INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1385, 'Q7Z460', 'CLIP-associating protein 1', 'GO:0000776===GO:0000777===GO:0043515===GO:0005828===k;s', 169451, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. {ECO:0000269|PubMed:11290329; ECO:0000269|PubMed:12837247; ECO:0000269|PubMed:15631994; ECO:0000269|PubMed:16866869; ECO:0000269|PubMed:16914514; ECO:0000269|PubMed:17543864}.', 'MEPRMESCLAQVLQKDVGKRLQVGQELIDYFSDKQKSADLEHDQTMLDKLVDGLATSWVNSSNYKVVLLGMDILSALVTRLQDRFKAQIGTVLPSLIDRLGDAKDSVREQDQTLLLKIMDQAANPQYVWDRMLGGFKHKNFRTREGICLCLIATLNASGAQTLTLSKIVPHICNLLGDPNSQVRDAAINSLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGNMIQSANDKNFDDEDSVDGNRPSSASSTSSKAPPSSRRNVGMGTTRRLGSSTLGSKSSAAKEGAGAVDEEDFIKAFDDVPVVQIYSSRDLEESINKIREILSDDKHDWEQRVNALKKIRSLLLAGAAEYDNFFQHLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAIMPTIFNLIPNSAKIMATSGVVAVRLIIRHTHIPRLIPVITSNCTSKSVAVRRRCFEFLDLLLQEWQTHSLERHISVLAETIKKGIHDADSEARIEARKCYWGFHSHFSREAEHLYHTLESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTTSRASTVSTKSVSTTGSLQRSRSDIDVNAAASAKSKVSSSSGTTPFSSAAALPPGSYASLGRIRTRRQSSGSATNVASTPDNRGRSRAKVVSQSQRSRSANPAGAGSRSSSPGKLLGSGYGGLTGGSSRGPPVTPSSEKRSKIPRSQGCSRETSPNRIGLARSSRIPRPSMSQGCSRDTSRESSRDTSPARGFPPLDRFGLGQPGRIPGSVNAMRVLSTSTDLEAAVADALKKPVRRRYEPYGMYSDDDANSDASSVCSERSYGSRNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLLGLQNLLKSQRTLSRVELKRLCEIFTRMFADPHSKRVFSMFLETLVDFIIIHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQIVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNTSVGSPSNTIGRTPSRHTSSRTSPLTSPTNCSHGGLSPSRLWGWSADGLAKHPPPFSQPNSIPTAPSHKALRRSYSPSMLDYDTENLNSEEIYSSLRGVTEAIEKFSFRSQEDLNEPIKRDGKKECDIVSRDGGAASPATEGRGGSEVEGGRTALDNKTSLLNTQPPRAFPGPRARDYNPYPYSDAINTYDKTALKEAVFDDDMEQLRDVPIDHSDLVADLLKELSNHNERVEERKGALLELLKITREDSLGVWEEHFKTILLLLLETLGDKDHSIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLASSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVVERIAKESLLQLLVDIIPGLLQGYDNTESSVRKASVFCLVAIYSVIGEDLKPHLAQLTGSKMKLLNLYIKRAQTTNSNSSSSSDVSTHS', 1538, 'Q7Z460; A2RU21; B7ZLX3; F5GWS0; O75118; Q2KHQ9; Q5H9P0; Q8N5B8;Q9BQT5;', 'KD01385', 'Homo sapiens (Human)', 'CLASP1', '#CLIP-associating protein 1#Cytoplasmic linker-associated protein 1#Multiple asters homolog 1#Protein Orbit homolog 1#hOrbit1', '-', 'ENSG00000074054', '-'),
(1386, 'P33895', 'Kinetochore protein NUF2', 'GO:0000778===GO:0031262===GO:0000780===c;k', 52973, 'Acts as 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:12514103}.', 'MSRNQDVFPILDLQELVICLQSCDFALATQENISRPTSDYMVTLYKQIIENFMGISVESLLNSSNQETGDGHLQEENENIYLDTLNVLVLNKICFKFFENIGVQDFNMTDLYKPEAQRTQRLLSAVVNYARFREERMFDCNSFILQMESLLGQLRSKFDDYNLIQQQLKQYEDVDGDNIPDEQELQKLEEQNKELEIQLKKLTKIQETLSIDYNDYKISKQSIFKDLEALSFQIVELESNRDKLIKISNTDMEELSEGIKELNDLLIQRKKTLDDLTAQQKNLQDTVTTFETIISELYDVLRIISSEVQESNRTETELVGLKQNLINNKLKLMNVLETGIMYKLEILQEQLDLQLKNLEKLSQDTKEESRLNDTKLMDLQIKYENEIKPKIDKTDIFIQEELISGKINKLNDEIKQLQKDFEVEVKEIEIEYSLLSGHINKYMNEMLEYMQ', 451, 'P33895; D6W1Z8; Q6B1X5;', 'KD01386', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'NUF2', '#Kinetochore protein NUF2', '-', '-', '854085'),
(1387, 'Q95QJ7', 'G-protein regulator 1', 'GO:0005818', 60128, 'Complex of gpr-1 and gpr-2; in association with lin-5; activates G-protein signaling to affect mitotic spindle force. Polarity determinants (par genes) may regulate lin-5/gpr-1/gpr- 2/goa-1 locally to create the asymmetric forces that drive spindle movement. {ECO:0000269|PubMed:12730122}.', 'MDVSYYDGPKDEVAEAMLKSAVTAMRLGQYEDGKGRLEEIMEFGTSNFQLLGTIYMYYGRVCRHLNHDAKALEFFEHELNMFKLIFNYPEACDSTRRIVEQALKMGKFPKARRFAEDLIDYTSNKKNGEKYIGQARILFASVCLEGCERDVESNQDEKKKLLSICAEQIAAVKLFNENNTEGAVSETKIMLLEAKCLSLDEKYEESRRKYQECIDFAIKTDQFEAVHIAYYDKALYAETDLLFFIIRDLRSALFYATKFGKERDVVKYKSKLSEEMLRNGEFHEAYLYGLEALVSIRKLGLNEYIGDVLLTIAKCLIALGKRRQAAYFIILGSVLTINQNSFKLFYEQIDVAMNQERSETATDQDVCLAIDSSPDPTSSNDMINKFVVELEHATNVETWEMIVNGIIDDQKKPVAIEKKENEEPVDMMDLIFSMSSRMDDQRTELPAARFIPPRPVSSASKKTTKSHRILPGLRANWTKVQSMKFDGHTMNRILKRSKKSKSSLDSTNSMQGDDTRSDDVTMTSK', 525, 'Q95QJ7; P34408;', 'KD01387', 'Caenorhabditis elegans', 'gpr-1', '#G-protein regulator 1', '-', '-', '176210'),
(1388, 'Q8N554', 'Zinc finger protein 276', 'k', 67219, 'May be involved in transcriptional regulation.', 'MKRDRLGRFLSPGSSRQCGASDGGGGVSRTRGRPSLSGGPRVDGATARRAWGPVGSCGDAGEDGADEAGAGRALAMGHCRLCHGKFSSRSLRSISERAPGASMERPSAEERVLVRDFQRLLGVAVRQDPTLSPFVCKSCHAQFYQCHSLLKSFLQRVNASPAGRRKPCAKVGAQPPTGAEEGACLVDLITSSPQCLHGLVGWVHGHAASCGALPHLQRTLSSEYCGVIQVVWGCDQGHDYTMDTSSSCKAFLLDSALAVKWPWDKETAPRLPQHRGWNPGDAPQTSQGRGTGTPVGAETKTLPSTDVAQPPSDSDAVGPRSGFPPQPSLPLCRAPGQLGEKQLPSSTSDDRVKDEFSDLSEGDVLSEDENDKKQNAQSSDESFEPYPERKVSGKKSESKEAKKSEEPRIRKKPGPKPGWKKKLRCEREELPTIYKCPYQGCTAVYRGADGMKKHIKEHHEEVRERPCPHPGCNKVFMIDRYLQRHVKLIHTEVRNYICDECGQTFKQRKHLLVHQMRHSGAKPLQCEVCGFQCRQRASLKYHMTKHKAETELDFACDQCGRRFEKAHNLNVHMSMVHPLTQTQDKALPLEAEPPPGPPSPSVTTEGQAVKPEPT', 614, 'Q8N554; Q0VGA1; Q2TBE8; Q3B7H7;', 'KD01388', 'Homo sapiens (Human)', 'ZNF276', '#Zinc finger protein 276#Zfp-276#Zinc finger protein 477', '-', 'ENSG00000158805', '-'),
(1389, 'Q6FIT7', 'Probable kinetochore protein SPC25', 'GO:0000777', 27923, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MENNGKSRGTQLVGQIDDLTRELQDAQKVVVSRINERNRLVSDMMERYRSNLRILQEQRVTVLSELDRYKEEESRMKEALQNLNSTKEEFKREMDAYQLKAEKMRLQKQQLQKQLDDLNKMFADRANEIQKYKEMVTRQRQLDSPEIKLYEKLLGLQIDKADTHMLKFTFTDFGREREYKSVIVDVSQLNDDSSPLRIKEIESGVSASTVNELETVLNQQGIVQFLIEVRKVLVKSE', 237, 'Q6FIT7;', 'KD01389', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'SPC25', '#Probable kinetochore protein SPC25', '-', '-', '2891252'),
(1390, 'O60016', 'Histone-lysine N-methyltransferase; H3 lysine-9 specific', 'GO:0051315===k', 55918, 'Histone methyltransferase. Catalytic 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. {ECO:0000269|PubMed:16024659; ECO:0000269|PubMed:8138176}.', 'MSPKQEEYEVERIVDEKLDRNGAVKLYRIRWLNYSSRSDTWEPPENLSGCSAVLAEWKRRKRRLKGSNSDSDSPHHASNPHPNSRQKHQHQTSKSVPRSQRFSRELNVKKENKKVFSSQTTKRQSRKQSTALTTNDTSIILDDSLHTNSKKLGKTRNEVKEESQKRELVSNSIKEATSPKTSSILTKPRNPSKLDSYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRLTQGVIPPDPNFQSGCNCSSLGGCDLNNPSRCECLDDLDEPTHFAYDAQGRVRADTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFAPAGTFITCYLGEVITSAEAAKRDKNYDDDGITYLFDLDMFDDASEYTVDAQNYGDVSRFFNHSCSPNIAIYSAVRNHGFRTIYDLAFFAIKDIQPLEELTFDYAGAKDFSPVQSQKSQQNRISKLRRQCKCGSANCRGWLFG', 490, 'O60016; O74565;', 'KD01390', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'clr4', '#Histone-lysine N-methyltransferase; H3 lysine-9 specific#2.1.1.43#Cryptic loci regulator 4#Histone H3-K9 methyltransferase#H3-K9-HMTase#Lysine N-methyltransferase 1', '-', '-', '2540825'),
(1391, 'A6QQR4', 'DNA excision repair protein ERCC-6-like', 'GO:0000777', 140510, 'DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase (By similarity). {ECO:0000250}.', 'MEVSRGFAEAGALSPEQAASYLRYVKEAKEATKNGDLEQALKLFNLAKDIFPNEKVMSRIQKIQEALEELAEHGDDEFIDVCNSGLLLYQELHNQLYEYQKEGIAFLYSLYRDGRRGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTSLISTWLREFVKWTPGMRVKTFHGPSKDERTRNLCRIQQRNGVIITTYQMLINNWQQLSSLNGQEFLWDYVILDEAHKIKSSSTKSAICARAIPASNRILLTGTPIQNNLQELWSLFDFACQGSLLGTLRTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPYFLRRTKEEVQKKKSSNPEVQLSEKSPDVGAICEMPSLSRKNDLIIWIRLVPLQEEIYRKFVSLDHIKELLMETRSPLAELGVLKKLCDHPRLLSARACGLLNLGAAKFSVQDEIEGEDSSDVDHIDQISDDTLMEESGKMLFLMDLLKKLRDEGHQTLVFSQSRRILNIIERLLKNRHFKILRIDGTITHLVEREKRISLFQQNKDYSVFLLTTQVGGVGLTLTAASRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFKDSLIRQTTGDKKNPFRYFSKQELRELFTIEDFQNSATQLQLQSLHAAQRRSDKNLDEHIAFLHSLRIAGISDHDLMYTRDLSVKEELDVIEDSHYIQQRVQKAQFLVESESQNTELLMERQKMGNEGIWLREPVYQTKKKRPKVNKPQPQPSSHLPVYHTQEEISSLMASIIIDDLPKEDEKDLSRIKLNDTIPQDGRHPCVITLNDDFVTTLPKGCGDVEEIFPDSLSGMALQKEASQEGFMQESEQESPLASFNYLPSKSARVDLGPNLDQLEDDEVLHHCNPSPANPKTKEYQRPESNVSVIKIADDDLTAAHSALQDAQANEAKLEEEPLASSGQYACDFNLFLEDSADNGQNLSSQFLEHVEKENSLCGSAANSRAESVHSKACLSVDLSEEDDEPEEVVNVKIRRKARRIDSDNEDEHTFKDTSSTNPFNTSPFPFLSVKQFDASTPKNDISLPERFFSPKISDSINKSVNSRRSLASRRSLINVVLDHVEDMEERLDNSSEAKVVEDHLEEGAEESGDEAPEHTKEDPSRETLSSENKSSQLSTSKPGALAQETSPGDPEPLSDGQLVDSPQDEAMEAVNDYDTLVLHGKELKECGKIQEALDCLVKALDIKSSDPEVMLMTLSLYKQLNKT', 1242, 'A6QQR4; Q0V8L7;', 'KD01391', 'Bos taurus (Bovine)', 'ERCC6L', '#DNA excision repair protein ERCC-6-like#3.6.4.12#ATP-dependent helicase ERCC6-like', '-', '-', '782916'),
(1392, 'Q9DBR7', 'Protein phosphatase 1 regulatory subunit 12A', 'GO:0000776', 114996, 'Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex; involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN- dependent suppression of HIF1A activity (By similarity). {ECO:0000250}.', 'MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERVMLRDARQWLNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEELQKKQTLLHSEKRDKKSPLIESTANMENNQPQKAFKNKETLIIEPEKNASRIESLEHEKADEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPMASVSNAHTSSTQAAPAAVTAPTLSSNQGTPTSPVKKFPISTTKISPKEEERKDESPASWRLGLRKTGSYGALAEISASKEAQKEKDTAGVMRSASSPRLSSSLDNKEKEKDNKGTRLAYVTPTIPRRLASTSDIEEKENRESSSLRTSSSYTRRKWEDDLKKNSSINEGSTYHRSCSFGRRQDDLISCSVPSTTSTPTVTSAAGLQRSLPSSTSTAAKTPPGSSSAGTQSSTSNRLWAEDSTEKEKDSAPTAVTIPVAPTVVNAAAPSTTTLTTTTAGTVSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESEASREDEYKQKYSRTYDETYTRYRPVSTSSSSAPSSSSLSTLGSTLYASSQLNRPNSLVGITSAYSRGLAKENEREGEKKEEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQERQSDTEDGSSKRETQTDSVSRYDSSSTSSSDRYDSLLGRSASYSYLEDRKPYSSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSQLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK', 1029, 'Q9DBR7; Q05A74; Q8CBV2; Q99NB6;', 'KD01392', 'Mus musculus (Mouse)', 'Ppp1r12a', '#Protein phosphatase 1 regulatory subunit 12A#Myosin phosphatase-targeting subunit 1#Myosin phosphatase target subunit 1', '-', '-', '17931'),
(1393, 'Q9VRQ2', 'Mad2RE72064p', 'k', 23405, '', 'MSTAQATKNCITLKGSAQIIVEYLKYGINSILFQRGIYPAEDFNNTQQYGLTILMSKDPKIKTFLQNVLSQTEEWLSKNMINKISMVITNAHTKEVLECWDFNMQAELGDGDISDPTKATTTKELSRIQNEIRDVMRQISATVSYLPLLDCICTFDIMIHTLQNTELPAKWDETGAIVIQNPQAVQLRSFSTGLHKVDTVVNYKMST', 207, 'Q9VRQ2;', 'KD01393', 'Drosophila melanogaster (Fruit fly)', 'mad2', '#Mad2 {ECO:0000313|EMBL:AAF50740.1}#RE72064p {ECO:0000313|EMBL:AAL48090.1}', '-', '-', '38656'),
(1394, 'P82266', 'Probable 125 kDa kinesin-related protein', 'GO:0003777', 113683, 'Responsible for microtubule translocation. May be important for the organization of phragmoplast-specific arrays of microtubules (By similarity). {ECO:0000250}.', 'MSSRHDKEKGVNVQVLLRCRPFSDDELRSNAPQVLTCNDLQREVAVSQNIAGKHIDRVFTFDKVFGPSAQQKDLYDQAVVPIVNEVLEGFNCTIFAYGQTGTGKTYTMEGECRRSKSAPCGGLPAEAGVIPRAVKQIFDTLEGQQAEYSVKVTFLELYNEEITDLLAPEDLSRVAAEEKQKKPLPLMEDGKGGVLVRGLEEEIVTSANEIFTLLERGSSKRRTAETFLNKQSSRSHSLFSITIHIKEATPEGEELIKCGKLNLVDLAGSENISRSGARDGRAREAGEINKSLLTLGRVISALVEHLGHVPYRDSKLTRLLRDSLGGRTKTCIIATVSPAVHCLEETLSTLDYAHRAKNIRNKPEVNQKMMKSTLIKDLYGEIERLKAEVYASREKNGVYMPKERYYQEESERKVMAEQIEQMGGQIENYQKQLEELQDKYVGQVRECSDLTTKLDITEKNLSQTCKVLASTNEELKKSQYAMKEKDFIISEQKKSENVLVQQACILQSNLEKATKDNSSLHQKIGREDKLSADNRKVVDNYQVELSEQISNLFNRVASCLSQQNVHLQGVNKLSQSRLEAHNKAILEMKKKVKASRDLYSSHLEAVQNVVRLHKANANACLEEVSALTTSSACSIDEFLASGDETTSSLFDELQSALSSHQGEMALFARELRQRFHTTMEQTQEMSEYTSTFFQKLMEESKNAETRAAEANDSQINSIIDFQKTYEAQSKSDTDKLIADLTNLVSSHIRRQHELVDSRLHNFKDAVSSNKTFLDEHVSAVNNLTKDAKRKWETFSMQAENEAREGADFSAAKHCRMELLLQQSVGHAESAFKHCKITHESLKEMTSKQVTDVSSLVRSACDSNEQHDAEVDSARTAAEKDVTKNSDDIIQQIERMSEDEKASVSKILENVRSHEKTLESFQQDQCCQARCIEDKAQETFQQQYMEYEPTGATPTKNEPEIPTKATIESLRAMPIETLVEEFRENNSYESFATKETKPQQLTRSPLSQVN', 1009, 'P82266;', 'KD01394', 'Arabidopsis thaliana (Mouse-ear cress)', 'At2g36200', '#Probable 125 kDa kinesin-related protein', '-', '-', '818192'),
(1395, 'Q9NQS7', 'Inner centromere protein', 'GO:0000776===GO:0000777===k;m;s', 105429, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Probably acts through association with AURKB or AURKC. Seems to bind directly to microtubules. Controls the kinetochore localization of BUB1. {ECO:0000269|PubMed:12925766; ECO:0000269|PubMed:15316025; ECO:0000269|PubMed:16760428}.', 'MGTTAPGPIHLLELCDQKLMEFLCNMDNKDLVWLEEIQEEAERMFTREFSKEPELMPKTPSQKNRRKKRRISYVQDENRDPIRRRLSRRKSRSSQLSSRRLRSKDSVEKLATVVGENGSVLRRVTRAAAAAAAATMALAAPSSPTPESPTMLTKKPEDNHTQCQLVPVVEIGISERQNAEQHVTQLMSTEPLPRTLSPTPASATAPTSQGIPTSDEESTPKKSKARILESITVSSLMATPQDPKGQGVGTGRSASKLRIAQVSPGPRDSPAFPDSPWRERVLAPILPDNFSTPTGSRTDSQSVRHSPIAPSSPSPQVLAQKYSLVAKQESVVRRASRRLAKKTAEEPAASGRIICHSYLERLLNVEVPQKVGSEQKEPPEEAEPVAAAEPEVPENNGNNSWPHNDTEIANSTPNPKPAASSPETPSAGQQEAKTDQADGPREPPQSARRKRSYKQAVSELDEEQHLEDEELQPPRSKTPSSPCPASKVVRPLRTFLHTVQRNQMLMTPTSAPRSVMKSFIKRNTPLRMDPKCSFVEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGASKALNVTVDVQSPACTSYQMTPQGHRAPPKINPDNYGMDLNSDDSTDDEAHPRKPIPTWARGTPLSQAIIHQYYHPPNLLELFGTILPLDLEDIFKKSKPRYHKRTSSAVWNSPPLQGARVPSSLAYSLKKH', 918, 'Q9NQS7; A8MQD2; Q5Y192;', 'KD01395', 'Homo sapiens (Human)', 'INCENP', '#Inner centromere protein', '-', 'ENSG00000149503', '-'),
(1396, 'Q9Z0Y1', 'Dynactin subunit 3', 'GO:0000777', 20978, 'Together with dynein may be involved in spindle assembly and cytokinesis. {ECO:0000250|UniProtKB:O75935}.', 'MAALTDVQRLQSRVEELERWVYGPGGTRGSRKVADGLVKVQVALGNIASKRERVKILYKKIEDLIKYLDPEYIDRIAIPEASKLQFILAEEQFILSQVALLEQVNALVPVLDSASIKAVPEHAARLQRLAQIHIQQQDQCVAITEESKALLEGYNKTTMLLSKQFVQWDELLCQLEAAKQVKPAEE', 186, 'Q9Z0Y1; Q9CR43; Q9D039;', 'KD01396', 'Mus musculus (Mouse)', 'Dctn3', '#Dynactin subunit 3#Dynactin light chain p24', '-', '-', '53598'),
(1397, 'P0C664', 'Protein zwilch homolog', 'GO:0000777', 72283, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. {ECO:0000250}.', 'MSIKLEDLHSFNEAVLFKGEEDEAPAPVLLLDKYRVRLVPITELPLVSNYSNTSQLGLNSEEVLVIDSPIESAEKQKTSSLLNRRENKKTIKSEKEDESMDMETAEGDKENTVSETGGGPLVTSFLTLDKLEKDGVNDVEIVGLDCEIQFFDANPIPFEDGISLQRFLRLESSKNFSAAVDKLPIWISTIGHHFPSVCWLAAGRTNKNVQVSGATRILGYFNENSQKLVKQLNEACGAAQVNRYRAVYDVIRKIATPTREAPGEVIIDMRWNTKSSLVLLEQPDNAADCTIKIDLGWGDNRFFIDETIFEQLFFVLNLADVLANPEKEVVFRSESDKFDDLVQEMKQLVEACSHEDNVFASNEKSEQVTDKVWNIVRKCSDVKQATMLFKNFLQALTYGKIKSHVQEGNKSHLASLIRASKTCDFRMPILERLSTIEMMMEIGVESLRGRIINKFSDTLQFPSDELTFILKTCENDLSTLEGTLHSSVVSLLPITMAMATIHQIFGFLNVKDLVVLPDLARRVLTKYTTGMVEKAKRGETETDYVFETTLPLLRMNKEAFMHKRPRIWTCENTNTVGANVQTRAMTTLELEPSLEHVCRLVNASRPVRPIDEDNRKPTEEERNADYTVSHTIFSYLPKL', 639, 'P0C664; A8WVW7;', 'KD01397', 'Caenorhabditis briggsae', 'zwl-1', '#Protein zwilch homolog', '-', '-', '8581386'),
(1398, 'P53298', 'Central kinetochore subunit OKP1', 'GO:0000778===GO:0008608===GO:0000817===k', 47349, '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.', 'MAADRDNFLQNIENDSINNGQAMDLSPNRSSSESDSSILMNVNDIKTLRLDVAPEAKSTQSKKSLFYENSDDAEEGEIEERTNKEEGQYHHKGSKQLRFEVGKESTGKLQSHLSDGSATSGEGNVRPWEFRKVIQAEYRERLPRNYELKHWKKPSKIMIGSILRLLETNTVSALDSVFEKYEKEMNQMTHGDNNEVKRIYSKKERLLEIILTKIKKKLRQAKFPSRISERDLDIEYIYSKRQFIQNRYSQELQNNERLEAILSREQNLLEETRKLCMNLKTNNKKRLTEKLIQKDLHPVLNKAMEYTYGLESTNGFMHPDGPVTFRNDSHELNLMLNDPIKSTADVRLDKEEVLSLLPSLKEYTKKSKELKETMGQMISDSHEEEIKEVFVPHHESHQDKTEEDIH', 406, 'P53298; D6VUW3;', 'KD01398', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'OKP1', '#Central kinetochore subunit OKP1#Outer kinetochore protein 1', '-', '-', '853090'),
(1399, 'Q09750', 'Paired amphipathic helix protein pst1', 'k', 171456, 'Has a role in modulating the nuclear import of TF1 virus-like particles. Essential for viability.', 'MAKDWQDARLGQCHRLEDYSNVAINYTGPYLTPSGTMAYHPGNAPLFTQAPPHTNPQGPPPFPLFNSISPVYDPATGRLLYRNVNTQVSHTAIPNPANGYAAVYGGPPSQLPPPPQPQSHPNVTVISASPARAIEQQPTILSSTDSNIPRPGTVKSSASPFVPNQNPSAPPPPPQEYRQLNVTDALSYLDLVKLQFHQEPEIYNEFLDIMKEFKSQAIETPEVITRVSKLFAGYPNLIQGFNTFLPPGYSIEISSADPGSLAGIHITTPQGPLMINDLGKTTAPPPPHGSTTPLPAAASYTSMNMKQSSASHPVLQPPAPSTLQFNPSPSPAAPSYPPVDASVKQAADLDQAINFVNNVKNRFSHKPEAYNSFLDILKSYQHDQRPIQLVYFQVSQLFAEAPDLLEEFKRFLPDVSVNAPAETQDKSTVVPQESATATPKRSPSATPTSALPPIGKFAPPTTAKAQPAPEKRRGEPAVQTRNHSKRTRTATSSVEETTPRAFNVPIAQNKNPSELEFLEHARQYLANESKYNEFIKLLELYSQEVFDKNALVERCYVFFGSNEHLMNWLKDLVKYNPANPIPVPRPRVDLTQCKSCGPSYRLLPKIELLLPCSGRDDLCWTILNDAWVSFPTLASEDSGFIAHRKNQFEENLHKLEEERYEYDRHIGANMRFIELLQIHADKMLKMSEVEKANWTLPSNLGGKSVSIYHKVIKKVYGKEHAQQIIENLQKNPSVTIPIVLERLKKKDREWRSLQNHWNELWHDIEEKNFYRSLDHQGVSFKSVDKKSTTPKFLISELRNLAQQQKVELSEGKVTPSHQFLFSYKDPNIITDIARLFGVFLIHGSTHSAEDNEKMSNFLRSFLSLFFDVPYDSFIPYLPTHFNEEESDIDSLSSSLIEKPRASSSPIHHANNNGLRLLKDVLKKTYRGARENRSSVKEDYVSESTERTPDASEIDEHISEHEENDDESSSVFSTGEVWVNCKFTDTDGSLLDDGTKLSDRSVYNLFGNMSLYCFFRLFHTLYSRLEEIKNLEQMAYSKQHDVKSNPVAVELGLVRHPSERLGFALPTADTVYEQAIQLCERLMEGEIDQNGFEDALRCLYGIHAFRLYTVEKLVTSIIKQLHSVTTNRRLAQVFMYYEKDRVQRRTSPRQQIMYRIQTETAFGPDENLCCIDWNSQTRQSAIRLMGREDLTMGTLKSDAEKWCYYIGSYIMSSPTEGILPEHVRIPFLRKCLPSDEGNEDDESSSVVKSANAIITSFLESGLALTIPINTVKIRYENGTEDVFARNSEQVYNGPYDKIRDYRQSKWREWLNSDEGWTQGLSKDKVRRIKPCTIESLFNESTLRSGKAERFSENAGVESIGKKGKNLLNESGNGKKLDKGLPPKVNGKSSVTRGNKTNLKARNGRNNDDSSNKINLSEKEKEKESIEDEEKNREGSMSPVAKHASDVEDDHDVAKSTAPDFETSSHRPERSSEKKSPSPVFTSVKQTAENDADNEDDKTDMDDQTEETLDADNTMEEEPSKDDL', 1522, 'Q09750;', 'KD01399', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'pst1', '#Paired amphipathic helix protein pst1#SIN3 homolog 1', '-', '-', '2540018'),
(1400, 'Q5APC8', 'DASH complex subunit DAM1', 'GO:0008608===GO:0042729', 31906, '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}.', 'MSSSKPVTPRNDRRQNSGRRHSHRSSGIQLPSMSPKVHHYPIDAENLPMDSPEIVEKFASLAESMETLDLHMHDLCHIHDHISNQFNESFASFLYGLSMTMWCVDFPGCPSREQWEALISKRERKERIEVLKKRLADAQKLNDRLKLRLSDEAKQKPQQLTSQQRPTHGPTRQIKQQPRSVNFNTHSSDSISTNSYTSGDFNTNRRVSRIPQPSRSNLPSSRFQAPSKSGPNLNQPPRYMRGLFDGNNTLNTSNYSRIKKPIHNRSVNNLQNRPPFR', 277, 'Q5APC8;', 'KD01400', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'DAM1', '#DASH complex subunit DAM1#Outer kinetochore protein DAM1', '-', '-', '3634820'),
(1401, 'Q9P3W4', 'Dynein intermediate light chain dil1', 'GO:0005868', 41078, 'Component of the cytoplasmic dynein which acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). Promotes oscillatory nuclear movement and efficient pairing of homologous centromeres during meiotic prophase. {ECO:0000250; ECO:0000269|PubMed:20404563}.', 'MDELLEKLLNDLKKKEPKACSIICIGEDLDIIQCMNEHGCFSGGSYSELSNDCETVNFRGIAYKCFFTKDQVKVNFWQISHLTGGLFNFLVSQALNEHGLDLLWIIMVVAQTLSALVSFPEKLLNILRNMKTILINTEETVRNRFEESQNKKLVALLDKNSTTLDISSGILLNFTVVLKQLKHALGLHTSVDNSQEFILQFLRTTLLSVPTSSIVSISADPTSWNNLNVLMKYNFMFQKFKPRDFHAQTIQSETMFIPPCWDTISKIQSVNHEFNIALFKQTAKNFYDTLDISLLLGLFDKSISMLNCHSSKISDGDIPYKSHQVFLQELQNKYSEIKTYSSNKLNKSSIKSSLWKDLIQ', 360, 'Q9P3W4;', 'KD01401', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dil1', '#Dynein intermediate light chain dil1', '-', '-', '2543586'),
(1402, 'Q8RVQ9', 'Histone H3-like centromeric protein HTR12', 'GO:0000777===k', 19709, '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}.', 'MARTKHRVTRSQPRNQTDAAGASSSQAAGPTTTPTRRGGEGGDNTQQTNPTTSPATGTRRGAKRSRQAMPRGSQKKSYRYRPGTVALKEIRHFQKQTNLLIPAASFIREVRSITHMLAPPQINRWTAEALVALQEAAEDYLVGLFSDSMLCAIHARRVTLMRKDFELARRLGGKGRPW', 178, 'Q8RVQ9; Q8LCW8; Q9LNI6;', 'KD01402', 'Arabidopsis thaliana (Mouse-ear cress)', 'HTR12', '#Histone H3-like centromeric protein HTR12#Centromeric histone CENH3', '-', '-', '839104'),
(1403, 'Q3T140', 'Dynein light chain roadblock-type 1', 'GO:0005868', 10990, '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 (By similarity). {ECO:0000250}.', 'MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYANLMHNFILKARSTVREIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE', 96, 'Q3T140;', 'KD01403', 'Bos taurus (Bovine)', 'DYNLRB1', '#Dynein light chain roadblock-type 1#Dynein light chain 2A; cytoplasmic', '-', '-', '513342'),
(1404, 'P30260', 'Cell division cycle protein 27 homolog', 'c;k;s', 91867, 'Component of the anaphase promoting complex/cyclosome (APC/C); a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of ''Lys-11''-linked polyubiquitin chains and; to a lower extent; the formation of ''Lys-48''- and ''Lys-63''-linked polyubiquitin chains. {ECO:0000269|PubMed:18485873}.', 'MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDIVTEFGDSACFTLSLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKFTSLQNFSNCLPNSCTTQVPNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSAVISPDTVPLGTGTSILSKQVQNKPKTGRSLLGGPAALSPLTPSFGILPLETPSPGDGSYLQNYTNTPPVIDVPSTGAPSKKSVARIGQTGTKSVFSQSGNSREVTPILAQTQSSGPQTSTTPQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSKTNKGGITQPNINDSLEITKLDSSIISEGKISTITPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYNTGWVLCQIGRAYFELSEYMQAERIFSEVRRIENYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQESSMTDADDTQLHAAESDEF', 824, 'P30260; G3V1C4; Q16349; Q96F35;', 'KD01404', 'Homo sapiens (Human)', 'CDC27', '#Cell division cycle protein 27 homolog#Anaphase-promoting complex subunit 3#APC3#CDC27 homolog#CDC27Hs#H-NUC', 'BIOMD0000000186,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Dissociation variant;BIOMD0000000187,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Convey variant;', 'ENSG00000004897', '-'),
(1405, 'Q9NQT8', 'Kinesin-like protein KIF13B', 'GO:0003777', 202789, 'Involved in reorganization of the cortical cytoskeleton. Regulates axon formation by promoting the formation of extra axons. May be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes. {ECO:0000269|PubMed:20194617}.', 'MGDSKVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNPVNTNLSKGDARGQPKVFAYDHCFWSMDESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNEDPNARIIRDLREEVEKLREQLTKAEAMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVGDDKCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKKKAEREDEDQDPSMKNENSSEQLDVDGDSSSEVSSEVNFNYEYAQMEVTMKALGSNDPMQSILNSLEQQHEEEKRSALERQRLMYEHELEQLRRRLSPEKQNCRSMDRFSFHSPSAQQRLRQWAEEREATLNNSLMRLREQIVKANLLVREANYIAEELDKRTEYKVTLQIPASSLDANRKRGSLLSEPAIQVRRKGKGKQIWSLEKLDNRLLDMRDLYQEWKECEEDNPVIRSYFKRADPFYDEQENHSLIGVANVFLESLFYDVKLQYAVPIINQKGEVAGRLHVEVMRLSGDVGERIAGGDEVAEVSFEKETQENKLVCMVKILQATGLPQHLSHFVFCKYSFWDQQEPVIVAPEVDTSSSSVSKEPHCMVVFDHCNEFSVNITEDFIEHLSEGALAIEVYGHKINDPRKNPALWDLGIIQAKTRSLRDRWSEVTRKLEFWVQILEQNENGEYCPVEVISAKDVPTGGIFQLRQGQSRRVQVEVKSVQESGTLPLMEECILSVGIGCVKVRPLRAPRTHETFHEEEEDMDSYQDRDLERLRRKWLNALTKRQEYLDQQLQKLVSKRDKTEDDADREAQLLEMRLTLTEERNAVMVPSAGSGIPGAPAEWTPVPGMETHIPVIFLDLNADDFSSQDNLDDPEAGGWDATLTGEEEEEFFELQIVKQHDGEVKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQLSHPADMQLVLRKRICVNVHGRQGFAQSLLKKMSHRSSIPGCGVTFEIVSNIPEDAQGVEEREALARMAANVENPASADSEAYIEKYLRSVLAVENLLTLDRLRQEVAVKEQLTGKGKLSRRSISSPNVNRLSGSRQDLIPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGPVRRRSTGLRLGAPEARRSATLSGSATNLASLTAALAKADRSHKNPENRKSWAS', 1826, 'Q9NQT8; B4DGY5; B5MC45; F8VPJ2; O75134; Q9BYJ6;', 'KD01405', 'Homo sapiens (Human)', 'KIF13B', '#Kinesin-like protein KIF13B#Kinesin-like protein GAKIN', '-', 'ENSG00000197892', '-'),
(1406, 'P87314', 'Protein hir1', 'k', 103686, 'Probably required for replication-independent chromatin assembly. Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. Repressor of histone gene transcription in G1 arrested cells. Required for repression of htb1 gene expression outside of S phase. {ECO:0000269|PubMed:15121850; ECO:0000269|PubMed:16428807}.', 'MKIKKIPWLGHFDDRGHRLSIFSIHIHPDGSRIATGGLDGTIRIWSTEAINRENENENENEDLPKQLCCMSTHTGTVTSVRFSPNGQYLASGSDDRVVIIWHKEEAIPGLGSTFGSGEKHTENWRSYRRLLGHDNDIQDLCWSYDSQLVVSVGLDSSIIVWNGTTFERLKRIEAHQSHVKGITFDPAGKYFATESDDRTIKVWRVSDFSIEKTITGPFNNSPLSTYFRRPSWSPDGKHIAAPNAMNGPVSCVSIIERGTWTSEINLIGHEGPVEVTAFNPKLFRDKNDKLVCILACGGQDRSLSIWSSALPRPLLSCQNVFQKSIGDVCWSPDGLSLFLCSYDGNVLVCTFEKEEFGDMVSDEEISKALAKYGHGRHGIVLPESAKQLELEETAYAILKKPSSLSTTDPTLVPQSSSTPKSAQKTPQKLPAFLPNRLTAETVDTNKLTASKEQIASPKRPGPSDNGNEIPTKFVQKVTITKEGKKRVAPQLLTTLSATPSTSRLASTQLQHTGSSQLPPQQFSQPINSLPKGGVPILIVGNKTKVNHENDESDQALQEEKIEEGLLKNYYSSLIDSSTSISNINFEAPRYKTNIVHSLNNEQKYVLEVKNGTSEKNPTRIVALENGNTKWMDYLPRPVILVTGSIHFWSIACDDGSLHLYSLTGSRLLPPIMIESKASFLHCNNAYLLCISSSGMVYAWNVVNKTALFTANSLAPILSRVSNNVTIENNSTDIPHVVIASISKEGVPSVTLSTGETYVYSSTMLCWQRITEPWWAIGSREWDSSGLLQSNTQTESQPLKIYEHRTNNVLMDSGRGKLLQKMVADAITEEGYDDFETIVTINHLENKIASARLLKLDDEFLVTSEVYVRLLMHHGLWQKLEEFLGELRTQTKCSIKLSGREVVAKMLVVLRQAVQTDNEFDRANKLIEKYAST', 932, 'P87314; Q9US78;', 'KD01406', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hip1', '#Protein hir1#Histone transcription regulator 1 homolog', '-', '-', '2540219'),
(1407, 'Q753W9', 'Probable kinetochore protein SPC24', 'GO:0000778===GO:0031262', 22966, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MPSQAPGPDVLENPADLLRQTRENFSIAHDLQLLNATEENLRRLMQRTQQLEAKGAQELSELQAQQTERAQAAEAMRAEKETQAQHLQALTHSQDLVRLANELEELEQQLVSLRAELDEGMTQLLQTSEPTAAFQGDAEHEQQSPEVQTNLLKLQLYSSLGVTLDTEHNQALIERGDAAGIDLIALEDDSLSPFFRTKYVWDRL', 204, 'Q753W9;', 'KD01407', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'SPC24', '#Probable kinetochore protein SPC24', '-', '-', '4622011'),
(1408, 'Q753W8', 'DASH complex subunit HSK3', 'GO:0008608===GO:0051987===GO:0042729', 7971, '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}.', 'MDQTKRRHYSQLSQQLQLLQKNLEATTQHVETMSVQCNEHLVNKLGKIQASWFIGGNRCFEQELLGKR', 68, 'Q753W8;', 'KD01408', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'HSK3', '#DASH complex subunit HSK3#Outer kinetochore protein HSK3', '-', '-', '4622012'),
(1409, 'Q27171', 'Dynein heavy chain; cytoplasmic', 'GO:0003777', 528637, '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.', 'MEESETQLNVKVQEQGKLYSANEIENFNQYLSAICLSLLIIDKDQWNVACHEDVNQQNICQFLSDSQIKALIVSKTVENEKFNIQIRSEYEASNNYAHTICFLKRHTFQYDNQLQPQQFSNHVQVINVGYAESQGGANPFTLSHNYVQNCFIPIFTQYKGEIDKKRIVDQSSYNDLIKKLNEVNLAFIKCRQNVEVPEIILQFDPRIKEAVKQRGGKPTIEDAAQLNKPDIVQSISQTVTRWISDINQISNTKLELTNASIVDEINYWMSMERSLFFIENQLKQPEVDFTIEVLTQAKKMNITAQFKEIALKQSLQKCQSCNQFMKEFPINNLLIATNLVEIKDAMIQIFQHMKKLSNIQETYTIPRSLQLAESFSRELTNEMIKYFKGFQILHIKYVDFKGLIIKTQEIFSQWDEEYKIFKQSIVKKSVHQKDQYGQFEHIKLQKQIQHIQRLREMHENLKEVIEQIIQNDQEEQKENVQQFATLQEIQQAYDIFKNVEVFDLSRDGEDQFFRALKQYEIAIESVEATITTNLRDSLGSASSAKEMFRILAKFNKLFSRPRIKGAIQEYQSQLLKTVHKDIQSLQNKFKETYQKSQNSRLASARDIPLTSGFVIWSKQLQIRLQKYMQKVEQILGPQWAEDTDGKKCKEMGETFERILDSGPALEDWKQEINHHNKAVSQNEKLFEVVTRRRGLEIRVNYEKKLSQLFKEVRNLSNMKTKVPYSISHIANDAKASYPFALSLQESLHTYIQITSQLNAKSAKLVAALRKEVQLQIGQGFNYLWTHKTQLQPYVKKFTDKVFELEQAVNGLNERIGQIESLCEAMKTCPVDSLADKLKDIQEVIDSLCFNNFSNLHIWIQDIDKQIESILCDRVTVQMKEWLNQFINYQKIQERGLVNQTVVHELKLQDQIIYVDPPVEYAKYFWFQEFHKMIGQICSLPRLVANRFDNTIQQNTGPWGTQRDLDYSTTINKINQQLIKDAYSQIGQLLEDMEQYVQTWLNYQSLWELDIKQVEQILQDDIEKWQQMLTDIKQGRATFDNSTTEEHFGAIIIDYRMVQVKINHKYDAWHKELLNHFGNKFGEQLRVFNKNVTTEKEKLLKINFQDLTSDIIESITIIQEQDKKFPGWSADIESFKNGQKVLDRQRYQYPGDWLSFEQVEMQWNQFKQIRSKKLQSQESEMNNIQSKIQQDERYLNQQIQEIEEQWKTSKPDSGDCSPNEAEQILKSLNEQLISVQEKYEKCSQAKEILKMDPPTHQQKLNVLLESISDLQDVWQELGKIWKVMQSIKEQLISALQNKKIKDTCDEAQKQLNGVSTKTRNYDAFEKMKEKVKNYIKMNKLIMDLKDESMKERHWRQLLSKLKINESLNQLQMQHLWNANLLNYENLAKDIMTVARGEQVLETMISQVKDFWNSFELELVKYQTKCKLIRGWDELFQKLDEDLNNLASMKISPFYKTFEAEISQWDDKLQKVKLTMDIWIDVQRRWVYLEGIFFGSSDIKTQLQNEYNKFKDIDSQFTNLMKKVAQKPQLMDVQGIPNLAKTLERLSDFLQKIQKALGDYLETQRQAFARFYFVGDDDLLDIIGNSKDVTNVQRHFPKMYAGIVQLQSRKDGNDDVVLGMSSKEGEVVPFSKEVKIAEDPRINIWLGKVDNEMMNSLALDLEKSVLDIQANQQNRMKVIEEHPAQIILLALQVGWCFSVESSFNNEQQMKQTLQYVLEFLSELAESVLKDHPKQLRQKFEQIITDFVHQRDVIRLLMNNKINSKNDFGWQYHMRFNWNSKEADPGKRLLIQMGNAQFHYGFEYLGVAEKLVQTPLTDKCFLTLTQALHLRMGGSPFGPAGTGKTESVKALGAQLGRFVLVFNCDETFDFNAMGRIFVGLCQVGAWGCFDEFNRLEERMLSACSQQILLIQTGLREKQKQIELMGKDVKLSSQMGVFVTMNPGYAGRSNLPENLKQLFRQMAMVKPDRELIAQVMLFSQGFRTAEKLAGKIVSLFELCDNQLSSQPHYDFGLRALKSVLNSAGNMKRQEMIDRKQEPVPQSEIEEFEQTILLRSVCDTVVPKLIKDDIKLLETLLQGVFPGSCIPEIKEEQLRKELALACQRKNLQSSKNFIEKVLQLYQIQRLQHGLMLVGPCGCGKSAAWRVLLEAMYKCDKVKGEFYIVDPKAISKDELYGRLDNTTLEWTDGVFTSILRKIISNQRQESTRRHWIIFDGDVDPEWAENLNSVLDDNKLLTLPNGERLAIPPNVRMIFEVETLKYATLATVSRCGMVWFSEETINDENIFYHFLERLKQDDYDQQKSEDDNNKQVNSQESELRTKCVKALESIIKFLSQFLQIAQKPEYKHVMEFTRIRVLESTFALVRRSISNIIEYNENNSEVPLEDDQINDFMVKQFLIAVMWGVAGSMNLYQRTQYSKEICQLLPHNVILPQFNDSAPSLIDFEVTLPEAQWSQYKKKVPQIEIDPQRVTDADLIIETVDTLRHKDVLCGWLNEHRPFLLCGPPGSGKTMTLMSTLKALTDFEMIFINFSSSTMPQLIIKQFDHYCEYKKTTNGVFLQPKNQKWLVVFCDEINLPDQDKYGTMAIITFLRQLTEQHGFWRSSDRQWISLDRIQFVGACNPPTDVGRKPLTPRFLRHCPLILVDFPGPESLKQIYGTFNKAMLRRTVNLKQYSEQLTNAMVEFYTKSQQHFTADQQAHYIYSPRELTRWKYALNEALEPLESVEDLVRLWAHEGLRLFQDRLVHEHEKEWCNKLIDQVAYNNFNNLKDEALQRPILFSNYLHKVYQSVDREELRKYIQGRLKQFNEEELSVPLVVFDDVLDHILRIDRVLKQPLGHLLLVGSSGVGKTTLTRFVSWINNLTVFQIKAGRDYQLADFDNDLREVMKRAGAKGEKITFIFDESNVLGPSFLEKMNALLASGEIPGLFENDEYLALINLLKENSNQNKQFDSSEEQLFKNFTYQVQRNLHVVFTMNPKNPDFSNRTASSPALFNRCVIDWFGDWTNEALFQVGKAFTMYIDPPENAFSKKIKDETQRQHILVSTLVYIQNTIIELNNKLQKGAKRFNYITPRDYLDFLKHFEKLHNEKKSQLEDQQLHLNVGLDKLKETEQQVLEMQKSLDQKKVELLTKERQAGEKLQTIIEEKKIAEKKKEDSTRLSSDAEKKAKEMEVRQSQVNKELNEALPALENAKQCVNSIKKDDLNQIRALGSPPALVKLTMEAVVCAINSLEKSPEWKDVQKSMANMNFINNVINFNTETMPPKVKKFILTKYLSAQEWNIDRINFASKAAGPLAMWLDSQLKYADILQKVDPLRQEVAKLLQESDELNTQKKIYDDEVAAAEAKIHNLQQEYSELISQKESIKSEMLKVQEKVTRSQALLSDLSGERVRWEEASQNFKSQLATMIGDVLLLLAIPVLYWVLDHFYRKVVINTWKDYLSGQANIFYRQDLSLIEFLSRPSDRLNWQLHTLPSDDLCMENAIILYRFQRYPLVIDPSGQALSFISSLYKDKKLARTSFTDESFLKTLETCLRFGCPLLVQDVEKVDPILNSVLNNETYKTGGRVLIRVGNQEIDFSQGFTMFMITRDSTARFTPDLCSRVTFVNFTVTQSSLQEQCLNIFLRNESPETEEKRLNLMKLQGEYIVKLRELEDQLLDSLNNSRGSILEDEKVIQTLEKLKKEAAVIVQEMKQADTIMNEVMNTTHSYVPLANTTSKIFFSLTSLANIHYLYQFSLQFFMDTIYNVLNKNEQLQKIPKQDLIKRRILIFNEMFKEIYKRMNFSLLQEDKLVFAITLAQVKLGDNTLGQEFLNVFKPPTVMETTFSNTFLQGKLSIQQLKQLEGITQQNQTFNRLIDNLNKNEDRWLNFLNDEAPENDIPTQWYNEVQRDDIVKLDWIDSHQLKRQLDDLHILRIFRADRFQIIARKLINQILGEGFMDEQTVDMKLVVEKEASNKIPILLCSAPGFDPSFKVEQLSREMGIKLTSVAIGSAEGFDQAEYEITQSVKSGSWVMLKNVHLATSWLNDLEKKLFRLTPNANFRIFLTMEFNPKIPTTLIRQSYKLVFEPPDGIKASLIRTFKTVLSQQRTDRQPVERARLHFLLAWLHAVILERLRFTPIGWSKTYEFNEADQRCSLDLIDEYVDALGIRQNIDPSKLPWDAFRTILTQNLYGGKVDNEYDQKILQSLVEQFFTEQSFNHNHPLFFTLEGKEAITVPEGRTYLDFMQWIEQLPKTESPEWSGLPSNVERVQRDQLTQKLITKVQNLQQEGEEEITQIEVQTEKTQKKDNKKSDQVQWLQDLLEKVEKFKAILPNKISPLERTADSINDPLFRFLDREITVASKLLKAVRQNIEELIQLAQGKILATNILRQLAKDVFNNIVPAQWNKYNVITMPLNDWVGDFKRRIDQFDLLGKTKDFQKGQVWFGGLLFPEAYLTATRQYVAQANKWSLEELELQMIPEDQGIDEDSFVIEGVSMEGGHLDSKTLQVRIVNEISVALKPITLKWCKTSQKGVVGDDEIVLPVYLNKTRKNLIFSLKVKMGKLNRYTLYQKGLSFILFN', 4540, 'Q27171; Q6LED7;', 'KD01409', 'Paramecium tetraurelia', 'DHC-8', '#Dynein heavy chain; cytoplasmic#DHC08#Dynein heavy chain; cytosolic#DYHC', '-', '-', '-'),
(1410, 'Q5A1Q5', 'Probable kinetochore protein NUF2', 'GO:0000777', 56648, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSRQSFYADPSSAGRQMKYRKDLFPLLDTREITACLLECEFNVTQELIVKPTADFVTNLFEQFLDTFMGIPLGTIRKKARKMSRINPLESDQANGKPQQSPEEEFNDNQENDKTKDTFSALQLLTLHRYLAIFFSTCGINDFVLTDIARPDGYRIRRILSAVINFIRFREDQSPKFDHLANECEATADKVSEVQAENSATMQKINAIKEKLEMDSENDESNRKNLQYINSYNRKLETKLRELKVMQERLTKEHDDYKQEKALLAKKLYDINFLYNETQEQVANLTKYAETDLSILVKITEDLSNDLSSMQTNYKNLEKSYQNMGITIDSIQVNEINLKDLLKLAEDITRNVEKRQIEGKILKDNQDNLDELTRKQMELEGQILIVQNQLNKSNKKYQDLIVQADKKESAVKLKLEETKQEFNDILSEKEKHNEEHKRIMDQIVKIQQETTAIQDAFVKESKEVELKLINLMSIIKRYMSDLRNNI', 485, 'Q5A1Q5;', 'KD01410', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '3642613'),
(1411, 'Q6ZR08', 'Dynein heavy chain 12; axonemal', 'GO:0003777', 356942, '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}.', 'MSDANKAAIAAEKEALNLKLPPIVHLPENIGVDTPTQSKLLKYRRSKEQQQKINQLVIDGAKRNLDRTLGKRTPLLPPPDYPQTMTSEMKKKGFNYIYMKQCVESSPLVPIQQEWLDHMLRLIPESLKEGKEREELLESLINEVSSDFENSMKRYLVQSVLVKPPVKSLEDEGGPLPESPVGLDYSNPWHSSYVQARNQIFSNLHIIHPTMKMLLDLGYTTFADTVLLDFTGIRAKGPIDCESLKTDLSIQTRNAEEKIMNTWYPKVINLFTKKEALEGVKPEKLDAFYSCVSTLMSNQLKDLLRRTVEGFVKLFDPKDQQRLPIFKIELTFDDDKMEFYPTFQDLEDNVLSLVERIAEALQNVQTIPSWLSGTSTPVNLDTELPEHVLHWAVDTLKAAVHRNLEGARKHYETYVEKYNWLLDGTAVENIETFQTEDHTFDEYTEFIEKFLSLASEIMLLPQWIHYTMVRLDCEDLKTGLTNKAKAFANILLNDIASKYRKENECICSEFEAIKEHALKVPETTEEMMDLISYVEKARTVGIEELILRIQESKRQMSYFLDVFLFPQEDLALNATVLMWPRKINPIFDENDELIENAKHKKENELMAKREKLILEIEKESRRMEEFTEFAELERMQQYVTDVRQLQKRIQESEEAVQFINKEEELFKWELTKYPELDKLKVNIEPYQKFFNFVLKWQRSEKRWMDGGFLDLNGESMEADVEEFSREIFKTLKFFQTKLKKELQEKRKAARKRSLEEEKIEEEPKDNATITMCRMRARHWKQISEIVGYDLTPDSGTTLRKVLKLNLTPYLEQFEVISAGASKEFSLEKAMNTMIGTWEDIAFHISLYRDTGVCILSSVDEIQAILDDQIIKTQTMRGSPFIKPFEHEIKAWEDRLIRIQETIDEWLKVQAQWLYLEPIFCSEDIMQQMPEEGRQFQTVDRHWRDIMKFCAKDPKVLAATSLTGLLEKLQNCNELLEKIMKGLNAYLEKKRLFFPRFFFLSNDEMLEILSETKDPLRVQPHLKKCFEGIAKLEFLPNLDIKAMYSSEGERVELIALISTSAARGAVEKWLIQVEDLMLRSVHDVIAAARLAYPESARRDWVREWPGQVVLCISQMFWTSETQEVISGGTEGLKKYYKELQNQLNEIVELVRGKLSKQTRTTLGALVTIDVHARDVVMDMIKMGVSHDTDFLWLAQLRYYWENENARVRIINCNVKYAYEYLGNSPRLVITPLTDRCYRTLIGAFYLNLGGAPEGPAGTGKTETTKDLAKALAVQCVVFNCSDGLDYLAMGKFFKGLASSGAWACFDEFNRIELEVLSVVAQQILCIQRAIQQKLVVFVFEGTELKLNPNCFVAITMNPGYAGRSELPDNLKVLFRTVAMMVPNYALIAEISLYSYGFLNARPLSVKIVMTYRLCSEQLSSQFHYDYGMRAVKAVLVAAGNLKLKYPNENEDILLLRSIKDVNEPKFLSHDIPLFNGITSDLFPGIKLPEADYHEFLECAHEACNVHNLQPVKFFLEKIIQTYEMMIVRHGFMLVGEPFAAKTKVLHVLADTLTLMNEHGYGEEEKVIYRTVNPKSITMGQLFGQFDPVSHEWTDGIVANTFREFALSETPDRKWVVFDGPIDTLWIESMNTVLDDNKKLCLMSGEIIQMSPQMSLIFETMDLSQASPATVSRCGMIYLEPSQLGWEPLVSSWLNSLKGPLCEPEYQALLRGLFAWLIPPSLNQRVELFQLNYLYTTIVSKILKILITFRISNYFKYVPLKTQCTFIKFFLHQQACFIFSLIWSIGGSCDTDGRRVFDTFIRLIILGKDDENPVPDSVGKWECPFDEKGLVYDYMYELKNKGRWVHWNELIKNTNLGDKQIKIQDIIVPTMDTIRYTFLMDLSITYAKPLLFVGPTGTGKSVYVKDKLMNHLEKDQYFPFYINLSARTSANQVQNIIMARLDKRRKGVFGPPMGKKCIIFIDDMNMPALEKYGAQPPIELLRQFFDCGHWYDLKDTSKITLVDIELIAAMGPPGGGRNPVTPRCIRHFNICSINSFSDETMVRIFSSIVAFYLRTHEFPPEYFVIGNQIVNGTMEIYKQSVENLLPTPTKSHYTFNLRDFSRVIRGCLLIERDAVANKHTMIRLFVHEVLRVFYDRLINDDDRRWLFQLTKTVIKDHFKESFHSIFSHLRKQNAPVTEEDLRNLMFGDYMNPDLEGDDRVYIEIPNIHHFSDVVDQCLDEYNQTHKTRMNLVIFRYVLEHLSRICRVLKQSGGNALLVGLGGSGRQSLTRLATSMAKMHIFQPEISKSYGMNEWREDMKSFIAVPVTNRIVDNKSKILEKRLRYLNDHFTYNLYCNICRSLFEKDKLLFSFLLCANLLLARKEIEYQELMFLLTGGVSLKSAEKNPDPTWLQDKSWEEICRASEFPAFRGLRQHFCEHIYEWREIYDSKEPHNAKFPAPMDKNLNELQKIIILRCLRPDKITPAITNYVTDKLGKKFVEPPPFDLTKSYLDSNCTIPLIFVLSPGADPMASLLKFANDKSMSGNKFQAISLGQGQGPIAAKMIKAAIEEGTWVCLQNCHLAVSWMPMLEKICEDFTSETCNSSFRLWLTSYPSSKFPVTILQNGVKMTNEPPTGLRLNLLQSYLTDPVSDPEFFKGCRGKELAWEKLLFGVCFFHALVQERKKFGPLGWNIPYGFNESDLRISIRQLQLFINEYDTIPFEAISYLTGECNYGGRVTDDWDRRLLLTMLADFYNLYIVENPHYKFSPSGNYFAPPKGTYEDYIEFIKKLPFTQHPEIFGLHENVDISKDLQQTKTLFESLLLTQGGSKQTGASGSTDQILLEITKDILNKLPSDFDIEMALRKYPVRYEESMNTVLVQEMERFNNLIITIRNTLRDLEKAIKGVVVMDSALEALSGSLLVGKVPEIWAKRSYPSLKPLGSYITDFLARLNFLQDWYNSGKPCVFWLSGFFFTQAFLTGAMQNYARKYTTPIDLLGYEFEVIPSDTSDTSPEDGVYIHGLYLDGARWDRESGLLAEQYPKLLFDLMPIIWIKPTQKSRIIKSDAYVCPLYKTSERKGTLSTTGHSTNFVIAMLLKTDQPTRHWIKRGVALLCQLDD', 3092, 'Q6ZR08; A6NGI2; Q6ZTR8; Q8N7R9; Q8WXK2; Q92816;', 'KD01411', 'Homo sapiens (Human)', 'DNAH12', '#Dynein heavy chain 12; axonemal#Axonemal beta dynein heavy chain 12#Axonemal dynein heavy chain 12-like protein#Axonemal dynein heavy chain 7-like protein#Ciliary dynein heavy chain 12#Dynein heavy chain 7-like; axonemal#Dynein heavy chain domain-containing protein 2', '-', 'ENSG00000174844', '-'),
(1412, 'Q21215', 'Guanine nucleotide-binding protein subunit beta-2-like 1', 'GO:0000776===c;k;m', 35830, '', 'MVQEQMKLTGTLEGHTGWVTQIATYTRNDKTTVLSSSRDKTILVWDVDSVAPVDEGPIGRPVRSLTGHNHFVSDVVISSDGQFALSGSWDKTLRLWDLNQGVSTRQFISHTKDVLSVAFSADNRQIVSGSRDKSIKLWNTLAQCKYTITDDCHTDWVSTVRFSPSNRDPVIVSAGWDKVVKVWNLGNCRLKTNHIGHTGYVNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLPGNDVINAMSFSPNRYWLCAAVGSSIKIWDLEDKKEIEELKPEIASSGSSRGSSPQCISLAWSQDGQTLFAGYTDNIIRVYQVSIRASN', 325, 'Q21215;', 'KD01412', 'Caenorhabditis elegans', 'rack-1', '#Guanine nucleotide-binding protein subunit beta-2-like 1', '-', '-', '177895'),
(1413, 'Q4WVA0', 'Probable kinetochore protein nuf2', 'GO:0000778===GO:0051455===GO:0031617===GO:0031262', 54724, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MAYNHRMSQQFHGTQQHHNRGRKKEDENDALMRLPDKEIAGCINDIGIPFTAADLIKPNPQQIQMVFEWFAELLMNTTKETVEPAMRAAAEDICGDYPDIVPLETRNLMGFFISLRRLMMECGVNDFTFTDLTKPTHDRLVKIFSYLINFVRFRESQTQVIDEHFNKTEKTKARIDTLFMENQEMEQRLEEMRRSLKANEAQVKEKVRRNDELKARLLELRRNQERIAETLERVKADKARRQAQLEEKTERSVRTRQEVEKLRPYAMQSPVSLQSALTELSENLLREKAQIDAMEKRARALQTSSDTFTVVGNDVQACIKLLEDISVELQKEEEEESRASRNKEAISERGNNVREVEQTEKLLQRQLARWNERIEALRKNAQEKAEVAQARMDELRDVQKKLREERAEKQRDMERRRIRIEQTEKKMADLKENIENEIQSAHEEYLKLESHIKLYITEMEKCL', 463, 'Q4WVA0;', 'KD01413', 'Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSA1100) (Aspergillus fumigatus)', 'nuf2', '#Probable kinetochore protein nuf2', '-', '-', '3511093'),
(1414, 'Q6FIN2', 'DASH complex subunit ASK1', 'GO:0008608===GO:0042729', 22429, '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}.', 'MDRELERLDQEITLELQKIDGNLSHCFDVITKQVIPRVVAYGQVCDAISDSCEWLGTLCKSSGVVDLKRDVLLERTPVRDSDAHGNAHGDTHGNAHGDAHGEANAERSYGDVAGGEEHNSTVQSEVSDSTMGKYREDDTREQGEDDSVQRQKKRKVSLLIQERYGSSSSVMPSPDKRVPQQSLGSSPVKEQVPLPGTVIHFSTK', 204, 'Q6FIN2;', 'KD01414', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'ASK1', '#DASH complex subunit ASK1#Associated with spindles and kinetochores protein 1#Outer kinetochore protein ASK1', '-', '-', '2891202'),
(1415, 'Q6PFD9', 'Nuclear pore complex protein Nup98-Nup96', 'GO:0000776', 197241, 'Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC (By similarity). {ECO:0000250}.', 'MFNKSFGTPFGGSTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFGFGTSTGTSNSLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGGGTTAGLFGSSPATSSATGLFSSSTTNSAFSYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTPNTGFSFGNTSTLGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQPNTGFGAVGSTLFGNNKLTTFGTSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNNSGSSIFGSKPAAGTLGTGLGTGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTSTAILGFGAPQAPVALTDPNASAAQQAVLQQHLNSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNHDSEDLASPSEYPENGERFSFLSKPVDENNQQDGEDDSLVSRFYTNPIAKPIPQTPESVGNKNNSSSNVEDTIVALNMRAALRNGLEGSSEETSFHDESLQDDREEIENNAYHIHPAGIVLTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVIVYVDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHFSKYGLQDSDEEEEEHPPKTTSKKLKTAPLPPAGQATTFQMTLNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVPDSVLEESVPEDQEPVSASTHIASSLGINPHVLQIMKASLLVDEEDVDAMDQRFGHIPSKGETVQEICSPRLPISASHSSKSRSIVGGLLQSKFASGTFLSPSASVQECRTPRTSSRMNIPSTSPWSVPLPLATVFTVPSPAPEVQLKTVGIRRQPGLVPLEKSITYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLHGSHELENHQVADSMEYGFLPNPVAVKSLSESPFKVHLEKLGLRQRKLDEDLQLYQTPLELKLKHSTVHVDELCPLIVPNPGVSVIHDYADWVKDSPGDFLELPIVKHWSLTWTLCEALWGHLKELDGQLDEPSEYIQTLERRRAFSRWLSHTAAPQIEEEVSLTRRDSPVEAVFSYLTGSRISGACCLAQQSGDHRLALLLSQLVGSQSVRELLTMQLADWHQLQADSFIHDERLRIFALLAGKPVWQLSEQKQINVCSQLDWKRTLAIHLWYLLPPTASISRALSMYEEAFQNTPEGDKYACSPLPSYLEGCGCMVEEEKDSRRPLQDVCFHLLKLYSDRHYELNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSEQCEGVLQASYAGQLESEGLWEWAIFVFLHIDNSGMREKAVRELLTRHCQLSETPESWAKEAFLTQKLCVPAEWIHEAKAVRAHMESNKHLEALYLFKAGHWNRCHKLVIRHLASDAIINENYDYLKGFLEDLAPPERSSLIQDWETSGLVYLDYIRVIEMLHRIQQVDCSGYELEHLHTKVTSLCNRIEQIPCYNAKDRLAQSDMAKRVANLLRVVLSLQHAPDATSNSTPDPQRVPLRLLAPHIGRLPMPEDYALEELRGLTQSYLRELTVGSQ', 1816, 'Q6PFD9; Q68G59;', 'KD01415', 'Mus musculus (Mouse)', 'Nup98', '#Nuclear pore complex protein Nup98-Nup96#Nuclear pore complex protein Nup98#98 kDa nucleoporin#Nucleoporin Nup98#Nup98#Nuclear pore complex protein Nup96#96 kDa nucleoporin#Nucleoporin Nup96#Nup96', '-', '-', '269966'),
