', 'Bardet-Biedl syndrome 4 protein homolog', 'GO:0003777', 55632, 'May be required for microtubule anchoring at the centrosome. Required for ciliogenesis (By similarity). {ECO:0000250}.', 'MYEPGTEQINCNGRLIELPTLEVVRPAPKMPSDANIDWLLHIYFTRREFTRCRRLIERELNRHLNPEYLYFVQGLIDREEGNHIEALRHLQKSAELNPRNIETYKEIGRTLYIMGRFSQALGVFREAEQRSSRQDHEIYHYLGELLYRAATTQSQKDVASQQQDEARTYFELAVQSGRKLESYVRLAELYRKDKQYQKAIEILENCLHLTPENSEVLIEISVLYLKINETQKAHDRLAEVVSIERKCSPKGLLAFGAILQSRNDIDGALSKYSQIANAEPEIAELWNNIGLCFFKKQKFIVAISSLRKSVWLSPLNYNALYNLSLIYIASEQYASAFHTLAAAINLRKDNAECYMLLGLCLRKLDDMENAFVALERASSMATGQQGAGRNPLVVLNFALFCYETGRLALSTEQYNRFMSQAQDLLLPTEYKFQATKLKSLLRISNQGNGILLDSADMGESDLGHNRATELLPDELPLEVNAVVSQN', 486, 'A1Z8E9;', 'KD01016', 'Drosophila melanogaster (Fruit fly)', 'BBS4', '#Bardet-Biedl syndrome 4 protein homolog', '-', '-', '36167'),
(1017, 'Q9P2P6', 'StAR-related lipid transfer protein 9', 'GO:0003777', 516343, 'Microtubule-dependent motor protein required for spindle pole assembly during mitosis. Required to stabilize the pericentriolar material (PCM). {ECO:0000269|PubMed:22153075}.', 'MANVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRPDGFGDSREKVMAFGFDYCYWSVNPEDPQYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSSCRIKVSFLEIYNERVRDLLKQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNLPSEMASKINLVDLAGSERADPSYCKDRIAEGANINKSLVTLGIVISTLAQNSQVFSSCQSLNSSVSNGGDSGILSSPSGTSSGGAPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVNEDANLKLIRELREEIERLKALLLSFELRNFSSLSDENLKELVLQNELKIDQLTKDWTQKWNDWQALMEHYSVDINRRRAGVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVNGREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQRRQVGEAAAGRGSLEWLDLDGDLAASRLGLSPLLWKERRALEEQCDEDHQTPRDGETSHRAQIQQQQSYVEDLRHQILAEEIRAAKELEFDQAWISQQIKENQQCLLREETWLASLQQQQQEDQVAEKELEASVALDAWLQTDPEIQPSPFVQSQKRVVHLQLLRRHTLRAAERNVRRKKVSFQLERIIKKQRLLEAQKRLEKLTTLCWLQDDSTQEPPYQVLSPDATVPRPPCRSKLTSCSSLSPQRLCSKHMPQLHSIFLSWDPSTTLPPRPDPTHQTSEKTSSEEHLPQAASYPARTGCLRKNGLHSSGHGQPCTARAALARKGASAPDACLTMSPNSVGIQEMEMGVKQPHQMVSQGLASLRKSANKLKPRHEPKIFTSTTQTRGAKGLADPSHTQAGWRKEGNLGTHKAAKGASCNSLYPHGPRQTAGHGKAVKTFWTEYKPPSPSRASKRHQRVLATRVRNITKKSSHLPLGSPLKRQQNTRDPDTMVPLTDFSPVMDHSREKDNDLSDTDSNYSLDSLSCVYAKALIEPLKPEERKWDFPEPENSESDDSQLSEDSLAEKRYQSPKNRLGGNRPTNNRGQPRTRTRASVRGFTAASDSDLLAQTHRSFSLDSLIDAEEELGEDQQEEPFPGSADEIPTETFWHLEDSSLPVMDQEAICRLGPINYRTAARLDAVLPMSSSFYLDPQFQPHCELQPHCELQPHCELQPHCEQAESQVEPSYSEQADSLQGMQLSRESPLMSMDSWFSCDSKINPSSPPGIVGSLCPSPDMQEFHSCKGERPGYWPNTEELKPSDAETVLPYSSKLHQGSTELLCSARDEHTASAADTSRLSLWGIQRLIQPGADGTFQGRCIPDMTQQGSSEASHNSSVSNVLAASATTLTHVGSTHERDWSALQQKYLLELSCPVLEAIGAPKPAYPYLEEDSGSLAQASSKGGDTLLPVGPRVSSNLNLNNFPVHLSRIRRLRAEKEQDSLNAKLEGVSDFFSTSEKEASYDETYSADLESLSASRSTNAQVFATENAIPDSMTEACEVKQNNLEECLQSCRKPGLMTSSDEDFFQKNACHSNVTTATKADHWSQGWAPLRKNSAVQPGQLSPDSHYPLEEEKTDCQESSKEAVRRHINVSFALPSGPELYLHSAPWNPLSSSLQPPLLETFYVTKSRDALTETALEIPACREVRVPSPPPREAWGFGHNHQALQGAYLKNNLPVLLQNQNSKIASSQQVTAEIPVDLNTREVIRESGKCPGNITEESHDSVYSSVTQNRHFLPSTSTKVCEFENQVVILNKKHSFPALEGGEVTAQSCCGASSDSTESGKSLLFRESEAREEEELDQNTVLRQTINVSLEKDMPGESAVSLKSRSVDRRVSSPVMVAQGGGPTPKWEGKNETGLLEKGLRPKDSSEEFKLPGTKPAYERFQLVACPQERNPSECKSQEMLNPNREPSGKKQNKRVNNTDEMARLIRSVMQLENGILEIESKQNKQVHASHTPGTDKELVFQDQKEQEKTDHAFRPDSSGNPLPSKDQPSSPRQTDDTVFRDSEAGAMEVNSIGNHPQVQKITPNPFRSREGVRESEPVREHTHPAGSDRPARDICDSLGKHTTCREFTNTSLHPQRMKALARALPLQPRLERSSKNNGQFVKASASLKGQPWGLGSLEELETVKGFQESQVAEHVSSSNQEEPKAQGKVEEMPMQRGGSLQEENKVTQKFPSLSQLCRDTFFRQETVSPLLSRTEFCTAPLHQDLSNTLPLNSPRWPRRCLHVPVALGISSLDCVLDLTMLKIHNSPLVTGVEHQDQSTETRSHSPEGNVRGRSSEAHTAWCGSVRSMAMGSHSQSGVPESIPLGTEDRISASTSPQDHGKDLRITLLGFSTSEDFASEAEVAVQKEIRVSSLNKVSSQPEKRVSFSLEEDSDQASKPRQKAEKETEDVGLTSGVSLAPVSLPRVPSPEPRLLEPSDHASMCLAILEEIRQAKAQRKQLHDFVARGTVLSYCETLLEPECSSRVAGRPQCKQIDQSSSDQTRNEGEAPGFHVASLSAEAGQIDLLPDERKVQATSLSADSFESLPNTETDREPWDPVQAFSHAAPAQDRKRRTGELRQFAGASEPFICHSSSSEIIEKKKDATRTPSSADPLAPDSPRSSAPVEEVRRVVSKKVVAALPSQAPYDDPRVTLHELSQSVPQETAEGIPPGSQDSSPEHQEPRTLDTTYGEVSDNLLVTAQGEKTAHFESQSVTCDVQNSTSASGPKQDHVQCPEASTGFEEGRASPKQDTILPGALTRVALEAPTQQCVQCKESVGSGLTEVCRAGSKHSRPIPLPDQRPSANPGGIGEEAPCRHPREALDGPVFSRNPEGSRTLSPSRGKESRTLPCRQPCSSQPVATHAYSSHSSTLLCFRDGDLGKEPFKAAPHTIHPPCVVPSRAYEMDETGEISRGPDVHLTHGLEPKDVNREFRLTESSTCEPSTVAAVLSRAQGCRSPSAPDVRTGSFSHSATDGSVGLIGVPEKKVAEKQASTELEAASFPAGMYSEPLRQFRDSSVGDQNAQVCQTNPEPPATTQGPHTLDLSEGSAESKLVVEPQHECLENTTRCFLEKPQFSTELRDHNRLDSQAKFVARLKHTCSPQEDSPWQEEEQHRDQASGGGEGFAQGVNPLPDEDGLDGCQILDAGREEVAVAKPPVSKILSQGFKDPATVSLRQNETPQPAAQRSGHLYTGREQPAPNHRGSLPVTTIFSGPKHSRSSPTPQFSVVGSSRSLQELNLSVEPPSPTDEDTQGPNRLWNPHLRGYSSGKSVARTSLQAEDSNQKASSRLDDGTTDHRHLKPATPPYPMPSTLSHMPTPDFTTSWMSGTLEQAQQGKREKLGVQVRPENWCSQMDKGMLHFGSSDISPYALPWRPEEPARISWKQYMSGSAVDVSCSQKPQGLTLSNVARCSSMDNGLEDQNSPFHSHLSTYANICDLSTTHSSTENAQGSNEAWEVFRGSSSIALGDPHIPTSPEGVAPTSGHDRRPQFRGPSGEADCLRSKPPLAKGSAAGPVDEIMLLYPSEAGCPVGQTRTNTFEQGTQTLGSRRHWSSTDISFAQPEASAVSAFDLASWTSMHNLSLHLSQLLHSTSELLGSLSQPDVARREQNTKRDIPDKAPQALMMDGSTQTTVDEGSQTDLTLPTLCLQTSEAEPQGANVILEGLGSDTSTVSQEEGDVPGVPQKREAEETAQKMAQLLYLQEESTPYKPQSPSIPSSHLRFQKAPVGQHLPSVSPSVSDAFLPPSSQPEESYCLVVSSPSPSSPHSPGLFPSTSEYPGDSRVQKKLGPTSALFVDRASSPILTLSASTQEPGLSPGSLTLSAPSTHPVEGHQKLDSSPDPVDAPRTPMDNYSQTTDELGGSQRGRSSLQRSNGRSFLELHSPHSPQQSPKLQFSFLGQHPQQLQPRTTIGVQSRLLPPPLRHRSQRLGNSFVPEKVASPEHCPLSGREPSQWQSRTENGGESSASPGEPQRTLDRPSSWGGLQHLSPCPVSELTDTAGLRGSALGLPQACQPEELLCFSCQMCMAPEHQHHSLRDLPVHNKFSNWCGVQKGSPGGLDMTEEELGASGDLSSEKQEQSPPQPPNDHSQDSEWSKREQIPLQVGAQNLSLSVELTEAKLHHGFGEADALLQVLQSGTGEALAADEPVTSTWKELYARQKKAIETLRRERAERLGNFCRTRSLSPQKQLSLLPNKDLFIWDLDLPSRRREYLQQLRKDVVETTRSPESVSRSAHTPSDIELMLQDYQQAHEEAKVEIARARDQLRERTEQEKLRIHQKIISQLLKEEDKLHTLANSSSLCTSSNGSLSSGMTSGYNSSPALSGQLQFPENMGHTNLPDSRDVWIGDERGGHSAVRKNSAYSHRASLGSCCCSPSSLSSLGTCFSSSYQDLAKHVVDTSMADVMAACSDNLHNLFSCQATAGWNYQGEEQAVQLYYKVFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTARLHQRVTNSISLVYLVCNTTLCALKQPRDFCCVCVEAKEGHLSVMAAQSVYDTSMPRPSRKMVRGEILPSAWILQPITVEGKEVTRVIYLAQVELGAPGFPPQLLSSFIKRQPLVIARLASFLGR', 4700, 'Q9P2P6; Q68DG2; Q6AI01; Q6ZWK0; Q9UF70;', 'KD01017', 'Homo sapiens (Human)', 'STARD9', '#StAR-related lipid transfer protein 9#START domain-containing protein 9#StARD9', '-', 'ENSG00000159433', '-'),
(1018, 'P11103', 'Poly [ADP-ribose] polymerase 1', 'k', 113100, 'Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK; forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN- gamma to directly regulate its transcription; and is thus involved importantly in Th1 cytokine production (By similarity). Involved in the base excision repair (BER) pathway; by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1; UIMC1/RAP80; and BRCA1 to DNA damage sites (By similarity). {ECO:0000250}.', 'MAEASERLYRVQYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGQSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVAGKGQDGSGGKAEKTLGDFAAEYAKSNRSMCKGCLEKIEKGQMRLSKKMVDPEKPQLGMIDRWYHPTCFVKKRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAIKNEGKRKGDEVDGTDEVAKKKSRKETDKYSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRKEWVTPKEFREISYLKKLKVKKQDRIFPPESSAPITVHWPLSVTSAPTAVNSSAPADKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKASLCISIKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQDLLSAHSLSPWGAEVKAEPGEVVAPRGKSAAPSKKSKGCFKEEGVNKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRLGTVIGSNKLEQMPSKEEAVEQFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVKPGTKSKLPKPVQELVGMIFDVDSMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQPVSQGSSESQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLIMLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSASITLEGVEVPLGTGIPSGVNDTALLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW', 1013, 'P11103; Q9JLX4; Q9QVQ3;', 'KD01018', 'Mus musculus (Mouse)', 'Parp1', '#Poly [ADP-ribose] polymerase 1#PARP-1#2.4.2.30#ADP-ribosyltransferase diphtheria toxin-like 1#ARTD1#NAD(+) ADP-ribosyltransferase 1#ADPRT 1#Poly[ADP-ribose] synthase 1#msPARP', '-', '-', '-'),
(1019, 'Q9V8W3', 'Rab proteins geranylgeranyltransferase component A', 'GO:0005818', 56827, 'Binds unprenylated Rab proteins; presents it to the catalytic component B; and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab to a protein acceptor (By similarity). {ECO:0000250}.', 'MLDDLPEQFDLVVIGTGFTESCIAAAGSRIGKSVLHLDSNEYYGDVWSSFSMDALCARLDQEVEPHSALRNARYTWHSMEKESETDAQSWNRDSVLAKSRRFSLDLCPRILYAAGELVQLLIKSNICRYAEFRAVDHVCMRHNGEIVSVPCSRSDVFNTKTLTIVEKRLLMKFLTACNDYGEDKCNEDSLEFRGRTFLEYLQAQRVTEKISSCVMQAIAMCGPSTSFEEGMQRTQRFLGSLGRYGNTPFLFPMYGCGELPQCFCRLCAVYGGIYCLKRAVDDIALDSNSNEFLLSSAGKTLRAKNVVSAPGYTPVSKGIELKPHISRGLFISSSPLGNEELNKGGGGVNLLRLLDNEGGREAFLIQLSHYTGACPEGLYIFHLTTPALSEDPASDLAIFTSQLFDQSDAQIIFSSYFTIAAQSSKSPAAEHIYYTDPPTYELDYDAAIANARDIFGKMFPDADFLPRAPDPEEIVVDGEDPSALNEHTLPEDLRAQLHDMQQATQEMDIQE', 511, 'Q9V8W3; O97142;', 'KD01019', 'Drosophila melanogaster (Fruit fly)', 'Rep', '#Rab proteins geranylgeranyltransferase component A#Rab escort protein homolog#REP', '-', '-', '37246'),
(1020, 'Q969G3', 'SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1', 'k', 46649, 'Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons; npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A; are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Required for the coactivation of estrogen responsive promoters by Swi/Snf complexes and the SRC/p160 family of histone acetyltransferases (HATs). Also specifically interacts with the CoREST corepressor resulting in repression of neuronal specific gene promoters in non-neuronal cells. {ECO:0000250}.', 'MSKRPSYAPPPTPAPATQMPSTPGFVGYNPYSHLAYNNYRLGGNPGTNSRVTASSGITIPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQSSIVPEEEQAANKGEEKKDDENIPMETEETHLEETTESQQNGEEGTSTPEDKESGQEGVDSMAEEGTSDSNTGSESNSATVEEPPTDPIPEDEKKE', 411, 'Q969G3; B3KMC1; B4DFR4; C0IMW4; C0IMW5; C0IMW7; H7C3F6; O43539;', 'KD01020', 'Homo sapiens (Human)', 'SMARCE1', '#SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1#BRG1-associated factor 57#BAF57', '-', 'ENSG00000073584', '-'),
(1021, 'Q04431', 'Spindle pole body component KRE28', 'GO:0000778', 44675, 'Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1; BIK1 and SLK19) and motors (CIN8; KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint. {ECO:0000269|PubMed:19893618}.', 'MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKILSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQETGHNFAERQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQRLTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDMQYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEASSKFNNKYRNNTKVQIFEVMDDIISELTNE', 385, 'Q04431; D6VTF3; Q6Q537;', 'KD01021', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '852145'),
(1022, 'Q6XXL8', 'Dynein light chain Tctex-type 3', 'GO:0000777===GO:0005868', 13037, '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}.', 'MEEYHRPCDEVGFNADEAHNIVKECIDGVLGGEDYNQNNINQWTASIVEQSLAHLVKLGKAYKYIVTCAVVQRSPYGFHTASSCFWDTTSDGTCTVRWENRTMNCIVNVFAIAIVL', 116, 'Q6XXL8;', 'KD01022', 'Ovis aries (Sheep)', 'DYNLT3', '#Dynein light chain Tctex-type 3#T-complex-associated testis-expressed 1-like', '-', '-', '443256'),
(1023, 'O97102', 'CG4494-PALD07775pSmt3Ubiquitin-like protein SMT3', 'k;m', 10124, '', 'MSDEKKGGETEHINLKVLGQDNAVVQFKIKKHTPLRKLMNAYCDRAGLSMQVVRFRFDGQPINENDTPTSLEMEEGDTIEVYQQQTGGAP', 90, 'O97102;', 'KD01023', 'Drosophila melanogaster (Fruit fly)', 'smt3', '#CG4494-PA {ECO:0000313|EMBL:AAF52470.1}#LD07775p {ECO:0000313|EMBL:AAL28638.1}#Smt3 {ECO:0000313|EMBL:AAF31702.1}#Ubiquitin-like protein SMT3 {ECO:0000313|EMBL:AAD19219.1}', '-', '-', '33981'),
