-- Table structure for table `protein`
--

CREATE TABLE IF NOT EXISTS `protein` (
  `ProteinID` bigint(20) NOT NULL AUTO_INCREMENT,
  `UniprotID` varchar(45) NOT NULL,
  `Name` longtext NOT NULL,
  `Evidence` longtext NOT NULL,
  `MolecularWeight` double NOT NULL,
  `Function` longtext,
  `Sequence` longtext NOT NULL,
  `Length` bigint(20) NOT NULL,
  `altUniprotACC` longtext NOT NULL,
  `DBid` varchar(7) NOT NULL,
  `Organism` longtext NOT NULL,
  `Gene` longtext,
  `allNames` longtext,
  `BioModel` longtext NOT NULL,
  `1000Gene` longtext NOT NULL,
  `GeneAnnotation` longtext NOT NULL,
  PRIMARY KEY (`ProteinID`)
) ENGINE=InnoDB  DEFAULT CHARSET=latin1 AUTO_INCREMENT=1555 ;

--
-- Dumping data for table `protein`
--

INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(1, 'Q8C263', 'Spindle and kinetochore-associated protein 3', 'GO:0000940', 45370, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it mediates the microtubule-stimulated oligomerization (By similarity). {ECO:0000250}.', 'MNPIQSFHCKLRGLATTLDSETARLLRALDGEDSDFEDSPGRILHDLHSEVQTLKDNVNALLDEARLENQESTRFKKATKILMEKNSADVRKLREFFQKYGYQARDKEDSGCEHRVNNSTPELAVCKDIQKAGVKELSDPCVPSGSVSEEPLRSPQLSDFGLQRYIISQVPANPPQTAASLKEERVAETPPAKDPSVQVLKTPRCALRMDDFECETPKLEHFGISEHTMCLNEDYTMGLKNMKNIKSSLLSGVSGEAIGTGPVTSDNSFAIPGPIIQQMEENDVEYVSSPLPPKFCTPGLKIPSTMDRTDLVSIDYPLSKPNSSSTDLEIKDCVPLILNSDECYQSFAEPPSSAITSCENFATPSPPKVTAIPEDILQMITKHSSNLASPLDVKVMPRRKGTRGAANKENW', 411, 'Q8C263; Q149T5; Q149T6;', 'KD00001', 'Mus musculus (Mouse)', 'Ska3', '#Spindle and kinetochore-associated protein 3', '-', '-', '219114'),
(2, 'Q8R480', 'Nuclear pore complex protein Nup85', 'GO:0000777', 74776, 'Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP98/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2- activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl- inositol 3-kinase-Rac-lammellipodium protrusion cascade.', 'MEELDCEPAVTWIPGVNSKKKQMCFDWGPGEMLLCETSFNQTGKSEKVPSCPFIYIIRKDVDVYSQILRKLFNESHGIFVGLQKIEEELSGKSRKAQLVRVSKNYRSVIRACMEEMHQVAIAAKDPASGRQFSSQVSILSAMELIWNLCEILFIEVAPAGPLLLHLLDWVRLHVCEVDSLSADVLGGDNPSKHENFWDLVTVLVLQGRLDEARQMLAKEADANPSCAGMCRVLGDLMRTMPILSPGNTQTLTELELKWQHWREECERHLQDNTFAANPRLESLCKIMLGDEAALLEQKELLSNWYHFLVTRLLYSNPTVKPIDLHFYAQSSLDMFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCRLLQSHNLYFGSNMREFLLLEYASGLFAHHSLWQLGVDYFDYCPELGRVSLELHIERIPLNTEQKALKVLRICEQRQMTEQVKSICKILAMKAVRNNRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGSAMMLSDRLTFLGKYREFHRLYGEKRFGDAASLLLSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELMRCLEDLASGRPECGEPDAQRLQDDDIETTKVEMLRLALARNLARAIIREGSLEGS', 656, 'Q8R480; A2A9W9; A2A9X0; Q9CYI9;', 'KD00002', 'Mus musculus (Mouse)', 'Nup85', '#Nuclear pore complex protein Nup85#85 kDa nucleoporin#FROUNT#Nucleoporin Nup85#Pericentrin-1', '-', '-', '445007'),
(3, 'Q90828', 'Cytoplasmic dynein 1 light intermediate chain 1', 'GO:0000776===GO:0003777===GO:0005868', 55893, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes (By similarity). {ECO:0000250}.', 'MAAVGRAGSFGSSSASGAANNASAELRAGGEEDDGQNLWSCILSEVSTRSRSKLPSGKSVLLLGEDGAGKTSLIGKIQGIEEYKKGRGMEYLYLNVHDEDRDDQTRCNVRILDGDLYHKGLLKFAMEANSLKDTLIMLVVDMSRPWTAMDSLQKWASVVREHIDKLKIPPEEMKEMEQKLVRDFQEYVEPGEDFPASPQRRNTSLQEDKDDSVILPLGADTLTCNLGIPVVVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRRFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPFNVPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKAEDSFEDSIRKPPVRKFVHEKEIVAEDDQVFLMKQQSQLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVTSNVASVTPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGGVGGSPGGGSAGGTGSNLPPSAKKSGQKPVLTDVQAELDRISRKPEMVSPTSPTSPTEGEAS', 515, 'Q90828;', 'KD00003', 'Gallus gallus (Chicken)', 'DYNC1LI1', '#Cytoplasmic dynein 1 light intermediate chain 1#Dynein light chain A#DLC-A#Dynein light intermediate chain 1; cytosolic#LIC57/59', '-', '-', '420668'),
(4, 'Q4FZB7', 'Histone-lysine N-methyltransferase SUV420H1', 'GO:0000780', 99187, 'Histone methyltransferase that specifically trimethylates ''Lys-20'' of histone H4. H4 ''Lys-20'' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions; thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1; RBL1 and RBL2) (By similarity). Plays a role in myogenesis by regulating the expression of target genes; such as EID3. {ECO:0000250; ECO:0000269|PubMed:23720823}.', 'MKWLGESKIMVVNGRRNGGKLSNDHQQNQSKLQHTGKDTLKAGKNAVERRSNRCNGNSGFEGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHFSKSDSFSHNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKEHVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNRLKKLGDSSKNSDSQSVSSNTDADTTQEKNNATSNRKSSVGVKKNSKSRTLTRQSMSRIPASSNSTSSKLTHINNSRVPKKLKKPAKPLLSKIKLRNHCKRLEQKNASRKLEMGNLVLKEPKVVLYKNLPIKKDKEPEGPAQAAVASGCLTRHAAREHRQNPVRGAHSQGESSPCTYITRRSVRTRTNLKEASDIKLEPNTLNGYKSSVTEPCPDSGEQLQPAPVLQEEELAHETAQKGEAKCHKSDTGMSKKKSRQGKLVKQFAKIEESTPVHDSPGKDDAVPDLMGPHSDQGEHSGTVGVPVSYTDCAPSPVGCSVVTSDSFKTKDSFRTAKSKKKRRITRYDAQLILENNSGIPKLTLRRRHDSSSKTNDQENDGMNSSKISIKLSKDHDNDNNLYVAKLNNGFNSGSGSSSTKLKIQLKRDEENRGSYTEGLHENGVCCSDPLSLLESRMEVDDYSQYEEESTDDSSSSEGDEEEDDYDDDFEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA', 885, 'Q4FZB7; B7WNX7; Q3SX56; Q4V775; Q6P150; Q96E44; Q9BUL0; Q9H022;Q9H2K3; Q9NXV3; Q9Y393;', 'KD00004', 'Homo sapiens (Human)', 'SUV420H1', '#Histone-lysine N-methyltransferase SUV420H1#2.1.1.43#Lysine N-methyltransferase 5B#Suppressor of variegation 4-20 homolog 1#Su(var)4-20 homolog 1#Suv4-20h1', '-', 'ENSG00000110066', '-'),
(5, 'Q07832', 'Serine/threonine-protein kinase PLK1', 'GO:0000776===GO:0000942===SCL', 68301, 'Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle; including the regulation of centrosome maturation and spindle assembly; the removal of cohesins from chromosome arms; the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors; and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA; BUB1B/BUBR1; CCNB1; CDC25C; CEP55; ECT2; ERCC6L; FBXO5/EMI1; FOXM1; KIF20A/MKLP2; CENPU; NEDD1; NINL; NPM1; NUDC; PKMYT1/MYT1; KIZ; PPP1R12A/MYPT1; PRC1; RACGAP1/CYK4; SGOL1; STAG2/SA2; TEX14; TOPORS; p73/TP73; TPT1 and WEE1. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ; NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome; an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55; ECT2; KIF20A/MKLP2; CENPU; PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1; thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1; CDC25C; FOXM1; CENPU; PKMYT1/MYT1; PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1; a key mitotic transcription regulator; leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1; FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGOL1: required for spindle pole localization of isoform 3 of SGOL1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1; a negative regulator of the APC/C complex during prophase; leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS; leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73; leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA; and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis.Phosphorylates MISP; leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning (By similarity). Together with MEIKIN; acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (PubMed:25533956). {ECO:0000250|UniProtKB:P53350; ECO:0000269|PubMed:22405274; ECO:0000269|PubMed:25533956}.', 'MNAAAKAGKLARAPADLGKGGVPGDAVPGAPVAAPLAKEIPEVLVDPRSRRQYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQKEKMSMEISIHRSLAHQHVVGFHDFFEDSDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNQVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYEGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTIHELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSSRKPLKVLNKGVENPLPDRPREKEEPVVRETNEAIECHLSDLLQQLTSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLNYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGTVQINFFQDHTKLILCPLMAAVTYINEKRDFQTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS', 603, 'Q07832;', 'KD00005', 'Mus musculus (Mouse)', 'Plk1', '#Serine/threonine-protein kinase PLK1#2.7.11.21#Polo-like kinase 1#PLK-1#Serine/threonine-protein kinase 13#STPK13', '-', '-', '18817'),
(6, 'Q62871', 'Cytoplasmic dynein 1 intermediate chain 2', 'GO:0005868', 71178, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. Involved in membrane-transport; such as Golgi apparatus; late endosomes and lysosomes. {ECO:0000269|PubMed:11340075}.', 'MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAAVSVQEESDLEKKRREAEALLQSMGLTTDSPIVFSEHWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSALQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVTAQPKEDEEEEDDVAAPKPPVEPEEEKILKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEEAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWSTKNNKPLYSFEDNSDYVYDVIGSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINASRADAEEEAATRIPA', 638, 'Q62871; Q62872; Q62873;', 'KD00006', 'Rattus norvegicus (Rat)', 'Dync1i2', '#Cytoplasmic dynein 1 intermediate chain 2#Cytoplasmic dynein intermediate chain 2#Dynein intermediate chain 2; cytosolic#DH IC-2', '-', '-', '-'),
(7, 'Q2V0Z5', 'Kinetochore proteinMinichromosome instability 12-like protein', 'k', 27126, '', 'MEGSKSEAVFDSMNLNPQIFINEAINSVEDYVDQAFDFYARDASKSLKIKGSDKQKSQALSNGIARVRGLLLSVIDNRLKLWESYSLRFCFAVPDGFVLPKSEESSSVHQDGLYDLELDAELDSLRDKLNVVGKRSVELDSELQALERSSVSRERSLRLVNEALELYDESSMDEIFKEMTKMASELRASVERLKTRRMKASESAKVKRLKNHGKEFSAMTFDGKLEDLEKFQAELRKM', 238, 'Q2V0Z5;', 'KD00007', 'Arabidopsis thaliana (Mouse-ear cress)', 'AtMIS12', '#Kinetochore protein {ECO:0000313|EMBL:BAE66672.1}#Minichromosome instability 12-like protein {ECO:0000313|EMBL:AED93975.1}', '-', '-', '833516'),
(8, 'Q3KR99', 'Protein Spindly', 'GO:0043515===GO:0034501===GO:0000940', 69112, 'Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. {ECO:0000255|HAMAP-Rule:MF_03041}.', 'MEADITNLRNKLKECEDERLKAAQYGLQLLERQTELQSQLDKCHEEMMTTAENYNQEKYALQREVELKSRMLESLSCECEALRQQQKAQLEQLEMQLHRSHRQEVHGLRNKLENLKVELDEARLSEKQLKQKLDHQGELLSHKSEELRLLSEQRALSSVSSELLSLQTELTEAEGVKNALREEVNELQCKQEQLECLNASLLHQVDRLKEEKEEREKEAVSYYNALEKARVENQDLQVQLGHALQQAADPNSKGNSLFAEVEDRRVAMERRLNLMKDKYQSLKKQNAFTRDQMNKMKLQISTLLRMRGSQTEFEQQERLFAMLEQKNGEIKHLLGEINKLEKFKNLYENMESKSSTSDSACALEDSTYYTDLLQLKLDKLNKENESTKGELSIQRMKALFESQRTLDIERKLFANERHLQLSESENLKLRAKLDELKLKYEPEERIEVPVLKRRREVLPLNINTPEETAAASATGEDVSRLPLERKEESCLDNLKDNTVQWKQPASLSPHKSLPLDTQPKKEKCVTLVASPASTEVLHEQSGNTPSSPRLTEESRLPTKVKERKEATSKLEKGASKKSHTIMYVSSKSTPEMQCPQQ', 597, 'Q3KR99;', 'KD00008', 'Rattus norvegicus (Rat)', 'Spdl1', '#Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041}#Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041}#Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041}', '-', '-', '303037'),
(9, 'Q569M3', 'Histone H3-like centromeric protein A', 'GO:0000777===SCL===k', 17343, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. {ECO:0000269|PubMed:15964249}.', 'MRPGSTPPSRRKSRPPRRVSPPLPTTSRTSPRRPHAQQQRRASRASPKKRFRPGTRALMEIRKYQKSTELLIRKAPFSRLVREVCMTYACGMNYNWQSMALMALQEASEAFLVRLFEDSYLCSLHAKRVTLYVQDIQLARRIRGVNEGLG', 150, 'Q569M3;', 'KD00009', 'Xenopus laevis (African clawed frog)', 'cenpa', '#Histone H3-like centromeric protein A#Centromere protein A#CENP-A', '-', '-', '735079'),
(10, 'Q4WHG1', 'Histone acetyltransferase esa1', 'GO:0034508', 55969, 'Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4; H3; H2B; H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac; H4K8ac; H4K12ac and H4K16ac; histone H3 to form H3K14ac; histone H2B to form H2BK16ac; and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me. {ECO:0000250|UniProtKB:Q08649}.', 'MLLLMFALLQDGELRKAEILSIRQRKDGPSFYVHYVDFNKRLDEWIDASRLDLSHEVEWPQPEKPEKKKTGVGNKAPSKNAQKRARADSRDVSATPDLLTGKNVNVGKAQRPSKAGGKENRDGTPLSMPIVTAEAISTDGTPKAESDDVEMVDVSFTDGKSIKEEERALGLMSREEEIERLRTSGSMTQNPTEIHRVRNLNRLQMGKYDIEPWYFSPYPASFSDADIIYIDEFCLSYFDDKRAFERHRTKCTLVHPPGNEIYRDDYISFFEVDGRRQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMCTRDETGCHLVGYFSKEKDSAEGYNLACILTLPQYQRRGFGRLLISFSYELSKREGKLGSPEKPLSDLGLLGYRQYWRETLVEILMEPGRETVSENELALLTSMTEKDVHETLVVLNMLRYYKGNWVIVLTDYVVEQHKKRLEKEKLKGARKIDPARLQWKPPVFTASSRTWNW', 483, 'Q4WHG1;', 'KD00010', 'Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSA1100) (Aspergillus fumigatus)', 'esa1', '#Histone acetyltransferase esa1#2.3.1.48 {ECO:0000250|UniProtKB:Q08649}', '-', '-', '3506677'),