(1416, 'Q12267', 'Structural maintenance of chromosomes protein 4', 'k', 162189, 'Central component of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.', 'MSDSPLSKRQKRKSAQEPELSLDQGDAEEDSQVENRVNLSENTPEPDLPALEASYSKSYTPRKLVLSSGENRYAFSQPTNSTTTSLHVPNLQPPKTSSRGRDHKSYSQSPPRSPGRSPTRRLELLQLSPVKNSRVELQKIYDRHQSSSKQQSRLFINELVLENFKSYAGKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLIHKSEAFPSLQSCSVAVHFQYVIDESSGTSRIDEEKPGLIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQMKPKAEKESDDGLLEYLEDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETALEFLEKEKQLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKVLTALSRLQKSGRINGFHGRLGDLGVIDDSFDVAISTACPRLDDVVVDTVECAQHCIDYLRKNKLGYARFILLDRLRQFNLQPISTPENVPRLFDLVKPKNPKFSNAFYSVLRDTLVAQNLKQANNVAYGKKRFRVVTVDGKLIDISGTMSGGGNHVAKGLMKLGTNQSDKVDDYTPEEVDKIERELSERENNFRVASDTVHEMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEMAYVKAVSDKAQLNVVMKNLERLRGEYNDLQSETKTKKEKIKGLQDEIMKIGGIKLQMQNSKVESVCQKLDILVAKLKKVKSASKKSGGDVVKFQKLLQNSERDVELSSDELKVIEEQLKHTKLALAENDTNMNETLNLKVELKEQSEQLKEQMEDMEESINEFKSIEIEMKNKLEKLNSLLTYIKSEITQQEKGLNELSIRDVTHTLGMLDDNKMDSVKEDVKNNQELDQEYRSCETQDESEIKDAETSCDNYHPMNIDETSDEVSRGIPRLSEDELRELDVELIESKINELSYYVEETNVDIGVLEEYARRLAEFKRRKLDLNNAVQKRDEVKEQLGILKKKRFDEFMAGFNIISMTLKEMYQMITMGGNAELELVDSLDPFSEGVTFSVMPPKKSWRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAQQLVGVYKRDNRTKSTTIKNIDILNRT', 1418, 'Q12267; D6VY86;', 'KD01416', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SMC4', '#Structural maintenance of chromosomes protein 4', '-', '-', '850775'),
(1417, 'P38313', 'Central kinetochore subunit AME1', 'GO:0000776===GO:0034501===GO:0008608===GO:0000817===SCL===c;k', 37462, '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.', 'MDRDTKLAFRLRGSHSRRTDDIDDDVIVFKTPNAVYREENSPIQSPVQPILSSPKLANSFEFPITTNNVNAQDRHEHGYQPLDAEDYPMIDSENKSLISESPQNVRNDEDLTTRYNFDDIPIRQLSSSITSVTTIDVLSSLFINLFENDLIPQALKDFNKSDDDQFRKLLYKLDLRLFQTISDQMTRDLKDILDINVSNNELCYQLKQVLARKEDLNQQIISVRNEIQELKAGKDWHDLQNEQAKLNDKVKLNKRLNDLTSTLLGKYEGDRKIMSQDSEDDSIRDDSNILDIAHFVDLMDPYNGLLKKINKINENLSNELQPSL', 324, 'P38313; D6VQK7;', 'KD01417', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'AME1', '#Central kinetochore subunit AME1#Associated with microtubules and essential protein 1', '-', '-', '852512'),
(1418, 'P53692', 'Structural maintenance of chromosomes protein 6', 'k', 130929, 'Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis. {ECO:0000269|PubMed:10473635}.', 'MTTELTNVSLEEAITEKTSENRRKRDSDVLQTEEVDLSNVKRIRASRNQDNRPERQSRLQRSSSLIEQVRGNEDGENDVLNQTRETNSNFDNRVGVIECIHLVNFMCHDSLKINFGPRINFVIGHNGSGKSAILTGLTICLGAKASNTNRAPNMKSLVKQGKNYARISVTISNRGFEAYQPEIYGKSITIERTIRREGSSEYRLRSFNGTVISTKRDELDNICDHMGLQIDNPMNILTQDTARQFLGNSSPKEKYQLFMKGIQLKQLEENYSLIEQSLINTKNVLGNKKTGVSYLAKKEEEYKLLWEQSRETENLHNLLEQKKGEMVWAQVVEVEKELLLAEKEFQHAEVKLSEAKENLESIVTNQSDIDGKISSKEEVIGRAKGETDTTKSKFEDIVKTFDGYRSEMNDVDIQKRDIQNSINAAKSCLDVYREQLNTERARENNLGGSQIEKRANESNNLQREIADLSEQIVELESKRNDLHSALLEMGGNLTSLLTKKDSIANKISDQSEHLKVLEDVQRDKVSAFGKNMPQLLKLITRETRFQHPPKGPMGKYMTVKEQKWHLIIERILGNVINGFIVRSHHDQLILKELMRQSNCHATVVVGKYDPFDYSSGEPDSQYPTVLKIIKFDDDEVLHTLINHLGIEKMLLIEDRREAEAYMKRGIANVTQCYALDPRNRGYGFRIVSTQRSSGISKVTPWNRPPRIGFSSSTSIEAEKKILDDLKKQYNFASNQLNEAKIEQAKFKRDEQLLVEKIEGIKKRILLKRREVNSLESQELSVLDTEKIQTLERRISETEKELESYAGQLQDAKNEEHRIRDNQRPVIEEIRIYREKIQTETQRLSSLQTELSRLRDEKRNSEVDIERHRQTVESCTNILREKEAKKVQCAQVVADYTAKANTRCERVPVQLSPAELDNEIERLQMQIAEWRNRTGVSVEQAAEDYLNAKEKHDQAKVLVARLTQLLQALEETLRRRNEMWTKFRKLITLRTKELFELYLSQRNFTGKLVIKHQEEFLEPRVYPANRNLATAHNRHEKSKVSVQGLSGGEKSFATICMLLSIWEAMSCPLRCLDEFDVFMDAVNRLVSIKMMVDSAKDSSDKQFIFITPQDMGQIGLDKDVVVFRLSDPVVSSSALPPSTAP', 1140, 'P53692;', 'KD01418', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'smc6', '#Structural maintenance of chromosomes protein 6#DNA repair protein rad18', '-', '-', '2539020');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1419, 'Q2KJ93', '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 (By similarity). {ECO:0000250}.', 'MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL', 191, 'Q2KJ93;', 'KD01419', 'Bos taurus (Bovine)', 'CDC42', '#Cell division control protein 42 homolog', '-', '-', '532712'),
(1420, 'P30277', 'G2/mitotic-specific cyclin-B1', 'GO:0000942===GO:0051987', 47391, 'Essential for the control of the cell cycle at the G2/M (mitosis) transition.', 'MALRVTRNTKINTENKAKVSMAGAKRVPVAVAASKPLLRSRTALGDIGNKVSEQSRIPLKKETKKLGSGTVTVKALPKPVDKVPVCEPEVELDEPEPEPVMEVKHSPEPILVDTPSPSPMETSGCAPAEEYLCQAFSDVILAVSDVDADDGGDPNLCSEYVKDIYAYLRQLEEEQSVRPKYLLGREVTGNMRAILIDWLIQVQMKFRLLQETMYMTVSIIDRFMQDSCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTNNTYTKHQIRQMEMKILRVLNFSLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELSMLDYDMVHFAPSQIAAGAFCLALKILDNGEWTPTLQHYLSHTEESLLPVMQHLAKNIVMVNRGLTKHMTIKNKYATSKHAKISTLAQLNCTLVQNLSKAVTKA', 423, 'P30277;', 'KD01420', 'Rattus norvegicus (Rat)', 'Ccnb1', '#G2/mitotic-specific cyclin-B1', '-', '-', '25203'),
(1421, 'Q6FN12', 'Probable kinetochore protein SPC24', 'GO:0000777', 23155, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MASTEEIVQMMQEASAEFAEADDVSFLDKMNSNIAQLEQQLREQMDESRQNIAKLEINLIDTEKSIGSLRELMKDATDEATIMKGSDKLNNLIDELQATENEIQMMNSEIEKKVSKLVEDEDNTSSEYEMISKELEQEYDPVFASNILKLKLYRSLGVRLDLDNNQILIQNKELGTIDTLPLEDELTEFFKVKYIWSRIGK', 201, 'Q6FN12;', 'KD01421', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'SPC24', '#Probable kinetochore protein SPC24', '-', '-', '2890132'),
(1422, 'P32908', 'Structural maintenance of chromosomes protein 1', 'k', 141280, 'Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase; the complex is cleaved and dissociates from chromatin; allowing sister chromatids to segregate.', 'MGRLVGLELSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNILKDLIYRGVLNDENSDDYDNEGAASSNPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVEQIAAQSPVELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQKFQALWQLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKLVSDLRLIKVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNCLHEKYLTEGGSILEEKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESANNQEYDLNFKLRETLVKIDDLSANQRETMKERKLRENIAMLKRFFPGVKGLVHDLCHPKKEKYGLAVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYILSINAIDYEPEYEKAMQYVCGDSIICNTLNIAKDLKWKKGIRGKLVTIEGALIHKAGLMTGGISGDANNRWDKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIFKEFTSKIGFTIKEYENHSGELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINIPISSETTIDDLPISSTDNEAITISNSIDINYKGLPKKYKENNTDSARKELEQKIHEVEEILNELQPNARALERYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKNPNSNVELAGGNASLTIEDEDEPFNAGIKYHATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNPDLQFIVISLKNTMFEKSDALVGVYRQQQENSSKIITLDLSNYAE', 1225, 'P32908; D6VTM2;', 'KD01422', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SMC1', '#Structural maintenance of chromosomes protein 1#DA-box protein SMC1', '-', '-', '850540'),
(1423, 'Q9UTS6', 'Dynein light chain Tctex-type', 'GO:1902423===GO:0044816', 12254, 'Acts as a non-catalytic accessory component of a dynein complex. {ECO:0000250}.', 'MSCPIDSKKLEEICLEAAQPVLKASEYDGDKTAEMNQSVIYAVLNALNKETQSYKWIVSSTLVQKLPEDHPSRGVHAAHAACWNCEKDGMTTIKESGEAIDVVLSIMWISI', 111, 'Q9UTS6; Q9UTG7;', 'KD01423', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dlc1', '#Dynein light chain Tctex-type#TCTEX-1 protein homolog', '-', '-', '3361491'),
(1424, 'Q1T7C1', 'Centromere protein K', 'GO:0000777', 30720, 'Component of the CENPA-HI complex; a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. {ECO:0000250}.', 'MSDSVCPIDAKEELLRECENIWKEMEKCQSKLTLLAAEPVPESDAKVSLLLTRMQALRAEYHQWQKRNPELISTNPEVLLLLGEEELQKVKKELEMVLSAVQLKNEKLKEDLEREQQWHDEQVQILNAFKEIEEEMKKEVVTDSEKRVFQELKNQMLELKEYKKKLMNALGEFLEEHFPLPEKNGNAKKKRYSEEPPEQVITIHEILEILLNQLMSTPHEPYVTVDDSFWPPYLELLLRSGIVLRHPEDPNRIRLEAFHE', 260, 'Q1T7C1;', 'KD01424', 'Gallus gallus (Chicken)', 'CENPK', '#Centromere protein K#CENP-K', '-', '-', '427162'),
(1425, 'Q60575', 'Kinesin-like protein KIF1B', 'GO:0003777', 204081, 'Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility.', 'MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQNRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLIDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTASMGSLTSSPSSCSLNSQVGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSNTGEVIVTLEPCERSETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKKEKEEADLLLEQQRLDYESKLQALQRQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPVPPELLPSEMEKTHEDRPFPRTVVAVEVQDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVASSAQDDSETTMTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDAMEDFDDEAFVDDTGSDAGTEEGSELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFSSAAMTRSGLSLEELRIVEGQGQSSEVISPPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLGFYHVQNIAVEVTESFVDYIKTKPIVFEVFGHYQQHPLHLQGQDLNSPPQPSRRFFPPPMPLSKPVPATKLNTMNKTTLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAVLSLNIISAKSLKAAHSSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRNLFGSGYSKSPDSNRVTGIYELSLCKMADTGSPGMQRRRRKVLDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSVPKSLSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSADVESLVDREKELATKCLQLLTHTFNREFSQVHGSISDCKLSDISPIGRDPSVSSFSSSTLTPSSTCPSLVDSRSSSMDQKTPEANSRASSPCQEFEQFQIVPTVETPYLARAGKNEFLNLVPDIEEVRAGSVVSKKGYLHFKEPLSSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQPKY', 1816, 'Q60575; Q9R0B4; Q9WVE5; Q9Z119;', 'KD01425', 'Mus musculus (Mouse)', 'Kif1b', '#Kinesin-like protein KIF1B', '-', '-', '16561'),
(1426, 'O60832', 'H/ACA ribonucleoprotein complex subunit 4', 'k;t', 57674, 'Isoform 1: Required for ribosome biogenesis and telomere maintenance. 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. Each rRNA can contain up to 100 pseudouridine (''psi'') residues; which may serve to stabilize the conformation of rRNAs. Also required for correct processing or intranuclear trafficking of TERC; the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.', 'MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFDKLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGVLRYEDGIEVNQEIVVITTKGEAICMAIALMTTAVISTCDHGIVAKIKRVIMERDTYPRKWGLGPKASQKKLMIKQGLLDKHGKPTDSTPATWKQEYVDYSESAKKEVVAEVVKAPQVVAEAAKTAKRKRESESESDETPPAAPQLIKKEKKKSKKDKKAKAGLESGAEPGDGDSDTTKKKKKKKKAKEVELVSE', 514, 'O60832; F5BSB3; O43845; Q96G67; Q9Y505;', 'KD01426', 'Homo sapiens (Human)', 'DKC1', '#H/ACA ribonucleoprotein complex subunit 4#5.4.99.-#CBF5 homolog#Dyskerin#Nopp140-associated protein of 57 kDa#Nucleolar protein NAP57#Nucleolar protein family A member 4#snoRNP protein DKC1', '-', 'ENSG00000130826', '-'),
(1427, 'P23594', 'Serine/threonine-protein phosphatase PP2A-1 catalytic subunit', 'k', 41938, 'Exact function not known; phosphatase 2A performs an essential cellular function.', 'MDTDLDVPMQDAVTEQLTPTVSEDMDLNNNSSDNNAEEFSVDDLKPGSSGIADHKSSKPLELNNTNINQLDQWIEHLSKCEPLSEDDVARLCKMAVDVLQFEENVKPINVPVTICGDVHGQFHDLLELFKIGGPCPDTNYLFMGDYVDRGYYSVETVSYLVAMKVRYPHRITILRGNHESRQITQVYGFYDECLRKYGSANVWKMFTDLFDYFPITALVDNKIFCLHGGLSPMIETIDQVRELNRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGFTFGQDVSEQFNHTNDLSLIARAHQLVMEGYAWSHQQNVVTIFSAPNYCYRCGNQAAIMEVDENHNRQFLQYDPSVRPGEPSVSRKTPDYFL', 369, 'P23594; D6VRL4;', 'KD01427', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'PPH21', '#Serine/threonine-protein phosphatase PP2A-1 catalytic subunit#3.1.3.16', '-', '-', '851421'),
(1428, 'P46675', 'Protein STU2', 'GO:0000776===GO:0000778===c;k', 100918, 'May play a role in the attachment; organization; and/or dynamics of microtubule ends at the spindle pole body.', 'MSGEEEVDYTTLPLEERLTYKLWKARLEAYKELNQLFRNSVGDISRDDNIQIYWRDPTLFAQYITDSNVVAQEQAIVALNSLIDAFASSSLKNAHNITLISTWTPLLVEKGLTSSRATTKTQSMSCILSLCGLDTSITQSVELVIPFFEKKLPKLIAAAANCVYELMAAFGLTNVNVQTFLPELLKHVPQLAGHGDRNVRSQTMNLIVEIYKVTGNNSDLLEEILFKKLKPIQVKDLHKLFAKVGDEPSSSKMLFEWEKRELEKKRSQEEEARKRKSILSNDEGEYQIDKDGDTLMGMETDMPPSKQQSGVQIDTFSMLPEETILDKLPKDFQERITSSKWKDRVEALEEFWDSVLSQTKKLKSTSQNYSNLLGIYGHIIQKDANIQAVALAAQSVELICDKLKTPGFSKDYVSLVFTPLLDRTKEKKPSVIEAIRKALLTICKYYDPLASSGRNEDMLKDILEHMKHKTPQIRMECTQLFNASMKEEKDGYSTLQRYLKDEVVPIVIQIVNDTQPAIRTIGFESFAILIKIFGMNTFVKTLEHLDNLKRKKIEETVKTLPNFSIASGSTHSTIETNKQTGPMENKFLLKKSSVLPSKRVASSPLRNDNKSKVNPIGSVASASKPSMVAANNKSRVLLTSKSLATPKNVVANSTDKNEKLIEEYKYRLQKLQNDEMIWTKERQSLLEKMNNTENYKIEMIKENEMLREQLKEAQSKLNEKNIQLRSKEIDVNKLSDRVLSLENELRNMEIELDRNKKRNDTNLQSMGTISSYSIPSSTVSSNYGVKSLSSALPFKEEEDVRRKEDVNYERRSSESIGDLPHRVNSLNIRPYRKNGTGVSSVSDDLDIDFNDSFASEESYKRAAAVTSTLKARIEKMKAKSRREGTTRT', 888, 'P46675; D6VY47;', 'KD01428', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'STU2', '#Protein STU2#Suppressor of tubulin 2', '-', '-', '850734'),
(1429, 'A6ZZR4', 'DASH complex subunit ASK1', 'GO:0008608===GO:0042729', 32046, '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 (By similarity). {ECO:0000250}.', 'MDSASKEETLEKLDQEITVNLQKIDSNLSFCFHKITQDIIPHVATYSEICERIMDSTEWLGTMFQETGLVNLQANAAAPVGNAPVKSVVSNNVGIFPTSAEEASRESQTDNGPNEADSAVHVNRDVHSMFTNDSIDDFHTANITSTGQILKLPDSSDEDTGSEAVPSREQTDLTGEGHGGADDEQDESTIQRQSRKRKISLLLQQQYGSSSSMVPSPIVPNKMRKQLAHEEHINNDGDNDDENSNNIESSPLKQGHHHPKGQADDNNEGPDEEESTKEVPKPGTIIHFSTNR', 292, 'A6ZZR4;', 'KD01429', 'Saccharomyces cerevisiae (strain YJM789) (Baker''s yeast)', 'ASK1', '#DASH complex subunit ASK1#Associated with spindles and kinetochores protein 1#Outer kinetochore protein ASK1', '-', '-', '-'),
(1430, 'Q1T7B8', 'Centromere protein O', 'GO:0000776===GO:0034508', 36593, 'Component of the CENPA-HI complex; a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). Involved in kinetochore assembly and required for recovery from spindle damage. {ECO:0000250; ECO:0000269|PubMed:18094054}.', 'MEEERNSDEKENALCGRSLTAASRDGGGRMPAAPLAQGKVERGKVYSGDGVLGYLEMLEAQAHELGLKQEEKEQQEKKLDRLKARVQELRARRDELRAKVELQEKRLLDKEGVMTDPAQPSAQTVLEWKVKSLKAMLQVFYLTGISGKLTKQGVCFCISTAYEGTYLDSYYVDLLIKPLVKIQRHSVPVFIPLEQIAKKYLQTDIRRFLSVLSDHLNAYVGRRRQADQLEEHFSDHIDGTLQRNSLCNLLVFNYTVSSNSKTFPFNVRLLYGDLCCSLPTEAIISCTPGTLPLLAEMAAAHSNAFRHMALHKAFDSLINAKESQN', 325, 'Q1T7B8; Q5ZJK9;', 'KD01430', 'Gallus gallus (Chicken)', 'CENPO', '#Centromere protein O#CENP-O', '-', '-', '422014'),
(1431, 'Q5ALU2', 'Probable kinetochore protein SPC24', 'GO:0000777', 29187, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MTTSVDKLNKLIEEVNNQDELQLIEEINLYIKTLYELRQVKIDQLSNIIHQLNQQIITSNKEINQLNKINDYNYELINVNNFNFVSQQSFQFTNFDRSSSSSSESTNNIFQMINKRLNELDNLKVVIVKELTDLETNLNNLKYKQNNLHESMEDINDKLDKLLNDMDKSGIMEQDPSILRINLFRNLGIKLENMPPNANSGGGGDSNSNSNNNNNTEEDCVIITDDNNNVNILNIEPKLSDYFISNYIWDKL', 252, 'Q5ALU2;', 'KD01431', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'SPC24', '#Probable kinetochore protein SPC24', '-', '-', '3635732'),
(1432, 'Q2KIW5', 'Centromere protein U', 'GO:0000777', 46674, '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}.', 'DRPRPARLSHARFSKNHSGRTHSMKDKAGRKHRPLDVFDFPDHSQLSSFSRLGENEKDEESYETFDPPLHSTAIYADEEEFSKQCGSHLPSTPQEKEAKRSSDTSEIEASENESVKISAKKPRRKLKPISDESESPEESDVRRKVKPTENISTQHEAVSATALPGLSEKPAEAVTPQKTGPQSAESSAEKATLATEHQLETQKNKMLPGKRKKPRSYTTDTSDCAPVWCLKEKKASEIMELDVFLSAFENILLEYEQKIDSRVCKAAINKFHSNLKEELIKMVQEIQMLKTLKRKNAKIISNIEKKRQRLIEVQDELLQVEPELKQLQIKYEELQERKASLRKAAYFLSNLKQLHQDYSDVQEEEPSVKETYDSSSLPALLFKARPLLGAEHHLQNINYQLENLLDQK', 408, 'Q2KIW5;', 'KD01432', 'Bos taurus (Bovine)', 'CENPU', '#Centromere protein U#CENP-U#MLF1-interacting protein', '-', '-', '-'),
(1433, 'Q09373', 'WD repeat-containing protein fzy-1', 'k', 56384, '', 'MNNKGRTPGSAGRTVRSSAQQNGLTMRKRDMTPTRNTNLLPNATFVGDRFLGVRLDQDELDHANHLMTSKLYSNKENLNNSMSEPNSPEKKSVEGEALKQMMRHKSTGALTDADDGDRILCYKKNLAPPPAIGYINQAKVLYSTNSVINPASSVKKSTRHVKETATKVLDGPGLTKDLYSRHLDWGCHNWVAVALGHELYLWNTETCVIKNLFEDNAPTNEGLITSVRWSQEGRYISLGYASGAVKIYDPNRPKTTEYVRELRTLRVGGASRCASIAWRKQGVMTCGYKSGDIVNHDVRISQHVVSSWGGDNGHCRDVTALEWSADENMCVSGSSDRTAKIWDGRHVRGSTVIQDPEPMFTIDEHTGQVRTAQFCSFRDGILATGGGINDGTVKLWDVKRQFQKVRELNVCETGGVGGIVFNRPYSEMLTASDDGFLRIYRFNANYKLSHEIQASNEPIMDLVGSPFDEVLIGDMEETLKVFQLFNVDKSTNILDRTAPKNVGLNVR', 507, 'Q09373; Q09661;', 'KD01433', 'Caenorhabditis elegans', 'fzy-1', '#WD repeat-containing protein fzy-1#Fizzy protein 1', '-', '-', '266859'),
(1434, 'P23595', 'Serine/threonine-protein phosphatase PP2A-2 catalytic subunit', 'GO:0000780===k', 43047, 'Exact function not known; phosphatase 2A performs an essential cellular function.', 'MDMEIDDPMHGSDEDQLSPTLDEDMNSDDGKNNTKARSNDEDTDEELEDFNFKPGSSGIADHKSSKPLKLTNTNINQLDQWIEHLSKCEPLSEDDVARLCKMAVDVLQFEENVKPINVPVTICGDVHGQFHDLLELFKIGGPCPDTNYLFMGDYVDRGYYSVETVSYLVAMKVRYPHRITILRGNHESRQITQVYGFYDECLRKYGSANVWKMFTDLFDYFPVTALVDNKIFCLHGGLSPMIETIDQVRDLNRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGFTFGQDISEQFNHTNDLSLIARAHQLVMEGYSWSHQQNVVTIFSAPNYCYRCGNQAAIMEVDENHNRQFLQYDPSVRPGEPTVTRKTPDYFL', 377, 'P23595; D6VRG5;', 'KD01434', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'PPH22', '#Serine/threonine-protein phosphatase PP2A-2 catalytic subunit#3.1.3.16', '-', '-', '851339'),
(1435, 'P32504', 'Centromere DNA-binding protein complex CBF3 subunit A', 'GO:0000778===GO:0031518===GO:0000780===k;m', 111917, 'Acts as a 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.', 'MRSSILFLLKLMKIMDVQQQQEAMSSEDRFQELVDSLKPRTAHQYKTYYTKYIQWCQLNQIIPTPEDNSVNSVPYKDLPISAELIHWFLLDTLITDDKPGEKREETEDLDEEEENSFKIATLKKIIGSLNFLSKLCKVHENPNANIDTKYLESVTKLHTHWIDSQKAITTNETNNTNTQVLCPPLLKVSLNLWNPETNHLSEKFFKTCSEKLRFLVDFQLRSYLNLSFEERSKIRFGSLKLGKRDRDAIIYHKVTHSAEKKDTPGHHQLLALLPQDCPFICPQTTLAAYLYLRFYGIPSVSKGDGFPNLNADENGSLLQDIPILRGKSLTTYPREETFSNYYTTVFRYCHLPYKRREYFNKCNLVYPTWDEDTFRTFFNEENHGNWLEQPEAFAFPDKIPFDFKKIMNFKSPYTSYSTNAKKDPFPPPKDLLVQIFPEIDEYKRHDYEGLSQNSRDFLDLMEVLRERFLSNLPWIYKFFPNHDIFQDPIFGNSDFQSYFNDKTIHSKGSPILSFDILPGFNKIYKNKTNFYSLLIERPSQLTFASSHNPDTHPTQKQESEGPLQMSQLDTTQLNELLKQQSFEYVQFQTLSNFQILLSVFNKIFEKLEMKKSSRGYILHQLNLFKITLDERIKKSKIDDADKFIRDNQPIKKEENIVNEDGPNTSRRTKRPKQIRLLSIADSSDESSTEDSNVFKKDGESIEDGAYGENEDENDSEMQEQLKSMINELINSKISTFLRDQMDQFELKINALLDKILEEKVTRIIEQKLGSHTGKFSTLKRPQLYMTEEHNVGFDMEVPKKLRTSGKYAETVKDNDDHQAMSTTASPSPEQDQEAKSYTDEQEFMLDKSIDSIEGIILEWFTPNAKYANQCVHSMNKSGNKSWRANCEALYKERKSIVEFYIYLVNHESLDRYKAVDICEKLRDQNEGSFSRLAKFLRKWRHDHQNSFDGLLVYLSN', 956, 'P32504; D6VUS0; E9P954;', 'KD01435', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CBF2', '#Centromere DNA-binding protein complex CBF3 subunit A#Centromere-binding factor 2#Chromosome transmission fidelity protein 14#Kinetochore protein CTF14', '-', '-', '853041'),
(1436, 'Q0IHP2', 'Inner centromere protein', 'GO:0032133', 104130, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Probably acts through association with aurkb or aurkc. Seems to bind directly to microtubules (By similarity). {ECO:0000250}.', 'MNDAECLSHLLQVCARKTEEFVRTLDSKHMVWLLEIEEEARKMFSSDFNAEPELMPKTPSQKRRRKKRTSIVPDENRDPSGRRISRRRSSANWSNSVRRLSIRNQNKTNEDSMQEEPAQPKRMTRARAQASIMCPSVVEMALPESPSQLYQKNVQVTISEQDRRSAEQKLVGSATEESEMKTDVLPVPKIAKDTISEIVNTVVPPPVPETPAVPVTPENKSRAAAKLKIAGSSTPIEAAEMVDLTCESPRPANELANEQPLNLTNQSVTPTGSKSDRRSVRRSLVVVKPSSRRSSLASQFSLASKRESMTREAVRKSIRQSIAKKKAAMETSSASSQRSCQSSIEIIDDEITIKIRPETAPSESVSEEAHTIESPRRSLRSRTFKKIAISNLPDSEEPQRRVTRQMVAMDAEPTPETTDDAQNIRRKSYKRAVDELSDDERPSEGERSPPRKKTPSPPCPPSKIVKPPPHMKSFLHTVQKNQLLMMTPGSIGKNIMMKSFIKRNTPLKMDPKEKERQRLDALRKKEEAELQRKQKIEEGKKRKQEELKLRREERLRKVLQARERVEQLEEEKKKKIEQKFAQIDEKSEKVREDRMAEEKAKKKITAKKQEEVECRRRQEEEARKLKAKQMEEEERRHQDLLQKKREEEELERQKKIAEAKRLAEQRQAEQERERQREQQLLAEKERLRAERERIEREKALQLQRELERAAQEKEQQRREAEERKKREQQERLEQERLERLHKEQEAKRLQEEQQRKAKEQAAAASAPVMNVTVDMQNSPACESYEMTPKSYKAPSVKVNEENYGMDLNSDDSTDDESQPRKPIPAWASGNLLAQAIRQQYYKPMDVDRMYGTIDSPKLEELFYKSKPRYYKRTSSAVWHSPPLSSNRHHLAVGYGLKY', 898, 'Q0IHP2; Q28GE7; Q5XHA5;', 'KD01436', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'incenp', '#Inner centromere protein', '-', '-', '496453'),
(1437, 'Q9QYM8', 'Centromere protein H', 'GO:0000776===GO:0000777===GO:0043515===GO:0051382===GO:0051383===SCL', 28135, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate (By similarity). {ECO:0000250}.', 'MEEQPRERSEAGAEACEEKRGLSQAAEERIEDRISLLLRLRAQTKQQLLEYKSMIDTNEEKTPEQIMQEKQIEVKIEELENEIEDVKSNIEMKSLALSRMKLSVALRDNMENMGPENCVLTDDMKHILKLQKLIMKSQEESSELEKKLLDVRKKRLQLKQASRSKLLEIQIEKNKQKEDVDKMENSEMIKTMKKKLQTEIKITTVVQHTFQGLILASKTNWAEDPALRETVLQLEKDLNTL', 241, 'Q9QYM8; Q8R3K9; Q9D079; Q9D0N1;', 'KD01437', 'Mus musculus (Mouse)', 'Cenph', '#Centromere protein H#CENP-H', '-', '-', '26886'),
(1438, 'Q757M3', 'Probable kinetochore protein NUF2', 'GO:0000778===GO:0051455===GO:0031617===GO:0031262', 53091, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSSDNFPLLDIPELVTCLQECDFSLATIQNVERPSSQFVITLYKQIIDTFMGVSPDSLLEDSRNFVENGDTSEQEVYDASLVYHDTLKILALNKICYKFFLDIGVSDFNVMDLYKPDPHRTRRFLSAVANYARFREEAMLELDGDQHPDGVRYLEQTDKLLKELRLKFDANNLLHSRVQKYKEFQKSDDLEALESDNKNMESELRHLNQVQETLTVDYERYKAEKQRHLSELETLGYELIELESERDKLRKYSQTDAEVLRKGVRELSLLLEQQQVQLEKLEQKQKNLQISFETFQASTQELYEVLQIVSTDLQDSHLKESTLLDAKHKLMQNHKNLNNLLSAGIMAKITLLQEQLDSQKRKLAELELNTQAKESENSATLKRLRKQHTDDVLPEVRNIEQRYKTKVADTITNYESQMRNIKVDFDNEVALIENECSLLFNHIKNYMTTIGEKLG', 455, 'Q757M3;', 'KD01438', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '4621045'),
(1439, 'Q63517', 'Centromere protein I', 'GO:0000776===GO:0034508', 85651, 'Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Required for the localization of CENPF; MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to kinetochores. Involved in the response of gonadal tissues to follicle-stimulating hormone (By similarity). {ECO:0000250}.', 'MATPRLTRNSQQQNRISQGSNSRQTTLLDWKVKDKAGNSKSVLEESSSLEDSNHADDQTEDALQTAVEYFQKGPKKASLSKDSVLEKHLKTVENVAWNNGLAPEAIDILLNVALSGKFGNALSTRILKCMIPETHISEDSVVKAVSWLCVGKCSGNTKVLFYRWLVAMFDFIDHKKQINSLYGFFFVSLQDDTLCPYVCHLLYLLTKKENVKPFRARKLLDLQAKMGMQPHLQALLSLYKFFAPTLISVSLPVRKKIFFNNSKNLWTPALLAVKLRNQGIFPEPLKLQLGPTSGRSLKRKWNYHSVIPAVNSAKKECREKMSLFDYLSNDRSLPVEQLQSFPQLLENIHCLELPSQMSSVLNSSLLLHYVNCVKDESILLRLSYWLSQTLQEECVWYNMNDYQQEKEFINFLDMVIRVQCFLQEGFYSCEAFLYKSLPLWDGFSCRSQFLKLLAWIPFSSFSEIKPLLLDHLAPLFFTSSIYFKCSLLQCLKDLLQNWLLWLSTEAQVQPMTDSPLETTLGGSMDSVSQLIEYIGWLSMVAIRLESSSTLLVHFILDFYEKVCDIYINYDLPLVVLFPPVVFHSAFLSLDATILNQLCYIMYRYRDNLTAAKKKDLVQKAKSEFSISSKICKEFNYYLTALVHCLWSSRPFETGVYIDPQIIENTGETQYKHNLNFVHHPCLLNYAASFLLQESPEEMPVHLSSIRGKKWNWYLDHLYSEGFQGLNLFIKSSIDHSSVSKTEKNT', 745, 'Q63517;', 'KD01439', 'Rattus norvegicus (Rat)', 'Cenpi', '#Centromere protein I#CENP-I#FSH primary response protein 1#Follicle-stimulating hormone primary response protein#Leucine-rich primary response protein 1', '-', '-', '25448'),
(1440, 'A5GFW1', 'Aurora kinase A', 'GO:0032133===GO:0000780', 45516, 'Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle; centrosome duplication; centrosome separation as well as maturation; chromosomal alignment; spindle assembly checkpoint; and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins; including ARHGEF2; BORA; BRCA1; CDC25B; DLGP5; HDAC6; KIF2A; LATS2; NDEL1; PARD3; PPP1R2; PLK1; RASSF1; TACC3; p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway; and particularly the checkpoint-response pathways critical for oncogenic transformation of cells; by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors; the protein phosphatase type 1 (PP1) isoforms; to inhibit their activity (By similarity). Necessary for proper cilia disassembly prior to mitosis (By similarity). Interacts with SIRT2 (By similarity). {ECO:0000250}.', 'MDKCKENCISGLKTTVPPGDGPKRVPVTQHFPAQHLPSANSGQAQRVLCPSNSSQRLPSHTQKLVSSHKPVQNLKQKQSQATSGPRPVSRPLSNTQQSEQPQPAAPGNNPEKEAASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKTQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGAVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVPEGARDLISRLLKHNPSHRPTLKEVLEHPWITANSKPASSHKKESTSKQP', 402, 'A5GFW1;', 'KD01440', 'Sus scrofa (Pig)', 'AURKA', '#Aurora kinase A#2.7.11.1#Aurora 2#Aurora/IPL1-related kinase 1#ARK-1#Aurora-related kinase 1#Serine/threonine-protein kinase 15#Serine/threonine-protein kinase 6#Serine/threonine-protein kinase aurora-A', '-', '-', '574063'),
(1441, 'O88554', 'Poly [ADP-ribose] polymerase 2', 'k', 63397, '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.', 'MAPRRQRSGSGRRVLNEAKKVDNGNKATEDDSPPGKKMRTCQRKGPMAGGKDADRTKDNRDSVKTLLLKGKAPVDPECAAKLGKAHVYCEGDDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKTGQHSLVTCSGDLNKAKEIFQKKFLDKTKNNWEDRENFEKVPGKYDMLQMDYAASTQDESKTKEEETLKPESQLDLRVQELLKLICNVQTMEEMMIEMKYDTKRAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALVEACNEFYTRIPHDFGLSIPPVIRTEKELSDKVKLLEALGDIEIALKLVKSERQGLEHPLDQHYRNLHCALRPLDHESNEFKVISQYLQSTHAPTHKDYTMTLLDVFEVEKEGEKEAFREDLPNRMLLWHGSRLSNWVGILSHGLRVAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAQGLLRGKHSTKGMGKMAPSPAHFITLNGSTVPLGPASDTGILNPEGYTLNYNEFIVYSPNQVRMRYLLKIQFNFLQLW', 559, 'O88554; Q99N29;', 'KD01441', 'Mus musculus (Mouse)', 'Parp2', '#Poly [ADP-ribose] polymerase 2#PARP-2#mPARP-2#2.4.2.30#ADP-ribosyltransferase diphtheria toxin-like 2#ARTD2#NAD(+) ADP-ribosyltransferase 2#ADPRT-2#Poly[ADP-ribose] synthase 2#pADPRT-2', '-', '-', '11546'),
(1442, 'Q9FHN8', 'Kinesin-like calmodulin-binding protein', 'GO:0003777', 143449, 'Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis. Possesses basal and microtubule-stimulated ATPase activities. {ECO:0000269|PubMed:14688294; ECO:0000269|PubMed:8636137; ECO:0000269|PubMed:9177205; ECO:0000269|PubMed:9634584; ECO:0000269|PubMed:9712269}.', 'MEGQRGSNSSLSSGNGTEVATDVSSCFYVPNPSGTDFDAESSSLPPLSPAPQVALSIPAELAAAIPLIDRFQVEAFLRLMQKQIQSAGKRGFFYSKKSSGSNVRERFTFEDMLCFQKDPIPTSLLKINSDLVSRATKLFHLILKYMGVDSSDRSTPPSLDERIDLVGKLFKKTLKRVELRDELFAQISKQTRHNPDRQYLIKAWELMYLCASSMPPSKDIGGYLSEYIHNVAHDATIEPDAQVLAVNTLKALKRSIKAGPRHTTPGREEIEALLTGRKLTTIVFFLDETFEEISYDMATTVSDAVEELAGTIKLSAFSSFSLFECRKVVSSSKSSDPGNEEYIGLDDNKYIGDLLAEFKAIKDRNKGEILHCKLVFKKKLFRESDEAVTDLMFVQLSYVQLQHDYLLGNYPVGRDDAAQLCALQILVGIGFVNSPESCIDWTSLLERFLPRQIAITRAKREWELDILARYRSMENVTKDDARQQFLRILKALPYGNSVFFSVRKIDDPIGLLPGRIILGINKRGVHFFRPVPKEYLHSAELRDIMQFGSSNTAVFFKMRVAGVLHIFQFETKQGEEICVALQTHINDVMLRRYSKARSAANSLVNGDISCSSKPQNFEVYEKRLQDLSKAYEESQKKIEKLMDEQQEKNQQEVTLREELEAIHNGLELERRKLLEVTLDRDKLRSLCDEKGTTIQSLMSELRGMEARLAKSGNTKSSKETKSELAEMNNQILYKIQKELEVRNKELHVAVDNSKRLLSENKILEQNLNIEKKKKEEVEIHQKRYEQEKKVLKLRVSELENKLEVLAQDLDSAESTIESKNSDMLLLQNNLKELEELREMKEDIDRKNEQTAAILKMQGAQLAELEILYKEEQVLRKRYYNTIEDMKGKIRVYCRIRPLNEKESSEREKQMLTTVDEFTVEHPWKDDKRKQHIYDRVFDMRASQDDIFEDTKYLVQSAVDGYNVCIFAYGQTGSGKTFTIYGHESNPGLTPRATKELFNILKRDSKRFSFSLKAYMVELYQDTLVDLLLPKSARRLKLEIKKDSKGMVFVENVTTIPISTLEELRMILERGSERRHVSGTNMNEESSRSHLILSVVIESIDLQTQSAARGKLSFVDLAGSERVKKSGSAGCQLKEAQSINKSLSALGDVIGALSSGNQHIPYRNHKLTMLMSDSLGGNAKTLMFVNVSPAESNLDETYNSLLYASRVRTIVNDPSKHISSKEMVRLKKLVAYWKEQAGKKGEEEDLVDIEEDRTRKDEADS', 1260, 'Q9FHN8; O22326; O23102; Q0WM77; Q39130; Q8VZV4;', 'KD01442', 'Arabidopsis thaliana (Mouse-ear cress)', 'KCBP', '#Kinesin-like calmodulin-binding protein#Protein ZWICHEL', '-', '-', '836723'),
(1443, 'Q02111', 'Protein kinase C theta type', 'c;k', 81573, 'Calcium-independent; phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non- redundant functions in T-cell receptor (TCR) signaling; including T-cells activation; proliferation; differentiation and survival; by mediating activation of multiple transcription factors such as NF-kappa-B; JUN; NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells; is required for the activation of NF-kappa-B and JUN; which in turn are essential for IL2 production; and participates to the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues; inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex; which then activates IKK complex; resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non- canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation; acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1;4;5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB; which is a prerequisite for the activation of TCR. During T-cells differentiation; plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses; and; in the development of inflammatory autoimmune diseases; is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation; mediates T-cell protective survival signal by phosphorylating BAD; thus protecting T-cells from BAD-induced apoptosis; and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets; regulates signal transduction downstream of the ITGA2B; CD36/GP4; F2R/PAR1 and F2RL3/PAR4 receptors; playing a positive role in ''outside-in'' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1; thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1; which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at ''Ser-504'' and ''Ser-532'' and negatively regulates its ability to phosphorylate PKB/AKT1. {ECO:0000269|PubMed:10746729; ECO:0000269|PubMed:12782715; ECO:0000269|PubMed:1508194; ECO:0000269|PubMed:15263025; ECO:0000269|PubMed:16493044; ECO:0000269|PubMed:19047061}.', 'MSPFLRIGLSNFDCGTCQACQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGRTEIWLELKPQGRMLMNARYFLEMSDTKDMSEFENEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARSLRDSEHIFREGPVEIGLPCSTKNETRPPCVPTPGKREPQGISWDSPLDGSNKSAGPPEPEVSMRRTSLQLKLKIDDFILHKMLGKGSFGKVFLAEFKRTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYAAEVILGLQFLHSKGIVYRDLKLDNILLDRDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLVYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEREAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPYDCSNFDKEFLSEKPRLSFADRALINSMDQNMFSNFSFINPGMETLICS', 707, 'Q02111;', 'KD01443', 'Mus musculus (Mouse)', 'Prkcq', '#Protein kinase C theta type#2.7.11.13#nPKC-theta', '-', '-', '18761'),
(1444, 'P36012', 'Histone H3-like centromeric protein CSE4', 'GO:0000776===GO:0000777===GO:0000780===k', 26841, '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. Required for functional chromatin architecture at the yeast 2-micron circle partitioning locus and promotes equal plasmid segregation. {ECO:0000269|PubMed:10454560; ECO:0000269|PubMed:10499801; ECO:0000269|PubMed:10891506; ECO:0000269|PubMed:11063678; ECO:0000269|PubMed:11606525; ECO:0000269|PubMed:15590827; ECO:0000269|PubMed:16207811; ECO:0000269|PubMed:16966420; ECO:0000269|PubMed:7698647; ECO:0000269|PubMed:9584087; ECO:0000269|PubMed:9741625}.', 'MSSKQQWVSSAIQSDSSGRSLSNVNRLAGDQQSINDRALSLLQRTRATKNLFPRREERRRYESSKSDLDIETDYEDQAGNLEIETENEEEAEMETEVPAPVRTHSYALDRYVRQKRREKQRKQSLKRVEKKYTPSELALYEIRKYQRSTDLLISKIPFARLVKEVTDEFTTKDQDLRWQSMAIMALQEASEAYLVGLLEHTNLLALHAKRITIMKKDMQLARRIRGQFI', 229, 'P36012; D6VXN8;', 'KD01444', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog#Chromosome segregation protein 4', '-', '-', '853817'),
(1445, 'Q96RK4', 'Bardet-Biedl syndrome 4 protein', 'GO:0003777', 58282, 'The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor; which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8; the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex; together with the LTZL1; controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. {ECO:0000269|PubMed:15107855; ECO:0000269|PubMed:17574030; ECO:0000269|PubMed:22072986}.', 'MAEERVATRTQFPVSTESQKPRQKKAPEFPILEKQNWLIHLHYIRKDYEACKAVIKEQLQETQGLCEYAIYVQALIFRLEGNIQESLELFQTCAVLSPQSADNLKQVARSLFLLGKHKAAIEVYNEAAKLNQKDWEISHNLGVCYIYLKQFNKAQDQLHNALNLNRHDLTYIMLGKIHLLEGDLDKAIEVYKKAVEFSPENTELLTTLGLLYLQLGIYQKAFEHLGNALTYDPTNYKAILAAGSMMQTHGDFDVALTKYRVVACAVPESPPLWNNIGMCFFGKKKYVAAISCLKRANYLAPFDWKILYNLGLVHLTMQQYASAFHFLSAAINFQPKMGELYMLLAVALTNLEDIENAKRAYAEAVHLDKCNPLVNLNYAVLLYNQGEKKNALAQYQEMEKKVSLLKDNSSLEFDSEMVEMAQKLGAALQVGEALVWTKPVKDPKSKHQTTSTSKPASFQQPLGSNQALGQAMSSAAAYRTLPSGAGGTSQFTKPPSLPLEPEPAVESSPTETSEQIREK', 519, 'Q96RK4; B4E178; Q53DZ5; Q8NHU9; Q96H45;', 'KD01445', 'Homo sapiens (Human)', 'BBS4', '#Bardet-Biedl syndrome 4 protein', '-', 'ENSG00000140463', '-'),
(1446, 'P40013', 'Protein BIM1', 'k', 38362, 'Binds microtubules.', 'MSAGIGESRTELLTWLNGLLNLNYKKIEECGTGAAYCQIMDSIYGDLPMNRVKFNATAEYEFQTNYKILQSCFSRHGIEKTVYVDKLIRCKFQDNLEFLQWLKKHWIRHKDESVYDPDARRKYRPIITNNSATKPRTVSNPTTAKRSSSTGTGSAMSGGLATRHSSLGINGSRKTSVTQGQLVAIQAELTKSQETIGSLNEEIEQYKGTVSTLEIEREFYFNKLRDIEILVHTTQDLINEGVYKFNDETITGHGNGNGGALLRFVKKVESILYATAEGFEMNDGEDELNDKNLGEHGTVPNQGGYANSNGEVNGNEGSNHDVIMQNDEGEVGVSNNLIIDEETF', 344, 'P40013; D3DLR4;', 'KD01446', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'BIM1', '#Protein BIM1', '-', '-', '856736'),
(1447, 'P40014', 'Kinetochore protein SPC25', 'GO:0000778===GO:0031262===GO:0000780===c;k', 25244, '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:12514103}.', 'MASIDAFSDLERRMDGFQKDVAQVLARQQNHARQQLQQFQAEMRQLHNQHQHLIDELQRLATQRTALQQQIHAAQQATNTTREQWRSYHERESELSRRQSTLAAQSRELDSLLQQRGKECVQLRARWAAQSGNDAAEVALYERLLQLRVLPGASDVHDVRFVFGDDSRCWIEVAMHGDHVIGNSHPALDPKSRATLEHVLTVQGDLAAFLVVARDMLLASL', 221, 'P40014; D3DLR6;', 'KD01447', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SPC25', '#Kinetochore protein SPC25', '-', '-', '856738'),
(1448, 'P40960', 'WD repeat-containing protein PAC11', 'GO:0005868', 60074, 'Required for viability in the absence of the kinesin- related CIN8 mitotic motor. May be a dynein intermediate chain.', 'MERLKQLEEKRRQLKELRERRKQASLFPGSETMGHHPTEVHAKATMVSVSVQTDMEEGSKIQEPQSAYLRRKEVITYDKGIQTDQIEEEQLQENENHTTTDAVAIETTAADENNKDKAENDQPRLELAKPFLVEEAAATLSNASFARLETEVSASGQQAPSNMQQDKDNLMQWNMVSENLQSETDCDCIAQEYDPGKGVLVVVYLRLPPADLQYASSEAAWSVVNVVKCDNASGRNGLLIDMVEFRGTRIMTATILRRYHPESNVISILLATLTGKIILYELRLKQKKPETPVVYVVQRNMVARHYFQHPVVAVIETSSVQDQERVLVAADNGNIMELSCLDLTVLRKPQQLRPVPLSQLLSLENDTCTYTERLQRLAKFDEVGIACMAYTSEDPQYVWIGGEDGGIYKVFWDQPGPLYLSLDNNGFQPAENHSTRVTGLEFHWDDARRLMLLLSCSTDWTVRLWDARAGKAIIGAPLLLGGPVLRARWLEKNNGGENSRTLRCQVWCADGRLVVVNWAFDAKTSLYTATVIS', 533, 'P40960; D6VTB1; Q03398;', 'KD01448', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'PAC11', '#WD repeat-containing protein PAC11', '-', '-', '852099'),
(1449, 'O94446', 'Histone acetyltransferase mst1', 'GO:0034508', 54390, 'Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4; H3; H2B; H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac; H4K8ac; H4K12ac and H4K16ac; histone H3 to form H3K14ac; and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me (By similarity). {ECO:0000250|UniProtKB:Q08649; ECO:0000269|PubMed:16199868}.', 'MSNDVDDESKIETKSYEAKDIVYKSKVFAFKDGEYRKAEILMIQKRTRGVVYYVHYNDYNKRLDEWITIDNIDLSKGIEYPPPEKPKKAHGKGKSSKRPKAVDRRRSITAPSKTEPSTPSTEKPEPSTPSGESDHGSNAGNESLPLLEEDHKPESLSKEQEVERLRFSGSMVQNPHEIARIRNINKICIGDHEIEPWYFSPYPKEFSEVDIVYICSFCFCYYGSERQFQRHREKCTLQHPPGNEIYRDDYISFFEIDGRKQRTWCRNICLLSKLFLDHKMLYYDVDPFLFYCMCRRDEYGCHLVGYFSKEKESSENYNLACILTLPQYQRHGYGKLLIQFSYELTKREHKHGSPEKPLSDLGLISYRAYWAEQIINLVLGMRTETTIDELANKTSMTTNDVLHTLQALNMLKYYKGQFIICISDGIEQQYERLKNKKRRRINGDLLADWQPPVFHPSQLRFGW', 463, 'O94446; Q9USC8;', 'KD01449', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mst1', '#Histone acetyltransferase mst1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}', '-', '-', '2543506'),
(1450, 'Q2NKY7', 'Septin-2', 'GO:0000777', 41572, 'Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules; thus facilitating efficient vesicle transport; and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase; may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. In cilia; required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein (By similarity). {ECO:0000250}.', 'MSKQQQTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIICYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQLQLQGGDGDSGVHGQHV', 361, 'Q2NKY7;', 'KD01450', 'Bos taurus (Bovine)', 'SEPT2', '#Septin-2', '-', '-', '511612'),
(1451, 'Q14141', 'Septin-6', 'GO:0000777===SCL', 49717, 'Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. May play a role in HCV RNA replication. {ECO:0000269|PubMed:17229681; ECO:0000269|PubMed:17803907}.', 'MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVRLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADAISKSELTKFKIKITSELVSNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCTE', 434, 'Q14141; Q5JTK0; Q969W5; Q96A13; Q96GR1; Q96P86; Q96P87;', 'KD01451', 'Homo sapiens (Human)', 'SEPT6', '#Septin-6', '-', 'ENSG00000125354', '-'),
(1452, 'Q61686', 'Chromobox protein homolog 5', 'GO:0000776===c;k', 22186, 'Component of heterochromatin that recognizes and binds histone H3 tails methylated at ''Lys-9'' (H3K9me); leading to epigenetic repression. In contrast; it is excluded from chromatin when ''Tyr-41'' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity). {ECO:0000250}.', 'MGKKTKRTADSSSSEDEEEYVVEKVLDRRMVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSEGNKRKSSFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKESAKS', 191, 'Q61686; Q9CS35; Q9CXD1;', 'KD01452', 'Mus musculus (Mouse)', 'Cbx5', '#Chromobox protein homolog 5#Heterochromatin protein 1 homolog alpha#HP1 alpha', '-', '-', '12419'),