(1024, 'Q6FXI5', 'Kinesin-like protein CIN8', 'GO:0003777', 111387, 'Required for assembly of the mitotic spindle. Interact with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly; CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediated by KAR3 (By similarity). {ECO:0000250}.', 'MVVTTEAVTSRSERDAEPVQEPLVEKLATEELNILVAVRCRGRNEREIKAKSSVVVDVPDNGVTNEVSINTTDDVGIAAKMNSKTYTVDKVFGPSASQKLVYEEIAEPLFQDFIKGYNCTILVYGMTSTGKTYTMTGDEKLHNGELGDAAGIIPRVLFELFDTLEANKDDYLVKCSFVELYNEELKDLLDSTNTATNSDNKKLRIFDSNVNGTSASGSSSRSSSRNNSPRSAPDNSRAQMLRRKLGRHNTTGNSKISNNNHNKFSRFKQTSQESTRAHASNNHQNVHIPNNNSNNTNQQQSPIDQSASIYIQNLEEFHITSAMEGLQLLQKGLKQRQVASTKMNDFSSRSHSIFTITLYKEQNGELFRVSKMNLVDLAGSENISRSGAMNQRAKEAGSINQSLLTLGRVINSLADKSEHIPFRESKLTRLLQDSLGGNTKTALIATISPAKMTSEETCSTLEYASKAKNIKNKPQLGAFIMKDILVRSITSELAKIKSDLLSTKSKEGVYMSHEHYKDLHYDIECYKTELEESKRAIESLTAQNAMLQQERLSLKDDNACYKANIASLKDNVVTLQSSLKEQITKETNIRSLLKDVQGANEEMKKTIHLFEFKQQELQQSISTFISDEISNIRDTLKKHIEYLQNNGDLKDTEISGNLMRLEKEVVKVIKAAEEEASKSYGECVKMMLKETPRLFESVSGRLDNISKLAEENHSKIAETLSDVSEEYNNLKQYLTNNFFKNNHEELLSHHVQNTYAQLEENSAQLMQNFTMMLDKHIQENKRHMLENILGVTDEVINNELQMFGEQRAKWEKSSALINQCDSVNHSFHQALGSNLVEIRDVVSSSRDNIGATISSIQSRTRNRQSIEEMIQGNDVIRQQITRIKQKNKSLSLFKEHSTETATTSIGSVNKVEGNLKVIMDKVLNDPQLSRGKAEVPDEELHRLEKIPLGITNKENVVDLQHRYPALQEKRKPEDEVLLQAKLQRRNPD', 988, 'Q6FXI5;', 'KD01024', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'CIN8', '#Kinesin-like protein CIN8', '-', '-', '2886646'),
(1025, 'P78759', 'Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 2 isoform', 'k;m', 72465, '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. Has a role in cell shape control and septum formation. {ECO:0000269|PubMed:10757751; ECO:0000269|PubMed:11380623}.', 'MKGLRSKFVKALSLKDEQGSHKNGHSKSHYISKNGSYVETDDVKHTDTHHSSKHELKKLKSHFLKDTLKHKRNHHANSNNEKHENSDKKIHTTVLASGHEDSDYSTFLPVIETSKVKDANHFPPNYPEPKNDSVSSNIDEFPNDSISSASFLSVPQSTPPYLVSQPTPLNKFLAGAENVDIPHSLRPVPRREHSSQFQVSEKRTLVRLPSFDDVHTSEREELFIKKLEQCNIIFDFNDPSSDLASKEIKREALLQMIDYVSENRGISSASLFPYVVNTFSLNVFRPISPALNDYSSDMFALDDEPFLEPAWPHLEEVYLLFIKFLESPDFRASKAKSLVDRRFFNRLLALFDTEDPRERELLKTTLHRIYGKFLNLRSYIRKSMNNVFLQFIYEREKFHGIAELLEILGSIINGFAVPLKEEHKIFLSKVLIPLHQTKSVFLYHPQLTYCIVQFIDKDPSLTKAVLTGILKYWPRINSFKELLFLNEIEDIFEVLEPSEFVNIMSPLFQQLARSISSMHFQVAERALCLWSNEYFTSLVSQNVVTLLPIIYPSLYKTANEHWNSTIQAIACNVLQIFVDMDADFFNGLVEDYKQAIIKQEEVMIIRKQQWCQIEALAAENKPTDYLR', 627, 'P78759;', 'KD01025', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'par2', '#Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 2 isoform#PP2A; B subunit; B'' delta 2 isoform', '-', '-', '2542891'),
(1026, 'Q9USQ4', 'NASP-related protein sim3', 'k', 43903, 'Histone H3 and H3-like CENP-A-specific chaperone. Promotes delivery and incorporation of CENP-A in centromeric chromatin; probably by escorting nascent CENP-A to CENP-A chromatin assembly factors. Required for central core silencing and normal chromosome segregation. {ECO:0000269|PubMed:18158900}.', 'MSSDTKTLENSKGNSATDADTKNPSSSDSRAIEQLVTQGNMAYAQKNYEEAVDKYGQALMQSESIHGSESLENRNVLWLYGKSLFQIAIENSQVLGNALGAKESVSQATESFEEPEAIGSFTFSGQKIENKYTVNEENSSIAHPEKESEEKETNEASPASEEDEDDFNVAWEVLDLTRVMQSKAVDAYPDSKDEKIRLADIYDLLGELSLEIENFSQASQDLKTALEWKEKVYNVSNNTLLSEAHYKLALALEFTNPEDPSNKSRACEHVEKAAEILKNVLNERENEVTDKKGKGKQKAEESTLTSDLENLREMLSELEQKTLDLKHGAPSLEEAVMSKMHESSLLSKDSSSLAQAVAEAVKNANDLGGLVKRKRTKQEVTSSSQKEGPKDKKKKD', 396, 'Q9USQ4;', 'KD01026', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'sim3', '#NASP-related protein sim3#CENP-A escort protein sim3#Silencing in the middle of the centromere protein 3', '-', '-', '2540895'),
(1027, 'Q28WQ1', 'Kinesin-like protein unc-104', 'GO:0003777', 189344, 'Required for presynaptic maturation; has a role in axonal transport of dense-core vesicles carrying synaptic vesicle precursors; components required for the morphological transformation of axonal growth cones to mature boutons. {ECO:0000250|UniProtKB:A1ZAJ2}.', 'MSSVKVAVRVRPFNSREIGRESKCIIEMTGATTAITNPKVPPNTSEAVKRFNFDYSYWSHDPRDSDFSTQTMVYKDIGEEMLQHSFDGYNVCIFAYGQTGAGKSYTMMGRQEEQQEGIIPMICQDLFTRIHDTETDELKYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTDYQDIHDLIDEGNKARTVAATNMNETSSRSHAVFTIFFTQRRHDTMTDLTTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVASKKKHNKKADFIPYRDSALTWLLRENLGGNSKTAMIAAISPADINYDETLSTLRYADRAKQIVCKAVVNEDANAKLIRELKEEIQKLRDLLKAEGIEVQEEDELNKSTTGIKSPSKSRNRNGSTTEMAVDQLQASEKLIAELNETWEEKLKRTEEIRLQREAVFAEMGVAVKEDGITVGVFSPKKTPHLVNLNEDPNLSECLLYYIKDGLTRLGTHEANVPQDIQLSGSHILKEHCTFENRNSTVTLLPHKDAIIFVNGRQLVEPEVLKTGSRVILGKNHVFRFTNPEQARELREKITENEAENEVEKADAPQVDWNFAQCELLEKQGIDLKAEMKKRLDNLEEQYKREKMQADQQFEEQRKTYEARIDALQKQVEEQSMTMSMYSSYSPEDFHQEEDVYNNPMYESCWTAREAGLAAWAFRKWRYHQFTSLRDDLWGNAIFLKEANAISVELKKKVQFQFTLLTDTLYSPLPPELASSVAPLQQEDEFGAPPVSKTLVAVEVTDTKNGATHYWSLEKLRQRLELMREMYHNEAEMSPTSPDYNVESLTGGDPFYDRFPWFRMVGRSFIYLSNLLYPVPLVHKVAIVNERGDVRGYLRIAVQPVLDEESIDFNNGVKQSARLVFNEDDAKPKYRALNEKDDVQRYIDNGGHDSKLEELEDVDSGRGIDSNSASDCPENAEEPGEHLQVGKEFTFRVTVLQATGIGAEYADIFCQFNFLHRHEEAFSTEPVKNSASGAPLGFYHVQNITVPVTKSFIEYLKTQPIMFKIFGHYQTHPLHKDAKQDFVSRPPPRRMLPPSIPISQPVRSPKFGPLPCPPSSTVLAKHDVLVWFEICELAPNGEYVPSVVEHSDDLPCRGLFLLHQGIQRRIRITIVHEPTPEVKWKDINELVVGRIRNTPESSDEQDEDACVLSLGLFPGEVLDVPGDDRSFYRFEAAWDSSLHNSALLNRVSQGGETIYITLSAYLELENCARPAIVTKDLSMVIYGRDARTGPRSLKHLFSGQYRNPEANRLSGVYELSLRRASEAGSPGVQRRQRRVLDTSSTYVRGEENLHGWRPRGDSLIFDHQWELEKLTRLEEVGRMRHLLLLRERLGMDTNPNPTTKTEKDVCNLAARAATSPVHMVIPQSPQTPVKDPQQIMPEREYNQREQDLMLKCLKLVQAGRYAKNEANDTQTQSDVSPSDEGCADMTVSCISSNSMEDNKFVIRRRLCSPDRADAPNGWEAPAPATQPALPLRLYVPELEEIRVSPVVARKGLLNVLEHGGSGWKKRWVTVRRPYVFIYRSEKDPVERAVLNLATAQVECSEDQAAMVKIPNTFSVVTKHRGYLLQTLGDKEVHDWLYAINPLLAGQIKSRLARRTLEPASQTASQIQASSAANANSANK', 1671, 'Q28WQ1;', 'KD01027', 'Drosophila pseudoobscura pseudoobscura (Fruit fly)', 'unc-104', '#Kinesin-like protein unc-104', '-', '-', '4805677'),
(1028, 'Q5NVF5', 'Dynein light chain Tctex-type 3', 'GO:0000777===GO:0005868', 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, 'Q5NVF5;', 'KD01028', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'DYNLT3', '#Dynein light chain Tctex-type 3', '-', '-', '100174155'),
(1029, 'Q12188', 'Meiotic recombination protein REC8', 'GO:0000780', 77202, 'Replaces the SCC1 mitosis-specific cohesin to ensure sister chromatid cohesion during meiosis. Is cleaved by ESP1 shortly before the first meiotic division; and dissociates from chromatin; allowing sister chromatids to segregate. Is protected from cleavage by SPO13. {ECO:0000269|PubMed:10412984; ECO:0000269|PubMed:10691741; ECO:0000269|PubMed:11081626; ECO:0000269|PubMed:11163190; ECO:0000269|PubMed:12101124; ECO:0000269|PubMed:12663816; ECO:0000269|PubMed:12665553; ECO:0000269|PubMed:12717442; ECO:0000269|PubMed:15062096; ECO:0000269|PubMed:15120066; ECO:0000269|PubMed:15620644; ECO:0000269|PubMed:15819623; ECO:0000269|PubMed:16027219; ECO:0000269|PubMed:9784122}.', 'MAPLSLNFKDDKKYKGLTTVWLLSALGNSIVKESNNYYSNKSNSTGNISSSTVKKKDIVNISIPKTCDEIQNFENDFSLRYISNLLYGVTICYNKKTEYVLNDLNHLLVQLQKNDVYAFKAKNKSTRINGLNSNNSIIGNKNNNYTWEECVFFDDDPLYDITKVPALEFLNTTLQDNVSFIEEAKSIRRQDYINELSNSNRFELHGDMTNSDAQSNLGSNVRNSFPLDEIPVDVDFNLDLDDIVSHQGTPLGSHSSSQKDGNDFKFNYQGDELVLNFENDNENNSNGGEDTSVENEGPVANLKDYELGLEAQASEEENDLQQKLNTRMQRGHRADVGGQFSKVQFDAKTSYPNEVLKFNHGNYSHLMEKNRIRKLTGQNFLTSNISSLVRSCGEEEFFSTNWLSIFNDFSNIKTSEWDLYPQGFSSVERGRKRAHSLVSTQSSSSTRSHEYGRKSFRNNKNDNYSSDMENDNLLLNLEQINEDLEDGHYIEENSQGNILDFNLNLPPSSFGRSHTRNSTRSSGFNEDIVGALRRRVGPSEQNFAEEDDSSNSCFSDGSQQNLQQDKTNFQDVILDYQTKKFYDYIKERSIVVGRTTRSNPPFKRKMLLVDIIPSRMGEAQTGANFDDVERGVSRQIAASAFLSLLNLATKGMVKLNEYPVADAVTKDLKLRREDEIIVYA', 680, 'Q12188; D6W418;', 'KD01029', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'REC8', '#Meiotic recombination protein REC8#Cohesin REC8#Sporulation protein 69', '-', '-', '856115'),
(1030, 'Q02733', 'Increased recombination centers protein 15', 'GO:0051315', 54156, '', 'MGGEDEILSTMEDFAAVYDVLVIGCGPGGFTAAMQASQAGLLTACVDQRASLGGAYLVDGAVPSKTLLYESYLYRLLQQQELIEQRGTRLFPAKFDMQAAQSALKHNIEELGNVYKRELSKNNVTVYKGTAAFKDPHHVEIAQRGMKPFIVEAKYIVVATGSAVIQCPGVAIDNDKIISSDKALSLDYIPSRFTIMGGGTIGLEIACIFNNLGSRVTIVESQSEICQNMDNELASATKTLLQCQGIAFLLDTRVQLAEADAAGQLNITLLNKVSKKTYVHHCDVLMVSIGRRPLLKGLDISSIGLDERDFVENVDVQTQSLLKYPHIKPIGDVTLGPMLALKAEEQAIRAIQSIGCTGSDGTSNCGFPPNVLYCQPQIGWVGYTEEGLAKARIPYQKGRVLFSQNVRYNTLLPREENTTVSPFIKVLIDSRDMKILGVHMINDDANELLSQASMAVSLGLTAHDVCKVPFPHPSLSESFKQAVQLAMANGTSPGVHVRE', 499, 'Q02733; D6W3Z5;', 'KD01030', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'IRC15', '#Increased recombination centers protein 15', '-', '-', '856090');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1031, 'P30153', 'Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform', 'k;s', 65309, 'The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregation and for centromeric localization of SGOL1 in mitosis. {ECO:0000269|PubMed:16580887}.', 'MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA', 589, 'P30153; Q13773; Q6ICQ3; Q96DH3;', 'KD01031', 'Homo sapiens (Human)', 'PPP2R1A', '#Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform#Medium tumor antigen-associated 61 kDa protein#PP2A subunit A isoform PR65-alpha#PP2A subunit A isoform R1-alpha', '-', 'ENSG00000105568', '-'),
(1032, 'P38432', 'Coilin', 'k', 62608, 'Component of nuclear coiled bodies; also known as Cajal bodies or CBs; which are involved in the modification and assembly of nucleoplasmic snRNPs. {ECO:0000269|PubMed:7679389}.', 'MAASETVRLRLQFDYPPPATPHCTAFWLLVDLNRCRVVTDLISLIRQRFGFSSGAFLGLYLEGGLLPPAESARLVRDNDCLRVKLEERGVAENSVVISNGDINLSLRKAKKRAFQLEEGEETEPDCKYSKKHWKSRENNNNNEKVLDLEPKAVTDQTVSKKNKRKNKATCGTVGDDNEEAKRKSPKKKEKCEYKKKAKNPKSPKVQAVKDWANQRCSSPKGSARNSLVKAKRKGSVSVCSKESPSSSSESESCDESISDGPSKVTLEARNSSEKLPTELSKEEPSTKNTTADKLAIKLGFSLTPSKGKTSGTTSSSSDSSAESDDQCLMSSSTPECAAGFLKTVGLFAGRGRPGPGLSSQTAGAAGWRRSGSNGGGQAPGASPSVSLPASLGRGWGREENLFSWKGAKGRGMRGRGRGRGHPVSCVVNRSTDNQRQQQLNDVVKNSSTIIQNPVETPKKDYSLLPLLAAAPQVGEKIAFKLLELTSSYSPDVSDYKEGRILSHNPETQQVDIEILSSLPALREPGKFDLVYHNENGAEVVEYAVTQESKITVFWKELIDPRLIIESPSNTSSTEPA', 576, 'P38432; B2R931;', 'KD01032', 'Homo sapiens (Human)', 'COIL', '#Coilin#p80-coilin', '-', 'ENSG00000235115', '-'),
(1033, 'P23880', 'Serine/threonine-protein phosphatase PP1-2', 'k', 36829, 'Essential role in cell cycle control. PP1 is perhaps required for exit from mitosis.', 'MDYDIDAIIEKLVKARNGKPSKQVQLSDAEIRYLCTTSRSIFLSQPMLLELEAPLKICGDIHGQYSDLLRLFEYGGYPPDANYLFLGDYVDRGKQSLEVICLLFAYKIKYPENFFLLRGNHEFASINRIYGFYDECKRRYSIKLWKTFTDCFNCMPVAAVIDEKIFCMHGGLSPDLNSLDQIQRIIRPTDIPDTGLLCDLVWSDPEKDLTGWGENDRGVSYTFGADVVSRFLQKHDLDLICRAHQVVEDGYEFFGKRQLVTIFSAPNYCGEFDNVGAMMSVNEDLLCSFQILKPAEKRQRVSQSSIKESKSATNSLKKSKNN', 322, 'P23880;', 'KD01033', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'sds21', '#Serine/threonine-protein phosphatase PP1-2#3.1.3.16#Suppressor protein SDS21', '-', '-', '2539179'),
(1034, 'Q02732', 'Central kinetochore subunit CTF19', 'GO:0000778===GO:0008608===GO:0000817===k', 42782, '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.', 'MDFTSDTTNSHDTSNSHLSLEDAVGTHHAGEADVNIDGDEKQQLSLLDDDQVRALKLQEEKDALLTRRNTLLQEIQTYQNILMKENNSKTKNGDILQNDITQDFLNLISISSSNPNSAISDRKRVERINGLTNLQKELVTKYDTLPLLNMNLRLSYLRDHTYPHLQVSVQSRDRVHNDGIEVLVVNYKFCRNTMNPFEIQFKMFYKFEDSTLLKWEILRISTNVRLKAKQLLATRNFQKCLLSLYEFDKIKSKKTGIFQNLINLLKRKTRCYLMNNSDSLIVERVIREGRLTTIKLQINFIITMPGERGKPRNCFLPMSKISIALWKGGERFNQIDLDEICYGLIKEYGVKTGLKEICNVCLFPDMYAR', 369, 'Q02732; D6W3Z4;', 'KD01034', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CTF19', '#Central kinetochore subunit CTF19#Chromosome transmission fidelity protein 19#Minichromosome maintenance protein 18', '-', '-', '856089'),