(11, 'Q54CI8', 'Cytoplasmic dynein 1 light intermediate chain 1', 'GO:0003777===GO:0005868', 56713, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes (By similarity). {ECO:0000250}.', 'MVEQQQQEEDIWGQILRESSNKNNYFEKRDVAILGDPTSGKSLLLSKFDTVSNVESLKSIALSYTFSDIYEDDTSEDPVGRINYWSLEGEASQNDLLKFSLNKENIKNCMVIITLDFSQPWNLVESLKKWLGILEEHIKSIFKDDKNGFKNLQDKLSIKWHEYEEPTTTAATTTTTTTSNNIENNTNKTSPTTDKIQTNNVQKKKKKKVNISSAEDASVLPPLSENILINNLGVPILVACCKSDSVVMLEKDFDYKDELFDYIQQYLRRICLQYGAGLIYTSARKEINCGVTLEYIENILFGFELKSKTQLIEKDQIFVPAGWDTLAKIQVDFENQKVCKDTDEPYENIVKKPSIIKRREQTQTNSIICDDDQDFLGKIKSQLDNDDQSSINSPSTPSPLSQSSNNNNSNNNINNTSTPSINTPLQPTDKPLSDIKSSNNPVAASPSAERAALANFFTSLISKDKTSSRKDLKSSLASPPTTSVSSNAREDAKKELDKLKQQKK', 504, 'Q54CI8;', 'KD00011', 'Dictyostelium discoideum (Slime mold)', 'dync1li1', '#Cytoplasmic dynein 1 light intermediate chain 1#Dynein light intermediate chain 1; cytosolic', '-', '-', '8628947'),
(12, 'P52590', 'Nuclear pore complex protein Nup107', 'GO:0000777', 107209, 'Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Required for the assembly of peripheral proteins into the NPC. May anchor NUP62 to the NPC (By similarity). {ECO:0000250}.', 'MDRSGFGGMSSPVIRDPEVTRTARKHSAHKRVLIQANQDENFGTTTPRSQIIPRTPSSFRQPFTPPSRSLLRHPDISYIFGTEGRSPRHIQSSGYLGNLSMVTNLDDSNWAAAFSSQRLGFYTNTEHHSMTEDINLSTVMLREDDPGEAASMSMFSDFLQSFLKHSSTTVFDLVEEYENICASQVNILSKIVSRATRWDWQKFSKTASMLWLLQQEMVTWRLLASLYRDRIQSSLEEENMFAIAGINASEKTVVEALFQRDSLVRQSQLVVDWLESIAKDEIGDFSDNIEFYAKSVYWENTLHSLKQRQLLSYIGSTRPLVTELDPDAPIRQKMPLDDLDREDEVRLLKYLFTLIRAGMTEEAQRLCKRCGQAWRAATLEGWKLHHDPNVNGGTELEPVEGNPYRRIWKISCWRMAEDELFNKYERAIYAALSGNLKQLLPVCDTWEDTVWAYFRVMVDSLVEQEIRTSVMTLDETEELPREYMEANWTLEKVFEELQATDKKRVLEENQEHYHVVQKFLILGDIDGLMDEFSKWLSKSRSSLPGHLLRFMTHLILFFRTLGLQTKEEVSIEVLKTYIQLLINEKHTNLIAFYTCHLPQDLAVAQYALFLEGVTECEQRHQCLELAKEADLDVATITKTVVENIRKKDNGEFSHHDLAPSLDTATTEEDRLKIDVIDWLVFDPAQRAEALRQGNAIMRKFLALKKHEAAKEVFVKIPQDSIAEIYNQWEEQGMESPLPAEDDNAIREHLCIRAYLEAHETFNERFKHMNSAPQKPTLLSQATFTEKVAHEHKEKKYEMDHNIWKGHLDALTADVKEKMYNVLLFVDGGWMVDVREDAEEDPERAHQMVLLRKLCLPMLCFLLHTILHSTGQYQECLQLADMVSSERHKLYLVFSKEELRKLLQKLRESSLMLLDQGLDPLGYEIQS', 926, 'P52590;', 'KD00012', 'Rattus norvegicus (Rat)', 'Nup107', '#Nuclear pore complex protein Nup107#107 kDa nucleoporin#Nucleoporin Nup107#p105', '-', '-', '-'),
(13, 'Q4R5P6', 'Cytoplasmic dynein 1 light intermediate chain 2', 'GO:0003777===GO:0005868', 54072, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes (By similarity). {ECO:0000250}.', 'MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKSILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEEGCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSSPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPGAGGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA', 492, 'Q4R5P6;', 'KD00013', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'DYNC1LI2', '#Cytoplasmic dynein 1 light intermediate chain 2#Dynein light intermediate chain 2; cytosolic', '-', '-', '-'),
(14, 'Q8NK13', 'E3 ubiquitin ligase complex SCF subunit scon-3', 'GO:0051382===GO:0031518', 19910, 'Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes; which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression; probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}.', 'MAENDERALQKVSLQSNDGQIITVDRVVAERSLLIKNLIEDLGDEAVMNEAIPLPNVNEPVLRKVVEWCEHHRKDPPQTTEDENDSRKKSTEIDEWDQKFMQVDQEMLFEIILAANYMDIKPLLDVGCKTVANMIKGKSPEEIRKTFNITNDFTPEEEEQIRRENEWAEDR', 171, 'Q8NK13; U9W3K7;', 'KD00014', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'scon-3', '#E3 ubiquitin ligase complex SCF subunit scon-3#Sulfur control protein 3#Sulfur metabolite repression control scon-3', '-', '-', '3875176'),
(15, 'Q8J1G4', 'Kinesin-like protein KIP1', 'GO:0003777', 127690, 'Required for assembly of the mitotic spindle. Interact with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly; CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediate by KAR3 (By similarity). {ECO:0000250}.', 'MLEQAEKLMKRNSSGAMSAPQSKPLARSRSSTMPTTTQKRVRSSQQSEGEPEYNIKVYVRCRSRNEREIREKSSVVISTLGNNGREVILTNPGTGSNKTYTFDRVFGVESDQESMFNQVARAYINEMIEGYNCTVFAYGQTGTGKTYTMSGDITMMGSSEDDPNFVLLSEHAGIIPRVLVELFRELREVSEDYSVKVSFLELYNEKLRDLLVDDKDVSLEDHNFNGMAPPESIRIYDSLKTDRTSPNGYSIFVKGMEEMYIRSAQEGLKLLMDGSLKRKVAATKCNDLSSRSHTIFTITTNVTKIHPISGEQYVKVGKLNLVDLAGSENINRSGAENKRAQEAGLINKSLLTLGRVINALVDHSQHIPYRESKLTRLLQDSLGGKTKTCIIATISPAKISMEETVSTLEYATRAKSIKNTPQVNQLMAKESCIIEYIQEIERLRKELRASHSKEGIYITQEKFETYESNSILVEEQQAKIDNLQEQLRRLKEKFLEQTKLIKEKDGQIKELDVANRKYLEQSKDLTIYINGIHSKLEDYEHTMIGIHNNNMKLLEDINDNRGNIHEDLLAKVDHIETCNLIISREITSLISIRNVLQAYSDRFKTVLGGVFEELQEKLTQVGRTTEESQLDVDLSFVDEKFEEVTDIIKATCENLVRTMDEHVSNMKLETTDLTSSCASLLEKECQALHGKLQKYVESMKQELNSTLQEMVRDLDMKASSMLNVVQCTKDGLISHKKELEADLESQKREHFDIAQTMEEQLQKIVGKERQNIQESMKASYDFLMKQMVETELRQKNFEESIVSKVKGLLSHSNNGMSKMSSYAVGRLYDSAIGGVNSIENTVSSATFSMKNDLQEFQMDISPICDSRRFGDEFTAVETRISEAIREELTPKLQDITSKACNLIGLGVQDINQKALGVSDDQRRELRSVINNTNNHADRLRSEIGTLVNYVSQEHRDNIMQISQTQDEILQEQIASIGRTFDVLGNINKPDANVRTSVPIEHELNSAINELPPLYMPQRPLSLCSHGRQLLDEAYSGNENLSPSTGKFSNFPTPCGDMSAQTPTTPMPVPDQPLTKMPVPQTISSLRSLRRLTMDICEHSADMTLGSIHESQKAMDSSRRYTLEPRLFEK', 1129, 'Q8J1G4;', 'KD00015', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'KIP1', '#Kinesin-like protein KIP1', '-', '-', '4619762'),
(16, 'Q6CNF3', 'Probable kinetochore protein NDC80', 'GO:0000777', 78517, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MDELRDIRTTGPEDVLNSVDPYRYTSQIPNGKSNNGLNAKMNGNNTLTNMINRSIAKNMGQNASSGSMRRSMRQSLRNSLPRSSIGPQQQQQMNSTQNSTYHNTARDPRPLRDKNFQNLLQQEIFSYLTDQKFDVETNHPISLKSLKQPTQKDFIYMFKWLYLRLDPGYVFTKSLEHEVYSILRTIHYPYLATINKSQISAVGGSNWPKFVGMLHWLVIINKKLDECLEHLDVSINNQVTQDITVLNQPLKTAEEQEKKQEKYELMVERLFIDYITESYKSFLRLEDDYEPYLHDLELSFQRFVHIIETDIAQLTSTTEHLSVECESIVAKNYELKNIKEKNTGLEQEYKRLSHGVQITQAKSKEWPDKLKEIEDEIDKKKRDIRQVSLQIDELTSVLKRKNISGEEIEHKNKESDSISKSLDTVSSRLDQFTGLVRQQRLETESVYKNLQDTLKQYKSATEGLVIARKNLGDHIDESSIELVLPSDLMSEEMIGLTVEELIGDKKSFTDPIKKNLNKIAEDIKMRITNIQTENSKLQIKLEDLRNEITTKNEDLDQLEQQLSSIKSEYEEYRQESQSQLLSQNIKIEKLERKIQNARVESQQKISSIEREAEETRLKLEELKLLQNRERLELHNKVIQLIEYVSNFKINTQSSIEELQNATQKELQRLQTEV', 673, 'Q6CNF3;', 'KD00016', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '2894656'),
(17, 'Q5XI51', 'Kinesin-like protein KIF2B', 'GO:0000777===GO:0003777', 75004, 'Plus end-directed microtubule-dependent motor required for spindle assembly and chromosome movement. Has microtubule depolymerization activity (By similarity). {ECO:0000250|UniProtKB:Q8N4N8}.', 'MASQFCLPLAPRLSPLKPLKSHFTDFQVGICVAIQRSDKRIHLAVVTEINRENSWVTVEWVEKGVKKGKKIELETVLLLNPALASTEHQRSRRPLRPVSVIPATAIGDQRTATKWIAMIPHRNETPSGDSQTLVIPSNPCLMKRKKSPCLREIEKLQKQREKRRRLQLEIRARRALDINTGNPNFETMRMIEEYRRHLDSSKMSRLEPPEDHRICVCVRKRPLNERETTMKDLDIITIPSHNVVMVHESKQKVDLTRYLENQTFCFDHAFDDTASNELVYQFTARPLVESIFRKGMATCFAYGQTGSGKTHTMGGAFSGKAQECSKGIYALVAQDVFLLLRTPAYEKLELKVYGTFFEIYGGKVYDLLNWKKKLQVLEDGNQQIQVVGLQEQEVGCVEEVLNLVELGNSCRTSGQTSVNAHSSRSHAVFQLILKCGGKLHGKFSLVDLAGNERGADTAKATRKRQLEGAEINKSLLALKECIRALGKNKSHTPFRASKLTQVLRDSFIGQNSYTCMIATISPGMTSCENTLNTLRYANRVKELALEARPYPPTDHEMPLTLENGNTNSEKSLQKDDIIQIPTVQKEEEKESDELTSTKEPAASWSRSGPWWEAIQETAEGVNCDVDFCIAQSLSILEQKIGVLTEIQKKLQLLRDDLQKKSQAE', 664, 'Q5XI51;', 'KD00017', 'Rattus norvegicus (Rat)', 'Kif2b', '#Kinesin-like protein KIF2B', '-', '-', '287624'),
(18, 'Q86ZC1', 'Kinesin heavy chain', 'GO:0003777', 98369, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Its motor activity is directed toward the microtubule''s plus end.', 'MSNSIKVVCRFRPQNRIENEQGAQPVVKFEADDTCALDSNGAAGSFTFDRVFGMSSRQKDIFDFSIKPTVDDILNGYNGTVFAYGQTGAGKSYTMMGTNLDNDDGRGVIPRIVEQIFASILSSPGTIEYTVRVSYMEIYMERIRDLLQPQNDNLPIHEEKNRGVYVKGLLEVYVSSVQEVYEVLKRGGDARVVASTNMNAESSRSHSIFVITITQKNVETGSAKSGQLFLVDLAGSEKVGKTGASGQTLEEAKKINKSLSALGMVINNLTDGKSSHIPYRDSKLTRILQESLGGNSRTTLIINCSPSSYNAEETLSTLRFGMRAKAIKNKAKVNAELSPAELKALLRKAQSQVTTFETYVSTLEGEVQLWRKGESVPKEQWAPPLAGVSGAKAAAAQTPRPSTPSRLATESRAETPVAERSATPGIPIDKDEREEFLRRENELQDQITEKETQIAAAEKTLRDTKEELTYLKERDTKVNKDNEKLTSEANEFKMQLERLAFESKEAQITMDSLKEANAELTAELDELKQQLLNVKMSAKESTAALDEKEKRKAEKMAQMMAGFDLGGDVFSENEATIKKVIDHIDSLHEQSSAGEAIPPDEFEELKAKLVETQGIVRQAELSMFGSSSNDANVKRREELEQRLQVLEQEYEDLLERNLGEGDVAEIKERLEKAYSNNQDIKVELVEDLKKEVAQKSAEIEKFKAVNEDLQQRVKSGSASNGTAPGSASGKTVQQQIAEFDVMKKSLMRDLQNRCERVVELEISLDETREQYNNVLRSSNNRAQQKKMAFLERNLEQLTHVQRQLVEQNGSLKKEVAIAERKLIARNERIQSLESLLQDSQEKLTTASHRYGFPLYFRIDFNHTSIALLTFPLDSKPNCQQ', 880, 'Q86ZC1;', 'KD00018', 'Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)', 'klp1', '#Kinesin heavy chain', '-', '-', '-'),
(19, 'Q8J1G7', 'Kinesin-like protein CIN8', 'GO:0005828===GO:0000778', 106848, 'Required for assembly of the mitotic spindle. Interact with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly; CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediated by KAR3 (By similarity). {ECO:0000250}.', 'MPDHEVQTRKSRMLDDAQEELNITVAVRCRGRNEREIKAKSSVVVTVPDVTGSNEVSINTTDEVGIAAKMNSRTYTVDKVFGPSADQSLIFKEIAEPLFDDFMKGYNCTVLVYGMTSTGKTYTMTGDEKLYDGQLSDSAGIIPRIMFKLFDALEATDSDFLVKCSYIELYNEELKDLLDESHDSSKRLRIFDSSSMNHSSRASSQSNSPREPEVAHNGFSRRRQRPPPVKANRMSATKQQLSESGSGIYVQNVQEFHIINAREGINVLQKGLKHRQVASTKMNDFSSRSHTIFTIMLYKNCDGELFRVSKMNLVDLAGSENISRSGAQNQRAKEAGSINQSLLTLGRVINSLADKSIHIPFRESKLTRLLQDSLGGNTKTALIATISPAKINADETSSTLEYAAKAKNIKNRPQLGALMMKDILVKNISSELAKIKSDFLSTKSKDGIYMSHEHYQEIVNDLENCQTEIQESKRQIESLTSQNNLLLKDKKASQEVTELQNSKIKKLQSTIEYLYDKIERQHHNETELATTIHKLKEALHTMQGSLKSYETHELRLQNDIKEVLYQGITSYRESMNQHLEKVKVSMLDKNLSIKENINNITTIFDDTLKSVEANGSDMCDTLVKLIKETPSMYLKEFNETVSSLKSELSSYSNALTNKLTEISEENNHLREYLDQHLFKNSTQEVLDLRMESVYQKVKNDSDQLLSKLVSMVGAHVEESRTLMVNSMKDTVNEIIDNERSLFQPIRDRWIASCDNINQCDASHQNFEAKSTSGLDKLKELSDASLKSSEDAVNKAKHRTDSFHDFVQKLCCDQSLKKQMHDISDKHRMLEDHFDDNVKYFKESSKGFEDMDCSIKKIIHEMSPEVGDIKSVETLMERINARTFSPVRPTGKTPSRQVLKNAITSKASSRSMSPIKTLDTNVRIISPVKRGTIEFGAEGPPTKKVR', 945, 'Q8J1G7;', 'KD00019', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'CIN8', '#Kinesin-like protein CIN8', '-', '-', '4619538'),
(20, 'P40236', 'Casein kinase I homolog hhp2', 'GO:0051455===GO:0033551', 45832, 'Involved in DNA repair. May regulate the activity of protein(s) involved in double strand break repair caused by gamma rays.', 'MTVVDIKIGNKYRIGRKIGSGSFGQIYLGLNTVNGEQVAVKLEPLKARHHQLEYEFRVYNILKGNIGIPTIRWFGVTNSYNAMVMDLLGPSLEDLFCYCGRKFTLKTVLLLADQLISRIEYVHSKSFLHRDIKPDNFLMKKHSNVVTMIDFGLAKKYRDFKTHVHIPYRDNKNLTGTARYASINTHIGIEQSRRDDLESLGYVLLYFCRGSLPWQGLQADTKEQKYQRIRDTKIGTPLEVLCKGLPEEFITYMCYTRQLSFTEKPNYAYLRKLFRDLLIRKGYQYDYVFDWMILKYQKRAAAAAAASATAPPQVTSPMVSQTQPVNPITPNYSSIPLPAERNPKTPQSFSTNIVQCASPSPLPLSFRSPVPNKDYEYIPSSLQPQYSAQLRRVLDEEPAP', 400, 'P40236;', 'KD00020', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hhp2', '#Casein kinase I homolog hhp2#2.7.11.1', '-', '-', '2541929'),
(21, 'P40235', 'Casein kinase I homolog hhp1', 'GO:0051455===GO:0033551', 42450, 'Involved in DNA repair. Has a probable role in repairing alkylated DNA and may regulate the activity of protein(s) involved in double strand break repair caused by gamma rays.', 'MALDLRIGNKYRIGRKIGSGSFGDIYLGTNVVSGEEVAIKLESTRAKHPQLEYEYRVYRILSGGVGIPFVRWFGVECDYNAMVMDLLGPSLEDLFNFCNRKFSLKTVLLLADQLISRIEFIHSKSFLHRDIKPDNFLMGIGKRGNQVNIIDFGLAKKYRDHKTHLHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLVYFCRGSLPWQGLKATTKKQKYEKIMEKKISTPTEVLCRGFPQEFSIYLNYTRSLRFDDKPDYAYLRKLFRDLFCRQSYEFDYMFDWTLKRKTQQDQQHQQQLQQQLSATPQAINPPPERSSFRNYQKQNFDEKGGDINTTVPVINDPSATGAQYINRPN', 365, 'P40235;', 'KD00021', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'hhp1', '#Casein kinase I homolog hhp1#2.7.11.1', '-', '-', '2540718'),