(1453, 'Q8CG48', 'Structural maintenance of chromosomes protein 2', 'GO:0051383', 134239, 'Central component of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity). {ECO:0000250}.', 'MYVKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEAHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLRAEDTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACAEAQRVNTKSQSAFDLKKKNLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMIACKNDISKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKKDQDAFEAVKKAKEKLETEMKKLNYEENKEEKLLEKHRQLSRDINNLKGKHEALLAKFPNLQFAYKDPEKNWNRNSVKGLVASLINVKDNSTATALEVVAGERLYNVVVDTEVTAKKLLEKGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVDYKPELQKGMEFVFGTTFVCNNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAEKHLFGQPNSAYDFKTNNPKEAGQRLQKLQEVKEKLGRNVNLRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFVDGVSTVARFTQSQAGKIPKEAKSRGKEPN', 1191, 'Q8CG48; Q52KE9; Q61076; Q9CS17; Q9CSD8;', 'KD01453', 'Mus musculus (Mouse)', 'Smc2', '#Structural maintenance of chromosomes protein 2#SMC protein 2#SMC-2#Chromosome-associated protein E#FGF-inducible protein 16#XCAP-E homolog', '-', '-', '14211'),
(1454, 'Q8CG47', 'Structural maintenance of chromosomes protein 4', 'GO:0051383', 146895, 'Central component of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity). {ECO:0000250}.', 'MRRKGTKPSTACHQEEGPPPSQDGAHSDEEMEQPAGEAESAAPAKPPGEELDNRSLEEILNSIPPPPPPAMASEAGAPRLMITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVEVHFQKIIDKEGDDYEVLPNSNFYVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKGQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDIAISSCCHALDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRLFDLVKVKNEEIRQAFYFALRDTLVANNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTKSVAVNPKQIASKGLC', 1286, 'Q8CG47; Q8BTS7; Q8BTY9; Q99K21;', 'KD01454', 'Mus musculus (Mouse)', 'Smc4', '#Structural maintenance of chromosomes protein 4#SMC protein 4#SMC-4#Chromosome-associated polypeptide C#XCAP-C homolog', '-', '-', '70099'),
(1455, 'O14285', 'DASH complex subunit spc34', 'GO:0000778===GO:0042729===GO:0031134===GO:0000779===SCL', 19011, 'Component of the DASH complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. {ECO:0000269|PubMed:16079914}.', 'MSDLLNYLQSIAATSEKLLEPENPNAARFTDAVLHTHAITDLIRDTQKEELIAAEFKSLPKDWSERLASENPADYVACIEELLDIYPMQGGREYLETLVEKYNLHMSGIENLENVLLEQKEQLQQLEKRQTDQVSARENILQRETSEIQRLEREIEKVKQLIQS', 164, 'O14285;', 'KD01455', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'spc34', '#DASH complex subunit spc34#Outer kinetochore protein spc34', '-', '-', '2542102'),
(1456, 'P40969', 'Centromere DNA-binding protein complex CBF3 subunit B', 'GO:0000778===GO:0031518===k', 71358, 'Acts as a 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.', 'MFNRTTQLKSKHPCSVCTRRKVKCDRMIPCGNCRKRGQDSECMKSTKLITASSSKEYLPDLLLFWQNYEYWITNIGLYKTKQRDLTRTPANLDTDTEECMFWMNYLQKDQSFQLMNFAMENLGALYFGSIGDISELYLRVEQYWDRRADKNHSVDGKYWDALIWSVFTMCIYYMPVEKLAEIFSVYPLHEYLGSNKRLNWEDGMQLVMCQNFARCSLFQLKQCDFMAHPDIRLVQAYLILATTTFPYDEPLLANSLLTQCIHTFKNFHVDDFRPLLNDDPVESIAKVTLGRIFYRLCGCDYLQSGPRKPIALHTEVSSLLQHAAYLQDLPNVDVYREENSTEVLYWKIISLDRDLDQYLNKSSKPPLKTLDAIRRELDIFQYKVDSLEEDFRSNNSRFQKFIALFQISTVSWKLFKMYLIYYDTADSLLKVIHYSKVIISLIVNNFHAKSEFFNRHPMVMQTITRVVSFISFYQIFVESAAVKQLLVDLTELTANLPTIFGSKLDKLVYLTERLSKLKLLWDKVQLLDSGDSFYHPVFKILQNDIKIIELKNDEMFSLIKGLGSLVPLNKLRQESLLEEEDENNTEPSDFRTIVEEFQSEYNISDILS', 608, 'P40969; D6VZZ0;', 'KD01456', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CEP3', '#Centromere DNA-binding protein complex CBF3 subunit B#Centromere protein 3', '-', '-', '855204');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1457, 'Q39255', 'SKP1-like protein 1A', 'k', 17857, 'Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1; RBX1 and a F- box protein; it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends of the type of F- box protein. In the SCF complex; it serves as an adapter that links the F-box protein to CUL1. SCF(UFO) is required for vegetative and floral organ development as well as for male gametogenesis. SCF(TIR1) is involved in auxin signaling pathway. SCF(COI1) regulates responses to jasmonates. SCF(EID1) and SCF(AFR) are implicated in phytochrome A light signaling. SCF(ADO1); SCF(ADO2); SCF(ADO3) are related to the circadian clock. SCF(ORE9) seems to be involved in senescence. SCF(EBF1/EBF2) may regulate ethylene signaling. Plays a role during embryogenesis and early postembryonic development; especially during cell elongation and division. Contributes to the correct chromosome segregation during tetrad formation. {ECO:0000269|PubMed:10398681; ECO:0000269|PubMed:10500191; ECO:0000269|PubMed:10528262; ECO:0000269|PubMed:11526079; ECO:0000269|PubMed:12970487; ECO:0000269|PubMed:14688296}.', 'MSAKKIVLKSSDGESFEVEEAVALESQTIAHMVEDDCVDNGVPLPNVTSKILAKVIEYCKRHVEAAASKAEAVEGAATSDDDLKAWDADFMKIDQATLFELILAANYLNIKNLLDLTCQTVADMIKGKTPEEIRTTFNIKNDFTPEEEEEVRRENQWAFE', 160, 'Q39255; P92992;', 'KD01457', 'Arabidopsis thaliana (Mouse-ear cress)', 'SKP1A', '#SKP1-like protein 1A#SKP1-like 1#UFO-binding protein 1', '-', '-', '843928'),
(1458, 'P40957', 'Spindle assembly checkpoint component MAD1', 'GO:0000776===k', 87651, 'Central component of the spindle assembly checkpoint. Thought to recruit MAD2 to unattached kinetochores. During checkpoint activity; MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint complex (MCC). The formation of a MAD1- BUB1-BUB3 complex seems to be required for the spindle checkpoint mechanism.', 'MDVRAALQCFFSALSGRFTGKKLGLEIYSIQYKMSNSGGSSPFLESPGGSPDVGSTNGQSNRQIQALQFKLNTLQNEYEIEKLQLQKQTNILEKKYKATIDELEKALNDTKYLYESNDKLEQELKSLKERSANSMNDKDKCIEELRTTLQNKDLEMETLRQQYDSKLSKVTNQCDHFKLEAESSHSLLMKYEKEIKRQSVDIKDLQHQVMEKDDELSSVKASKMINSHPNYSTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQSQDTSTFWKLENEKLQNKLSQLHVLESQYENLQLENIDLKSKLTKWEIYNDSDDDDDNNVNNNDNNNNNKNDNNNDNNNDTSNNNNINNNNRTKNNIRNNPEEIIRDWKLTKKECLILTDMNDKLRLDNNNLKLLNDEMALERNQILDLNKNYENNIVNLKRLNHELEQQKSLSFEECRLLREQLDGLYSAQNNALLEVENSETHASNKNVNEDMNNLIDTYKNKTEDLTNELKKLNDQLLSNSNDVETQRKKRKLTSDQIGLNYSQRLNELQLENVSVSRELSKAQTTIQLLQEKLEKLTKLKEKKIRILQLRDGPFIKDQFIKKNKLLLLEKENADLLNELKKNNPAVETVPISVYDSLNFELKQFEQEVFKSNKRFSRLKQVFNNKSLEFIDVVNSLLGFKLEFQQDSRVKIFSCFKPEKYLIADLNENTLKSNLDADIEGWDDLMNLWVEDRGQLPCFLATITLRLWEQRQAK', 749, 'P40957; D6VU58;', 'KD01458', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MAD1', '#Spindle assembly checkpoint component MAD1#Mitotic arrest deficient protein 1', 'BIOMD0000000195,Tyson2001_Cell_Cycle_Regulation;', '-', '852794'),
(1459, 'Q3V300', 'Kinesin-like protein KIF22', 'GO:0003777', 73190, 'Kinesin family that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA (By similarity). {ECO:0000250}.', 'MSLRAKTCPQRREMASATSGPGRCVSKGGLGRRPPLARVRVAVRLRPFMDGETEAKELPCVRAIDSCSLEVANWKKYQETLKYQFDAFYGEKSTQQEVYVGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLAREESAEGRPWDVSVAMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLTQKPITSFSDFEQHFLPASRNRAVGATRLNQRSSRSHAVLLVKVDQRERLTPFRQREGKLYLIDLAGSEDNRRTGNQGIRLKESGAINTSLFVLGKVVDALNQGLPRIPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYQDTISALNFTARSKEVINRPFTNESLQPHALAPVKLSQKELLGPSEAKKAKGPEEESTGSPESTAAPASASQKLSLLQKLSNMDPAMLENLLSMERLLGSQGSQGTPLLNTPKRERMVLMKTVEEKNLEIERLKMKQKELEAKVLAQEAPDPREKENTPTILQPPASYSGTVAKPLKKAVVMPLQRIQKQRESSNQIQLLKKGPKRKLEPSPESEAVEKDEDYWEVQISPELLAHGRKKLLDLLNEGSARELRSLQRIGQKKAQLIVGWRELHGPFSEVEDLEQVEGISGKQVESFLKANLLSLAASQHSGPS', 660, 'Q3V300; O35232; Q99LC7;', 'KD01459', 'Mus musculus (Mouse)', 'Kif22', '#Kinesin-like protein KIF22', '-', '-', '110033'),
(1460, 'P32914', 'Transcription elongation factor SPT4', 'k', 11158, 'The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation; and plays a role in pre- mRNA processing. The complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene. Structural and functional component of the centromeric and heterochromatic loci linking chromatin structure with kinetochore function and gene silencing. {ECO:0000269|PubMed:12554661; ECO:0000269|PubMed:12556496; ECO:0000269|PubMed:15057281; ECO:0000269|PubMed:15780939; ECO:0000269|PubMed:16172632; ECO:0000269|PubMed:8483459; ECO:0000269|PubMed:9450930}.', 'MSSERACMLCGIVQTTNEFNRDGCPNCQGIFEEAGVSTMECTSPSFEGLVGMCKPTKSWVAKWLSVDHSIAGMYAIKVDGRLPAEVVELLPHYKPRDGSQVE', 102, 'P32914; D6VUJ8; Q0P6T7; Q45U23;', 'KD01460', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SPT4', '#Transcription elongation factor SPT4#Chromatin elongation factor SPT4', '-', '-', '852955'),
(1461, 'B4M3W0', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 23882, 'Acts as a component of the essential kinetochore- associated Ndc80 complex; which is required for chromosome segregation and spindle checkpoint activity during meiosis and mitosis. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. Participates in SAC signaling that responds specifically to disruptions in spindle microtubule dynamics (By similarity). {ECO:0000250|UniProtKB:Q9V3V7}.', 'MSNQFNTRKRLMAMLANEMRLEQEENAIAKQSAKFHSKFATTMENIKRQQHESKKLNTLLNQRRDEVEKRNALKNAVRDKLAEEEQHCAEMQAQLGKKKQERDKLIACAHILSEAANTYINRKALPERVKGVAVSPDNGQWIPFDFNAHDRQGLAALWTQVNRSSRNINKWRQLSSVGNSSMPAPSGKENANVSMTSVIEIDLTSPPSQK', 210, 'B4M3W0;', 'KD01461', 'Drosophila virilis (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6632413'),
(1462, 'O45952', 'Chromosome segregation and cytokinesis defective protein 1', 'k', 26782, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of chromosome segregation and cytokinesis during mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation. In the complex; it may be required to direct the Aurora B/air-2 to centromeric DNA. {ECO:0000269|PubMed:12707312}.', 'MPPRKIKKDPAVVAMADTLETRVKDLLEEYKKKLREVALQTAKAESDRIIATIKPKYRDMPIMEFLASPPDDFYIESGEEEEEGEAAVAVKQELPSEPDMEIDDAAAAQKTSIPIGQNSGRNTVQVKQEPEIDDDAAHETSIPIAPSGQNSGRNTAADEHRRNEIITPAGQVLPLPTLQPEKPFRAPHVDEEIAFSVNGSPLVLAGRTTATAAGKENRKKSKKSGAASKKAAAAAGPLQPETENAGTSV', 249, 'O45952;', 'KD01462', 'Caenorhabditis elegans', 'csc-1', '#Chromosome segregation and cytokinesis defective protein 1', '-', '-', '175006'),
(1463, 'Q2NKX8', 'DNA excision repair protein ERCC-6-like', 'GO:0000777===k', 141103, 'DNA helicase that acts as an essential component of the spindle assembly checkpoint. Contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. Acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. {ECO:0000269|PubMed:17218258}.', 'MEASRRFPEAEALSPEQAAHYLRYVKEAKEATKNGDLEEAFKLFNLAKDIFPNEKVLSRIQKIQEALEELAEQGDDEFTDVCNSGLLLYRELHNQLFEHQKEGIAFLYSLYRDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVKTFHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRGQEFVWDYVILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGSLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPYFLRRTKEDVQKKKSSNPEARLNEKNPDVDAICEMPSLSRKNDLIIWIRLVPLQEEIYRKFVSLDHIKELLMETRSPLAELGVLKKLCDHPRLLSARACCLLNLGTFSAQDGNEGEDSPDVDHIDQVTDDTLMEESGKMIFLMDLLKRLRDEGHQTLVFSQSRQILNIIERLLKNRHFKTLRIDGTVTHLLEREKRINLFQQNKDYSVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFKDSLIRQTTGEKKNPFRYFSKQELRELFTIEDLQNSVTQLQLQSLHAAQRKSDIKLDEHIAYLQSLGIAGISDHDLMYTCDLSVKEELDVVEESHYIQQRVQKAQFLVEFESQNKEFLMEQQRTRNEGAWLREPVFPSSTKKKCPKLNKPQPQPSPLLSTHHTQEEDISSKMASVVIDDLPKEGEKQDLSSIKVNVTTLQDGKGTGSADSIATLPKGFGSVEELCTNSSLGMEKSFATKNEAVQKETLQEGPKQEALQEDPLESFNYVLSKSTKADIGPNLDQLKDDEILRHCNPWPIISITNESQNAESNVSIIEIADDLSASHSALQDAQASEAKLEEEPSASSPQYACDFNLFLEDSADNRQNFSSQSLEHVEKENSLCGSAPNSRAGFVHSKTCLSWEFSEKDDEPEEVVVKAKIRSKARRIVSDGEDEDDSFKDTSSINPFNTSLFQFSSVKQFDASTPKNDISPPGRFFSSQIPSSVNKSMNSRRSLASRRSLINMVLDHVEDMEERLDDSSEAKGPEDYPEEGVEESSGEASKYTEEDPSGETLSSENKSSWLMTSKPSALAQETSLGAPEPLSGEQLVGSPQDKAAEATNDYETLVKRGKELKECGKIQEALNCLVKALDIKSADPEVMLLTLSLYKQLNNN', 1250, 'Q2NKX8; Q8NCI1; Q96H93; Q9NXQ8;', 'KD01463', 'Homo sapiens (Human)', 'ERCC6L', '#DNA excision repair protein ERCC-6-like#3.6.4.12#ATP-dependent helicase ERCC6-like#PLK1-interacting checkpoint helicase#Tumor antigen BJ-HCC-15', '-', 'ENSG00000186871', '-'),
(1464, 'Q9D0F1', 'Kinetochore protein NDC80 homolog', 'GO:0000776===GO:0000777===GO:0000778===GO:0000942===GO:0008608===GO:0051315===GO:0031262', 73962, '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}.', 'MKRSSVSTCGAGRLSMQELRTLDLNKPGLYTPQTKERSTFGKLSTHKPTSERKVSIFGKRTSGHGSRNSQLGIFSSSEKIKDPRPLNDKAFIQQCIRQLYEFLTENGYVYSVSMKSLQAPSTKEFLKIFAFLYGFLCPSYELPGTKCEEEVPRIFKALGYPFTLSKSSMYTVGAPHTWPHIVAALVWLIDCIKIDTAMKESSPLFDDGQLWGEETEDGIKHNKLFLEYTKKCYEKFMTGADSFEEEDAELQAKLKDLYKVDASKLESLEAENKALNEQIARLEEEREREPNRLMSLKKLKASLQADVQNYKAYMSNLESHLAVLKQKSNSLDEEIGRVEQECETVKQENTRLQSIVDNQKYSVADIERINHEKNELQQTINKLTKDLEAEQQQMWNEELKYARGKEAIEAQLAEYHKLARKLKLIPKGAENSKGYDFEIKFNPEAGANCLVKYRTQVYAPLKELLNESEEEINKALNKKRHLEDTLEQLNTMKTESKNTVRMLKEEIQKLDDLHQQAVKEAEEKDKKSASELESLEKHKHLLESGVNDGLSEAMDELDAVQREYQLTVKTTTEERRKVENNLQRLLEMVATHVGSLEKHLEEENAKADREYEEFMSEDLLENIREMAEKYKRNAAQLKAPDK', 642, 'Q9D0F1; Q3TQT6; Q3UWM5; Q99P70;', 'KD01464', 'Mus musculus (Mouse)', 'Ndc80', '#Kinetochore protein NDC80 homolog#Kinetochore protein Hec1#Kinetochore-associated protein 2', '-', '-', '67052'),
(1465, 'Q4R630', 'Kinetochore protein NDC80 homolog', 'GO:0000776===GO:0000777===GO:0031262', 73868, '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}.', 'MKRSSVSTGGAGRLSMQELRSQDVNKQGLYTPQTKERPTFGKLSINKPTSERKVSLFGKRTSGHGSRNSQLGIFSSSEKIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAMKESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLFNVDAFKLESLEAKNRALNEQIARLEQEREKEPNRLESLRKLKASLQGDVQKYQAYMSNLESHSAILDQKLNGLNEEIARVELECETIKQENTRLQNIIDNQKYSVADIERINHERNELQQTINKLTKDLEAEQQKLWNEELKYARGKEAIETQLAEYHKLARKLKLIPKGAENSKGYDFEIKFNPEAGANCLVKYRAQVYVPLKELLNETEEEINKARNKKMGLEDTLEQLNAMITESKRSVRTLKEEVQKLDDLYQQKIKEAEEEDEKCASELESLEKHKHLLESTVNQGLSEAMNELDAVQREYQLVVQTTTEERRKVGNNLQRLLEMVATHVGSVEKHLEEQIAKADREYEECMSEDLSENIKEIRDKYEKKAALIKSSGE', 642, 'Q4R630;', 'KD01465', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'NDC80', '#Kinetochore protein NDC80 homolog#Kinetochore protein Hec1#Kinetochore-associated protein 2', '-', '-', '101925531'),
(1466, 'Q9UTP3', 'Kinetochore protein fta6', 'GO:0000778===SCL', 6739, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. {ECO:0000269|PubMed:16079914}.', 'MEDKYILLSAVETFKSRLEELLMQSAKVQKQTMLRKELASSMNDMASTVQEALNKKKSS', 59, 'Q9UTP3;', 'KD01466', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'fta6', '#Kinetochore protein fta6#Sim4 complex subunit fta6#Sim4-mal2-associated protein 6', '-', '-', '2542646'),
(1467, 'Q8N4N8', 'Kinesin-like protein KIF2B', 'GO:0000777===GO:0003777===SCL===c;k;m', 76254, 'Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. Has microtubule depolymerization activity. {ECO:0000269|PubMed:17538014}.', 'MASQFCLPESPCLSPLKPLKPHFGDIQEGIYVAIQRSDKRIHLAVVTEINRENYWVTVEWVEKAVKKGKKIDLETILLLNPALDSAEHPMPPPPLSPLALAPSSAIRDQRTATKWVAMIPQKNQTASGDSLDVRVPSKPCLMKQKKSPCLWEIQKLQEQREKRRRLQQEIRARRALDVNTRNPNYEIMHMIEEYRRHLDSSKISVLEPPQEHRICVCVRKRPLNQRETTLKDLDIITVPSDNVVMVHESKQKVDLTRYLQNQTFCFDHAFDDKASNELVYQFTAQPLVESIFRKGMATCFAYGQTGSGKTYTMGGDFSGTAQDCSKGIYALVAQDVFLLLRNSTYEKLDLKVYGTFFEIYGGKVYDLLNWKKKLQVLEDGNQQIQVVGLQEKEVCCVEEVLNLVEIGNSCRTSRQTPVNAHSSRSHAVFQIILKSGRIMHGKFSLVDLAGNERGADTTKASRKRQLEGAEINKSLLALKECILALGQNKPHTPFRASKLTLVLRDSFIGQNSSTCMIATISPGMTSCENTLNTLRYANRVKKLNVDVRPYHRGHYPIGHEAPRMLKSHIGNSEMSLQRDEFIKIPYVQSEEQKEIEEVETLPTLLGKDTTISGKGSSQWLENIQERAGGVHHDIDFCIARSLSILEQKIDALTEIQKKLKLLLADLHVKSKVE', 673, 'Q8N4N8; Q96MA2; Q9BXG6;', 'KD01467', 'Homo sapiens (Human)', 'KIF2B', '#Kinesin-like protein KIF2B', '-', 'ENSG00000141200', '-'),
(1468, 'P26309', 'APC/C activator protein CDC20', 'k', 67360, 'Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). At the metaphase-to-anaphase transition; recognizes and binds proteins containing a D-box including the B-type cyclins CLB2 and CLB5; HSL1 and securin PDS1; and recruits them in a C-box-dependent manner to the APC/C for ubiquitination and subsequent proteolysis. Required for sister chromatid separation and disassembly of the mitotic spindle. Target of the spindle checkpoint pathway through participation in the mitotic checkpoint complex (MCC) and the MAD2-CDC20 subcomplex. MCC and presumably the MAD2-CDC20 subcomplex inhibit the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20 until proper attachment of all chromosomes to the spindle. {ECO:0000269|PubMed:12152084; ECO:0000269|PubMed:15198982; ECO:0000269|PubMed:15879521}.', 'MPESSRDKGNAAISGNRSVLSIASPTKLNILSSDWSRNQGKVSKNSLKRSSSLNIRNSKRPSLQASANSIYSRPKITIGAPPLIRRDSSFFKDEFDAKKDKATFSAYSSRSYPTIGSESVVSQTSLSQPTTSREVDEQFTVAADRYIPILQGASQNKVDPETLHEALPPPNASPISHLRAQTKIVFKQNVAEACGLDMNKRILQYMPEPPKCSSLRQKSYIMKKRTHYSYQQEQKIPDLIKLRKINTNPERILDAPGFQDDFYLNLLSWSKKNVLAIALDTALYLWNATTGDVSLLTDFENTTICSVTWSDDDCHISIGKEDGNTEIWDVETMSLIRTMRSGLGVRIGSLSWLDTLIATGSRSGEIQINDVRIKQHIVSTWAEHTGEVCGLSYKSDGLQLASGGNDNTVMIWDTRTSLPQFSKKTHTAAVKALSWCPYSPNILASGGGQTDKHIHFWNSITGARVGSINTGSQVSSLHWGQSHTSTNGGMMNKEIVATGGNPENAISVYNYETKFKVAEVVHAHEARICCSQLSPDGTTLATVGGDENLKFYKIFDPRCTGRSREDGLMDGMLGLIGKEGCRTNDKENRSKNSSEIHTRRPSSTSQYLIR', 610, 'P26309; D6VU31;', 'KD01468', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CDC20', '#APC/C activator protein CDC20#Cell division control protein 20', 'BIOMD0000000056,Chen2004 - Cell Cycle Regulation;BIOMD0000000195,Tyson2001_Cell_Cycle_Regulation;BIOMD0000000265,Conradie2010_RPControl_CellCycle;BIOMD0000000297,Ciliberto2003_Morphogenesis_Checkpoint;BIOMD0000000370,Vinod2011_MitoticExit;BIOMD0000000409,Queralt2006_MitoticExit_Cdc55DownregulationBySeparase;', '-', '852762'),
(1469, 'Q6TGU2', 'Nucleoporin seh1', 'GO:0000777===GO:0051315', 39817, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (By similarity). Required for the regulation of the TORC1 pathway by amino acids (By similarity). {ECO:0000250}.', 'MFVAKSIAADHKDLIHDVSYDFHGRRMATCSSDQSVKVWDKGDDGEWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKQRGQSHWIKRTTLVDSRTSVTDVKFAPKHMGLMLTTCSADGVVRIYEAPDVMNLSQWSLQHEISCKLACSCISWNPSSSRAHPPMIAVGGDDSNGAYSGKVQIHEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHVLAIATKDVRIFKLLPLRRESANSSGPTKFEVQVMAQFDSHNSQVWRVSWNITSTLLASSGDDGCVRLWKANYMDNWKCTGILRGDGSPVNGSSGPSAALSAVGVPGAAQMIVGAATAGRKKAQLMPG', 364, 'Q6TGU2; Q1LXR9;', 'KD01469', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'seh1l', '#Nucleoporin seh1#Nup107-160 subcomplex subunit seh1', '-', '-', '334749'),
(1470, 'Q6PG16', 'Holliday junction recognition protein', 'GO:0000777', 74199, 'Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerization and prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds Holliday junctions (By similarity). {ECO:0000250}.', 'MESMGRQDRRLHQQLKESSSRFQTLMKRLIAKYNQPFEDDPLVEMRTLTYETPQGLRVWGGKLMKKEDKEYTQVIDRLNGQAPEGDSESSGADTSLEENWPSCSSAMREASGDPRQRQPAVPGNTLETDLRRKYLTQVDILPQDEEYFKNAEKRGGKDTVMTWVPSVTSSVTPASGCQDAISAKSSGGPEVSALSSRGQGPSYPCPADMAIVARSDGLSLLGTSSNSVSSQSFEVDDLCNVTISDLYEGMMHSMSRLLRSKPSCIISTKTYINQSWKLRRRPSRKQGLHKNRTHCPRSKPSQRSARKGPASCSEPGKEAGILRDYGNLLHVAPHKTGLELKSVSLEGSKRQVHKSSPAWKELQMMPQKDLDLNRERENRVMTLQWLISPVKVVPRPRMLPSQVEKWYREIKIKFDKLHQEYCLSSGKQPRLTDPTESWAVDVYRSGSKSPGSRQDVETCRPSSPFGREKTERPGEALEDLRGNGKSVKTKSCLLRSCPSPEGSPSRSPSHSQLSSGLQEHNSEPTGKAVWPSTAISAPSIGSPGCGKDNYYELKKEFNRLYQKYCLSPQRAKVTSCGRVSPMKAAAALPCQSEHLKRLNPDSPQQSSQKRSISPGCHRRVLQDSTAQTASTLVRDSWLPTKRCKLSYPVACAHQAKFHDTSGASGWP', 667, 'Q6PG16; Q6BCZ4; Q8C9A7;', 'KD01470', 'Mus musculus (Mouse)', 'Hjurp', '#Holliday junction recognition protein#Fetal liver expressing gene 1 protein homolog#mFleg1', '-', '-', '212427'),
(1471, 'P40958', 'Mitotic spindle checkpoint component MAD2', 'k', 22284, 'Central component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Thought to be recruited to unattached kinetochores by MAD1. During checkpoint activity; MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint complex (MCC). MCC and presumably the MAD2-CDC20 subcomplex inhibit the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20. {ECO:0000269|PubMed:15879521; ECO:0000269|PubMed:8232541}.', 'MSQSISLKGSTRTVTEFFEYSINSILYQRGVYPAEDFVTVKKYDLTLLKTHDDELKDYIRKILLQVHRWLLGGKCNQLVLCIVDKDEGEVVERWSFNVQHISGNSNGQDDVVDLNTTQSQIRALIRQITSSVTFLPELTKEGGYTFTVLAYTDADAKVPLEWADSNSKEIPDGEVVQFKTFSTNDHKVGAQVSYKY', 196, 'P40958; D6VWF2;', 'KD01471', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MAD2', '#Mitotic spindle checkpoint component MAD2#Mitotic MAD2 protein', 'BIOMD0000000056,Chen2004 - Cell Cycle Regulation;', '-', '853422'),
(1472, 'Q1T769', 'Protein MIS12 homolog', 'GO:0051382===GO:0000444===SCL', 24691, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis. {ECO:0000250}.', 'MSVRPMAYETQFFGFTPQTCMLRIYLAFQDYLFEMMVVVESVILKKLEALPAVQISRFEIRKSTEKFLHFMKARFDQLFEKMEEVLLQLVLSIPDNVLLPEDRVHQQYPYSQEEFCALQDEISQLQQQCRAEAAAGQALRAELEEQRAVQAELEKVVQWFDGLENVCREHGTGNFKESLVFLTQNCKKLQDVLRDVEEKSKKIKKRQQLL', 210, 'Q1T769;', 'KD01472', 'Gallus gallus (Chicken)', 'MIS12', '#Protein MIS12 homolog', '-', '-', '693254'),
(1473, 'Q1T765', 'Centromere protein N', 'GO:0034508', 40344, 'Probable component of a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. {ECO:0000250}.', 'MDEVIVEYIRRTVLKIPRDEIMAVLQKWGFLSEAQLQTINFRQTKEGISHSVAQLCEESSADLKQAALLDIIYNHIYPNKRVWSVYHMNKTGEETDFFDFRDFKKKFRRQIQSALINVTINFREYEDNAIWIRIAWGTPYTKPNQYKTSYVVYHSQTPYVFISASVLRSNLPLLCQAMVVASNYHDIHEMELRSHCLNSLKDIVFKRYSQNFQTNYPLQERNVLTENVDLRINDENRSEKERIYRLNQESFGNGPQPKLDFAQYKLETMFKSDPKWDVLEKKEPFRCLVKFSSPHLLESLKSLAPAGLADAPLSPLLTCIPQKARNYFKIREKKSLHPGSFVSP', 344, 'Q1T765;', 'KD01473', 'Gallus gallus (Chicken)', 'CENPN', '#Centromere protein N#CENP-N', '-', '-', '693246'),
(1474, 'Q1T763', 'Centromere protein R', 'GO:0000777===SCL', 19562, 'Transcription coregulator that can have both coactivator and corepressor functions. Involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. Probable component of a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). {ECO:0000250}.', 'MSAKRSLKLDSVKKYNPVEASPLAKKKDLNSYSPTTGTCQISPFSSPTSHNAEDLRNGLSHGDETNSESRLSRRGQPQTAEDAFAELQSNVKSSLVRILKARENLTSLQALEGSRELENIIGVSDSSHILSAEVQKTQALMSQAEELQLLKRNHGQLPAREYAQPASSSAFLQLLLNSL', 179, 'Q1T763;', 'KD01474', 'Gallus gallus (Chicken)', 'CENPR', '#Centromere protein R#CENP-R#Nuclear receptor-interacting factor 3', '-', '-', '424689'),
(1475, 'Q3E7Y6', 'N-terminal-borealin-like protein', 'GO:0032133', 8547, 'Component of the aurora kinase complex; also called chromosomal passenger complex (CPC); essential for chromosome segregation and metaphase chromosome alignment. Mediates the SLI15-BIR1 interaction within the CPC. {ECO:0000269|PubMed:19158380}.', 'MIPALTPEERQKLRSAILHRMQLELETTEKLIENIKEETLKKLNLLQQPDATSAPQSKELIREVLEQEGRRIE', 73, 'Q3E7Y6; D3DLE8;', 'KD01475', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'NBL1', '#N-terminal-borealin-like protein', '-', '-', '2746858'),
(1476, 'Q96BK5', 'PIN2/TERF1-interacting telomerase inhibitor 1', 'GO:0000776===GO:0000777', 37035, '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. {ECO:0000269|PubMed:15381700; ECO:0000269|PubMed:17198684; ECO:0000269|PubMed:19117989; ECO:0000269|PubMed:19265708; ECO:0000269|PubMed:19393617; ECO:0000269|PubMed:19553660}.', 'MSMLAERRRKQKWAVDPQNTAWSNDDSKFGQRMLEKMGWSKGKGLGAQEQGATDHIKVQVKNNHLGLGATINNEDNWIAHQDDFNQLLAELNTCHGQETTDSSDKKEKKSFSLEEKSKISKNRVHYMKFTKGKDLSSRSKTDLDCIFGKRQSKKTPEGDASPSTPEENETTTTSAFTIQEYFAKRMAALKNKPQVPVPGSDISETQVERKRGKKRNKEATGKDVESYLQPKAKRHTEGKPERAEAQERVAKKKSAPAEEQLRGPCWDQSSKASAQDAGDHVQPPEGRDFTLKPKKRRGKKKLQKPVEIAEDATLEETLVKKKKKKDSK', 328, 'Q96BK5; B2R9B1; Q548A5; Q6QWG9; Q7Z7J8; Q96QD7; Q9HBU7; Q9NWW2;', 'KD01476', 'Homo sapiens (Human)', 'PINX1', '#PIN2/TERF1-interacting telomerase inhibitor 1#Liver-related putative tumor suppressor#Pin2-interacting protein X1#Protein 67-11-3#TRF1-interacting protein 1', '-', 'ENSG00000254093', '-'),
(1477, 'Q96JM3', 'Chromosome alignment-maintaining phosphoprotein 1', 'GO:0000777===GO:0034501===GO:0051315===GO:0031134===SCL===k;s', 89099, 'Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore. {ECO:0000269|PubMed:21063390}.', 'MEAFQELRKPSARLECDHCSFRGTDYENVQIHMGTIHPEFCDEMDAGGLGKMIFYQKSAKLFHCHKCFFTSKMYSNVYYHITSKHASPDKWNDKPKNQLNKETDPVKSPPLPEHQKIPCNSAEPKSIPALSMETQKLGSVLSPESPKPTPLTPLEPQKPGSVVSPELQTPLPSPEPSKPASVSSPEPPKSVPVCESQKLAPVPSPEPQKPAPVSPESVKATLSNPKPQKQSHFPETLGPPSASSPESPVLAASPEPWGPSPAASPESRKSARTTSPEPRKPSPSESPEPWKPFPAVSPEPRRPAPAVSPGSWKPGPPGSPRPWKSNPSASSGPWKPAKPAPSVSPGPWKPIPSVSPGPWKPTPSVSSASWKSSSVSPSSWKSPPASPESWKSGPPELRKTAPTLSPEHWKAVPPVSPELRKPGPPLSPEIRSPAGSPELRKPSGSPDLWKLSPDQRKTSPASLDFPESQKSSRGGSPDLWKSSFFIEPQKPVFPETRKPGPSGPSESPKAASDIWKPVLSIDTEPRKPALFPEPAKTAPPASPEARKRALFPEPRKHALFPELPKSALFSESQKAVELGDELQIDAIDDQKCDILVQEELLASPKKLLEDTLFPSSKKLKKDNQESSDAELSSSEYIKTDLDAMDIKGQESSSDQEQVDVESIDFSKENKMDMTSPEQSRNVLQFTEEKEAFISEEEIAKYMKRGKGKYYCKICCCRAMKKGAVLHHLVNKHNVHSPYKCTICGKAFLLESLLKNHVAAHGQSLLKCPRCNFESNFPRGFKKHLTHCQSRHNEEANKKLMEALEPPLEEQQI', 812, 'Q96JM3; B3KU06; Q6P181; Q8NC88; Q9BST0;', 'KD01477', 'Homo sapiens (Human)', 'CHAMP1', '#Chromosome alignment-maintaining phosphoprotein 1#Zinc finger protein 828', '-', 'ENSG00000198824', '-'),
(1478, 'Q91XJ0', 'Calcium-responsive transcription coactivator', 'GO:0000777===GO:0000780', 43999, 'Transcriptional activator which is required for calcium- dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex; a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons; transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx; RB1 is dephosphorylated by calcineurin; which leads to release of the repressor complex. At the same time; there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism; which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter; and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP. {ECO:0000269|PubMed:14716005; ECO:0000269|PubMed:15866867; ECO:0000269|PubMed:19081374}.', 'MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILDYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALSQSGSSQGLHPQGSLSDTVSTGLPPASLMQGQIGNGPNHVSMQQTAQSTLPTTSMSMSGSGHGTGPGYSHSGPTSQSVPMQGQGAISNYVSRTNINMQSNPVSMMHQQAARPTTTQRRVEASITRARRPLHDGPGWQGGSMMGQRPMAPYRPSQQGSSQQYLGQEEYYSEQYSHSQGSAEPMSQQYYPDGHSDYAYQQSSYTEQSYDRSFEDPTQHYYEGGNSQYSQQQAGYQQGTAQQQTYSQQQYPNQQSYPGQQQGYGPAQGAPSQYSGYQQGQGQQYGSYRTSQTGPSAQQQRPYGYEQGQYGNYQQ', 401, 'Q91XJ0;', 'KD01478', 'Rattus norvegicus (Rat)', 'Ss18l1', '#Calcium-responsive transcription coactivator#SS18-like protein 1', '-', '-', '192352'),
(1479, 'P62505', 'DASH complex subunit dad3', 'GO:0042729===GO:0031134', 9738, '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}.', 'MSLEEKRALQNQILAEYANLASNLETLVKVLQDMVYNPSNNILDSLRDLEKEVGLVYTLYKASVWAILADLENNQEGKSGMFQDES', 86, 'P62505; Q7LGI9;', 'KD01479', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dad3', '#DASH complex subunit dad3#Outer kinetochore protein dad3', '-', '-', '3361558'),
(1480, 'O60879', 'Protein diaphanous homolog 2', 'k', 125569, 'Could be involved in oogenesis. Involved in the regulation of endosome dynamics. Implicated in a novel signal transduction pathway; in which isoform 3 and CSK are sequentially activated by RHOD to regulate the motility of early endosomes through interactions with the actin cytoskeleton. {ECO:0000269|PubMed:12577064}.', 'MEQPGAAASGAGGGSEEPGGGRSNKRSAGNRAANEEETKNKPKLNIQIKTLADDVRDRITSFRKSTVKKEKPLIQHPIDSQVAMSEFPAAQPLYDERSLNLSEKEVLDLFEKMMEDMNLNEEKKAPLRNKDFTTKREMVVQYISATAKSGGLKNSKHECTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSNPVSWVNNFGHEGLGLLLDELEKLLDKKQQENIDKKNQYKLIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQPNMMTEIVKILSAICIVGEENILDKLLGAITTAAERNNRERFSPIVEGLENQEALQLQVACMQFINALVTSPYELDFRIHLRNEFLRSGLKTMLPDLKEKENDELDIQLKVFDENKEDDLTELSHRLNDIRAEMDDMNEVYHLLYNMLKDTAAENYFLSILQHFLLIRNDYYIRPQYYKIIEECVSQIVLHCSGMDPDFKYRQRLDIDLTHLIDSCVNKAKVEESEQKAAEFSKKFDEEFTARQEAQAELQKRDEKIKELEAEIQQLRTQAQVLSSSSGIPGPPAAPPLPGVGPPPPPPAPPLPGGAPLPPPPPPLPGMMGIPPPPPPPLLFGGPPPPPPLGGVPPPPGISLNLPYGMKQKKMYKPEVSMKRINWSKIEPTELSENCFWLRVKEDKFENPDLFAKLALNFATQIKVQKNAEALEEKKTGPTKKKVKELRILDPKTAQNLSIFLGSYRMPYEDIRNVILEVNEDMLSEALIQNLVKHLPEQKILNELAELKNEYDDLCEPEQFGVVMSSVKMLQPRLSSILFKLTFEEHINNIKPSIIAVTLACEELKKSESFNRLLELVLLVGNYMNSGSRNAQSLGFKINFLCKIRDTKSADQKTTLLHFIADICEEKYRDILKFPEELEHVESASKVSAQILKSNLASMEQQIVHLERDIKKFPQAENQHDKFVEKMTSFTKTAREQYEKLSTMHNNMMKLYENLGEYFIFDSKTVSIEEFFGDLNNFRTLFLEAVRENNKRREMEEKTRRAKLAKEKAEQEKLERQKKKKQLIDINKEGDETGVMDNLLEALQSGAAFRDRRKRIPRNPDNRRVPLERSRSRHNGAISSK', 1101, 'O60879; A6NG19; O60878; Q8WX06; Q8WX48; Q9UJL2;', 'KD01480', 'Homo sapiens (Human)', 'DIAPH2', '#Protein diaphanous homolog 2#Diaphanous-related formin-2#DRF2', '-', 'ENSG00000236256', '-'),
(1481, 'Q12262', 'Central kinetochore subunit MCM16', 'GO:0000778===k', 21138, 'Component of the central kinetochore; which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle- microtubule attachments and proper chromosome segregation. {ECO:0000269|PubMed:9862478}.', 'MTNSSEKQWERIQQLEKEHVEVYRELLITLDRLYLIRKHNHAVILSHTQQRLLEIRHQLQINLEKTALLIRLLEKPDNTNVLFTKLQNLLEESNSLDYELLQSLGAQSSLHKQLIESRAERDELMSKLIELSSKFPKPTIPPDDSDTAGKQVEVEKENETIQELMIALQIHSGYTNISYTI', 181, 'Q12262; D6W454;', 'KD01481', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MCM16', '#Central kinetochore subunit MCM16#Minichromosome maintenance protein 16', '-', '-', '856159'),
(1482, 'Q4R5U8', 'Centromere protein T', 'GO:0000777===GO:0051382', 60497, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome- associated complex that binds specifically to histone H3- containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis (By similarity). {ECO:0000250}.', 'MADHNPDGDPTPRTLLRRVLDTADPRTPRRPRSARAGAQRALLETASSRRLSGQTKTIAKGRSRGARSIGRSAHVQARGHLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQVVQPSRRESSRGSLELQLPELEPSTTLAPGLLAPGRRKQRLRLSMFQQGVDQGLPLSQEPQGNADASSLTSSLNLTFATPLQPQSVQRPGLARRPPARRAVDVGAFLRDLRDTSLAPPNIVLEDTQPFSQPTVGSPNVYHSLPCTPHTGAEDAEQAAGRRTQSSGPGLQNNSPGKPAQFLAGEAEEVDAFALGFLSTSSGVSGEDEVEPLHNGVEEAEKKMKEEGVSVSEMEATGAQGPSRAEEPEGHTQVTEAEGSQGTAEAEGPGASSGDEDASSRAASPELASSTPESLQARRHHQFPEPAPPPGAAVLSSEPAEPLLVRCPPRSRTTGPRPRQDPHKAGLSHYVKLFSFFAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVLVERHLPLEYRQLLIPCAYSGNSVFPAQ', 561, 'Q4R5U8; Q4R7F5;', 'KD01482', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'CENPT', '#Centromere protein T#CENP-T', '-', '-', '101926328'),
(1483, 'Q8IWS0', 'PHD finger protein 6', 'GO:0000777===SCL===k', 41290, 'Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. {ECO:0000269|PubMed:23229552}.', 'MSSSVEQKKGPTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMVYCRKHKKTAHNSEADLEESFNEHELEPSSPKSKKKSRKGRPRKTNFKGLSEDTRSTSSHGTDEMESSSYRDRSPHRSSPSDTRPKCGFCHVGEEENEARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMKCTLCSQPGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNHSGNDERDEEDEERESKSRGKVEIDQQQLTQQQLNGN', 365, 'Q8IWS0; A8K230; B4E0G4; D3DTG3; E9PC97; Q5JRC7; Q5JRC8; Q96JK3;Q9BRU0;', 'KD01483', 'Homo sapiens (Human)', 'PHF6', '#PHD finger protein 6#PHD-like zinc finger protein', '-', 'ENSG00000156531', '-'),
(1484, 'Q5BH14', 'Probable kinetochore protein nuf2', 'GO:0000777', 54529, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MAYNHRISQQFHSSQQHGRGSRKKEDENDALMRLPDKEIAGCINDIGIPFTAADLIKPNPQQVQMVLEWFAELLMNTTRETVEPAMRAAADDICGDFPDIVPTDTRNLMGFFVNMRRLMAECGVNDFTFTDLTKPTHDRLVKIFSYLINFVRFRESQTAVIDEHFNKTEKTKQRIETLYTENQEMEQRLEEMRRVLKANEAEVKEKVRRNDELKSRLRELGRTQEKVAETLERVKAEKARQQNLLKEKMERTVRTRQEVEKLRPYVMESPASLQSSLTELSESLLREKNQIDAMEKRARALQTSSDTFTVVSNDVQACIKLLEDIAVELQKEEDEESRASRNKEAISERGNNVREVEQTEKLLQRQLARWNERIEALRNTAHEKAQVAQKRMEELREVQIKLREERTEKQRDMERRRIRIEQTEKKMADLKESIETEIQSAHDEYLKLESHIKLYITEMEKSL', 463, 'Q5BH14; C8VQ44;', 'KD01484', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'nuf2', '#Probable kinetochore protein nuf2', '-', '-', '2875944'),
(1485, 'Q9P7X7', 'Actin-related protein 4', 'GO:0008608===GO:0031134', 48773, 'Chromatin interaction component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Is required for NuA4 complex integrity. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair (By similarity). {ECO:0000250}.', 'MTSAFYGGDEVSAIVIDPGSKWTRIGFSGEDIPKCVLPSYCGEFSDGRRLFGEEYIYKSNPGMEIKNAIRNGWVENWDVTVDLWRYGLEQQLKTNPLEHPILITEPFDNPPENRVKTLETMFESLRCPATYLAKQETCAAFASGKGTACLVDIGAERSSVSAIYDGFVLQKGYQVQHFSGNAINDILAQTLRDKNFEVMPKYLVKSKNPVEIGQPANCELRPRDTTDSYHQFQVQRVYDEWKEECALISDVPFSSETTIAESEFEFPDGSRMMFGAERYQIPEHLFVPGSDEEMNEEPSKPIEQTENNEVSQQDSSVTNTSSRILGIPQLFQNCISECDVDIRASLLNNVIVCGGTSLMQGFSLRLQNELSKLYPGSRLKIHASGHVVERSYASWLGGSILSSLGTFHQLWISRQEYEEHGSDRLALIEKRCK', 433, 'Q9P7X7;', 'KD01485', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'alp5', '#Actin-related protein 4#Actin-like protein arp4#Actin-like protein 4#Altered polarity protein 5', '-', '-', '2541318'),
(1486, 'Q924W5', 'Structural maintenance of chromosomes protein 6', 'k', 127198, 'Core component of the SMC5-SMC6 complex; a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components (By similarity). {ECO:0000250}.', 'MAKRKEENFCSPENAKRPRQEELEDFDKDGDEDECTISFTNGTSTLTAAEVGIIESIQLRNFMCHSMLGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGKAVATNRGSSLKGFVKAGQNSADISITLRNRGDDAFRANVYGDSIVVQQHISVDGSRSYKLKSEKGTVVSTRKEELIAILDHFNIQVDNPVSVLTQEMSKQFLQSKNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLSTMKTNLEYLKHEMAWAVVNEIEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAFNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRICWLKEKVKALQDQEHTVNQEAEQFEQAIEKDKQEHGRVRKEDIEVRHALNYNQRQLKELKDSKTDRLKRFGPHVPALLEAIDDAYRRRQFTHKPIGPLGACIHLRDPELALAIESCLKGLLQAYCCHNHADERVLQSLMKKFYPPGTSRPQIIVSEFRDEVYDVRLRAAYHPEFPTVLTALEIDNAVVANSLIDMRSIETVLLIKNNSVARAVMQSQKPPKNCREAFTADGDQVFAGRYYSSESTRPKFLSRDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQHYEDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARETYLDLDNKVRTLRRFIKLLEEIMTHRYKTYQQFRRCLTLRCKLYFDNLLSQRAYCGKMNFDHKNETLSITVQPGEGNKASFNDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQRFRQFILLTPQSMSSLPSSKLIRILRMSDPERGQTTLPFRPVTQEEDDSAS', 1097, 'Q924W5; Q3UFI5; Q3UX54; Q499E1; Q5DTN2; Q8BFU9; Q8R0T4; Q9CSK7;Q9CV94; Q9CZZ5; Q9D169; Q9D6B2;', 'KD01486', 'Mus musculus (Mouse)', 'Smc6', '#Structural maintenance of chromosomes protein 6#SMC protein 6#SMC-6#mSMC6', '-', '-', '67241'),
(1487, 'Q9SV36', 'Armadillo repeat-containing kinesin-like protein 1', 'GO:0003777', 117375, 'Involved in the control of root hair tip growth by promoting microtubule depolymerization and limiting the accumulation of endoplasmic microtubules. In vitro; binds to polymerized actin through ARM repeats; and to polymerized tubulin through N-terminal motor domain. {ECO:0000269|PubMed:17957256; ECO:0000269|PubMed:17971038}.', 'MSSSNSSSAVRSSAKHAAERIQQHLPPNSNHAVSLSSSSLNLPARTSIVAPGIAHSSRLKDRPSASSSSSSSSVSASSPSTRRSGTPVRRSQSKDFDDDNDPGRVRVSVRVRPRNGEELISDADFADLVELQPEIKRLKLRKNNWNSESYKFDEVFTDTASQKRVYEGVAKPVVEGVLSGYNGTIMAYGQTGTGKTYTVGKIGKDDAAERGIMVRALEDILLNASSASISVEISYLQLYMETIQDLLAPEKNNISINEDAKTGEVSVPGATVVNIQDLDHFLQVLQVGETNRHAANTKMNTESSRSHAILTVYVRRAMNEKTEKAKPESLGDKAIPRVRKSKLLIVDLAGSERINKSGTDGHMIEEAKFINLSLTSLGKCINALAEGSSHIPTRDSKLTRLLRDSFGGSARTSLIITIGPSARYHAETTSTIMFGQRAMKIVNMVKLKEEFDYESLCRKLETQVDHLTAEVERQNKLRNSEKHELEKRLRECENSFAEAEKNAVTRSKFLEKENTRLELSMKELLKDLQLQKDQCDLMHDKAIQLEMKLKNTKQQQLENSAYEAKLADTSQVYEKKIAELVQRVEDEQARSTNAEHQLTEMKNILSKQQKSIHEQEKGNYQYQRELAETTHTYESKIAELQKKLEGENARSNAAEDQLRQMKRLISDRQVISQENEEANELKIKLEELSQMYESTVDELQTVKLDYDDLLQQKEKLGEEVRDMKERLLLEEKQRKQMESELSKLKKNLRESENVVEEKRYMKEDLSKGSAESGAQTGSQRSQGLKKSLSGQRATMARLCEEVGIQKILQLIKSEDLEVQIQAVKVVANLAAEEANQVKIVEEGGVEALLMLVQSSQNSTILRVASGAIANLAMNEKSQDLIMNKGGAQLLAKMVTKTDDPQTLRMVAGALANLCGNEKFLKLLKEEEGIKGLLTMAQSGNIDIIAQVARGMANFAKCETREIMQGRRKGRSLLLEEGVLEWLTSNSHIDSASTQRHIELALCHLAQNEENANDFKRTGSVTEIVRISVESSRDDIRSLAKKILKTNPYFSS', 1051, 'Q9SV36; A9CP38; F4JE41;', 'KD01487', 'Arabidopsis thaliana (Mouse-ear cress)', 'ARK1', '#Armadillo repeat-containing kinesin-like protein 1#Protein MORPHOGENESIS OF ROOT HAIR 2', '-', '-', '824652'),
(1488, 'Q12248', 'DASH complex subunit DAD1', 'GO:0008608===GO:0051987===GO:0042729===SCL===c;k', 10516, '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}.', 'MMASTSNDEEKLISTTDKYFIEQRNIVLQEINETMNSILNGLNGLNISLESSIAVGREFQSVSDLWKTLYDGLESLSDEAPIDEQPTLSQSKTK', 94, 'Q12248; D6VS02;', 'KD01488', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DAD1', '#DASH complex subunit DAD1#DUO1 and DAM1-interacting protein 1#Outer kinetochore protein DAD1', '-', '-', '851579'),
(1489, 'P63167', 'Dynein light chain 1; cytoplasmic', 'GO:0000776===GO:0005868===c;k;m;s', 10366, 'Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.', 'MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG', 89, 'P63167; Q15701;', 'KD01489', 'Homo sapiens (Human)', 'DYNLL1', '#Dynein light chain 1; cytoplasmic#8 kDa dynein light chain#DLC8#Dynein light chain LC8-type 1#Protein inhibitor of neuronal nitric oxide synthase#PIN', '-', 'ENSG00000248008', '-'),
(1490, 'P63169', '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, 'P63169; Q15701;', 'KD01490', 'Oryctolagus cuniculus (Rabbit)', 'DYNLL1', '#Dynein light chain 1; cytoplasmic#8 kDa dynein light chain#DLC8#Dynein light chain LC8-type 1#Protein inhibitor of neuronal nitric oxide synthase#PIN', '-', '-', '100008650'),
(1491, 'P63168', '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, 'P63168; Q15701; Q3UGE7;', 'KD01491', 'Mus musculus (Mouse)', 'Dynll1', '#Dynein light chain 1; cytoplasmic#8 kDa dynein light chain#DLC8#Dynein light chain LC8-type 1#Protein inhibitor of neuronal nitric oxide synthase#PIN#mPIN', '-', '-', '56455'),