(1035, 'Q9USQ1', 'Chromosome transmission fidelity protein 18', 'GO:0051455', 108651, 'Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Replication factor C (RFC) complex has an essential but redundant activity in sister chromatid cohesion establishment. Acts as a PCNA loader; loading PCNA onto primed templates. An RFC-like complex (ctf18- RFC) is formed where ctf18 replaces rfc1 in the RFC complex along with the association of dcc1 and ctf8. This complex is required for efficient establishment of chromosome cohesion during S-phase. {ECO:0000269|PubMed:15226378; ECO:0000269|PubMed:16040599}.', 'MDSIPNEDDLEKLLVAEQNVPYGKNYESFEDEENYLLELRNANALENLEHRSIPNDLFHSSQPVGSPTRNGDDIPSTLDLYSSDNAAIDTDISEDETINQRHAPQTDYRYPNTSANPKMGLEESMDIDMPSIDLDISNAAAFPRDSNLLFRNYNSHTKTSEKGSPVNFEKENQDSNVLFSTGRTSVLHIDAEQSQTNNTVTPLKDDALSLFSFENDVNGAVNDNSLDQKLSASKNSQRVSLPFFSKIELDEGSSFSGPKISARTSSGKIIYFPKKKNRHSDGLLLQPKRLADEISQVNEIGKDFNQDLLNSVRIWSENFLIVSKEKSVALKTEKLDSLQITNCTTKPQSQKLWVDTYRPQLFRDLLGDERVHRAAMHWIKAWDPCVFGKSRLQPSKSMRFNPRFTNITSDSDRPDKRIMMLTGLAGAGKTTLAHVIAHQAGYKVLEINASDDRTAHTVHEKVSSAISNHSALSSQPTCVIVDEIDGGDPAFVRALLSLLESDEKATEYSQAGNSKKKKKFKKLCRPIICICNDLYTPALRPLRPYAQIIYFRPPPQASLVGRLRTICRNENIAVDSRSLTLLTDIYNSDIRSCINSLQLLSLNNKRIDSETIKLLQPKSNSFSTSSLIQSLFLQLDNKQIRAIEASQPTYSHLDALLARIDGANDSESVLMNCFHTYLDLPFTDSLLSKPALTSEWLYFFDQLHSQCYKGNYELWRYIPYSIIHFHYLYATPEKCRLPHPPRSDLEALKLYRTRKEILDSFISTLNAYENQMHGERSILLELIRTILITINPTLKQKEDSMPRSALPSKIEHAINILNHYNLRFQQLPVGDGNYVYRLEPPLDELVWDAPTSSYSVRQMLSQELLKKRLADIKKQTLTDNPTSSNSSRKRKDFNSGKAIKRDFFGRIISEPKSEAVTSNNAALNTGDHPVSIKHAINIKFHDGFSNAVRKPISLNEILNF', 960, 'Q9USQ1; Q9UTY7;', 'KD01035', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ctf18', '#Chromosome transmission fidelity protein 18', '-', '-', '2541270'),
(1036, 'Q90ZS5', 'Spindle checkpoint protein Bub1', 'k', 127275, '', 'MDLQSQAQMFEAHIQGYKGDDPLDLWDRYVLWAEEALPPQEKQNIFCLLERLVRNFIGDKRYCNDERYLKYCIRFADTINEPGQYFEYLYNQGIGHQSAALHVTWAQLLETQGDLQSASALYQKAIHSNAKPMEILDQHYRTFQIRNSQANIANRGAPVEPLGNSQILNQMNPTSASSNVDQLSVAKCESSTPSENHPSQESACNVDRSGNKWVTISKSAVVPQPVKCVGVEVKQVPMYCKDKLVCADSELSFEEFRASIYRKKYEQRRKMQQWEEEERKYKKFKEEAALQEQLLKQKMEQLSSLLHVQGRQEVLPQNTARQMPEVPQTTNSHFSISSGPITQNLPESETQASLVTDEPISVPTSLSAPAMPQMASSSMSSFGRKGCSPAAAEEWMPAPVDQSSVLSVAAPHVPRARVSEQSILNKSQSNLDRSTATVLEMSKQVCQDTSSIVQGLRVQPGKKEVSAVGNSSGYLANTSHVTPNTSLGLVQATPSKVLPSPTVNTKEALGFIMDIFQTSTLPDNVEEEEEETQDEIDQEFEAFCRNDNKTGPNTVGFPVLPNVAPALPSDFCIFEDNVGKVNDLQSKPVEVKSLRERPALRPPLKSNEEVKAAESLVDDSTVWAVRCNKTLASSPNSTGDFALAARLASTPANKQTQPTWQTLEDKENAVADSVVHTVFDFAEDKVIQVSKSRKLSPIQEQSPEHSKISGAVQSPSCTVIPAESPAAELISDYVEQTGQKLAACKLSDTLYQPALGSLEDPWGVTTQTLDPYEEEKTETIVNAPPELVIIENAWDEKLIDRLLSELPKSLGSHENYYPCHTMVPVLKPKMEVKLGSNSFYIDNLLGEGAFAHVYQASLLDTNIQSNQKFILKVQKPAKPWEFYIGTQIRERINPELRHLFIGFHAAHLFDNGSVLVGDLYNYGSLLNAINLYKKLSEKVMPAPLVMYFAINILYMVEQLHNIGIIHGDVKPDNFAIGERFLENESCSLDFVSHGLALIDLGQSIDMTLFPKGTAFMGKCDTSCFQCTEMLTKKPWNYQTDYFGVAGTVYCMMFGNYMKVKNEQGVWKPDGSFKRYQHGELWTEFFHTLLNVPDCHSPSPLRALREKLMSTFMLYTNKIKSFRNRLVILLLENKPSRK', 1137, 'Q90ZS5;', 'KD01036', 'Xenopus laevis (African clawed frog)', '', '#Spindle checkpoint protein Bub1 {ECO:0000313|EMBL:AAK52898.1}', '-', '-', '-'),
(1037, 'O00444', 'Serine/threonine-protein kinase PLK4', 'k;m', 108972, 'Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder; leading to the recruitment of centriole biogenesis proteins such as SASS6; CENPJ/CPAP; CCP110; CEP135 and gamma-tubulin. When overexpressed; it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates ''Ser-151'' of FBXW5 during the G1/S transition; leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis; centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1; leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. {ECO:0000269|PubMed:16244668; ECO:0000269|PubMed:16326102; ECO:0000269|PubMed:17681131; ECO:0000269|PubMed:18239451; ECO:0000269|PubMed:19164942; ECO:0000269|PubMed:21725316}.', 'MATCIGEKIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMNRYLKNRVKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPSFLSIEAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSTKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDKRRLLIGQPLPNKMTVFPKNKSSTDFSSSGDGNSFYTQWGNQETSNSGRGRVIQDAEERPHSRYLRRAYSSDRSGTSNSQSQAKTYTMERCHSAEMLSVSKRSGGGENEERYSPTDNNANIFNFFKEKTSSSSGSFERPDNNQALSNHLCPGKTPFPFADPTPQTETVQQWFGNLQINAHLRKTTEYDSISPNRDFQGHPDLQKDTSKNAWTDTKVKKNSDASDNAHSVKQQNTMKYMTALHSKPEIIQQECVFGSDPLSEQSKTRGMEPPWGYQNRTLRSITSPLVAHRLKPIRQKTKKAVVSILDSEEVCVELVKEYASQEYVKEVLQISSDGNTITIYYPNGGRGFPLADRPPSPTDNISRYSFDNLPEKYWRKYQYASRFVQLVRSKSPKITYFTRYAKCILMENSPGADFEVWFYDGVKIHKTEDFIQVIEKTGKSYTLKSESEVNSLKEEIKMYMDHANEGHRICLALESIISEEERKTRSAPFFPIIIGRKPGSTSSPKALSPPPSVDSNYPTRERASFNRMVMHSAASPTQAPILNPSMVTNEGLGLTTTASGTDISSNSLKDCLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPNGQTTRYGENEKLPDYIKQKLQCLSSILLMFSNPTPNFH', 970, 'O00444; B2RAL0; B7Z837; B7Z8G7; Q8IYF0; Q96Q95; Q9UD84; Q9UDE2;', 'KD01037', 'Homo sapiens (Human)', 'PLK4', '#Serine/threonine-protein kinase PLK4#2.7.11.21#Polo-like kinase 4#PLK-4#Serine/threonine-protein kinase 18#Serine/threonine-protein kinase Sak', '-', 'ENSG00000142731', '-'),
(1038, 'Q6P5F9', 'Exportin-1', 'GO:0000776', 123093, 'Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus; in association with RANBP3; binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm; disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1; respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap (By similarity). {ECO:0000250}.', 'MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFETLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLLEKRLNLREALMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDIPPRRQLYLTVLSKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTEIIMTKKLQNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTPLNPGNPVNNQMFIQDYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEERETALRQAQEEKHKLQMSVPGILNPHEIPEEMCD', 1071, 'Q6P5F9;', 'KD01038', 'Mus musculus (Mouse)', 'Xpo1', '#Exportin-1#Exp1#Chromosome region maintenance 1 protein homolog', '-', '-', '103573'),
(1039, 'P56387', 'Dynein light chain Tctex-type 3', 'GO:0000777===GO:0005868', 12958, '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.', 'MEGYQRPCDEVGFNADEAHNIVKECVDGVLGGNDYNENNINQWTASIVEQSITHLVKLGKAYKYIVTCAVVQRSPYGFHTASSCFWDTTSDGTCTIRWENRTMNCIVNVFAVAIVL', 116, 'P56387;', 'KD01039', 'Mus musculus (Mouse)', 'Dynlt3', '#Dynein light chain Tctex-type 3#Protein 91/23#T-complex-associated testis-expressed 1-like', '-', '-', '67117'),
(1040, 'Q9C701', 'Mitotic checkpoint protein BUB3.2', 'GO:0000777', 37670, 'Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20 (By similarity). {ECO:0000250}.', 'MTLVPAIGRELSNPPSDGISNLRFSNNSDHLLVSSWDKSVRLYDANGDLMRGEFKHGGAVLDCCFHDDSSGFSVCADTKVRRIDFNAGKEDVLGTHEKPVRCVEYSYAAGQVITGSWDKTIKCWDPRGASGTERTQIGTYMQPERVNSLSLVGNRLVVATAGRHVNIYDLRNMSQPEQRRESSLKYQTRCVRCYPNGTGYALSSVEGRVSMEFFDLSEAAQAKKYAFKCHRKSEDGRDIVYPVNAIAFHPIYGTFASGGCDGFVNIWDGNNKKRLYQYSKYPTSIAALSFSRDGGLLAVASSYTFEEGDKPHEPDAIFVRSVNEIEVKPKPKVYPNPPV', 339, 'Q9C701; Q9C6C4;', 'KD01040', 'Arabidopsis thaliana (Mouse-ear cress)', 'BUB3.2', '#Mitotic checkpoint protein BUB3.2#Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 3.2', '-', '-', '841414'),
(1041, 'Q60443', 'Kinesin-like protein KIFC1', 'GO:0003777', 68821, 'Minus end-directed microtubule-dependent motor required for bipolar spindle formation. May contribute to movement of early endocytic vesicles. {ECO:0000250|UniProtKB:Q9QWT9; ECO:0000269|PubMed:7744954}.', 'MKEALEPAKKRTRGLGAVTKIDTSRSKGPLLSSLSQPQGPTAAQKGPKKTGPRGCTAVGSVLKNQKLAPTAPAQKPVRKRPGKRPDWDLKGQLCDLTEELKCYREKTQKLDQENQGLQEQLKEAQEQAAALGTERNTLEGELASVRTQAEQCQQKLEALCARVLELEEWLGTKENLIQELQKEQLELQEERKALATRLEEQERRLQASEAALLSNESEVVCLRQKTAAQVTLLAEQGDRLHGLEMERRRLHNQLQELKGNIRVFCRVRPVLAGEPTPSPGFLLFPHGPAGPSDPPTRLSLSRSDDRRSTLTRAPAPTTRHDFSFDRVFPPGSKQEEVFEEISMLVQSALDGYPVCIFAYGQTGSGKTFTMEGRPGGDPQLEGLIPRRMRHLFSVAQEMSGQGWTYSFVASYVEIYNETVRDLLATGTRKGQGECEIRRARPGSEELTVTNARYVPVSCEREVEALLHLAHQNRAVARTAQNERSSRSHSVFQLQISGEHAARGLQCVAPLNLVDLAGSERLDPGLTLGPGERDRLRETQSINSSLSTLGLVIMALSNKESHVPYRNSKLTYLLQNSLGGSAKMLMFVNISPLEENVSESLNSLRFASKVNQCVIGTAQANKK', 622, 'Q60443;', 'KD01041', 'Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)', '', '#Kinesin-like protein KIFC1#CHO2 antigen', '-', '-', '-'),
(1042, 'O94235', 'Serine/threonine-protein kinase mph1', 'GO:0000778===GO:1990299', 75354, 'Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. {ECO:0000269|PubMed:9601094}.', 'MSKRNPPVTNIADLVSDSSLDEDSLSFLEELQDPELYFKNDTFSSKSSHSDGTVTGDTLRRQSSGATALERLVSHPRTKNFDLQGNGGQNSALKEVNTPAYQSMHHFEHLITPLPSTNASHSEVSLSAGVNDLNSNSEHDLLPKSVNKTPGSLSISRRRRIGRIGLGPPKRAEYTLTDPSKTSDTKNSTEADEDIEMKSREVSPASNSVAATTLKPLQLHNTPLQTSQEHPKPSFHPSQFESSFSPRVQFDHDVERRASELHSRPVTVFQEPQRSASQPYESHALSPKVAPLFDNSQATPIPKRQQDVVTVANLQFIKLGVVGKGGSSMVYRIFSPDNSRLYALKEVNFINADQTTIQGYKNEIALLRKLSGNDRIIKLYAAEVNDTLGQLNMVMECGETDLANLLMKNMKKPINLNFIRMYWEQMLEAVQVVHDQNIVHSDLKPANFLLVEGNLKLIDFGIAKAIGNDTTNIHRDSHIGTINYMAPEALTDMNAHTNSGVKLVKLGRPSDVWSLGCILYQMVYGRAPFAHLKMIQAIAAIPNEQYHIHFPEVALPANAVQEKEGSLPGVTVGPDLMDVMKRCLERDQRKRLTIPELLVHPFLNPLPSYLTPLAKKPLPVSGHTNNAHPLRLSTEISASQLSMIIERSVELSKHKRLNKELIDSMAYDCVSNLRKMPE', 678, 'O94235; Q9P7Z5; Q9URW0;', 'KD01042', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mph1', '#Serine/threonine-protein kinase mph1#2.7.12.2', '-', '-', '2540060'),
(1043, 'Q8R565', 'Histone H3-like centromeric protein A', 'GO:0000777', 14839, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro) (By similarity). {ECO:0000250}.', 'MGPRRKPRTPRRRPSSPVPGPSRRSSRPGKRRKFLWLKEIKKLQRSTDLLLRKLPFSRVVREICGKFTRGVDLCWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTIFPKDIQLTRRIRGIEGGLG', 129, 'Q8R565;', 'KD01043', 'Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)', 'CENPA', '#Histone H3-like centromeric protein A#Centromere protein A#CENP-A', '-', '-', '100689459'),
(1044, 'Q6CGV4', 'Probable kinetochore protein SPC25', 'GO:0000778===GO:0051455===GO:0031617', 27063, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MTTLPTLPPLPEDIVTGMEELKIVMSAALERQRSQLVQSRQDVNRVLKELEEESKGVSLEIESHMARQHDLRLQISELDKQIEDSKGTIVEYSRRRSELESKVEAAQRACDEGRQRLEEQQSLRRRQVQHVMEQSVRNVPELMYMEDLLGMKIEAVQDDQLRFVFVKLDPNDYAREFAFVLDMADVNYRVEQLEPTLDLSVVDRVVGKLNSSRNFPQFLKEIRQAFKDAIME', 232, 'Q6CGV4;', 'KD01044', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '2906159'),
(1045, 'Q9P6S5', 'DASH complex subunit ask1', 'GO:0000778===GO:0042729===GO:0031134===GO:0000779', 34593, '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. Plays a role in meiosis. {ECO:0000269|PubMed:16079914; ECO:0000269|PubMed:16303567}.', 'MNNLEQLERLEQSITLALYEIDANFSKCHRTVTTKILPIVEKYAKNCNTIWDSSKFWKQFFEASANVSLSGVEEPVPVESNPSDQDVMSNSTEADLQLHTKNEHLEKRHSFVGKSDFPDAAVQGDNTKNEDFVQSTPKKMDVSLEDISLDDAALTPIPARMQTPLRKPENNPHTGRSALLHRVLDTNWQVQVTPREPKNLQSQEVMDIDSSPFVSPSPISMKMDMPSLNDRNSSHALSLFAEFEHESYDSINPSGMSPPKTIQFSPHTMGVGSSQQANERSLSLQRKLETLNDSNDSFVKEEDSWEL', 307, 'Q9P6S5; P78949;', 'KD01045', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ask1', '#DASH complex subunit ask1#Associated with spindles and kinetochores protein 1#Meiotically up-regulated gene 181 protein#Outer kinetochore protein ask1', '-', '-', '2540498'),
(1046, 'P63087', 'Serine/threonine-protein phosphatase PP1-gamma catalytic subunit', 'GO:0000777', 36984, '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. In balance with CSNK1D and CSNK1E; determines the circadian period length; through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. {ECO:0000269|PubMed:21712997; ECO:0000269|PubMed:21930935}.', 'MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK', 323, 'P63087; O09186; O09189; P37139; Q64679;', 'KD01046', 'Mus musculus (Mouse)', 'Ppp1cc', '#Serine/threonine-protein phosphatase PP1-gamma catalytic subunit#PP-1G#3.1.3.16#Protein phosphatase 1C catalytic subunit', '-', '-', '19047'),