(22, 'Q91YJ2', 'Sorting nexin-4', 'GO:0005868', 51778, 'May be involved in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation (By similarity). {ECO:0000250}.', 'MEQAPPDPEKLLQPGPLEPLGGPGAVLEAAVGEENEGTREDGSGVDTMTGNNFWLKKIEISVSEAEKRTGRNAVNMQETYTAYLIETRSVEHADGQSVLTDSLWRRYSEFELLRNYLLVYYPHVVVPPLPEKRAEFVWHKLSADNMDPDFVERRRVGLENFLLRVASHPVLCRDKIFYSFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFTELRHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRKHELMQYDLETAAQDLAAKKQQCEELATGTVRTFSLKGMTTKLFGQETPEQREARIKVLEEQINEGEQQLKSKNLEGREFVKNAWADIERFKEQKNRDLKEALISYAVMQISMCKKGIQVWTNAKECFSKM', 450, 'Q91YJ2;', 'KD00022', 'Mus musculus (Mouse)', 'Snx4', '#Sorting nexin-4', '-', '-', '69150'),
(23, 'Q13352', 'Centromere protein R', 'GO:0000777===k', 20194, 'Transcription coregulator that can have both coactivator and corepressor functions. Isoform 1; but not other isoforms; is involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast; it does not coactivate nuclear receptors for retinoic acid; vitamin D; progesterone receptor; nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF- kappa-B subunit; possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells; but not in other cancer cells; via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A- associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:11713274; ECO:0000269|PubMed:12244126; ECO:0000269|PubMed:15082778; ECO:0000269|PubMed:15254226; ECO:0000269|PubMed:16622420}.', 'MPVKRSLKLDGLLEENSFDPSKITRKKSVITYSPTTGTCQMSLFASPTSSEEQKHRNGLSNEKRKKLNHPSLTESKESTTKDNDEFMMLLSKVEKLSEEIMEIMQNLSSIQALEGSRELENLIGISCASHFLKREMQKTKELMTKVNKQKLFEKSTGLPHKASRHLDSYEFLKAILN', 177, 'Q13352; B2R7D8; Q13353; Q5RJ42; Q5RJ44; Q5RJ45; Q7KYX2; Q96CD5;Q9UKB6;', 'KD00023', 'Homo sapiens (Human)', 'ITGB3BP', '#Centromere protein R#CENP-R#Beta-3-endonexin#Integrin beta-3-binding protein#Nuclear receptor-interacting factor 3', '-', 'ENSG00000142856', '-'),
(24, 'P47037', 'Structural maintenance of chromosomes protein 3', 'k', 141336, '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.', 'MYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLIHQGSGGSVMSASVEIVFHDPDHSMILPSGVLSRGDDEVTIRRTVGLKKDDYQLNDRNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALTNAKDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDRELNEVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYARFKSKDERDTWIHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMSRSLANGIINVKEITEKLKISPESVFGTLGELIKVNDKYKTCAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLSLDSDVKFPSNTTTQIQFTPLIKKIKYEPRFEKAVKHVFGKTIVVKDLGQGLKLAKKHKLNAITLDGDRADKRGVLTGGYLDQHKRTRLESLKNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFENDLLQEFDSELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELESKLIPQENDLESKMSEVGDAFIFGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEETNNKKLLEKANNQQRLLLKKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIGLLPEDALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLVPRGTAKLIIHRKNDNANDHDESIDVDMDAESNESQNGKDSEIMYTGVSISVSFNSKQNEQLHVEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFRVKYENKISTVIEVNREEAIGFIRGSNKFAEV', 1230, 'P47037; D6VWA9;', 'KD00024', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SMC3', '#Structural maintenance of chromosomes protein 3#DA-box protein SMC3', '-', '-', '853371'),
(25, 'F9W301', 'Kinesin-1-like protein PSS1', 'GO:0003777', 52130, 'Kinesin-like motor protein that exhibits microtubule- stimulated ATPase activity. Plays an essential role in male meiotic chromosomal dynamics; male gametogenesis and anther dehiscence. May play a minor and nonessential role in regulating meiotic spindle formation. {ECO:0000269|PubMed:21282525}.', 'MSNVTVCVRFRPLSHKERKTNGDKVCFKRLDSESFVFKDEREEDVIFSFDRVFYEDAEQSDVYNFLAVPIVADAISGINGTIITYGQTGAGKTYSMEGPSILHCNKQKTGLVQRVVDELFQSLQSSESMAMWSVKLSMVEIYLEKVRDLLDLSKDNLQIKESKTQGIYISGATEVSIQNSSDALECLSEGIANRAVGETQMNLASSRSHCLYIFSVQQGSTSDERVRGGKIILVDLAGSEKVEKTGAEGRVLDEAKTINKSLSVLGNVVNALTTGKPNHVPYRDSKLTRILQDALGGNSRAALLCCCSPSASNAPESLSTVRFGTRTKLIKTTPKSISPEVDSIKKPIPDSHGQNDLRDRILNKLRLSLKEEDVDLLEELFVQEGIIFDPNYSVADIDSACQDAASQEVSLLTQAVEELKETVEELTDENERLRGELELAQEAAAAAAAARADGALLGFVPAVAISSLLRPFGFVPD', 477, 'F9W301; B9FYS2; Q0J8E3; Q69UI4;', 'KD00025', 'Oryza sativa subsp. japonica (Rice)', 'PSS1', '#Kinesin-1-like protein PSS1 {ECO:0000303|PubMed:21282525; ECO:0000312|EMBL:DAA34941.1}#Pollen semi-sterility protein 1 {ECO:0000303|PubMed:21282525}', '-', '-', '4344521'),
(26, 'Q95R61', 'SD04909p', 'k;m', 35147, '', 'MRVEAFENAANAQNSMRPKRGKDLQGTPGSNNTPKIGKLPAPTVGRFFTPTQTTSTLPLSSAQPKKGPASASKATSLLKTATGTNLRSVNSTSTKTLSRENSGDDFRKGLHNLAEERKKLREQKHQQAAQQREAKERERAERMAKLAAERAKKQEERKRIEERKRQELEELQRKMRQQEEAEALKKAKHKELEQQKLQQLTGAKPKKMLPPPPKTKYTWEMLHEDDSTDDEGKVTHKRPPAPTWSRSHVRGEAIAMQSHCPTDIIDSFFSVAPTTPDLKQIFPNIDPSQLKRNSSVLWSTPPRYSELPKY', 310, 'Q95R61;', 'KD00026', 'Drosophila melanogaster (Fruit fly)', 'Incenp', '#SD04909p {ECO:0000313|EMBL:AAL29146.1}', '-', '-', '-'),
(27, 'Q9JJ79', 'Cytoplasmic dynein 2 heavy chain 1', 'GO:0003777', 492218, 'May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis. May play a role in transport between endoplasmic reticulum and Golgi or organization of the Golgi in cells (By similarity). {ECO:0000250}.', 'MAGSLSDVRKLFLFTTTQNYFGLRPELWDQTPLSNCPEVNNFLDDGNQMLLRVQRSDAGLAFSNTIDFDDTKDKVLVFFKLRPEVITDGNLHTNILVSSMLESPINSLYQAVRQVFAPMLLKDQEWSRNFDPKLQNLLSELEAGLGVVLRKSDTNLPKLKLKEDDTRGILTPSDEFQFWIEQAHRGSKQISKERASYFKELFETIAREFYNLDSLSLLEVVDLVETTRDVVDDVWRQAEHDHYPESRMLHLLDVIGGSFGRFVQKKLGSLKLWEDPYYLVKENLKAGISICEQWVIVCSHLTGQVWQRYVPHPWKSEKYFPETLDRLGKRLEEVLAIRTIHEKLLYFLPASEERIVCLSRVFEPFTGVNPVQYNPYTEPLWKAAVSQYEKIIAPAEQKIAGKLKNYISEIQDSPQQLLQAFLKYKELVKRPTISKELMLERETLLARLGDSAKDFRLDFENRCRGIPGDASGPLSGKNLSEVVNNIVWVRQLELKVDDTIKIAEALLSDLSGFRSFHRSAEDLLDQFKLYEQEQFDDWSREVQSGLSDSRSGLCIEANSRIMELDPNDGALKVHYSDRLVILLREVRQLSALGFVIPAKIQQVANVAQKFCKQAIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNSKAGSGGKSQITWDNPKELEGYIQKLQNAAERLATENRRLRKWHITFCEKVVILMNIDLLRQQQRWKDGLQELRTGLASVAAQGFQPSDMRAWRQHWNHQLYKALEHQYQMGLEALNENLPEINVDLTYKQGRLQFRPPFEEIRAKYYREMKRFIGIPNQFKGVGGAGDESIFSVMIDRNASGFLTIYSKAEDLFRRLSAVLHQHKEWVVIGQVDMEALVEKNLSTVHDWEKNFKALKIKGKEVERLPSAVKVDCLNINCSPVKTVIDDLIQKLFDLLVLSLKKSIQTHIHEIDTFVTEAMKVLTVIPQSVEEIGDTNLQYSNLQDRRPEILPLFQEAEDKNRLLRTVAGGGVETVSNLRAKWDKFELMMESHQLMIKDQIEVMKGNVKSRLQIYYQELDKFKARWDQLKPGDDIIETGQQNTMDQSAKSIKEKKIEFDDLEVIRKKLVDDCHHFGLEESNFSLAYSISKDIESCAQIWALYEEFQQGLQEMAKEDWITYRTKIYIFEEFLINWHERLRKVEEHSVMTVKLQSEVDRYKIIIPILKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVADTIVEKASDLKDLNSRAQGEVTIREALRELDLWGVGAVFSLIDYEDSQNRTIKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAQLDEYLQNLNHIQRKWVYLEPIFGRGALPKEQTRFNKVDEDFRSIMMDIRKDSRVTTLTTHAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFIGDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDEESKHITAMRSLEGEVVPFKSKVLLSNNVEAWLNDLALEMKQTLKQLLKECVTAGRSSQGAIDPSLFPSQILCLAEQIKFTEDVEDAIRDHSLHQIEAQLAAKLERYTSVDTSSEDPGNSESGILELKLKTLILDIIHNIDIVKQLNQAQVHTTDDWAWKKQVRFYMKSDHTCYVQMVDSELQYTYEYQGNAPKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVGLVKCGAWGCFDEFNRLEEAVLSAVSMQIQTIQDALKNHRSVCELLGKEVEVNANSGIFITMNPAGKGYGGRQKLPDNLKQLFRPVAMSRPDNDLIAEVILYSEGFKDAKELGRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQLKKSGTKQDVNENHIVVQALRLNTMSKFTFADCTRFDALIKDVFPGIDFKEVEYNELSSALKQVFEEANYEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKSTLWRMLRAALCKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSARQVVREPQDVSSWIICDGDIDPEWIESLNSVLDDNRLLTMPSGERIQFGPNVNFVFETHDLSCASPATISRMGMIFLSDEETDLNSLIKSWLRNQPVEYRSNLENWIGDYFSKALQWVLKQNDYVVETSLVGTVMNGLSHLHGCKYHDQFIINLIRGLGGNLNMKSRLEFTKEVFNWARETPPDSHRPMDTYFDCDRGQLASYVLKKPESLTADDFSSGHSLPVIQTPDMQRGLDYFKPWLSSETKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTTSRHLLQKLSQTCMVISTNTGRVYRPKDCERLVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDENLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCAVDYPEREQLQTIYGAYLEAVLHKNLKNHSIWGSSSKIYLLAGSMVQVYEQVRAKFTVDDYSHYFFTPCILTQWVLGLFRYDLEGGSSNHPLDYVLEVVAYEARRLFRDKIVGVKELHLFDNILTSVLQGDWGSDILDNMADSFYVTWGAQHISGAKIAPGQPLPPHGKPLGKLSSADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRTDLKHVLHLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLKDQASQDGFFGPVFNYFTYRIQQNLHIVLIMDSANLNFIINCESNPALHKKCRVLWMEGWSDSSMKKIPEMLFSEADIEEKYEKKRKDEKKKSSVDPDFIKSFLLIHESCKAYGATPSRYMTFLRVYSAISSSKRKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKHRIAEEVVKIEERKSKIDDELKEVQPLVNEAKLAVGNIRPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFDARNIPKEIRESVEELLFKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKNCLEEWTKAAGLEKFDLRRFLCTESEQLIWKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSHLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILENKDLIESLNQTKASSALIQDSLKESYKLQISLDRERDAYLPLAESASKMYFIISDLSKINNMYRFSLASFLRLFQRALQNKQDSESTEQRIQCLVNSLKHMVYEYICRCLFKADQLMFALHFVRGMHPEFFQENEWDTFTGVVVGDMLRKADSQQRIRDQLPSWIDQERSWAVATLKISLPGLYQTLCFEDGTLWRTYYHHSMCEQEFPSILAKKVSLFQQVLVVQALRPDRLQSAMALFACKALGLKELSPLPLNLKRLYKETLEIEPILIIISPGADPSQELQELANAERSSERYHQVAMGQGQADLAIQMLKECARNGDWLCLKNLHLVVSWLPVLEKELNTLQPKESFRLWLTAEVHPNFTPILLQSSLKITYESPPGLKKNLMRTYESWTPEQISKKDNIHRAHALFSLAWFHAACQERRNFIPQGWTKFYEFSLSDLRAGYHVIDRLFDGSKDVQWEFVHGLLENSIYGGRIDNYFDLRVLQSYLKQFFNSSIIDVLNQRNKKSIFPYSISLPDSCSILDYRAVIEKLPEDDKPSFFGLPANIARSSQRMTSSQVISQLRILGRSVTAGCKFDREIWSNELSPVLNLWKKLNQNSNLIHQKVSPPNDRQGSPILSFIILEQFNAIRLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLTWQSKWEGPEDPLQYLRGLVARTLAIQNWVEKAEKQALLADTLDLSELFHPDTFLNALRQETARATGCSVDSLKFVASWKGRLQEAKLQIKISGLLLEGCSFDGSRLSENQHDSPSVSSVLPCYMGWTPQGSYGPYSPDECISLPVYTSAERDCVVTNIDVPCGGNQDQWIQCGAALFLKNQ', 4306, 'Q9JJ79; P70576; Q63167;', 'KD00027', 'Rattus norvegicus (Rat)', 'Dync2h1', '#Cytoplasmic dynein 2 heavy chain 1#Cytoplasmic dynein 2 heavy chain#Dynein cytoplasmic heavy chain 2#Dynein heavy chain isotype 1B#Dynein-like protein 4', '-', '-', '65209'),
(28, 'Q9EQU5', 'Protein SET', 'k', 33378, 'Multitasking protein; involved in apoptosis; transcription; nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase; NME1. In the course of cytotoxic T- lymphocyte (CTL)-induced apoptosis; GZMA cleaves SET; disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes; most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however; isoform 2 specific activity is higher (By similarity). {ECO:0000250}.', 'MAPKRQSAILPQPKKPRPAAAPKLEDKSASPGLPKGEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDDEEGEAEDDDDDDEEEEGLEDIDEEGDEDEGEEDDDEDEGEEGEEDEGEDD', 289, 'Q9EQU5; A2BE95; Q9CY82; Q9D0A9; Q9Z181;', 'KD00028', 'Mus musculus (Mouse)', 'Set', '#Protein SET#Phosphatase 2A inhibitor I2PP2A#I-2PP2A#Template-activating factor I#TAF-I', '-', '-', '56086'),
(29, 'Q2TBY0', 'Spindle and kinetochore-associated protein 2', 'GO:0000940', 14129, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis; when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it is required for SKA1 localization (By similarity). {ECO:0000250}.', 'MEAEVDKLELMFQKADSDLDYIQYRLEYEIKTNYPDSAGKKNPVTLLKELSAIKSRYQTLHVRFKPIAVEQKETKSRICATFNKTMTLIQELQKETDMELLPLTEEEKTAAEQLRAHMSDL', 121, 'Q2TBY0;', 'KD00029', 'Bos taurus (Bovine)', 'SKA2', '#Spindle and kinetochore-associated protein 2#Protein FAM33A', '-', '-', '615847'),
(30, 'Q4R628', 'Kinesin-like protein KIF3A', 'GO:0003777', 80341, '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}.', 'MPINKSEKPESCDNVKVVVRCRPLNEREKSMCYKQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAVPELRGIIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGIDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEISGSDISGSEEDDDEEGEVGEDGEKRKKRRDQAGKKKVSPDKMIEMQAKIDEERKALETKLDMEEEERNKARAELEKREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRKRAEQLRRELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQMLIIDNFIPRDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKEKDPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKTGRRKRSAKPETVIDSLLQ', 702, 'Q4R628;', 'KD00030', 'Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)', 'KIF3A', '#Kinesin-like protein KIF3A#Microtubule plus end-directed kinesin motor 3A', '-', '-', '-'),