(1492, 'P25651', 'Monopolin complex subunit CSM1', 'GO:0033551===k', 21751, 'Component of the monopolin complex which promotes monoorientation during meiosis I; required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication. {ECO:0000269|PubMed:11470404; ECO:0000269|PubMed:12689592; ECO:0000269|PubMed:15023545; ECO:0000269|PubMed:16487579; ECO:0000269|PubMed:18997772}.', 'MDPLTVYKNSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKELKTQTSQQAENSEVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGGSSDDYSIMDYKLGFVKGQAQVTEVIYAPVLKQRSTEELYSLQSKLPEYLFETLSFPLSSLNQFYNKIAKSLNKKREKKDETE', 190, 'P25651; D6VR86;', 'KD01492', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CSM1', '#Monopolin complex subunit CSM1#Chromosome segregation in meiosis protein 1', '-', '-', '850447'),
(1493, 'P67829', 'Casein kinase I isoform alpha', 'GO:0000777', 37567, '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 (By similarity). {ECO:0000250}.', 'MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF', 325, 'P67829; P35506;', 'KD01493', 'Ovis aries (Sheep)', 'CSNK1A1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', '-', '101120241'),
(1494, 'P36022', 'Dynein heavy chain; cytoplasmic', 'GO:0003777===GO:0005868', 471348, 'Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle. {ECO:0000269|PubMed:15642746}.', 'MCKNEARLANELIEFVAATVTGIKNSPKENEQAFIDYLHCQYLERFQFFLGLLDGREFDTLFVFLFEELDRTIVTIDIGEEAIYDANLANKKYSTLLIIKSRSVIVDAEPIATQISAIYLPGPVNAGNLASIITHGVSSVFGQLIKSDTKTYSVETIDKTRRKLDDISKQFQQLHTSIETPDLLAMVPSIIKLAVSKGATSHDYANYLPSNDLESMRFLNILQSIANKWFLVLKQTLAIDRDIKNGSFLDEVEFWSNFYEVLKSLIEQTQSQEFQVCLSVLTNAKRFHNLTNLLNEGSLSDKFKLADKYNQFLSSIPIDEVRQASNLEDLQELFPVLASSLKKFRYSGYPVQRFVVLMDKISQEVMDAILSNLSDLFQLEYGSFLGLYEKSAGMIEEWDDIVQDVNLLIREDLRKRAPQELLIQKLTFTSASVKATLDEILSTRKRFFSLAETIKSISPSTYHEEIQRLYHPFEQIHDISVNFRLKLEQAESEFSKNMLDLEKKLQNTLASFMDSDHCPTEKLSYLVKFKPLMELCPRIKVKVLENQQILLLEIKKDIRQLETGLELLPKILHVEALNNIPPISARISYFLNVQSRIDNIVQYLEALFGSNWNDTLEGRSISTSIVQLRKETNPHDVFLHWLGNFPEKATANLLTTPILKLIRNNEDDYELKVNFDFALAAAYSELRSLTYMAFQVPSHIVRIARTYMYLYPRAINLVELIQTFFSLSKSLSYTFYTNIFLKRNVQTVWLLLQQILITPWESLQEESSEMSCSVHSLARLEKSIDGILSDYQILKNSEPQFAKEFSGLKSFDGTADDLHEVEEIISNIQAIFENLFTKGLTNVSDHISTFNNLIISIILEKVRLNLKKMHFPKHVLKLSFNEGRITSSPSLAAMKRSLLKDIEALLNKVVLINFLHDPDHPLSTTLTFNSLVIKLKDDIQNCIEQVQNLHCKINSYVKEWQKMEFLWQITEEAFLEVVDNSTQRCFGILKGLLDSQSKFDLIISRNNFSKNLVLHTEDAQRHIRSKMDSWILYVSKHLLTIYERDARKLHEDMNRDREAVEDMDINFTSLKNITVIIEAVNVNKRHLTERDIQIKLLGSVMRALTKLKVRFPSHFVYIDQLDNDFSSLRQSLSYVEQELQKHRVVIAKSLEEGVENINNLSQSLNESWSVRKPISPTLTPPEALKILEFFNESITKLKKKMHSVAAAAKMLLIPVVLNDQLTHVVEEVKTYDLVWRSIKNLWEDVQRTFETPWCRVDVLLLQSDLANFLRRADELPRAVKQFEMYKSLFSQVNMLTSVNKILVELKDGALKPRHWNMIFRDIGKRQIQKNLLDKLEFSLKDVMVLNLTLNEILLTKIIERAQKEFVIEKSLNRIKKFWKEAQYEVIEHSSGLKLVREWDVLEQACKEDLEELVSMKASNYYKIFEQDCLDLESKLTKLSEIQVNWVEVQFYWLDLYGILGENLDIQNFLPLETSKFKSLTSEYKMITTRAFQLDTTIEVIHIPNFDTTLKLTIDSLKMIKSSLSTFLERQRRQFPRFYFLGNDDLLKIIGSGKHHDQVSKFMKKMFGSIESIIFLEDFITGVRSVEGEVLNLNEKIELKDSIQAQEWLNILDTEIKLSVFTQFRDCLGQLKDGTDIEVVVSKYIFQAILLSAQVMWTELVEKCLQTNQFSKYWKEVDMKIKGLLDKLNKSSDNVKKKIEALLVEYLHFNNVIGQLKNCSTKEEARLLWAKVQKFYQKNDTLDDLNSVFISQSGYLLQYKFEYIGIPERLIYTPLLLIGFATLTDSLHQKYGGCFFGPAGTGKTETVKAFGQNLGRVVVVFNCDDSFDYQVLSRLLVGITQIGAWGCFDEFNRLDEKVLSAVSANIQQIQNGLQVGKSHITLLEEETPLSPHTAVFITLNPGYNGRSELPENLKKSFREFSMKSPQSGTIAEMILQIMGFEDSKSLASKIVHFLELLSSKCSSMNHYHFGLRTLKGVLRNCSPLISEFGEGEKTVVESLKRVILPSLGDTDELVFKDELSKIFDSAGTPLNSKAIVQCLKDAGQRSGFSMSEEFLKKCMQFYYMQKTQQALILVGKAGCGKTATWKTVIDAMAIFDGHANVVYVIDTKVLTKESLYGSMLKATLEWRDGLFTSILRRVNDDITGTFKNSRIWVVFDSDLDPEYVEAMNSVLDDNKILTLPNGERLPIPPNFRILFETDNLDHTTPATITRCGLLWFSTDVCSISSKIDHLLNKSYEALDNKLSMFELDKLKDLISDSFDMASLTNIFTCSNDLVHILGVRTFNKLETAVQLAVHLISSYRQWFQNLDDKSLKDVITLLIKRSLLYALAGDSTGESQRAFIQTINTYFGHDSQELSDYSTIVIANDKLSFSSFCSEIPSVSLEAHEVMRPDIVIPTIDTIKHEKIFYDLLNSKRGIILCGPPGSGKTMIMNNALRNSSLYDVVGINFSKDTTTEHILSALHRHTNYVTTSKGLTLLPKSDIKNLVLFCDEINLPKLDKYGSQNVVLFLRQLMEKQGFWKTPENKWVTIERIHIVGACNPPTDPGRIPMSERFTRHAAILYLGYPSGKSLSQIYEIYYKAIFKLVPEFRSYTEPFARASVHLYNECKARYSTGLQSHYLFSPRELTRLVRGVYTAINTGPRQTLRSLIRLWAYEAWRIFADRLVGVKEKNSFEQLLYETVDKYLPNQDLGNISSTSLLFSGLLSLDFKEVNKTDLVNFIEERFKTFCDEELEVPMVIHESMVDHILRIDRALKQVQGHMMLIGASRTGKTILTRFVAWLNGLKIVQPKIHRHSNLSDFDMILKKAISDCSLKESRTCLIIDESNILETAFLERMNTLLANADIPDLFQGEEYDKLLNNLRNKTRSLGLLLDTEQELYDWFVGEIAKNLHVVFTICDPTNNKSSAMISSPALFNRCIINWMGDWDTKTMSQVANNMVDVIPMEFTDFIVPEVNKELVFTEPIQTIRDAVVNILIHFDRNFYQKMKVGVNPRSPGYFIDGLRALVKLVTAKYQDLQENQRFVNVGLEKLNESVLKVNELNKTLSKKSTELTEKEKEARSTLDKMLMEQNESERKQEATEEIKKILKVQEEDIRKRKEVVMKSIQDIEPTILEAQRGVKNIKKQQLTEIRSMVNPPSGVKIVMEAVCAILGYQFSNWRDIQQFIRKDDFIHNIVHYDTTLHMKPQIRKYMEEEFLSDPNFTYETINRASKACGPLYQWVNAQINFSKVLENVDPLRQEMKRIEFESLKTKANLLAAEEMTQDLEASIEVSKRKYSLLIRDVEAIKTEMSNVQANLDRSISLVKSLTFEKERWLNTTKQFSKTSQELIGNCIISSIYETYFGHLNERERADMLVILKRLLGKFAVKYDVNYRFIDYLVTLDEKMKWLECGLDKNDYFLENMSIVMNSQDAVPFLLDPSSHMITVISNYYGNKTVLLSFLEEGFVKRLENAIRFGSVVIIQDGEFFDPIISRLISREFNHAGNRVTVEIGDHEVDVSGDFKLFIHSCDPSGDIPIFLRSRVRLVHFVTNKESIETRIFDITLTEENAEMQRKREDLIKLNTEYKLKLKNLEKRLLEELNNSQGNMLENDELMVTLNNLKKEAMNIEKKLSESEEFFPQFDNLVEEYSIIGKHSVKIFSMLEKFGQFHWFYGISIGQFLSCFKRVFIKKSRETRAARTRVDEILWLLYQEVYCQFSTALDKKFKMIMAMTMFCLYKFDIESEQYKEAVLTMIGVLSESSDGVPKLTVDTNNDLRYLWDYVTTKSYISALNWFKNEFFVDEWNIADVVANSENNYFTMASERDVDGTFKLIELAKASKESLKIIPLGSIENLNYAQEEISKSKIEGGWILLQNIQMSLSWVKTYLHKHVEETKAAEEHEKFKMFMTCHLTGDKLPAPLLQRTDRFVYEDIPGILDTVKDLWGSQFFTGKISGVWSVYCTFLLSWFHALITARTRLVPHGFSKKYYFNDCDFQFASVYLENVLATNSTNNIPWAQVRDHIATIVYGGKIDEEKDLEVVAKLCAHVFCGSDNLQIVPGVRIPQPLLQQSEEEERARLTAILSNTIEPADSLSSWLQLPRESILNYERLQAKEVASSTEQLLQEM', 4092, 'P36022; D6VXB5;', 'KD01494', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DYN1', '#Dynein heavy chain; cytoplasmic#Dynein heavy chain; cytosolic#DYHC', '-', '-', '853928'),
(1495, 'P67828', 'Casein kinase I isoform alpha', 'GO:0000777', 37567, '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 (By similarity). {ECO:0000250}.', 'MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF', 325, 'P67828; P35506;', 'KD01495', 'Oryctolagus cuniculus (Rabbit)', 'CSNK1A1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', '-', '100009227'),
(1496, 'P63165', 'Small ubiquitin-related modifier 1', 'k;m', 11557, 'Ubiquitin-like protein that can be covalently attached to proteins as a monomer or 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 E3 ligases 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. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. {ECO:0000269|PubMed:18408734; ECO:0000269|PubMed:18538659; ECO:0000269|PubMed:21965678; ECO:0000269|PubMed:9019411; ECO:0000269|PubMed:9162015}.', 'MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV', 101, 'P63165; A8MUS8; B2R4I5; P55856; Q6FGG0; Q6NZ62; Q93068;', 'KD01496', 'Homo sapiens (Human)', 'SUMO1', '#Small ubiquitin-related modifier 1#SUMO-1#GAP-modifying protein 1#GMP1#SMT3 homolog 3#Sentrin#Ubiquitin-homology domain protein PIC1#Ubiquitin-like protein SMT3C#Smt3C#Ubiquitin-like protein UBL1', '-', 'ENSG00000241721', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1497, 'P67827', 'Casein kinase I isoform alpha', 'GO:0000777', 37567, '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 (By similarity). {ECO:0000250}.', 'MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF', 325, 'P67827; P35506; Q9GLY1; Q9GLY2; Q9GLY3;', 'KD01497', 'Bos taurus (Bovine)', 'CSNK1A1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', '-', '282684'),
(1498, 'P63170', '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, 'P63170; Q15701;', 'KD01498', 'Rattus norvegicus (Rat)', 'Dynll1', '#Dynein light chain 1; cytoplasmic#8 kDa dynein light chain#DLC8#Dynein light chain LC8-type 1#Protein inhibitor of neuronal nitric oxide synthase#PIN', '-', '-', '58945'),
(1499, 'O46480', 'Nuclear distribution protein nudE-like 1', 'GO:0000777', 38449, 'Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity; the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role; together with DISC1; in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors; which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL (By similarity). {ECO:0000250}.', 'MDGEDIPDFSSLKEETAYWKELSLKYKQTFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVMNSNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPLSAPGMLPLSV', 345, 'O46480;', 'KD01499', 'Oryctolagus cuniculus (Rabbit)', 'NDEL1', '#Nuclear distribution protein nudE-like 1#Protein Nudel', '-', '-', '100008657'),
(1500, 'P63171', 'Dynein light chain Tctex-type 1', 'GO:0005868', 12452, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site. May also be a accessory component of axonemal dynein (By similarity). {ECO:0000250}.', 'MEDYQAAEETAFVVDEVSNIVKEAIESAIGGNAYQHSKVNQWTTNVVEQTLSQLTKLGKPFKYIVTCVIMQKNGAGLHTASSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSI', 113, 'P63171; Q15763; Q32PD4;', 'KD01500', 'Bos taurus (Bovine)', 'DYNLT1', '#Dynein light chain Tctex-type 1#T-complex testis-specific protein 1 homolog', '-', '-', '282380'),
(1501, 'P63172', 'Dynein light chain Tctex-type 1', 'GO:0005868', 12452, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site. May also be a accessory component of axonemal dynein. {ECO:0000269|PubMed:18647839}.', 'MEDYQAAEETAFVVDEVSNIVKEAIESAIGGNAYQHSKVNQWTTNVVEQTLSQLTKLGKPFKYIVTCVIMQKNGAGLHTASSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSI', 113, 'P63172; Q15763; Q5VTU4;', 'KD01501', 'Homo sapiens (Human)', 'DYNLT1', '#Dynein light chain Tctex-type 1#Protein CW-1#T-complex testis-specific protein 1 homolog', '-', 'ENSG00000146425', '-'),
(1502, 'Q9H211', 'DNA replication factor Cdt1', 'k', 60390, 'Cooperates with CDC6 to promote the loading of the mini- chromosome maintenance complex onto chromatin to form the pre- replication complex necessary to initiate DNA replication. Binds DNA in a sequence-; strand-; and conformation-independent manner. Potential oncogene. {ECO:0000250|UniProtKB:Q8R4E9; ECO:0000269|PubMed:11125146; ECO:0000269|PubMed:14672932; ECO:0000269|PubMed:14993212; ECO:0000269|PubMed:21856198}.', 'MEQRRVTDFFARRRPGPPRIAPPKLACRTPSPARPALRAPASATSGSRKRARPPAAPGRDQARPPARRRLRLSVDEVSSPSTPEAPDIPACPSPGQKIKKSTPAAGQPPHLTSAQDQDTISELASCLQRARELGARVRALKASAQDAGESCTPEAEGRPEEPCGEKAPAYQRFHALAQPGLPGLVLPYKYQVLAEMFRSMDTIVGMLHNRSETPTFAKVQRGVQDMMRRRFEECNVGQIKTVYPASYRFRQERSVPTFKDGTRRSDYQLTIEPLLEQEADGAAPQLTASRLLQRRQIFSQKLVEHVKEHHKAFLASLSPAMVVPEDQLTRWHPRFNVDEVPDIEPAALPQPPATEKLTTAQEVLARARNLISPRMEKALSQLALRSAAPSSPGSPRPALPATPPATPPAASPSALKGVSQDLLERIRAKEAQKQLAQMTRCPEQEQRLQRLERLPELARVLRSVFVSERKPALSMEVACARMVGSCCTIMSPGEMEKHLLLLSELLPDWLSLHRIRTDTYVKLDKAADLAHITARLAHQTRAEEGL', 546, 'Q9H211; Q86XX9; Q96CJ5; Q96GK5; Q96H67; Q96HE6; Q9BWM0;', 'KD01502', 'Homo sapiens (Human)', 'CDT1', '#DNA replication factor Cdt1#Double parked homolog#DUP', '-', 'ENSG00000167513', '-'),
(1503, 'P53267', 'DASH complex subunit DAM1', 'GO:0008608===GO:0051987===GO:0042729===c;k', 38422, '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:11698664; ECO:0000269|PubMed:11724818; ECO:0000269|PubMed:15664196; ECO:0000269|PubMed:16415853; ECO:0000269|PubMed:16777964; ECO:0000269|PubMed:9817759}.', 'MSEDKAKLGTTRSATEYRLSIGSAPTSRRSSMGESSSLMKFADQEGLTSSVGEYNENTIQQLLLPKIRELSDSIITLDSNFTRLNFIHESLADLNESLGSLLYGIMSNSWCVEFSQAPHDIQDDLIAIKQLKSLEDEKNNLVMELSNMERGIKRKKDEQGENDLAKASQNKQFNQPLFPSSQVRKYRSYDNRDKRKPSKIGNNLQVENEEDYEDDTSSEASFVLNPTNIGMSKSSQGHVTKTTRLNNNTNSKLRRKSILHTIRNSIASGADLPIENDNVVNLGDLHPNNRISLGSGAARVVNGPVTKNRNSMFSGRAERKPTESRHSVAKKTEKKINTRPPFR', 343, 'P53267; D6VUP6; Q9P422;', 'KD01503', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DAM1', '#DASH complex subunit DAM1#DUO1 and MPS1-interacting protein 1#Kinetochore assembly protein DAM1#Outer kinetochore protein DAM1', '-', '-', '853010'),
(1504, 'Q60520', 'Paired amphipathic helix protein Sin3a', 'GO:0000776', 145088, 'Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in he control of the circadian rhythms. Required for the transcriptional repression of circadian target genes; such as PER1; mediated by the large PER complex through histone deacetylation. {ECO:0000269|PubMed:10734093; ECO:0000269|PubMed:21680841; ECO:0000269|PubMed:7889570; ECO:0000269|PubMed:8649810}.', 'MKRRLDDQESPVYAAQQRRIPGSTEAFSHQHRVLAPAPPVYEAVSETMQSATGIQYSVAPNYQVSAVPQSSGSHGPAIAAVHSSHHHPTAVQPHGGQVVQSHAHPAPPVAPVQGQQQFQRLKVEDALSYLDQVKLQFGSQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPDLIMGFNTFLPPGYKIEVQTNDMVNVTTPGQVHQIPTHGIQPQPQPPPQHPSQPSSQSAPTPAQPAPQPTAAKVSKPSQLQAHTPASQQTPPLPPYASPRSPPVQPHTPVTISLGTAPSLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALTEQEVYAQVARLFKNQEDLLSEFGQFLPDANSSVLLSKTTAEKVDSVRNDHGGTVKKPQLNNKPQRPSQNGCQIRRHSGTGATPPVKKKPKLMSLKESSMADASKHGVGTESLFFDKVRKALRSAEAYENFLRCLVIFNQEVISRAELVQLVSPFLGKFPELFNWFKNFLGYKESVHLESFPKERATEGIAMEIDYASCKRLGSSYRALPKSYQQPKCTGRTPLCKEVLNDTWVSFPSWSEDSTFVSSKKTQYEEHIYRCEDERFELDVVLETNLATIRVLEAIQKKLSRLSAEEQAKFRLDNTLGGTSEVIHRKALQRIYADKAADIIDGLRKNPSIAVPIVLKRLKMKEEEWREAQRGFNKVWREQNEKYYLKSLDHQGINFKQNDTKVLRSKSLLNEIESIYDERQEQATEENAGVPVGPHLSLAYEDKQILEDAAALIIHHVKRQTGIQKEDKYKIKQIMHHFIPDLLFAQRGDLSDVEEEEEEEMDVDEATGAPKKHNGVGGSPPKSKLLFSNTAAQKLRGMDEVYNLFYVNNNWYIFMRLHQILCLRLLRICSQAERQIEEENREREWEREVLGIKRDKSDSPAIQLRLKEPMDVDVEDYYPAFLDMVRSLLDGNIDSSQYEDSLREMFTIHAYIAFTMDKLIQSIVRQLQHIVSDEVCVQVTDLYLAENNNGATGGQLNSQTSRSLLESAYQRKAEQLMSDENCFKLMFIQSQGQVQLTVELLDTEEENSDDPVEAERWSDYVERYMSSDTTSPELREHLAQKPVFLPRNLRRIRKCQRGREQQEKEGKEGNSKKTMENVESLDKLECRFKLNSYKMVYVIKSEDYMYRRTALLRAHQSHERVSKRLHQRFQAWVDKWTKEHVPREMAAETSKWLMGEGLEGLVPCTTTCDTETLHFVSINKYRVKYGTVFKAP', 1274, 'Q60520; Q570Z7; Q60820; Q62139; Q62140; Q7TPU8; Q7TSZ2;', 'KD01504', 'Mus musculus (Mouse)', 'Sin3a', '#Paired amphipathic helix protein Sin3a#Histone deacetylase complex subunit Sin3a#Transcriptional corepressor Sin3a', '-', '-', '20466'),
(1505, 'P25644', 'DNA topoisomerase 2-associated protein PAT1', 'GO:0000776', 88511, 'Activator of decapping that functions as a general and active mechanism of translational repression and required for P- body formation. First decay factor recruited to mRNA; at a time when the mRNA is still associated with translation factors. Subsequently; PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex; stabilizes the 3'' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components; enhances the formation of retrotransposition-competent Ty1 virus-like particles. Necessary for accurate chromosome transmission during cell division. {ECO:0000269|PubMed:10394921; ECO:0000269|PubMed:10523645; ECO:0000269|PubMed:10747033; ECO:0000269|PubMed:10761922; ECO:0000269|PubMed:10779343; ECO:0000269|PubMed:10913177; ECO:0000269|PubMed:11027264; ECO:0000269|PubMed:11514438; ECO:0000269|PubMed:12773554; ECO:0000269|PubMed:16179257; ECO:0000269|PubMed:17429074; ECO:0000269|PubMed:17513695; ECO:0000269|PubMed:17875743; ECO:0000269|PubMed:18086885; ECO:0000269|PubMed:19901074; ECO:0000269|PubMed:20832728; ECO:0000269|PubMed:24247251; ECO:0000269|PubMed:8816497; ECO:0000269|PubMed:8972867}.', 'MSFFGLENSGNARDGPLDFEESYKGYGEHELEENDYLNDETFGDNVQVGTDFDFGNPHSSGSSGNAIGGNGVGATARSYVAATAEGISGPRTDGTAAAGPLDLKPMESLWSTAPPPAMAPSPQSTMAPAPAPQQMAPLQPILSMQDLERQQRQMQQQFMNFHAMGHPQGLPQGPPQQQFPMQPASGQPGPSQFAPPPPPPGVNVNMNQMPMGPVQVPVQASPSPIGMSNTPSPGPVVGATKMPLQSGRRSKRDLSPEEQRRLQIRHAKVEKILKYSGLMTPRDKDFITRYQLSQIVTEDPYNEDFYFQVYKIIQRGGITSESNKGLIARAYLEHSGHRLGGRYKRTDIALQRMQSQVEKAVTVAKERPSKLKDQQAAAGNSSQDNKQANTVLGKISSTLNSKNPRRQLQIPRQQPSDPDALKDVTDSLTNVDLASSGSSSTGSSAAAVASKQRRRSSYAFNNGNGATNLNKSGGKKFILELIETVYEEILDLEANLRNGQQTDSTAMWEALHIDDSSYDVNPFISMLSFDKGIKIMPRIFNFLDKQQKLKILQKIFNELSHLQIIILSSYKTTPKPTLTQLKKVDLFQMIILKIIVSFLSNNSNFIEIMGLLLQLIRNNNVSFLTTSKIGLNLITILISRAALIKQDSSRSNILSSPEISTWNEIYDKLFTSLESKIQLIFPPREYNDHIMRLQNDKFMDEAYIWQFLASLALSGKLNHQRIIIDEVRDEIFATINEAETLQKKEKELSVLPQRSQELDTELKSIIYNKEKLYQDLNLFLNVMGLVYRDGEISELK', 796, 'P25644; D6VR80; Q8NKJ3;', 'KD01505', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'PAT1', '#DNA topoisomerase 2-associated protein PAT1#Decapping activator and translational repressor PAT1#Topoisomerase II-associated protein PAT1#mRNA turnover protein 1', '-', '-', '850440'),
(1506, 'Q15691', 'Microtubule-associated protein RP/EB family member 1', 'c;k;m', 29999, 'Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration. {ECO:0000269|PubMed:12388762; ECO:0000269|PubMed:16109370; ECO:0000269|PubMed:19632184; ECO:0000269|PubMed:21646404}.', 'MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQETAVAPSLVAPALNKPKKPLTSSSAAPQRPISTQRTAAAPKAGPGVVRKNPGVGNGDDEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY', 268, 'Q15691; B2R6I7; E1P5M8; Q3KQS8;', 'KD01506', 'Homo sapiens (Human)', 'MAPRE1', '#Microtubule-associated protein RP/EB family member 1#APC-binding protein EB1#End-binding protein 1#EB1', '-', 'ENSG00000233204', '-'),
(1507, 'Q8BHX3', 'Borealin', 'GO:0032133', 32214, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex; it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment (By similarity). {ECO:0000250}.', 'MAPKKRSSRGTRTNTLRSRKLASFLKDFDREVQVRTKQIESDRQTLLKEVENLYNIEILRLPKALQGMKWLDYFALGGNKQALEEAAKADRDITEINNLTAEAIQTPLKSVKKRKVIEVEESIKEEEEEEEEGGGGGGRTKKSHKNLRSAKVKRCLPSKKRTQSIQGRGRSKRLSHDFVTPAMSRLEPSLVKPTPGMTPRFDSRVFKTPGLRTPAAKEQVYNISINGSPLADSKEISLSVPIGGGASLRLLASDLQRIDIAQLNPEALGNIRKLSSRLAQICSSIRTGR', 289, 'Q8BHX3; B1ARX0; B1ARX1; Q6NVD3; Q8BHB1; Q8BHQ5; Q8BHQ9; Q9CRN4;Q9CS02; Q9CTF4;', 'KD01507', 'Mus musculus (Mouse)', 'Cdca8', '#Borealin#Cell division cycle-associated protein 8#MESrg', '-', '-', '52276'),
(1508, 'Q5R6X7', 'Chromobox protein homolog 3', 'GO:0000779', 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 (By similarity). {ECO:0000250}.', 'MASNKTTLQKMGKKQNGKSKKVEEAEPEEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEAFLNSQKAGKEKDGTKRKSLSDSESDDSKSKKKRDAADKPRGFARGLDPERIIGATDSSGELMFLMKWKDSDEADLVLAKEANMKCPQIVIAFYEERLTWHSCPEDEAQ', 183, 'Q5R6X7;', 'KD01508', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'CBX3', '#Chromobox protein homolog 3#Heterochromatin protein 1 homolog gamma#HP1 gamma', '-', '-', '100173451'),
(1509, 'Q9XT96', 'Presenilin-2', 'GO:0000776', 50271, 'Probable catalytic subunit of the gamma-secretase complex; an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins (By similarity). {ECO:0000250}.', 'MLTFMASDSEEEVCDERTSLMSAESPTPRSCQDGRQGLEDGESAAQWRSQESEEDHEEEDPDRYVCSGVPGRPPGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFSEDTPSVGQRLLNSVLNTLIMISVIVTMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVLKTYNVAMDYPTLFLTVWNFGAVGMVCIHWKGPLVLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPDVFEPPLPGYPGEELEEEEERGVKLGLGDFIFYSVLVGKAAATGSGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI', 449, 'Q9XT96; Q2KI10;', 'KD01509', 'Bos taurus (Bovine)', 'PSEN2', '#Presenilin-2#PS-2#3.4.23.-#Presenilin-2 NTF subunit#Presenilin-2 CTF subunit', '-', '-', '282010'),
(1510, 'P40055', 'U3 small nucleolar RNA-associated protein 7', 'k', 62317, 'Involved in nucleolar processing of pre-18S ribosomal RNA. {ECO:0000269|PubMed:12068309}.', 'MGHKKNGHRRQIKERENQNKFERSTYTNNAKNNHTQTKDKKLRAGLKKIDEQYKKAVSSAAATDYLLPESNGYLEPENELEKTFKVQQSEIKSSVDVSTANKALDLSLKEFGPYHIKYAKNGTHLLITGRKGHVASMDWRKGQLRAELFLNETCHSATYLQNEQYFAVAQKKYTFIYDHEGTELHRLKQHIEARHLDFLPYHYLLVTAGETGWLKYHDVSTGQLVSELRTKAGPTMAMAQNPWNAVMHLGHSNGTVSLWSPSMPEPLVKLLSARGPVNSIAIDRSGYYMATTGADRSMKIWDIRNFKQLHSVESLPTPGTNVSISDTGLLALSRGPHVTLWKDALKLSGDSKPCFGSMGGNPHRNTPYMSHLFAGNKVENLGFVPFEDLLGVGHQTGITNLIVPGAGEANYDALELNPFETKKQRQEQEVRTLLNKLPADTITLDPNSIGSVDKRSSTIRLNAKDLAQTTMDANNKAKTNSDIPDVKPDVKGKNSGLRSFLRKKTQNVIDERKLRVQKQLDKEKNIRKRNHQIKQGLISEDHKDVIEEALSRFG', 554, 'P40055; D3DLY9;', 'KD01510', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'UTP7', '#U3 small nucleolar RNA-associated protein 7#U3 snoRNA-associated protein 7#U three protein 7', '-', '-', '856815'),
(1511, 'Q2NKU0', 'Centromere protein X', 'GO:0000777===GO:0051382', 8879, '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}.', 'MEETGAVFRKELVSKLLHLHFKDKKTKVSGDALQLVAELLKIFVVEAAIRSVRQAQAEGLAHVDVEQLEKVLPQLLLDF', 79, 'Q2NKU0;', 'KD01511', 'Bos taurus (Bovine)', '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', '-', '-', '618018'),
(1512, 'Q9XT97', 'Presenilin-1', 'GO:0000776', 53654, 'Probable catalytic subunit of the gamma-secretase complex; an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx; cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin; thus negatively regulating Wnt signaling. May also play a role in hematopoiesis (By similarity). {ECO:0000250}.', 'MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDSRERHEHGNERRRRGNTESVSNGRAPSSSQQVVEQEEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVAQRALHSILNAVIMISVIVIMTILLVVLYKYRCYKVIHAWLIVSSLLLLFFFSFIYLGEVFKTYNVAMDYISVALLIWNFGVVGMIAIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRKVSKNSNYNAQRPANSPVTTTGTESESQDPVTESDDGGFSEEWEAQRDSRLGPHHSTAESRSAVQDLSSSILASEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPVSITFGLIFYFATDYLVQPFMDQLAFHQFYI', 478, 'Q9XT97;', 'KD01512', 'Bos taurus (Bovine)', 'PSEN1', '#Presenilin-1#PS-1#3.4.23.-#Presenilin-1 NTF subunit#Presenilin-1 CTF subunit#Presenilin-1 CTF12#PS1-CTF12', '-', '-', '282705'),
(1513, 'Q556Y9', 'Mitotic spindle assembly checkpoint protein MAD2A', 'GO:0000776===GO:0000777', 23050, 'Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore- spindle attachment and inhibits the activity of the anaphase promoting complex until all chromosomes are aligned at the metaphase plate (By similarity). {ECO:0000250}.', 'MQAAVASKTNISLKGSTEIVTEFFSYSINTILFQRGLYPPESFTRVAKYGLPILVTNDQSLKDYLDNVLKQLSEWLLSGDVQKLVLVITDIVTKEVLERWVFDVTTDIPKEGEAPRQKPEKEIMNEIQAIIRQITASVTFLPLLPNACTFDLLVYTSKDLAVPQKWEESDPKFITNSQQVKLRSFTTTIHKVESMVAYKISND', 203, 'Q556Y9; Q86JT2;', 'KD01513', 'Dictyostelium discoideum (Slime mold)', 'mad2l1-1', '#Mitotic spindle assembly checkpoint protein MAD2A#Mitotic arrest deficient 2-like protein 1#MAD2-like protein 1', '-', '-', '8618872'),
(1514, 'P23098', 'Dynein beta chain; ciliary', 'GO:0003777', 511782, '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.', 'MADVVDPRLEFISEYILKSYKLKPDKWAKCINVEENKILMLEFLEKADNPQLVFTVNAAGLITPSYEFPSALKNTKAIYFIKKGREPVGKDNIKTTLVYGDLSYTPLEQLSALVDEILVPLLANPRNHEQWPVVVSQDVLRHVHNLKSSVYVVAGQVKGKTLLPLPVGSEKVETAAESEEKDDSYDRSLVHAIESVIIDWTHQIRDVLKRDSAQPLLEGLNPGPMVEINFWKAKCENLDCIFQQLRDPKVRKMKELLERTQSSYLPSFNNIERDVEAALTEAQDINCYLKPLIYQVESLDELEFPDMTPRLAPILHTVCLIWSNSDYYNTAPRIIVLLQEICNLLIDLCRTFLDPSEIFKLEPEESLEKVRGALAVLKAWRDLYDEHRAKLKDYFKDGREVKGWEFASPLVFTRMDNFTSRIETIQSLFETNVEFSKLEKTEMGSMKGRMLSQQVEKIHEEFQECAKVFTERPYDGLDPQCQEFLDDYEEFEKKVFDLDRRLGSILCQGFDDCCGLEAVFKMLDCYGPLLDRPVIRNDFECKYPVVLMLYDLELDQAKEIYDEHMRVEENDGNAPLNKNMPDVAGQLKWSAQLRDRISKPMGSLKHMEHPTGVRRILESEDAKVVFQKYEEMINLLNKYEQKVFENWTKGVDEVCKTNLDQSLITRDESTKLIKINFDPKLVAVLREVKYLQIRGEESIPESAASIYEKHETLRKYVANLDLTQAWYNKVRNTVLEVEFPLIEGQLADLDTRLKQAESELNWTSDSVWEYIQETRDQVHDLEKRVQQTKDNVDRIKKIMAEWTKQPLFERKELKKESLLALDDRQDRLKKRYAEISTAGEKIHSLIKENLGLFKADASSDIWKAYVDYVDDMVIDGFFNCIHCTLSYLLENTDPRHCAAPLFEARLELQVPDMIFNPSLDYGVADGFYDLVEMLISDTYKMASLVSRLAEHNGQEHYQADLEGMDDLSDVRNDLMDRVQTIMTKAQEYRNSFDNYAYLYVDDRKEFMRQFLLYNHVLTTEEIEAHAEDGVPECPPTLDQFKEQVDTYEKIYSEADEIEPEQVFDAWFRVDSKPFKAALLNIIKKWSFMFKQHLIDHVTNSLSELQEFIKVGNSGLTKTVEEGDYNGLVECMGHLMAVKERQAATDEMFEPIKQTIELLKTYDQEMSEEVHTQLQELPEQWNNTKKIAITVKQQVAPLQANEVAIIRRKCTSFDVRQHEFRERFRKEAPFIFTFEGPYQCLDRCHSEIYEMEEHMANLQESAGLFEVNMPDYKQLKACRREVRLLKALWDLIMIVRTSIEDWKTTPWLEINVEQMEMDCKKFAKDIRSLDKEMRAWDAYNGLDATVKNMLTSLRAVSELQNPAIRERHWQQLMAATKVKFTMDKETTLSDLLALNLHNFEDEVRNIVDKAVKEMGMEKVLKELNTTWSSMDFEYEPHSRTGISLLKSNEELIETLEDNQVQLQNLMTSKHIAHFLEEVSGWQKKLSTTDSVITIWFEVQRTWSHLESIFIGSEDIRNQLPEDSKRFDGIDTDFKELASEMEKTPNVVEATNRARLYDRLEAIQGSLVVCEKALAEYLETKRLAFPRFYFVSSADLLDILSQGNNPSQVQRHLSKLFDNMAKLKFKQDDEGNDTKLALGMYSKEGEYVDFDKECECTGQVEVWLNRVMDAMRSTVRSQFADAVVSYEEKPREQWLYDYPAQVALATTQVWWTTEVNISFARLEEGHENSMKDYNKKQIQQLNTLIGLLIGKLTKGDRQKIMTICTIDVHARDVVAMMVLKKVDNAQAFQWLSQLRHRWADDDKHCYANICDAQFKYSYEYLGNTPRLVITPLTDRCYITLTQSLHLVMSGAPAGPAGTGKTETTKDLGRALGIMVYVFNCSEQMDYKSCGNIYKGLSQTGAWGCFDEFNRISVEVLSVVAVQVKCVQDAIRDKKERFNFMGEEISLIPSVGIFITMNPGYAGRTELPENLKALFRPCAMVVPDFELICEIMLVAEGFLDARLLARKFITLYTLCKELLSKQDHYDWGLRAIKSVLVVAGSLKRGDPQRPEDQVLMRALRDFNVPKIVSDDTPVFMGLIGDLFPALDVPRRRDMDFEKVVKQSTLDLKLQAEDSFVLKVVQLEELLAVRHSVFVIGNAGTGKSQVLKVLNKTYSNMKRKPVLVDLNPKAVTNDELFGIINPATREWKDGLFSVIMRDMSNITHDGPKWIVLDGDIDPMWIESLNTVMDDNKVLTLASNERIPLTPSMRLLFEISHLKTATPATVSRAGILYINPSDLGWNPIVTSWIDTREVQSERANLTILFDKYLPTLLDTLRVRFKKIIPIPEQSMVQMLCYLLECLLTPENTPADCPKELYELYFVFASIWAFGGSMFQDQLVDYRVEFSKWWITEFKTIKFPNQGTVFDYFIDQESKKFLPWSEKVPVFELDPEIPMQAVLVHTNETTRVRFFMDLLMERGRPVMLVGNAGLGKSVLVGDKLSNLGEDSMVANVPFNYYTTSEMLQRVLEKPLEKKAGRNYGPPGTKKLVYFIDDMNMPEVDTYGTVQPHTLIRQHMDYKHWYDRQKLTLKEIHKCQYVSCMNPTAGSFTINSRLQRHFCVFALSFPGQDALSTIYNSILSQHLANISVSNALQKLSPTVVSATLDLHKKVAQSFLPTAIKFHYVFNLRDLSNVFQGLLYSGPDLLKAPIDFARLWMHECQRVYGDKMINDQDIEAFEKLVLEYAKKFFEDVDEEALKAKPNIHCHFATGIGDPKYMQVPNWPELNKILVEALDTYNEINAVMNLVLFEDAMQHVCRINRILESPRGNALLVGVGGSGKQSLARLASYISSLEVFQITLRKGYGIPDLKLDLATVCMKAGLKNIGTVFLMTDAQVSDEKFLVLINDLLASGEIPDLFADDEVENIIGGVRNEVKGMGLQDTRENCWKFFIDRLRRQLKTVLCFSPVGTTLRVRSRKFPAVVNCTSIDWFHEWPQEALVSVSMRFLDEVELLKGDIKKSIAEFMAYVHVSVNESSKLYLTNERRYNYTTPKSFLEQIKLYESLLSMKSKELTAKMERLENGLTKLQSTAQQVDDLKAKLASQEVELAQKNEDADKLIQVVGVETEKVSKEKAIADDEEKKVAIINEEVSKKAKDCSEDLAKAEPALLAAQEALNTLNKNNLTELKSFGSPPSAVLKVAAAVMVLLAPNGKIPKDRSWKAAKVVMNKVDAFLDSLINYDKENIHENCLKSIKEYLNDPEFEPEYIKGKSLAAGGLCSWVVNIVKFYNVYCDVEPKRIALQKANDELKAAQDKLALIKAKIAELDANLAELTAQFEKATSDKLKCQQEAEATSRTITLANRLVGGLASENVRWGEAVANFKIQEKTLPGDVLLITAFVSYIGCFTKTYRVDLQERMWLPFLKSQKDPIPITEGLDVLSMLTDDADIAVWNNEGLPSDRMSTENATILSNCQRWPLMIDPQLQGIKWIKQKYGDDLRVIRIGQRGYLDTIENAISSGDTVLIENMEESIDPVLDPVLGRNTIKKGRYIKIGDKEVEYNPDFRLILQTKLANPHYKPEMQAQTTLINFTVTRDGLEDQLLANVVAQERPDLEKLKSDLTKQQNDFKIILKELEDNLLSRLSSAEGNFLGDTALVENLETTKRTAAEISVKVEEAKVTEVKINEARELYRPAAARASLLYFILNDLNKINPIYQFSLKAFNTVFSLPIARAEPCEDVKERVVNLIDCITYSVFIYTTRGLFEADKLIFTTQVAFQVLLMKKEIAQNELDFLLRFPIQVGLTSPVDFLTNSAWGAIKSLSAMEDFRNLDRDIEGSAKRWKKFVESECPEKEKFPQEWKNKSALQKLCMMRALRADRMSYAVRNFIEEKLGSKYVEGRQVEFAKSYEETDPATPVFFILSPGVDPLKDVEALGKKLGFTFDNNNFHNVSLGQGQEIVAEQCMDLAAKEGHWVILQNIHLVAKWLSTLEKKLEQYSVGSHDSYRVYMSAEPAGSPEAHIIPQGILESSIKITNEPPTGMFANLHKALYNFNQDTLEMCAREAEFKVILFALCYFHAVVCERQKFGPQGWNRSYPFNTGDLTISVNVLYNYLEANSKVPWQDLRYLFGEIMYGGHITDDWDRRLCRTYLEEYMAPEMLDGELYLAPGFPVPPNSDYKGYHQYIDEILPPESPYLYGLHPNAEIGFLTTESDNLFKIVLELQPRDAGGGGGGGSSREEKIKSLLDEIVEKLPEEFNMMEIMAKVEDRTPYVVVAFQECERMNMLTSEIRRSLKELDLGLKGELTITPDMEDLSNALFLDQIPATWVKRAYPSLFGLTSWYADLLQRIKELEQWTADFALPNVVWLGGFFNPQSFLTAIMQSMARKNEWPLDKMCLQCDVTKKNKEDFSSAPREGSYVHGLFMEGARWDTQTNMIADARLKELAPNMPVIFIKAIPVDKQDTRNIYECPVYKTKQRGPTFVWTFNLKSKEKAAKWTLAGVALLLQV', 4466, 'P23098;', 'KD01514', 'Tripneustes gratilla (Hawaian sea urchin) (Echinus gratilla)', '', '#Dynein beta chain; ciliary', '-', '-', '-'),
(1515, 'Q9Z1B5', 'Mitotic spindle assembly checkpoint protein MAD2A', 'GO:0000776===GO:0000777===k', 23598, 'Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore- spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate (By similarity). {ECO:0000250}.', 'MAQQLAREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLTTTDPELIKYLNNVVEQLKEWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKEEGVRREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNCEEVRLRSFTTTIHKVNSMVAYKTPVND', 205, 'Q9Z1B5; Q9JI53;', 'KD01515', 'Mus musculus (Mouse)', 'Mad2l1', '#Mitotic spindle assembly checkpoint protein MAD2A#Mitotic arrest deficient 2-like protein 1#MAD2-like protein 1', '-', '-', '56150'),
(1516, 'Q59VC6', 'DASH complex subunit DAD2', 'GO:0008608===GO:0042729', 15543, '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}.', 'MSFTTKDKSDDSSIITTNYADNPNLSPIEQKILQQYQLMNNNLIKISNELELLTNTTDEFGKGKGSSIQLVENLRQLETKLVFVYTFFKGAVYSILNAQDYIAEQETNGLEETNEEEDGNEEDESENVELSGVSADEN', 138, 'Q59VC6; Q59V81;', 'KD01516', 'Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)', 'DAD3', '#DASH complex subunit DAD2#Outer kinetochore protein DAD2', '-', '-', '3644809'),
(1517, 'Q9W3D1', 'Caf1-180Chromatin assembly factor-1 p180 subunit', 'k', 133495, '', 'MHAGVVKTPLSGRKKDAAVPAKSAEKTASGGKKFVQTRLPFKLLTPGGGAVPTSSSSSSSPATIGSGPVTVILDEDDPAPRKRKLSYDDESPSEGTGCSTGQLRRSTSKENLDLASSIATKKVKTTDSVVEDVIELDEDEADKEIEDQDQLVEAKSSKEVKLKPKKSEGKKGSPAPIQIKLPLVNKRSKRRKSLKKSEEPLETSTADVAKGDSESSDDIEIIAEELNPQKRQKVQTPREKSPENSSTSGKHTEEVMQKNGKDSKKQEESMKAVKESKKEEPKTAEQNKKNDQATIDLFMGKKMETNKKDKPEVKTTAKDNKKDPLIAEDSKPKEVPKKETSKTGGKGKKEGAKPAEKSKKEEKEDSTTKSKKEKADSPANNQKEQQIGVKKKTSEPEDASNSHKSVTAKKDSKKDEASTQVKSDNESPEAAEISMILSTSEANSSSSEHEMDADTDTAATDRPSAQKETRLNRKSLPEVTGAPKGLTPKQQRLMEQRKKAREEKEQKLAEERRLKQQDKEHREQQKKQERDEKEQQRKLERDQKEQQRKMEKEEKERKRQAEVDSKNEEKRKRNEAKEEVQRKKDEERRKKEQEREEAEQKKKRAAESFSKFFVPKQPKCGSGSNNTSYLEHEQSSCDSSKASSQTLAFRPFQIKDDMLLAPIVRNSLGQEQRSQLDGLFRHRDEEADDEEEEEEQDIVRRKPPNRANLYLSELSSGRRKPLKMQRDVKLQRRTKDEEDDDDVQVIDYLSPAGLPIEVEQPKQLTRMKAKYLHFADNRRPPYYGTWRKKSSSISARRPLAQDKVLFDYEVDSDCEWEEEEPGESLSASEDEKEKESEEESEEEYNEWYVPHGHLSDEELQNDGDGMEDGHTREAQKAKLQVLQQEFAQEMKKQTKKIKARLLGPVWLDENGNKSELFPAIFAHTIDMYACWQVEPLSLEPPPEPERQDQTPEQPVPLQLDDRLMQQLVRLTHGNRNSKTFLINEYLEYLKTQATAEANQTTLPSKAVLREKFDELASWKTVELSTPEAAAASANSAKKGRKPKKRLCWVVASDMLEKFQLPDLQLQNQWNYTLTPKVSDGPDAAQQEQSPPADAVPAASPASNQTTNSAPTTPISGQTQAGQGVKKRATLIMSVPRDQPIPSATKNKLISQFLQRQSDASKPKEKMQEKPPPIVFDDVVMLSD', 1183, 'Q9W3D1;', 'KD01517', 'Drosophila melanogaster (Fruit fly)', 'Caf1-180', '#Caf1-180 {ECO:0000313|EMBL:AAF46399.1}#Chromatin assembly factor-1 p180 subunit {ECO:0000313|EMBL:AAK31263.1}', '-', '-', '31801'),
(1518, 'Q20060', 'Structural maintenance of chromosomes protein 4', 'k', 176572, 'Central component of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Also involved in chromosome segregation. {ECO:0000269|PubMed:11914278}.', 'MPPKTSAAPPQSDESDSDFDDAPVKKPQKKTTKPVNRHKEGSKDPEEELQRAVNEKFDGSDGEDDDSDLFSLQLPSRPDFLTKPNRADRLMIRNVEVDNFKSYFGKASIGPFHKSFTSIIGPNGSGKSNLIDSLLFVFGFRASKIRSAKVSNLIHKSAGRNPDKCTVTIHFQRIVDIPGHYEVVKDSEFTISRTAFQNNSSSYAIDGRPATKNEVEARLRRVDIDIEHNRFLILQGEVEQIAMMKPVKTTKSETGMVEYLEDIIGTNRLEPFVKLFQRRVNRLTCDLSQQRIARDHARNSKVAMENPVRAAIEFLMKENEATTIHMKLEQRRRQRYLDKIAPKQAELDKMKEEMKSIAETLDTNKNEYKQSEEAQKVMIEERSKLDKNFDSLSKELSDLGTEETRRKEALKRHQANISKAEAEKEKEVKKRSNLEAAPEKAERKIAKCQEEVEQLLEIEKTANEEADKNLDEFEKRSEAPKEEQKKIQETWAQKSNEFNKVRGEARIAREDFEDLKKLANSGTDKLIELKKRLESSEESYAKEKDELDKLKPEFDSWNDKLKQLSTELPTLRNTARQKNQDLAKTRDRLETLRQQNSSCSSSNKVIQALMKEKEAGRIKSFHGRLGDLGVIDPKYEGAICTNFGARLNYLIVGKEEDAKNVINFLVANKLPRQTVQPLDKIKCDKRDLAPNPTNPLPAPRLIDLIDCDPVLKPAFYDMVRSAIVGDSTQEAQRMHRMPACRGVTVCTLEGSMIHPSGSFTGGGKTVKGLILTDKNKMAKQVTPEDKAAERDLAEKLGKLRDEADELKGQEHEMDGQLIEARRKVAEMSNRLSIVTSSVQSAAPAIETLKKTIANQEKEAAKVKVDAKTLEDKQKIVEELEKKRDELGEEAAKVKARQAEIQSKLDGIFKELVQCHRDEAKESLQKRQKLEKDIAKETANISNSGRNIAKCDENISRHDKDIEKMKKKCEELMEKAIDDEEVKSKKETVERFEKQIKKLQTKGEEMTKKQSELSAAETKLEGELKKCSEGIKELKESMLADRLKVEDIEKKLAALKVNRIPRFQFLIESSRPEDLEMQIDDKMPVVDENQSPEEVERQKKHMACVMSDAAYALEFEMRQKVLENTESYENVDGEDRVPVELLSDEKINEISSRDAEEMQMKLKVCEQQVEALKAKVDISSIKAYVDKVKQYNEQVIKLTIATEVHRKHNQELQRIKQMRLEEFHSAFEFIGKHLVAVFKMLTDGGDAKLEYIDKDDPFRQGISFMVRPAKKAWKQIQFLSGGEKTLSSLALIFALHMFRPTPFYVMDEIDAALDYRNVSIIAQYVRQKTENAQFIIISLRNNMFELANRLVGIYKVDGCTRNVAIDPLRVCEMAKQITDSLGQATCTLPDEVTQRFNETMSRQNKEMIAQEKQYPNFPSSNEISKAEKIVNVEGRVRKELIQTTRDVTSRPQSKATTSGDGTERPASRSASRPESRINQMKYPAPRLVERSSSQNVRSPRKARNIEADETTPPSKRSNSASTPKRSPMKPLTPSSKKKEKAIVDDDDDME', 1549, 'Q20060;', 'KD01518', 'Caenorhabditis elegans', 'smc-4', '#Structural maintenance of chromosomes protein 4#SMC protein 4#SMC-4', '-', '-', '175603'),
(1519, 'Q24044', 'CG4274-PAFI02843pFizzyLD44795p', 'c;k', 57081, '', 'MSQFNFVSDLQNALIMDGETRGPAPRWKKKLEASLNGSVNTTRSVLSVSYNTSFSGVQAPTKTPGKSSEGKTKKSNTTPSKTPGGGDRFIPNRAATNFELAHFLVNKDSGDKSDEENDKATSSNSNESNVQASAHKGDRQKLISEVAQVGDSKGGRILCYQNKAPAAPETHNNPLKVVYSIKTPISTKSGSRYIPTTSERILDAPDFINDYYLNLMDWSADNIVAVALGSCVYLWNAQTGNIEQLTEFEEGDYAGSLSWIQEGQILAIGNSTGAVELWDCSKVKRLRVMDGHSARVGSLAWNSFLVSSGSRDGTIVHHDVRAREHKLSTLSGHTQEVCGLKWSTDFKYLASGGNDNLVNVWSAASGGVGTATDPLHKFNDHQAAVRALAWCPWQPSTLASGGGTADRCIKFWNVNNGTLMKSVDSKSQVCSLLFSRHYKELISAHGFANNQLTIWKYPTMVKQADLTGHTSRVLQMAMSPDGSTVISAGADETLRLWNCFAPDPLASKKAVSTSKGKQSVFRQSIR', 526, 'Q24044;', 'KD01519', 'Drosophila melanogaster (Fruit fly)', 'fzy', '#CG4274-PA {ECO:0000313|EMBL:AAF53523.1}#FI02843p {ECO:0000313|EMBL:ACL68690.1}#Fizzy {ECO:0000313|EMBL:AAA83150.1}#LD44795p {ECO:0000313|EMBL:ABK57089.1}', 'BIOMD0000000144,Calzone2007_CellCycle;', '-', '34968'),
(1520, 'Q9Y584', 'Mitochondrial import inner membrane translocase subunit Tim22', 'k', 20031, 'Essential core component of the TIM22 complex; a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex; it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity). {ECO:0000250}.', 'MAAAAPNAGGSAPETAGSAEAPLQYSLLLQYLVGDKRQPRLLEPGSLGGIPSPAKSEEQKMIEKAMESCAFKAALACVGGFVLGGAFGVFTAGIDTNVGFDPKDPYRTPTAKEVLKDMGQRGMSYAKNFAIVGAMFSCTECLIESYRGTSDWKNSVISGCITGGAIGFRAGLKAGAIGCGGFAAFSAAIDYYLR', 194, 'Q9Y584; Q9NWI8;', 'KD01520', 'Homo sapiens (Human)', 'TIMM22', '#Mitochondrial import inner membrane translocase subunit Tim22#Testis-expressed sequence 4', '-', 'ENSG00000177370', '-'),
(1521, 'P40066', 'Nucleoporin GLE2', 'k', 40523, '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. It is specifically important for nuclear mRNA export. {ECO:0000269|PubMed:10801828; ECO:0000269|PubMed:11689687; ECO:0000269|PubMed:8970155; ECO:0000269|PubMed:9463388}.', 'MSFFNRSNTTSALGTSTAMANEKDLANDIVINSPAEDSISDIAFSPQQDFMFSASSWDGKVRIWDVQNGVPQGRAQHESSSPVLCTRWSNDGTKVASGGCDNALKLYDIASGQTQQIGMHSAPIKVLRFVQCGPSNTECIVTGSWDKTIKYWDMRQPQPVSTVMMPERVYSMDNKQSLLVVATAERHIAIINLANPTTIFKATTSPLKWQTRCVACYNEADGYAIGSVEGRCSIRYIDDGMQKKSGFSFKCHRQTNPNRAPGSNGQSLVYPVNSIAFHPLYGTFVTAGGDGTFNFWDKNQRHRLKGYPTLQASIPVCSFNRNGSVFAYALSYDWHQGHMGNRPDYPNVIRLHATTDEEVKEKKKR', 365, 'P40066; D3DM14;', 'KD01521', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'GLE2', '#Nucleoporin GLE2#Nuclear pore protein GLE2#poly(A) RNA export protein RAE1', '-', '-', '856844'),
(1522, 'P40065', 'Monopolin complex subunit MAM1', 'GO:0000778===GO:0033551===k', 35753, 'Component of the monopolin complex which promotes monoorientation during meiosis I; required for chromosome segregation during meiosis. {ECO:0000269|PubMed:11163190; ECO:0000269|PubMed:11470404; ECO:0000269|PubMed:12586695; ECO:0000269|PubMed:12663816; ECO:0000269|PubMed:12689592; ECO:0000269|PubMed:12717442; ECO:0000269|PubMed:15226378; ECO:0000269|PubMed:15620645}.', 'MREKRTISNKDTNYLKFPNKLQRYSRFLSRKISNTSPEKQPKKNIKEHCLSSYHKEHSVKPKQNSGNVAAKEDKDTQHLQNNVANEEATECLTRSNLKKLQEKIFDRELNDIACDHCLCSTENRRDIKYSRLWFLFELEMSENWNENLRLSCYNKYVYSAIDESWKMENILLKEQEKHYEYFPIGQLLIPNNIDYTNKQKRKENIEDLTIEIDSIIETNHQKKRFLPQSVLIKREDEIAFDDFHLDARKVLNDLSATSENPFSSSPNTKKIKSKGKTLEVVPKKKNKKIIGALERKLHIDEN', 302, 'P40065; D3DM13; E9P8Y3;', 'KD01522', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MAM1', '#Monopolin complex subunit MAM1#Monopolar microtubule attachment during meiosis 1 protein 1', '-', '-', '856843'),
(1523, 'Q66JQ7', 'Protein CASC5', 'GO:0000777===GO:0034501===GO:0008608', 179337, 'Performs two crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Directly links spindle checkpoint proteins BUB1 and BUB1B to kinetochores. Part of the MIS12 complex; which may be fundamental for kinetochore formation and proper chromosome segregation during mitosis. Acts in coordination with CENPK to recruit the NDC80 complex to the outer kinetochore (By similarity). {ECO:0000250}.', 'MDGVYSEANEENDNTQRPVRRQHSSILKPPRSPLQDLKCGNQTNQEPNPPRKRKSSRRVSFADTIKVFQTESHMKTERNSEISGMNTLLCAPIQTQMQQKEFSITDCNHERKHANDQTVIFSDENQMDLTASHTVMITKGLSDCTKNENSTKIDTTSFLENLKHHAANSRIKKDLACSTVSLSQNIFSEKINSDNFIKRLKTGKHISSSTELDKENAEIPVYSKDSNSASSTYQMHASLGVDENSSNRTRIFREQDDGMNLTQCHTACIKTWIPPSTEAKIGEFKGDKTIYGNECMELTTNYTIQVLSSENNLSERETQTQNGMNVTTVDGATAPAPEKKTALKDKLNAAFQGSFPNPENKIHIIKCHPIESETHTVTQISSQSASTLAVTSKSICSSPAIEGYKTIFHSSSNDAMELTKCLSAMEEEKKLLKADDKYSKICTNPDAGPLREKTIYLEEDSMDITKSHTVAIDNKIFKHDQENIKKEIIAIPIFEKEMVLRNLMPMSKDEKRDVNYISVPQVSKESLQRSQTNTLSVSLTDKKMEFLADEDMDLTKSHTTKLSQVIPTTFDLASKNVTKSYSHSKSPLNEWESLDKQVVLGQHSKLPLPQRKDRDDPDCSHHKIMYSEELQTMDLTKSHTIVIGFGPSEVQEHSKINLEHKNSQLTAESIQTAVNVPAANSRVVTTNDMDMLKDRSTHKPELLKEKQNIKIYGRKSIGRLKIDKTILFSEGNEGDMDITKSCTVKINHRSLLDKHDSHLVSLAGTSKTILHARGQVEMEINRSHTTPLECKIISPSDITPGDLDKTMMSIDDHEELDMTKSHTVFIDYQAEAKGVLPDRLDFQLSKKESLQKPKVTSLAEEIYISKNSESNHLPAKGSQLTILEEGSNSGLGEETNDAQKPGFLNELLSGKTQRRKSLSLKNKSITFPENDKSYREIPQSSAVEINNETRLEDRKGFSFVPLAGTSKPVLSAYGPEDMEISIGQTTASEYKTVPPEEITTIPMDKTVMFVDNFGDLDVTRSHTVFIDCQAKEKVLDEYTNLGIQKTKTLSGSEGDTHIQEITKNPAAQHKHHMTTVIPSSTVVSDQSSMKIKFHKADRDEEVKGKEVEANMLKQTKPESCLLNITDGKNVDFTSSYTADVCRSSDKYSSLPNISSSDNSGGNTMSLCDKNKEKAYNCQVPNEFTYAAILPSTYHMDSKKLSVFPPCPSKEVTQTESAIALLKDEDPVEEPLGEMATFNSKHVSLNLAKDQTEAFVDVSVASQPHLSAQQSPSTQKGQDVARRDEGILAKAGKKALPFLLENVAASTWENESKIPTNVEHFAVTYEKELSISIQTDKCNTNVQSPSNSALTTQVIQTHANAEGALDFLVPSTVSCFSSTKPSLSNLNRKTEEVLDFQTVNLLPPAEQLLEEGSQAHSMSIVQATEIYRLGSRNDRDEESKTFCNEAETTSVPLKTAVKDKTRRCSLGIFLPKLPSKRSCSITGVDDLEQILADAADLTQLETQPVCSKDPGIGSVAAKLNLSPSQFINEENLPVYPGEILSSDSVSLDIEESVLIDTSQRESLPSENKTENCRAQKRTRVEENDVTNEKKIRTHDSAQDQEVSCLEPKNVLEF', 1612, 'Q66JQ7; A3KGI4; Q8CCH6; Q9CV38;', 'KD01523', 'Mus musculus (Mouse)', 'Casc5', '#Protein CASC5#Cancer susceptibility candidate gene 5 protein homolog#Kinetochore-null protein 1', '-', '-', '-'),
(1524, 'Q5RE09', 'Cytoplasmic dynein 1 light intermediate chain 2', 'GO:0003777===GO:0005868', 54060, '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.', 'MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRAGSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEEGCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSFPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPGAGGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA', 492, 'Q5RE09;', 'KD01524', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'DYNC1LI2', '#Cytoplasmic dynein 1 light intermediate chain 2#Dynein light intermediate chain 2; cytosolic', '-', '-', '100171820'),