(1047, 'P63088', 'Serine/threonine-protein phosphatase PP1-gamma catalytic subunit', 'GO:0000777', 36984, '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. In balance with CSNK1D and CSNK1E; determines the circadian period length; through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. {ECO:0000250|UniProtKB:P36873}.', 'MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK', 323, 'P63088; O09186; O09189; P37139; Q64679;', 'KD01047', 'Rattus norvegicus (Rat)', 'Ppp1cc', '#Serine/threonine-protein phosphatase PP1-gamma catalytic subunit#PP-1G#3.1.3.16#Protein phosphatase 1C catalytic subunit', '-', '-', '24669'),
(1048, 'Q8NEJ9', 'Neuroguidin', 'k', 35894, 'Involved in the translational repression of cytoplasmic polyadenylation element (CPE)-containing mRNAs. {ECO:0000250}.', 'MAALGVLESDLPSAVTLLKNLQEQVMAVTAQVKSLTQKVQAGAYPTEKGLSFLEVKDQLLLMYLMDLTHLILDKASGGSLQGHDAVLRLVEIRTVLEKLRPLDQKLKYQIDKLIKTAVTGSLSENDPLRFKPHPSNMMSKLSSEDEEEDEAEDDQSEASGKKSVKGVSKKYVPPRLVPVHYDETEAEREKKRLERAKRRALSSSVIRELKEQYSDAPEEIRDARHPHVTRQSQEDQHRINYEESMMVRLSVSKREKGRRKRANVMSSQLHSLTHFSDISALTGGTVHLDEDQNPIKKRKKIPQKGRKKKGFRRRR', 315, 'Q8NEJ9; A8K760; Q9Y400;', 'KD01048', 'Homo sapiens (Human)', 'NGDN', '#Neuroguidin#Centromere accumulated nuclear protein 1#CANu1#EIF4E-binding protein', '-', 'ENSG00000129460', '-'),
(1049, 'Q09884', 'Protein Dicer', 'k', 158040, 'Required for G1 arrest and mating in response to nitrogen starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints occurs downstream of dcr1. Required; indirectly; for regulated hyperphosphorylation of cdc2.', 'MDISSFLLPQLLRKYQQDVYNIASKQNTLLVMRTGAGKTLLAVKLIKQKLEEQILIQESNLEHKKISVFLVNKVPLVFQQAEYIRSQLPAKVGMFYGELSIEMSEQLLTNIILKYNVIVITADLFYLFLARGFLSINDLNLIIFDECHHAIGNDAYARIMNDFYHRAKAVLSKKHFTLPRIFGMTASPFTGKKGNLYHRLYQWEQLFDSKAHVVSENELADYFCLPEESYVMYSNKLVVPPSDSIIKKCEETLQGCKLISRAVKTALAETIDMGLWFGEQVWLYLVDFVETKRLKKKALGKQLSDDEELAIDRLKIFVEDWKNNKYSDNGPRIPVFDSTDVTDKVFKLLELLKATYRKSDSVRTVIFVERKATAFTLSLFMKTLNLPNIRAHSFIGHGPSDQGEFSMTFRRQKDTLHKFKTGKYNVLIATAVAEEGIDVPSCNLVIRFNICRTVTQYVQSRGRARAMASKFLIFLNTEELLIHERILHEEKNLKFALSELSNSNIFDSLVCEERERVTDDIVYEVGETGALLTGLYAVSLLYNFCNTLSRDVYTRYYPTFTAQPCLSGWYCFEVELPKACKVPAAQGSPAKSIRKAKQNAAFIMCLDLIRMGLIDKHLKPLDFRRKIADLETLEEDELKDEGYIETYERYVPKSWMKVPEDITRCFVSLLYTDANEGDNHIFHPLVFVQAHSFPKIDSFILNSTVGPRVKIVLETIEDSFKIDSHLLELLKKSTRYLLQFGLSTSLEQQIPTPYWLAPLNLSCTDYRFLENLIDVDTIQNFFKLPEPVQNVTDLQSDTVLLVNPQSIYEQYAFEGFVNSEFMIPAKKKDKAPSALCKKLPLRLNYSLWGNRAKSIPKSQQVRSFYINDLYILPVSRHLKNSALLIPSILYHIENLLVASSFIEHFRLDCKIDTACQALTSAESQLNFDYDRLEFYGDCFLKLGASITVFLKFPDTQEYQLHFNRKKIISNCNLYKVAIDCELPKYALSTPLEIRHWCPYGFQKSTSDKCRYAVLQKLSVKRIADMVEASIGACLLDSGLDSALKICKSLSVGLLDISNWDEWNNYFDLNTYADSLRNVQFPYSSYIEETIGYSFKNKKLLHLAFIHPSMMSQQGIYENYQQLEFLGDAVLDYIIVQYLYKKYPNATSGELTDYKSFYVCNKSLSYIGFVLNLHKYIQHESAAMCDAIFEYQELIEAFRETASENPWFWFEIDSPKFISDTLEAMICAIFLDSGFSLQSLQFVLPLFLNSLGDATHTKAKGDIEHKVYQLLKDQGCEDFGTKCVIEEVKSSHKTLLNTELHLTKYYGFSFFRHGNIVAYGKSRKVANAKYIMKQRLLKLLEDKSNLLLYSCNCKFSKKKPSDEQIKGDGKVKSLT', 1374, 'Q09884; Q9UUN1;', 'KD01049', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dcr1', '#Protein Dicer#Cell cycle control protein dcr1#RNA interference pathway protein dcr1#Endoribonuclease dcr1#3.1.26.-#ATP-dependent helicase dcr1#3.6.4.-', '-', '-', '2538930'),
(1050, 'Q6CQ94', 'DASH complex subunit SPC19', 'GO:0008608===GO:0042729', 17772, '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}.', 'MEEVLSEGVDALAACVDDMAKCLTVSKVTTDRSTKLAINMLQTKRVFQLVSEYDVQRARLDLMEDIEPLLQKLYSKLEKALTKLERERATLSQTFELNKLRFNNQESNPIIDNVKSDPVVIVSSTHEELERLKDLKNRKEELIQRIQELHEER', 153, 'Q6CQ94;', 'KD01050', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'SPC19', '#DASH complex subunit SPC19#Outer kinetochore protein SPC19', '-', '-', '2893108'),
(1051, 'P52286', 'Suppressor of kinetochore protein 1', 'GO:0000776===GO:0000777===GO:0051382===GO:0031518===SCL===k', 22330, 'Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex; which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding protein complex CBF3; which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII; found in centromeres and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK- like proteins into the kinetochore thus providing cell cycle- regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4 and of ROY1 with YPT52. {ECO:0000269|PubMed:17517885; ECO:0000269|PubMed:21389113; ECO:0000269|PubMed:8706131; ECO:0000269|PubMed:8706132; ECO:0000269|PubMed:9346238; ECO:0000269|PubMed:9346239; ECO:0000269|PubMed:9499404}.', 'MVTSNVVLVSGEGERFTVDKKIAERSLLLKNYLNDMHDSNLQNNSDSESDSDSETNHKSKDNNNGDDDDEDDDEIVMPVPNVRSSVLQKVIEWAEHHRDSNFPDEDDDDSRKSAPVDSWDREFLKVDQEMLYEIILAANYLNIKPLLDAGCKVVAEMIRGRSPEEIRRTFNIVNDFTPEEEAAIRRENEWAEDR', 194, 'P52286; D6VSW0; Q07186;', 'KD01051', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SKP1', '#Suppressor of kinetochore protein 1#Centromere DNA-binding protein complex CBF3 subunit D#E3 ubiquitin ligase complex SCF subunit SKP1', '-', '-', '851928'),
(1052, 'P36873', 'Serine/threonine-protein phosphatase PP1-gamma catalytic subunit', 'GO:0000777===c;k;m;s', 36984, '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. In balance with CSNK1D and CSNK1E; determines the circadian period length; through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the ''Ser-418'' residue of FOXP3 in regulatory T- cells (Treg) from patients with rheumatoid arthritis; thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). {ECO:0000269|PubMed:17936702; ECO:0000269|PubMed:20516061; ECO:0000269|PubMed:21712997; ECO:0000269|PubMed:23396208}.', 'MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK', 323, 'P36873;', 'KD01052', 'Homo sapiens (Human)', 'PPP1CC', '#Serine/threonine-protein phosphatase PP1-gamma catalytic subunit#PP-1G#3.1.3.16#Protein phosphatase 1C catalytic subunit', '-', 'ENSG00000186298', '-'),
(1053, 'Q4V8G7', 'Centromere protein U', 'GO:0000777', 46801, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression (By similarity). {ECO:0000250}.', 'MAARRSLRYSGDPGAKRSRNTLGSTNSRKQKAGQKPKRKDVFDFPNTSDVSSMLRELEEEEPYETFDPPLHSTAIYTDDELYKHCVSSTSPATHRGKESRNLNPSENEASGNDSIKLSAKKPRRKLEPISDESDSSEDNVRRSVSIERPRARKPPAAPAAASSSSSPSERPAEQVTPRKTSFPQPSAVEETPAAQSQLKTQKKVRPSPGRRKRPRRGSTHSDASESMHILCLEGKRQSDVMELDVVLSAFERTFLDYKQRVESESCNQAISKFYFKIKGELIRMLKEVQMLKALKRKNTKIISNMEKKRQRLIDVQDELIRLEPQLKQLQTKYDDLKKRKSALKNSKHFLSNLKQLYQDYSNVREEEPKEKEKYDSSSLPALLFKARSILGAEKHLKTINYHLGKLLKQD', 410, 'Q4V8G7;', 'KD01053', 'Rattus norvegicus (Rat)', 'Cenpu', '#Centromere protein U#CENP-U#MLF1-interacting protein', '-', '-', '306464'),
(1054, 'P36874', 'Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A', 'GO:0000777', 36956, 'Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division; and participates in the regulation of glycogen metabolism; muscle contractility and protein synthesis (By similarity). Promotes nuclear envelope reassembly by targeting nuclear membrane vesicles to chromatin at the end of mitosis. Acts by dephosphorylating membrane proteins such as lamin B receptor (lbr) to regulate the binding of membrane proteins to chromatin. {ECO:0000250; ECO:0000269|PubMed:17448463}.', 'MADVDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNASRPVTPPRGMITKQAKK', 323, 'P36874; Q5EAX1;', 'KD01054', 'Xenopus laevis (African clawed frog)', 'ppp1cc-a', '#Serine/threonine-protein phosphatase PP1-gamma catalytic subunit A#PP-1G-A#xPP1-gamma1#3.1.3.16', '-', '-', '397767'),
(1055, 'P39951', 'Cyclin-dependent kinase 1', 'GO:0034501', 34135, 'Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition; and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin; APC; AMPH; APC; BARD1; Bcl- xL/BCL2L1; BRCA2; CALD1; CASP8; CDC7; CDC20; CDC25A; CDC25C; CC2D1A; CSNK2 proteins/CKII; FZR1/CDH1; CDK7; CEBPB; CHAMP1; DMD/dystrophin; EEF1 proteins/EF-1; EZH2; KIF11/EG5; EGFR; FANCG; FOS; GFAP; GOLGA2/GM130; GRASP1; UBE2A/hHR6A; HIST1H1 proteins/histone H1; HMGA1; HIVEP3/KRC; LMNA; LMNB; LMNC; LBR; LATS1; MAP1B; MAP4; MARCKS; MCM2; MCM4; MKLP1; MYB; NEFH; NFIC; NPC/nuclear pore complex; PITPNM1/NIR2; NPM1; NCL; NUCKS1; NPM1/numatrin; ORC1; PRKAR2A; EEF1E1/p18; EIF3F/p47; p53/TP53; NONO/p54NRB; PAPOLA; PLEC/plectin; RB1; UL40/R2; RAB4A; RAP1GAP; RCC1; RPS6KB1/S6K1; KHDRBS1/SAM68; ESPL1; SKI; BIRC5/survivin; STIP1; TEX14; beta-tubulins; MAPT/TAU; NEDD1; VIM/vimentin; TK1; FOXO1; RUNX1/AML1; SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis; CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation; Golgi dynamics; nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate; CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation; chromosome decondensation; reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C- mediated dephosphorylation and restoring cell cycle progression. In proliferating cells; CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity; leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome; an important step for spindle formation. In addition; CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl- xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast; CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines; as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing (By similarity). CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. {ECO:0000250; ECO:0000269|PubMed:10542199; ECO:0000269|PubMed:17200138; ECO:0000269|PubMed:19821535}.', 'MEDYIKIEKIGEGTYGVVYKGRHRTTGQIVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQFMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLVYDPAKRISGKMALKHPYFDDLDNQIKKM', 297, 'P39951; Q5BJB4;', 'KD01055', 'Rattus norvegicus (Rat)', 'Cdk1', '#Cyclin-dependent kinase 1#CDK1#2.7.11.22#2.7.11.23#Cell division control protein 2 homolog#Cell division protein kinase 1#p34 protein kinase', '-', '-', '54237'),
(1056, 'O60566', 'Mitotic checkpoint serine/threonine-protein kinase BUB1 beta', 'GO:0000776===GO:0000777===GO:0034501===GO:0000940===GO:0000778===k;t', 119545, '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 is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C; independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. May play a role for tumor suppression. {ECO:0000269|PubMed:10477750; ECO:0000269|PubMed:11702782; ECO:0000269|PubMed:14706340; ECO:0000269|PubMed:15020684; ECO:0000269|PubMed:19411850; ECO:0000269|PubMed:19503101}.', 'MAAVKKEGGALSEAMSLEGDEWELSKENVQPLRQGRIMSTLQGALAQESACNNTLQQQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPLDMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGIQQKAEPLERLQSQHRQFQARVSRQTLLALEKEEEEEVFESSVPQRSTLAELKSKGKKTARAPIIRVGGALKAPSQNRGLQNPFPQQMQNNSRITVFDENADEASTAELSKPTVQPWIAPPMPRAKENELQAGPWNTGRSLEHRPRGNTASLIAVPAVLPSFTPYVEETARQPVMTPCKIEPSINHILSTRKPGKEEGDPLQRVQSHQQASEEKKEKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKEQREAELLTSAEKRAEMQKQIEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQKIPGMTLSSSVCQVNCCARETSLAENIWQEQPHSKGPSVPFSIFDEFLLSEKKNKSPPADPPRVLAQRRPLAVLKTSESITSNEDVSPDVCDEFTGIEPLSEDAIITGFRNVTICPNPEDTCDFARAARFVSTPFHEIMSLKDLPSDPERLLPEEDLDVKTSEDQQTACGTIYSQTLSIKKLSPIIEDSREATHSSGFSGSSASVASTSSIKCLQIPEKLELTNETSENPTQSPWCSQYRRQLLKSLPELSASAELCIEDRPMPKLEIEKEIELGNEDYCIKREYLICEDYKLFWVAPRNSAELTVIKVSSQPVPWDFYINLKLKERLNEDFDHFCSCYQYQDGCIVWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCNKNNQALKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILANCSSPYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLSQNISELKDGELWNKFFVRILNANDEATVSVLGELAAEMNGVFDTTFQSHLNKALWKVGKLTSPGALLFQ', 1050, 'O60566; B2R6U0; B4DL09; B4DLG3; O60501; O60627; O60758; O75389;Q59HH6; Q8WV50; Q96KM4;', 'KD01056', 'Homo sapiens (Human)', 'BUB1B', '#Mitotic checkpoint serine/threonine-protein kinase BUB1 beta#2.7.11.1#MAD3/BUB1-related protein kinase#hBUBR1#Mitotic checkpoint kinase MAD3L#Protein SSK1', 'BIOMD0000000193,Ibrahim2008_MCC_assembly_model_KDM;', 'ENSG00000156970', '-'),