(31, 'Q6P3R1', 'Kinesin-like protein KIF22', 'GO:0003777', 71391, 'Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA (By similarity). {ECO:0000250}.', 'MAKRVSILDQHKKPSSARVRVAVRLRPYMEKEDEKAPAACVRGLDSQSLEIVNWRNQLETMQYQFDAFYGDSATQREIYMGSVCHILPHLLIGQNASVFAYGPTGAGKTHTMLGNPSQPGVIPRAVRDLLQMTRTAAGGPENENWTYTITMSYVEIYQEKVMDLLEPKNKDLPIREDKDHNILIPGVTQKTINSFGDFDEHFIPASQNRTVASTKLNDRSSRSHAVLLIKVQKSQQVSPFRQLTGKLYLIDLAGSEDNRRTGNQGIRLKESGAINSSLFTLSKVVDALNQGLPRIPYRDSKLTRLLQDSLGGTAHSVMIANIAPEQKYYFDTLTALNFAAKSKQIINKPFSQETTQSIAALPAMKRPREEAETAAGSRQRKKSKTDSTESSPNTSMDAASKRKLNLAALDPAVVERLLKLDKILTEKGMKEAQLLSTPKRERMALLKKWEESQMEIERLKEKQKELEQKAIEAEARLEKSTNSDCNLSDSSVSECTFRAPLRGRNTSTAKAKKVLRVLPMQGNSQLQSTIEEGIPVFEKKKKKPVSCDGRENQPTWEVNVRTDLLESGRERILKLLNTGSVKELKSLQKIGDKKAKLIIGWREVNGPFKNVEDLASLEGISAKQVTSFIKANILSIIAS', 639, 'Q6P3R1;', 'KD00031', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'kif22', '#Kinesin-like protein KIF22#Chromokinesin kid', '-', '-', '394855'),
(32, 'Q9Y4B5', 'Microtubule cross-linking factor 1', 'GO:2000576', 209526, 'Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation. Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells. {ECO:0000269|PubMed:23902687}.', 'METLNGPAGGGAPDAKLQPPGQHHRHHHLHPVAERRRLHRAPSPARPFLKDLHARPAAPGPAVPSSGRAPAPAAPRSPNLAGKAPPSPGSLAAPGRLSRRSGGVPGAKDKPPPGAGARAAGGAKAALGSRRAARVAPAEPLSRAGKPPGAEPPSAAAKGRKAKRGSRAPPARTVGPPTPAARIPAVTLAVTSVAGSPARCSRISHTDSSSDLSDCPSEPLSDEQRLLPAASSDAESGTGSSDREPPRGAPTPSPAARGAPPGSPEPPALLAAPLAAGACPGGRSIPSGVSGGFAGPGVAEDVRGRSPPERPVPGTPKEPSLGEQSRLVPAAEEEELLREMEELRSENDYLKDELDELRAEMEEMRDSYLEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPPREPGWLGEGASPGAGGGAPLQEELKSARLQISELSGKVLKLQHENHALLSNIQRCDLAAHLGLRAPSPRDSDAESDAGKKESDGEESRLPQPKREGPVGGESDSEEMFEKTSGFGSGKPSEASEPCPTELLKAREDSEYLVTLKHEAQRLERTVERLITDTDSFLHDAGLRGGAPLPGPGLQGEEEQGEGDQQEPQLLGTINAKMKAFKKELQAFLEQVNRIGDGLSPLPHLTESSSFLSTVTSVSRDSPIGNLGKELGPDLQSRLKEQLEWQLGPARGDERESLRLRAARELHRRADGDTGSHGLGGQTCFSLEMEEEHLYALRWKELEMHSLALQNTLHERTWSDEKNLMQQELRSLKQNIFLFYVKLRWLLKHWRQGKQMEEEGEEFTEGEHPETLSRLGELGVQGGHQADGPDHDSDRGCGFPVGEHSPHSRVQIGDHSLRLQTADRGQPHKQVVENQQLFSAFKALLEDFRAELREDERARLRLQQQYASDKAAWDVEWAVLKCRLEQLEEKTENKLGELGSSAESKGALKKEREVHQKLLADSHSLVMDLRWQIHHSEKNWNREKVELLDRLDRDRQEWERQKKEFLWRIEQLQKENSPRRGGSFLCDQKDGNVRPFPHQGSLRMPRPVAMWPCADADSIPFEDRPLSKLKESDRCSASENLYLDALSLDDEPEEPPAHRPEREFRNRLPEEEENHKGNLQRAVSVSSMSEFQRLMDISPFLPEKGLPSTSSKEDVTPPLSPDDLKYIEEFNKSWDYTPNRGHNGGGPDLWADRTEVGRAGHEDSTEPFPDSSWYLTTSVTMTTDTMTSPEHCQKQPLRSHVLTEQSGLRVLHSPPAVRRVDSITAAGGEGPFPTSRARGSPGDTKGGPPEPMLSRWPCTSPRHSRDYVEGARRPLDSPLCTSLGFASPLHSLEMSKNLSDDMKEVAFSVRNAICSGPGELQVKDMACQTNGSRTMGTQTVQTISVGLQTEALRGSGVTSSPHKCLTPKAGGGATPVSSPSRSLRSRQVAPAIEKVQAKFERTCCSPKYGSPKLQRKPLPKADQPNNRTSPGMAQKGYSESAWARSTTTRESPVHTTINDGLSSLFNIIDHSPVVQDPFQKGLRAGSRSRSAEPRPELGPGQETGTNSRGRSPSPIGVGSEMCREEGGEGTPVKQDLSAPPGYTLTENVARILNKKLLEHALKEERRQAAHGPPGLHSDSHSLGDTAEPGPMENQTVLLTAPWGL', 1905, 'Q9Y4B5; E9PAY7; Q6ZMQ9; Q8IWA9;', 'KD00032', 'Homo sapiens (Human)', 'MTCL1', '#Microtubule cross-linking factor 1#Coiled-coil domain-containing protein 165#PAR-1-interacting protein#SOGA family member 2', '-', 'ENSG00000168502', '-'),
(33, 'Q8NBT2', 'Kinetochore protein Spc24', 'GO:0000777===GO:0031262===k', 22478, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. {ECO:0000269|PubMed:14738735}.', 'MAAFRDIEEVSQGLLSLLGANRAEAQQRRLLGRHEQVVERLLETQDGAEKQLREILTMEKEVAQSLLNAKEQVHQGGVELQQLEAGLQEAGEEDTRLKASLLYLTRELEELKEIEADLERQEKEVDEDTTVTIPSAVYVAQLYHQVSKIEWDYECEPGMVKGIHHGPSVAQPIHLDSTQLSRKFISDYLWSLVDTEW', 197, 'Q8NBT2; B4DZZ7; C9JGC4;', 'KD00033', 'Homo sapiens (Human)', 'SPC24', '#Kinetochore protein Spc24#hSpc24', '-', 'ENSG00000161888', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(34, 'Q9Z1S0', 'Mitotic checkpoint serine/threonine-protein kinase BUB1 beta', 'GO:0000776===GO:0000777===GO:0034501===GO:0000940===GO:0000778===SCL===k', 118392, 'Essential component of the mitotic checkpoint. Required for normal mitosis progression and tumor suppression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C; independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. Essential for tumor suppression. May play a role in regulating aging and fertility (By similarity). {ECO:0000250}.', 'MAEASEAMCLEGAEWELSKENIQPLRHGRVMSTLQGALAKQESAGHTALQQQKRAFESEIRFYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNEPLDMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEGIERKAEPLDRLQSQHRQFQSRVSRQAFLALGNEEEEALEPSEPQRSSLAELKSRGKKMARAPISRVGGALKAPGQSRGFLNAVPQPVHGNRRITVFDENADTASRTELSKPVAQPWMAPPVPRAKENELQPGPWSTDRPAGRRPHDNPASVTSIPSVLPSFTPYVEESAQQTVMTPCKIEPSINHVLSTRKPGREEGDPLQRVQSHQQGCEEKKEKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKERREAELLTSAKKREEMQKQIEEMERRLKAMQAVQQEGAGGQQEEKMPTEDPARLQIASGPQEMSGVPLSCSICPLSSNPREISPAENILQEQPDSKGSSMPFSIFDESLSDKKDKSPATGGPQVLNAQRRPLSVLKTTEVGTTNEDVSPDICDELTELEPLSEDAIITGFRNVTLCPNPEDTCDFARAARLASTPFHEILSSKGIAADPEGLLQEEDLDGKAAEAHHTVHHQALIIKKLSPIIEESREATHSSGFSRSSSSAPSTSSIKGFQLLEKLELTNDGAEDAIQSPWCSQYRLQLLKSLLELSAFAEFSVEDRPMPVLEIGKEIELGPEDYVIKQEHLTCDDYRLFWVAPRSSAELTMIKASSQPIPWDFYINLKLKERLNEDYDQLCSCCQYQDGHVVWYQYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHDPYDYVNKDDHAVRIMDFSYSVDLRVQLDAFAYSGFRTAQILEGQKILANCSSPYHVDLLGIADLAHLLLFKEHLHVFWDGLLWKLSQSTSELKDSELWNKFFVRILNASDKSTVSVLGELAAEMGGAFDATFHSHLNRALWKLGKTISPEALLTQQDKQPGGSQSPA', 1052, 'Q9Z1S0; A2ARS1;', 'KD00034', 'Mus musculus (Mouse)', 'Bub1b', '#Mitotic checkpoint serine/threonine-protein kinase BUB1 beta#2.7.11.1#MAD3/BUB1-related protein kinase#BubR1#Mitotic checkpoint kinase MAD3L', '-', '-', '12236'),
(35, 'Q6GPL3', 'Aurora kinase B-B', 'GO:0034501===GO:0032133', 42015, 'Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint; a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Phosphorylates ''Ser-10'' of histone H3 during mitosis (By similarity). {ECO:0000250}.', 'MSYKENLIPSSCSSSSSSSSKFATPSSATAAQRVLRKQPYVSIFTTPSDNLLAQRAQLAPRVTPAASSSVPGRVALGTDVASHNTALAEAPKRKFTIDDFDIGRPLGKGKFGNVYLAREKQNKFIMALKVLFKSQLEKEGVEHQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHGRFDEQRSATFMEELADALQYCHERKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCYEFLVGMPPFDSPSHSETHRRIVNVDLKFPPFLSEGSKDLISKLLRYHPAQRLPLKGVMEHPWVKANSRRVLPPVYQSSHPK', 368, 'Q6GPL3;', 'KD00035', 'Xenopus laevis (African clawed frog)', 'aurkb-b', '#Aurora kinase B-B#2.7.11.1#Aurora/IPL1-related kinase 2-B#AIRK2-B#XAIRK2-B#Serine/threonine-protein kinase 12-B#Serine/threonine-protein kinase aurora-B-B#xAurora-B-B', '-', '-', '444083'),
(36, 'Q75EQ0', 'DASH complex subunit DAM1', 'GO:0005828===GO:0008608===GO:0051987===GO:0042729', 36698, '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}.', 'MSKESVRESKAATEYRLSISSNPGSRRSSFGGSSEHPAGSGIGNNKASNGELREATLVDTLLLPQVQELKDSMITLDANLTHMNFIHESLVDLNESVSALLYGLMCNSWCVDFPNMPHHTARELGISKELARLKEEKQQLLADLQGTAQAPSLVLKEKEPNTSKQKFQLPKPPMVSTRSVVAPVRTISEEEEDDNTAASFVSNPTVMGQPPHAPPPVARSNNAKGRRRYSILQQIRNHDLTGQKHMVANLGGTVKARAATHPIPESAGEKRKSLAVSAVRIGNNKRLQTSRPPSGGRDVTMARKRSGTQPAILNTNSITHSSTGAVPASSAQGRRPPFR', 339, 'Q75EQ0;', 'KD00036', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DAM1', '#DASH complex subunit DAM1#Outer kinetochore protein DAM1', '-', '-', '4618458'),
(37, 'O08788', 'Dynactin subunit 1', 'GO:0000776', 141676, 'Required for the cytoplasmic dynein-driven retrograde movement of vesicles and organelles along microtubules. Dynein- dynactin interaction is a key component of the mechanism of axonal transport of vesicles and organelles.', 'MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMGVEVGRLRAFLQGGQEATDIALLLRDLETSCSDTRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCTILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEPQRGGAPGQAPGALPGPGLVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKLSLPPHEGPGGNLVAGALYRKTSQLLEKLNQLSTHTHVVDITRSSPAAKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHSRLIS', 1281, 'O08788; E9QLJ1; Q3TZG7;', 'KD00037', 'Mus musculus (Mouse)', 'Dctn1', '#Dynactin subunit 1#150 kDa dynein-associated polypeptide#DAP-150#DP-150#p150-glued', '-', '-', '13191'),
(38, 'O35231', 'Kinesin-like protein KIFC3', 'GO:0003777', 92556, 'Minus-end microtubule-dependent motor protein. Involved in apically targeted transport. Required for zonula adherens maintenance. {ECO:0000269|PubMed:11581287}.', 'MVPSRRTWNLGATPSLRGLWRVGRVQEPKPGMARPAPASPAARPFPHTGQGRLRTGRGKDILPSGEEDSTSRTAARPSLAQCRALSVDWPGPRSPHRLYLTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVRPVTKEDGEGPEATNAVTFDPDDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLRFAERVRSVELGPGSRRTELGSWSSQEHLEWEPACQTPQPTARAHSAPGSGTSSRPGSIRRKLQPSA', 824, 'O35231; O35072; Q1WNZ8; Q3UX36; Q3V0U4; Q6NS71; Q8R3Y4; Q91YQ2;Q99KP7;', 'KD00038', 'Mus musculus (Mouse)', 'Kifc3', '#Kinesin-like protein KIFC3', '-', '-', '16582'),
(39, 'Q8WVJ2', 'NudC domain-containing protein 2', 'GO:0000777===SCL', 17676, 'May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone. {ECO:0000269|PubMed:20133715}.', 'MSAPFEERSGVVPCGTPWGQWYQTLEEVFIEVQVPPGTRAQDIQCGLQSRHVALSVGGREILKGKLFDSTIADEGTWTLEDRKMVRIVLTKTKRDAANCWTSLLESEYAADPWVQDQMQRKLTLERFQKENPGFDFSGAEISGNYTKGGPDFSNLEK', 157, 'Q8WVJ2; B2R4V0;', 'KD00039', 'Homo sapiens (Human)', 'NUDCD2', '#NudC domain-containing protein 2', '-', 'ENSG00000170584', '-'),
(40, 'Q9M0N8', 'Mitotic-spindle organizing protein 1B', 'GO:0005828', 7835, 'Required for gamma-tubulin complex recruitment to the centrosome (By similarity). During mitosis; modulates gamma- tubulin complex localization; spindle stability and chromosomal segregation. Necessary for gametophyte development and embryogenesis. {ECO:0000250}.', 'MDEEASRTARESLELVFRMSNILDTGLDRHTLSVLIALCDLGVNPEALATVVKELRRESIPDSVTTTPSIH', 71, 'Q9M0N8;', 'KD00040', 'Arabidopsis thaliana (Mouse-ear cress)', 'GIP1', '#Mitotic-spindle organizing protein 1B#GCP3-interacting protein 1#AtGIP1#Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1B#AtGIP1B', '-', '-', '826539'),
(41, 'Q10654', 'G2/mitotic-specific cyclin-B3', 'GO:0051383', 44757, 'Could be involved at the G2/M (mitosis) transition. Interacts with the CDK1 and CDK2 protein kinases. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.', 'MMLRSQAKNVDLTSQADSRHQQKRKQAEQLDALKNPSEPAAKKQHSKGLTELRAHISGFKIDSAKRDPLGKSRTSRRDVENLPPQKSRYVDPCPHYDYDLEEAGNPDSISDYAQGIFDYYRHREVHFRVRKYLHKHPEVDVKTRAILIDWMVEIQETFELNHETLYNAVKLTDMYLCKTKNVDKNTIQKLACVAIFIAAKYDERSPPLVDDLIYLSGDRFSRDELLAMERELFATVGYDLGSPLSYRYLRRFGRVCRVDMKTLTMGRFILETSLMVYEYAMVSQSRLAAAAFVLAMRMLDKNNEYEWNPVLEKYSGFTGEEVMPLVEHMNHILHFSKDKWAQLTSVRQKYSHEVFFHVASIPMLPDTLKVVDSHTYAPVPMLSYP', 385, 'Q10654; Q95ZP8; Q9U378;', 'KD00041', 'Caenorhabditis elegans', 'cyb-3', '#G2/mitotic-specific cyclin-B3', '-', '-', '180040'),
(42, 'Q3UA16', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 26457, '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}.', 'MGEDELALLNQSINEFGDKFRNRLDDNHSQVLGLRDAFKDSMKAFSEKMSLKLKEEERMTEMILEYKNQLCKQNKLIQEKKENVLKMIAEVKGKEQESEELTAKIQELKEEYARKRETISTANKANEERLKGLQKSADLYRDYLGLEIRKIHGNKLQFIFTSIDPKNPESPYMFSMSINEAKEYEVYDSSPHLECLAEFQEKVRKTNNFSAFLANIRKAFIAKVHN', 226, 'Q3UA16; Q9D021; Q9D1K6;', 'KD00042', 'Mus musculus (Mouse)', 'Spc25', '#Kinetochore protein Spc25', '-', '-', '66442'),
(43, 'Q5XLR4', 'Borealin', 'GO:0032133', 30382, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (By similarity). {ECO:0000250}.', 'MAPRKRTQNAKSKKNPKAPKLEAFLLDFDDEVHTIVERLKEKTNNLLKDADNLYKTALIKLPMAVRKMNWIEYCNLEKPKSPVDDSKVREEAAQVELAIAGNHTIPKVAAKEAKSSANSEDENMAPLKSTMKKKKASKKAPSTSKKPRTLSISKQGGTIQRTTRKPLITPARSFLDSSIIGATPLITPRFDPRLPKTPALRSALHREKVYSMSVNGSPLSAGGEDIVISVPIGNGECIQLLASEMDSVDLSQLDEKALRSIRNLQNRLTTLCGSSK', 276, 'Q5XLR4; Q5U3V2;', 'KD00043', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'cdca8', '#Borealin#Cell division cycle-associated protein 8#Dasra-B#DasraB#DrDasraB', '-', '-', '492815'),