(1525, 'O00399', 'Dynactin subunit 6', 'GO:0000777===SCL', 20747, '', 'MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQALIINAYPDNITPDTEDPEPKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKTMKGSSTPVKN', 190, 'O00399; B2RAC1;', 'KD01525', 'Homo sapiens (Human)', 'DCTN6', '#Dynactin subunit 6#Dynactin subunit p27#Protein WS-3', '-', 'ENSG00000104671', '-'),
(1526, 'Q9VEN2', 'Chromosome alignment defect 1', 'k', 109539, '', 'MANAVVDEETLEAMVYERSKAWSSKMADFASLEDGMEIDVAEFDNLFHGEDEDPDLDDVAKEAVEDNVPDEAKLEMGHINATSVTELTLILCANEDNEAKAEIEEILNQTVPVVEEHKRKWREAGLDRILDTFDEKQIEHHVGRWMRRHNSVYLEASPPKYLPPHHNSISDESDESMHSIDTARYIQQSRRRNAHMTNKNMTTIKMYRKHSHKRDELRAKYAYGDEQEHRHHMQAVLLRRRERERQLAYLASTPMQCVYSSGHHMRRKNLRKRRINSWMFDSASSSEEDTSFGGCDCHSCRRHYALSRSVYQSCPYGRGQREYHHRQMASRTMHTMRRQHTFDMEMDLRPRLPENECSCCNSDRLCSNVIHIANSSTEEWVVENRSNHLTQETQEKTRKQKHQPMDARKVSHQPVCSKGHEQKPLSSKATSVSKLVLSKEKYMQMFDSESSDEDNALAKKGLLCCSDKKKGMTFPTPNAAGKITHPTSSAKKAIRKEARPNGLAQIQEEGPTATNSPIESTYLPVAHMKSVSIDGSSGTSATFESPAKKAPKRGIRETSPLNGNELQQLISTIPIADEKASSLMEKVDNCIGRESFDDRNKDFMHMENSSTKTAVEKSTKQKRVSGKKSEIPKSIITNNEILEKNSTETLSEKQVAAKAKKQSVRKTGATGKPSTSRLKKSEKTKTTSSVTSTSKLEQVREEESDVSSEVLAKPKPQCSTTASILKQGGDGASNSEDDLQIALAMSKATYKEEQQKRKKTKREPSNKQPQSPAEKSMTVFNNQSVACNSTALANDTACYRVLPKRRGVKRAAAVSTTEEKTATNSSSSPTSSLEEMGSPTGGDPDCTVVTSTTGCEPPASERQEIPATIKITKRGILLHSPSAPEGASFTLTEQGLGKIIGERWARKYLKYHIGSRSFDSRHSVYYQPTPQLAAALSAPQDAQNIGNISGSSASDDDIFEQINRYGTVYSILENNSGDK', 979, 'Q9VEN2;', 'KD01526', 'Drosophila melanogaster (Fruit fly)', 'cal1', '#Chromosome alignment defect 1 {ECO:0000313|EMBL:AAF55389.1}', '-', '-', '42065'),
(1527, 'Q8N0S6', 'Centromere protein L', 'k', 38998, 'Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:16716197}.', 'MDSYSAPESTPSASSRPEDYFIGATPLQKRLESVRKQSSFILTPPRRKIPQCSQLQEDVDPQKVAFLLHKQWTLYSLTPLYKFSYSNLKEYSRLLNAFIVAEKQKGLAVEVGEDFNIKVIFSTLLGMKGTQRDPEAFLVQIVSKSQLPSENREGKVLWTGWFCCVFGDSLLETVSEDFTCLPLFLANGAESNTAIIGTWFQKTFDCYFSPLAINAFNLSWMAAMWTACKMDHYVATTEFLWSVPCSPQSLDISFAIHPEDAKALWDSVHKTPGEVTQEEVDLFMDCLYSHFHRHFKIHLSATRLVRVSTSVASAHTDGKIKILCHKYLIGVLAYLTELAIFQIE', 344, 'Q8N0S6; Q5TEL5; Q96ND4;', 'KD01527', 'Homo sapiens (Human)', 'CENPL', '#Centromere protein L#CENP-L#Interphase centromere complex protein 33', '-', 'ENSG00000120334', '-'),
(1528, 'Q6BXB6', 'Probable kinetochore protein SPC24', 'GO:0000777', 26412, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MFHEKPDKLLLSSIESFEIEPDLLTLRRIEEVINKTNQYRSNTIENYETKLNTMKSEFQSLMSEINLLTKVSGINYENLKLLGNGNEESMGDLSNKNIFNVMNEKSIELDNLKLSLAKNLNDLESQINSMNITKKDLMEKYELVKMKNDNLINDNILKNPDSKAIKINIYKNLGVEIESGEEGETENKQDKVIIYNKETNLSSILNIDDKYSEYFITNYIWDRLQGY', 227, 'Q6BXB6;', 'KD01528', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'SPC24', '#Probable kinetochore protein SPC24', '-', '-', '2913209'),
(1529, 'P79955', 'Carboxy-terminal kinesin 2', 'GO:0003777', 71949, 'Promotes mitotic spindle assembly.', 'MDSTDKKVQVASRLPVPPKRKYVSNDENQEQMQRKRLRSSLESELPAVRVAASIATSKPRAAPVAALPKPQVIGRQSLAVMRPKNSGPGITSTSFSGKTKVSSSVTQPAAIGAEKKKRAAWDLKGQVNDMRDTVSNYKGKMQNLTGENARLLNSKEKLQREVEVLASENSKLSQERCTLESQLREVRQQVSTFEREVARLTELCQRQEKELSSHTNTIEELQGANAILTKQLLDKEVKLDCVSGENTSLKHTVNEQTDEIAALKVCLAEKDTEVHSLDTERRRLHNLVQELKGNIRVFCRVRPTLTPERELPAGHISFPSNDGKAIVLSKMEESHIGREKKDAVKYDFNFDCVFPPPCSQESVFEEISLLVQSALDGYPVCIFAYGQTGSGKTYTMEGPEDVTDDSMGMIPRAIHQIFSSAEELKAKGWQYTFTASFLEIYNETIRDLLINRPDKKLEYEIRKVNSANMLLYVTNLRYVKVSCVEEVHELLKIAKANRSVAKTAINDRSSRSHSVFQLKIEGENKQRDLKTSSMISLIDLAGSERLDRSLSTGDRLKETQCINTSLSTLGMVITSLCNKDSHIPYRNSKLTYLLQNSLGGNAKVLMFVNISPLEENFAESLNSLRFASKVNECVIGTARANRK', 643, 'P79955;', 'KD01529', 'Xenopus laevis (African clawed frog)', '', '#Carboxy-terminal kinesin 2#XCTK2', '-', '-', '394322'),
(1530, 'P58062', 'Serine protease inhibitor Kazal-type 7', 'c;k', 9232, 'Probable serine protease inhibitor.', 'MKITGGLLLLCTVVYFCSSSEAASLSPKKVDCSIYKKYPVVAIPCPITYLPVCGSDYITYGNECHLCTESLKSNGRVQFLHDGSC', 85, 'P58062; Q32LY0;', 'KD01530', 'Homo sapiens (Human)', 'SPINK7', '#Serine protease inhibitor Kazal-type 7#Esophagus cancer-related gene 2 protein#ECRG-2', '-', 'ENSG00000145879', '-'),
(1531, 'O14965', 'Aurora kinase A', 'GO:0032133===GO:0000780===c;k;s', 45809, 'Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle; centrosome duplication; centrosome separation as well as maturation; chromosomal alignment; spindle assembly checkpoint; and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins; including ARHGEF2; BORA; BRCA1; CDC25B; DLGP5; HDAC6; KIF2A; LATS2; NDEL1; PARD3; PPP1R2; PLK1; RASSF1; TACC3; p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway; and particularly the checkpoint-response pathways critical for oncogenic transformation of cells; by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors; the protein phosphatase type 1 (PP1) isoforms; to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. {ECO:0000269|PubMed:11039908; ECO:0000269|PubMed:11551964; ECO:0000269|PubMed:12390251; ECO:0000269|PubMed:13678582; ECO:0000269|PubMed:14523000; ECO:0000269|PubMed:14702041; ECO:0000269|PubMed:14990569; ECO:0000269|PubMed:15128871; ECO:0000269|PubMed:15147269; ECO:0000269|PubMed:15987997; ECO:0000269|PubMed:17125279; ECO:0000269|PubMed:17360485; ECO:0000269|PubMed:17604723; ECO:0000269|PubMed:18056443; ECO:0000269|PubMed:18615013; ECO:0000269|PubMed:19351716; ECO:0000269|PubMed:19357306; ECO:0000269|PubMed:19668197; ECO:0000269|PubMed:19812038; ECO:0000269|PubMed:20643351; ECO:0000269|PubMed:9606188}.', 'MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRVPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS', 403, 'O14965; E1P5F9; O60445; O75873; Q9BQD6; Q9UPG5;', 'KD01531', 'Homo sapiens (Human)', 'AURKA', '#Aurora kinase A#2.7.11.1#Aurora 2#Aurora/IPL1-related kinase 1#ARK-1#Aurora-related kinase 1#hARK1#Breast tumor-amplified kinase#Serine/threonine-protein kinase 15#Serine/threonine-protein kinase 6#Serine/threonine-protein kinase aurora-A', '-', 'ENSG00000087586', '-'),
(1532, 'G5EEM5', 'Zygote defective protein 9', 'GO:0000776===c;k', 156189, 'Plays a major role in organizing microtubules and spindle poles during mitosis and meiosis in one-cell stage embryos. Required for default nucleus positioning in oocytes. {ECO:0000269|PubMed:12956952; ECO:0000269|PubMed:15866166; ECO:0000269|PubMed:16054029; ECO:0000269|PubMed:17666432; ECO:0000269|PubMed:2249759; ECO:0000269|PubMed:3949074; ECO:0000269|PubMed:6684994; ECO:0000269|PubMed:9606208}.', 'MSNWDYLDEVDILPKLPPNFDELRESKKWQERKEALEALLKVLTDNERLSTKASYAELIGHLQMVLAKDANINCQALAAKCIGKFATGLRAKFSSFAGPLLPVIFEKMKEKKPMLREPLVDCSNEVGRTMQSLETGQEDILAALAKPNPQIKQQTALFVARQLDLVVPAKQPKGFIKAVVPVFGKLTGDADQDVREASLQGLGAVQRIIGDKNVKNLLGDASSDEGKMKKIGEYAEKSTASFAEEQAKNAPPVAPTSSTPSASAASGDPSGGTATAVVSSGAPVAEADPWDFLDAFDVLSKMPDGFDTNIESKKWQERKEALEGLLQLITANPKLDPKANYGALVERLQKVLEKDANINVAALAANCITGIANGLRTKFQPFAVSVTPIIFEKFKEKKPTLRDPLVACIDAVVATTNLEAVGEIVLAALGKPNPSIKTQTDLFLQRCFMKLNSQTMPKKTLKTLIPSLIKHSGDSDSEVREASYAAMGAMMRAIGEKPSLQLLADIASDNLKMSKIKEFHQKALDEAGPAEIAEMVKSIHKADAPPAAAPPKKTAPPKKQPEDEEVVEEEDEPLKPPPGDKKKKVPVKENEENEPPVVAPKAELLLSDNEDKKQRIKEEKQLKLVKWNFQAPTDEHISQLQTLLGNQAKVSLMSQLFHKDFKQHLAALDSLVRLADTSPRSLLSNSDLLLKWCTLRFFETNPAALIKVLELCKVIVELIRDTETPMSQEEVSAFVPYLLLKTGEAKDNMRTSVRDIVNVLSDVVGPLKMTPMLLDALKSKNARQRSECLLVIEYYITNAGISPLKSLSVEKTVAPFVGDKDVNVRNAAINVLVACFKFEGDQMWKAAGRMADKDKSLVEERIKRTGVKPGSGVVTSPPTGGPKILVPQQQGSVVRRPASRSRTREPEPEEVQSDTFTIRQDTMPPKTSSRYALRDDVFSSAMGRLDGTQVITPPQPVNGWSNNTFQMKRTNSSSSISSIDTSDQIQRSINNISSSLADVAQDAMFQVTYVLNQPEQRHLVDRRADLVFRASAAQLDLVIEEFNAGRDVSGTMDACTQMLFILMGGVETEHGLEPLNASPDTVKAIISSVLRCIIQIGNTESGYGMARSLNRLAMRLIYRVELSNLLCGLILAMTESLQMNTGITELVSKLSSKWCDELEKRRAQLRASDIVDSFNAFYVCALTELKMDISDSHILIVDNYLERVILQQGDVVLDAARRLSRPHMHLTSMINKILQMMRERKIDPIMPGTLEARMPQEDEAVVVRSGVQVSIDNILRDTSMAVKHIEQLNILIASSDRSWNEYMEYLKNNPMGELIKELVGECSRKKRIDFNLSHVVKSSMAVFKAMAATGPVQEEGRITPTDINRMDTMIVGTPLSRGDATITRARGNMIRPKRTTLSRDQMANIRHTLDRVKNH', 1415, 'G5EEM5;', 'KD01532', 'Caenorhabditis elegans', 'zyg-9', '#Zygote defective protein 9 {ECO:0000303|PubMed:9606208}', '-', '-', '174350');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1533, 'Q8BW22', 'Calcium-responsive transactivator', 'GO:0000776===GO:0000777===GO:0000780', 43729, 'Transcriptional activator which is required for calcium- dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex; a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons; transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx; RB1 is dephosphorylated by calcineurin; which leads to release of the repressor complex. At the same time; there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism; which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter; and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP. {ECO:0000269|PubMed:14716005; ECO:0000269|PubMed:19081374}.', 'MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILDYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALSQSGSSQGLHPQGSLSDTVSTGLPPASLMQGQIGNGPNHVSMQQTAQSTLPTTSMSLSGSGHGTGPGYSHSGPTSQSVPMQGQGAISNYVSRTNINMQSNPVSMMHQQAATSHYNSAQGGSQHYQGQAPIAMMGQGGQGGSMMGQRPMAPYRPSQQGSSQQYLGQEEYYSEQYSHSQGSAEPMSQQYYPDGHGDYAYQQSSYTEQSYDRSFEDPTQHYYEGGNSQYSQQQAGYQQGTAQQQTYSQQQYPNQQSYPGQQQGYGPAQGAPSQYSSYQQGQGQQYGSYRTSQTGPSAQQQRPYGYEQGQYGNYQQ', 402, 'Q8BW22; Q6A014; Q7TQF3; Q8BYQ7;', 'KD01533', 'Mus musculus (Mouse)', 'Ss18l1', '#Calcium-responsive transactivator#SS18-like protein 1', '-', '-', '269397'),
(1534, 'Q7M6Z5', 'Kinesin-like protein KIF27', 'GO:0003777', 158880, 'Plays an essential role in motile ciliogenesis. {ECO:0000250}.', 'MEEIPIKVAVRIRPLLCKEVLHNHQVCVRDIPKTQQIIIGRDRVFTFDFVFGKNSTQDEVYSTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHVASVVDGQKGIIPRAIQEIFQSISGNPNIDFKIKVSYIEVYKEDLRDLLELETSMKDLHIREDEKGNTVIVGAKECQVDSVEDVMGLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVGKSAEATEDGEWCSHRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHVPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSDFDESLNSLKYANRARNIRNKPTLNFSPQADRMDEMEFEIKLLREALQSHQASISQTSQTASENVPDQNRIHSLEEQIAQLQEECLGYQDCIEQAFAFLVDLKDAVRLNQKQQHKLQQWFSRTQEVRKAVLTPLPGNQSIGNLEEGPQHVTVLQLKRELKKYQCALAADQVVFTQKELELEELRRQMQLMAQESKGHAVSLKEAQKVNRLQNEKIIEQQLLVDQLSEELAKRSSSMPTSTKESCGDGPDARAPEKRPHTAPFDSHWGHYVYIPSRQDFKKVCSSSPVYSLDQVFAGFRTRSQMLMGHLEDQDEVLHCQFSDNSDDEDSEGQEKPRVRSRSHSWVKKPGSVCSLVEMSDTQAECQRSYLGNGDLKMESLQESQELNLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELIKTGDNAKSVSRQYSLKVTKLEHEAEQAKVELTETRKQLQELEGKDLSDVALKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRASELEQNVDHLKYQKVQLQRRLREESEKKKQLDAEVKRDQQKLKELQLNAGQGEGLHPKAEDTDAFNLNRRKGPFRSVDQLQKLDEQRKWLDEEVEKVLSQRQELEMLEEELKKREAIVSKKEALLQEKSHLENKKLRSSQALSTDSLKISARLNLLDQELSEKSLLLENSPTEEKVKISEQVQALQREREQLQRQRNSVDEKLRHGRVLSPKEEHLLFQLEEGIEALEAAIEFKNESIQNRQSSLKSSFQNLSQSESNVLEKLVCLNIAEIRAILFKYFNKVINLREAERKQQLQNKEMKMKVLERDNMVHELESALEYLRLQCDRRLTLQQKEHEQKMQLLLHHFKDQDGEGIIETLNKYEDKIQQLEKDLYFYKKTSRDLKKRLKDPVQGAVQWQRTLTEHHDAGDGVLNPEEAAVLSEELKWASRTENTKLNGREKEVDNSSSSLKTPPLTQQILEDGPDSLPVCGSLAPSSGQLQSSADKTEAHAFTQSQSPPPPQLQPVRSIAQLQGVKPVKVCRRELRQISALELTLRRSSLGAGVRSVTADSLEEPEES', 1394, 'Q7M6Z5;', 'KD01534', 'Rattus norvegicus (Rat)', 'Kif27', '#Kinesin-like protein KIF27', '-', '-', '246209'),
(1535, 'Q5T7B8', 'Kinesin-like protein KIF24', 'GO:0003777', 151903, 'Microtubule-dependent motor protein that acts as a negative regulator of ciliogenesis by mediating recruitment of CCP110 to mother centriole in cycling cells; leading to restrict nucleation of cilia at centrioles. Mediates depolymerization of microtubules of centriolar origin; possibly to suppress aberrant cilia formation. {ECO:0000269|PubMed:21620453}.', 'MASWLYECLCEAELAQYYSHFTALGLQKIDELAKITMKDYSKLGVHDMNDRKRLFQLIKIIKIMQEEDKAVSIPERHLQTSSLRIKSQELRSGPRRQLNFDSPADNKDRNASNDGFEMCSLSDFSANEQKSTYLKVLEHMLPDDSQYHTKTGILNATAGDSYVQTEISTSLFSPNYLSAILGDCDIPIIQRISHVSGYNYGIPHSCIRQNTSEKQNPWTEMEKIRVCVRKRPLGMREVRRGEINIITVEDKETLLVHEKKEAVDLTQYILQHVFYFDEVFGEACTNQDVYMKTTHPLIQHIFNGGNATCFAYGQTGAGKTYTMIGTHENPGLYALAAKDIFRQLEVSQPRKHLFVWISFYEIYCGQLYDLLNRRKRLFAREDSKHMVQIVGLQELQVDSVELLLEVILKGSKERSTGATGVNADSSRSHAVIQIQIKDSAKRTFGRISFIDLAGSERAADARDSDRQTKMEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELKKGIKCCTSVTSRNRTSGNSSPKRIQSSPGALSEDKCSPKKVKLGFQQSLTVAAPGSTRGKVHPLTSHPPNIPFTSAPKVSGKRGGSRGSPSQEWVIHASPVKGTVRSGHVAKKKPEESAPLCSEKNRMGNKTVLGWESRASGPGEGLVRGKLSTKCKKVQTVQPVQKQLVSRVELSFGNAHHRAEYSQDSQRGTPARPASEAWTNIPPHQKEREEHLRFYHQQFQQPPLLQQKLKYQPLKRSLRQYRPPEGQLTNETPPLFHSYSENHDGAQVEELDDSDFSEDSFSHISSQRATKQRNTLENSEDSFFLHQTWGQGPEKQVAERQQSLFSSPRTGDKKDLTKSWVDSRDPINHRRAALDHSCSPSKGPVDWSRENSTSSGPSPRDSLAEKPYCSQVDFIYRQERGGGSSFDLRKDASQSEVSGENEGNLPSPEEDGFTISLSHVAVPGSPDQRDTVTTPLREVSADGPIQVTSTVKNGHAVPGEDPRGQLGTHAEYASGLMSPLTMSLLENPDNEGSPPSEQLVQDGATHSLVAESTGGPVVSHTVPSGDQEAALPVSSATRHLWLSSSPPDNKPGGDLPALSPSPIRQHPADKLPSREADLGEACQSRETVLFSHEHMGSEQYDADAEETGLDGSWGFPGKPFTTIHMGVPHSGPTLTPRTGSSDVADQLWAQERKHPTRLGWQEFGLSTDPIKLPCNSENVTWLKPRPISRCLARPSSPLVPSCSPKTAGTLRQPTLEQAQQVVIRAHQEQLDEMAELGFKEETLMSQLASNDFEDFVTQLDEIMVLKSKCIQSLRSQLQLYLTCHGPTAAPEGTVPS', 1368, 'Q5T7B8; Q2TB93; Q5T7B5; Q5T7B7; Q6ZU97; Q6ZUZ2; Q86XZ0; Q9NV43;', 'KD01535', 'Homo sapiens (Human)', 'KIF24', '#Kinesin-like protein KIF24', '-', 'ENSG00000186638', '-'),
(1536, 'Q7M6Z4', 'Kinesin-like protein KIF27', 'GO:0003777', 158956, 'Plays an essential role in motile ciliogenesis. {ECO:0000269|PubMed:19305393}.', 'MEEIPIKVAVRIRPLLCKEVLHNHQVCVRDIPNTQQIIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHVASVVEGQKGIIPRAIQEIFQSISENPSIDFKIKVSYIEVYKEDLRDLLELETSMKDLHIREDEKGNTVIVGAKECQVESVEDVMSLLQVGNAARHTGTTQMNEHSSRSHAIFTISVCQVEKNAEAAENGEWYSHRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSDFDESLNSLKYANRARNIRNKPALNISPQADRMDEMEFEIKLLREALQSHQASISQASQASSENVPDQNRIHSLEEQVAQLQEECLGYQDCIEQAFAFLVDLKDAVKLNQKQQHKLQEWFSRTQEVRKAVLTPLPGNQGIGNLEEGPQHLTVLQLKRELKKYQCALAADQVVFTQKDLELEELRTQVQLMMQESKGHAVSLKEAQKVNRLQNEKIIEQQLLVDQLSAELAKRSLSVPTSAKESCGDGPDARASEKRPHTAPFESHWGHYVYIPSRQDFKKVCSSTPVYSLDQVFAGFRTRSQMLMGHLEDQDEVLHCQFSDNSDDEDSEGQEKPRVRSRSHSWAKKPGSVCSLVELSDTQAESQRSYLGNGDLKMESLQESQEINLQKLRTSELILNKAKQKMRELTINIRMKEDLIKELIKTGNNAKSVSRQYSLKVTKLEHEAEQAKVELTETRKQLQELESKDLSDVALKVKLQKEFRKKMDAAKMRVQVLQKKQQDSKKLASLSIQNEKRASELEHNVDHLKYQKVQLQRRLREEGEKKKQLDAEIKRDQQKIKELQLKAGQGEGLNPKAEDQDGFNLNRRKSPFRSGDQFQKLDEQRKWLDEEVEKVLSQRQELEMLEEDLKKREAIVSKKEALLQEKSLLENKKLRSSQALSTDGLKISARLNLLDQELSEKSLQLESSPTEEKMKISEQVQALQRERDQLQRQRNSVDERLKHGRVLSPKEEHLLFQLEEGIEALEAAIEFKNESIQSRQNSLKASFQNLSQSEANVLEKLVCLNITEIRAILFKYFNKVINLRETERKQQLQNKEMKMKVLERDNVVHELESALEHLRLQCDRRLTLQQKEHEQKMQLLLQHFKDQDGDSIIETLKNYEDKIQQLEKDLYFYKKTSRDLKKRLKDPAQGAAQWQRTLTEHHDAGDGVLNPEETTVLSEELKWASRTENTKLNGSEREVDNSSSSLKTQPLTQQIPEDGPDSLPARSSIAPSSGQLQSIADKTEARPFTHSQSPVPHQFQPVRSIGPLQGVKPVKLCRRELRQISAMELSLRRCSLGAGGRSMTADSLEDPEEN', 1394, 'Q7M6Z4; Q14AX5; Q8BMB9;', 'KD01536', 'Mus musculus (Mouse)', 'Kif27', '#Kinesin-like protein KIF27', '-', '-', '75050'),
(1537, 'O14576', 'Cytoplasmic dynein 1 intermediate chain 1', 'GO:0000776===GO:0000777===GO:0003777===GO:0005868===SCL===c;k;m', 72955, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores.', 'MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETEALLQSIGISPEPPLVQPLHFLTWDTCYFHYLVPTPMSPSSKSVSTPSEAGSQDSGDLGPLTRTLQWDTDPSVLQLQSDSELGRRLHKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSEEDEEDEEMVESKVGQDSELENQDKKQEVKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYNNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNNDTEVPTASVAIEGASALNRVRWAQAGKEVAVGDSEGRIWVYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA', 645, 'O14576; B4DME3; F5H050; G5E9K1; Q8TBF7; Q9Y2X1;', 'KD01537', 'Homo sapiens (Human)', 'DYNC1I1', '#Cytoplasmic dynein 1 intermediate chain 1#Cytoplasmic dynein intermediate chain 1#Dynein intermediate chain 1; cytosolic#DH IC-1', '-', 'ENSG00000158560', '-'),
(1538, 'Q99JD4', 'CLIP-associating protein 2', 'GO:0000777', 140638, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). {ECO:0000250}.', 'MRRLICKRICDYKSFDDEESVDGNRPSSAASAFKVPAPKTPGNPVNSARKPGSAGGPKAGGTSKEGGAGAVDEDDFIKAFTDVPSIQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSAVAGRVSVGGSKASPLPGSLQRSRSDIDVNAAAGAKAHHAAGQAVRSGRLGAGALNPGSYASLEDTSDKMDGTASEDGRVRAKLSTPLVAVGNAKTDSRGRSRTKMVSQSQPGSRSGSPGRVLTTTALSTVSSGAQRILVNSASAQKRSKIPRSQGCSREASPSRLSVARSSRIPRPSVSQGCSREASRESSRDTSPVRSFQPLGPGYGMSQSSRLSSSVSAMRVLNTGSDVEEAVADALLLGDIRTKKKPARRRYESYGMHSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASSNWSERKEGLLGLQNLLKNQRTLSRVELKRLCEIFTRMFADPHGKVFSMFLETLVDFIQVHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRESFPNDLQFNILMRFTVDQTQTPSLKVKVAILKYIETLAKQMDPGDFINSSETRLAVSRVITWTTEPKSSDVRKAAQSVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLRNTGNGTQSSMGSPLTRPTPRSPANWSSPLTSPTNTSQNTLSPSAFDYDTENMNSEDIYSSLRGVTEAIQNFSFRSQEDMSEPLKRDPKKEDGDTVCSGPGMSDPRAGGDAPDSSQPALDNKASLLHSVPLHSSPRSRDYNPYNYSDSISPFNKSALKEAMFDDDADQFPDDLSLDHSDLVAELLKELSNHNERIEERKIALYELMKLTQEESFSVWDEHFKTILLLLLETLGDKEPTIRALALKVLKEILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEAASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLIQGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGSAGADPTTDVSGQS', 1286, 'Q99JD4;', 'KD01538', 'Rattus norvegicus (Rat)', 'Clasp2', '#CLIP-associating protein 2#Cytoplasmic linker-associated protein 2', '-', '-', '114514'),
(1539, 'Q8TF76', 'Serine/threonine-protein kinase haspin', 'GO:2000751', 88495, 'Serine/threonine-protein kinase that phosphorylates histone H3 at ''Ser-3'' (H3T3ph) during mitosis. This positions and activates AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion; metaphase alignment and normal progression through the cell cycle. {ECO:0000269|PubMed:11228240; ECO:0000269|PubMed:15681610; ECO:0000269|PubMed:17084365; ECO:0000269|PubMed:20705812; ECO:0000269|PubMed:20929775}.', 'MAASLPGPGSRLFRTYGAADGRRQRRPGREAAQWFPPQDRRRFFNSSGSSDASIGDPSQSDDPDDPDDPDFPGSPVRRRRRRPGGRVPKDRPSLTVTPKRWKLRARPSLTVTPRRLGLRARPPQKCSTPCGPLRLPPFPSRDSGRLSPDLSVCGQPRDGDELGISASLFSSLASPCPGSPTPRDSVISIGTSACLVAASAVPSGLHLPEVSLDRASLPCSQEEATGGAKDTRMVHQTRASLRSVLFGLMNSGTPEDSEFRADGKNMRESCCKRKLVVGNGPEGPGLSSTGKRRATGQDSCQERGLQEAVRREHQEASVPKGRIVPRGIDRLERTRSSRKSKHQEATETSLLHSHRFKKGQKLGKDSFPTQDLTPLQNVCFWTKTRASFSFHKKKIVTDVSEVCSIYTTATSLSGSLLSECSNRPVMNRTSGAPSSWHSSSMYLLSPLNTLSISNKKASDAEKVYGECSQKGPVPFSHCLPTEKLQRCEKIGEGVFGEVFQTIADHTPVAIKIIAIEGPDLVNGSHQKTFEEILPEIIISKELSLLSGEVCNRTEGFIGLNSVHCVQGSYPPLLLKAWDHYNSTKGSANDRPDFFKDDQLFIVLEFEFGGIDLEQMRTKLSSLATAKSILHQLTASLAVAEASLRFEHRDLHWGNVLLKKTSLKKLHYTLNGKSSTIPSCGLQVSIIDYTLSRLERDGIVVFCDVSMDEDLFTGDGDYQFDIYRLMKKENNNRWGEYHPYSNVLWLHYLTDKMLKQMTFKTKCNTPAMKQIKRKIQEFHRTMLNFSSATDLLCQHSLFK', 798, 'Q8TF76; Q5U5K3; Q96MN1; Q9BXS7;', 'KD01539', 'Homo sapiens (Human)', 'GSG2', '#Serine/threonine-protein kinase haspin#2.7.11.1#Germ cell-specific gene 2 protein#H-haspin#Haploid germ cell-specific nuclear protein kinase', '-', 'ENSG00000177602', '-'),
(1540, 'O45935', 'Kinesin-like protein', 'k', 123139, '', 'MSSDASLRVVVRARPMNGRETKEGASRCVQFYENTKQIVINESATFTFDAVFADTSDQESVYETTALPLLDRIFAGFNATVLAYGQTGSGKTYTMGTEDNVGTDEMRRGIIPRLVSALFQRIMNTEAPESFAVTVSMFEVYGDNVYDLLRPDKVKLNVHGDEKNCTVVNLTAVPVIDLKGALKQLAVGCHYRTKAETAMNAMSSRSHAVFTVFVEKTATAECDSAFSAKLQLVDLAGSERLKKTEAEGNRMKEGININGGLLILSQVIAALATKQKHIPYRNSVITRVLQDSLGGNSFTVFLACISPADSNSQETLNTLRYADRAKQIKNKPIVNKNPKAEEIAILQAQLKRLQKENADLKQGIAPAEVRFNDANNSAEILSLKEEVVRKTEQLKERAMKQSECIIRMSALTQKNSRLEEDKAKLQSMLTDVRNTVLNEEMLDAAEVVRSIQQVVGDTEESTTLADDDNDETALGGQDDTIYDTERLPELQAELDDLEKQIAMKDENRQKALDEQRAFIEAMQQRESEKTQLVVRISELETEMNKLRQEGKKVTTAAKLAEERRQKLKDLERQHAEDKKVLNDMKKLQETRRRMEETLKKTEDELKNLKTQRLRLLREQRAEASKFQAFKQKHEREMAQMKSKLQKRENDVAIQKRMTDQKLTVLQMRLTEANRANKTLRELNLKRANRKSSPTNASALQNMIEEELEHEMCAQRSHWLCEDLRRQRHDLMQNINTVESMKFEGGKRRRISASADPNVSVVIEGEEEFEVKRQKELTFLRASLETLNEEIKDSLRNETIAGNEERANSRWEKVPAEMRPAFEAVYAQAVAHIRKEIELEFKLARTKSEFTAKIASKASHEEKRKKEDEEMRAKYRELAQCLEDAKSGLHEKIAFLLCLIKENRVDENAIQQFESLKNQFCDVEQKVKKASRRKTTNFMGGLTPKPELQRNERARRAVKYYGNVVNSEDVTMDDSRHQKRKDHSLLAVEMNRTTDDNVKRRVAMSPIKCDDDTRLTEEDEDIENEAMNNATFVKDSFNSATIVLDDSQPSPSNSTFVIGAAPTSEADGVPPIKRKSRRTDLGPL', 1083, 'O45935;', 'KD01540', 'Caenorhabditis elegans', 'klp-19', '#Kinesin-like protein {ECO:0000256|RuleBase:RU000394}', '-', '-', '176750'),
(1541, 'O95072', 'Meiotic recombination protein REC8 homolog', 'GO:0000778===c;k', 62614, 'Required during meiosis for separation of sister chromatids and homologous chromosomes. Proteolytic cleavage of REC8 on chromosome arms by separin during anaphase I allows for homologous chromosome separation in meiosis I and cleavage of REC8 on centromeres during anaphase II allows for sister chromatid separation in meiosis II (By similarity). {ECO:0000250}.', 'MFYYPNVLQRHTGCFATIWLAATRGSRLVKREYLRVNVVKTCEEILNYVLVRVQPPQPGLPRPRFSLYLSAQLQIGVIRVYSQQCQYLVEDIQHILERLHRAQLQIRIDMETELPSLLLPNHLAMMETLEDAPDPFFGMMSVDPRLPSPFDIPQIRHLLEAAIPERVEEIPPEVPTEPREPERIPVTVLPPEAITILEAEPIRMLEIEGERELPEVSRRELDLLIAEEEEAILLEIPRLPPPAPAEVEGIGEALGPEELRLTGWEPGALLMEVTPPEELRLPAPPSPERRPPVPPPPRRRRRRRLLFWDKETQISPEKFQEQLQTRAHCWECPMVQPPERTIRGPAELFRTPTLSGWLPPELLGLWTHCAQPPPKALRRELPEEAAAEEERRKIEVPSEIEVPREALEPSVPLMVSLEISLEAAEEEKSRISLIPPEERWAWPEVEAPEAPALPVVPELPEVPMEMPLVLPPELELLSLEAVHRAVALELQANREPDFSSLVSPLSPRRMAARVFYLLLVLSAQQILHVKQEKPYGRLLIQPGPRFH', 547, 'O95072; A8K576; D3DS62; Q658V5; Q6IA92; Q8WUV8; Q9BTF2; Q9NVQ9;', 'KD01541', 'Homo sapiens (Human)', 'REC8', '#Meiotic recombination protein REC8 homolog#Cohesin Rec8p', '-', 'ENSG00000100918', '-'),
(1542, 'Q28G25', 'Bardet-Biedl syndrome 4 protein homolog', 'GO:0003777', 56991, 'May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. Required for ciliogenesis (By similarity). {ECO:0000250}.', 'MAEEQQEVVPQESGLRKSRVQKVPELPILERRNWLIHLHYVRKDYESCKAVIKEQLQATQGVCEYAVYVQALILRLEGKIQESLELFQTCAVLNPTSSDNLKQVARSLFLLGKHKAAVEVYNEAARLNQKDWEICHNLGVCYLFLKDLSKSKEQLTLALQLHRQDLSAITLGKIQLQEGDIDGAIQTFTQALQLSPENTELLTTLGLLYLQNGLFQKAFEYLGNALTYDPSNYKGILAAGCMMQSHGDYDVALSKYRVAASSVPESSPLWNNIGMCFYGKKKYVAAISCLKRALYLSPFDWRVLYNLGLVHLSMQQYASAFHFLSAAISLHHGNAGLYMLLAVALTYLDDIENAKSSYQQAASLDQTDPLVNLNFAVLLYNQGDKKGALGQYQELERKVSALRETSTEFDPEMVDMAQKLGAALQVGESLVWTRQTKDPKGKQRGAGKGPGAEQAPLGSNQALGRAMSSAAGYSKASGLSSGITISTVSKHPSLPLEPEDPSLTSSTAPDYRRGHS', 516, 'Q28G25;', 'KD01542', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'bbs4', '#Bardet-Biedl syndrome 4 protein homolog', '-', '-', '549034'),
(1543, 'O14974', 'Protein phosphatase 1 regulatory subunit 12A', 'GO:0000776', 115281, 'Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex; involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN- dependent suppression of HIF1A activity. {ECO:0000269|PubMed:18477460; ECO:0000269|PubMed:19245366; ECO:0000269|PubMed:20354225}.', 'MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIEPEKNASRIESLEQEKVDEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPLASVTNANTSSTQAAPVAVTTPTVSSGQATPTSPIKKFPTTATKISPKEEERKDESPATWRLGLRKTGSYGALAEITASKEGQKEKDTAGVTRSASSPRLSSSLDNKEKEKDSKGTRLAYVAPTIPRRLASTSDIEEKENRDSSSLRTSSSYTRRKWEDDLKKNSSVNEGSTYHKSCSFGRRQDDLISSSVPSTTSTPTVTSAAGLQKSLLSSTSTTTKITTGSSSAGTQSSTSNRLWAEDSTEKEKDSVPTAVTIPVAPTVVNAAASTTTLTTTTAGTVSSTTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESETSREDEYKQKYSRTYDETYQRYRPVSTSSSTTPSSSLSTMSSSLYASSQLNRPNSLVGITSAYSRGITKENEREGEKREEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPYSSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSLLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK', 1030, 'O14974; B4DZ09; F8VWB4; Q2NKL4; Q569H0; Q86WU3; Q8NFR6; Q9BYH0;', 'KD01543', 'Homo sapiens (Human)', 'PPP1R12A', '#Protein phosphatase 1 regulatory subunit 12A#Myosin phosphatase-targeting subunit 1#Myosin phosphatase target subunit 1#Protein phosphatase myosin-binding subunit', 'BIOMD0000000088,Maeda2006_MyosinPhosphorylation;', 'ENSG00000058272', '-'),
(1544, 'P40977', '1-phosphatidylinositol 4;5-bisphosphate phosphodiesterase 1', 'k', 102673, 'The production of the second messenger molecules diacylglycerol (DAG) and inositol 1;4;5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.', 'MNCEMVTSPESVNLGDSNRAVSPFCLPDCSENAVAQTRSKTLDNAALDLPYVGNRKKSEQDFFKMLSSRDRDAHSTLRKRSNSLSSFLSTKSTSASENKFHGGLNWLSLKLNLLLRLQGRMNSARTNTSMNPYSCDSNENLSTLSSVNQNFNSRQLLATIVPESIQNGCSLLRITKKKVRQRKVSLDPISGYLMLDKNTGKAYKKLCVDDIKEIRQGRDARNYREQYKISSENEKRWFTIIYCADNKLKAMHMISPTLDAHNQWIMALEGLKTYRLNEFIIGLNLVCHQGEKMIDYSENLNPWEKLEKEQSAQLDLGDVHRMCQMLHLNASMEFLEETFQKADADHSGKLSFEEFQHFVSLLKTRSEIVDIFKEYTSGSDKMSLEQFRHFLSTSQKARLDSDSIRTLYVSFCSNDDSKMGLIEFTSFLLSPHNSPVVPVIQDMSRPLNEYLISSSHNTYLLGKQFGGESSIEGYIRSLQRGCKCIEIDCWDGPNGPVVCHGHTFTSMIKFNDVIDAIRKYAFVVSPYPLFISLEIHCCPDQQRQMVSYMKQAFGDTLVMKPVTANESVLPSPEDLLNKILLKVKCSATPLHQFSTDILKVGITDSSTDTTESSELENSELTGLRKGKRRMKNIIVQELQQLAPYARSLKFRNFSLPESKTYSHIFSFSERTIKKHGKAMVPRLSKHNLRYLCRVYPGPLRVGSTNFNPQVYWRLGVQMVALNWQTYDTGLQINDALFIADPPTGYLLKPPCQRIIGTTVGEEGLPRKIKLTIDVISGQQLRRARELSNSETLSPYVEIQVHSMEESPFRWCSKVVHENGFRPFWGETMVYESIISDDFYSMIRFLVHHRGSNGNDSIFANFTCPIDRLQQGYRHIRLLDMQGENLLFSSLFLKIKKEDI', 899, 'P40977;', 'KD01544', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'plc1', '#1-phosphatidylinositol 4;5-bisphosphate phosphodiesterase 1#3.1.4.11#Phospholipase C-1#PLC-1', '-', '-', '2541439'),
(1545, 'O43172', 'U4/U6 small nuclear ribonucleoprotein Prp4', 'k', 58449, 'Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex; one of the building blocks of the spliceosome.', 'MASSRASSTQATKTKAPDDLVAPVVKKPHIYYGSLEEKERERLAKGESGILGKDGLKAGIEAGNINITSGEVFEIEEHISERQAEVLAEFERRKRARQINVSTDDSEVKACLRALGEPITLFGEGPAERRERLRNILSVVGTDALKKTKKDDEKSKKSKEEYQQTWYHEGPNSLKVARLWIANYSLPRAMKRLEEARLHKEIPETTRTSQMQELHKSLRSLNNFCSQIGDDRPISYCHFSPNSKMLATACWSGLCKLWSVPDCNLLHTLRGHNTNVGAIVFHPKSTVSLDPKDVNLASCAADGSVKLWSLDSDEPVADIEGHTVRVARVMWHPSGRFLGTTCYDRSWRLWDLEAQEEILHQEGHSMGVYDIAFHQDGSLAGTGGLDAFGRVWDLRTGRCIMFLEGHLKEIYGINFSPNGYHIATGSGDNTCKVWDLRQRRCVYTIPAHQNLVTGVKFEPIHGNFLLTGAYDNTAKIWTHPGWSPLKTLAGHEGKVMGLDISSDGQLIATCSYDRTFKLWMAE', 522, 'O43172; O43445; O43864; Q5T1M8; Q96DG2; Q96IK4;', 'KD01545', 'Homo sapiens (Human)', 'PRPF4', '#U4/U6 small nuclear ribonucleoprotein Prp4#PRP4 homolog#hPrp4#U4/U6 snRNP 60 kDa protein#WD splicing factor Prp4', '-', 'ENSG00000136875', '-'),
(1546, 'O42934', 'Chromo domain-containing protein 2', 'k', 42955, 'Component of the kinetochore which plays a role in stabilizing microtubules and so allowing accurate chromosome segregation. {ECO:0000269|PubMed:10835380}.', 'MVKSADLDLMNSIISESDENFSPPPFTVEEAENSINNKSSTASLESPQNGSWHPSLYGLSVPEKTHIQNSLDLYSHGNSGSQKTHNVSFSCEIRKVKSSKLSPISNMEDSEDKKEEDESSSYKNEFKSSSSASVSSNFEKTSGSDDHNSQSPVPLNEGFEYIASSGSEDKNSDEEFAVEMILDSRMKKDGSGFQYYLKWEGYDDPSDNTWNDEEDCAGCLELIDAYWESRGGKPDLSSLIRLTRSRARSSNEASYVEKDESSNSDDSISYKRRRSRNAANRITDYVDSDLSESSMKEKQSKIEKYMKSDKSSKNFKPPFQKKSWEDLVDCVKTVQQLDNGKLIAKIKWKNGYVSTHDNIIIHQKCPLKIIEYYEAHIKFT', 380, 'O42934;', 'KD01546', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'chp2', '#Chromo domain-containing protein 2', '-', '-', '2540047'),
(1547, 'Q5R4H3', 'Kinesin-like protein KIF3A', 'GO:0003777', 80270, 'Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro (By similarity). Plays a role in primary cilia formation (By similarity). {ECO:0000250}.', 'MPINKSEKPESCDNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAIPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEIGEDGEKRKKRRDQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQGEIEGLLENIRQLSRELRLQMLIIDNFIPRDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKEKDPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKTGRRKRSAKPETVIDSLLQ', 702, 'Q5R4H3;', 'KD01547', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'KIF3A', '#Kinesin-like protein KIF3A#Microtubule plus end-directed kinesin motor 3A', '-', '-', '100173987'),
(1548, 'Q292S8', 'Kinesin-like protein costa', 'GO:0003777', 135215, '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 (By similarity). {ECO:0000250}.', 'MEIPIQVAVRICPYTEPSENRKPVAGAEADASAFGNAEAKAESFSDSEDNKNDASNRQRPEESTDANGNSEGGRQLKKETLPTDSNGNENGTIVPLGSGCCVQAIPISASALGLPSALPGGRAQDSIAAGLIQVGAHTVPVTHALGSGTTQSQLYYQTVFPLISLFLEGFDASVVTYGQRGQGKTYTLYGPGFECVYGEADQGVVQRCVRDIFAHIAGHSERTYAVNVGFVEICEGEVCDLLDMGNVHCQSVEEVFRWLQIGLATRQPKSAHSLFTLTLEQQWVSKEGLIQHRLSTASFSDLCATERWGEPPPGNPRDAGLQMLELVVNTLTDPSIMYGVNGNIPYGQTTLTTLLKDSFGGRAQTLVILCVSPQEQHVAETLGNLQFAFKVQCVRNYVIMNTYSDDNTPISPETMPNGSSNPGAGPLAQVAAGDNFGLQFAASQWFKLVSNAEGLFAKLMASNLISELEKEQIEEWLFLKQECEECLSSTEAMRSQKQLVPIQEAEEPEESVSEPPNSDNDTDNESQRPDLADKLESLMEEFRAKTDALIQSKHAEFLTKHPKAVMQSQERDKESKLDAPPEKDKEKIEERKTSIAGRRRSIQPGASLSTAELALLNRVALQQPTAQPPPSVLDPESSIDPLESSAGEGLRQAAIAAAAANAPIEQLQKKLRKLHAEIEGRQRQLKEIEQTMQVKQNIISELVKNSDTRSHAKQRFQKKKAKLEAECDKAKKHLAKALIQGREKGETERWSAIIAHIEHRLEDLSSMKHIAGESGQKLKKLQQSMAESRKQQEELEKKIRKESKLRDQLETELAKLKESRDGASGGKELVKLDSPEQQGRQLKAVQARITHLNHILREKSDNLEECAGGEGPAPAQQESLRHEIRNLRGTRDLLLDERCHLDRKLKRDKMLTQREERKLLECDEAIEAIDAAIEFKNELICGHKSIDTSDRLQREKGEQMLMARLNKLSPEEMRTLLYKYFNKVIDLRDSSRKLELQLVQLERERDAWEWKERVLSNAVRQARLEGERNAVLLQRQHEMKLTLMLRHLAEETSASSASYGERALAPGHQTSSGDFDYELDFYKAAATTTTTTNHKALVKPPKSTPSGAALEKYKDKEQRGAGRNIFAKFQVLTRYASSAASAAAAGSCSSTVDESTALIESTTTATATTTTTTTTTTTGGKGKERGLPNIRQDQLKRLMPAPTVTKVTRQKNKIIIQDASRRN', 1223, 'Q292S8;', 'KD01548', 'Drosophila pseudoobscura pseudoobscura (Fruit fly)', 'cos', '#Kinesin-like protein costa#Kinesin-like protein costal2', '-', '-', '4803492'),
(1549, 'O14980', 'Exportin-1', 'GO:0000776', 123386, '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 (Ran-GTP). 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. Several viruses; among them HIV-1; HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with; and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization. {ECO:0000269|PubMed:14612415; ECO:0000269|PubMed:15574332; ECO:0000269|PubMed:20921223; ECO:0000269|PubMed:9311922; ECO:0000269|PubMed:9323133; ECO:0000269|PubMed:9837918}.', 'MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD', 1071, 'O14980; A6NL14; A8K1K5; D6W5E2; Q63HP8; Q68CP3; Q99433;', 'KD01549', 'Homo sapiens (Human)', 'XPO1', '#Exportin-1#Exp1#Chromosome region maintenance 1 protein homolog', '-', 'ENSG00000103145', '-'),
(1550, 'Q58G59', 'Kinesin-like protein kif7', 'GO:0003777', 154837, 'Acts downstream of smo as an intracellular repressor of hedgehog signaling pathway; mainly through the suppression of gli1 activity. This negative regulatory effect is enhanced in conjunction with the suppressor of fused (sufu) protein. Positively regulates gli2a activity by promoting its dissociation from sufu. Involved in the regulation of microtubular dynamics. {ECO:0000269|PubMed:15647323; ECO:0000269|PubMed:24339784}.', 'MSPKGVGHSKVEESAVQVAVRVRPLLPKEILHSHESCITSDPEERRVTLGNDRHFHCDFVFEDGSTQEEVYTNCVQPLIEAFFHGFNATVSAYGQTGSGKTYTIGEASISAFRDDEQGIIPRAVAEIFKLLDENDLIDFSVRVSYMEVYKEVFRDLLEVETASKDIHIREDERGNVVLCGVKECEVEGLDEVLSLLESGKTARHTGATQMNPHSSRSHTIFTVLMEQRRGGSRAANGSVQILSSKFHFVDLAGSERILKTGNTGERLKESIQINSGLLVLGNVIGALGDPKRKGTHIPYRDSKITRILKDSLGGNAKTLMIACISPSSSDFDESLNTLNYAKRARNIQNRATVNCRGEPDRIEGLELQIKALRRALENRQRSETRIIARSDPEKRLRPFEVDVRKLQAESAHYRTCTDSAYRLLTELQGEGTLNAGQILRVKEWLCGVEEERSGLTSASGLDSGIESSSTEDSTALKRRQAVLNNQDLVKEDWRGEREDYTSQLQAQIQQLEQENTDFLVALEDAMEQYKQQSDKLQEQQDLIAELHSLLAQPGGAGFLHLKQRPHTAPINSLLQTPDRLTPPCDSDVGRSLARQLDVGASVDSSSYSEQTQWDGTHGNTHCESSRKLNRDEDGHMQTTRDKRKSINVTWTKKDIAIPQGPFGGTRTALPQTLGLCHPLGMQFNRRTSNSSIGESSVWESVRGFGGEFCSDRGLLQAQQKIRELSITIRMKEELIKELVKTGKDAQAMNRQYSRKISELEAEAEQARVELTEAQKQLQELEVQGGRDAVDRSKAQECRRKIAAAQSKVQVLKQKQRDTAQLASLSAQSERRVQELERNVQNMKQQQDLLQRRLREESQQKRRLETEMQKGKHRVKELEIKNEQQQKILRIKTEEIAAFQRQRRSGSNGSVVSLEEQQKIEEQKRWLDEEMEKVLDQRRGLEDLEGELTKREEILAKKEALLWERSGLESKKLRSSQALSQDLLTLSSRIESLERELTERNGLLRSGSAQDSQQIRQEISNLRQEKELLLKQRVELDDKLRQGNLLSPEEERTLFQLDEAIEALDAAIEYKNEAITQRQRQLRASGSMLTQWEMNLMAKLTYLSASETRALLCKYFDKVVSLREEERRLQMALAELELRVEEQQNLVGWLEAALERQQLEADRRLTQQQKEHERNIQLLLQQCREQMDEGLAGRLRQYEGLIHNLSKELNFCKIANQELNIKLREMCGPVNLTGEQCKGLNCDSLLLAGAQSRVAEDVKPIIDAERVQKSREEMREPVNAPLPATWRRSSLPTEDQYTMEELRQRAACELPNNRIVQPGMNSTHWSGSTSLPVTRPRREPRRSSLNTAPLYSSSAIIDVRRNPV', 1363, 'Q58G59;', 'KD01550', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'kif7', '#Kinesin-like protein kif7#Kinesin-like protein costal2', '-', '-', '544651'),
(1551, 'Q6NRI8', 'Centromere protein S', 'GO:0000777', 15179, 'Probable DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Probable component of a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). {ECO:0000250}.', 'MAEGQEEHFSRTQRLKAAVHYVVGSLCQEVADDKEIDFSKQAIAAISEITFRQCESFAKDLEIFARHAKRTTINMDDVKLLARRSRSLYAHISKCSDEIAANSLEQKEKKKKKSVSGGNVSRNSDMDTVVPESKD', 135, 'Q6NRI8;', 'KD01551', 'Xenopus laevis (African clawed frog)', 'apitd1', '#Centromere protein S#CENP-S#Apoptosis-inducing TAF9-like domain-containing protein 1 homolog#FANCM-interacting histone fold protein 1', '-', '-', '431958'),
(1552, 'Q9BTE1', 'Dynactin subunit 5', 'GO:0000777===SCL', 20127, '', 'MELGELLYNKSEYIETASGNKVSRQSVLCGSQNIVLNGKTIVMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQKFLPLTQV', 182, 'Q9BTE1; A8K9X8; H3BN51; H3BQA4;', 'KD01552', 'Homo sapiens (Human)', 'DCTN5', '#Dynactin subunit 5#Dynactin subunit p25', '-', 'ENSG00000166847', '-'),
(1553, 'Q6BPA9', 'Probable kinetochore protein NUF2', 'GO:0000777', 56914, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSRPSSIYRPGNSSLTSRRIHHVIPQDSFPLLDFKEISICLQSCDFIANEELVSRPTSQYIKTLLEQLLDSFMGLSADNINGMVRNVNKNDLSMTKTQDAQMEEEPENGGSQIEDDDDITSSVRLILLHRGAYEFFSICGVNDFTLMDIMRPEPQRIRRILSAVVNYARFREENSVECEKLVSISEGNLEQLKVVQNENSRLSNKINDLKYKIEANETDEGNKKATLKQITTYNSKLENELKKLKKNQEILTLEHSKYKDEKRRLIEKLEDHNYLIMESNKELDKLKSYLLSNPEILTKIIEDLKTNLSEYQTNLADLESKNKNMTISIESFQLVEQELKNLFRILEEVLNDLTKEETSLDKLNKYQEFKEQQNLTLNDLNRQIQQVTRQLNNTEEKIKRLRHQSSERSEASKQKLISLKDGYDTLVKERKVKEQELNKKKDFISELETKMNGERSNFQIELRNAELAVAKLNSHVKLYLTEMNKKVD', 488, 'Q6BPA9;', 'KD01553', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '2902630'),
(1554, 'Q32P85', 'Dynein light chain roadblock-type 2', 'GO:0005868', 10846, '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 (By similarity). {ECO:0000250}.', 'MAEVEETLKRIQSHKGVIGTMVVNAEGIPIRTTLDNSTTVQYAGLLHQLTMKAKSTVRDIDPQNDLTFLRIRSKKHEIMVAPDKEYLLIVIQNPCE', 96, 'Q32P85;', 'KD01554', 'Bos taurus (Bovine)', 'DYNLRB2', '#Dynein light chain roadblock-type 2#Dynein light chain 2B; cytoplasmic', '-', '-', '768062');

-- --------------------------------------------------------

--
-- Table structure for table `ptms`
--

CREATE TABLE IF NOT EXISTS `ptms` (
  `PTMsID` bigint(20) NOT NULL AUTO_INCREMENT,
  `PTMsProteinID` bigint(20) NOT NULL,
  `Position` int(11) NOT NULL,
  `PTMsPTMType` varchar(45) NOT NULL,
  `PTMsKinase` longtext NOT NULL,
  `PubMeds` longtext,
  PRIMARY KEY (`PTMsID`),
  KEY `PTMsProteinID` (`PTMsProteinID`)
) ENGINE=InnoDB  DEFAULT CHARSET=latin1 AUTO_INCREMENT=4028 ;

--
-- Dumping data for table `ptms`
--

INSERT INTO `ptms` (`PTMsID`, `PTMsProteinID`, `Position`, `PTMsPTMType`, `PTMsKinase`, `PubMeds`) VALUES
(1, 1, 34, 'Phosphoserine', 'unknown', '-'),
(2, 1, 119, 'Phosphoserine', 'unknown', '-'),
(3, 1, 154, 'Phosphoserine', 'unknown', '-'),
(4, 1, 324, 'Phosphoserine', 'unknown', '-'),
(5, 2, 1, 'N-acetylmethionine', 'unknown', '-'),
(6, 2, 92, 'N6-acetyllysine', 'unknown', '23806337'),
(7, 5, 103, 'Phosphoserine', 'unknown', '-'),
(8, 5, 210, 'Phosphothreonine', 'AURKA', '-'),
(9, 5, 214, 'Phosphothreonine', 'unknown', '-'),
(10, 5, 269, 'Phosphoserine', 'autocatalysis', '-'),
(11, 5, 335, 'Phosphoserine', 'autocatalysis', '-'),
(12, 5, 375, 'Phosphoserine', 'unknown', '-'),
(13, 5, 450, 'Phosphoserine', 'unknown', '-'),
(14, 5, 498, 'Phosphothreonine', 'unknown', '-'),
(15, 6, 2, 'N-acetylserine', 'unknown', '-'),
(16, 6, 90, 'Phosphoserine', 'unknown', '11340075'),
(17, 6, 97, 'Phosphoserine', 'unknown', '-'),
(18, 6, 101, 'Phosphoserine', 'unknown', '-'),
(19, 6, 104, 'Phosphoserine', 'unknown', '-'),
(20, 8, 1, 'N-acetylmethionine', 'unknown', '-'),
(21, 8, 508, 'Phosphoserine', 'unknown', '-'),
(22, 10, 295, 'N6-acetyllysine', 'autocatalysis', '-'),
(23, 12, 1, 'N-acetylmethionine', 'unknown', '-'),
(24, 12, 4, 'Phosphoserine', 'unknown', '-'),
(25, 12, 11, 'Phosphoserine', 'unknown', '-'),
(26, 12, 46, 'Phosphothreonine', 'unknown', '-'),
(27, 12, 55, 'Phosphothreonine', 'unknown', '-'),
(28, 12, 58, 'Phosphoserine', 'unknown', '-'),
(29, 12, 64, 'Phosphothreonine', 'unknown', '-'),
(30, 12, 69, 'Phosphoserine', 'unknown', '-'),
(31, 12, 86, 'Phosphoserine', 'unknown', '-'),
(32, 13, 194, 'Phosphoserine', 'unknown', '-'),
(33, 13, 383, 'Phosphoserine', 'unknown', '-'),
(34, 13, 391, 'Phosphoserine', 'unknown', '-'),
(35, 13, 394, 'Phosphothreonine', 'unknown', '-'),
(36, 13, 405, 'Phosphoserine', 'unknown', '-'),
(37, 13, 407, 'Phosphoserine', 'unknown', '-'),
(38, 13, 441, 'Phosphothreonine', 'unknown', '-'),
(39, 13, 443, 'Phosphoserine', 'unknown', '-'),
(40, 13, 446, 'Phosphoserine', 'unknown', '-'),
(41, 13, 459, 'Phosphoserine', 'unknown', '-'),
(42, 13, 486, 'Phosphoserine', 'unknown', '-'),
(43, 17, 125, 'Phosphothreonine', 'PLK1', '-'),
(44, 17, 147, 'Phosphoserine', 'unknown', '-'),
(45, 17, 204, 'Phosphoserine', 'PLK1', '-'),
(46, 22, 1, 'N-acetylmethionine', 'unknown', '-'),
(47, 23, 17, 'Phosphoserine', 'unknown', '18669648;20068231'),
(48, 23, 28, 'Phosphoserine', 'unknown', '11713274'),
(49, 23, 71, 'Phosphoserine', 'unknown', '20068231'),
(50, 24, 112, 'N6-acetyllysine', 'unknown', '18614053'),
(51, 24, 113, 'N6-acetyllysine', 'unknown', '18614053'),
(52, 28, 2, 'N#N#N-trimethylalanine', 'NTM1', '20668449'),
(53, 28, 7, 'Phosphoserine', 'unknown', '-'),
(54, 28, 23, 'N6-acetyllysine', 'unknown', '23806337'),
(55, 28, 67, 'N6-acetyllysine', 'unknown', '23806337'),
(56, 28, 145, 'Phosphotyrosine', 'unknown', '17947660'),
(57, 28, 149, 'N6-acetyllysine', 'unknown', '-'),
(58, 28, 171, 'N6-acetyllysine', 'unknown', '-'),