(1057, 'O94244', 'Histone acetyltransferase type B subunit 2', 'GO:0051382===GO:0000778===GO:0061638===k', 48435, 'Regulatory subunit of the histone acetylase B (HAT-B) complex. The complex acetylates ''Lys-12'' of histone H4 which is required for telomeric silencing (By similarity). Required for correct chromosome segregation where it has a role in the formation and/or maintenance of specialized chromatin at the centromere. Has a role in kinetochore assembly. Maintains the deacetylated state of histones specifically in the central core of the centromeres. {ECO:0000250|UniProtKB:P39984; ECO:0000269|PubMed:15369671}.', 'MSEEVVQDAPLENNELNAEIDLQKTIQEEYKLWKQNVPFLYDLVITHALEWPSLTIQWLPDKKTIPGTDYSIQRLILGTHTSGNDQNYLQIASVQLPNFDEDTTEFTPSTIRRAQATGSYTIEISQKIPHDGDVNRARYMPQKPEIIATMGEGGNAYIFDTTCHDALTTGEALPQAVLKGHTAEGFGLCWNPNLPGNLATGAEDQVICLWDVQTQSFTSSETKVISPIAKYHRHTDIVNDVQFHPQHEALLASVSDDCTLQIHDTRLNPEEEAPKVIQAHSKAINAVAINPFNDYLLATASADKTVALWDLRNPYQRLHTLEGHEDEVYGLEWSPHDEPILASSSTDRRVCIWDLEKIGEEQTPEDAEDGSPELLFMHGGHTNRISEFSWCPNERWVVGSLADDNILQIWSPSRVIWGRDHVQVSPRDLE', 430, 'O94244;', 'KD01057', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis16', '#Histone acetyltransferase type B subunit 2#Kinetochore protein mis16', '-', '-', '2539214'),
(1058, 'Q12158', 'Sister chromatid cohesion protein 1', 'k', 63290, 'Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. 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 ESP1 and dissociates from chromatin; allowing sister chromatids to segregate. {ECO:0000269|PubMed:10403247; ECO:0000269|PubMed:9335333; ECO:0000269|PubMed:9335334; ECO:0000269|PubMed:9491073}.', 'MVTENPQRLTVLRLATNKGPLAQIWLASNMSNIPRGSVIQTHIAESAKEIAKASGCDDESGDNEYITLRTSGELLQGIVRVYSKQATFLLTDIKDTLTKISMLFKTSQKMTSTVNRLNTVTRVHQLMLEDAVTEREVLVTPGLEFLDDTTIPVGLMAQENSMERKVQGAAPWDTSLEVGRRFSPDEDFEHNNLSSMNLDFDIEEGPITSKSWEEGTRQSSRNFDTHENYIQDDDFPLDDAGTIGWDLGITEKNDQNNDDDDNSVEQGRRLGESIMSEEPTDFGFDLDIEKEAPAGNIDTITDAMTESQPKQTGTRRNSKLLNTKSIQIDEETENSESIASSNTYKEERSNNLLTPQPTNFTTKRLWSEITESMSYLPDPILKNFLSYESLKKRKIHNGREGSIEEPELNVSLNLTDDVISNAGTNDNSFNELTDNMSDFVPIDAGLNEAPFPEENIIDAKTRNEQTTIQTEKVRPTPGEVASKAIVQMAKILRKELSEEKEVIFTDVLKSQANTEPENITKREASRGFFDILSLATEGCIGLSQTEAFGNIKIDAKPALFERFINA', 566, 'Q12158; D6VRY5; Q05325;', 'KD01058', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MCD1', '#Sister chromatid cohesion protein 1', '-', '-', '851561'),
(1059, 'A1ZAJ2', 'Kinesin-like protein unc-104', 'GO:0003777', 189345, 'Required for presynaptic maturation; has a role in axonal transport of dense-core vesicles carrying synaptic vesicle precursors; components required for the morphological transformation of axonal growth cones to mature boutons. {ECO:0000269|PubMed:17643120}.', 'MSSVKVAVRVRPFNSREIARESKCIIEMAGATTAITNPKVPPNTSDSVKRFNFDYSYWSHDHHDADFSTQSMVYKDIGEEMLQHSFDGYNVCIFAYGQTGAGKSYTMMGRQEEQQEGIIPMICKDLFTRIQDTETDDLKYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTDYQDIHDLIDEGNKARTVAATNMNETSSRSHAVFTIFFTQRRHDLMTNLTTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVASKKKNTKKADFIPYRDSALTWLLRENLGGNSKTAMIAAISPADINYDETLSTLRYADRAKQIVCKAVVNEDANAKLIRELKEEIQKLRDLLKAEGIEVQEEDELTKSTVIKSPTKSRNRNGSTTEMAVDQLQASEKLIAELNETWEEKLKRTEEIRVQREAVFAEMGVAVKEDGITVGVFSPKKTPHLVNLNEDPNLSECLLYYIKEGLTRLGTHEANVPQDIQLSGSHILKEHCTFENKNSTVTLLPHKDAIIYVNGRKLVEPEVLKTGSRVILGKNHVFRFTNPEQARELRDKIETENEAENEVEKTDTQQVDWNFAQCELLEKQGIDLKAEMKKRLDNLEEQYKREKLQADQQFEEQRKTYEARIDALQKQVEEQSMTMSMYSSYSPEDFHQEEDVYTNPMYESCWTAREAGLAAWAFRKWRYHQFTSLRDDLWGNAIFLKEANAISVELKKKVQFQFTLLTDTLYSPLPPELASTVAPVHQEDEFGAPPVSKTLVAVEVTDTKNGATHHWSLEKLRQRLELMREMYHNEAEMSPTSPDYNVESLTGGDPFYDRFPWFRMVGRSFIYLSNLLYPVPLVHKVAIVNERGDVRGYLRIAVQPVLDEESIDFNNGVKQSARLVFNEDDAKPKYRALNEKDDVQRYIDNGGLDSKLEELEDVDSGRGIDSNSASECHENSEEPGEHLQVGKEFTFRVTVLQATGIGAEYADIFCQFNFLHRHEEAFSTEPVKNSASGAPLGFYHVQNITVPVTKSFIEYLKTQPIMFKIFGHYQTHPLHKDAKQDFVSRPPPRRMLPPSIPISQPVRSPKFGPLPCAPTSTVLAKHDVLVWFEICELAPNGEYVPSVVEHSDDLPCRGLFLLHQGIQRRIRITIVHEPTTEVKWKDINELVVGRIRNTPESSDEQDEDACVLSLGLFPGEALEVPGDDRSFYRFEAAWDSSLHNSALLNRVSQGGETIYITLSAYLELENCARPAIITKDLSMVIYGRDARTGPRSLKHLFSGQYRNPEANRLTGVYELALRRASEAGSPGVQRRQRRVLDTSSTYVRGEENLHGWRPRGDSLIFDHQWELEKLTRLEEVGRMRHLLLLRERLGMDTNPNPTTKTEKDVCNLAARAATSPVHMVIPQSPQTPVKDPQQIIPEREYNQREQDLMLKCLKLVQGRYTKSEANDTQTQSDVSPSDEGCADMTVSCISSNSMENNKFVIRRRLCSPDRADAPNGWEAPAPATQPALPLRLYVPELEEIRVSPVVARKGLLNVLEHGGSGWKKRWVIVRRPYVFIYRSEKDPVERAVLNLATAHVECSEDQAAMVKIPNTFSVVTKHRGYLLQTLGDKEVHDWLYAINPLLAGQIKSRLARRTLEPASQTASQIQATNAANANSASK', 1670, 'A1ZAJ2; A8DX00; A8DYG5; Q9NBL1;', 'KD01059', 'Drosophila melanogaster (Fruit fly)', 'unc-104', '#Kinesin-like protein unc-104#Protein immaculate connections#DUnc104', '-', '-', '36876'),
(1060, 'P33176', 'Kinesin-1 heavy chain', 'GO:0003777', 109685, 'Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. {ECO:0000250}.', 'MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTVDKDITLTNDKPATAIGVIGNFTDAERRKCEEEIAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDALSEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKAKLITDLQDQNQKMMLEQERLRVEHEKLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEIDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPSAIRGGGAFVQNSQPVAVRGGGGKQV', 963, 'P33176; A0AVB2; Q5VZ85;', 'KD01060', 'Homo sapiens (Human)', 'KIF5B', '#Kinesin-1 heavy chain#Conventional kinesin heavy chain#Ubiquitous kinesin heavy chain#UKHC', '-', 'ENSG00000170759', '-'),
(1061, 'Q8S949', 'Kinesin-like protein NACK2', 'GO:0003777', 107229, 'Probable plus end-directed motor protein that may function in the NACK-PQR (NPK1-NQK1/MEK1-NRK1) MAP kinase signaling pathway; which is essential for somatic cell cytokinesis; especially for the cell-plate formation and its expansion. May regulates the activity and the localization of NPK1; probably by association through the non-catalytic region of the kinase. {ECO:0000269|PubMed:11955449}.', 'MVIGTPVTTPLSKIVRTPSRVPGSRRTTPSKIREEKILVTIRVRPLSPKEQAAYDLIAWDFPDEQTIVSKNLNHERHTGPYSFDYVFDPTCSTSKVYEQGARDVALSALNGINATIFAYGQTSSGKTFTMRGITESAVNDIYGRIKLTTERDFVLKFSALEIYNETVVDLLNRESVSLRLLDDPEKGVIVEKQVEEIVKDEEHLKTLIGTVEAHRQVGETALNDKSSRSHQIIRLTIESSIRENSGCVKSFLATLNLVDLAGSERASQTSADGTRLKEGSHINRSLLTVTNVIRKLSCSGGKRSGHIPYRDSKLTRILQASLGGNSRTAIICTLSPALSHLEQSRNTLCFATSAKEVTTTAQVNMVVAEKQLLKHLQKEVSRLEAELRSPDPAASPCLRSLLIEKERKIQKMEEEMNELKRQRDLAQSQLELERRSKKELKGSDHHGPSRQVVKCLSFTPEDEEVSGASLSTNLGRKSLLERQAAIRRSTNSTNPSMLVHEIRKLEMRQRQLGDEANHALQLLHKEFASHRIGSQGATETIAKLFSEIKELQKISCIPEQIEIKDKASLKEEIARLRSQESNIASLEQKLENVQRSIDELVMHLPSCHESADSRTAPSKKKRVLPFNLSNTSNIPNIIRSPCSPMSPSSCNIVEGEIENRAPPECNNVGSAGDSFCSQLSTPVKSKDDNCTPGSRQSNSVNMKKMQTMFKKAAEDNIRSIKAYVTELKERVAKLQYQKQLLVCQVLELEANEAASDEADISDQSPLSWHLVFEDQRQQIIMLWHLCHVSLVHRTQFYMLFKGDPSDQIYLEVELRRLTWLDEHLAGLGNASPALLGDDAAGYVSSSIKALKQEREYLAKRVSSKLNAEEREMLYVKWDIPPDGKQRRRLQLVNKLWSDPLNMQNVRDSAEVVAKLVGFCETGEHVSKEMFQLNFVSPSDKKTWIGWNLISNLLHL', 955, 'Q8S949;', 'KD01061', 'Nicotiana tabacum (Common tobacco)', 'NACK2', '#Kinesin-like protein NACK2#NPK1-activating kinesin 2', '-', '-', '-'),
(1062, 'Q86Y97', 'Histone-lysine N-methyltransferase SUV420H2', 'GO:0000780', 52113, 'Histone methyltransferase that specifically trimethylates ''Lys-20'' of histone H4. H4 ''Lys-20'' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1; RBL1 and RBL2) (By similarity). {ECO:0000250}.', 'MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPPLRRQQHLRSALETFLRQRDLEAAYRALTLGGWTARYFQSRGPRQEAALKTHVYRYLRAFLPESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREADEGLLRAGENDFSIMYSTRKRSAQLWLGPAAFINHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGEGAFRTRPREPALPPRPLDKYQLRETKRRLQQGLDSGSRQGLLGPRACVHPSPLRRDPFCAACQPLRLPACSARPDTSPLWLQWLPQPQPRVRPRKRRRPRPRRAPVLSTHHAARVSLHRWGGCGPHCRLRGEALVALGQPPHARWAPQQDWHWARRYGLPYVVRVDLRRLAPAPPATPAPAGTPGPILIPKQALAFAPFSPPKRLRLVVSHGSIDLDVGGEEL', 462, 'Q86Y97; Q8WZ10; Q9BRZ6;', 'KD01062', 'Homo sapiens (Human)', 'SUV420H2', '#Histone-lysine N-methyltransferase SUV420H2#2.1.1.43#Lysine N-methyltransferase 5C#Suppressor of variegation 4-20 homolog 2#Su(var)4-20 homolog 2#Suv4-20h2', '-', 'ENSG00000133247', '-'),
(1063, 'P33981', 'Dual specificity protein kinase TTK', 'c;k', 97072, 'Phosphorylates proteins on serine; threonine; and tyrosine. Probably associated with cell proliferation. Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere; and for the mitotic checkpoint. {ECO:0000269|PubMed:18243099}.', 'MESEDLSGRELTIDSIMNKVRDIKNKFKNEDLTDELSLNKISADTTDNSGTVNQIMMMANNPEDWLSLLLKLEKNSVPLSDALLNKLIGRYSQAIEALPPDKYGQNESFARIQVRFAELKAIQEPDDARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERGAVPLEMLEIALRNLNLQKKQLLSEEEKKNLSASTVLTAQESFSGSLGHLQNRNNSCDSRGQTTKARFLYGENMPPQDAEIGYRNSLRQTNKTKQSCPFGRVPVNLLNSPDCDVKTDDSVVPCFMKRQTSRSECRDLVVPGSKPSGNDSCELRNLKSVQNSHFKEPLVSDEKSSELIITDSITLKNKTESSLLAKLEETKEYQEPEVPESNQKQWQSKRKSECINQNPAASSNHWQIPELARKVNTEQKHTTFEQPVFSVSKQSPPISTSKWFDPKSICKTPSSNTLDDYMSCFRTPVVKNDFPPACQLSTPYGQPACFQQQQHQILATPLQNLQVLASSSANECISVKGRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMKYVLGQLVGLNSPNSILKAAKTLYEHYSGGESHNSSSSKTFEKKRGKK', 857, 'P33981; A8K8U5; B2RDW2; E1P543; Q15272; Q5TCS0; Q9BW51; Q9NTM0;', 'KD01063', 'Homo sapiens (Human)', 'TTK', '#Dual specificity protein kinase TTK#2.7.12.1#Phosphotyrosine picked threonine-protein kinase#PYT', '-', 'ENSG00000112742', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1064, 'Q9QXL2', 'Kinesin-like protein KIF21A', 'GO:0003777', 186536, 'Microtubule-binding motor protein probably involved in neuronal axonal transport. In vitro; has a plus-end directed motor activity. {ECO:0000269|PubMed:10225949}.', 'MLGAADESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYTQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGFDVNIMEEEQGIISRAVRHLFKSIDEKKTSAIKNGLPPPEFKVNAQFLELYNEEVLDLFDTTRDIDAKNKKSNIRIHEDSTGGIYTVGVTTRTVNTEPEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQTDAENATDNKLISESSPMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDRASQQINALRSEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRARITQLVSEQANQVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARSPYFSASSAFSPTILSSDKETIEIIDLAKKDLEKLKRKEKKKKKRLQKLEESGREERSVAGKDDNADTDQEKKEEKGVSEKENNELDVEENQEVSDHEDEEEEEEDEEEEDDIEGEESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVKCEYEKKLHAMNKELQRLQTAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSESPAPDTGSSAASGEADTSRPGTQQKMRIPVARVQALPTPTTNGTRKKYQRKGFTGRVFTSKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLRQREELTKRREKLSKRREKIVKESGEGDKSVANIIEEMESLTANIDYINDSIADCQANIMQMEEAKEEGETLDVTAVINACTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQDLDGAPPENEEDSSEEDGPLHSPGSEGSTLSSDLMKLCGEVKPKNKARRRTTTQMELLYADSSEVASDTSAGDASLSGPLAPVAEGQEIGMNTETSGTSARDKELLAPSGLPSKIGSISRQSSLSEKKVPEPSPVTRRKAYEKADKPKAKEHKHSDSGASETSLSPPSSPPSRPRNELNVFNRLTVPQGTPSVQQDKSDESDSSLSEVHRGIINPFPACKGVRASPLQCVHIAEGHTKAVLCVDSTDDLLFTGSKDRTCKVWNLVTGQEIMSLGVHPNNVVSVKYCNYTSLVFTVSTSYIKVWDIRESAKCIRTLTSSGQVTLGEACSASTSRTVAIPSGESQINQIALNPTGTFLYAASGNAVRMWDLKRFQSTGKLTGHLGPVMCLTVDQISNGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNFEPPHYDGIEALAIQGDNLFSGSRDNGIKKWDLAQKGLLQQVPNAHKDWVCALGLVPGHPVLLSGCRGGILKLWNVDTFVPVGEMRGHDSPINAICVNSTHVFTAADDRTVRIWKAHNLQDGQLSDTGDLGEDIASN', 1672, 'Q9QXL2; Q6P5H1; Q6ZPJ8; Q8BWZ9; Q8BXF1;', 'KD01064', 'Mus musculus (Mouse)', 'Kif21a', '#Kinesin-like protein KIF21A', '-', '-', '16564'),