(44, 'Q8WVK7', 'Spindle and kinetochore-associated protein 2', 'GO:0000940===k', 14188, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis; when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it is required for SKA1 localization. {ECO:0000269|PubMed:17093495; ECO:0000269|PubMed:19289083}.', 'MEAEVDKLELMFQKAESDLDYIQYRLEYEIKTNHPDSASEKNPVTLLKELSVIKSRYQTLYARFKPVAVEQKESKSRICATVKKTMNMIQKLQKQTDLELSPLTKEEKTAAEQFKFHMPDL', 121, 'Q8WVK7; A6NIL3; B3KPL3; E9PCB8;', 'KD00044', 'Homo sapiens (Human)', 'SKA2', '#Spindle and kinetochore-associated protein 2#Protein FAM33A', '-', 'ENSG00000182628', '-'),
(45, 'B3LW62', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 24974, '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}.', 'MAVGLDRADKSNYALRLKEMFNKEIRLQCRETNISKMSSKFHDNLLTAMEKADWQQRELERIERQLVLNRQELEKRLLLEKELTRELEATKLQEATVREHNNELMECIHALKRATGTSINHDALPARVKGVTVLRNTDGDQWIPFDLAVTDTEGLNSLCQKLQSNNIDVNKWRQLVSLATEMSMKWNYSTPNRRDNAKVDIIEIDLTSPTNQIIL', 215, 'B3LW62;', 'KD00045', 'Drosophila ananassae (Fruit fly)', 'Spc25', '#Kinetochore protein Spc25 {ECO:0000250|UniProtKB:Q9V3V7}', '-', '-', '6499713'),
(46, 'Q9EQW7', 'Kinesin-like protein KIF13A', 'GO:0003777', 195813, 'Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane; endosomal sorting during melanosome biogenesis and cytokinesis. During melanosome maturation; required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abcission step in cytokinesis: mediates translocation of ZFYVE26; and possibly TTC19; to the midbody during cytokinesis (By similarity). Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. {ECO:0000250; ECO:0000269|PubMed:11106728}.', 'MSDTKVKVAVRVRPMNRRELELNTKCVVEMEGNQTVLHPPPSNTKQGERKPPKVFAFDYCFWSMDESNTTKYAGQEVVFKCLGEGILEKAFQGYNACIFAYGQTGSGKSFSMMGHAEQLGLIPRLCCALFQRIALEQNESQTFKVEVSYMEIYNEKVRDLLDPKGSRQSLKVREHKVLGPYVDGLSQLAVTSFEDIESLMSEGNKSRTVAATNMNEESSRSHAVFNIIITQTLYDLQSGNSGEKVSKVSLVDLAGSERVSKTGAAGERLKEGSNINKSLTTLGLVISSLADQAAGKGKNKFVPYRDSVLTWLLKDNLGGNSQTSMIATISPAADNYEETLSTLRYADRAKRIVNHAVVNEDPNAKVIRELREEVEKLREQLSKAEAMKPPELKEKLEESEKLIKELTVTWEEKLRKTEAIAQERQRQLESMGISLETSGIKVGDDKCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCEIDIAADGDITLTPKENARSCVNGTLVCNTTQLWHGDRILWGNNHFFRINLPKRKRRDWLKDFERETSSAEHDLDAASEASSEPDYNYEFAQMEVIMKTLNSNDPVQNVVQVLEKQYLEEKRTALEEQRLMYERELEQLRQQLSPERQPPSSASDRLAYSSQTAQQKVTQWAEERDELFRQSLAKLREQLVKANTLVREANFLAEEMSKLTDYQVTLQIPAANLSANRKRGAIVSEPAIQARRKGKGTQVWTIEKLENKLIDMRDLYQEWKENVPEAKRLYGKRGDPFYEAQENHNLIGVANVFLECLFCDVKLQYAVPIISQQGEVAGRLHVEVTRITGTIPERMAEDDSSENSSESGSLEVVDSSGEVIHRVKKLTCRVIIKEATGLPISLSNFVFCQYTFWDQCESTVAAPVVDPDVPSPQSKDAQYTVTFSHCKDYVVTVTEEFLEFISDGALAIEVWGHRCAGNGSPIWEVDSLHAKTRTLHDRWNEVTRRIEVWISILELNELGDYAAVELHQAKDVNTGGVFQLRQGHSRRVQVTVKPVQHSGTLPLMVEAILSVSIGCVTARSTKLQRGLDSYQEEDLNCVRERWSDALIKRREYLDEQIKKVSNKKEKTEDDMEREARLVEQWVGLTEERNAVLVPAPGSGIPGAPADWVPPPGMETHIPVLFLDLNADDLSANEQLVGPHASGVNSILPKEHGSQFFYLPIIKHSDDEVSATASWDSSVHDSLHLNRVTPQNERIYLIVKTTVQLSHPAAMELVLRKRIAANIYNKQSFTQSLKRRISLINICYSCGVTYEIVSNIPKATEEIEDRETLALLAARSENEGTLDGETYIEKYTRGVLQVENILSLERLRQAVTVKEALSTKARHIRRSLSTPNVHNVSSSRPDLSGFDEDDKGWPENQLDVSDYSSSYQDVACYGTLPRDSPRRSKEGCPSENPHALTVSPFKAFSPQPPKFFKPLMPVKEEHKKRLALEARPLLSQEDSEEEENELEALSRKLMLTQPYVPVEFADFSVYNASLENREWSSSKADLTDSRALEKAVSRSPTTSSLTSGYFSHSASNATLSDMAVPSSDSSDQLAVSTKEVECAEPPGPSLAPDVRRASNQELTEVGRGSGKDETIAVPLEENSALPKGTPSPQSIPEESSRMPCRTASCSELDVGPSKDGHQAREFCPGEVTIEHTTNILEDHSFTEFMGVSDGKDFDGLADCSVGEPSRRRALTNETDHKGIPERPPDADRLHPKIENDQEATATR', 1749, 'Q9EQW7; O35062;', 'KD00046', 'Mus musculus (Mouse)', 'Kif13a', '#Kinesin-like protein KIF13A', '-', '-', '-'),
(47, 'O35216', 'Histone H3-like centromeric protein A', 'GO:0051382===GO:0000939===GO:0000778===GO:0000780===k', 15509, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro) (By similarity). {ECO:0000250}.', 'MGPRRKPQTPRRRPSSPAPGPSRQSSSVGSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRVTLFPKDIQLTRRIRGFEGGLP', 134, 'O35216; Q545C9;', 'KD00047', 'Mus musculus (Mouse)', 'Cenpa', '#Histone H3-like centromeric protein A#Centromere protein A#CENP-A', '-', '-', '12615'),
(48, 'P33322', 'H/ACA ribonucleoprotein complex subunit 4', 'k', 54705, 'Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex; which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5; instead of the normal N1. Pseudouridine (''psi'') residues may serve to stabilize the conformation of rRNAs. May function as a pseudouridine synthase. Binds in vitro to centromeres and microtubules. It is a centromeric DNA-CBF3-binding factor which is involved in mitotic chromosome segregation. Essential for cell growth. {ECO:0000269|PubMed:10523634; ECO:0000269|PubMed:8336724; ECO:0000269|PubMed:9315678; ECO:0000269|PubMed:9472021; ECO:0000269|PubMed:9848653}.', 'MSKEDFVIKPEAAGASTDTSEWPLLLKNFDKLLVRSGHYTPIPAGSSPLKRDLKSYISSGVINLDKPSNPSSHEVVAWIKRILRCEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCIVRLHDALKDEKDLGRSLENLTGALFQRPPLISAVKRQLRVRTIYESNLIEFDNKRNLGVFWASCEAGTYMRTLCVHLGMLLGVGGHMQELRRVRSGALSENDNMVTLHDVMDAQWVYDNTRDESYLRSIIQPLETLLVGYKRIVVKDSAVNAVCYGAKLMIPGLLRYEEGIELYDEIVLITTKGEAIAVAIAQMSTVDLASCDHGVVASVKRCIMERDLYPRRWGLGPVAQKKKQMKADGKLDKYGRVNENTPEQWKKEYVPLDNAEQSTSSSQETKETEEEPKKAKEDSLIKEVETEKEEVKEDDSKKEKKEKKDKKEKKEKKEKKDKKEKKEKKEKKRKSEDGDSEEKKSKKSKK', 483, 'P33322; D6VYH9;', 'KD00048', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CBF5', '#H/ACA ribonucleoprotein complex subunit 4#5.4.99.-#Centromere-binding factor 5#Centromere/microtubule-binding protein CBF5#H/ACA snoRNP protein CBF5#Small nucleolar RNP protein CBF5#p64''', '-', '-', '850872'),
(49, 'Q8C5S7', 'Meiotic recombination protein REC8 homolog', 'GO:0000778===GO:0000780', 67425, '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. {ECO:0000269|PubMed:12034751; ECO:0000269|PubMed:15515002; ECO:0000269|PubMed:15935783; ECO:0000269|PubMed:16855401}.', 'MFYYPNVLQRHTGCFATIWLAATRGSRLVKREYLNVNVVKTCEEILNYVLVRVQPPVAGLPRPRFSLYLSAQLQIGVIRVYFQQCQYLVEDIQHILEHLHRAQLRIRIDMEEADLPSLLLPNCLAMMETLEDAPEPFFGKMSVDPRLPSPFDIPQIRHLLEAATPEKTRKETLPEATPDPRKPDRTLATVQSPEVITLQEAEPIRMLQIEGEQDLPEISRGDLELLIAEKDDAILLEERQRGRLLRQRRASLPLDESREEPRALEGAGLVSALSPPAPAQVEGIQEALPGQVFPPEVQKMTGWEPGALLTEVTPPQELRLPAPPSTEKRLPSLQRPLPRRHRRRQLLFWDKETQISREKFEEQLQTGAHCWEYPVAQPPKRMLTSPAELFRTPTLSGWLPPELLGLWTHCAQVPQRMLRQRPQLETEETVEEERAADEEERRKTEALSEIEVLREAQEPSGPLMLSSELSLEAAEDEKSRTSLIPPEWWAWSEEGQPEPPALPMLPELPEVPMEMPPRPELSSEAVLRAVALKLQANKELDFSSLVPPLSPRKLASRVFYLLLVLSTQKILLVEQQKPYGPLLIRPGPKFP', 591, 'Q8C5S7; Q3UIN9; Q9JK52;', 'KD00049', 'Mus musculus (Mouse)', 'Rec8', '#Meiotic recombination protein REC8 homolog#Cohesin Rec8p', '-', '-', '56739'),
(50, 'P34470', 'Histone H3-like centromeric protein hcp-3', 'GO:0000777===GO:0051382===GO:0000779===k', 32997, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Not required for chromosome segregation during meiosis. {ECO:0000269|PubMed:10524621; ECO:0000269|PubMed:11402065; ECO:0000269|PubMed:14522947; ECO:0000269|PubMed:16273096}.', 'MADDTPIIEEIAEQNESVTRIMQRLKHDMQRVTSVPGFNTSAAGVNDLIDILNQYKKELEDDAANDYTEAHIHKIRLVTGKRNQYVLKLKQAEDEYHARKEQARRRASSMDFTVGRNSTNLVDYSHGRHHMPSYRRHDSSDEENYSMDGTNGDGNRAGPSNPDRGNRTGPSSSDRVRMRAGRNRVTKTRRYRPGQKALEEIRKYQKTEDLLIQKAPFARLVREIMQTSTPFGADCRIRSDAISALQEAAEAFLVEMFEGSSLISTHAKRVTLMTTDIQLYRRLCLRHL', 288, 'P34470;', 'KD00050', 'Caenorhabditis elegans', 'hcp-3', '#Histone H3-like centromeric protein hcp-3#CENP-A homolog#CeCENP-A#Holocentric chromosome-binding protein 3', '-', '-', '176359'),
(51, 'O96689', 'FI11703pRad21 mitotic cohesinVerthandi; isoform A', 'k', 79945, '', 'MFYEHIILAKKGPLARIWLAAHWDKKITKAHVFETNIEKSVEGILQPKVKLALRTSGHLLLGVVRIYSRKAKYLLADCNEAFVKIKMAFRPGMVDLPEGHREANVNAITLPEVFHDFDTALPELNDIDIEAQFSINQSRADEITMREDYGSLSLSLQDDGFGDIGFEAETPEIIRCSIPSNINDKIFDNDVLENIESLDPHSLDAHADMPGSRLDGDGFGDSFGQPALFEDDLFGDPSQPVEQITKESTTVLNADDSDEDAIDNIHNVPSPATSLVNSIEDEKEENNLNGHASVSENVPMNEITLVQNEDEGFALAPLDVSMYKGVTKAKRKRKLIIDEIKNISGEEMKAQLADTSDILTTLDLAPPTKRLMYWKETGGVEKLFSLPSRSIPARALFGNYNRQLFSHSTFFEDFSSVVPMEILALEFYTKENENALIIFNKKGRKRKNDNMSNLFLDHVPDSVVQSLEAPEVLRANHKSLGVSTVSVEIVSKEQESISCQNELTFFDNMRSPDLLSLNEMEQFSSINELPLTPRNMNHEMGDDFNQGDSTPAGLDHGHATPQHGNIGEMDHDSVIPTKKTAVILNESVGTSVLSDNGVSKRTNNILKGWDNYEIPSFVGQNHGDEQMENETDEQFEERVLNKRAAHLFIDVRAHFIAKDSLELSQLTSGNSRKQAAQKFYSLLVLKKFKVLHIDQSAPYADITITRGPTFENPKI', 715, 'O96689;', 'KD00051', 'Drosophila melanogaster (Fruit fly)', 'vtd', '#FI11703p {ECO:0000313|EMBL:ACX61578.1}#Rad21 mitotic cohesin {ECO:0000313|EMBL:AAD04175.1}#Verthandi; isoform A {ECO:0000313|EMBL:EAA46289.1}', '-', '-', '3354896'),
(52, 'A8MT69', 'Centromere protein X', 'GO:0000777===GO:0051382', 8959, '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. {ECO:0000269|PubMed:19620631; ECO:0000269|Ref.5; ECO:0000269|Ref.6}.', 'MEGAGAGSGFRKELVSRLLHLHFKDDKTKVSGDALQLMVELLKVFVVEAAVRGVRQAQAEDALRVDVDQLEKVLPQLLLDF', 81, 'A8MT69; O00281; O00282; Q96DD4; Q96F51;', 'KD00052', 'Homo sapiens (Human)', 'STRA13', '#Centromere protein X#CENP-X#FANCM-interacting histone fold protein 2#Fanconi anemia-associated polypeptide of 10 kDa#Retinoic acid-inducible gene D9 protein homolog#Stimulated by retinoic acid gene 13 protein homolog', '-', 'ENSG00000169689', '-'),
(53, 'Q9H900', 'Protein zwilch homolog', 'GO:0000776===GO:0000777===SCL===k', 67214, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. {ECO:0000269|PubMed:15824131}.', 'MWERLNCAAEDFYSRLLQKFNEEKKGIRKDPFLYEADVQVQLISKGQPNPLKNILNENDIVFIVEKVPLEKEETSHIEELQSEETAISDFSTGENVGPLALPVGKARQLIGLYTMAHNPNMTHLKINLPVTALPPLWVRCDSSDPEGTCWLGAELITTNNSITGIVLYVVSCKADKNYSVNLENLKNLHKKRHHLSTVTSKGFAQYELFKSSALDDTITASQTAIALDISWSPVDEILQIPPLSSTATLNIKVESGEPRGPLNHLYRELKFLLVLADGLRTGVTEWLEPLEAKSAVELVQEFLNDLNKLDGFGDSTKKDTEVETLKHDTAAVDRSVKRLFKVRSDLDFAEQLWCKMSSSVISYQDLVKCFTLIIQSLQRGDIQPWLHSGSNSLLSKLIHQSYHGTMDTVSLSGTIPVQMLLEIGLDKLKKDYISFFIGQELASLNHLEYFIAPSVDIQEQVYRVQKLHHILEILVSCMPFIKSQHELLFSLTQICIKYYKQNPLDEQHIFQLPVRPTAVKNLYQSEKPQKWRVEIYSGQKKIKTVWQLSDSSPIDHLNFHKPDFSELTLNGSLEERIFFTNMVTCSQVHFK', 591, 'Q9H900; B3KVB8; Q6N049; Q8N404; Q96SY7; Q9NWG7;', 'KD00053', 'Homo sapiens (Human)', 'ZWILCH', '#Protein zwilch homolog#hZwilch', '-', 'ENSG00000174442', '-'),
(54, 'O02053', 'SAN-1', 'k', 45060, '', 'MAEEPYVFTLKKRNNDDAEDDWDRYSENVRPTRRGRKIDALKRNVEEVVTEETARLKLDQLLEELQNLECSEESEELQKILDFCSWFEEKLAIGFHKVYYELLWKIISRHGFLEKYKEDERMLKIWEKMADNSAGHAHDIYQFAISRKSLVKCAALYARWSQSVELAGAYVEARRVLILARTNCAVPIQIVNDAEDALEMREMRRHLQERDSDDDEEEEETRKAFTNLPVIGDNHTVPIVRLPSMCSDTTKKAMKFDTGNVERVNPVCKDNQMQPFEVLSYTDADDVEYLRNVHELHAHIERYAIKETTNPSITGSSTSEAAAVTIYPVSSSEFEVWTVEGSGPTKAKARMAIKRVFKDLSFEEYAASLLPNHPSMVRATAKKLDFDETL', 390, 'O02053;', 'KD00054', 'Caenorhabditis elegans', 'san-1', '#SAN-1 {ECO:0000313|EMBL:CCD73299.1}', '-', '-', '172342'),
(55, 'Q9C0W0', 'Kinetochore protein mis15', 'GO:0051382===GO:0000778===GO:0061638===GO:0000779===k', 47394, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. Has a role in the maintenance of core chromatin structure and kinetochore function. Located in the inner regions of the centromeres and is essential for sister chromatid segregation during the G1/S phase following mitosis. Required for correct chromosome segregation where it has a role in the formation and/or maintenance of specialized chromatin at the centromere. {ECO:0000269|PubMed:15369671; ECO:0000269|PubMed:15897182; ECO:0000269|PubMed:16079914; ECO:0000269|PubMed:16855021}.', 'MRTELSSNIRIKHDKKIQKLLNRFPRDFLVKLCVEWIQKQTYPPNAKDINLEDMLDDEEWNPEAFYKNVPKSMLKRSIIHRMLVYDWPNGFYLGQIAQLEILALAHGFVSMRWTASKVHHSAEKTVLPNPLVFLELLKSELESIFVYHTYISRHETLPITFIRLVLWDSKRPTALHTYPSSKQIFYLGLMDDSDVLLHNIFLRNDVCHSLFLQCLSRLLYRLKAGSALRPIDLVSKNLTTFCTNVGVNKEANALGAWQIYAKNLVDRSPLDTRPILSDDNSSLIADSTQNCEKHREMAIQRRFGDTHSQVLDKLLITLDHDYIEKSTEKDKVLEENVESYNPTEQRPLVVMQLRGQHILEGLKDICRQDALDPFTMPSYLTGETGLSILYVRDGLVLQRQESLGQQEIN', 409, 'Q9C0W0; A1IU53; O13613;', 'KD00055', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis15', '#Kinetochore protein mis15#Sim4 complex subunit mis15', '-', '-', '2541321'),