(59, 30, 690, 'Phosphoserine', 'unknown', '-'),
(60, 32, 77, 'Phosphoserine', 'unknown', '20068231'),
(61, 32, 263, 'Phosphoserine', 'unknown', '20068231'),
(62, 32, 549, 'Phosphoserine', 'unknown', '18669648;19369195;19690332'),
(63, 32, 618, 'Phosphoserine', 'unknown', '18669648'),
(64, 32, 621, 'Phosphothreonine', 'unknown', '18669648'),
(65, 32, 685, 'Phosphoserine', 'unknown', '20068231'),
(66, 32, 776, 'Phosphoserine', 'unknown', '18669648;20068231'),
(67, 32, 901, 'Phosphoserine', 'unknown', '18669648'),
(68, 32, 923, 'Phosphoserine', 'unknown', '18669648'),
(69, 32, 1385, 'Phosphoserine', 'unknown', '18669648'),
(70, 32, 1388, 'Phosphoserine', 'unknown', '18669648'),
(71, 32, 1399, 'Phosphoserine', 'unknown', '20068231'),
(72, 32, 1417, 'Phosphothreonine', 'unknown', '16964243;18669648'),
(73, 32, 1421, 'Phosphoserine', 'unknown', '16964243;18669648'),
(74, 32, 1427, 'Phosphotyrosine', 'unknown', '18669648'),
(75, 32, 1561, 'Phosphoserine', 'unknown', '18669648'),
(76, 32, 1578, 'Phosphoserine', 'unknown', '18669648'),
(77, 32, 1583, 'Phosphoserine', 'unknown', '18669648'),
(78, 32, 1592, 'Phosphoserine', 'unknown', '18669648'),
(79, 32, 1661, 'Phosphoserine', 'unknown', '18669648'),
(80, 32, 1667, 'Phosphothreonine', 'unknown', '18669648'),
(81, 32, 1675, 'Phosphothreonine', 'unknown', '16964243;18669648'),
(82, 32, 1679, 'Phosphoserine', 'unknown', '16964243'),
(83, 32, 1683, 'Phosphoserine', 'unknown', '18669648'),
(84, 32, 1812, 'Phosphoserine', 'unknown', '18669648'),
(85, 32, 1814, 'Phosphoserine', 'unknown', '18669648'),
(86, 33, 11, 'Phosphoserine', 'unknown', '19690332'),
(87, 34, 243, 'N6-acetyllysine', 'PCAF', '-'),
(88, 34, 428, 'Phosphoserine', 'unknown', '-'),
(89, 34, 535, 'Phosphoserine', 'unknown', '-'),
(90, 34, 659, 'Phosphoserine', 'unknown', '-'),
(91, 34, 665, 'Phosphoserine', 'PLK1', '-'),
(92, 34, 781, 'Phosphothreonine', 'PLK1', '-'),
(93, 34, 998, 'Phosphothreonine', 'PLK1', '-'),
(94, 34, 1033, 'Phosphoserine', 'unknown', '-'),
(95, 37, 108, 'Phosphothreonine', 'unknown', '-'),
(96, 39, 2, 'N-acetylserine', 'unknown', '22814378'),
(97, 39, 145, 'Phosphotyrosine', 'unknown', '-'),
(98, 42, 12, 'Phosphoserine', 'unknown', '-'),
(99, 44, 101, 'Phosphoserine', 'unknown', '18691976'),
(100, 46, 1274, 'Phosphoserine', 'unknown', '-'),
(101, 47, 16, 'Phosphoserine', 'unknown', '-'),
(102, 47, 22, 'Phosphoserine', 'unknown', '-'),
(103, 48, 47, 'Phosphoserine', 'unknown', '19779198'),
(104, 48, 378, 'Phosphothreonine', 'unknown', '17287358;17330950;18407956;19779198'),
(105, 52, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(106, 53, 88, 'Phosphoserine', 'unknown', '18691976'),
(107, 58, 215, 'Phosphoserine', 'unknown', '-'),
(108, 58, 219, 'Phosphothreonine', 'CDK1;MAPK1', '-'),
(109, 58, 242, 'Phosphoserine', 'CDK1', '-'),
(110, 58, 245, 'Phosphothreonine', 'CDK1;MAPK1', '-'),
(111, 61, 13, 'Phosphoserine', 'unknown', '-'),
(112, 61, 23, 'Phosphothreonine', 'unknown', '-'),
(113, 61, 63, 'Phosphoserine', 'unknown', '19690332'),
(114, 61, 101, 'Phosphoserine', 'unknown', '-'),
(115, 61, 140, 'Phosphothreonine', 'unknown', '-'),
(116, 61, 168, 'Phosphoserine', 'unknown', '-'),
(117, 61, 196, 'Phosphoserine', 'unknown', '-'),
(118, 61, 258, 'Phosphoserine', 'unknown', '19690332'),
(119, 61, 261, 'Phosphoserine', 'unknown', '19690332'),
(120, 61, 295, 'Phosphoserine', 'unknown', '-'),
(121, 61, 361, 'Phosphoserine', 'unknown', '19690332;23071339'),
(122, 61, 364, 'Phosphoserine', 'unknown', '19690332;23071339'),
(123, 61, 389, 'Phosphoserine', 'unknown', '-'),
(124, 61, 391, 'Phosphoserine', 'unknown', '-'),
(125, 61, 393, 'Phosphoserine', 'unknown', '-'),
(126, 61, 397, 'Phosphoserine', 'unknown', '-'),
(127, 61, 398, 'Phosphothreonine', 'unknown', '-'),
(128, 61, 445, 'Phosphoserine', 'unknown', '24275569'),
(129, 63, 530, 'Phosphothreonine', 'unknown', '18669648'),
(130, 63, 546, 'Phosphoserine', 'unknown', '18669648'),
(131, 64, 449, 'Phosphotyrosine', 'unknown', '-'),
(132, 64, 521, 'Phosphoserine', 'AMPK', '20074060'),
(133, 64, 524, 'Phosphoserine', 'AMPK', '20074060'),
(134, 65, 88, 'Phosphoserine', 'unknown', '-'),
(135, 66, 37, 'N6-acetyllysine', 'unknown', '-'),
(136, 66, 38, 'N6-acetyllysine', 'unknown', '-'),
(137, 66, 226, 'Phosphoserine', 'unknown', '21406692'),
(138, 66, 232, 'Phosphoserine', 'unknown', '21406692'),
(139, 69, 22, 'Phosphoserine', 'unknown', '-'),
(140, 69, 25, 'Phosphoserine', 'unknown', '-'),
(141, 71, 997, 'Phosphoserine', 'unknown', '18407956'),
(142, 71, 1018, 'Phosphoserine', 'unknown', '18407956'),
(143, 71, 1047, 'Phosphothreonine', 'unknown', '19779198'),
(144, 71, 1063, 'Phosphoserine', 'unknown', '17287358'),
(145, 71, 1167, 'Phosphoserine', 'unknown', '18407956;19779198'),
(146, 72, 116, 'Phosphothreonine', 'unknown', '18669648;20068231'),
(147, 72, 122, 'Phosphoserine', 'unknown', '20068231'),
(148, 72, 138, 'Phosphoserine', 'unknown', '20068231'),
(149, 72, 226, 'Phosphothreonine', 'unknown', '20068231'),
(150, 72, 280, 'Phosphoserine', 'unknown', '18669648'),
(151, 80, 32, 'Phosphoserine', 'unknown', '18669648'),
(152, 80, 60, 'Phosphoserine', 'unknown', '18669648'),
(153, 80, 539, 'Phosphothreonine', 'unknown', '20068231'),
(154, 80, 956, 'Phosphoserine', 'unknown', '20068231'),
(155, 80, 1076, 'Phosphoserine', 'unknown', '18669648;18691976;19690332;20068231'),
(156, 80, 1773, 'Phosphoserine', 'unknown', '18669648'),
(157, 80, 1831, 'Phosphoserine', 'unknown', '20068231'),
(158, 80, 1845, 'Phosphoserine', 'unknown', '18669648'),
(159, 81, 2, 'N-acetylalanine', 'unknown', '-'),
(160, 81, 777, 'N6-acetyllysine', 'unknown', '-'),
(161, 82, 198, 'Phosphothreonine', 'PKA', '-'),
(162, 83, 579, 'Phosphoserine', 'unknown', '-'),
(163, 83, 582, 'Phosphothreonine', 'unknown', '-'),
(164, 83, 1167, 'Phosphoserine', 'unknown', '21406692'),
(165, 83, 1237, 'Phosphothreonine', 'unknown', '18669648;19690332;21406692'),
(166, 83, 1241, 'Phosphoserine', 'unknown', '19690332'),
(167, 86, 2, 'N-acetylserine', 'unknown', '-'),
(168, 86, 30, 'Phosphotyrosine', 'unknown', '-'),
(169, 86, 334, 'Phosphoserine', 'unknown', '-'),
(170, 86, 373, 'N6-acetyllysine', 'unknown', '-'),
(171, 86, 424, 'Phosphoserine', 'unknown', '-'),
(172, 86, 426, 'Phosphothreonine', 'unknown', '-'),
(173, 87, 349, 'Phosphoserine', 'unknown', '18407956'),
(174, 88, 2, 'N-acetylserine', 'unknown', '22814378'),
(175, 88, 90, 'Phosphoserine', 'unknown', '-'),
(176, 88, 97, 'Phosphoserine', 'unknown', '18669648'),
(177, 88, 101, 'Phosphoserine', 'unknown', '21406692'),
(178, 88, 104, 'Phosphoserine', 'unknown', '19690332'),
(179, 89, 226, 'Phosphoserine', 'unknown', '-'),
(180, 91, 2, 'N-acetylalanine', 'unknown', '-'),
(181, 91, 931, 'Phosphoserine', 'unknown', '-'),
(182, 93, 2, 'N-acetylserine', 'unknown', '22223895;22814378'),
(183, 93, 460, 'Phosphoserine', 'unknown', '16964243;18669648;21406692'),
(184, 93, 590, 'Phosphoserine', 'unknown', '18220336;18669648;19690332;20068231;21406692;24275569'),
(185, 93, 611, 'Phosphoserine', 'unknown', '-'),
(186, 93, 612, 'Phosphothreonine', 'unknown', '20068231'),
(187, 94, 639, 'Phosphoserine', 'unknown', '18669648;20068231'),
(188, 94, 703, 'Phosphoserine', 'unknown', '19690332'),
(189, 94, 707, 'Phosphoserine', 'unknown', '19690332'),
(190, 95, 38, 'Phosphoserine', 'unknown', '18407956'),
(191, 96, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(192, 97, 2, 'N-acetylalanine', 'unknown', '-'),
(193, 97, 414, 'Phosphothreonine', 'unknown', '16641100'),
(194, 99, 244, 'Phosphothreonine', 'unknown', '18669648'),
(195, 102, 2, 'N-acetylalanine', 'unknown', '-'),
(196, 102, 367, 'N6-acetyllysine', 'unknown', '-'),
(197, 107, 1, 'N-acetylmethionine', 'unknown', '-'),
(198, 107, 16, 'Phosphoserine', 'unknown', '-'),
(199, 107, 61, 'N6-acetyllysine', 'unknown', '-'),
(200, 107, 214, 'Phosphoserine', 'unknown', '-'),
(201, 107, 428, 'Phosphoserine', 'unknown', '-'),
(202, 110, 2, 'N-acetylalanine', 'unknown', '19608861'),
(203, 110, 5, 'N6-acetyllysine', 'unknown', '16319397;16627869'),
(204, 110, 8, 'N6-acetyllysine', 'unknown', '16319397;16627869;19608861'),
(205, 110, 12, 'N6-acetyllysine', 'unknown', '16627869;19608861'),
(206, 110, 14, 'N6-acetyllysine', 'unknown', '19608861'),
(207, 113, 333, 'Phosphoserine', 'unknown', '-'),
(208, 113, 422, 'Phosphoserine', 'unknown', '-'),
(209, 113, 436, 'Phosphothreonine', 'unknown', '-'),
(210, 113, 442, 'Phosphoserine', 'unknown', '-'),
(211, 113, 460, 'Phosphothreonine', 'unknown', '-'),
(212, 113, 1334, 'Phosphoserine', 'unknown', '-'),
(213, 113, 1360, 'Phosphoserine', 'unknown', '-'),
(214, 113, 1391, 'Phosphoserine', 'unknown', '-'),
(215, 114, 358, 'Phosphoserine', 'unknown', '-'),
(216, 114, 360, 'Phosphoserine', 'unknown', '-'),
(217, 114, 648, 'N6-acetyllysine', 'unknown', '-'),
(218, 114, 713, 'N6-acetyllysine', 'unknown', '-'),
(219, 114, 957, 'Phosphoserine', 'unknown', '-'),
(220, 114, 966, 'Phosphoserine', 'unknown', '-'),
(221, 114, 970, 'Phosphoserine', 'unknown', '-'),
(222, 114, 1037, 'N6-acetyllysine', 'unknown', '-'),
(223, 118, 40, 'Phosphoserine', 'unknown', '-'),
(224, 118, 50, 'Phosphoserine', 'unknown', '-'),
(225, 118, 280, 'Phosphothreonine', 'unknown', '-'),
(226, 118, 281, 'Phosphothreonine', 'unknown', '-'),
(227, 118, 335, 'Phosphoserine', 'PKA;PAK', '-'),
(228, 122, 1, 'N-acetylmethionine', 'unknown', '-'),
(229, 123, 14, 'Phosphoserine', 'unknown', '-'),
(230, 123, 755, 'Phosphoserine', 'unknown', '-'),
(231, 123, 773, 'Phosphoserine', 'unknown', '-'),
(232, 123, 821, 'Phosphoserine', 'unknown', '-'),
(233, 123, 1021, 'Phosphoserine', 'unknown', '17242355'),
(234, 123, 1057, 'Phosphothreonine', 'unknown', '-'),
(235, 123, 1092, 'Phosphoserine', 'unknown', '-'),
(236, 123, 1172, 'Phosphoserine', 'unknown', '-'),
(237, 124, 467, 'Phosphoserine', 'unknown', '-'),
(238, 124, 499, 'Phosphothreonine', 'unknown', '-'),
(239, 128, 1, 'N-acetylmethionine', 'unknown', '20068231;21406692;22814378'),
(240, 128, 4, 'Phosphoserine', 'unknown', '17081983;18691976;20068231;21406692'),
(241, 128, 282, 'Phosphothreonine', 'unknown', '20068231'),
(242, 128, 1106, 'Phosphoserine', 'CK1', '17081983;18669648;19043076;20068231;21406692'),
(243, 128, 1205, 'Phosphothreonine', 'unknown', '20068231'),
(244, 128, 1213, 'Phosphoserine', 'unknown', '16964243;17081983;18669648;18691976;20068231;21406692'),
(245, 128, 1247, 'Phosphoserine', 'unknown', '17081983;17924679;18691976;19690332;20068231;21406692'),
(246, 128, 1295, 'Phosphoserine', 'unknown', '21406692'),
(247, 128, 1297, 'Phosphoserine', 'unknown', '21406692'),
(248, 128, 1299, 'Phosphoserine', 'unknown', '21406692'),
(249, 128, 1302, 'Phosphoserine', 'unknown', '21406692'),
(250, 128, 1332, 'Phosphoserine', 'unknown', '17081983;18669648;18691976;20068231;21406692'),
(251, 128, 1337, 'Phosphoserine', 'unknown', '17081983;18669648;18691976;20068231;21406692'),
(252, 128, 1343, 'Phosphothreonine', 'PLK3', '17081983;18062778;18669648;20068231;21406692'),
(253, 128, 1351, 'Phosphoserine', 'unknown', '17081983;18669648;20068231;21406692'),
(254, 128, 1354, 'Phosphoserine', 'unknown', '17081983;20068231;21406692'),
(255, 128, 1374, 'Phosphoserine', 'unknown', '16964243;17081983;19690332;20068231;21406692'),
(256, 128, 1377, 'Phosphoserine', 'unknown', '16964243;17081983;18691976;20068231;21406692'),
(257, 128, 1387, 'Phosphoserine', 'unknown', '19690332'),
(258, 128, 1392, 'Phosphoserine', 'unknown', '18669648'),
(259, 128, 1393, 'Phosphoserine', 'unknown', '18669648;19690332'),
(260, 128, 1422, 'N6-acetyllysine', 'unknown', '-'),
(261, 128, 1442, 'N6-acetyllysine', 'unknown', '-'),
(262, 128, 1449, 'Phosphoserine', 'unknown', '18669648'),
(263, 128, 1469, 'Phosphoserine', 'CK2', '10942766;18669648;21406692'),
(264, 128, 1470, 'Phosphothreonine', 'unknown', '18669648;21406692'),
(265, 128, 1471, 'Phosphoserine', 'unknown', '18669648;20068231;21406692'),
(266, 128, 1474, 'Phosphoserine', 'unknown', '18669648;20068231;21406692'),
(267, 128, 1476, 'Phosphoserine', 'unknown', '21406692'),
(268, 128, 1495, 'Phosphoserine', 'unknown', '20068231'),
(269, 128, 1504, 'Phosphoserine', 'unknown', '18220336;19690332;20068231'),
(270, 128, 1525, 'Phosphoserine', 'unknown', '16964243;17081983;18669648;19690332;20068231;21406692'),
(271, 129, 219, 'Phosphoserine', 'unknown', '18257517'),
(272, 129, 547, 'Phosphoserine', 'unknown', '18257517'),
(273, 129, 553, 'Phosphoserine', 'unknown', '18257517'),
(274, 131, 285, 'Phosphoserine', 'unknown', '18257517'),
(275, 131, 286, 'Phosphoserine', 'unknown', '18257517'),
(276, 140, 689, 'Phosphoserine', 'unknown', '15345747'),
(277, 141, 75, 'Phosphoserine', 'unknown', '-'),
(278, 141, 101, 'N6-acetyllysine', 'unknown', '23806337'),
(279, 141, 114, 'Phosphoserine', 'unknown', '-'),
(280, 141, 120, 'Phosphoserine', 'unknown', '-'),
(281, 141, 156, 'Phosphoserine', 'unknown', '-'),
(282, 143, 2, 'N-acetylserine', 'unknown', '-'),
(283, 143, 460, 'Phosphoserine', 'unknown', '-'),
(284, 143, 590, 'Phosphoserine', 'unknown', '-'),
(285, 143, 611, 'Phosphoserine', 'unknown', '-'),
(286, 143, 612, 'Phosphothreonine', 'unknown', '-'),
(287, 144, 2, 'N#N#N-trimethylglycine', 'unknown', '23978223'),
(288, 144, 2, 'N#N-dimethylglycine', 'unknown', '23978223'),
(289, 144, 2, 'N-methylglycine', 'unknown', '23978223'),
(290, 144, 156, 'Phosphoserine', 'unknown', '18220336;20068231'),
(291, 144, 165, 'Phosphoserine', 'unknown', '20068231'),
(292, 144, 398, 'Phosphothreonine', 'unknown', '20068231'),
(293, 146, 312, 'Phosphoserine', 'unknown', '17372656'),
(294, 148, 600, 'Phosphoserine', 'unknown', '-'),
(295, 148, 646, 'Phosphoserine', 'unknown', '-'),
(296, 148, 649, 'Phosphoserine', 'unknown', '-'),
(297, 148, 656, 'Phosphothreonine', 'unknown', '-'),
(298, 148, 684, 'Phosphoserine', 'unknown', '-'),
(299, 148, 688, 'Phosphoserine', 'unknown', '-'),
(300, 148, 695, 'Phosphoserine', 'unknown', '-'),
(301, 148, 708, 'Phosphothreonine', 'unknown', '-'),
(302, 148, 711, 'Phosphoserine', 'unknown', '-'),
(303, 148, 794, 'Phosphoserine', 'unknown', '-'),
(304, 148, 1088, 'Phosphoserine', 'unknown', '-'),
(305, 148, 1096, 'Phosphothreonine', 'unknown', '-'),
(306, 148, 1193, 'Phosphoserine', 'unknown', '-'),
(307, 148, 1220, 'Phosphoserine', 'unknown', '16452087'),
(308, 149, 330, 'Phosphoserine', 'CDK2 (in cyclin E-CDK2 complex); by CDK5 (in cyclin p35-CDK5)', '-'),
(309, 149, 334, 'Phosphoserine', 'unknown', '-'),
(310, 152, 2, 'N-acetylalanine', 'unknown', '-'),
(311, 152, 6, 'Phosphotyrosine', 'unknown', '-'),
(312, 152, 83, 'Phosphoserine', 'unknown', '-'),
(313, 152, 86, 'Phosphotyrosine', 'unknown', '-'),
(314, 153, 2, 'N-acetylserine', 'unknown', '-'),
(315, 153, 7, 'Phosphoserine', 'unknown', '-'),
(316, 153, 14, 'Phosphoserine', 'unknown', '-'),
(317, 153, 21, 'Phosphoserine', 'unknown', '-'),
(318, 153, 527, 'Phosphoserine', 'PLK1', '-'),
(319, 153, 531, 'Phosphoserine', 'unknown', '-'),
(320, 153, 667, 'Phosphoserine', 'unknown', '-'),
(321, 153, 823, 'Phosphoserine', 'unknown', '-'),
(322, 153, 855, 'Phosphothreonine', 'unknown', '-'),
(323, 153, 865, 'Phosphoserine', 'unknown', '-'),
(324, 154, 143, 'Phosphoserine', 'unknown', '17330950'),
(325, 155, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(326, 155, 513, 'Phosphoserine', 'unknown', '20068231'),
(327, 155, 515, 'Phosphoserine', 'unknown', '20068231'),
(328, 159, 268, 'Phosphoserine', 'unknown', '19779198'),
(329, 164, 605, 'Phosphoserine', 'unknown', '18257517'),
(330, 164, 611, 'Phosphoserine', 'unknown', '18257517'),
(331, 164, 613, 'Phosphoserine', 'unknown', '18257517'),
(332, 166, 2, 'N-acetylserine', 'unknown', '-'),
(333, 166, 29, 'Phosphotyrosine', 'unknown', '-'),
(334, 166, 333, 'Phosphoserine', 'unknown', '-'),
(335, 166, 372, 'N6-acetyllysine', 'unknown', '-'),
(336, 166, 423, 'Phosphoserine', 'unknown', '-'),
(337, 166, 425, 'Phosphothreonine', 'unknown', '-'),
(338, 167, 1157, 'Phosphoserine', 'unknown', '17081983;18669648;18691976;19690332;20068231;21406692'),
(339, 168, 391, 'Phosphoserine', 'unknown', '-'),
(340, 168, 446, 'N6-acetyllysine', 'unknown', '-'),
(341, 168, 448, 'Phosphothreonine', 'unknown', '16641100'),
(342, 168, 450, 'Phosphoserine', 'unknown', '16641100'),
(343, 168, 454, 'Phosphotyrosine', 'unknown', '16641100'),
(344, 168, 693, 'N6-acetyllysine', 'unknown', '-'),
(345, 169, 2, 'N-acetylvaline', 'unknown', '-'),
(346, 170, 2, 'N#N-dimethylproline', 'NTM1', '20668449'),
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(677, 281, 839, 'Phosphoserine', 'unknown', '17081983;18669648;20068231;21406692'),
(678, 281, 888, 'Phosphoserine', 'unknown', '17081983;18318008;18669648;18691976;20068231;21406692;24275569'),
(679, 281, 897, 'Phosphoserine', 'unknown', '24275569'),
(680, 281, 934, 'Phosphoserine', 'unknown', '18669648;20068231'),
(681, 281, 1000, 'Phosphothreonine', 'unknown', '18669648'),
(682, 281, 1023, 'Phosphoserine', 'unknown', '18669648'),
(683, 281, 1028, 'Phosphoserine', 'unknown', '16964243;18669648'),
(684, 281, 1043, 'Phosphoserine', 'unknown', '18669648'),
(685, 281, 1060, 'Phosphoserine', 'unknown', '16964243;18669648'),
(686, 281, 1070, 'Phosphothreonine', 'unknown', '18669648'),
(687, 282, 426, 'Phosphoserine', 'unknown', '-'),
(688, 282, 497, 'Phosphoserine', 'NEK2', '-'),
(689, 284, 14, 'Phosphoserine', 'NEK2', '17621308'),
(690, 284, 256, 'Phosphoserine', 'unknown', '20068231;21406692'),
(691, 284, 436, 'Phosphoserine', 'unknown', '18220336'),
(692, 284, 507, 'Phosphoserine', 'NEK2', '17621308;18669648;20068231'),
(693, 286, 384, 'N6-acetyllysine', 'autocatalysis', '-'),
(694, 289, 86, 'Phosphothreonine', 'unknown', '-'),
(695, 289, 333, 'Phosphoserine', 'unknown', '-'),
(696, 289, 345, 'Phosphoserine', 'unknown', '-'),
(697, 289, 346, 'Phosphoserine', 'unknown', '-'),
(698, 289, 357, 'Phosphoserine', 'unknown', '-'),
(699, 291, 2, 'N-acetylserine', 'unknown', '-'),
(700, 291, 138, 'Phosphoserine', 'unknown', '-'),
(701, 291, 145, 'Phosphoserine', 'unknown', '-'),
(702, 291, 155, 'Phosphoserine', 'unknown', '-'),
(703, 291, 199, 'Phosphoserine', 'unknown', '-'),
(704, 291, 358, 'Phosphothreonine', 'unknown', '-'),
(705, 292, 2, 'N-acetylalanine', 'unknown', '-'),
(706, 292, 6, 'N6-acetyllysine', 'unknown', '-'),
(707, 292, 69, 'N6-acetyllysine', 'unknown', '19608861'),
(708, 292, 74, 'N6-acetyllysine', 'unknown', '19608861'),
(709, 292, 118, 'Phosphoserine', 'unknown', '18669648'),
(710, 292, 120, 'Phosphothreonine', 'unknown', '18669648'),
(711, 293, 43, 'Phosphothreonine', 'CDK1', '-'),
(712, 294, 1, 'N-acetylmethionine', 'unknown', '-'),
(713, 294, 513, 'Phosphoserine', 'unknown', '-'),
(714, 295, 79, 'Phosphoserine', 'unknown', '21406692'),
(715, 295, 119, 'Phosphoserine', 'unknown', '18669648;18691976;20068231;21406692'),
(716, 295, 175, 'Phosphoserine', 'unknown', '20068231'),
(717, 295, 263, 'Phosphoserine', 'unknown', '24275569'),
(718, 297, 43, 'Phosphothreonine', 'CDK1', '-'),
(719, 298, 186, 'Phosphothreonine', 'CDK1', '-'),
(720, 301, 105, 'N6-acetyllysine', 'unknown', '18614053;19608861;19907496'),
(721, 301, 106, 'N6-acetyllysine', 'unknown', '18614053;19608861;19907496'),
(722, 301, 140, 'N6-acetyllysine', 'unknown', '19608861'),
(723, 301, 783, 'Phosphothreonine', 'unknown', '20068231'),
(724, 301, 787, 'Phosphoserine', 'unknown', '17525332;20068231'),
(725, 301, 1013, 'Phosphoserine', 'unknown', '-'),
(726, 301, 1065, 'Phosphoserine', 'unknown', '17525332;18669648;24275569'),
(727, 301, 1067, 'Phosphoserine', 'unknown', '17525332;18669648;20068231;21406692;24275569'),
(728, 301, 1083, 'Phosphoserine', 'unknown', '20068231;21406692'),
(729, 301, 1190, 'N6-acetyllysine', 'unknown', '19608861'),
(730, 302, 687, 'Phosphoserine', 'unknown', '18669648;20068231'),
(731, 305, 17, 'Phosphoserine', 'unknown', '-'),
(732, 305, 71, 'Phosphoserine', 'unknown', '-'),
(733, 306, 309, 'Leucine methyl ester', 'unknown', '-'),
(734, 307, 322, 'Leucine methyl ester', 'unknown', '-'),
(735, 309, 550, 'Phosphothreonine', 'unknown', '18257517'),
(736, 315, 3, 'Asymmetric dimethylarginine', 'PRMT6; alternate', '17898714;18077460;18079182'),
(737, 315, 3, 'Citrulline', 'unknown', '16567635'),
(738, 315, 4, 'Phosphothreonine', 'GSG2', '15681610;16185088'),
(739, 315, 5, 'Allysine', 'unknown', '-'),
(740, 315, 5, 'N6#N6#N6-trimethyllysine', 'unknown', '16185088;16267050;16457588;17194708'),
(741, 315, 5, 'N6#N6-dimethyllysine', 'unknown', '16185088;16267050;16457588;17194708'),
(742, 315, 5, 'N6-acetyllysine', 'unknown', '17194708'),
(743, 315, 5, 'N6-crotonyllysine', 'unknown', '21925322'),
(744, 315, 5, 'N6-methyllysine', 'unknown', '16185088;16267050;16457588;17194708'),
(745, 315, 7, 'Phosphothreonine', 'PKC', '20228790'),
(746, 315, 9, 'Citrulline', 'unknown', '15345777;16567635'),
(747, 315, 9, 'Symmetric dimethylarginine', 'PRMT5; alternate', '-'),
(748, 315, 10, 'N6#N6#N6-trimethyllysine', 'unknown', '11242053;16185088;16267050;16457588;17194708;7309716'),
(749, 315, 10, 'N6#N6-dimethyllysine', 'unknown', '11242053;16185088;16267050;16457588;17194708;7309716'),
(750, 315, 10, 'N6-acetyllysine', 'unknown', '16185088;16267050;16457588;16497732;17194708'),
(751, 315, 10, 'N6-crotonyllysine', 'unknown', '21925322'),
(752, 315, 10, 'N6-methyllysine', 'unknown', '11242053;16185088;16267050;16457588;17194708;7309716'),
(753, 315, 11, 'Phosphoserine', 'AURKB; AURKC; RPS6KA3; RPS6KA4;RPS6KA5', '10464286;11856369;12560483;15681610;15851689;16185088'),
(754, 315, 12, 'Phosphothreonine', 'PKC', '12560483;18066052'),
(755, 315, 15, 'N6-acetyllysine', 'unknown', '16185088;16267050;16497732;17194708;7309716'),
(756, 315, 18, 'Asymmetric dimethylarginine', 'CARM1; alternate', '15345777;15471871;16497732'),
(757, 315, 18, 'Citrulline', 'unknown', '15345777;16497732;16567635'),
(758, 315, 19, 'N6-acetyllysine', 'unknown', '16267050;17194708'),
(759, 315, 19, 'N6-crotonyllysine', 'unknown', '21925322'),
(760, 315, 19, 'N6-methyllysine', 'unknown', '16267050;17194708'),
(761, 315, 24, 'N6-acetyllysine', 'unknown', '16267050;17194708;7309716'),
(762, 315, 24, 'N6-crotonyllysine', 'unknown', '21925322'),
(763, 315, 24, 'N6-methyllysine', 'unknown', '17194708'),
(764, 315, 27, 'Citrulline', 'unknown', '16567635'),
(765, 315, 28, 'N6#N6#N6-trimethyllysine', 'unknown', '16185088;16267050;17194708;7309716'),
(766, 315, 28, 'N6#N6-dimethyllysine', 'unknown', '16185088;16267050;17194708;7309716'),
(767, 315, 28, 'N6-acetyllysine', 'unknown', '16267050;17194708;19608861'),
(768, 315, 28, 'N6-crotonyllysine', 'unknown', '21925322'),
(769, 315, 28, 'N6-methyllysine', 'unknown', '16185088;16267050;17194708;7309716'),
(770, 315, 29, 'Phosphoserine', 'AURKB; AURKC;RPS6KA5', '10464286;11856369;15681610;15684425;15851689;16185088'),
(771, 315, 32, 'Phosphoserine', 'unknown', '15851689;16185088'),
(772, 315, 37, 'N6#N6#N6-trimethyllysine', 'unknown', '16185088;16267050;17194708;7309716'),
(773, 315, 37, 'N6#N6-dimethyllysine', 'unknown', '16185088;16267050;17194708;7309716'),
(774, 315, 37, 'N6-acetyllysine', 'unknown', '17189264;17194708;19608861'),
(775, 315, 37, 'N6-methyllysine', 'unknown', '16185088;16267050;17194708;7309716'),
(776, 315, 38, 'N6-methyllysine', 'unknown', '-'),
(777, 315, 42, 'Phosphotyrosine', 'unknown', '19783980'),
(778, 315, 57, 'N6#N6#N6-trimethyllysine', 'unknown', '17194708;22387026'),
(779, 315, 57, 'N6-acetyllysine', 'unknown', '17194708'),
(780, 315, 57, 'N6-crotonyllysine', 'unknown', '21925322'),
(781, 315, 57, 'N6-methyllysine', 'EHMT2; alternate', '17194708;22387026'),
(782, 315, 58, 'Phosphoserine', 'unknown', '20850016'),
(783, 315, 65, 'N6-methyllysine', 'unknown', '16267050;17194708'),
(784, 315, 80, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(785, 315, 80, 'N6#N6-dimethyllysine', 'unknown', '15525939;16267050;17194708'),
(786, 315, 80, 'N6-acetyllysine', 'unknown', '17194708'),
(787, 315, 80, 'N6-methyllysine', 'unknown', '15525939;16267050;17194708'),
(788, 315, 81, 'Phosphothreonine', 'unknown', '20850016'),
(789, 315, 87, 'Phosphoserine', 'unknown', '24275569'),
(790, 315, 108, 'Phosphothreonine', 'unknown', '-'),
(791, 315, 116, 'N6-acetyllysine', 'unknown', '19520870'),
(792, 315, 123, 'N6-acetyllysine', 'unknown', '19520870;23415232'),
(793, 315, 123, 'N6-methyllysine', 'unknown', '16267050;17194708'),
(794, 317, 8, 'Phosphoserine', 'unknown', '21406692'),
(795, 317, 316, 'Phosphoserine', 'unknown', '24275569'),
(796, 317, 370, 'Phosphoserine', 'unknown', '18669648;19690332;21406692'),
(797, 317, 455, 'Phosphoserine', 'unknown', '21406692'),
(798, 317, 525, 'Phosphoserine', 'unknown', '18669648'),
(799, 317, 529, 'Phosphoserine', 'unknown', '18669648'),
(800, 317, 596, 'Phosphoserine', 'unknown', '18669648;19690332;21406692'),
(801, 317, 1029, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(802, 319, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(803, 319, 14, 'Phosphoserine', 'unknown', '18669648'),
(804, 320, 40, 'Phosphoserine', 'unknown', '-'),
(805, 320, 50, 'Phosphoserine', 'unknown', '-'),
(806, 320, 278, 'Phosphothreonine', 'unknown', '-'),
(807, 320, 279, 'Phosphothreonine', 'unknown', '-'),
(808, 320, 333, 'Phosphoserine', 'PKA;PAK', '-'),
(809, 322, 268, 'Phosphoserine', 'unknown', '17287358'),
(810, 322, 489, 'Phosphoserine', 'unknown', '18407956;19779198'),
(811, 323, 1859, 'Phosphothreonine', 'unknown', '22768111'),
(812, 323, 1962, 'Phosphoserine', 'unknown', '22768111'),
(813, 324, 104, 'N6-acetyllysine', 'unknown', '-'),
(814, 324, 249, 'Phosphoserine', 'unknown', '-'),
(815, 324, 268, 'Phosphoserine', 'unknown', '-'),
(816, 324, 922, 'Phosphoserine', 'unknown', '-'),
(817, 324, 934, 'Phosphothreonine', 'unknown', '-'),
(818, 324, 976, 'Phosphoserine', 'unknown', '-'),
(819, 327, 215, 'Phosphoserine', 'unknown', '-'),
(820, 327, 219, 'Phosphothreonine', 'CDK1;MAPK1', '-'),
(821, 327, 242, 'Phosphoserine', 'CDK1', '-'),
(822, 327, 245, 'Phosphothreonine', 'CDK1;MAPK1', '-'),
(823, 334, 235, 'Phosphoserine', 'unknown', '18669648'),
(824, 334, 242, 'Phosphoserine', 'unknown', '20068231'),
(825, 334, 270, 'Phosphothreonine', 'unknown', '20068231'),
(826, 334, 344, 'Phosphoserine', 'unknown', '17081983;18669648;19690332;20068231;21406692'),
(827, 336, 53, 'N6-acetyllysine', 'unknown', '-'),
(828, 340, 64, 'Phosphotyrosine', 'SRC', '-'),
(829, 340, 188, 'Cysteine methyl ester', 'unknown', '-'),
(830, 342, 1, 'N-acetylmethionine', 'unknown', '-'),
(831, 342, 2, 'N-acetylserine', 'unknown', '-'),
(832, 343, 2, 'N-acetylserine', 'unknown', '-'),
(833, 343, 145, 'Phosphotyrosine', 'unknown', '17947660'),
(834, 344, 1, 'N-acetylmethionine', 'unknown', '-'),
(835, 344, 4, 'Phosphoserine', 'unknown', '-'),
(836, 344, 11, 'Phosphoserine', 'unknown', '-'),
(837, 344, 46, 'Phosphothreonine', 'unknown', '-'),
(838, 344, 55, 'Phosphothreonine', 'unknown', '-'),
(839, 344, 58, 'Phosphoserine', 'unknown', '-'),
(840, 344, 65, 'Phosphothreonine', 'unknown', '-'),
(841, 344, 70, 'Phosphoserine', 'unknown', '-'),
(842, 344, 87, 'Phosphoserine', 'unknown', '-'),
(843, 346, 412, 'Phosphoserine', 'unknown', '-'),
(844, 346, 427, 'Phosphoserine', 'unknown', '-'),
(845, 346, 452, 'Phosphoserine', 'unknown', '-'),
(846, 346, 543, 'Phosphoserine', 'unknown', '-'),
(847, 346, 562, 'Phosphoserine', 'unknown', '-'),
(848, 346, 581, 'Phosphoserine', 'unknown', '-'),
(849, 347, 78, 'Phosphothreonine', 'unknown', '-'),
(850, 352, 1, 'N-acetylmethionine', 'unknown', '19369195;19608861;22814378'),
(851, 352, 4, 'Phosphotyrosine', 'PKR', '20395957'),
(852, 352, 6, 'N6-acetyllysine', 'unknown', '19608861'),
(853, 352, 9, 'N6-acetyllysine', 'unknown', '-'),
(854, 352, 14, 'Phosphothreonine', 'PKMYT1', '18669648;19690332;7569953'),
(855, 352, 15, 'Phosphotyrosine', 'PKMYT1; WEE1; WEE2;PKC/PRKCD', '18669648;19690332;19917613;7569953'),
(856, 352, 19, 'Phosphotyrosine', 'unknown', '18691976;19369195'),
(857, 352, 39, 'Phosphoserine', 'unknown', '18691976;19369195'),
(858, 352, 77, 'Phosphotyrosine', 'unknown', '18691976'),
(859, 352, 161, 'Phosphothreonine', 'CAK', '19690332;20068231;20360007;21406692'),
(860, 352, 178, 'Phosphoserine', 'unknown', '19369195'),
(861, 352, 222, 'Phosphothreonine', 'unknown', '18691976;19369195'),
(862, 352, 245, 'N6-succinyllysine', 'unknown', '-'),
(863, 352, 248, 'Phosphoserine', 'unknown', '19369195'),
(864, 353, 2, 'N-acetylalanine', 'unknown', '-'),
(865, 353, 113, 'N6-acetyllysine', 'unknown', '-'),
(866, 353, 274, 'N6-acetyllysine', 'autocatalysis', '-'),
(867, 355, 199, 'Phosphothreonine', 'IPL1', '12408861;17330950'),
(868, 356, 31, 'Phosphoserine', 'unknown', '20068231'),
(869, 356, 50, 'Phosphoserine', 'unknown', '21406692'),
(870, 356, 249, 'Phosphoserine', 'unknown', '20068231'),
(871, 362, 88, 'Phosphothreonine', 'unknown', '18407956'),
(872, 363, 917, 'Phosphoserine', 'unknown', '-'),
(873, 365, 2, 'N-acetylalanine', 'unknown', '20388717'),
(874, 365, 358, 'Phosphoserine', 'unknown', '18669648'),
(875, 365, 409, 'Phosphothreonine', 'CDK2', '15037602'),
(876, 365, 428, 'Phosphoserine', 'unknown', '15037602;18669648;19690332;20068231'),
(877, 365, 435, 'Phosphoserine', 'unknown', '19690332'),
(878, 365, 436, 'Phosphothreonine', 'unknown', '19690332'),
(879, 365, 442, 'Phosphoserine', 'unknown', '15037602;17081983;18669648;19690332;20068231;21406692'),
(880, 365, 524, 'N6-acetyllysine', 'unknown', '19608861'),
(881, 366, 2, 'N-acetylalanine', 'unknown', '-'),
(882, 366, 358, 'Phosphoserine', 'unknown', '-'),
(883, 366, 411, 'Phosphothreonine', 'CDK2', '-'),
(884, 366, 430, 'Phosphoserine', 'unknown', '-'),
(885, 366, 437, 'Phosphoserine', 'unknown', '-'),
(886, 366, 438, 'Phosphothreonine', 'unknown', '-'),
(887, 366, 444, 'Phosphoserine', 'unknown', '15037602;19131326'),
(888, 366, 526, 'N6-acetyllysine', 'unknown', '-'),
(889, 367, 1, 'N-acetylmethionine', 'unknown', '20068231'),
(890, 367, 607, 'N6-acetyllysine', 'unknown', '19608861');
INSERT INTO `ptms` (`PTMsID`, `PTMsProteinID`, `Position`, `PTMsPTMType`, `PTMsKinase`, `PubMeds`) VALUES
(891, 367, 1058, 'Phosphoserine', 'unknown', '18669648;19690332'),
(892, 367, 1061, 'Phosphoserine', 'unknown', '17081983;18669648;19690332;20068231;21406692'),
(893, 367, 1112, 'Phosphothreonine', 'unknown', '19690332'),
(894, 367, 1177, 'Phosphoserine', 'unknown', '20068231'),
(895, 367, 1178, 'Phosphoserine', 'unknown', '20068231'),
(896, 368, 430, 'Phosphoserine', 'PLK1', '-'),
(897, 370, 23, 'N6-acetyllysine', 'unknown', '-'),
(898, 370, 34, 'Phosphothreonine', 'CDK1;CDK15', '-'),
(899, 370, 48, 'Phosphothreonine', 'unknown', '-'),
(900, 370, 90, 'N6-acetyllysine', 'unknown', '-'),
(901, 370, 110, 'N6-acetyllysine', 'unknown', '-'),
(902, 370, 112, 'N6-acetyllysine', 'unknown', '-'),
(903, 370, 115, 'N6-acetyllysine', 'unknown', '-'),
(904, 370, 117, 'Phosphothreonine', 'AURKB', '-'),
(905, 370, 129, 'N6-acetyllysine', 'unknown', '-'),
(906, 371, 685, 'Phosphoserine', 'unknown', '18327897'),
(907, 371, 689, 'Phosphoserine', 'unknown', '18327897'),
(908, 371, 885, 'Phosphoserine', 'unknown', '18327897'),
(909, 371, 886, 'Phosphoserine', 'unknown', '18327897'),
(910, 371, 887, 'Phosphoserine', 'unknown', '18327897'),
(911, 374, 477, 'Phosphoserine', 'unknown', '19779198'),
(912, 374, 508, 'Phosphoserine', 'unknown', '15665377'),
(913, 374, 552, 'Phosphoserine', 'unknown', '18407956'),
(914, 374, 587, 'Phosphoserine', 'unknown', '17287358'),
(915, 374, 751, 'Phosphoserine', 'unknown', '18407956'),
(916, 374, 765, 'Phosphoserine', 'unknown', '19779198'),
(917, 376, 1, 'N-acetylmethionine', 'unknown', '-'),
(918, 376, 16, 'Phosphoserine', 'unknown', '-'),
(919, 376, 61, 'N6-acetyllysine', 'unknown', '-'),
(920, 376, 214, 'Phosphoserine', 'unknown', '-'),
(921, 376, 428, 'Phosphoserine', 'unknown', '-'),
(922, 380, 22, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(923, 380, 28, 'Phosphoserine', 'unknown', '19690332'),
(924, 380, 39, 'Phosphothreonine', 'unknown', '19690332'),
(925, 380, 41, 'Phosphoserine', 'unknown', '19690332;20068231'),
(926, 380, 50, 'Phosphoserine', 'unknown', '19690332'),
(927, 380, 143, 'Phosphoserine', 'unknown', '20068231'),
(928, 380, 381, 'N6-acetyllysine', 'unknown', '-'),
(929, 380, 679, 'N6-acetyllysine', 'unknown', '19608861'),
(930, 380, 1056, 'Phosphoserine', 'unknown', '20068231'),
(931, 381, 10, 'Phosphoserine', 'unknown', '-'),
(932, 381, 39, 'Phosphoserine', 'unknown', '-'),
(933, 381, 131, 'Phosphoserine', 'unknown', '-'),
(934, 381, 319, 'Phosphoserine', 'unknown', '-'),
(935, 381, 353, 'Phosphoserine', 'unknown', '17242355'),
(936, 381, 355, 'Phosphoserine', 'unknown', '17242355'),
(937, 381, 371, 'Phosphoserine', 'unknown', '-'),
(938, 381, 375, 'Phosphoserine', 'unknown', '-'),
(939, 381, 414, 'N6-acetyllysine', 'unknown', '23806337'),
(940, 381, 498, 'Phosphoserine', 'unknown', '-'),
(941, 381, 636, 'Phosphoserine', 'unknown', '-'),
(942, 381, 648, 'Phosphoserine', 'unknown', '-'),
(943, 381, 948, 'Phosphoserine', 'unknown', '-'),
(944, 381, 1289, 'Phosphotyrosine', 'unknown', '17947660'),
(945, 381, 1405, 'Phosphoserine', 'unknown', '-'),
(946, 384, 2, 'N-acetylserine', 'unknown', '-'),
(947, 384, 1123, 'N6-acetyllysine', 'unknown', '-'),
(948, 384, 3478, 'N6-acetyllysine', 'unknown', '-'),
(949, 384, 4281, 'N6-acetyllysine', 'unknown', '23806337'),
(950, 384, 4366, 'Phosphoserine', 'unknown', '-'),
(951, 385, 179, 'N6-acetyllysine', 'unknown', '-'),
(952, 385, 211, 'Phosphoserine', 'unknown', '-'),
(953, 386, 10, 'Phosphothreonine', 'PKA; in vitro', '11994303'),
(954, 386, 25, 'Phosphoserine', 'unknown', '11994303'),
(955, 386, 26, 'Phosphoserine', 'unknown', '11994303'),
(956, 386, 201, 'Phosphothreonine', 'PKA', '10567586;11994303'),
(957, 386, 260, 'Phosphoserine', 'autocatalysis', '11994303'),
(958, 386, 326, 'Phosphoserine', 'autocatalysis', '11994303'),
(959, 386, 340, 'Phosphoserine', 'CDK1', '11994303'),
(960, 387, 2, 'N-acetylalanine', 'unknown', '-'),
(961, 388, 2, 'N-acetylalanine', 'unknown', '22814378'),
(962, 388, 6, 'Phosphotyrosine', 'unknown', '15144186'),
(963, 388, 83, 'Phosphoserine', 'unknown', '19690332'),
(964, 388, 86, 'Phosphotyrosine', 'unknown', '-'),
(965, 390, 86, 'Phosphothreonine', 'unknown', '-'),
(966, 390, 333, 'Phosphoserine', 'unknown', '-'),
(967, 390, 345, 'Phosphoserine', 'unknown', '-'),
(968, 390, 346, 'Phosphoserine', 'unknown', '-'),
(969, 390, 357, 'Phosphoserine', 'unknown', '-'),
(970, 392, 73, 'N6-acetyllysine', 'unknown', '19608861'),
(971, 392, 126, 'Phosphoserine', 'CDK1', '12447691;12524548'),
(972, 392, 128, 'Phosphoserine', 'unknown', '12447691'),
(973, 392, 133, 'Phosphoserine', 'PLK1', '12447691;12524548'),
(974, 392, 147, 'Phosphoserine', 'unknown', '12447691;12524548'),
(975, 392, 321, 'Phosphothreonine', 'unknown', '18691976'),
(976, 393, 2, 'N-acetylserine', 'unknown', '-'),
(977, 393, 457, 'Phosphoserine', 'unknown', '-'),
(978, 393, 587, 'Phosphoserine', 'unknown', '-'),
(979, 393, 608, 'Phosphoserine', 'unknown', '-'),
(980, 396, 34, 'Phosphoserine', 'unknown', '-'),
(981, 396, 119, 'Phosphoserine', 'unknown', '-'),
(982, 396, 152, 'Phosphoserine', 'unknown', '-'),
(983, 396, 155, 'Phosphoserine', 'unknown', '-'),
(984, 396, 260, 'Phosphothreonine', 'unknown', '-'),
(985, 396, 306, 'Phosphoserine', 'unknown', '-'),
(986, 397, 88, 'Phosphothreonine', 'TTK', '19530738'),
(987, 397, 94, 'Phosphothreonine', 'TTK', '19530738'),
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(1620, 627, 785, 'Phosphoserine', 'unknown', '18327897'),
(1621, 627, 792, 'Phosphoserine', 'unknown', '18327897'),
(1622, 627, 826, 'Phosphothreonine', 'unknown', '18327897'),
(1623, 629, 307, 'Phosphotyrosine', 'unknown', '-'),
(1624, 629, 309, 'Leucine methyl ester', 'unknown', '8206937'),
(1625, 633, 36, 'Phosphoserine', 'unknown', '20068231'),
(1626, 633, 233, 'Phosphoserine', 'unknown', '18669648'),
(1627, 639, 326, 'N6-acetyllysine', 'unknown', '-'),
(1628, 639, 386, 'N6-acetyllysine', 'unknown', '-'),
(1629, 639, 419, 'N6-acetyllysine', 'unknown', '-'),
(1630, 639, 453, 'Phosphoserine', 'unknown', '-'),
(1631, 639, 502, 'N6-acetyllysine', 'unknown', '-'),
(1632, 639, 531, 'N6-acetyllysine', 'unknown', '-'),
(1633, 639, 551, 'N6-acetyllysine', 'unknown', '23806337'),
(1634, 639, 596, 'Phosphoserine', 'unknown', '-'),
(1635, 639, 597, 'Phosphoserine', 'unknown', '-'),
(1636, 639, 706, 'Phosphoserine', 'unknown', '-'),
(1637, 639, 787, 'N6-acetyllysine', 'unknown', '23806337'),
(1638, 639, 797, 'N6-acetyllysine', 'unknown', '-'),
(1639, 639, 822, 'N6-acetyllysine', 'unknown', '23806337'),
(1640, 639, 829, 'N6-acetyllysine', 'unknown', '23806337'),
(1641, 639, 1259, 'Phosphoserine', 'unknown', '19144319'),
(1642, 639, 1760, 'N6-acetyllysine', 'unknown', '23806337'),
(1643, 639, 1762, 'Phosphothreonine', 'unknown', '-'),
(1644, 639, 1963, 'Phosphoserine', 'unknown', '-'),
(1645, 639, 2116, 'Phosphoserine', 'unknown', '-'),
(1646, 639, 2118, 'Phosphoserine', 'unknown', '-'),
(1647, 639, 2141, 'Phosphoserine', 'unknown', '-'),
(1648, 639, 2223, 'Phosphoserine', 'unknown', '17242355;19131326;19144319'),
(1649, 642, 1, 'N-acetylmethionine', 'unknown', '19413330'),