(1065, 'Q9QXL1', 'Kinesin-like protein KIF21B', 'GO:0003777', 186180, 'Microtubule-binding motor protein probably involved in neuronal dendritic transport. In vitro; has a plus-end directed motor activity. {ECO:0000269|PubMed:10225949}.', 'MAGQGDCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGFDTVTSEEEQGIIPRAIAHLFRGIDERKRRAQEKGVTGPEFKVSAQFLELYNEEILDLFDSTRDPDARHRRSNIKIHEDANGGIYTTGVTSRLINSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRVCAQPDLVNETVTGLPDGAAPTGTEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDKTSQQISALRAEIARLQMELMEYKAGKRVIGEDGTEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARNPYSLGASPAGPAFGGSPATSMEDASEVIRKAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQAENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEIVLRRKTQEVSALRRLAKPMSERVAGRVGLKPPNMDSGAEVSASTTSSEAESGARSVSSIVRQWNRKIDHFLGDRPTATVNGGRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKREHLQAESPEEEKGLQELAEEIEVLAANIDYINDSITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMTGSSQNHLLLDALREKAEAHPELQALIYNVQHENGYASTDEEVSEFSEGSFSQSFTMKGSTSHDDFKFKGEPKLSAQMKAVSAECLGPPLDSSTKNITKSLASLVEIKEDGVGFSIRDPYYRDKVSRTVSLPTRGSTFPRQSRGATDTSPLTRRKSYDRGQPIRSTDMGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDKSDDSDSSLSEVLRGIITPIGGAKGARTAPLQCISMAEGHTKPILCLDATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSSSYIKVWDIRDSAKCIRTLTSSGQVISGDACIATSTRAITSAQGEHQINQMALSPSGSMLYVASGNAVRIWELNRFQPIGKLTGHIGPVMCLTVTQTSNQHDLVVTGSKDHYVKMFQLGDCVTGTIGPTHNFEPPHYDGIECLAIQGDILFSGSRDNGIKKWDLDQQELIQQIPNAHKDWVCALAFVPGRPMLLSACRAGFIKVWNVDNFTPIGEIKGHDSPINAICTNSKHIFTASSDCRVKLWNYVPGLTPCLPRRVLAIKGRAPPCPDLPPPPLTLPILPFPVFPPPRSELLLHVT', 1668, 'Q9QXL1; E9PUY6; P97424;', 'KD01065', 'Mus musculus (Mouse)', 'Kif21b', '#Kinesin-like protein KIF21B#Kinesin-like protein KIF6', '-', '-', '16565'),
(1066, 'Q09858', 'Kinetochore protein nnf1', 'GO:0000777===GO:0031617===GO:0000779===k', 16808, '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.', 'MTSRKEQLDAFLSRTLSETIAHIPLEKFAQCFPSMKKGKVIAVIHQQLIEFFEKSCKQEYANLIKERDLNKKLDMLDECIHDAEFRKLHGESEVDISNKQPQEILKAHLYSHKRELLDKLNQDLLDIDKENEGLSTQIAAGRKSN', 145, 'Q09858;', 'KD01066', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'nnf1', '#Kinetochore protein nnf1#NMS complex subunit nnf1', '-', '-', '-'),
(1067, 'Q9USR9', 'Centromere protein 3', 'GO:0000778===GO:0051315===GO:1903394===GO:0051455===GO:0000779', 72052, 'Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. Binds to the central core and inner repeats of the centromere. {ECO:0000269|PubMed:15791413}.', 'MTMNETSAIPARQRENQFFEIGVVGRKTGFTVPRDVKKGDDGFEDMDAYFLSDGSIHLDEDNGDIEQDMPPVTRLQPTSPMAVNAASDEASHASSSDSSDKNPDIPSSPLLMNSRALRASRGSSGPLIVPIDHSAFQAEDEGTADKTKVDGNKLSIQPRKANRIVDFSRIKASPDRKKFEPRRSTELPSKIPSSTPKDDNVQESPAFPDENITALQKNVANFTSIKDSGGRDNLYIQTISKPRRSYVQNNKSEQTIKPSKQNKQKEEKKTISQGNKPNSRDEDSELSIDVPLSMLNRSLANNSQKNKKRTPNKPLQESSINSVKEGESNPVVKRKRGRPRKNKLEIGNSVQTSEATQVKGAKKPAIRNAKKMSNEKDDSLNSQSDSASGEFIKTIARNNLQEIKQVEREDTLVGVRRSKRTRIAPLAFWKNERVVYELHRDENRIPALPEVKQIIRVDDPSPSIRQGRKKRHAKRSGVEIKSNLEAKSNDVEEYDAFYKDEINCEVLSWNEQNPKASEERVVGYSLPSVNLQQISNQQLKFASLFKEEPSFAAGVVEMPAGAEKPVKPSKHNIMSFCILQGKIEVTVNATTFRMKKDGVFIVPRGNYYSIKNIGKEAVRLYYTHATDTLENKRRGIGDFPNER', 643, 'Q9USR9; Q9USY5;', 'KD01067', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cnp3', '#Centromere protein 3#CENP-C homolog', '-', '-', '2539620'),
(1068, 'P67963', 'Casein kinase I isoform alpha', 'GO:0000777', 38901, 'Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. May play a role in segregating chromosomes during mitosis (By similarity). {ECO:0000250}.', 'MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKSKSNMKGF', 337, 'P67963; O57528; P70065; P79789; P79790; Q5D074;', 'KD01068', 'Xenopus laevis (African clawed frog)', 'csnk1a1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', '-', '379624'),
(1069, 'P67962', 'Casein kinase I isoform alpha', 'GO:0000777', 38901, 'Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. May play a role in segregating chromosomes during mitosis (By similarity). {ECO:0000250}.', 'MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKSKSNMKGF', 337, 'P67962; O57528; P70065; P79789; P79790;', 'KD01069', 'Gallus gallus (Chicken)', 'CSNK1A1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', '-', '395924'),
(1070, 'Q9FKP4', 'Kinesin-like protein KCA2', 'GO:0003777', 140396, 'Kinesin-like protein required for chloroplast movements and anchor to the plasma membrane. Mediates chloroplast movement via chloroplast actin (cp-actin) filaments. Required for the chloroplast avoidance response under high intensity blue light. {ECO:0000269|PubMed:15247388; ECO:0000269|PubMed:20418504}.', 'MAEQKSTNMWNWEVTGFESKKSPSSEEGVHRTPSSMLRRYSIPKNSLPPHSSELASKVQSLKDKVQLAKDDYVGLRQEATDLQEYSNAKLERVTRYLGVLADKSRKLDQYALETEARISPLINEKKRLFNDLLTTKGNVKVFCRARPLFEDEGPSIIEFPDNCTIRVNTSDDTLSNPKKEFEFDRVYGPQVGQASLFSDVQPFVQSALDGSNVSIFAYGQTHAGKTYTMEGSNQDRGLYARCFEELMDLANSDSTSASQFSFSVSVFELYNEQVRDLLSGCQSNLPKINMGLRESVIELSQEKVDNPSEFMRVLNSAFQNRGNDKSKSTVTHLIVSIHICYSNTITRENVISKLSLVDLAGSEGLTVEDDNGDHVTDLLHVTNSISALGDVLSSLTSKRDTIPYENSFLTRILADSLGGSSKTLMIVNICPSARNLSEIMSCLNYAARARNTVPSLGNRDTIKKWRDVANDARKEVLEKERENQRLKQEVTGLKQALKEANDQCVLLYNEVQRAWRVSFTLQSDLKSENAMVVDKHKIEKEQNFQLRNQIAQLLQLEQEQKLQAQQQDSTIQNLQSKVKDLESQLSKALKSDMTRSRDPLEPQPRAAENTLDSSAVTKKLEEELKKRDALIERLHEENEKLFDRLTEKSVASSTQVSSPSSKASPTVQPADVDSAGTLPSSVDKNEGTITLVKSSSELVKTTPAGEYLTAALNDFDPEQYEGLAAIADGANKLLMLVLAAVIKAGASREHEILAEIRDSVFSFIRKMEPRRVMDTMLVSRVRILYIRSLLARSPELQSIKVSPVERFLEKPYTGRTRSSSGSSSPGRSPVRYYDEQIYGFKVNLKPEKKSKLVSVVSRIRGHDQDTGRQQVTGGKLREIQDEAKSFAIGNKPLAALFVHTPAGELQRQIRSWLAESFEFLSVTADDVSGVTTGQLELLSTAIMDGWMAGVGAAVPPHTDALGQLLSEYAKRVYTSQMQHLKDIAGTLASEEAEDAGQVAKLRSALESVDHKRRKILQQMRSDAALFTLEEGSSPVQNPSTAAEDSRLASLISLDAILKQVKEITRQASVHVLSKSKKKALLESLDELNERMPSLLDVDHPCAQREIDTAHQLVETIPEQEDNLQDEKRPSIDSISSTETDVSQWNVLQFNTGGSSAPFIIKCGANSNSELVIKADARIQEPKGGEIVRVVPRPSVLENMSLEEMKQVFGQLPEALSSLALARTADGTRARYSRLYRTLAMKVPSLRDLVGELEKGGVLKDTKST', 1264, 'Q9FKP4;', 'KD01070', 'Arabidopsis thaliana (Mouse-ear cress)', 'KCA2', '#Kinesin-like protein KCA2#Kinesin CDKA-1-associated protein 2#Kinesin-like protein for actin based chloroplast movement 2', '-', '-', '836671'),
(1071, 'Q9NXR1', 'Nuclear distribution protein nudE homolog 1', 'GO:0000776===GO:0000777', 38808, 'Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post- mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. {ECO:0000269|PubMed:17600710; ECO:0000269|PubMed:21529752}.', 'MEDSGKTFSSEEEEANYWKDLAMTYKQRAENTQEELREFQEGSREYEAELETQLQQIETRNRDLLSENNRLRMELETIKEKFEVQHSEGYRQISALEDDLAQTKAIKDQLQKYIRELEQANDDLERAKRATIMSLEDFEQRLNQAIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQEKPRTPMPSSVEAERTDTAVQATGSVPSTPIAHRGPSSSLNTPGSFRRGLDDSTGGTPLTPAARISALNIVGDLLRKVGALESKLASCRNLVYDQSPNRTGGPASGRSSKNRDGGERRPSSTSVPLGDKGLGKRLEFGKPPSHMSSSPLPSAQGVVKMLL', 346, 'Q9NXR1; Q49AQ2;', 'KD01071', 'Homo sapiens (Human)', 'NDE1', '#Nuclear distribution protein nudE homolog 1#NudE', '-', 'ENSG00000072864', '-'),
(1072, 'Q09472', 'Histone acetyltransferase p300', 'k', 264161, 'Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at ''Lys-122'' (H3K122ac); a modification that localizes at the surface of the histone octamer and stimulates transcription; possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at ''Lys-27'' (H3K27ac). Also functions as acetyltransferase for nonhistone targets. Acetylates ''Lys-131'' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection; it is recruited by the viral protein Tat. Regulates Tat''s transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2; correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at ''Lys-626'' which is essential for its transcriptional coactivator activity (PubMed:10733570; PubMed:11430825; PubMed:11701890; PubMed:12402037; PubMed:12586840; PubMed:12929931; PubMed:14645221; PubMed:15186775; PubMed:15890677; PubMed:16617102; PubMed:16762839; PubMed:18722353; PubMed:18995842; PubMed:23415232; PubMed:23911289; PubMed:23934153; PubMed:8945521). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). {ECO:0000269|PubMed:10733570; ECO:0000269|PubMed:11430825; ECO:0000269|PubMed:11701890; ECO:0000269|PubMed:12402037; ECO:0000269|PubMed:12586840; ECO:0000269|PubMed:12929931; ECO:0000269|PubMed:14645221; ECO:0000269|PubMed:15186775; ECO:0000269|PubMed:15890677; ECO:0000269|PubMed:16617102; ECO:0000269|PubMed:16762839; ECO:0000269|PubMed:18722353; ECO:0000269|PubMed:18995842; ECO:0000269|PubMed:23415232; ECO:0000269|PubMed:23911289; ECO:0000269|PubMed:23934153; ECO:0000269|PubMed:8945521; ECO:0000305|PubMed:20955178}.', 'MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH', 2414, 'Q09472; B1AKC2;', 'KD01072', 'Homo sapiens (Human)', 'EP300', '#Histone acetyltransferase p300#p300 HAT#2.3.1.48 {ECO:0000269|PubMed:23415232; ECO:0000269|PubMed:23934153; ECO:0000269|PubMed:8945521}#E1A-associated protein p300', '-', 'ENSG00000255302', '-'),
(1073, 'Q8S950', 'Kinesin-like protein NACK1', 'GO:0003777', 108604, 'Probable plus end-directed motor protein that functions in the NACK-PQR (NPK1-NQK1/MEK1-NRK1) MAP kinase signaling pathway; which is essential for somatic cell cytokinesis; especially for the cell-plate formation and its expansion. Regulates the activity and the localization of NPK1 by association through the non-catalytic region of the kinase. {ECO:0000269|PubMed:11955449; ECO:0000269|PubMed:22006334}.', 'MTVRTPGTPASKIDKTPATTPNGHRGREEKIVVTVRLRPLNKRELSAKDHAAWECIDDHTIIYRPVPQERAAQPASSFTFDKVFGPDSITEAVYEEGVKNVALSSLMGINATIFAYGQTSSGKTYTMRGITEKAVNDIYAHIMSTPEREFRIRISGLEIYNENVRDLLNSESGRSLKLLDDPEKGTVVEKLVEETASNDQHLRHLISICEAQRQVGETALNDTSSRSHQIIRLTIESTLRESSDCVRSYVASLNFVDLAGSERASQTNADGARLREGCHINLSLMTLTTVIRKLSVGKRSGHIPYRDSKLTRILQHSLGGNARTAIICTLSPASSHVEQSRNTLYFATRAKEVTNNAQVNMVVSDKQLVKHLQKEVARLEAELRTPDPANEKDWKIQQMEMEIEELKRQRDLAQSQVDELRRKLQEEQGPKPSESVSPVVKKCLSFSGTLSPNLEEKAPVRSERTRNTMGRQSMRQSLAAPFTLMHEIRKLEHLQEQLGDEANRALEVLQKEVACHRLGNQDAAETIAKLQAEIREMRSIRPLPKEVEVGSVVAVNKSVSANLKEEIARLHSQGSTIADLEEQLENVQKSLDKLVMSLPSNNDQQSNNDTTQKAKHPSKKKKLLPLTSSNSINRQNFLKSPCSPLSTARQVLDCEVENRAPDSDDLSCEIQPDETPTKSDGGDVSSKEGTPYRRSSSVNMRKMQKMFQEAAEENVRNIRSYVTELKERVAKLQYQKQLLVCQVLELEANEAAGYNLEDDENIHQIPEESPVSWQITFKEQRQQIIDLWDVCYVSIIHRSQFYLLFKGDPADEIYLEVELRRLTWLQQHLAELGNATPARVGNEPTVSLSSSIRALKREREFLAKRLTTRLTAEERDYLYIKWEVPLEGKQRRMQFINKLWTNPHDAKHVHESAEIVAKLVGFCEGGNMSREMFELNFVLPSDRRPWFAGWNQISDLLHI', 959, 'Q8S950;', 'KD01073', 'Nicotiana tabacum (Common tobacco)', 'NACK1', '#Kinesin-like protein NACK1#NPK1-activating kinesin-1', '-', '-', '-'),
(1074, 'Q9CZX5', 'PIN2/TERF1-interacting telomerase inhibitor 1', 'GO:0000776===GO:0000777', 37221, '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}.', 'MSMLAERRRKQKWTVDPRNTAWSNDDSKFGQKMLEKMGWSKGKGLGAQEQGATEHIKVKVKNNHLGLGATNNNEDNWIAHQDDFNQLLAALNTCHGQETADSSDKKEKKSFSLEEKSKISKNRVHYMKFTKGKDLSSRSETDLDCIFGKRRNKKLAQDGCSNSSADEVNTSLTTTTTTTSAFTIQEYFAKRMAQLKNKPQASAPGSDLSETPVERKKGKKKNKEAADTDVENSPQHKAKRHKKKKRVEAERGPVAKKRDRAELQPGGPSEDECSDASVEAAEDCVQTPDIQDDVPKPKKRKAKKKLQRPEGVEIDATLDRAPVKKKKKKVSR', 332, 'Q9CZX5; Q14BS4; Q3V450; Q8C6E5; Q91WZ9; Q9D0C2;', 'KD01074', 'Mus musculus (Mouse)', 'Pinx1', '#PIN2/TERF1-interacting telomerase inhibitor 1#67-11-3 protein#LPTS1#Liver-related putative tumor suppressor#Pin2-interacting protein X1#TRF1-interacting protein 1', '-', '-', '72400'),