(56, 'Q7ZW63', 'Kinetochore protein Nuf2', 'GO:0000777===GO:0031262', 53632, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSENTFPVYKVDVIVQFYRTEVLTGQESKHFTKNDLTPTPKPESVQRLYMRILQLLFRFRPECHYTVPLSENIQYPMLYESFAPIMSVYMRMCQFLPVCRVYDFSLSDLLNPKTKRTITILSAIQNFLHFRKQRLEITAAHQQSFRADMDRLQAYTREIKEAEKKIEKLTTIPPEQQAEAKELASALAELSTNTQHEYQDVSAINEKVAQFKTEIAELSQKLTQRKVEVATLKDEISKLKSQIVESPEELKNEMERMRETAKNIKMSKELADERLVELQMLVQCASQVEAEIQILLKQLQDLQSSMSKTKQRKEEVQSLEVMNESLQKELKSLSSEEAQLKRALTMKLDKESKQQIRRQKKKEVKDQQVKNIYGQYDKMHQKRQEIVKKIEECNRETKQFKEKMQALRENCNQRTQKAQEIYERLLTTLEQYHKRIEKILVETNADALKMKSHF', 454, 'Q7ZW63;', 'KD00056', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'nuf2', '#Kinetochore protein Nuf2#Cell division cycle-associated protein 1', '-', '-', '393280'),
(57, 'P34440', 'Histone H3-like centromeric protein cpar-1', 'GO:0000777', 29085, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Not required for chromosome segregation during meiosis. {ECO:0000269|PubMed:16273096}.', 'MADDGPIIEEIAEKNGRVARIMQRLQHDTQRVTSVPGFNTSATGYADLIALLDQYKNDLEAVGFNDLEQARRRAPSVDITVGSNSTNLVDYSHGRHDMPSHRRHDSSDEEITAANSHHQSPINVGNRNDTDGTNGRNGSRAGSSSSDRVRMIAGRNRISKTRRYRPGQKALEEIRKYQESEDLLIPKAPFARLVREIMQTSTPFSSDLRIRSDAINALQEASEALLVQMFDGSSLISAHSKRATLTTTDVQLYRRLCLPNL', 261, 'P34440;', 'KD00057', 'Caenorhabditis elegans', 'cpar-1', '#Histone H3-like centromeric protein cpar-1#CENP-A-related protein 1#Centromeric protein A related', '-', '-', '186223'),
(58, 'Q5R8T7', 'Nuclear distribution protein nudE-like 1', 'GO:0000777', 38405, '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}.', 'MDSEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYISGNVNCGVLNGNGTKFSRSGHTSFFDKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV', 345, 'Q5R8T7; Q5R555;', 'KD00058', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'NDEL1', '#Nuclear distribution protein nudE-like 1#Protein Nudel', '-', '-', '100173007'),
(59, 'O44218', 'Centromere/kinetochore protein zw10', 'GO:0000777', 82076, 'Required for accurate chromosome segregation. {ECO:0000250}.', 'MAARAQIKLLPEMFQSNGCASLEDTKSTVSKVQTRTERFQERVRKHIDENYSEFMTNHTSPDIFLEESSSLGREINDLLETVGTEGLAALNGSSTQLADHSRELRELMLGLQVSEHILKIDELFQCVEEAKGTKDYLVVLDLVGRLRSLIYGEGEAATQDVVRIFQALECYETIKVKYHVQAHLLQQNMQERFDRLVQLNCKSFPNSKCVTLLVSKEEGQLHDIVIALFQERYNPVRLCEFLLENCIEPLILKPVGVECNENAEAGTYVQLSLSYSTKESGTASGTSTQLRPNYKQVLEHFRLLLQTLSGINHSLSSSQHVFSIIGDHVKDRMMHLLVNDCLIPAVPETMEEYQASTLCEDVAHFEQYLADSFLINPEVDRGLSQFIEQYGTYYRNRLCSRVLESTREIIQRDLQDMVLVAPNNQAMDVTGCDPFLFPRCMVSRSAQDFMKLMERILRQPTEKPGEDEADPLAGVIGMMLQTYIDEVPKVHKKLLESIPQQSVLFHNNCMYFTHWVAQNANKGIESFPALVKTLQATGTMHFRVQVTYQTSILMDIMESFEFESPHTLGTGPLKLVRQCLRQLELLKNVWQNVLPDNVYNSTFVELLHAFINELVRHIFTQRDISATMASDLSDLIDVVLEKAPKLFRDPHEVHQVRSWMKLQQLKTMMNASLKEITELWCKGAGPLTANYKADEIRYLIRALFQDTDRRAKAITQIM', 718, 'O44218; Q29GT8;', 'KD00059', 'Drosophila pseudoobscura pseudoobscura (Fruit fly)', 'mit(1)15', '#Centromere/kinetochore protein zw10#Mitotic 15 protein', '-', '-', '4815208'),
(60, 'Q6CXI8', 'DASH complex subunit DAD2', 'GO:0042729', 14980, '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}.', 'MAFETEIETKRRELNYLKHVSALTQKLKAQLDELSVQVAQMNSNAVTVKDVMANWDSVLRSISQASISLLQYTENDYETGKWASKEEHRNQQGAEDESAASESSEDNQQRQQDQLPPLPETLVRVKVADDVE', 132, 'Q6CXI8;', 'KD00060', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'DAD2', '#DASH complex subunit DAD2#Outer kinetochore protein DAD2', '-', '-', '2896437'),
(61, 'Q13422', 'DNA-binding protein Ikaros', 'k', 57528, 'Transcription regulator of hematopoietic cell differentiation (PubMed:17934067). Binds gamma-satellite DNA (PubMed:17135265; PubMed:19141594). Plays a role in the development of lymphocytes; B- and T-cells. Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Repressor of the TDT (fikzfterminal deoxynucleotidyltransferase) gene during thymocyte differentiation. Regulates transcription through association with both HDAC-dependent and HDAC-independent complexes. Targets the 2 chromatin-remodeling complexes; NuRD and BAF (SWI/SNF); in a single complex (PYR complex); to the beta- globin locus in adult erythrocytes. Increases normal apoptosis in adult erythroid cells. Confers early temporal competence to retinal progenitor cells (RPCs) (By similarity). Function is isoform-specific and is modulated by dominant-negative inactive isoforms (PubMed:17135265; PubMed:17934067). {ECO:0000250|UniProtKB:Q03267; ECO:0000269|PubMed:10204490; ECO:0000269|PubMed:17135265; ECO:0000269|PubMed:17934067; ECO:0000269|PubMed:19141594}.', 'MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRLPNGKLKCDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS', 519, 'Q13422; A4D260; B4E0Z1; D3DVM5; O00598; Q53XL2; Q69BM4; Q8WVA3;', 'KD00061', 'Homo sapiens (Human)', 'IKZF1', '#DNA-binding protein Ikaros#Ikaros family zinc finger protein 1#Lymphoid transcription factor LyF-1', '-', 'ENSG00000185811', '-'),
(62, 'O44219', 'Centromere/kinetochore protein zw10', 'GO:0000777', 81262, 'Required for accurate chromosome segregation. {ECO:0000250}.', 'MAETQVLLETYQGQGNNNATNIEATKAAIKKMLVRIERFQTRVRKHIDENYVDFMPNHTSPDIFLEKSSALGDEISDLLATVGNEGLSVLSDASVELAALSRDLREKLFGLRVSEHILKLDDLFQCVEEAKSTKDCLVVLDLMGRLRSLIYGEGTSDDISPDVERIFQSLECYESIKVKYHVQAHLLQQNLQERFDRLVQLSCKSFPTSKCVTLLISKDEALLQDIVIALFQESYNPTKLCAFLLENCIEPLIQKPVSVEYNVNAKDGTHIQLTLSYSIKEPDTSSLLRPNYKDVFEHFRLLLKTLCGINSSLNGTQHVFTVIGDHVKERMLQLLLDECLIRVPETMDEYNSSTLCEDVAEFEHQLVDTFLINPELDTTLTEFTKQFDTYYRNRLSERVLATAREIIQRDLQDMTLVAPSNLSANVASDPLLFPRCMVSKSAQVDFVKLMERVVRQPDKAAEGTPDPLGGVIGLLLDAYINEVPKVHKKLLKSIPQQSALFYNNCMYLTHWVAQHTKDNIDGFPSLVKILQSTGNKHLRVQVSYQESILMDIMSSFEFENPHTLGTAPLRLVRQCLRQLELLKNVWQQVPAENVYNNSFCELLQAFINELVQRVFSLRDISATMASELSDLIDVVLEKASILFHDKNDVVHVRSWLKLQQLKIMMNASLKEFSELWCDGVGPLTANYHADEIKHLIRALFQDTDRRAKAITQIV', 714, 'O44219;', 'KD00062', 'Drosophila grimshawi (Fruit fly) (Idiomyia grimshawi)', 'mit(1)15', '#Centromere/kinetochore protein zw10#Mitotic 15 protein', '-', '-', '-'),
(63, 'Q9HAQ2', 'Kinesin-like protein KIF9', 'GO:0003777', 89986, '', 'MGTRKKVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGATENYKHRGILPRALQQVFRMIEERPTHAITVRVSYLEIYNESLFDLLSTLPYVGPSVTPMTIVENPQGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEETLSSLRFASRMKLVTTEPAINEKYDAERMVKNLEKELALLKQELAIHDSLTNRTFVTYDPMDEIQIAEINSQVRRYLEGTLDEIDIISLRQIKEVFNQFRVVLSQQEQEVESTLRRKYTLIDRNDFAAISAIQKAGLVDVDGHLVGEPEGQNFGLGVAPFSTKPGKKAKSKKTFKEPLSSLARKEGASSPVNGKDLDYVSTSKTQLVPSSKDGDVKDMLSRDRETSSIEPLPSDSPKEELRPIRPDTPPSKPVAFEEFKNEQGSEINRIFKENKSILNERRKRASETTQHINAIKREIDVTKEALNFQKSLREKQGKYENKGLMIIDEEEFLLILKLKDLKKQYRSEYQDLRDLRAEIQYCQHLVDQCRHRLLMEFDIWYNESFVIPEDMQMALKPGGSIRPGMVPVNRIVSLGEDDQDKFSQLQQRVLPEGPDSISFYNAKVKIEQKHNYLKTMMGLQQAHRK', 790, 'Q9HAQ2; Q86Z28; Q9H8A4;', 'KD00063', 'Homo sapiens (Human)', 'KIF9', '#Kinesin-like protein KIF9', '-', 'ENSG00000227398', '-'),
(64, 'Q07866', 'Kinesin light chain 1', 'GO:0003777', 65310, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity.', 'MYDNMSTMVYIKEDKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSNMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDTDSTKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGTSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPENMEKRRSRESLNVDVVKYESGPDGGEEVSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR', 573, 'Q07866; A6NF62; F8VTM4; Q7RTM2; Q7RTM3; Q7RTM5; Q7RTP9; Q7RTQ3;Q7RTQ5; Q7RTQ6; Q86SF5; Q86TF5; Q86V74; Q86V75; Q86V76; Q86V77;Q86V78; Q86V79; Q96H62;', 'KD00064', 'Homo sapiens (Human)', 'KLC1', '#Kinesin light chain 1#KLC 1', '-', 'ENSG00000126214', '-'),
(65, 'Q5RA78', 'Protein zwilch homolog', 'GO:0000777', 67186, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores (By similarity). {ECO:0000250}.', 'MWERLNCAAEDFYSRLLQKFNEEKKGIRKDPFLYEADVQVQLISKGQPNPLKNILNENDIVFIVEKVPLEKEETSHIEELQSEETAISDFSTGENVGPLALPVGKARQLIGLYTMAHNPNMTHLKINLPVTALPPLWVRCDSSDPEGTCWLGAELITTNNSITGIVLYVVSCKADKNYSVNLENLKNLHKKRHHLSTVTSKGFAQYELFKSSALDDTITASQTAIALDISWSPADEILQIPPLSSTATLNIKVESGEPRGPLNHLYRELKFLLVLADGLRTGVTEWLEPLEAKSAVELVQEFLNDLNKLDGFGDSTKKDTEVETLKHDTAAVDRSVKRLFKVRSDLDFAEQLWCKMSSSVISYQDLVKCFTLIIQSLQRGDIQPWLHSGSNSLLSKLIHQSYHGTMDTVSLSGTIPVQMLLEIGLDKLKKDYISFFIGQELASLNHLEYFIAPSVDIQEQVYRVQKLHHILEILVSCMPFIKSQHELLFSLTQICIKYYKQNPLDEQHIFQLPVRPTAVKNLYQSEKPQKWRVEIYSGQKKIKTVWQLSDSSPIDHLNFHKPDFSELTLNGSLEERIFFTNMVTCSQVHFK', 591, 'Q5RA78;', 'KD00065', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'ZWILCH', '#Protein zwilch homolog', '-', '-', '100172715'),
(66, 'Q9UGN5', 'Poly [ADP-ribose] polymerase 2', 'k', 66206, '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.', 'MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW', 583, 'Q9UGN5; Q8TEU4; Q9NUV2; Q9UMR4; Q9Y6C8;', 'KD00066', 'Homo sapiens (Human)', 'PARP2', '#Poly [ADP-ribose] polymerase 2#PARP-2#hPARP-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', '-', 'ENSG00000129484', '-'),
(67, 'B0BN28', 'Spindle and kinetochore-associated protein 1', 'GO:0000940', 29421, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis; when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it mediates the interaction with microtubules (By similarity). {ECO:0000250}.', 'MASDLEQLCSYVNEKIENIKKILSLRKLGQDPTLKTTLSKIGDEIITVNELLNQFELEIQYQEQTNSSLKELCKSLEEEFKDVEHLKEHIPSHLPQVTVTQSSTHKPDLDPKESVKAEEPVLPKKPPKEQRVIKEMHFITTDEFSGVPAYMKSRLTYCQINDVIKEINKAVVSKYKIIHQPKASMSSVKRNLYQRFINEETKDTKGRHFIVEADIKEFTTLKVDKKFHVIMNILRHCQRLSEVRGGGLTRYVIT', 254, 'B0BN28;', 'KD00067', 'Rattus norvegicus (Rat)', 'Ska1', '#Spindle and kinetochore-associated protein 1', '-', '-', '291441'),
(68, 'O96695', 'Rough deal protein', 'k', 240736, '', 'MWSNFEASSLEDETISNIFSSRGIFQISSEEEVNKYPDVMASVQCGKMVIGIDKSLLLLEDELVAKCSFLAFGAAIEAIAISSSGNLIVCGLSDGEVHGVFIKGLLLFSVAVNLEDVSLTGGTFRSIHQLDQRFYFTCKNGSIYSLSDIDETCLETLGNMSLNENETIACEKALLEDVTIQRLSKGRSSCSVDCAVLLKRLLTGNISAENNQDDLEAQPGLVITGDQSTMNFRNAANDVTRINLPAQYGSLKQIFNLEHYIIALTDSGHLVEICPYTRTVYMCQTTQQKNLLIEDLLVMECSEDNIELLVLTKSTAEGRFIKIVEYPTLNVKNEVEVPDHAWLVRHAKCAVNLYYLAAKEVNQSSIPSVVEMMLVSETDPSDRFKKLICKGRLEEAEEFGKQFELCLQPIYEAKAKRILVELCNSNSQNVDTKFQDLLQLLSQVESKAFIKSHRMINLNSRHILERYLHEVKKRLTFEDDEEDMLEIDEQLHRLKTLAIIDPYECNTDWQKFIYDNNLVRMVKSLFNTDMPTACLIWRRHSSSILPLLNEDELRTLLGFIPSNTKPFNVVQWLRQFIPMVSNTHPSIMPFITDWSIEMTRNLQYSPHWPDIGLEFCTKILDIFEEIQFTYSDVRRQQERNVGKLRDLVNALQDLSVLKTNYNMGFTLDNYMQDSIDATALSILQHVQLDKLQRLVKNFMYPIFQEKGRQPLDVIKQYISQLVASRLSSSSWLDRAMACIELLHNEDSRLECALSVLQNAPVPWPDTLAPLIRLRASTHPLAVKINAEYEIQVIKIMKVKYGWPADSSDINLELFMMRIVKLNLPDMLDDISALTKAAPELSTSANFNCCYQMARRGQVEMAYEFFKKLNGEKNSKSAKEVVEIMANILENSSSASFESDIKVQEHLNVLELFKLFLPHVESVYERRYLVIKHRFRLRKFGILLSCSSELIPLHRRHCLLDEAIERIIERAQATLNVSAFIASEISELCTALGLPKVFGLHRICQRIGCLPLSCALAYHVVSFVDCVPANAGEFVNLALELLVQQIESAKGKNQETASSLQLINENDPLSFYLAYELLASALLHESSRRHDLVELIKYIRVAVIHYPLDAIKSHYDGKEQAVNEHICRALDGISVALGETTINFSCALNGSFDVKTLTVPTTTKKRYSVSMFDEVEVQPIQQQPQKKSVGGRMAIVKFLARTLLLMVIETEPNNSLLMQVRNELPENTKADVESVCADFFLSLEHLTKVKEHDAWYVMSQYLLDFQKQNCRTKRIINEGFITLQLRRIFRNAMGSKDVNFIELFTMLVVDSEALALLEKLSVEVKTDLQKINFLTLSAMYHEHIEDLDSVQMIRTKRLKLFYYLEFCQQDHRIKGKFNADMDNIEDLLKEFHNKQLDVQLLERMSRLWVRLPKDSYYPDTKHIERPGVALRGEEGYFGDEELVMLSSAQEMRDMCQPYINEINNVELFTSKLKHFIEDINIYFYELYMCVINILMYFDSAPKEMEIWMNILHFLRHKMITRRRNRPGQVETDTWLKSQRENGVMPKISRYRLPFKPIVEQPLKDILDSELNVDNCQSWFPLIQMYTALKGSKDSSQNCDYFCMSAVKNSISEYKSKNDSESWSLHPTNNAFLQSILRLVEKVNNPNKAFLILYFVSNYARDGADQVEASYECWKFVKEKGHLITDPKSREQVAKVKRRYPIQKTQHLLYVYGLTDEKLLRQVENPTELIQALYHHELILKSSKVDINALVAEIAKLHDLCLATIQYRLLQKWLALTMESAGDGTILEETFMEEQNWPEQATAESSNSQDASENVNRAFYILSSWPKAEAVKFLVGLIFKGGSVNTSTQLQMYECYSKLNDGSNSFTNTISQRQFISIKCVHELKALGYKSNLEKFSDDHCNKIDILKMIWQRNAQNPLSLEVMANICLGFDIHLPQIWNGILKRMVMFHMVRDVNALLDVLSCRPHLLHLDGLAQAWDYVLCHPLQNAVELRSFKQEELLHKTLLRLQGCPVVHALNLLQFAQLCIVVHRPHMAASLLSFCQSSEQRQKIKKMIHSHPVENLRQQILDLEDAGILPVALNFALKELNLVSVEIWILLFP', 2098, 'O96695;', 'KD00068', 'Drosophila melanogaster (Fruit fly)', 'rod', '#Rough deal protein {ECO:0000313|EMBL:AAD12541.1}', '-', '-', '-'),