(1650, 642, 22, 'Phosphoserine', 'unknown', '20068231'),
(1651, 647, 2471, 'Cysteine methyl ester', 'unknown', '-'),
(1652, 649, 43, 'Phosphoserine', 'unknown', '17081983;21406692'),
(1653, 649, 310, 'Phosphoserine', 'PKA', '14576165'),
(1654, 649, 346, 'Phosphoserine', 'PKC', '14576165'),
(1655, 649, 367, 'Phosphoserine', 'unknown', '21406692'),
(1656, 650, 329, 'Phosphoserine', 'unknown', '19144319'),
(1657, 650, 346, 'Phosphoserine', 'PKC', '-'),
(1658, 650, 367, 'Phosphoserine', 'unknown', '17242355'),
(1659, 650, 370, 'Phosphothreonine', 'unknown', '17242355'),
(1660, 650, 371, 'Phosphoserine', 'unknown', '17242355'),
(1661, 651, 6, 'Phosphoserine', 'unknown', '24275569'),
(1662, 651, 42, 'Phosphothreonine', 'unknown', '18669648'),
(1663, 651, 52, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692;24275569'),
(1664, 651, 54, 'Phosphoserine', 'unknown', '24275569'),
(1665, 651, 98, 'Phosphoserine', 'unknown', '24275569'),
(1666, 651, 153, 'Phosphoserine', 'unknown', '24275569'),
(1667, 658, 89, 'Phosphoserine', 'unknown', '-'),
(1668, 658, 91, 'Phosphoserine', 'unknown', '-'),
(1669, 658, 175, 'Phosphoserine', 'unknown', '-'),
(1670, 659, 89, 'Phosphoserine', 'unknown', '20068231;21406692;24275569'),
(1671, 659, 91, 'Phosphoserine', 'unknown', '21406692'),
(1672, 659, 175, 'Phosphoserine', 'unknown', '21406692'),
(1673, 660, 1, 'N-acetylmethionine', 'unknown', '-'),
(1674, 661, 4, 'Nitrated tyrosine', 'unknown', '-'),
(1675, 662, 460, 'Phosphothreonine', 'unknown', '18257517'),
(1676, 664, 69, 'Phosphoserine', 'unknown', '20068231'),
(1677, 664, 165, 'Phosphoserine', 'NEK2', '12386167'),
(1678, 665, 278, 'Phosphoserine', 'unknown', '18407956'),
(1679, 665, 280, 'Phosphoserine', 'unknown', '18407956'),
(1680, 666, 54, 'Phosphoserine', 'unknown', '17287358'),
(1681, 666, 68, 'Phosphothreonine', 'unknown', '17287358'),
(1682, 666, 74, 'Phosphoserine', 'unknown', '17287358;18407956'),
(1683, 666, 88, 'Phosphoserine', 'unknown', '17287358'),
(1684, 668, 2, 'N-acetylalanine', 'unknown', '19413330'),
(1685, 668, 12, 'Phosphoserine', 'unknown', '21406692'),
(1686, 668, 24, 'Phosphoserine', 'unknown', '18318008;20068231;21406692'),
(1687, 668, 27, 'Phosphoserine', 'unknown', '18318008;20068231;21406692;24275569'),
(1688, 668, 44, 'Phosphoserine', 'unknown', '20068231;24275569'),
(1689, 668, 47, 'Phosphoserine', 'unknown', '20068231;24275569'),
(1690, 669, 297, 'Phosphoserine', 'unknown', '24275569'),
(1691, 669, 399, 'Phosphoserine', 'unknown', '18669648;19690332'),
(1692, 676, 1284, 'Phosphoserine', 'unknown', '18327897'),
(1693, 676, 1344, 'Phosphoserine', 'unknown', '18327897'),
(1694, 676, 1352, 'Phosphothreonine', 'unknown', '18327897'),
(1695, 676, 1374, 'Phosphoserine', 'unknown', '18327897'),
(1696, 676, 1385, 'Phosphoserine', 'unknown', '18327897'),
(1697, 676, 1392, 'Phosphoserine', 'unknown', '18327897'),
(1698, 676, 1396, 'Phosphoserine', 'unknown', '18327897'),
(1699, 679, 55, 'Phosphoserine', 'unknown', '18257517'),
(1700, 680, 2, 'N-acetylalanine', 'unknown', '22814378'),
(1701, 680, 744, 'Phosphoserine', 'unknown', '20068231'),
(1702, 680, 780, 'Phosphoserine', 'unknown', '18669648;20068231;24275569'),
(1703, 680, 1042, 'Phosphoserine', 'unknown', '18669648'),
(1704, 680, 1360, 'Phosphoserine', 'unknown', '18669648'),
(1705, 680, 1861, 'Phosphoserine', 'unknown', '18669648;21406692'),
(1706, 680, 1863, 'Phosphoserine', 'unknown', '18669648;21406692'),
(1707, 680, 1864, 'Phosphoserine', 'unknown', '18669648;21406692'),
(1708, 680, 2151, 'Phosphothreonine', 'unknown', '18669648'),
(1709, 680, 2260, 'Phosphoserine', 'unknown', '18669648'),
(1710, 680, 2270, 'Phosphoserine', 'unknown', '18669648'),
(1711, 680, 2283, 'Phosphoserine', 'unknown', '18669648'),
(1712, 680, 2473, 'Phosphoserine', 'unknown', '18669648'),
(1713, 680, 2535, 'Phosphoserine', 'unknown', '18669648'),
(1714, 680, 2671, 'Phosphoserine', 'unknown', '18220336;18669648'),
(1715, 680, 2674, 'Phosphoserine', 'unknown', '18669648'),
(1716, 680, 2679, 'Phosphothreonine', 'unknown', '18669648'),
(1717, 680, 2789, 'Phosphoserine', 'unknown', '18669648'),
(1718, 682, 2, 'N-acetylserine', 'unknown', '-'),
(1719, 682, 12, 'Phosphotyrosine', 'unknown', '-'),
(1720, 683, 961, 'Phosphoserine', 'unknown', '18307296'),
(1721, 684, 101, 'Phosphoserine', 'unknown', '-'),
(1722, 687, 1, 'N-acetylmethionine', 'unknown', '19413330;22814378'),
(1723, 688, 73, 'N6-acetyllysine', 'unknown', '-'),
(1724, 688, 123, 'Phosphoserine', 'CDK1', '-'),
(1725, 688, 125, 'Phosphoserine', 'unknown', '-'),
(1726, 688, 130, 'Phosphoserine', 'PLK1', '-'),
(1727, 688, 144, 'Phosphoserine', 'unknown', '-'),
(1728, 688, 318, 'Phosphothreonine', 'unknown', '-'),
(1729, 691, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(1730, 691, 149, 'Phosphoserine', 'PLK1', '19468300'),
(1731, 691, 154, 'Phosphoserine', 'unknown', '19690332;20068231;21406692'),
(1732, 691, 157, 'Phosphoserine', 'PLK1', '19468300;19468302;19690332;20068231;21406692'),
(1733, 691, 161, 'Phosphothreonine', 'unknown', '17081983'),
(1734, 691, 164, 'Phosphoserine', 'PLK1', '17081983;19468300;19468302'),
(1735, 691, 170, 'Phosphoserine', 'PLK1', '19468300;19468302'),
(1736, 691, 203, 'Phosphoserine', 'unknown', '16964243;17081983;18669648;19690332;20068231'),
(1737, 691, 206, 'Phosphoserine', 'unknown', '18669648;19690332'),
(1738, 691, 214, 'Phosphoserine', 'unknown', '19468302'),
(1739, 691, 257, 'Phosphoserine', 'unknown', '18669648'),
(1740, 691, 260, 'Phosphothreonine', 'unknown', '19468302'),
(1741, 691, 342, 'Phosphothreonine', 'unknown', '18669648;20068231'),
(1742, 691, 387, 'Phosphoserine', 'AURKB', '12689593'),
(1743, 691, 410, 'Phosphoserine', 'AURKB', '12689593'),
(1744, 691, 567, 'Phosphothreonine', 'unknown', '20068231'),
(1745, 691, 580, 'Phosphothreonine', 'unknown', '18669648'),
(1746, 691, 588, 'Phosphothreonine', 'unknown', '16964243;18669648;20068231'),
(1747, 691, 600, 'Phosphoserine', 'unknown', '18669648'),
(1748, 691, 601, 'Phosphothreonine', 'unknown', '18669648'),
(1749, 691, 606, 'Phosphothreonine', 'unknown', '18669648'),
(1750, 692, 520, 'Phosphothreonine', 'unknown', '17372656'),
(1751, 692, 933, 'Phosphothreonine', 'CDC2', '-'),
(1752, 692, 949, 'Phosphoserine', 'unknown', '17372656;18327897'),
(1753, 692, 1043, 'Phosphoserine', 'unknown', '18327897'),
(1754, 692, 1045, 'Phosphothreonine', 'unknown', '18327897'),
(1755, 692, 1050, 'Phosphoserine', 'unknown', '18327897'),
(1756, 692, 1054, 'Phosphoserine', 'unknown', '18327897'),
(1757, 699, 42, 'Phosphoserine', 'unknown', '21406692');
INSERT INTO `ptms` (`PTMsID`, `PTMsProteinID`, `Position`, `PTMsPTMType`, `PTMsKinase`, `PubMeds`) VALUES
(1758, 699, 335, 'Phosphoserine', 'unknown', '18669648'),
(1759, 699, 336, 'Phosphoserine', 'unknown', '18669648'),
(1760, 699, 350, 'Phosphoserine', 'unknown', '18669648'),
(1761, 699, 352, 'Phosphoserine', 'unknown', '18669648'),
(1762, 702, 2, 'N-acetylserine', 'unknown', '-'),
(1763, 702, 7, 'Phosphoserine', 'unknown', '-'),
(1764, 702, 14, 'Phosphoserine', 'unknown', '-'),
(1765, 702, 21, 'Phosphoserine', 'unknown', '-'),
(1766, 702, 527, 'Phosphoserine', 'PLK1', '-'),
(1767, 702, 823, 'Phosphoserine', 'unknown', '-'),
(1768, 702, 855, 'Phosphothreonine', 'unknown', '-'),
(1769, 702, 865, 'Phosphoserine', 'unknown', '-'),
(1770, 703, 9, 'Phosphoserine', 'PKB/AKT1; RPS6KA3;SGK3', '22057101;23395175'),
(1771, 703, 216, 'Phosphotyrosine', 'unknown', '-'),
(1772, 703, 389, 'Phosphoserine', 'unknown', '15345747'),
(1773, 704, 75, 'Phosphoserine', 'unknown', '-'),
(1774, 704, 101, 'N6-acetyllysine', 'unknown', '-'),
(1775, 704, 114, 'Phosphoserine', 'unknown', '-'),
(1776, 704, 120, 'Phosphoserine', 'unknown', '-'),
(1777, 704, 156, 'Phosphoserine', 'unknown', '-'),
(1778, 706, 607, 'Phosphoserine', 'unknown', '18327897'),
(1779, 706, 609, 'Phosphothreonine', 'unknown', '18327897'),
(1780, 706, 612, 'Phosphoserine', 'unknown', '18327897'),
(1781, 707, 1, 'N-acetylmethionine', 'unknown', '19413330'),
(1782, 707, 92, 'N6-acetyllysine', 'unknown', '-'),
(1783, 707, 223, 'Phosphoserine', 'unknown', '18691976'),
(1784, 708, 331, 'Phosphoserine', 'unknown', '-'),
(1785, 708, 335, 'Phosphoserine', 'unknown', '-'),
(1786, 714, 28, 'Phosphoserine', 'unknown', '18669648'),
(1787, 714, 30, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(1788, 714, 58, 'Phosphoserine', 'unknown', '20068231'),
(1789, 714, 77, 'Phosphoserine', 'unknown', '18669648'),
(1790, 714, 81, 'Phosphoserine', 'unknown', '18669648;20068231'),
(1791, 719, 31, 'Phosphoserine', 'unknown', '20068231'),
(1792, 724, 2, 'N-acetylserine', 'unknown', '-'),
(1793, 724, 5, 'N6-acetyllysine', 'unknown', '-'),
(1794, 724, 9, 'N6-acetyllysine', 'unknown', '-'),
(1795, 724, 106, 'N5-methylglutamine', 'unknown', '24352239'),
(1796, 724, 129, 'Phosphoserine', 'unknown', '15226425'),
(1797, 725, 194, 'Phosphoserine', 'unknown', '-'),
(1798, 725, 383, 'Phosphoserine', 'unknown', '-'),
(1799, 725, 391, 'Phosphoserine', 'unknown', '-'),
(1800, 725, 394, 'Phosphothreonine', 'unknown', '-'),
(1801, 725, 405, 'Phosphoserine', 'unknown', '-'),
(1802, 725, 407, 'Phosphoserine', 'unknown', '-'),
(1803, 725, 441, 'Phosphothreonine', 'unknown', '-'),
(1804, 725, 443, 'Phosphoserine', 'unknown', '-'),
(1805, 725, 446, 'Phosphoserine', 'unknown', '-'),
(1806, 725, 459, 'Phosphoserine', 'unknown', '-'),
(1807, 725, 486, 'Phosphoserine', 'unknown', '-'),
(1808, 726, 1011, 'Phosphothreonine', 'CDC2', '-'),
(1809, 729, 530, 'Phosphothreonine', 'unknown', '-'),
(1810, 730, 1314, 'Phosphothreonine', 'CDK1', '9774278'),
(1811, 730, 1348, 'Phosphothreonine', 'CDK1', '9774278'),
(1812, 730, 1353, 'Phosphothreonine', 'CDK1', '9774278'),
(1813, 731, 108, 'Phosphothreonine', 'unknown', '20068231'),
(1814, 731, 139, 'Phosphoserine', 'unknown', '17081983;18669648;20068231;21406692'),
(1815, 731, 145, 'Phosphothreonine', 'unknown', '17081983;18669648;20068231'),
(1816, 731, 239, 'N6-acetyllysine', 'unknown', '19608861'),
(1817, 731, 274, 'Phosphoserine', 'PLK1', '12852857'),
(1818, 731, 326, 'Phosphoserine', 'PLK1', '12852857'),
(1819, 733, 123, 'N6-acetyllysine', 'unknown', '19608861'),
(1820, 736, 168, 'Phosphothreonine', 'unknown', '18327897'),
(1821, 736, 477, 'Phosphothreonine', 'unknown', '18327897'),
(1822, 736, 480, 'Phosphoserine', 'unknown', '18327897'),
(1823, 736, 485, 'Phosphoserine', 'unknown', '18327897'),
(1824, 737, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(1825, 738, 242, 'Phosphothreonine', 'unknown', '17330950'),
(1826, 738, 257, 'Phosphothreonine', 'unknown', '18407956'),
(1827, 745, 146, 'Phosphothreonine', 'unknown', '18327897'),
(1828, 745, 152, 'Phosphoserine', 'unknown', '18327897'),
(1829, 745, 163, 'Phosphoserine', 'unknown', '18327897'),
(1830, 745, 205, 'Phosphoserine', 'unknown', '18327897'),
(1831, 745, 209, 'Phosphothreonine', 'unknown', '18327897'),
(1832, 745, 218, 'Phosphoserine', 'unknown', '18327897'),
(1833, 745, 220, 'Phosphoserine', 'unknown', '18327897'),
(1834, 745, 244, 'Phosphoserine', 'unknown', '18327897'),
(1835, 751, 151, 'Phosphoserine', 'unknown', '20068231'),
(1836, 751, 445, 'Phosphoserine', 'unknown', '16964243;18669648;20068231'),
(1837, 751, 581, 'Phosphoserine', 'unknown', '20068231'),
(1838, 751, 582, 'Phosphoserine', 'unknown', '18669648;20068231;21406692'),
(1839, 751, 589, 'Phosphoserine', 'unknown', '18669648;20068231'),
(1840, 751, 610, 'Phosphoserine', 'unknown', '21406692'),
(1841, 756, 19, 'Phosphoserine', 'unknown', '-'),
(1842, 756, 92, 'Phosphoserine', 'AURKB', '-'),
(1843, 756, 106, 'Phosphoserine', 'unknown', '-'),
(1844, 756, 108, 'Phosphoserine', 'unknown', '-'),
(1845, 756, 112, 'Phosphoserine', 'unknown', '-'),
(1846, 756, 162, 'Phosphoserine', 'unknown', '-'),
(1847, 756, 188, 'Phosphoserine', 'unknown', '-'),
(1848, 756, 626, 'Phosphoserine', 'unknown', '-'),
(1849, 757, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(1850, 759, 88, 'Phosphothreonine', 'TTK', '-'),
(1851, 759, 91, 'Citrulline', 'unknown', '-'),
(1852, 759, 94, 'Phosphothreonine', 'TTK', '-'),
(1853, 759, 106, 'Phosphothreonine', 'unknown', '-'),
(1854, 759, 110, 'Phosphoserine', 'unknown', '-'),
(1855, 759, 174, 'Phosphoserine', 'AURKB', '-'),
(1856, 759, 197, 'Phosphothreonine', 'unknown', '-'),
(1857, 759, 212, 'Phosphothreonine', 'unknown', '-'),
(1858, 759, 227, 'Phosphoserine', 'unknown', '-'),
(1859, 759, 232, 'Phosphoserine', 'unknown', '-'),
(1860, 759, 246, 'Phosphoserine', 'unknown', '-'),
(1861, 759, 252, 'Phosphoserine', 'unknown', '-'),
(1862, 763, 2, 'N-acetylalanine', 'unknown', '-'),
(1863, 763, 307, 'Phosphothreonine', 'unknown', '-'),
(1864, 763, 311, 'Phosphothreonine', 'unknown', '-'),
(1865, 767, 2, 'N-acetylalanine', 'unknown', '22814378'),
(1866, 770, 168, 'Phosphoserine', 'unknown', '17330950;18407956;19779198'),
(1867, 770, 171, 'Phosphoserine', 'unknown', '17330950;18407956;19779198'),
(1868, 772, 2, 'N-acetylalanine', 'unknown', '19413330;20068231;22223895;22814378'),
(1869, 772, 265, 'Phosphothreonine', 'unknown', '20068231'),
(1870, 772, 281, 'Phosphoserine', 'unknown', '21864708'),
(1871, 772, 331, 'Phosphoserine', 'unknown', '20068231;21864708'),
(1872, 773, 78, 'Phosphothreonine', 'unknown', '19779198'),
(1873, 773, 94, 'Phosphoserine', 'unknown', '18407956;19779198'),
(1874, 773, 509, 'Phosphothreonine', 'unknown', '19779198'),
(1875, 776, 222, 'Phosphoserine', 'unknown', '18407956'),
(1876, 777, 2, 'N-acetylserine', 'unknown', '-'),
(1877, 777, 5, 'N6-acetyllysine', 'unknown', '-'),
(1878, 777, 9, 'N6-acetyllysine', 'unknown', '-'),
(1879, 777, 106, 'N5-methylglutamine', 'unknown', '24352239'),
(1880, 777, 128, 'Phosphoserine', 'unknown', '15226425'),
(1881, 779, 17, 'Phosphoserine', 'unknown', '-'),
(1882, 779, 71, 'Phosphoserine', 'unknown', '-'),
(1883, 790, 75, 'Phosphoserine', 'unknown', '19690332'),
(1884, 790, 78, 'Phosphothreonine', 'unknown', '19690332'),
(1885, 790, 102, 'N6-acetyllysine', 'unknown', '-'),
(1886, 790, 115, 'Phosphoserine', 'unknown', '-'),
(1887, 790, 121, 'Phosphoserine', 'unknown', '-'),
(1888, 790, 157, 'Phosphoserine', 'unknown', '-'),
(1889, 792, 2, 'N-acetylvaline', 'unknown', '19413330;22223895'),
(1890, 792, 309, 'Phosphoserine', 'unknown', '20068231'),
(1891, 793, 2, 'N-acetylserine', 'unknown', '-'),
(1892, 793, 6, 'Phosphothreonine', 'unknown', '-'),
(1893, 793, 101, 'Phosphoserine', 'unknown', '-'),
(1894, 793, 208, 'Phosphothreonine', 'AURKA', '-'),
(1895, 793, 212, 'Phosphothreonine', 'unknown', '-'),
(1896, 793, 267, 'Phosphoserine', 'autocatalysis', '-'),
(1897, 793, 333, 'Phosphoserine', 'unknown', '-'),
(1898, 793, 373, 'Phosphoserine', 'unknown', '-'),
(1899, 793, 448, 'Phosphoserine', 'unknown', '-'),
(1900, 793, 496, 'Phosphothreonine', 'unknown', '-'),
(1901, 794, 88, 'Phosphoserine', 'unknown', '-'),
(1902, 797, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(1903, 797, 45, 'Phosphoserine', 'ATM or ATR', '18407956;19779198'),
(1904, 797, 48, 'Phosphoserine', 'unknown', '18407956;19779198'),
(1905, 797, 84, 'Phosphoserine', 'unknown', '18407956'),
(1906, 797, 138, 'Phosphothreonine', 'unknown', '17330950;19779198'),
(1907, 798, 1, 'N-acetylmethionine', 'unknown', '20068231'),
(1908, 798, 4, 'Phosphoserine', 'unknown', '18669648;20068231'),
(1909, 798, 11, 'Phosphoserine', 'unknown', '18669648;20068231'),
(1910, 798, 37, 'Phosphoserine', 'unknown', '17525332;18669648;19690332'),
(1911, 798, 46, 'Phosphothreonine', 'unknown', '16964243;18669648;19690332;20068231'),
(1912, 798, 55, 'Phosphothreonine', 'unknown', '18669648'),
(1913, 798, 58, 'Phosphoserine', 'unknown', '18669648'),
(1914, 798, 64, 'Phosphothreonine', 'unknown', '18669648'),
(1915, 798, 69, 'Phosphoserine', 'unknown', '18669648'),
(1916, 798, 86, 'Phosphoserine', 'unknown', '17081983;18669648'),
(1917, 800, 2, 'N-acetylserine', 'unknown', '19413330;20068231;21406692;22223895;22814378'),
(1918, 800, 4, 'Phosphoserine', 'unknown', '20068231;21406692'),
(1919, 800, 17, 'N6-acetyllysine', 'unknown', '-'),
(1920, 800, 21, 'N6-acetyllysine', 'unknown', '-'),
(1921, 800, 59, 'Phosphoserine', 'unknown', '17081983;18220336;19690332;20068231;21406692;24275569'),
(1922, 800, 66, 'Phosphoserine', 'unknown', '18220336;19690332;20068231;21406692'),
(1923, 800, 186, 'N6-acetyllysine', 'unknown', '-'),
(1924, 800, 255, 'Citrulline', 'unknown', '-'),
(1925, 800, 265, 'N6-acetyllysine', 'unknown', '19608861'),
(1926, 800, 266, 'Phosphotyrosine', 'unknown', '-'),
(1927, 800, 271, 'Phosphoserine', 'unknown', '17081983;17487921;18669648;19690332;20068231;24275569'),
(1928, 800, 286, 'Phosphothreonine', 'unknown', '24275569'),
(1929, 800, 352, 'N6-acetyllysine', 'unknown', '19608861'),
(1930, 800, 516, 'N6-acetyllysine', 'unknown', '19608861'),
(1931, 800, 524, 'N6-acetyllysine', 'unknown', '19608861'),
(1932, 800, 551, 'N6-acetyllysine', 'unknown', '19608861'),
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(2567, 1055, 19, 'Phosphotyrosine', 'unknown', '-'),
(2568, 1055, 39, 'Phosphoserine', 'unknown', '-'),
(2569, 1055, 77, 'Phosphotyrosine', 'unknown', '-'),
(2570, 1055, 161, 'Phosphothreonine', 'CAK', '-'),
(2571, 1055, 178, 'Phosphoserine', 'unknown', '-'),
(2572, 1055, 222, 'Phosphothreonine', 'unknown', '-'),
(2573, 1055, 245, 'N6-succinyllysine', 'unknown', '-'),
(2574, 1055, 248, 'Phosphoserine', 'unknown', '-'),
(2575, 1056, 250, 'N6-acetyllysine', 'PCAF', '19407811'),
(2576, 1056, 435, 'Phosphoserine', 'unknown', '19015317'),
(2577, 1056, 543, 'Phosphoserine', 'unknown', '19015317;21406692'),
(2578, 1056, 670, 'Phosphoserine', 'unknown', '18669648;18691976;19015317;20068231'),
(2579, 1056, 676, 'Phosphoserine', 'PLK1', '17785528'),
(2580, 1056, 792, 'Phosphothreonine', 'PLK1', '17376779'),
(2581, 1056, 1008, 'Phosphothreonine', 'PLK1', '17376779'),
(2582, 1056, 1042, 'Phosphothreonine', 'unknown', '20068231'),
(2583, 1056, 1043, 'Phosphoserine', 'unknown', '19015317'),
(2584, 1057, 425, 'Phosphoserine', 'unknown', '18257517'),
(2585, 1058, 161, 'Phosphoserine', 'unknown', '18407956'),
(2586, 1058, 175, 'Phosphoserine', 'CDC5', '11371343'),
(2587, 1058, 210, 'N6-acetyllysine', 'ECO1', '11864574'),
(2588, 1058, 263, 'Phosphoserine', 'CDC5', '11371343'),
(2589, 1058, 307, 'Phosphoserine', 'unknown', '18407956'),
(2590, 1058, 354, 'Phosphothreonine', 'unknown', '18407956'),
(2591, 1059, 1406, 'Phosphothreonine', 'unknown', '18327897'),
(2592, 1059, 1416, 'Phosphoserine', 'unknown', '18327897'),
(2593, 1059, 1419, 'Phosphothreonine', 'unknown', '18327897'),
(2594, 1060, 2, 'N-acetylalanine', 'unknown', '19413330;22223895;22814378'),
(2595, 1060, 933, 'Phosphoserine', 'unknown', '20068231'),
(2596, 1062, 416, 'Phosphothreonine', 'unknown', '19690332;20068231'),
(2597, 1062, 422, 'Phosphothreonine', 'unknown', '19690332;20068231'),
(2598, 1063, 1, 'N-acetylmethionine', 'unknown', '19369195;22814378'),
(2599, 1063, 7, 'Phosphoserine', 'unknown', '18691976;19369195'),
(2600, 1063, 33, 'Phosphothreonine', 'unknown', '18669648;18691976;19369195;20068231'),
(2601, 1063, 37, 'Phosphoserine', 'unknown', '18691976;20068231'),
(2602, 1063, 80, 'Phosphoserine', 'unknown', '18691976'),
(2603, 1063, 281, 'Phosphoserine', 'unknown', '18691976;19369195;20068231'),
(2604, 1063, 317, 'Phosphoserine', 'unknown', '18691976'),
(2605, 1063, 321, 'Phosphoserine', 'unknown', '18669648;19369195'),
(2606, 1063, 393, 'Phosphoserine', 'unknown', '18669648;18691976'),
(2607, 1063, 436, 'Phosphoserine', 'unknown', '18691976;19369195'),
(2608, 1063, 821, 'Phosphoserine', 'unknown', '17924679;18669648;18691976;19369195;20068231'),
(2609, 1064, 1, 'N-acetylmethionine', 'unknown', '-'),
(2610, 1064, 524, 'Phosphoserine', 'unknown', '-'),
(2611, 1064, 1241, 'Phosphoserine', 'unknown', '-'),
(2612, 1064, 1660, 'Phosphoserine', 'unknown', '17242355'),
(2613, 1064, 1662, 'Phosphothreonine', 'unknown', '-'),
(2614, 1064, 1671, 'Phosphoserine', 'unknown', '17242355'),
(2615, 1065, 580, 'Phosphoserine', 'unknown', '15345747'),
(2616, 1065, 583, 'Phosphothreonine', 'unknown', '15345747'),
(2617, 1065, 1168, 'Phosphoserine', 'unknown', '-'),
(2618, 1065, 1239, 'Phosphothreonine', 'unknown', '-'),
(2619, 1065, 1243, 'Phosphoserine', 'unknown', '-'),
(2620, 1071, 211, 'Phosphoserine', 'unknown', '18669648'),
(2621, 1071, 215, 'Phosphothreonine', 'unknown', '18669648'),
(2622, 1071, 228, 'Phosphothreonine', 'unknown', '18669648'),
(2623, 1071, 231, 'Phosphoserine', 'unknown', '18669648;24275569'),
(2624, 1071, 239, 'Phosphoserine', 'unknown', '18669648'),
(2625, 1071, 243, 'Phosphothreonine', 'unknown', '18669648;20068231'),
(2626, 1071, 246, 'Phosphothreonine', 'unknown', '18669648;20068231'),
(2627, 1071, 282, 'Phosphoserine', 'unknown', '18669648;20068231'),
(2628, 1072, 2, 'N-acetylalanine', 'unknown', '19413330;22223895'),
(2629, 1072, 89, 'Phosphoserine', 'AMPK', '11518699;16574662'),
(2630, 1072, 285, 'Phosphoserine', 'unknown', '-'),
(2631, 1072, 418, 'N6-acetyllysine', 'unknown', '18995842'),
(2632, 1072, 423, 'N6-acetyllysine', 'unknown', '18995842'),
(2633, 1072, 580, 'Omega-N-methylated arginine', 'CARM1', '11701890'),
(2634, 1072, 604, 'Omega-N-methylated arginine', 'CARM1', '11701890'),
(2635, 1072, 636, 'N6-acetyllysine', 'unknown', '19608861'),
(2636, 1072, 885, 'Phosphothreonine', 'unknown', '-'),
(2637, 1072, 887, 'Phosphothreonine', 'unknown', '-'),
(2638, 1072, 977, 'N6-acetyllysine', 'unknown', '19608861');
INSERT INTO `ptms` (`PTMsID`, `PTMsProteinID`, `Position`, `PTMsPTMType`, `PTMsKinase`, `PubMeds`) VALUES
(2639, 1072, 1020, 'N6-acetyllysine', 'unknown', '15632193'),
(2640, 1072, 1024, 'N6-acetyllysine', 'unknown', '15632193'),
(2641, 1072, 1038, 'Phosphoserine', 'unknown', '21406692;24275569'),
(2642, 1072, 1180, 'N6-acetyllysine', 'unknown', '-'),
(2643, 1072, 1336, 'N6-acetyllysine', 'unknown', '17065153'),
(2644, 1072, 1473, 'N6-acetyllysine', 'unknown', '17065153'),
(2645, 1072, 1499, 'N6-acetyllysine', 'autocatalysis', '15004546'),
(2646, 1072, 1542, 'N6-acetyllysine', 'unknown', '18995842;19608861'),
(2647, 1072, 1546, 'N6-acetyllysine', 'unknown', '18995842;19608861'),
(2648, 1072, 1549, 'N6-acetyllysine', 'autocatalysis', '15004546;18995842'),
(2649, 1072, 1554, 'N6-acetyllysine', 'autocatalysis', '15004546;19608861'),
(2650, 1072, 1555, 'N6-acetyllysine', 'unknown', '19608861'),
(2651, 1072, 1558, 'N6-acetyllysine', 'unknown', '15004546;19608861'),
(2652, 1072, 1560, 'N6-acetyllysine', 'autocatalysis', '15004546;19608861'),
(2653, 1072, 1583, 'N6-acetyllysine', 'unknown', '19608861'),
(2654, 1072, 1699, 'N6-acetyllysine', 'unknown', '18995842'),
(2655, 1072, 1704, 'N6-acetyllysine', 'unknown', '18995842'),
(2656, 1072, 1707, 'N6-acetyllysine', 'unknown', '18995842'),
(2657, 1072, 1734, 'Phosphoserine', 'unknown', '-'),
(2658, 1072, 1857, 'Phosphothreonine', 'unknown', '-'),
(2659, 1072, 1859, 'Phosphothreonine', 'unknown', '-'),
(2660, 1072, 2142, 'Asymmetric dimethylarginine', 'CARM1; alternate', '15731352'),
(2661, 1072, 2142, 'Citrulline', 'PADI4; alternate', '15731352'),
(2662, 1073, 145, 'Phosphothreonine', 'unknown', '22006334'),
(2663, 1073, 675, 'Phosphothreonine', 'unknown', '22006334'),
(2664, 1073, 690, 'Phosphothreonine', 'unknown', '22006334'),
(2665, 1075, 2, 'N-acetylalanine', 'unknown', '-'),
(2666, 1075, 931, 'Phosphoserine', 'unknown', '-'),
(2667, 1077, 2, 'N-acetylalanine', 'unknown', '-'),
(2668, 1077, 8, 'N6-acetyllysine', 'unknown', '-'),
(2669, 1078, 2, 'N-acetylserine', 'unknown', '22814378'),
(2670, 1082, 407, 'Phosphoserine', 'unknown', '-'),
(2671, 1082, 422, 'Phosphoserine', 'unknown', '-'),
(2672, 1082, 447, 'Phosphoserine', 'unknown', '-'),
(2673, 1082, 541, 'Phosphoserine', 'unknown', '-'),
(2674, 1082, 560, 'Phosphoserine', 'unknown', '-'),
(2675, 1082, 578, 'Phosphoserine', 'unknown', '-'),
(2676, 1087, 972, 'Phosphoserine', 'unknown', '18407956'),
(2677, 1090, 1, 'N-acetylmethionine', 'unknown', '22814378'),
(2678, 1092, 2, 'N-acetylserine', 'unknown', '22814378'),
(2679, 1093, 2, 'N-acetylalanine', 'unknown', '-'),
(2680, 1093, 23, 'Phosphoserine', 'unknown', '-'),
(2681, 1093, 25, 'Phosphoserine', 'unknown', '-'),
(2682, 1093, 368, 'Phosphoserine', 'CDK2 (in cyclin E-CDK2 complex); by CDK5 (in cyclin p35-CDK5)', '-'),
(2683, 1093, 372, 'Phosphoserine', 'unknown', '-'),
(2684, 1098, 2, 'N-acetylalanine', 'unknown', '-'),
(2685, 1098, 151, 'Phosphoserine', 'unknown', '24275569'),
(2686, 1098, 332, 'Phosphothreonine', 'unknown', '-'),
(2687, 1098, 337, 'Phosphoserine', 'unknown', '-'),
(2688, 1098, 365, 'Phosphoserine', 'SGK1', '11410590'),
(2689, 1098, 373, 'Phosphothreonine', 'autocatalysis', '1508179'),
(2690, 1098, 396, 'Phosphothreonine', 'unknown', '-'),
(2691, 1098, 399, 'Phosphoserine', 'unknown', '-'),
(2692, 1098, 401, 'Phosphothreonine', 'unknown', '16964243;18669648'),
(2693, 1098, 405, 'Phosphoserine', 'unknown', '-'),
(2694, 1098, 446, 'Phosphoserine', 'unknown', '18669648'),
(2695, 1098, 447, 'Phosphoserine', 'unknown', '18669648'),
(2696, 1098, 671, 'Omega-N-methylarginine', 'PRMT5', '21917714'),
(2697, 1098, 729, 'Phosphoserine', 'unknown', '18669648;21406692'),
(2698, 1098, 753, 'Phosphothreonine', 'MAPK1', '19710016'),
(2699, 1102, 1007, 'N6-acetyllysine', 'unknown', '-'),
(2700, 1102, 1167, 'Phosphoserine', 'unknown', '-'),
(2701, 1104, 448, 'Phosphotyrosine', 'unknown', '17947660'),
(2702, 1104, 520, 'Phosphoserine', 'AMPK', '-'),
(2703, 1104, 523, 'Phosphoserine', 'AMPK', '-'),
(2704, 1105, 443, 'Phosphoserine', 'unknown', '-'),
(2705, 1105, 574, 'Phosphoserine', 'unknown', '-'),
(2706, 1105, 575, 'Phosphoserine', 'unknown', '19131326'),
(2707, 1105, 582, 'Phosphoserine', 'unknown', '-'),
(2708, 1106, 171, 'Phosphothreonine', 'PKA', '11879579'),
(2709, 1111, 12, 'Phosphoserine', 'unknown', '-'),
(2710, 1112, 358, 'Phosphoserine', 'unknown', '17525332'),
(2711, 1112, 360, 'Phosphoserine', 'unknown', '17525332;18669648;20068231'),
(2712, 1112, 648, 'N6-acetyllysine', 'unknown', '19608861'),
(2713, 1112, 713, 'N6-acetyllysine', 'unknown', '19608861'),
(2714, 1112, 957, 'Phosphoserine', 'ATM', '11877377;18669648;19690332;20068231'),
(2715, 1112, 966, 'Phosphoserine', 'ATM;ATR', '11877377;14657349;17525332;20068231'),
(2716, 1112, 970, 'Phosphoserine', 'unknown', '18669648'),
(2717, 1112, 1037, 'N6-acetyllysine', 'unknown', '-'),
(2718, 1114, 2, 'N-acetylalanine', 'unknown', '-'),
(2719, 1114, 120, 'Phosphoserine', 'unknown', '-'),
(2720, 1114, 600, 'Omega-N-methylated arginine', 'unknown', '11701890'),
(2721, 1114, 624, 'Omega-N-methylated arginine', 'unknown', '11701890'),
(2722, 1114, 656, 'N6-acetyllysine', 'unknown', '23806337'),
(2723, 1114, 1015, 'N6-acetyllysine', 'unknown', '-'),
(2724, 1114, 1031, 'Phosphoserine', 'unknown', '-'),
(2725, 1114, 1217, 'N6-acetyllysine', 'unknown', '23806337'),
(2726, 1114, 1383, 'Phosphoserine', 'IKKA', '-'),
(2727, 1114, 1387, 'Phosphoserine', 'IKKA', '-'),
(2728, 1114, 1584, 'N6-acetyllysine', 'unknown', '-'),
(2729, 1114, 1587, 'N6-acetyllysine', 'unknown', '-'),
(2730, 1114, 1592, 'N6-acetyllysine', 'unknown', '-'),
(2731, 1114, 1593, 'N6-acetyllysine', 'unknown', '-'),
(2732, 1114, 1596, 'N6-acetyllysine', 'unknown', '23806337'),
(2733, 1114, 1598, 'N6-acetyllysine', 'unknown', '23806337'),
(2734, 1114, 1742, 'N6-acetyllysine', 'unknown', '-'),
(2735, 1114, 1745, 'N6-acetyllysine', 'unknown', '23806337'),
(2736, 1114, 2064, 'Phosphoserine', 'unknown', '-'),
(2737, 1114, 2077, 'Phosphoserine', 'unknown', '-'),
(2738, 1114, 2080, 'Phosphoserine', 'unknown', '-'),
(2739, 1117, 2, 'N-acetylserine', 'unknown', '-'),
(2740, 1117, 138, 'Phosphoserine', 'unknown', '-'),
(2741, 1117, 145, 'Phosphoserine', 'unknown', '-'),
(2742, 1117, 155, 'Phosphoserine', 'unknown', '-'),
(2743, 1117, 199, 'Phosphoserine', 'unknown', '-'),
(2744, 1117, 358, 'Phosphothreonine', 'unknown', '-'),
(2745, 1120, 170, 'Phosphothreonine', 'autocatalysis', '-'),
(2746, 1120, 171, 'Phosphoserine', 'autocatalysis', '-'),
(2747, 1120, 175, 'Phosphothreonine', 'autocatalysis', '-'),
(2748, 1120, 179, 'Phosphothreonine', 'autocatalysis', '-'),
(2749, 1120, 241, 'Phosphoserine', 'autocatalysis', '-'),
(2750, 1120, 356, 'Phosphoserine', 'STK3/MST2', '-'),
(2751, 1120, 389, 'Phosphoserine', 'unknown', '-'),
(2752, 1120, 396, 'Phosphoserine', 'unknown', '-'),
(2753, 1120, 401, 'Phosphoserine', 'unknown', '-'),
(2754, 1120, 436, 'Phosphoserine', 'STK3/MST2', '-'),
(2755, 1121, 114, 'Phosphoserine', 'unknown', '-'),
(2756, 1121, 248, 'Phosphoserine', 'unknown', '-'),
(2757, 1122, 2, 'N-acetylserine', 'unknown', '-'),
(2758, 1122, 145, 'Phosphotyrosine', 'unknown', '-'),
(2759, 1124, 2647, 'Phosphoserine', 'unknown', '18669648'),
(2760, 1124, 2698, 'Cysteine methyl ester', 'unknown', '-'),
(2761, 1125, 116, 'Phosphoserine', 'unknown', '-'),
(2762, 1125, 249, 'Phosphoserine', 'unknown', '-'),
(2763, 1128, 155, 'Phosphoserine', 'unknown', '-'),
(2764, 1128, 160, 'Phosphoserine', 'unknown', '-'),
(2765, 1128, 606, 'Phosphoserine', 'unknown', '-'),
(2766, 1128, 739, 'Phosphothreonine', 'unknown', '-'),
(2767, 1128, 807, 'Phosphoserine', 'unknown', '-'),
(2768, 1128, 860, 'Phosphoserine', 'unknown', '19144319'),
(2769, 1129, 2, 'N-acetylalanine', 'unknown', '-'),
(2770, 1129, 775, 'N6-acetyllysine', 'unknown', '-'),
(2771, 1131, 2, 'N#N#N-trimethylserine', 'unknown', '17435751;18762580;20668449'),
(2772, 1131, 2, 'N#N-dimethylserine', 'unknown', '17435751;18762580;20668449'),
(2773, 1131, 2, 'N-methylserine', 'unknown', '17435751;18762580;20668449'),
(2774, 1131, 2, 'Phosphoserine', 'unknown', '17435751'),
(2775, 1131, 11, 'Phosphoserine', 'unknown', '17081983;20068231;21406692;24275569'),
(2776, 1134, 155, 'Phosphoserine', 'unknown', '17081983'),
(2777, 1134, 160, 'Phosphoserine', 'unknown', '18669648'),
(2778, 1134, 605, 'Phosphoserine', 'unknown', '21406692'),
(2779, 1134, 738, 'Phosphothreonine', 'unknown', '18669648'),
(2780, 1134, 814, 'Phosphoserine', 'unknown', '17081983'),
(2781, 1134, 867, 'Phosphoserine', 'unknown', '17081983;18669648;20068231'),
(2782, 1134, 902, 'Phosphoserine', 'unknown', '17081983;18669648'),
(2783, 1135, 295, 'Phosphoserine', 'unknown', '18307296'),
(2784, 1136, 114, 'N6-acetyllysine', 'unknown', '19608861'),
(2785, 1136, 222, 'N6-acetyllysine', 'unknown', '19608861'),
(2786, 1136, 677, 'N6-acetyllysine', 'unknown', '19608861'),
(2787, 1136, 1158, 'N6-acetyllysine', 'unknown', '19608861'),
(2788, 1136, 1160, 'N6-acetyllysine', 'unknown', '19608861'),
(2789, 1137, 46, 'Phosphoserine', 'unknown', '-'),
(2790, 1137, 153, 'Phosphoserine', 'unknown', '-'),
(2791, 1137, 175, 'Phosphoserine', 'unknown', '-'),
(2792, 1137, 249, 'Phosphoserine', 'unknown', '-'),
(2793, 1138, 25, 'Phosphoserine', 'unknown', '24275569'),
(2794, 1138, 178, 'Phosphoserine', 'unknown', '18669648'),
(2795, 1138, 213, 'Phosphoserine', 'unknown', '18669648'),
(2796, 1138, 459, 'Phosphothreonine', 'unknown', '-'),
(2797, 1138, 495, 'Phosphoserine', 'unknown', '18669648;20068231;21406692'),
(2798, 1138, 512, 'N6-acetyllysine', 'unknown', '19608861'),
(2799, 1138, 668, 'Phosphoserine', 'unknown', '12968034;18669648'),
(2800, 1138, 671, 'Phosphoserine', 'unknown', '18220336;18669648'),
(2801, 1138, 688, 'Phosphoserine', 'unknown', '18669648'),
(2802, 1138, 702, 'Phosphoserine', 'unknown', '16964243;18220336;18669648;19690332;20068231;21406692'),
(2803, 1138, 737, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(2804, 1138, 739, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(2805, 1140, 43, 'Phosphoserine', 'unknown', '18669648'),
(2806, 1140, 62, 'Phosphoserine', 'unknown', '18691976;20068231'),
(2807, 1140, 66, 'Phosphoserine', 'unknown', '20068231'),
(2808, 1140, 111, 'Phosphothreonine', 'GSK3-beta', '18055457'),
(2809, 1140, 135, 'Phosphoserine', 'unknown', '18669648;18691976;20068231'),
(2810, 1140, 334, 'Phosphoserine', 'unknown', '20068231'),
(2811, 1140, 336, 'Phosphothreonine', 'unknown', '20068231'),
(2812, 1140, 341, 'Phosphoserine', 'unknown', '18691976;20068231'),
(2813, 1140, 362, 'Phosphoserine', 'unknown', '20068231'),
(2814, 1140, 937, 'Phosphothreonine', 'GSK3-beta', '18055457'),
(2815, 1140, 974, 'Phosphoserine', 'GSK3-beta', '18055457'),
(2816, 1140, 978, 'Phosphothreonine', 'GSK3-beta', '18055457'),
(2817, 1142, 2, 'N-acetylserine', 'unknown', '22814378'),
(2818, 1142, 6, 'Phosphothreonine', 'unknown', '18691976'),
(2819, 1142, 103, 'Phosphoserine', 'unknown', '18691976'),
(2820, 1142, 137, 'Phosphoserine', 'unknown', '12207013'),
(2821, 1142, 210, 'Phosphothreonine', 'AURKA', '12207013;18477460;18615013;18669648;18691976;19369195;20068231'),
(2822, 1142, 214, 'Phosphothreonine', 'unknown', '18669648;18691976;19369195'),
(2823, 1142, 269, 'Phosphoserine', 'autocatalysis', '-'),
(2824, 1142, 335, 'Phosphoserine', 'unknown', '12442251'),
(2825, 1142, 375, 'Phosphoserine', 'unknown', '18691976'),
(2826, 1142, 450, 'Phosphoserine', 'unknown', '18691976'),
(2827, 1142, 498, 'Phosphothreonine', 'unknown', '18691976'),
(2828, 1143, 47, 'Phosphothreonine', 'CDK1', '-'),
(2829, 1145, 11, 'Phosphoserine', 'unknown', '18327897'),
(2830, 1145, 15, 'Phosphoserine', 'unknown', '17372656;18327897'),
(2831, 1145, 102, 'Phosphoserine', 'unknown', '18327897'),
(2832, 1145, 103, 'Phosphoserine', 'unknown', '18327897'),
(2833, 1145, 113, 'Phosphoserine', 'unknown', '18327897'),
(2834, 1145, 127, 'Phosphothreonine', 'unknown', '17372656'),
(2835, 1145, 128, 'Phosphothreonine', 'unknown', '17372656;18327897'),
(2836, 1145, 134, 'Phosphothreonine', 'unknown', '17372656'),
(2837, 1146, 53, 'N6-acetyllysine', 'unknown', '-'),
(2838, 1147, 116, 'Phosphothreonine', 'unknown', '-'),
(2839, 1148, 7, 'Phosphoserine', 'AURKA;AURKB', '11756469;14667408;18239465'),
(2840, 1148, 17, 'Phosphoserine', 'unknown', '18669648;21406692;24275569'),
(2841, 1148, 19, 'Phosphoserine', 'unknown', '18669648;21406692;24275569'),
(2842, 1148, 27, 'Phosphoserine', 'unknown', '18669648;21406692'),
(2843, 1149, 53, 'N6-acetyllysine', 'unknown', '-'),
(2844, 1150, 106, 'Phosphoserine', 'unknown', '18669648'),
(2845, 1150, 144, 'Phosphothreonine', 'unknown', '18669648'),
(2846, 1150, 151, 'Phosphothreonine', 'unknown', '20068231'),
(2847, 1150, 154, 'Phosphothreonine', 'unknown', '20068231'),
(2848, 1150, 158, 'Phosphotyrosine', 'unknown', '20068231'),
(2849, 1150, 276, 'Phosphoserine', 'unknown', '20068231'),
(2850, 1150, 773, 'Phosphoserine', 'unknown', '20068231'),
(2851, 1150, 783, 'Phosphoserine', 'unknown', '20068231'),
(2852, 1150, 821, 'Phosphoserine', 'unknown', '20068231'),
(2853, 1150, 834, 'Phosphoserine', 'unknown', '18669648'),
(2854, 1150, 876, 'Phosphoserine', 'unknown', '20068231'),
(2855, 1150, 1248, 'Phosphoserine', 'unknown', '18669648;20068231'),
(2856, 1150, 1255, 'Phosphoserine', 'unknown', '20068231'),
(2857, 1150, 1259, 'Phosphoserine', 'unknown', '20068231'),
(2858, 1150, 1747, 'Phosphoserine', 'unknown', '16964243;18669648;20068231'),
(2859, 1150, 1748, 'Phosphoserine', 'unknown', '18669648'),
(2860, 1150, 1750, 'Phosphoserine', 'unknown', '16964243;18669648;20068231'),
(2861, 1150, 1988, 'Phosphoserine', 'unknown', '20068231'),
(2862, 1150, 2512, 'Phosphoserine', 'unknown', '18669648'),
(2863, 1150, 2513, 'Phosphoserine', 'unknown', '18669648;20068231'),
(2864, 1150, 2875, 'N6-acetyllysine', 'unknown', '19608861'),
(2865, 1150, 2996, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(2866, 1150, 3007, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(2867, 1150, 3018, 'Phosphoserine', 'unknown', '20068231'),
(2868, 1150, 3045, 'Phosphothreonine', 'unknown', '20068231'),
(2869, 1150, 3048, 'Phosphoserine', 'unknown', '20068231'),
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(3180, 1262, 846, 'Phosphothreonine', 'CDK1', '-'),
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(3182, 1263, 37, 'Phosphoserine', 'unknown', '18669648;19690332;24275569'),
(3183, 1263, 249, 'Phosphoserine', 'CDK1', '1756735;18220336;18669648;19690332;21406692'),
(3184, 1263, 252, 'Phosphothreonine', 'CDK1', '1756735;18220336;18669648'),
(3185, 1263, 356, 'Phosphothreonine', 'unknown', '18220336'),
(3186, 1263, 373, 'Phosphothreonine', 'CDK1', '1756735;19690332'),
(3187, 1263, 567, 'Phosphoserine', 'CDK2', '10499802'),
(3188, 1263, 612, 'Phosphoserine', 'CHEK2;CHEK1', '17380128;18669648'),
(3189, 1263, 795, 'Phosphoserine', 'unknown', '-'),
(3190, 1263, 807, 'Phosphoserine', 'CDK1;CDK3', '15084261;1756735;18669648;19690332'),
(3191, 1263, 810, 'N6-methyllysine', 'SMYD2', '22787429'),
(3192, 1263, 811, 'Phosphoserine', 'CDK1;CDK3', '15084261;1756735;18669648'),
(3193, 1263, 821, 'Phosphothreonine', 'CDK6', '15809340;16360038;20068231'),
(3194, 1263, 823, 'Phosphothreonine', 'unknown', '18669648'),
(3195, 1263, 826, 'Phosphothreonine', 'CDK4', '15809340;16360038;18669648;20068231'),
(3196, 1263, 841, 'Phosphothreonine', 'unknown', '19690332'),
(3197, 1263, 860, 'N6-methyllysine', 'SMYD2', '20870719'),
(3198, 1263, 873, 'N6-acetyllysine', 'PCAF', '20940255'),
(3199, 1263, 874, 'N6-acetyllysine', 'PCAF', '20940255'),
(3200, 1264, 195, 'Phosphothreonine', 'unknown', '17081983;20068231'),