(1075, 'P33175', 'Kinesin heavy chain isoform 5A', 'GO:0003777', 117019, 'Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH; NFM and NFL). {ECO:0000269|PubMed:12682084}.', 'MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEDSALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMRDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELARLQAHETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNNLFQNYQNLHLQAAPSSTSDMYFASSGATSVAPLASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQETAAS', 1027, 'P33175; Q5DTP1; Q6PDY7; Q9Z2F9;', 'KD01075', 'Mus musculus (Mouse)', 'Kif5a', '#Kinesin heavy chain isoform 5A#Kinesin heavy chain neuron-specific 1#Neuronal kinesin heavy chain#NKHC', '-', '-', '16572'),
(1076, 'P39057', 'Dynein beta chain; ciliary', 'GO:0003777', 511783, '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.', 'MGDVVDARLDFISEYILKSYKLKPDKWTKCINVEENKILMLEFLEKADNPQLVFTVNPAGLITPSYEFPSALKNTKAIYFIKKGREPVGKDNIKTNLVYGDLSYTPLEQLSALVDEVLVPLLANPRNHEQWPVVVSQDVLRHVHNLKSSVYVVAGQVKGKTLLPLPVGSEKVETAAGSEEKDDSYDRSLVHAIESVIIDWTHQIRDVLKRDSAQPLLEGLNPGPMVEINFWKAKCENLDCIFQQLRDPKVRKMKELLERTQSSYLPSFNNIERDVEAALTEAQDINIHLKPLVYQIESMDELEFSDLTPRLAPILHTVCLIWSNSDYYNTAPRVIVLLQEICNLLIDLCRTFLDPSEIFKLEPEESLEKVRGALTVLKNWRELYDEHRAKLKDYFKDGKEVKEWEFASPLVFTRMDNFIRRIETIQSLFETNVEFSKLEKTEMGSMKGRMLSQQVEKIHEEFQECAKVFTERPYDGLDPTCQEFLEDYEEFEKKVFDLDRRLGSILCQGFDDCCGLEAAFKMLDCYGPLLDRPVIRNDFECKYPIVLMLYDQELDQSKEIYDEHMRVEEANGNAPLNKNMPDVAGQLKWSAQLRDRISKPMGSLKHMEHPTGVRRILESEDAKVIFQKYEEMLNLLNKYEQKVFENWTKGVDEVCKTNLDQSLITRDDASKLIMVNFDPKLVSVLREVKYLQIRGEETIPESAASIYEKHETLRKYVANLDLTVAWYNKVRKTVLEVEFPLIEGQLADLDTRLRQAEADLNWTSDSVWEYIQETRDQVRDLEKRVQQTKDNVDRIKKIMAEWTKQPLFERKELKKESLLALDDRQDRLKKRYAEITTAGEKIHSLMKENLDLFKAEASSDIWKAYVDYVDDMVIDGFFNCIHCTLTYLLENTDPRHCAAPLFEARLELQVPDMIFNPSLDYGIADGFYDLVEMLISDTYKMASLVNRLAEHNGQEHYQADLEGMDDLSDVRNDLMDRVQTIMTKAQEYRNSFDNYAYLYVDDRKEFMRQFLLYNHVLTTEEIEAHAEDGVPECPPTLDQFKEQVDTYEKIYSEADEIEPEQVFDAWFRVDSKPFKAALLNIIKKWSFMFKQHLIDHVTNSLSELQEFIKVGNSGLTKTVEDGDYNGLVDCMGHLMAVKERQAATDEMFEPIKQTIELLKTYDQEMSEEVHTQLQELPEQWNNTKKIAITIKQQVAPLQANEVAIIRRKCTSFDVRQHEFRERFRKEAPFIFLFDGPYQCLDKCHSEIYEMEEHMAKLQESAGLFEVNMPDYKQLKACRREVRLLKGLWDLIMVVRTSIEDWKTTPWLEINVEQMEMDCKKFAKDIRSLDKEMRAWDAYNGLDATVKNMLTSLRAVSELQNPAIRERHWQQLMAATKVKFTMDKETTLSDLLALNLHNFEDEVRNIVDKAVKEMGMEKVLKELNTTWSSMDFDYEPHSRTGISLLKSNEELIETLEDNQVQLQNLMTSKHIAHFLEEVSGWQKKLSTTDSVITIWFEVQRTWSHLESIFIGSEDIRNQLPEDSKRFDGIDTDFKELAAEMEKTPNVVEATNKARLFDRLEAIQGSLVVCEKALAEYLETKRLAFPRFYFVSSADLLDILSQGNNPTQVQRHLSKLFDNMAKLKFKQDDEGNDTKLALGMYSKEGEYVDFDKECECTGQVEVWLNRVMDTMRSTVRSQFADAVVSYEEKPREQWLYDYPAQVALATTQVWWTTEVNISFARLEEGHENSMKDYNKKQILQLNTLIGLLIGKLTKGDRQKIMTICTIDVHARDVVAMMVLKKVDSAQAFQWLSQLRHRWADDDKHCYANICDAQFKYSYEYLGNTPRLVITPLTDRCYITLTQSLHLVMSGAPAGPAGTGKTETTKDLGRALGIMVYVFNCSEQMDYKSCGNIYKGLAQTGAWGCFDEFNRISVEVLSVVAVQVKCVQDAIRDKKERFNFMGEEISLIPSVGIFITMNPGYAGRTELPENLKALFRPCAMVVPDFELICEIMLVAEGFLEARLLARKFITLYTLCKELLSKQDHYDWGLRAIKSVLVVAGSLKRGDPQRPEDQVLMRALRDFNVPKIVSDDTPVFMGLIGDLFPALDVPRRRDLDFEKVVKQSTLDLKLQAEDSFVLKVVQLEELLAVRHSVFVIGNAGTGKSQVLKVLNKTYSNMKRKPVFIDLNPKAVTNDELFGIINPATREWKDGLFSVIMRDMSNITHDGPKWIVLDGDIDPMWIESLNTVMDDNKVLTLASNERIPLTPSMRLLFEISHLKTATPATVSRAGILYINPSDLGWNPIVTSWIDTREVQSERANLTILFDKYLPTLLDTLRIRFKKIIPIPEQSMVQMLCYLLECLLTPENTPADCPKELYELYFVFASIWAFGGSMFQDQLVDYRVEFSKWWITEFKTIKFPNQGTVFDYYIDQESKKFLPWSEKVPTFELDPEIPMQAVLVHTNETTRVRFFMDLLMERGRPVMLVGNAGLGKSVLVGDKLSNLGEDSMVANVPFNYYTTSEMLQRVLEKPLEKKAGRNYGPPGTKKLVYFIDDMNMPEVDTYGTVQPHTLIRQHMDYKHWYDRAKLTLKEIHKCQYVSCMNPTSGSFTINSRLQRHFCVFALSFPGQDALSTIYNSILSQHLANIAVSNALQKLSPTVVSATLDLHKKVAQSFLPTAIKFHYVFNLRDLSNVFQGLLYSGSDLLKSPIDFARLWMHECQRVYGDKMINDQDIEAFEKLVFEYAKKFFEDVDEEALKAKPNIHCHFATGIGDPKYMPCATWPELNKILVEALDTYNEINAVMNLVLFEDAMQHVCRINRILESPRGNALLVGVGGSGKQSLARLASYISSLEVFQITLRKGYGIPDLKLDLATVCMKAGLKNIGTVFLMTDAQVSDEKFLVLINDLLASGEIPDLFADDEVENIIGGVRNEVKGMGLQDTRENCWKFFIDRLRRQLKTVLCFSPVGTTLRVRSRKFPAVVNCTSIDWFHEWPQEALVSVSKRFLDEVELLKGDIKNSIAEFMAYVHVSVNESSKQYLTNERRYNYTTPKSFLEQIKLYESLLAMKSKELTAKMERLENGLTKLQSTAQQVDDLKAKLASQEVELAQKNEDADKLIQVVGVETEKVSKEKATVDDEEKKVAIINEEVSKKAKDCSEDLAKAEPALLAAQEALNTLNKNNLTELKSFGSPPSAVLKVAAAVMVLLAPNGKIPKDRSWKAAKVVMNKVDAFLDSLINYDEENIHENCQKAIKEYLNDPEFEPEYIKGKSLAAGGLCSWVVNIVKFYNVYCDVEPKRIALQKANDELKAAQDKLALIKAKIAELDANLAELTAQFEKATSDKLKCQQEAEATSRTITLANRLVGGLASENVRWGEAVANFKIQEKTLPGDVLLITAFVSYIGCFTKNYRVDLQDRMWLPFLKSQKDPIPITEGLDVLSMLTDDADIAVWNNEGLPSDRMSTENATILSNCQRWPLMIDPQLQGIKWIKQKYGDELRVIRIGQRGYLDTIENAISSGDTVLIENMEESIDPVLDPVLGRNTIKKGRYIKIGDKEVEYNPEFRLILQTKLANPHYKPEMQAQTTLINFTVTRDGLEDQLLANVVAQERPDLEKLKSDLTKQQNDFKIILKELEDNLLSRLSSAEGNFLGDTALVENLETTKRTAAEISVKVEEAKVTEVKINEARELYRPAAARASLLYFILNDLNKINPIYQFSLKAFNTVFSLSIARAEPCEDVKERVVNLIDCITYSVFIYTTRGLFEADKLIFTTQVAFQVLLMKKEIAQNELDFLLRFPIQVGLTSPVDFLTNSAWGAIKSLSAMEDFRNLDRDIEGSAKRWKKFVESECPEKEKFPQEWKNKSALQKLCMMRALRADRMSYAVRNFIEEKLGSKYVEGRQVEFAKSYEETDPATPVFFILSPGVDPLKDVEALGKKLGFTFDNNNFHNVSLGQGQEIVAEQCMDLAAKEGHWVILQNIHLVAKWLSTLEKKLEQYSIGSHESYRVYMSAEPAGSPESHIIPQGILESSIKITNEPPTGMFANLHKALYNFNQDTLEMCAREAEFKVILFALCYFHAVVCERQKFGPQGWNRSYPFNTGDLTISVNVLYNYLEANSKVPWQDLRYLFGEIMYGGHITDDWDRRLCRTYLEEYMAPEMLDGDLYLAPGFPVPPNSDYKGYHQYIDEILPPESPYLYGLHPNAEIGFLTTESDNLFKVVLELQPRDAGGGGGGGSSREEKIKSLLDEIVEKLPEEFNMMEIMGKVEDRTPYVVVAFQECERMNTLTSEIRRSLKELDLGLKGELTITPDMEDLSNALFLDQIPASWVKRAYPSLFGLSAWYADLLQRIKELEQWTADFALPNVVWLGGFFNPQSFLTAIMQSMARKNEWPLDKMCLQCDVTKKNKEDFSSAPREGSYVHGLFMEGARWDTQTNMIADARLKELAPNMPVIFIKAIPVDKQDTRNIYECPVYKTKQRGPTFVWTFNLKSKEKAAKWTLAGVALLLQV', 4466, 'P39057;', 'KD01076', 'Heliocidaris crassispina (Sea urchin) (Anthocidaris crassispina)', '', '#Dynein beta chain; ciliary', '-', '-', '-'),
(1077, 'P97633', 'Casein kinase I isoform alpha', 'GO:0000777', 37495, 'Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at ''Ser-45''. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis. {ECO:0000269|PubMed:11955436}.', 'MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQGKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF', 325, 'P97633; P97634;', 'KD01077', 'Rattus norvegicus (Rat)', 'Csnk1a1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', '-', '113927'),
(1078, 'Q04477', 'Kinetochore protein SPC24', 'GO:0000778===GO:0031262===GO:0000780===c;k', 24604, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is involved in chromosome segregation and spindle checkpoint activity. {ECO:0000269|PubMed:11266451; ECO:0000269|PubMed:11952896; ECO:0000269|PubMed:12514103}.', 'MSQKDNLLDNPVEFLKEVRESFDIQQDVDAMKRIRHDLDVIKEESEARISKEHSKVSESNKKLNAERINVAKLEGDLEYTNEESNEFGSKDELVKLLKDLDGLERNIVSLRSELDEKMKLYLKDSEIISTPNGSKIKAKVIEPELEEQSAVTPEANENILKLKLYRSLGVILDLENDQVLINRKNDGNIDILPLDNNLSDFYKTKYIWERLGK', 213, 'Q04477; D6VZU0;', 'KD01078', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SPC24', '#Kinetochore protein SPC24', '-', '-', '855144'),
(1079, 'Q0V9F7', 'Borealin-2', 'GO:0032133', 32323, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Contributes to CPC function by facilitating loading of the CPC onto chromosomes (By similarity). {ECO:0000250|UniProtKB:Q4V7H8}.', 'MPPKRNRKRLGTRGEGSGDSGVGMFERNDAVQEQKKEKIRLFMQDFVQQGKDRLAELKKDLESLSTTADKALEVELLKMPLAIRHMKVQDYLSLMGGDKTAVAAAAVKLDCSVDELSEPKLVRKSSKKVKVTTNVEYQDDIRTKVMTTTGKTRTVQKVPKSKSMLSLTGKNSKKTTALTRSVSATPIDKASKKLLVTNSSSKPAQRSSRTAMTPLSRSARSDAVFSFGDGTFLDEGVPFVKIPLADGQTVFSAGDDLDSLNVELLRGDTVQHIHNLVGQLTNLCAKASIQQHGNTL', 296, 'Q0V9F7;', 'KD01079', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'cdca9', '#Borealin-2 {ECO:0000250|UniProtKB:Q4V7H8}#Cell division cycle-associated protein 8.2#Cell division cycle-associated protein 9#Dasra-A {ECO:0000250|UniProtKB:Q4V7H8}', '-', '-', '779847'),
(1080, 'Q754Z1', 'Spindle assembly checkpoint component MAD1', 'GO:0000778', 75421, 'Central component of the spindle assembly checkpoint.', 'MSQTGDSSSFVEEPASPEARQRELERQVLGLEYRLRTEHSEAEMARLALERELAGMQGKYKQCMGELEAALADTRYLYEQNAALEARARAADEDAGGAAAAERAAAAEERARAAEARARELEEALQAARGEAAAAGRAAAGAAAGAAAAEQSGLLRKYEAEIERQMGELRALAERLAEREDEVAGLKAQRVLQAHRSYSAEEVEELGVLRRTLQEQLALSKELERANLEQANELKRLRQRSESQQFLQLENSKLRARLEKTDALRQQLDDLQLENVQLQEKLTKWEVYQADGSSPENVLHEMALAKQERLALVEQVGKLQLDLNNMKILNDELALERNQLLDLNKKYESSILNLKKLNYEIEQQKLLSFEECKLLRQQLDDLSEVDKDHTPDTRDRKKIQTLVDTYKNQTEDLTNELKKLNEQLLERSDLDGNPRKRRKASDDLAFNYSQRLNELQLRNKDLERRLANSDENASLLEEKLRKLQSLNEKKIRILQLRNNPLLKDQFVKQKQLTLLKQENLELAQQLDAQQGLEAVPRSVYERQQYDIQLLEDELFSINKRTTRLKEMFNRKSLEFIDAVNSLLGFKLEFQVGGKVKMIPCFKTDRYLIADLQTNTLKSNLDKVMPEWDAMLAEYVGKRQQLPCFLAKIMLLLAESSSSQ', 659, 'Q754Z1;', 'KD01080', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'MAD1', '#Spindle assembly checkpoint component MAD1#Mitotic arrest deficient protein 1', '-', '-', '4621713'),
(1081, 'Q03330', 'Histone acetyltransferase GCN5', 'k', 51069, 'Acetylates histone H2B to form H2BK11ac and H2BK16ac; histone H3 to form H3K9ac; H3K14ac; H3K18ac; H3K23ac; H3K27ac and H3K36ac; with a lower preference histone H4 to form H4K8ac and H4K16ac; and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Operates in concert with certain DNA-binding transcriptional activators such as GCN4 or HAP2/3/4. Its acetyltransferase activity seems to be dependent on the association in different multisubunit complexes. Functions as histone acetyltransferase component of the transcription regulatory histone acetylation (HAT) complexes SAGA; SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters; SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3; SPT8 and SPT20) and promoter selectivity; interaction with transcription activators (GCN5; ADA2; ADA3 and TRA1); and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac; H3K14ac; H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA; an altered form of SAGA; may be involved in positive transcriptional regulation. The ADA histone acetyltransferase complex preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B; leading to transcription regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3; at least after activation at the GAL1-10 locus. {ECO:0000269|PubMed:10026213; ECO:0000269|PubMed:16543222; ECO:0000269|PubMed:16543223}.', 'MVTKHQIEEDHLDGATTDPEVKRVKLENNVEEIQPEQAETNKQEGTDKENKGKFEKETERIGGSEVVTDVEKGIVKFEFDGVEYTFKERPSVVEENEGKIEFRVVNNDNTKENMMVLTGLKNIFQKQLPKMPKEYIARLVYDRSHLSMAVIRKPLTVVGGITYRPFDKREFAEIVFCAISSTEQVRGYGAHLMNHLKDYVRNTSNIKYFLTYADNYAIGYFKKQGFTKEITLDKSIWMGYIKDYEGGTLMQCSMLPRIRYLDAGKILLLQEAALRRKIRTISKSHIVRPGLEQFKDLNNIKPIDPMTIPGLKEAGWTPEMDALAQRPKRGPHDAAIQNILTELQNHAAAWPFLQPVNKEEVPDYYDFIKEPMDLSTMEIKLESNKYQKMEDFIYDARLVFNNCRMYNGENTSYYKYANRLEKFFNNKVKEIPEYSHLID', 439, 'Q03330; D6VV32; Q6B165;', 'KD01081', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'GCN5', '#Histone acetyltransferase GCN5#2.3.1.48', '-', '-', '853167'),
(1082, 'A6QPL4', 'Kinesin-like protein KIF22', 'GO:0003777', 73202, '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}.', 'MDAGLPARRRREMAAAISGAGRCRLSKVGAGRRPPPARVRVAVRLRPFVDGTAGENDTPCVRGLDSCSLEIANWRNHQETLKYQFDAFYGERSSQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGAEGRPWALSVTMSYLEIYQEKVLDLLEPSSGDLVIREDCRGNILIPGLTQKPITSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQLPVLAPVKLSQKELLGPSEAKRARGPEEEETESPELPIAPASASQKLSPLQKLSSMDPAMLERLLSLDRLLGSQGSQGTPLLSTPKRERMVLMKTVEEKDLEIERLKMKQKELEAKVLAQEAADPKEKENYSTTMLRPLARRTVTVAKPLKKAVVMPLQLIQEQAASPNAKIHILKKKGRKRKLESLDASQPEKAEDGWELQISPELLAHGRQKILDLLNEGSARDLRSLQRIGQKKAQLIVGWRELHGPFSQVEDLERVEGISGKQMESFLKANILGLAAGQGCGPS', 662, 'A6QPL4;', 'KD01082', 'Bos taurus (Bovine)', 'KIF22', '#Kinesin-like protein KIF22', '-', '-', '506294'),
(1083, 'Q6Q783', 'Histone-lysine N-methyltransferase SUV420H2', 'GO:0000780', 53159, 'Histone methyltransferase that specifically trimethylates ''Lys-20'' of histone H4. H4 ''Lys-20'' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1; RBL1 and RBL2). {ECO:0000269|PubMed:15145825}.', 'MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPTLRRQHHLRSALEAFLRQRDLEAAFRALTLGGWMAHYFQSRAPRQEAALKTHIFCYLRAFLPESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEDLLRAGENDFSIMYSTRKRSAQLWLGPAAFINHDCKPNCKFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGEGAFRLQPREPELRPKPLDKYELRETKRRLQQGLVSSQQSLMSRWACSHLSPLRPDPFCAACQPSCLLPASPHMDYLPLWLQRAPQPQPIVPPRKRHRRRRPRIRQASLPPVLRTACVPLHRWGGCGPHCQLRAEAMVTLHLRPQTRWTPQQDWYWARRYGLPSVGRVELTRLAPALPAAPAPAGNPGPVPTPDFIPKQALAFAPFCPPKRLRLVVSHGSIDLDINSGEP', 468, 'Q6Q783; Q5RKP6; Q8R1C5;', 'KD01083', 'Mus musculus (Mouse)', 'Suv420h2', '#Histone-lysine N-methyltransferase SUV420H2#2.1.1.43#Suppressor of variegation 4-20 homolog 2#Su(var)4-20 homolog 2#Suv4-20h2', '-', '-', '232811'),