(69, 'O88777', 'Presenilin-2', 'GO:0000776', 50051, '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}.', 'MLTFMASDSEEEVCDERTSLMSAESPTSRSCQDSRPGPEDGENTAQWRSQENEDDCEEDPDHYACSGVPGRPSGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVFKTYNVAMDYPTLFLAVWNFGAVGMVCIHWKGPLVLQQAYLIVISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFGEPSYPEAFEAPQPGYPGEEPEEEEERGVKLGLGDFIFYSVLVGKAAATGNGDWSTTLACFIAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNLVRPFMDTLASHQLYI', 448, 'O88777; O08947; O35546;', 'KD00069', 'Rattus norvegicus (Rat)', 'Psen2', '#Presenilin-2#PS-2#3.4.23.-#Presenilin-2 NTF subunit#Presenilin-2 CTF subunit', '-', '-', '81751'),
(70, 'P87169', 'Spindle assembly checkpoint component mad1', 'GO:0000778===k', 79890, 'Central component of the spindle assembly checkpoint. Has a role in the correct positioning of the septum. Required for anchoring mad2 to the nuclear periphery. {ECO:0000269|PubMed:14592707}.', 'MSSKLTVYQATTSMADSPRDPFQSRSQLPRFLATSVKKPNLKKPSVNSANETKNPKLASLEFQLENLKNDLKRKELEFEREQIELQRKLAEEHEQKNSLQLRLTLVEKQLEEQSTSYQKEIEEVRNEKEATQVKIHELLDAKWKEIAELKTQIEKNDQALSEKNHEVMVSNQALQMKDTNLTNLEKLFADSREQLETKCKELAAAEQQLQELSVHNQQLEESIKQVSSSIELEKINAEQRLQISELEKLKAAQEERIEKLSSNNRNVEILKEEKNDLESKLYRFEEYRDKVATLELENEKIQTELNSWKSLITNELPTPEAVSNKLVFLQNTNANLGERVSSLESQLSNKPANQPLGANEKDAAHITELETKLKELHEQNRRLQRQKSLATQEIDLLRENLKSYDDEEAILSEKNTDMKKLERIEGLVKLVDEYKLKLESMPVSLDVDETSDEVSLQKRRRKNEHKDAGYVTELYRKNQHLLFQVKEKTNIEAFLREQIITLESSIATLRQELAQVTEINSCRVLQHRSNPTLKYERIKAAQLEMLNAENSALKALLEDKKVDCLPIQSFKIAERKALDLKKEVAEREKRIQRLKEIFSVKSLEFREAVFSLFGYKLDFMPNGSVRVTSTYSREDNTAFIFDGESSTMKLVGNPSGPEFERLIRFWCDERKTIPGMLAALTLELLDKND', 689, 'P87169;', 'KD00070', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mad1', '#Spindle assembly checkpoint component mad1#Mitotic arrest deficient protein 1', '-', '-', '2540320'),
(71, 'P38198', 'Protein STU1', 'GO:0000777===c;k', 174177, 'Microtubule binding protein that promotes the stabilization of dynamic microtubules. Required for separation of the spindle poles during mitotic spindle formation. May cross-link overlapping antiparallel microtubules in the spindle midzone. {ECO:0000269|PubMed:12058056; ECO:0000269|PubMed:7806575}.', 'MSSFNNETNNNSNTNTHPDDSFPLYTVFKDESVPIEEKMALLTRFKGHVKKELVNESSIQAYFAALLFISGHYAYRSYPRLIFLSHSSLCYLIKRVAMQSPVQFNDTLVEQLLNHLIFELPNEKKFWLASIKAIEAIYLVNPSKIQAILANFLRRPSENQNGDYLNRIKSTLLTIDELIQINEKNNSNHLQLLRFFMLSFTNLLNNNLNEHANDDNNNVIIELIFDIMYKYLKMDDENSQDLIDGFINDLEVEKFKQKFISLAKSQDQHGSQEDKSTLFDEEYEFQLLLAEAKLPQLSNNLSSKDPAMKKNYESLNQLQQDLENLLAPFQSVKETEQNWKLRQSNIIELDNIISGNIPKDNPEEFVTVIKEVQLIELISRATSSLRTTLSLTALLFLKRLIHILNDQLPLSILDQIFVIFKNLLSSTKKISSQTAFHCLITLIIDINHFHNKLFQLSFLLINEKTVTPRFCSAILLRSFLIKFNDSNLSLNNSNTTSPTSKLENNIIYIEEWLKKGISDSQTTVREAMRLTFWYFYKCYPTNAKRLLSSSFSPQLKKATELAIPAHLNINYQVSRVSSTASASSATSRLYSHSSNNSSRKTSLLEQKRNYPSYAQPTQSSSTSLLNAPAVTAGGSVIASKLSNKLKTNLRSTSEYSSKENEKRARHHDSMNSVSNSNTKDNNNVTKRKVSAPPSSTAATKVSENYTNFDDFPSNQIDLTDELSNSYSNPLIKKYMDKNDVSMSSSPISLKGSNKLGEYETLYKKFNDASFPAQIKDALQYLQKELLLTSQQSSSAPKFEFPMIMKKLRQIMIKSPNDFKPFLSIEKFTNGVPLNYLIELYSINSFDYAEILKNRMNPEKPYELTNLIITIADLFNFLNANNCPNDFKLYYMKYKTTFFNYNFKLLLEIFRNLNIKHDNTLRSGTNDLMPKISMILFQIYGKEFDYTCYFNLIFEIYKFDNNRFNKLLADFDIVSTKMKICHELEKKDANFKVEDIISRESSVSFTPIDNKKSEGDEESDDAVDENDVKKCMEMTMINPFKNLETDKTLELKNNVGKRTSSTDSVVIHDDNDKDKKLSEMTKIVSVYQLDQPNPAKEEDDIDMENSQKSDLNLSEIFQNSGENTERKLKDDNEPTVKFSTDPPKIINEPEKLIGNGNENEKPDLETMSPIKINGDENMGQKQRITVKRERDVALTEQDINSKKMKLVNNKKSEKMHLLIMDNFPRDSLTVYEISHLLMVDSNGNTLMDFDVYFNHMSKAINRIKSGSFTMKHINYLIEPLITCFQNQKMTDWLTNENGFDELLDVAIMLLKSTDDTPSIPSKISSKSIILVHCLLVWKKFLNTLSENADDDGVSVRMCFEEVWEQILLMLNKFSDYGNEIYKLAQEFRDSLMLSHFFKKHSATRILSMLVTEIQPDTAGVKETFLIETLWKMLQSPTICQQFKKSNISEIIQTMSYFIMGTDNTSWNFTSAVVLARCLRVLQTTPDYTEQETERLFDCLPKNVFKMIMFIASNE', 1513, 'P38198; D6VPW5;', 'KD00071', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'STU1', '#Protein STU1#Suppressor of tubulin 1', '-', '-', '852246'),
(72, 'Q13416', 'Origin recognition complex subunit 2', 'GO:0000939===c;k', 65972, 'Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre- replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3; H3K20me3 and H4K27me3. Stabilizes LRWD1; by protecting it from ubiquitin- mediated proteasomal degradation. Also stabilizes ORC3. {ECO:0000269|PubMed:22427655; ECO:0000269|PubMed:22935713}.', 'MSKPELKEDKMLEVHFVGDDDVLNHILDREGGAKLKKERAQLLVNPKKIIKKPEYDLEEDDQEVLKDQNYVEIMGRDVQESLKNGSATGGGNKVYSFQNRKHSEKMAKLASELAKTPQKSVSFSLKNDPEITINVPQSSKGHSASDKVQPKNNDKSEFLSTAPRSLRKRLIVPRSHSDSESEYSASNSEDDEGVAQEHEEDTNAVIFSQKIQAQNRVVSAPVGKETPSKRMKRDKTSDLVEEYFEAHSSSKVLTSDRTLQKLKRAKLDQQTLRNLLSKVSPSFSAELKQLNQQYEKLFHKWMLQLHLGFNIVLYGLGSKRDLLERFRTTMLQDSIHVVINGFFPGISVKSVLNSITEEVLDHMGTFRSILDQLDWIVNKFKEDSSLELFLLIHNLDSQMLRGEKSQQIIGQLSSLHNIYLIASIDHLNAPLMWDHAKQSLFNWLWYETTTYSPYTEETSYENSLLVKQSGSLPLSSLTHVLRSLTPNARGIFRLLIKYQLDNQDNPSYIGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGTDGVEYLLIPVDNGTLTDFLEKEEEEA', 577, 'Q13416; Q13204; Q53TX5;', 'KD00072', 'Homo sapiens (Human)', 'ORC2', '#Origin recognition complex subunit 2', '-', 'ENSG00000115942', '-'),
(73, 'Q10290', 'Chromosome segregation protein mal2', 'GO:0034508===GO:0000779===k', 34515, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. Has a role in the maintenance of core chromatin structure and kinetochore function. Required for the localization of mis6 and cnp1 to the kinetochore. Required for the establishment of a functional centromere where it has a role in silencing. Also has a role in regulating metaphase spindle length. {ECO:0000269|PubMed:12242294; ECO:0000269|PubMed:16079914; ECO:0000269|PubMed:8887647}.', 'MDDEEGNATLIDEISVLEARRDVLLDELKSLDNATLSDLVQKPELSKNLSVNNEFLKETPLNQPALHYDRLSGISFFQPNDPEELSRKTLLVKNKKTGAIETAPSIPLLGVRFDIMLNPVNIGFTNLSENPISSASGMDEELEGGNRFDVPYYIIFRVFHDSFALYKYTIPSFLNIQEWADEYLTGKNPERFRIFLWKVDKLLTAYICRKNALLQINKSLTIDGTNISANLSCTHLVIQIPKVIQATLVCSSESTRVVKSRIYQYSDENWKRDHRLELSLLDNKRWVNILVSHLTAPESHASL', 303, 'Q10290;', 'KD00073', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mal2', '#Chromosome segregation protein mal2#Sim4 complex subunit mal2', '-', '-', '2542737');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(74, 'Q6P8A1', 'Kinetochore protein spc24', 'GO:0000777===GO:0031262', 22870, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MLCEQIKEYVDVSREIVKVMVSDSAAVALKKSLDRQEAMIDLLLDTETEASQLIRDFMAVEEKVAQTLLDTEETKQKTSSKLQKIERELQEKIEKNSSLESGIKFLQKELEELKMMEEEIADMEREADEDTTTVIPSAVYLAKLFHNVTKIDWDYNCDPSLIKGIHYGGEIAQPISIDSNQHSKIFICNYLWSLLSTDW', 199, 'Q6P8A1;', 'KD00074', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'spc24', '#Kinetochore protein spc24', '-', '-', '394654'),
(75, 'Q9NCG0', 'Kinesin-like protein', 'k', 257994, '', 'MSAKNASSIQVCIKVRPCEPGLTSLWQVKEGRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMARHIVHACMQGFNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSIMEESQSTLSFATRAKKIRIKPQVNEMVSDATMMKRLEREIKVLKDKLAEEERKNENQQKVEHLERQIKHDMHKIICGHSLSDKGQQKRRRTWCPTASGSHLELAETGTTEDRIDQFPKVSHLPKPVFFHTSNAGKRWDNIPKTINILGSLDIGTESNSISEEFLPAECIDFGSPRPDVLKPMLTIRQLPDLPLTPKGPLTTDKIKKEIQDLQMFTSLEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSIAPEQEDVAGDSICNKCEELEKLIADLESKKNSCECDQLRLEIVSVRDKLESVESAFNLASSGIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHNEHEHVQEIYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLFNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQFVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLNAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRRISVHDERRQSYWNDVREFGIMTDPVGMSSCSVFPLVFPLNESNFRQHNCNCAELNSKLQDCQRELFIRESQVTALKMELDHHPLKDENAQLTKRVIEEQDKAKVEQKRLKMKLQDLNARINDLTTASAKEPESNQMAQAAKPATVAAQTQTESDLETILEKTNVKYEEAVRMLRYRYNLIQELKEKLRQNENSDTSNITSLSAGQTSALKVAISNRYSSSSYIKYCFCRHSVSPKRRKFWQSNISMKPPSEFWRFEMMIWMLCGKNSRNMKQLHQINKSLGIIFVYICVCVWA', 2244, 'Q9NCG0;', 'KD00075', 'Drosophila melanogaster (Fruit fly)', 'cmet', '#Kinesin-like protein {ECO:0000256|RuleBase:RU000394}', '-', '-', '-'),
(76, 'Q91912', 'Mothers against decapentaplegic homolog', 'k', 52411, '', 'MSSILPFTPPVVKRLLGWKKSASGTTGAGGDEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTANTIDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPSTLSPVNHNLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS', 467, 'Q91912;', 'KD00076', 'Xenopus laevis (African clawed frog)', 'Mad2', '#Mothers against decapentaplegic homolog {ECO:0000256|RuleBase:RU361195}#MAD homolog {ECO:0000256|RuleBase:RU361195}#Mothers against DPP homolog {ECO:0000256|RuleBase:RU361195}#SMAD family member {ECO:0000256|RuleBase:RU361195}', '-', '-', '-'),
(77, 'Q91913', 'Mothers against decapentaplegic homolog', 'k', 52264, '', 'MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEYPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLEPSEPHMPHNATFPDSFQQPNSHPFPHSPNSSYPNSPGSGSTYPHSPASSDPGSPFQIPADTPPPAYMPPEDQMTQDNSQPMDTNLMVPNISQDINRADVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNRNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNFHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAECHRQNVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS', 464, 'Q91913;', 'KD00077', 'Xenopus laevis (African clawed frog)', 'Mad1', '#Mothers against decapentaplegic homolog {ECO:0000256|RuleBase:RU361195}#MAD homolog {ECO:0000256|RuleBase:RU361195}#Mothers against DPP homolog {ECO:0000256|RuleBase:RU361195}#SMAD family member {ECO:0000256|RuleBase:RU361195}', '-', '-', '-'),
(78, 'A1CH27', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 34309, 'Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). {ECO:0000250}.', 'MNSLVATPPVPPHFYEHSRFSSPHPMSNPIHTPSSRKRKADDDGNDHDGRMSASPTNSPAFTPRSLPTPRSFKRSRPNVFGRPLSLPRLLETLDTDALRGILRSMCERHPALADEVIHTSPRPSVTSALQVLRNYQTALQNSFPLGGNPESDYAYNRVRQPLGNLLDALSDFTPHFLPPNESQASVSLSYLDGATEIIHALPRWNSPQNNIERDSAYDEICKAWVLVIREAAKRGGGIQLQYGGWDQKLSKHNHNSGGRLQAAVNELGNSLGWMHGPDSQGYSSPAAGDLGSIRDQLLSGTYGLGTPVKVGPW', 313, 'A1CH27;', 'KD00078', 'Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCT3887 / NRRL 1)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '4704315'),
(79, 'P0CH66', 'Putative uncharacterized protein UM10309', 'GO:0034508', 64705, '', 'MILQPSSSKSKLTSHQDHHLVPHSISLRRLLSRLDKSELVSLVTRWLDNAGPSYIPPMLSRRQPKAGQEDSVTNLTLYHAILDLNEERRCRSMDELRLLWTGPMSDPRVPKARALDRISDVDWPEGLSYAMVAELDLFYAHARQLSKTWSTVKLEYDDDVDAAGRGWERLSETQIRLRLGNELGHYFEHHIYLHPRVKPEDRNAAAVRSWTDSFSYFRIVLAPIPSDVCGTGLHILHLPRTPFLLVSGSLGRGSENREMALSAFAAAAGATTVNYAKPAAGSAAAKKLLAELNDAGEDAAGNRRTLGELRGKDPLALREILLHESGRLSSTSDASAAPAGVAGGGKARQMQFSQGGSGQGAEDGPLIAPLKRRREEDLSLLGIRPPTPPASGSERDTVSLSSASTSARPTQRRSSLTPCSQTPQETHQHAREALTTRMESQREANELFGPKPNPYDPSNDALPRVERIEYELHLPFPAMQRYNTRSLIDMDAYNSDPEKPKIKLRLEGTHVLAGLRKLVAAGMDRSTSRLDAGEGQGDDDDEEDGQAEKYEGAVKPVKLDGLPGWLTEVRGTKVVVQPSPPGDDSSRDM', 589, 'P0CH66; Q4PB42;', 'KD00079', 'Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)', 'UMAG_10309', '#Putative uncharacterized protein UM10309', '-', '-', '3630713'),