(3201, 1264, 229, 'Phosphothreonine', 'unknown', '17525332'),
(3202, 1265, 2, 'N-acetylalanine', 'unknown', '-'),
(3203, 1265, 3, 'N6-acetyllysine', 'unknown', '-'),
(3204, 1265, 1236, 'Phosphoserine', 'unknown', '19690332;20068231'),
(3205, 1265, 1292, 'Phosphothreonine', 'unknown', '19690332'),
(3206, 1265, 1336, 'Phosphoserine', 'unknown', '17081983;18669648;20068231;21406692'),
(3207, 1265, 1340, 'Phosphoserine', 'unknown', '17081983;18669648;20068231;21406692'),
(3208, 1265, 1342, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3209, 1265, 1344, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3210, 1265, 1358, 'Phosphoserine', 'unknown', '21406692'),
(3211, 1265, 1375, 'Phosphoserine', 'unknown', '18669648;19690332'),
(3212, 1265, 1400, 'Phosphoserine', 'unknown', '17081983;18220336;18669648;19690332;20068231;21406692;24275569'),
(3213, 1265, 1403, 'Phosphothreonine', 'unknown', '19690332'),
(3214, 1265, 1413, 'Phosphoserine', 'unknown', '17081983;18220336;18669648;19690332;20068231;21406692;24275569'),
(3215, 1265, 1421, 'Phosphotyrosine', 'unknown', '18669648'),
(3216, 1265, 1424, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3217, 1265, 1441, 'Phosphoserine', 'unknown', '20068231;21406692'),
(3218, 1265, 1452, 'Phosphoserine', 'unknown', '20068231'),
(3219, 1265, 1454, 'Phosphoserine', 'unknown', '17525332;20068231;21406692'),
(3220, 1265, 1461, 'Phosphoserine', 'unknown', '19690332'),
(3221, 1265, 1466, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3222, 1265, 1473, 'Phosphoserine', 'unknown', '19690332'),
(3223, 1265, 1476, 'Phosphoserine', 'unknown', '19690332;20068231'),
(3224, 1265, 1522, 'Phosphoserine', 'unknown', '19690332;20068231;21406692;24275569'),
(3225, 1265, 1524, 'Phosphoserine', 'unknown', '19690332;20068231;21406692;24275569'),
(3226, 1265, 1526, 'Phosphoserine', 'unknown', '19690332;20068231'),
(3227, 1265, 1550, 'Phosphoserine', 'unknown', '18669648;21406692;24275569'),
(3228, 1265, 1552, 'Phosphoserine', 'unknown', '18669648;24275569'),
(3229, 1265, 1575, 'Phosphothreonine', 'unknown', '19690332;24275569'),
(3230, 1265, 1576, 'Phosphoserine', 'unknown', '24275569'),
(3231, 1265, 1581, 'Phosphoserine', 'unknown', '18220336;18669648;19690332;21406692;24275569'),
(3232, 1265, 1592, 'Phosphothreonine', 'unknown', '18669648'),
(3233, 1265, 1596, 'Phosphoserine', 'unknown', '18669648'),
(3234, 1265, 1609, 'Phosphotyrosine', 'unknown', '18669648'),
(3235, 1265, 1613, 'Phosphoserine', 'unknown', '18669648;20068231;21406692'),
(3236, 1271, 72, 'Phosphothreonine', 'unknown', '17242355'),
(3237, 1271, 128, 'N6-acetyllysine', 'unknown', '23806337'),
(3238, 1271, 294, 'Phosphoserine', 'unknown', '-'),
(3239, 1271, 307, 'N6-acetyllysine', 'unknown', '-'),
(3240, 1271, 312, 'Phosphoserine', 'unknown', '-'),
(3241, 1271, 340, 'Phosphothreonine', 'unknown', '-'),
(3242, 1271, 369, 'Phosphothreonine', 'unknown', '-'),
(3243, 1271, 375, 'N6-acetyllysine', 'unknown', '23806337'),
(3244, 1271, 486, 'Phosphoserine', 'unknown', '17242355'),
(3245, 1271, 737, 'Phosphoserine', 'unknown', '19144319'),
(3246, 1275, 333, 'Phosphoserine', 'unknown', '18669648'),
(3247, 1275, 425, 'Phosphoserine', 'unknown', '18669648;20068231;21406692;24275569'),
(3248, 1275, 439, 'Phosphothreonine', 'unknown', '19690332'),
(3249, 1275, 445, 'Phosphoserine', 'unknown', '19690332;24275569'),
(3250, 1275, 463, 'Phosphothreonine', 'unknown', '24275569'),
(3251, 1275, 1338, 'Phosphoserine', 'unknown', '18669648'),
(3252, 1275, 1364, 'Phosphoserine', 'unknown', '24275569'),
(3253, 1275, 1392, 'Phosphoserine', 'unknown', '24275569'),
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(3255, 1277, 628, 'Phosphoserine', 'unknown', '19779198'),
(3256, 1279, 77, 'Phosphoserine', 'unknown', '19779198'),
(3257, 1279, 356, 'Phosphothreonine', 'unknown', '17330950;19779198'),
(3258, 1279, 380, 'Phosphoserine', 'unknown', '17330950;18407956;19779198'),
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(3260, 1280, 147, 'Phosphoserine', 'unknown', '-'),
(3261, 1280, 204, 'Phosphoserine', 'PLK1', '-'),
(3262, 1281, 32, 'O-AMP-tyrosine', 'Haemophilus IbpA', '19362538;20622875'),
(3263, 1281, 35, 'O-AMP-threonine', 'Vibrio VopS', '19039103'),
(3264, 1281, 64, 'Phosphotyrosine', 'SRC', '14506284'),
(3265, 1281, 188, 'Cysteine methyl ester', 'unknown', '-'),
(3266, 1282, 64, 'Phosphotyrosine', 'SRC', '-'),
(3267, 1282, 188, 'Cysteine methyl ester', 'unknown', '-'),
(3268, 1284, 22, 'Phosphoserine', 'unknown', '-'),
(3269, 1284, 25, 'Phosphoserine', 'unknown', '-'),
(3270, 1284, 52, 'Phosphoserine', 'unknown', '17242355;19144319'),
(3271, 1286, 316, 'N6-acetyllysine', 'autocatalysis', '-'),
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(3273, 1292, 14, 'Phosphoserine', 'unknown', '24275569'),
(3274, 1292, 638, 'Phosphoserine', 'unknown', '24275569'),
(3275, 1294, 437, 'Phosphoserine', 'PLK1', '-'),
(3276, 1295, 2, 'N-acetylserine', 'unknown', '22223895'),
(3277, 1295, 41, 'Phosphoserine', 'unknown', '18669648;20068231;21406692'),
(3278, 1295, 42, 'Phosphoserine', 'unknown', '18669648;20068231;21406692'),
(3279, 1296, 41, 'Phosphoserine', 'AURKB', '-'),
(3280, 1296, 57, 'Phosphoserine', 'unknown', '-'),
(3281, 1296, 61, 'Phosphoserine', 'unknown', '-'),
(3282, 1296, 112, 'Phosphoserine', 'unknown', '-'),
(3283, 1296, 138, 'Phosphoserine', 'unknown', '-'),
(3284, 1296, 567, 'Phosphoserine', 'unknown', '-'),
(3285, 1296, 579, 'Phosphoserine', 'unknown', '-'),
(3286, 1297, 2, 'N-acetylalanine', 'unknown', '19369195;19608861;22814378'),
(3287, 1297, 8, 'N6-acetyllysine', 'unknown', '19608861'),
(3288, 1301, 466, 'Phosphoserine', 'unknown', '18669648;19690332;21406692'),
(3289, 1301, 498, 'Phosphothreonine', 'unknown', '21406692'),
(3290, 1301, 502, 'Phosphoserine', 'unknown', '18669648;21406692'),
(3291, 1303, 250, 'Phosphoserine', 'unknown', '19779198'),
(3292, 1306, 320, 'N6-acetyllysine', 'autocatalysis', '-'),
(3293, 1308, 112, 'Phosphoserine', 'unknown', '14657031'),
(3294, 1308, 490, 'Phosphoserine', 'unknown', '14657031'),
(3295, 1308, 560, 'Phosphoserine', 'unknown', '14657031;18691976;20068231'),
(3296, 1308, 581, 'Phosphothreonine', 'unknown', '14657031;16964243;18691976;19690332;20068231'),
(3297, 1308, 595, 'Phosphoserine', 'unknown', '14657031'),
(3298, 1308, 599, 'Phosphothreonine', 'unknown', '14657031'),
(3299, 1310, 58, 'Phosphoserine', 'unknown', '-'),
(3300, 1310, 93, 'Phosphoserine', 'unknown', '-'),
(3301, 1310, 132, 'Phosphoserine', 'unknown', '-'),
(3302, 1312, 1326, 'Phosphoserine', 'unknown', '-'),
(3303, 1313, 1, 'N-acetylmethionine', 'unknown', '-'),
(3304, 1313, 4, 'Phosphotyrosine', 'PKR', '-'),
(3305, 1313, 6, 'N6-acetyllysine', 'unknown', '-'),
(3306, 1313, 9, 'N6-acetyllysine', 'unknown', '-'),
(3307, 1313, 14, 'Phosphothreonine', 'PKMYT1', '-'),
(3308, 1313, 15, 'Phosphotyrosine', 'PKMYT1; WEE1;WEE2; alternate', '-'),
(3309, 1313, 15, 'Phosphotyrosine', 'WEE1;WEE2; alternate', '-'),
(3310, 1313, 19, 'Phosphotyrosine', 'unknown', '-'),
(3311, 1313, 39, 'Phosphoserine', 'unknown', '-'),
(3312, 1313, 77, 'Phosphotyrosine', 'unknown', '-'),
(3313, 1313, 161, 'Phosphothreonine', 'CAK', '-'),
(3314, 1313, 178, 'Phosphoserine', 'unknown', '-'),
(3315, 1313, 222, 'Phosphothreonine', 'unknown', '-'),
(3316, 1313, 245, 'N6-succinyllysine', 'unknown', '-'),
(3317, 1313, 248, 'Phosphoserine', 'unknown', '-'),
(3318, 1314, 207, 'Phosphoserine', 'unknown', '-'),
(3319, 1314, 213, 'Phosphothreonine', 'unknown', '-'),
(3320, 1314, 398, 'Phosphoserine', 'unknown', '-'),
(3321, 1314, 405, 'Phosphoserine', 'unknown', '-'),
(3322, 1314, 408, 'Phosphothreonine', 'unknown', '-'),
(3323, 1314, 419, 'Phosphoserine', 'unknown', '-'),
(3324, 1314, 421, 'Phosphoserine', 'unknown', '-'),
(3325, 1314, 486, 'Phosphoserine', 'unknown', '-'),
(3326, 1314, 510, 'Phosphoserine', 'unknown', '-'),
(3327, 1314, 512, 'Phosphothreonine', 'unknown', '-'),
(3328, 1314, 513, 'Phosphothreonine', 'unknown', '-'),
(3329, 1314, 516, 'Phosphoserine', 'unknown', '-'),
(3330, 1315, 2, 'N-acetylserine', 'unknown', '22814378'),
(3331, 1315, 305, 'N6-acetyllysine', 'unknown', '-'),
(3332, 1315, 306, 'Phosphotyrosine', 'unknown', '-'),
(3333, 1315, 320, 'Phosphothreonine', 'unknown', '16732323;18088087;18669648;20068231'),
(3334, 1317, 1144, 'Phosphoserine', 'unknown', '18669648'),
(3335, 1318, 55, 'Phosphoserine', 'unknown', '-'),
(3336, 1326, 849, 'Phosphoserine', 'unknown', '15866179'),
(3337, 1326, 850, 'Phosphoserine', 'unknown', '15866179'),
(3338, 1329, 2, 'N-acetylserine', 'unknown', '19413330'),
(3339, 1329, 30, 'Phosphotyrosine', 'unknown', '-'),
(3340, 1329, 334, 'Phosphoserine', 'unknown', '17081983;20068231'),
(3341, 1329, 373, 'N6-acetyllysine', 'unknown', '-'),
(3342, 1329, 424, 'Phosphoserine', 'unknown', '18669648'),
(3343, 1329, 426, 'Phosphothreonine', 'unknown', '18669648;20068231'),
(3344, 1330, 3, 'Asymmetric dimethylarginine', 'PRMT6; alternate', '-'),
(3345, 1330, 3, 'Citrulline', 'unknown', '-'),
(3346, 1330, 4, 'Phosphothreonine', 'GSG2', '-'),
(3347, 1330, 5, 'Allysine', 'unknown', '-'),
(3348, 1330, 5, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(3349, 1330, 5, 'N6#N6-dimethyllysine', 'unknown', '-'),
(3350, 1330, 5, 'N6-acetyllysine', 'unknown', '-'),
(3351, 1330, 5, 'N6-methyllysine', 'unknown', '-'),
(3352, 1330, 7, 'Phosphothreonine', 'PKC', '-'),
(3353, 1330, 9, 'Citrulline', 'unknown', '-'),
(3354, 1330, 9, 'Symmetric dimethylarginine', 'PRMT5; alternate', '-'),
(3355, 1330, 10, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(3356, 1330, 10, 'N6#N6-dimethyllysine', 'unknown', '-'),
(3357, 1330, 10, 'N6-acetyllysine', 'unknown', '-'),
(3358, 1330, 10, 'N6-methyllysine', 'unknown', '-'),
(3359, 1330, 11, 'Phosphoserine', 'AURKB; AURKC; RPS6KA3; RPS6KA4;RPS6KA5', '-'),
(3360, 1330, 12, 'Phosphothreonine', 'PKC', '-'),
(3361, 1330, 15, 'N6-acetyllysine', 'unknown', '-'),
(3362, 1330, 18, 'Asymmetric dimethylarginine', 'CARM1; alternate', '-'),
(3363, 1330, 18, 'Citrulline', 'unknown', '-'),
(3364, 1330, 19, 'N6-acetyllysine', 'unknown', '19608861'),
(3365, 1330, 19, 'N6-methyllysine', 'unknown', '-'),
(3366, 1330, 24, 'N6-acetyllysine', 'unknown', '19608861'),
(3367, 1330, 24, 'N6-methyllysine', 'unknown', '-'),
(3368, 1330, 27, 'Citrulline', 'unknown', '-'),
(3369, 1330, 28, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(3370, 1330, 28, 'N6#N6-dimethyllysine', 'unknown', '-'),
(3371, 1330, 28, 'N6-acetyllysine', 'unknown', '-'),
(3372, 1330, 28, 'N6-methyllysine', 'unknown', '-'),
(3373, 1330, 29, 'Phosphoserine', 'AURKB; AURKC;RPS6KA5', '18691976'),
(3374, 1330, 37, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(3375, 1330, 37, 'N6#N6-dimethyllysine', 'unknown', '-'),
(3376, 1330, 37, 'N6-acetyllysine', 'unknown', '-'),
(3377, 1330, 37, 'N6-methyllysine', 'unknown', '-'),
(3378, 1330, 38, 'N6-methyllysine', 'unknown', '-'),
(3379, 1330, 42, 'Phosphotyrosine', 'unknown', '-'),
(3380, 1330, 57, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(3381, 1330, 57, 'N6-acetyllysine', 'unknown', '-'),
(3382, 1330, 57, 'N6-methyllysine', 'EHMT2; alternate', '-'),
(3383, 1330, 58, 'Phosphoserine', 'unknown', '20850016'),
(3384, 1330, 65, 'N6-methyllysine', 'unknown', '-'),
(3385, 1330, 80, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(3386, 1330, 80, 'N6#N6-dimethyllysine', 'unknown', '-'),
(3387, 1330, 80, 'N6-acetyllysine', 'unknown', '-'),
(3388, 1330, 80, 'N6-methyllysine', 'unknown', '-'),
(3389, 1330, 81, 'Phosphothreonine', 'unknown', '20850016'),
(3390, 1330, 87, 'Phosphoserine', 'unknown', '-'),
(3391, 1330, 108, 'Phosphothreonine', 'unknown', '-'),
(3392, 1330, 116, 'N6-acetyllysine', 'unknown', '-'),
(3393, 1330, 123, 'N6-acetyllysine', 'unknown', '-'),
(3394, 1330, 123, 'N6-methyllysine', 'unknown', '-'),
(3395, 1334, 98, 'Phosphoserine', 'unknown', '-'),
(3396, 1334, 99, 'Phosphoserine', 'unknown', '-'),
(3397, 1338, 11, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;24275569'),
(3398, 1338, 12, 'Phosphoserine', 'unknown', '18669648;20068231;24275569'),
(3399, 1338, 13, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692;24275569'),
(3400, 1338, 14, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692;24275569'),
(3401, 1338, 40, 'N6-acetyllysine', 'unknown', '-'),
(3402, 1338, 92, 'Phosphoserine', 'unknown', '18669648;18691976;19690332;20068231'),
(3403, 1338, 95, 'Phosphoserine', 'unknown', '21406692'),
(3404, 1338, 97, 'Phosphoserine', 'unknown', '19690332;20068231;21406692'),
(3405, 1339, 2, 'N-acetylserine', 'unknown', '-'),
(3406, 1339, 30, 'Phosphotyrosine', 'unknown', '-'),
(3407, 1339, 334, 'Phosphoserine', 'unknown', '-'),
(3408, 1339, 373, 'N6-acetyllysine', 'unknown', '-'),
(3409, 1339, 424, 'Phosphoserine', 'unknown', '-'),
(3410, 1339, 426, 'Phosphothreonine', 'unknown', '-'),
(3411, 1341, 2, 'N-acetylalanine', 'unknown', '-'),
(3412, 1341, 367, 'N6-acetyllysine', 'unknown', '-'),
(3413, 1344, 179, 'N6-acetyllysine', 'unknown', '19608861'),
(3414, 1344, 211, 'Phosphoserine', 'unknown', '18669648'),
(3415, 1345, 11, 'Phosphoserine', 'unknown', '-'),
(3416, 1346, 314, 'Phosphoserine', 'unknown', '17525332;19369195'),
(3417, 1346, 375, 'Phosphoserine', 'unknown', '19369195'),
(3418, 1346, 563, 'Phosphoserine', 'unknown', '19369195;19690332'),
(3419, 1346, 593, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(3420, 1346, 596, 'Phosphoserine', 'unknown', '18669648;18691976;19369195;19690332;20068231;21406692'),
(3421, 1346, 609, 'Phosphothreonine', 'CDK1', '16760428'),
(3422, 1346, 655, 'Phosphoserine', 'unknown', '18691976;19369195'),
(3423, 1347, 449, 'Phosphotyrosine', 'unknown', '-'),
(3424, 1347, 521, 'Phosphoserine', 'AMPK', '-'),
(3425, 1347, 524, 'Phosphoserine', 'AMPK', '-'),
(3426, 1348, 124, 'Phosphoserine', 'ial', '-'),
(3427, 1348, 125, 'Phosphoserine', 'ial', '-'),
(3428, 1348, 126, 'Phosphoserine', 'ial', '-'),
(3429, 1348, 331, 'Phosphothreonine', 'PLK1', '15621529'),
(3430, 1352, 96, 'Phosphoserine', 'unknown', '20068231'),
(3431, 1352, 130, 'Phosphothreonine', 'unknown', '20068231'),
(3432, 1352, 146, 'Phosphoserine', 'unknown', '19690332'),
(3433, 1352, 183, 'Phosphothreonine', 'unknown', '19690332'),
(3434, 1352, 189, 'Phosphoserine', 'unknown', '19690332'),
(3435, 1352, 225, 'Phosphoserine', 'unknown', '17081983;20068231;21406692'),
(3436, 1352, 261, 'Phosphoserine', 'unknown', '18669648'),
(3437, 1352, 316, 'Phosphoserine', 'unknown', '18669648'),
(3438, 1352, 439, 'Phosphoserine', 'unknown', '20068231;21406692'),
(3439, 1352, 538, 'Phosphoserine', 'unknown', '19690332;20068231'),
(3440, 1352, 709, 'Phosphoserine', 'unknown', '21406692'),
(3441, 1352, 710, 'Phosphoserine', 'unknown', '21406692'),
(3442, 1352, 734, 'Phosphothreonine', 'unknown', '20068231'),
(3443, 1352, 763, 'Phosphoserine', 'unknown', '19690332;20068231'),
(3444, 1352, 773, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(3445, 1354, 1, 'N-acetylmethionine', 'unknown', '-'),
(3446, 1357, 80, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3447, 1357, 116, 'Phosphoserine', 'unknown', '18669648'),
(3448, 1357, 216, 'Phosphoserine', 'unknown', '20068231'),
(3449, 1357, 229, 'Phosphoserine', 'unknown', '-'),
(3450, 1357, 321, 'N6-acetyllysine', 'unknown', '-'),
(3451, 1357, 423, 'Phosphoserine', 'unknown', '-'),
(3452, 1357, 426, 'Phosphoserine', 'unknown', '18669648;24275569'),
(3453, 1357, 449, 'N6-acetyllysine', 'unknown', '19608861'),
(3454, 1359, 66, 'Phosphoserine', 'unknown', '-'),
(3455, 1359, 321, 'Phosphoserine', 'unknown', '-'),
(3456, 1359, 342, 'Phosphoserine', 'unknown', '-'),
(3457, 1359, 946, 'Phosphoserine', 'GSK3-beta', '-'),
(3458, 1362, 2, 'N-acetylalanine', 'unknown', '19413330'),
(3459, 1363, 412, 'Phosphoserine', 'unknown', '18669648;19690332;20068231'),
(3460, 1363, 427, 'Phosphoserine', 'unknown', '18669648;19690332'),
(3461, 1363, 452, 'Phosphoserine', 'unknown', '17525332'),
(3462, 1363, 543, 'Phosphoserine', 'unknown', '20068231'),
(3463, 1363, 562, 'Phosphoserine', 'unknown', '20068231'),
(3464, 1363, 581, 'Phosphoserine', 'unknown', '20068231'),
(3465, 1364, 2, 'N-acetylserine', 'unknown', '-'),
(3466, 1364, 460, 'Phosphoserine', 'unknown', '-'),
(3467, 1364, 590, 'Phosphoserine', 'unknown', '15345747;17242355;18630941'),
(3468, 1364, 611, 'Phosphoserine', 'unknown', '-'),
(3469, 1364, 612, 'Phosphothreonine', 'unknown', '-'),
(3470, 1365, 2, 'N-acetylalanine', 'unknown', '-'),
(3471, 1366, 1, 'N-acetylmethionine', 'unknown', '-'),
(3472, 1366, 7, 'Phosphoserine', 'unknown', '-'),
(3473, 1366, 27, 'Phosphoserine', 'unknown', '-'),
(3474, 1366, 28, 'Phosphothreonine', 'unknown', '-'),
(3475, 1366, 40, 'Phosphoserine', 'unknown', '-'),
(3476, 1366, 44, 'Phosphoserine', 'unknown', '-'),
(3477, 1366, 49, 'Phosphoserine', 'unknown', '-'),
(3478, 1366, 479, 'Phosphoserine', 'unknown', '-'),
(3479, 1366, 786, 'N6-acetyllysine', 'unknown', '23806337'),
(3480, 1367, 674, 'Phosphoserine', 'unknown', '18691976'),
(3481, 1370, 186, 'Phosphothreonine', 'CDK1', '-'),
(3482, 1371, 34, 'Phosphoserine', 'unknown', '18669648;20068231'),
(3483, 1371, 119, 'Phosphoserine', 'unknown', '18669648'),
(3484, 1371, 152, 'Phosphoserine', 'unknown', '20068231'),
(3485, 1371, 155, 'Phosphoserine', 'unknown', '15144186;18669648;19690332;20068231;21406692'),
(3486, 1371, 265, 'Phosphothreonine', 'unknown', '20068231'),
(3487, 1371, 267, 'Phosphoserine', 'unknown', '20068231'),
(3488, 1371, 318, 'Phosphoserine', 'unknown', '19690332'),
(3489, 1371, 384, 'Phosphothreonine', 'unknown', '18669648'),
(3490, 1372, 2, 'N-acetylalanine', 'unknown', '-'),
(3491, 1376, 1123, 'Phosphoserine', 'unknown', '17242355;19131326');
INSERT INTO `ptms` (`PTMsID`, `PTMsProteinID`, `Position`, `PTMsPTMType`, `PTMsKinase`, `PubMeds`) VALUES
(3492, 1378, 70, 'N6#N6-dimethyllysine', 'unknown', '18438403'),
(3493, 1378, 127, 'Phosphoserine', 'unknown', '17081983;18669648;19690332;21406692'),
(3494, 1378, 133, 'Phosphoserine', 'unknown', '21406692'),
(3495, 1378, 142, 'N6-methyllysine', 'SETD7', '21151116'),
(3496, 1378, 143, 'Phosphoserine', 'PKB/AKT1', '18669648;21151116'),
(3497, 1378, 152, 'Phosphoserine', 'unknown', '18669648'),
(3498, 1378, 154, 'Phosphoserine', 'unknown', '18669648;21565170'),
(3499, 1378, 160, 'N6-acetyllysine', 'unknown', '21947282'),
(3500, 1378, 173, 'N6-acetyllysine', 'unknown', '19608861'),
(3501, 1378, 188, 'N6-acetyllysine', 'unknown', '21947282'),
(3502, 1378, 259, 'N6-acetyllysine', 'unknown', '21947282'),
(3503, 1378, 366, 'N6-acetyllysine', 'unknown', '21947282'),
(3504, 1378, 394, 'Phosphoserine', 'unknown', '18669648;20068231'),
(3505, 1378, 509, 'Phosphoserine', 'unknown', '-'),
(3506, 1378, 714, 'Phosphoserine', 'unknown', '17081983;20068231;21406692'),
(3507, 1378, 732, 'Phosphoserine', 'unknown', '18220336'),
(3508, 1378, 749, 'N6-acetyllysine', 'unknown', '21947282'),
(3509, 1378, 891, 'N6-acetyllysine', 'unknown', '21947282'),
(3510, 1378, 957, 'N6-acetyllysine', 'unknown', '21947282'),
(3511, 1378, 961, 'N6-acetyllysine', 'unknown', '21947282'),
(3512, 1378, 975, 'N6-acetyllysine', 'unknown', '21947282'),
(3513, 1378, 1054, 'N6-acetyllysine', 'unknown', '21947282'),
(3514, 1378, 1111, 'N6-acetyllysine', 'unknown', '19608861;21947282'),
(3515, 1378, 1113, 'N6-acetyllysine', 'unknown', '19608861;21947282'),
(3516, 1378, 1115, 'N6-acetyllysine', 'unknown', '19608861;21947282'),
(3517, 1378, 1117, 'N6-acetyllysine', 'EHMT2', '21947282'),
(3518, 1378, 1119, 'N6-acetyllysine', 'unknown', '-'),
(3519, 1378, 1121, 'N6-acetyllysine', 'unknown', '-'),
(3520, 1378, 1349, 'N6-acetyllysine', 'unknown', '21947282'),
(3521, 1378, 1415, 'N6-acetyllysine', 'unknown', '21947282'),
(3522, 1379, 183, 'Phosphoserine', 'unknown', '18257517'),
(3523, 1382, 110, 'Phosphoserine', 'unknown', '18669648'),
(3524, 1382, 135, 'Phosphoserine', 'unknown', '21406692'),
(3525, 1382, 172, 'Phosphoserine', 'unknown', '21406692'),
(3526, 1382, 299, 'Phosphoserine', 'unknown', '21406692'),
(3527, 1382, 653, 'Phosphothreonine', 'unknown', '18669648;20068231;21406692'),
(3528, 1382, 772, 'Phosphoserine', 'unknown', '21406692'),
(3529, 1382, 773, 'Phosphoserine', 'unknown', '21406692'),
(3530, 1382, 821, 'Phosphothreonine', 'unknown', '18669648'),
(3531, 1382, 824, 'Phosphoserine', 'unknown', '18669648'),
(3532, 1382, 860, 'Phosphoserine', 'unknown', '20068231'),
(3533, 1382, 1008, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3534, 1382, 1086, 'Phosphoserine', 'unknown', '18669648'),
(3535, 1382, 1087, 'Phosphothreonine', 'unknown', '18669648'),
(3536, 1382, 1089, 'Phosphothreonine', 'unknown', '18669648'),
(3537, 1382, 1104, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3538, 1382, 1116, 'Phosphoserine', 'unknown', '20068231;21406692'),
(3539, 1384, 431, 'Phosphoserine', 'PLK1', '22405274'),
(3540, 1385, 600, 'Phosphoserine', 'unknown', '18669648;19690332;21406692'),
(3541, 1385, 646, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3542, 1385, 649, 'Phosphoserine', 'unknown', '18669648'),
(3543, 1385, 656, 'Phosphothreonine', 'unknown', '18669648'),
(3544, 1385, 684, 'Phosphoserine', 'unknown', '21406692'),
(3545, 1385, 688, 'Phosphoserine', 'unknown', '18669648;19690332'),
(3546, 1385, 695, 'Phosphoserine', 'unknown', '18669648'),
(3547, 1385, 711, 'Phosphothreonine', 'unknown', '18669648'),
(3548, 1385, 714, 'Phosphoserine', 'unknown', '18669648'),
(3549, 1385, 797, 'Phosphoserine', 'unknown', '19690332'),
(3550, 1385, 1091, 'Phosphoserine', 'unknown', '18669648;19690332'),
(3551, 1385, 1099, 'Phosphothreonine', 'unknown', '18669648'),
(3552, 1385, 1196, 'Phosphoserine', 'unknown', '18088087'),
(3553, 1385, 1223, 'Phosphoserine', 'unknown', '20068231'),
(3554, 1391, 14, 'Phosphoserine', 'unknown', '-'),
(3555, 1391, 755, 'Phosphoserine', 'unknown', '-'),
(3556, 1391, 773, 'Phosphoserine', 'unknown', '-'),
(3557, 1391, 815, 'Phosphothreonine', 'unknown', '-'),
(3558, 1391, 989, 'Phosphoserine', 'unknown', '-'),
(3559, 1391, 1021, 'Phosphoserine', 'unknown', '-'),
(3560, 1391, 1055, 'Phosphothreonine', 'unknown', '-'),
(3561, 1391, 1061, 'Phosphoserine', 'unknown', '-'),
(3562, 1391, 1090, 'Phosphoserine', 'unknown', '-'),
(3563, 1391, 1173, 'Phosphoserine', 'unknown', '-'),
(3564, 1391, 1180, 'Phosphoserine', 'unknown', '-'),
(3565, 1392, 67, '(3S)-3-hydroxyasparagine', 'HIF1AN', '-'),
(3566, 1392, 100, '(3S)-3-hydroxyasparagine', 'HIF1AN', '-'),
(3567, 1392, 226, '(3S)-3-hydroxyasparagine', 'HIF1AN', '-'),
(3568, 1392, 299, 'Phosphoserine', 'unknown', '-'),
(3569, 1392, 422, 'Phosphoserine', 'unknown', '-'),
(3570, 1392, 432, 'Phosphoserine', 'unknown', '-'),
(3571, 1392, 443, 'Phosphothreonine', 'unknown', '8662509'),
(3572, 1392, 445, 'Phosphoserine', 'NUAK1', '17242355'),
(3573, 1392, 472, 'Phosphoserine', 'NUAK1', '-'),
(3574, 1392, 473, 'Phosphoserine', 'CDK1', '-'),
(3575, 1392, 477, 'Phosphoserine', 'unknown', '-'),
(3576, 1392, 507, 'Phosphoserine', 'unknown', '8662509'),
(3577, 1392, 601, 'Phosphoserine', 'unknown', '-'),
(3578, 1392, 666, 'Phosphoserine', 'unknown', '8662509'),
(3579, 1392, 690, 'Phosphoserine', 'PKA;PKG; in vitro', '-'),
(3580, 1392, 693, 'Phosphoserine', 'PKA;PKG; in vitro', '-'),
(3581, 1392, 694, 'Phosphothreonine', 'ROCK1; ROCK2; CDC42BP; ZIPK/DAPK3;RAF1', '8662509'),
(3582, 1392, 851, 'Phosphoserine', 'ROCK2', '-'),
(3583, 1392, 861, 'Phosphoserine', 'unknown', '-'),
(3584, 1392, 870, 'Phosphoserine', 'unknown', '8662509'),
(3585, 1392, 909, 'Phosphoserine', 'NUAK1', '8662509'),
(3586, 1392, 994, 'Phosphoserine', 'unknown', '-'),
(3587, 1395, 119, 'Phosphoserine', 'unknown', '18669648;20068231'),
(3588, 1395, 143, 'Phosphoserine', 'unknown', '20068231'),
(3589, 1395, 148, 'Phosphoserine', 'unknown', '18669648'),
(3590, 1395, 195, 'Phosphothreonine', 'unknown', '15316025'),
(3591, 1395, 197, 'Phosphoserine', 'unknown', '19690332'),
(3592, 1395, 199, 'Phosphothreonine', 'unknown', '19690332'),
(3593, 1395, 213, 'Phosphothreonine', 'unknown', '19690332'),
(3594, 1395, 214, 'Phosphoserine', 'unknown', '19690332'),
(3595, 1395, 239, 'Phosphothreonine', 'unknown', '18669648;18691976;19690332;20068231'),
(3596, 1395, 263, 'Phosphoserine', 'unknown', '17081983;18691976;19369195;20068231;21406692'),
(3597, 1395, 269, 'Phosphoserine', 'unknown', '18691976'),
(3598, 1395, 275, 'Phosphoserine', 'unknown', '17081983;18691976;20068231'),
(3599, 1395, 292, 'Phosphothreonine', 'unknown', '18669648;20068231'),
(3600, 1395, 296, 'Phosphoserine', 'unknown', '18669648'),
(3601, 1395, 306, 'Phosphoserine', 'unknown', '18669648;18691976;19690332;21406692'),
(3602, 1395, 312, 'Phosphoserine', 'unknown', '18669648;20068231'),
(3603, 1395, 314, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3604, 1395, 330, 'Phosphoserine', 'unknown', '20068231'),
(3605, 1395, 400, 'Phosphoserine', 'unknown', '18691976'),
(3606, 1395, 406, 'Phosphothreonine', 'unknown', '18691976'),
(3607, 1395, 446, 'Phosphoserine', 'unknown', '18669648'),
(3608, 1395, 476, 'Phosphoserine', 'unknown', '18691976'),
(3609, 1395, 510, 'Phosphoserine', 'unknown', '18669648'),
(3610, 1395, 514, 'Phosphoserine', 'unknown', '18669648'),
(3611, 1395, 828, 'Phosphoserine', 'unknown', '18669648;19369195;19690332;21406692'),
(3612, 1395, 831, 'Phosphoserine', 'unknown', '18669648;19690332'),
(3613, 1395, 832, 'Phosphothreonine', 'unknown', '18669648;19690332'),
(3614, 1395, 892, 'Phosphothreonine', 'AURKB', '12925766'),
(3615, 1395, 893, 'Phosphoserine', 'AURKB', '12925766'),
(3616, 1395, 894, 'Phosphoserine', 'AURKB', '12925766;18669648'),
(3617, 1395, 899, 'Phosphoserine', 'unknown', '18669648;18691976;19369195;19690332;20068231'),
(3618, 1395, 914, 'Phosphoserine', 'unknown', '18669648'),
(3619, 1396, 2, 'N-acetylalanine', 'unknown', '-'),
(3620, 1398, 70, 'Phosphoserine', 'unknown', '18407956;19779198'),
(3621, 1399, 442, 'Phosphoserine', 'unknown', '18257517'),
(3622, 1399, 446, 'Phosphothreonine', 'unknown', '18257517'),
(3623, 1399, 1443, 'Phosphoserine', 'unknown', '18257517'),
(3624, 1402, 5, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(3625, 1402, 5, 'N6#N6-dimethyllysine', 'unknown', '-'),
(3626, 1402, 5, 'N6-methyllysine', 'unknown', '-'),
(3627, 1402, 11, 'Phosphoserine', 'unknown', '-'),
(3628, 1402, 63, 'N6-acetyllysine', 'unknown', '-'),
(3629, 1402, 63, 'N6-methyllysine', 'unknown', '-'),
(3630, 1402, 75, 'N6#N6#N6-trimethyllysine', 'unknown', '-'),
(3631, 1402, 75, 'N6#N6-dimethyllysine', 'unknown', '-'),
(3632, 1402, 75, 'N6-methyllysine', 'unknown', '-'),
(3633, 1403, 2, 'N-acetylalanine', 'unknown', '-'),
(3634, 1404, 205, 'Phosphothreonine', 'unknown', '14657031;18669648'),
(3635, 1404, 209, 'Phosphothreonine', 'unknown', '14657031'),
(3636, 1404, 244, 'Phosphothreonine', 'unknown', '14657031'),
(3637, 1404, 291, 'Phosphoserine', 'unknown', '14657031'),
(3638, 1404, 313, 'Phosphothreonine', 'unknown', '14657031'),
(3639, 1404, 339, 'Phosphoserine', 'unknown', '18669648'),
(3640, 1404, 366, 'Phosphothreonine', 'unknown', '19690332'),
(3641, 1404, 386, 'Phosphoserine', 'unknown', '20068231'),
(3642, 1404, 426, 'Phosphoserine', 'unknown', '14657031;18669648'),
(3643, 1404, 430, 'Phosphothreonine', 'unknown', '14657031'),
(3644, 1404, 435, 'Phosphoserine', 'unknown', '14657031'),
(3645, 1404, 438, 'Phosphoserine', 'unknown', '18669648'),
(3646, 1404, 446, 'Phosphothreonine', 'unknown', '14657031;18669648'),
(3647, 1404, 821, 'Phosphoserine', 'unknown', '22139841'),
(3648, 1405, 661, 'Phosphoserine', 'unknown', '20068231'),
(3649, 1405, 1379, 'Phosphoserine', 'unknown', '18669648'),
(3650, 1405, 1381, 'Phosphoserine', 'MARK2', '20194617'),
(3651, 1405, 1382, 'Phosphoserine', 'unknown', '18669648'),
(3652, 1405, 1410, 'Phosphoserine', 'MARK2', '19690332;20194617;24275569'),
(3653, 1405, 1432, 'Phosphoserine', 'unknown', '18669648'),
(3654, 1405, 1438, 'Phosphoserine', 'unknown', '18669648'),
(3655, 1405, 1537, 'Phosphoserine', 'unknown', '24275569'),
(3656, 1405, 1545, 'Phosphothreonine', 'unknown', '24275569'),
(3657, 1405, 1559, 'Phosphoserine', 'unknown', '24275569'),
(3658, 1405, 1644, 'Phosphoserine', 'unknown', '18088087'),
(3659, 1405, 1797, 'Phosphoserine', 'unknown', '24275569'),
(3660, 1415, 524, 'Phosphoserine', 'unknown', '-'),
(3661, 1415, 603, 'N6-acetyllysine', 'unknown', '-'),
(3662, 1415, 608, 'Phosphoserine', 'unknown', '-'),
(3663, 1415, 612, 'Phosphoserine', 'unknown', '-'),
(3664, 1415, 618, 'Phosphoserine', 'unknown', '-'),
(3665, 1415, 623, 'Phosphoserine', 'unknown', '-'),
(3666, 1415, 625, 'Phosphoserine', 'unknown', '-'),
(3667, 1415, 653, 'Phosphoserine', 'unknown', '19144319'),
(3668, 1415, 670, 'Phosphothreonine', 'unknown', '19144319'),
(3669, 1415, 673, 'Phosphoserine', 'unknown', '-'),
(3670, 1415, 681, 'Phosphoserine', 'unknown', '-'),
(3671, 1415, 839, 'Phosphoserine', 'unknown', '-'),
(3672, 1415, 888, 'Phosphoserine', 'unknown', '17242355;19144319'),
(3673, 1415, 934, 'Phosphoserine', 'unknown', '-'),
(3674, 1415, 1027, 'Phosphoserine', 'unknown', '17242355'),
(3675, 1415, 1042, 'Phosphoserine', 'unknown', '-'),
(3676, 1415, 1059, 'Phosphoserine', 'unknown', '-'),
(3677, 1415, 1069, 'Phosphothreonine', 'unknown', '-'),
(3678, 1416, 2, 'N-acetylserine', 'unknown', '22814378'),
(3679, 1416, 43, 'Phosphothreonine', 'unknown', '18407956'),
(3680, 1416, 113, 'Phosphoserine', 'unknown', '18407956'),
(3681, 1417, 41, 'Phosphoserine', 'unknown', '17330950;18407956;19779198'),
(3682, 1417, 45, 'Phosphoserine', 'unknown', '17330950;19779198'),
(3683, 1417, 53, 'Phosphoserine', 'unknown', '19779198'),
(3684, 1417, 59, 'Phosphoserine', 'unknown', '18407956'),
(3685, 1417, 101, 'Phosphoserine', 'unknown', '18407956'),
(3686, 1419, 64, 'Phosphotyrosine', 'SRC', '-'),
(3687, 1419, 188, 'Cysteine methyl ester', 'unknown', '-'),
(3688, 1420, 116, 'Phosphoserine', 'CDK1', '-'),
(3689, 1420, 118, 'Phosphoserine', 'unknown', '-'),
(3690, 1420, 123, 'Phosphoserine', 'PLK1', '-'),
(3691, 1420, 137, 'Phosphoserine', 'unknown', '-'),
(3692, 1420, 311, 'Phosphothreonine', 'unknown', '-'),
(3693, 1425, 2, 'N-acetylserine', 'unknown', '-'),
(3694, 1425, 1057, 'Phosphoserine', 'unknown', '-'),
(3695, 1425, 1454, 'Phosphoserine', 'unknown', '18630941'),
(3696, 1425, 1487, 'Phosphoserine', 'unknown', '17242355'),
(3697, 1425, 1573, 'Phosphoserine', 'unknown', '-'),
(3698, 1425, 1603, 'Phosphoserine', 'unknown', '-'),
(3699, 1425, 1610, 'Phosphoserine', 'unknown', '-'),
(3700, 1425, 1613, 'Phosphoserine', 'unknown', '-'),
(3701, 1426, 2, 'N-acetylalanine', 'unknown', '19413330;22223895'),
(3702, 1426, 21, 'Phosphoserine', 'unknown', '17081983;18669648;18691976;19690332;20068231;21406692'),
(3703, 1426, 451, 'Phosphoserine', 'unknown', '20068231;21406692'),
(3704, 1426, 453, 'Phosphoserine', 'unknown', '20068231;21406692'),
(3705, 1426, 455, 'Phosphoserine', 'unknown', '21406692'),
(3706, 1426, 485, 'Phosphoserine', 'unknown', '18669648;19690332;20068231;21406692'),
(3707, 1426, 494, 'Phosphoserine', 'unknown', '16964243;18669648;19690332;20068231;21406692;24275569'),
(3708, 1426, 513, 'Phosphoserine', 'unknown', '17081983;19369195;20068231;21406692'),
(3709, 1427, 369, 'Leucine methyl ester', 'unknown', '11060018'),
(3710, 1428, 2, 'Phosphoserine', 'unknown', '18407956'),
(3711, 1428, 277, 'Phosphoserine', 'unknown', '19779198'),
(3712, 1428, 813, 'Phosphoserine', 'unknown', '17330950;19779198'),
(3713, 1429, 26, 'Phosphoserine', 'unknown', '-'),
(3714, 1429, 118, 'Phosphoserine', 'unknown', '-'),
(3715, 1429, 134, 'Phosphoserine', 'unknown', '-'),
(3716, 1429, 140, 'Phosphothreonine', 'unknown', '-'),
(3717, 1429, 155, 'Phosphoserine', 'unknown', '-'),
(3718, 1429, 156, 'Phosphoserine', 'unknown', '-'),
(3719, 1429, 200, 'Phosphoserine', 'IPL1', '-'),
(3720, 1429, 216, 'Phosphoserine', 'unknown', '-'),
(3721, 1429, 250, 'Phosphoserine', 'CDC28', '-'),
(3722, 1432, 72, 'Phosphothreonine', 'PLK1', '-'),
(3723, 1432, 104, 'Phosphothreonine', 'unknown', '-'),
(3724, 1432, 105, 'Phosphoserine', 'unknown', '-'),
(3725, 1432, 130, 'Phosphoserine', 'unknown', '-'),
(3726, 1432, 133, 'Phosphoserine', 'unknown', '-'),
(3727, 1432, 135, 'Phosphoserine', 'unknown', '-'),
(3728, 1432, 187, 'Phosphoserine', 'unknown', '-'),
(3729, 1434, 38, 'Phosphoserine', 'unknown', '19779198'),
(3730, 1434, 43, 'Phosphothreonine', 'unknown', '17330950;18407956;19779198'),
(3731, 1434, 377, 'Leucine methyl ester', 'unknown', '11060018;11697862'),
(3732, 1435, 566, 'Phosphoserine', 'unknown', '18407956'),
(3733, 1435, 706, 'Phosphotyrosine', 'unknown', '19779198'),
(3734, 1436, 874, 'Phosphoserine', 'unknown', '-'),
(3735, 1436, 875, 'Phosphoserine', 'unknown', '-'),
(3736, 1437, 1, 'N-acetylmethionine', 'unknown', '-'),
(3737, 1440, 41, 'Phosphoserine', 'unknown', '-'),
(3738, 1440, 51, 'Phosphoserine', 'unknown', '-'),
(3739, 1440, 287, 'Phosphothreonine', 'unknown', '-'),
(3740, 1440, 288, 'Phosphothreonine', 'unknown', '-'),
(3741, 1440, 342, 'Phosphoserine', 'PKA;PAK', '-'),
(3742, 1441, 36, 'N6-(ADP-ribosyl)lysine', 'unknown', '18436469'),
(3743, 1441, 36, 'N6-acetyllysine', 'unknown', '18436469'),
(3744, 1441, 37, 'N6-(ADP-ribosyl)lysine', 'unknown', '18436469'),
(3745, 1441, 37, 'N6-acetyllysine', 'unknown', '18436469'),
(3746, 1441, 208, 'Phosphoserine', 'unknown', '-'),
(3747, 1443, 90, 'Phosphotyrosine', 'LCK', '-'),
(3748, 1443, 219, 'Phosphothreonine', 'autocatalysis', '-'),
(3749, 1443, 348, 'Phosphoserine', 'unknown', '-'),
(3750, 1443, 538, 'Phosphothreonine', 'PDPK1', '-'),
(3751, 1443, 676, 'Phosphoserine', 'autocatalysis', '-'),
(3752, 1443, 685, 'Phosphoserine', 'unknown', '-'),
(3753, 1443, 695, 'Phosphoserine', 'autocatalysis', '-'),
(3754, 1446, 2, 'N-acetylserine', 'unknown', '22814378'),
(3755, 1446, 157, 'Phosphoserine', 'unknown', '17287358'),
(3756, 1447, 2, 'N-acetylalanine', 'unknown', '22814378'),
(3757, 1449, 279, 'N6-acetyllysine', 'autocatalysis', '-'),
(3758, 1450, 17, 'Phosphotyrosine', 'unknown', '-'),
(3759, 1450, 190, 'N6-acetyllysine', 'unknown', '-'),
(3760, 1450, 218, 'Phosphoserine', 'unknown', '-'),
(3761, 1451, 2, 'N-acetylalanine', 'unknown', '12665801;19413330'),
(3762, 1451, 367, 'N6-acetyllysine', 'unknown', '19608861'),
(3763, 1452, 11, 'Phosphoserine', 'unknown', '-'),
(3764, 1452, 12, 'Phosphoserine', 'unknown', '-'),
(3765, 1452, 13, 'Phosphoserine', 'unknown', '-'),
(3766, 1452, 14, 'Phosphoserine', 'unknown', '-'),
(3767, 1452, 40, 'N6-acetyllysine', 'unknown', '-'),
(3768, 1452, 92, 'Phosphoserine', 'unknown', '-'),
(3769, 1452, 95, 'Phosphoserine', 'unknown', '-'),
(3770, 1452, 97, 'Phosphoserine', 'unknown', '-'),
(3771, 1453, 114, 'N6-acetyllysine', 'unknown', '-'),
(3772, 1453, 222, 'N6-acetyllysine', 'unknown', '-'),
(3773, 1453, 677, 'N6-acetyllysine', 'unknown', '-'),
(3774, 1453, 1158, 'N6-acetyllysine', 'unknown', '-'),
(3775, 1453, 1160, 'N6-acetyllysine', 'unknown', '23806337'),
(3776, 1454, 21, 'Phosphoserine', 'unknown', '-'),
(3777, 1454, 27, 'Phosphoserine', 'unknown', '-'),
(3778, 1454, 40, 'Phosphoserine', 'unknown', '-'),
(3779, 1454, 141, 'Phosphoserine', 'unknown', '-'),
(3780, 1454, 379, 'N6-acetyllysine', 'unknown', '23806337'),
(3781, 1454, 677, 'N6-acetyllysine', 'unknown', '-'),
(3782, 1456, 575, 'Phosphoserine', 'unknown', '18407956'),
(3783, 1458, 502, 'Phosphothreonine', 'unknown', '18407956'),
(3784, 1459, 407, 'Phosphoserine', 'unknown', '-'),
(3785, 1459, 422, 'Phosphoserine', 'unknown', '-'),
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--
-- Constraints for dumped tables
--

--
-- Constraints for table `disorderprediction`
--
ALTER TABLE `disorderprediction`
  ADD CONSTRAINT `DisorderPredictionDisorderPredictorID` FOREIGN KEY (`DisorderPredictionDisorderPredictorID`) REFERENCES `disorderpredictor` (`DisorderPredictorID`),
  ADD CONSTRAINT `DisorderPredictionProteinID` FOREIGN KEY (`DisorderPredictionProteinID`) REFERENCES `protein` (`ProteinID`);

--
-- Constraints for table `interaction`
--
ALTER TABLE `interaction`
  ADD CONSTRAINT `InteractionProteinID` FOREIGN KEY (`InteractionProteinID`) REFERENCES `protein` (`ProteinID`);

--
-- Constraints for table `mutation`
--
ALTER TABLE `mutation`
  ADD CONSTRAINT `mut_proteinID` FOREIGN KEY (`mut_proteinID`) REFERENCES `protein` (`ProteinID`);

--
-- Constraints for table `pathway`
--
ALTER TABLE `pathway`
  ADD CONSTRAINT `path_proteinID` FOREIGN KEY (`path_proteinID`) REFERENCES `protein` (`ProteinID`);

--
-- Constraints for table `pdb`
--
ALTER TABLE `pdb`
  ADD CONSTRAINT `PDBProteinID` FOREIGN KEY (`PDBProteinID`) REFERENCES `protein` (`ProteinID`);

--
-- Constraints for table `pfam`
--
ALTER TABLE `pfam`
  ADD CONSTRAINT `PfamProteinID` FOREIGN KEY (`PfamProteinID`) REFERENCES `protein` (`ProteinID`);

--
-- Constraints for table `ptms`
--
ALTER TABLE `ptms`
  ADD CONSTRAINT `PTMsProteinID` FOREIGN KEY (`PTMsProteinID`) REFERENCES `protein` (`ProteinID`);

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/*!40101 SET CHARACTER_SET_RESULTS=@OLD_CHARACTER_SET_RESULTS */;
/*!40101 SET COLLATION_CONNECTION=@OLD_COLLATION_CONNECTION */;