(1084, 'Q59ZG8', 'DASH complex subunit DAD2', 'GO:0000776===GO:0042729', 14049, '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}.', 'MSKTNTAIYQKIAEKRANLERFREFKELTDDLVLQLESIGDKLETMNGGTASVALILANWKSVVQSISLASLALMKESNDNNKEAFPEPLVRVRVGQSNEENQDEEEADEEEGVRDSEEVEESTE', 125, 'Q59ZG8;', 'KD01084', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'DAD2', '#DASH complex subunit DAD2#Outer kinetochore protein DAD2', '-', '-', '3643465'),
(1085, 'P21613', 'Kinesin heavy chain', 'GO:0003777', 109407, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport.', 'MDVASECNIKVICRVRPLNEAEERAGSKFILKFPTDDSISIAGKVFVFDKVLKPNVSQEYVYNVGAKPIVADVLSGCNGTIFAYGQTSSGKTHTMEGVLDKPSMHGIIPRIVQDIFNYIYGMDENLEFHIKISYYEIYLDKIRDLLDVTKTNLAVHEDKNRVPFVKGATERFVSSPEEVMEVIDEGKNNRHVAVTNMNEHSSRSHSVFLINVKQENVETQKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALADGNKSHVPYRDSKLTRILQESLGGNARTTMVICCSPASYNESETKSTLLFGQRAKTIKNVVSVNEELTADEWKRRYEKEKERVTKLKATMAKLEAELQRWRTGQAVSVEEQVDLKEDVPAESPATSTTSLAGGLIASMNEGDRTQLEEERLKLYQQLDDKDDEINNQSQLIEKLKEQMMEQEDLIAQSRRDYENLQQDMSRIQADNESAKDEVKEVLQALEELAMNYDQKSQEVEDKNKENENLSEELNQKLSTLNSLQNELDQLKDSSMHHRKRVTDMMINLLKDLGDIGTIVGGNAAETKPTAGSGEKIEEEFTVARLYISKMKSEVKTLVSRNNQLENTQQDNFKKIETHEKDLSNCKLLIQQHEAKMASLQEAIKDSENKKRMLEDNVDSLNEEYAKLKAQEQMHLAALSEREKETSQASETREVLEKQMEMHREQHQKQLQSLRDEISEKQATVDNLKDDNQRLSLALEKLQADYDKLKQEEVEKAAKLADLSLQIDRREQAKQDLKGLEETVAKELQTLHNLRKLFVQDLQNKVKKSCSKTEEEDEDTGGNAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATMERVKSLESALKDAKEGAMRDRKRYQHEVDRIKEAVRQKNLARRGHAAQIAKPIRPGQHQSVSPAQAAAIRGGGGLSQNGPMITSTPIRMAPESKA', 967, 'P21613;', 'KD01085', 'Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii)', '', '#Kinesin heavy chain', '-', '-', '-'),
(1086, 'C7GKW3', '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, 'C7GKW3;', 'KD01086', 'Saccharomyces cerevisiae (strain JAY291) (Baker''s yeast)', 'KRE28', '#Spindle pole body component KRE28', '-', '-', '-'),
(1087, 'P27895', 'Kinesin-like protein CIN8', 'GO:0005828===GO:0000778===GO:0003777===k', 113311, 'Required for assembly of the mitotic spindle. Interacts with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly; CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediated by KAR3. {ECO:0000269|PubMed:1618897; ECO:0000269|PubMed:1643659}.', 'MPAENQNTGQDRSSNSISKNGNSQVGCHTVPNEELNITVAVRCRGRNEREISMKSSVVVNVPDITGSKEISINTTGDTGITAQMNAKRYTVDKVFGPGASQDLIFDEVAGPLFQDFIKGYNCTVLVYGMTSTGKTYTMTGDEKLYNGELSDAAGIIPRVLLKLFDTLELQQNDYVVKCSFIELYNEELKDLLDSNSNGSSNTGFDGQFMKKLRIFDSSTANNTTSNSASSSRSNSRNSSPRSLNDLTPKAALLRKRLRTKSLPNTIKQQYQQQQAVNSRNNSSSNSGSTTNNASSNTNTNNGQRSSMAPNDQTNGIYIQNLQEFHITNAMEGLNLLQKGLKHRQVASTKMNDFSSRSHTIFTITLYKKHQDELFRISKMNLVDLAGSENINRSGALNQRAKEAGSINQSLLTLGRVINALVDKSGHIPFRESKLTRLLQDSLGGNTKTALIATISPAKVTSEETCSTLEYASKAKNIKNKPQLGSFIMKDILVKNITMELAKIKSDLLSTKSKEGIYMSQDHYKNLNSDLESYKNEVQECKREIESLTSKNALLVKDKLKSKETIQSQNCQIESLKTTIDHLRAQLDKQHKTEIEISDFNNKLQKLTEVMQMALHDYKKRELDLNQKFEMHITKEIKKLKSTLFLQLNTMQQESILQETNIQPNLDMIKNEVLTLMRTMQEKAELMYKDCVKKILNESPKFFNVVIEKIDIIRVDFQKFYKNIAENLSDISEENNNMKQYLKNHFFKNNHQELLNRHVDSTYENIEKRTNEFVENFKKVLNDHLDENKKLIMQNLTTATSAVIDQEMDLFEPKRVKWENSFDLINDCDSMNNEFYNSMAATLSQIKSTVDTSSNSMNESISVMKGQVEESENAISLLKNNTKFNDQFEQLINKHNMLKDNIKNSITSTHSHITNVDDIYNTIENIMKNYGNKENATKDEMIENILKEIPNLSKKMPLRLSNINSNSVQSVISPKKHAIEDENKSSENVDNEGSRKMLKIE', 1000, 'P27895; D3DLI9;', 'KD01087', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CIN8', '#Kinesin-like protein CIN8#Chromosome instability protein 8', '-', '-', '856648'),
(1088, 'P69852', 'DASH complex subunit HSK3', 'GO:0008608===GO:0051987===GO:0042729===c;k', 8088, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A; and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally; thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids. {ECO:0000269|PubMed:15664196; ECO:0000269|PubMed:16415853; ECO:0000269|PubMed:16777964}.', 'MNANKQRQYNQLAHELRELQTNLQETTKQLDIMSKQCNENLVGQLGKVHGSWLIGSYIYYMEQMLGKTQ', 69, 'P69852; D6VX58;', 'KD01088', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'HSK3', '#DASH complex subunit HSK3#Helper of ASK1 protein 3#Outer kinetochore protein HSK3', '-', '-', '853719'),
(1089, 'Q6FU23', 'DASH complex subunit DUO1', 'GO:0042729', 23577, '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}.', 'MSESLDNSAINQLIPEIFDQMRHNAARTRDAKKPSAMVEESGSITTQSLLRELETLDKVIATIRSIDSVVKGALPSHMNKIHHVCKSTNKMLDNWINIQSQAGYAHHIMDSRTGSKTGSNSNEEVVEQYKQEIAELQKSIKMEEDKLIPAQVKGNGNGPTGQRLYGNSYRQPTGRVTKATALRNARNRPSGIPQISSRLTRPTASSNLKRQR', 212, 'Q6FU23;', 'KD01089', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'DUO1', '#DASH complex subunit DUO1#Outer kinetochore protein DUO1', '-', '-', '2887579'),
(1090, 'P69851', 'DASH complex subunit DAD4', 'GO:0008608===GO:0051987===GO:0042729===SCL===c;k', 8155, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A; and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally; thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids. {ECO:0000269|PubMed:15664196; ECO:0000269|PubMed:16415853; ECO:0000269|PubMed:16777964}.', 'MENPHEQVQANILSRIIGNVKRLNESVAILNQELVTINNRNKNLEIMGAICDNYHSSVQFNLEATNNKKPPL', 72, 'P69851; D6VSV2;', 'KD01090', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DAD4', '#DASH complex subunit DAD4#DUO1 and DAM1-interacting protein 4#Helper of ASK1 protein 2#Outer kinetochore protein DAD4', '-', '-', '851919'),
(1091, 'P69850', 'DASH complex subunit DAD3', 'GO:0008608===GO:0051987===GO:0042729===SCL===k', 10848, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A; and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally; thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids. {ECO:0000269|PubMed:15664196; ECO:0000269|PubMed:16415853; ECO:0000269|PubMed:16777964}.', 'MEHNLSPLQQEVLDKYKQLSLDLKALDETIKELNYSQHRQQHSQQETVSPDEILQEMRDIEVKIGLVGTLLKGSVYSLILQRKQEQESLGSNSK', 94, 'P69850; D6VQM9;', 'KD01091', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DAD3', '#DASH complex subunit DAD3#DUO1 and DAM1-interacting protein 3#Outer kinetochore protein DAD3', '-', '-', '852535'),
(1092, 'Q12143', 'Kinetochore-associated protein NSL1', 'GO:0000776===GO:0000818===c;k', 25416, 'Acts as essential component of the kinetochore MIND complex; which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules. NSL1 facilitates the attachment of two of the DASH complex components; DAD2 and SPC19; to the kinetochore in a microtubule-dependent manner. {ECO:0000269|PubMed:12455957; ECO:0000269|PubMed:14633972; ECO:0000269|PubMed:14657030}.', 'MSQGQSKKLDVTVEQLRSIYHQFHDILEEKTDLHLPKKEYDDDAVRREVQIQLQEFLLSAMTMASKSLEVVNADTVGKTVKQLIMESQEKYMEPFDLDLNEQVRKMYQEWEDETVKVAQLRQTGPAKINEVYNNSKDEYLAQLDGRIGVLQARMMQQQSADHDDSTDDADDHINWEHIKQDYVASLNELYQTQQDLPKVRYNVEKVKRLMDFLEED', 216, 'Q12143; D6W3D7; Q6B152;', 'KD01092', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'NSL1', '#Kinetochore-associated protein NSL1', '-', '-', '855843'),
(1093, 'Q8VDQ8', 'NAD-dependent protein deacetylase sirtuin-2', 'GO:0051987', 43256, 'Isoform 2: Deacetylates alpha-tubulin.', 'MAEPDPSDPLETQAGKVQEAQDSDSDTEGGATGGEAEMDFLRNLFTQTLGLGSQKERLLDELTLEGVTRYMQSERCRKVICLVGAGISTSAGIPDFRSPSTGLYANLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFIRLLKEKGLLLRCYTQNIDTLERVAGLEPQDLVEAHGTFYTSHCVNTSCRKEYTMGWMKEKIFSEATPRCEQCQSVVKPDIVFFGENLPSRFFSCMQSDFSKVDLLIIMGTSLQVQPFASLISKAPLATPRLLINKEKTGQTDPFLGMMMGLGGGMDFDSKKAYRDVAWLGDCDQGCLALADLLGWKKELEDLVRREHANIDAQSGSQAPNPSTTISPGKSPPPAKEAARTKEKEEQQ', 389, 'Q8VDQ8; E9PXF5; Q9CXS5; Q9EQ18; Q9ERJ9; U5TP50;', 'KD01093', 'Mus musculus (Mouse)', 'Sirt2', '#NAD-dependent protein deacetylase sirtuin-2#3.5.1.-#Regulatory protein SIR2 homolog 2#SIR2-like protein 2#mSIR2L2', '-', '-', '64383'),
(1094, 'P53397', 'N-glycosylase/DNA lyase', 'GO:0031518', 42781, 'DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7;8-dihydro-8-oxoguanine and 2;6-diamino-4-hydroxy-5-N- methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta- lyase activity that nicks DNA 3'' to the lesion.', 'MSYKFGKLAINKSELCLANVLQAGQSFRWIWDEKLNQYSTTMKIGQQEKYSVVILRQDEENEILEFVAVGDCGNQDALKTHLMKYFRLDVSLKHLFDNVWIPSDKAFAKLSPQGIRILAQEPWETLISFICSSNNNISRITRMCNSLCSNFGNLITTIDGVAYHSFPTSEELTSRATEAKLRELGFGYRAKYIIETARKLVNDKAEANITSDTTYLQSICKDAQYEDVREHLMSYNGVGPKVADCVCLMGLHMDGIVPVDVHVSRIAKRDYQISANKNHLKELRTKYNALPISRKKINLELDHIRLMLFKKWGSYAGWAQGVLFSKEIGGTSGSTTTGTIKKRKWDMIKETEAIVTKQMKLKVELSDLHIKEAKID', 376, 'P53397; D6VZB3;', 'KD01094', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'OGG1', '#N-glycosylase/DNA lyase#8-oxoguanine DNA glycosylase#3.2.2.-#DNA-(apurinic or apyrimidinic site) lyase#AP lyase#4.2.99.18', '-', '-', '854942'),
(1095, 'Q01649', 'Spindle pole body-associated protein CIK1', 'GO:0003777', 69070, 'A developmentally regulated protein important for microtubule functions. Targets KAR3 to the cytoplasmic microtubules during mating. Essential for KAR3 function during prophase of meiosis I. Required for interhomolog recombination; synapsis of homologous chromosomes and establishment of a meiosis I spindle. {ECO:0000269|PubMed:10087265; ECO:0000269|PubMed:11729143}.', 'MNNSKIPKLSFHSDPNNVTRDFPKTKRQKVQKREMDMILTPNNNKLNILHSSGSGIRRCYTDDTSATYTKKLTFGGDPKIIERVKNNERKVRKDIDSLLNAISEIEKESVRIHARELPAITLELDAKVKACRELQNEIDGLSTEMDLKDNQCDLQRKNVELSSKNIVSMHAVKVQEFENDLEEELSNAKREWTYKLMEVENLKPDERLTDEMRQLKTEFEEVNRKLFILQNENENECKNYKKELDKKFEIFKKVKNDARIELDGEQERLSKVLKDLQDTHGELKENIKTCRDEFNDFEKRIGEAEVNFHSMELAVVPLKKKLASTSQALTQVQEEKKQVEGEANNWKKKYVNELEKVQQELYTRQNLATSIEEIKGYTRCFAYANERQMPDEFHINYVDRCICENSGEKRVQVFDRVVLEEIHKDHKRLYNECIPFLEKYISKLINCSIIVVSQQPTAPMKKTLLKQLIEQYGENYKMTLNILHLDGSIKHSDVGLDNPTEIRDLSQDEECMNILTLDTKLGKDEESHSMNIYIGSMSTVQLNRELDDAPSVLSHILTKTKQCFVFKINAGENIEKALALAGKLKRTITLPQLD', 594, 'Q01649; D6W023;', 'KD01095', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CIK1', '#Spindle pole body-associated protein CIK1#Chromosome instability and karyogamy protein 1', '-', '-', '855238'),
(1096, 'Q68FB1', 'Biorientation of chromosomes in cell division protein 1', 'GO:0000777', 18256, 'Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000250}.', 'MAESGSGAGSGSSSVGGVSNPTSLAPGDSQLIALIVEQLKSRGQFDGFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNADMNKNQLRNGLRQSVIQSGMLEAGVDRIISQVVDPKLNHIFRPQIEKAIQEYLAAQTKEEPAPPLPPGPPEPQEQEPPGPSQSVS', 169, 'Q68FB1; Q28H68;', 'KD01096', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'bod1', '#Biorientation of chromosomes in cell division protein 1#Biorientation defective protein 1#Protein FAM44B', '-', '-', '493221'),
(1097, 'Q90ZF9', 'Centromere protein H', 'GO:0000777===GO:0051382===SCL', 26800, 'Component of the CENPA-HI complex; a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. Required for the localization of CENPC but not CENPA to the centromere. It however may be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:11500386}.', 'MAGRLSESVGSGPGAEAETAADPDAKRDVLEHLCARTHLKQLVMEFDTACPPDEGCNSGAEVNFIESAKETLEEVGKVKSAFESKALVIKRIQLMDALRKRVKENDGCARLIVETMRDIIKLNWEIIQAHQQARVIRENLNDIRRKRYFLKQAEGEKALRIFTTVRKKKEVVRMKIAEKLKFIHRNVQYERKVTTLVQNILQNIIVGCQINWAKDPSLRAIILQLEKDISIQNLL', 235, 'Q90ZF9;', 'KD01097', 'Gallus gallus (Chicken)', 'CENPH', '#Centromere protein H#CENP-H', '-', '-', '395316');