(80, 'Q8NG31', 'Protein CASC5', 'GO:0000777===GO:0034501===GO:0008608===k', 265391, 'Performs two crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Required for attachment of the kinetochores to the spindle microtubules. Directly links 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. {ECO:0000269|PubMed:15502821; ECO:0000269|PubMed:17981135; ECO:0000269|PubMed:18045986}.', 'MDGVSSEANEENDNIERPVRRRHSSILKPPRSPLQDLRGGNERVQESNALRNKKNSRRVSFADTIKVFQTESHMKIVRKSEMEGCSAMVPSQLQLLPPGFKRFSCLSLPETETGENLLLIQNKKLEDNYCEITGMNTLLSAPIHTQMQQKEFSIIEHTRERKHANDQTVIFSDENQMDLTSSHTVMITKGLLDNPISEKSTKIDTTSFLANLKLHTEDSRMKKEVNFSVDQNTSSENKIDFNDFIKRLKTGKCSAFPDVPDKENFEIPIYSKEPNSASSTHQMHVSLKEDENNSNITRLFREKDDGMNFTQCHTANIQTLIPTSSETNSRESKGNDITIYGNDFMDLTFNHTLQILPATGNFSEIENQTQNAMDVTTGYGTKASGNKTVFKSKQNTAFQDLSINSADKIHITRSHIMGAETHIVSQTCNQDARILAMTPESIYSNPSIQGCKTVFYSSCNDAMEMTKCLSNMREEKNLLKHDSNYAKMYCNPDAMSSLTEKTIYSGEENMDITKSHTVAIDNQIFKQDQSNVQIAAAPTPEKEMMLQNLMTTSEDGKMNVNCNSVPHVSKERIQQSLSNPLSISLTDRKTELLSGENMDLTESHTSNLGSQVPLAAYNLAPESTSESHSQSKSSSDECEEITKSRNEPFQRSDIIAKNSLTDTWNKDKDWVLKILPYLDKDSPQSADCNQEIATSHNIVYCGGVLDKQITNRNTVSWEQSLFSTTKPLFSSGQFSMKNHDTAISSHTVKSVLGQNSKLAEPLRKSLSNPTPDYCHDKMIICSEEEQNMDLTKSHTVVIGFGPSELQELGKTNLEHTTGQLTTMNRQIAVKVEKCGKSPIEKSGVLKSNCIMDVLEDESVQKPKFPKEKQNVKIWGRKSVGGPKIDKTIVFSEDDKNDMDITKSYTIEINHRPLLEKRDCHLVPLAGTSETILYTCRQDDMEITRSHTTALECKTVSPDEITTRPMDKTVVFVDNHVELEMTESHTVFIDYQEKERTDRPNFELSQRKSLGTPTVICTPTEESVFFPGNGESDRLVANDSQLTPLEEWSNNRGPVEVADNMELSKSATCKNIKDVQSPGFLNEPLSSKSQRRKSLKLKNDKTIVFSENHKNDMDITQSCMVEIDNESALEDKEDFHLAGASKTILYSCGQDDMEITRSHTTALECKTLLPNEIAIRPMDKTVLFTDNYSDLEVTDSHTVFIDCQATEKILEENPKFGIGKGKNLGVSFPKDNSCVQEIAEKQALAVGNKIVLHTEQKQQLFAATNRTTNEIIKFHSAAMDEKVIGKVVDQACTLEKAQVESCQLNNRDRRNVDFTSSHATAVCGSSDNYSCLPNVISCTDNLEGSAMLLCDKDEEKANYCPVQNDLAYANDFASEYYLESEGQPLSAPCPLLEKEEVIQTSTKGQLDCVITLHKDQDLIKDPRNLLANQTLVYSQDLGEMTKLNSKRVSFKLPKDQMKVYVDDIYVIPQPHFSTDQPPLPKKGQSSINKEEVILSKAGNKSLNIIENSSAPICENKPKILNSEEWFAAACKKELKENIQTTNYNTALDFHSNSDVTKQVIQTHVNAGEAPDPVITSNVPCFHSIKPNLNNLNGKTGEFLAFQTVHLPPLPEQLLELGNKAHNDMHIVQATEIHNINIISSNAKDSRDEENKKSHNGAETTSLPPKTVFKDKVRRCSLGIFLPRLPNKRNCSVTGIDDLEQIPADTTDINHLETQPVSSKDSGIGSVAGKLNLSPSQYINEENLPVYPDEINSSDSINIETEEKALIETYQKEISPYENKMGKTCNSQKRTWVQEEEDIHKEKKIRKNEIKFSDTTQDREIFDHHTEEDIDKSANSVLIKNLSRTPSSCSSSLDSIKADGTSLDFSTYRSSQMESQFLRDTICEESLREKLQDGRITIREFFILLQVHILIQKPRQSNLPGNFTVNTPPTPEDLMLSQYVYRPKIQIYREDCEARRQKIEELKLSASNQDKLLVDINKNLWEKMRHCSDKELKAFGIYLNKIKSCFTKMTKVFTHQGKVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQLSLSEWDVVEWSDDQAVFTFVYDTIQLTITFEESVVGFPFLDKRYRKIVDVNFQSLLDEDQAPPSSLLVHKLIFQYVEEKESWKKTCTTQHQLPKMLEEFSLVVHHCRLLGEEIEYLKRWGPNYNLMNIDINNNELRLLFSSSAAFAKFEITLFLSAYYPSVPLPSTIQNHVGNTSQDDIATILSKVPLENNYLKNVVKQIYQDLFQDCHFYH', 2342, 'Q8NG31; Q8NHE1; Q8WXA6; Q9HCK2; Q9NR92;', 'KD00080', 'Homo sapiens (Human)', 'CASC5', '#Protein CASC5#ALL1-fused gene from chromosome 15q14 protein#AF15q14#Bub-linking kinetochore protein#Blinkin#Cancer susceptibility candidate gene 5 protein#Cancer/testis antigen 29#CT29#Kinetochore-null protein 1#Protein D40/AF15q14', '-', 'ENSG00000137812', '-'),
(81, 'O54692', 'Centromere/kinetochore protein zw10 homolog', 'GO:0000776===GO:0000777===GO:0005828===GO:0034501===k', 88063, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (By similarity). {ECO:0000250}.', 'MASFVTEVLAHSGSLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPTMQSAQALVTQVDTLSNDIDQLKSRIETEVCRDLHISTVEFTNLKQQLERDSVVLTLLKQLQEFSSAIEEYNSALAEKKYIPAARHLEEAQECLKLLKSRKCFDLKMLKSLSMELTVQKQNILYHLGEDWQKLVVWKFPPAKDTSSLESCLQTELHLCTEQPEKEDMTPLPSISSVLLAFSILGELPTKLKSFGQMLLKYILKPLVTCPSLHAVIERQPSSVSICFESLTTDLEHPSPPEAFAKIRLVLEVLQKQLLDLPLDADLEIGKVPGIVLAEMLGEGIWEDLSECLIRNCLVYSIPTNSSKLQEYEEIIQSTEEFEKFLKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARNLMTSEIHNTVKIGPDCKEALPDLPSPDADHKLQVQTVCKAQFTDAGNLEPETSLDPQSFSLPTCRISEAVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLRKLPQLAAIHHNNCMYIAHHLLTLGHQFRLRLAPILCDGTTTFVDLVPGFRRLGTECFLAQMQAQKGELLERLSSARSFANMDDEENYSAASKAVRQVLHQLRRLGIVWQDVLPVNIYCKAMGTLLNTAIAEMMSRITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSDENKNKKYQEEVPVYVSKWMPFKELMIMLQASLQEIGDRWADGKGPLATAFPSSEVKALIRALFQNTERRAAALAKIK', 779, 'O54692; Q3TIA5; Q3ULW1; Q921H3;', 'KD00081', 'Mus musculus (Mouse)', 'Zw10', '#Centromere/kinetochore protein zw10 homolog', '-', '-', '26951'),
(82, 'Q9UQB9', 'Aurora kinase C', 'GO:0008608===GO:0032133===GO:0000780', 35591, 'Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB; AURKC phosphorylates histone H3 at ''Ser-10'' and ''Ser-28''. Phosphorylates TACC1; another protein involved in cell division; at ''Ser-228''. {ECO:0000269|PubMed:15316025; ECO:0000269|PubMed:15499654; ECO:0000269|PubMed:15670791; ECO:0000269|PubMed:15938719; ECO:0000269|PubMed:21493633; ECO:0000269|PubMed:21531210}.', 'MSSPRAVVQLGKAQPAGEELATANQTAQQPSSPAMRRLTVDDFEIGRPLGKGKFGNVYLARLKESHFIVALKVLFKSQIEKEGLEHQLRREIEIQAHLQHPNILRLYNYFHDARRVYLILEYAPRGELYKELQKSEKLDEQRTATIIEELADALTYCHDKKVIHRDIKPENLLLGFRGEVKIADFGWSVHTPSLRRKTMCGTLDYLPPEMIEGRTYDEKVDLWCIGVLCYELLVGYPPFESASHSETYRRILKVDVRFPLSMPLGARDLISRLLRYQPLERLPLAQILKHPWVQAHSRRVLPPCAQMAS', 309, 'Q9UQB9; O60681; O75442; Q6AZY8; Q6DLZ0; Q9UPK5;', 'KD00082', 'Homo sapiens (Human)', 'AURKC', '#Aurora kinase C#2.7.11.1#Aurora 3#Aurora/IPL1-related kinase 3#ARK-3#Aurora-related kinase 3#Aurora/IPL1/Eg2 protein 2#Serine/threonine-protein kinase 13#Serine/threonine-protein kinase aurora-C', '-', 'ENSG00000105146', '-'),
(83, 'O75037', 'Kinesin-like protein KIF21B', 'GO:0003777', 182662, 'Microtubule-binding motor protein probably involved in neuronal dendritic transport. In vitro; has a plus-end directed motor activity (By similarity). {ECO:0000250}.', 'MAGQGDCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDSTRDPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVNEAVTGLPDGTPPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDKTSQQISALRAEIARLQMELMEYKAGKRVIGEDGAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKAEAHPELQALIYNVQQENGYASTDEEISEFSEGSFSQSFTMKGSTSHDDFKFKSEPKLSAQMKAVSAECLGPPLDISTKNITKSLASLVEIKEDGVGFSVRDPYYRDRVSRTVSLPTRGSTFPRQSRATETSPLTRRKSYDRGQPIRSTDVGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDKSDDSDSSLSEVLRGIISPVGGAKGARTAPLQCVSMAEGHTKPILCLDATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSTSYIKVWDIRDSAKCIRTLTSSGQVISGDACAATSTRAITSAQGEHQINQIALSPSGTMLYAASGNAVRIWELSRFQPVGKLTGHIGPVMCLTVTQTASQHDLVVTGSKDHYVKMFELGECVTGTIGPTHNFEPPHYDGIECLAIQGDILFSGSRDNGIKKWDLDQQELIQQIPNAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAICTNAKHIFTASSDCRVKLWNYVPGLTPCLPRRVLAIKGRATTLP', 1637, 'O75037; B2RP62; B7ZMI0; Q5T4J3;', 'KD00083', 'Homo sapiens (Human)', 'KIF21B', '#Kinesin-like protein KIF21B', '-', 'ENSG00000116852', '-'),
(84, 'Q9NCF9', 'Kinesin-like protein', 'k', 221863, '', 'MSTKNASSIQVCIKVRPCEPGLTSLWQVKEGRSIQLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNGIVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSDHSDNDTVKQSVLSLVDLAGSEQVDPADHASSLMIFRNLVKSLSESVDSKPNSFRDSKLPRIMLPSLGGNVLTSIICTITPSFVEESSSTISFGTCAKKIRCKPQVCKIDSETTMMRQLDRGISMLKDKLAKKKIKNESQLVLQELEGRIKRDMLKIVSSASLDDYRLQKRRRTWTLTASGSEGDAPVLALPEPEESRLPRPSKLTNLPKPLFQRRGIAPKAKGICKTLKEKRLQTDNMDTMPGRAKQLGRETASRIPSVMMSKKYQESVPNCDAPQTEISALTASNQVAKETIEKYEEQVKRLKETIERLEMENGKAVNLGEQFETHKAKSKQMEEELLSSISEKDSTIVSLQQSLEELSRDVLRNSKEDQMRSMCPELESSCERICNKCLELERLLPLASASGLDSVACQFDQLRSEIAATRMKLESMLSTFSHASCEVSQKTTDCKRLSEQISTAHDDFGQLQEKYNNLKHKWSSQKLAIDTMQVDYNTIQQKYLQLQDEYRHLELRSDEQCQQLQDENSKLQAEIGTLKERVEEIHSELLEVPNPDTHPEDMELQNQELKKRLSKLQWEFDEIQLNYECLSNELMSTIQECDALREEHKQRTTNSDLESMKSSGVGTECSDPENELDTDLLQQFTKLSKSIQQIELTDYSGGRRLFIYNHAEQDQSVPSLKLCLEPAKYLEGDGKQHDASDSVFLKGFLKCQRFQIVKINQEQNLVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQIETIKNQNAKTKILCEELQTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSSDLLPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENTTVREAKVGLENSLKAVQENMSAQESQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDRQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALNEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFKSLQKAWIKQSLAIEAANKRSLEMEQMVDKRTREYEELRSTLKTREINFRSEKERMDGTISSLLEDKRNLEEKLCTVTELLAKLKRELPALHTQKVNGGDVSIELNSSNGSPTPAAVPATKKPLDCNSAECVPKKSSSLETAERKNRRMTAYDENRKQFC', 1931, 'Q9NCF9;', 'KD00084', 'Drosophila melanogaster (Fruit fly)', 'cana', '#Kinesin-like protein {ECO:0000256|RuleBase:RU000394}', '-', '-', '-'),
(85, 'Q7SXI6', 'Nuclear distribution protein nudE-like 1-A', 'GO:0000776', 38629, 'Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end (By similarity). {ECO:0000250}.', 'MDADMIPKFTTKEEEIDFWKALSLKYKKSYKEAQEELLEFQEGSRELETELETQLGQAEHRIRDLQADNQRLQHELDSLKEKLEYQYAQSYKQISVLEDDLSQTRGIKEQLHKYVRELEQANDDLERAKRATITSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRDTRSEVTRMSAPSSPTPDNDKTDSAVQASLSLPATPLSKNLDNAFTSQTVLANGSTNAALTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQAARKNYVTNVNGNLINGDISNYSHSLHTSYFDKARTVNGLDPGDGTHITAPPRSNSPSGLVLSV', 344, 'Q7SXI6;', 'KD00085', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'ndel1a', '#Nuclear distribution protein nudE-like 1-A', '-', '-', '394244'),
(86, 'Q6Q137', 'Septin-7', 'GO:0000777', 50680, 'Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements (By similarity). {ECO:0000250}.', 'MSVSARSAAAEERSVNSSTMVAQQKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKIF', 437, 'Q6Q137;', 'KD00086', 'Bos taurus (Bovine)', 'SEPT7', '#Septin-7#CDC10 protein homolog', '-', '-', '408000'),
(87, 'P80428', 'Actin-related protein 4', 'GO:0051382', 54832, '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. ARP4 recognizes H2AS128ph (gamma-H2A) and 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. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to gamma-H2A as a response to DNA damage. {ECO:0000269|PubMed:10911987; ECO:0000269|PubMed:10952318; ECO:0000269|PubMed:11937627; ECO:0000269|PubMed:12353039; ECO:0000269|PubMed:14622406; ECO:0000269|PubMed:14645854; ECO:0000269|PubMed:14690608; ECO:0000269|PubMed:15045029; ECO:0000269|PubMed:15610740}.', 'MSNAALQVYGGDEVSAVVIDPGSYTTNIGYSGSDFPQSILPSVYGKYTADEGNKKIFSEQSIGIPRKDYELKPIIENGLVIDWDTAQEQWQWALQNELYLNSNSGIPALLTEPVWNSTENRKKSLEVLLEGMQFEACYLAPTSTCVSFAAGRPNCLVVDIGHDTCSVSPIVDGMTLSKSTRRNFIAGKFINHLIKKALEPKEIIPLFAIKQRKPEFIKKTFDYEVDKSLYDYANNRGFFQECKETLCHICPTKTLEETKTELSSTAKRSIESPWNEEIVFDNETRYGFAEELFLPKEDDIPANWPRSNSGVVKTWRNDYVPLKRTKPSGVNKSDKKVTPTEEKEQEAVSKSTSPAANSADTPNETGKRPLEEEKPPKENNELIGLADLVYSSIMSSDVDLRATLAHNVVLTGGTSSIPGLSDRLMTELNKILPSLKFRILTTGHTIERQYQSWLGGSILTSLGTFHQLWVGKKEYEEVGVERLLNDRFR', 489, 'P80428; D6VWA2;', 'KD00087', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'ARP4', '#Actin-related protein 4#Actin-like protein ARP4#Actin-like protein 4', '-', '-', '853364'),
(88, 'Q13409', 'Cytoplasmic dynein 1 intermediate chain 2', 'GO:0003777===GO:0005868===c;k;m', 71457, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150- glued) DCNT1. Involved in membrane-transport; such as Golgi apparatus; late endosomes and lysosomes.', 'MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTPESPIVFSEYWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSVLQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNADYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA', 638, 'Q13409; B7ZA04; D3DPD4; D3DPD5; D3DPD6; Q32LY9; Q53S84; Q5BJF8;Q7Z4X1; Q96NG7; Q96S87; Q9BXZ5; Q9NT58;', 'KD00088', 'Homo sapiens (Human)', 'DYNC1I2', '#Cytoplasmic dynein 1 intermediate chain 2#Cytoplasmic dynein intermediate chain 2#Dynein intermediate chain 2; cytosolic#DH IC-2', '-', 'ENSG00000077380', '-'),
(89, 'Q32LL9', 'Centromere protein N', 'GO:0000777===GO:0034508', 39411, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate (By similarity). {ECO:0000250}.', 'MDETLAEFFRRTILKIPMTEMMTILKTWNFMSENQLQTVNFRQRKESIVQDLVLLCEENHASLNDAAHLDIIYTQFHRHQKIWDVFQMSKAPGDDIDLFDMEQFKSSFKKILQRALKNVTVSFRDAEENSVWIRIAWGTQYKKPNQYKPAYVVYYSQTPYAFTSSSRLKSNLPLLGQALTVASKHHQIVKMDLRSRYLDSLKAIVFKQYNQSFETHNCTTSLQEGSLGLDINMDSRIIHENKVEKERVQRVTQEIFGDYPQPRLEFAQYKLETKFKSDLNGGILAEREEPLRCLVKFSSPHLLEALKSLAPAGIADAPLSPLLTCIPNKGKNYFKIRDK', 339, 'Q32LL9;', 'KD00089', 'Bos taurus (Bovine)', 'CENPN', '#Centromere protein N#CENP-N', '-', '-', '513551'),
(90, 'B3DLE8', 'Protein Spindly', 'GO:0043515===GO:0034501===GO:0000940', 70708, 'Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. {ECO:0000255|HAMAP-Rule:MF_03041}.', 'MEESETVLKLRLQLKEAEEERIKAAQYGLELLESQSDLQNQLEEQRNEMTSTIENLEQEKYSLQREVELKNRMLESLTSECENIRQQQKLCLEQLQEQLERNHHRELSEIKDKLEKLKAELDEARLSEKQLKHKLEYQSEVLANKSEELRMMSERVHETMSSEMLTLQLEKTELESAKANLEQEVNELQYREQQLLLTNGTQSRQLERLQDEKEDREKEAVGYFKALEKAREANQDLQAQLDIALQQAQDPNSKGNSLFAEVEDRRAEMERQLISMKVQFQSLQKQHAFSRQQMHRMKVQIATLLQLKGSQSDPEQLERLQAMVAQKNSEFETLVMKVRQLEKSQQICENGPVANSSDGLGQGDETYYVDLLKMKLVNSSKEIEKIKDELSLQRMKALAESQRVLDLERKLFANDRHLKLSQGENMKLRVNLDEMKMKYEPDEIAKIRTQKRRKEQLPLDCAIDNTSATVTSGSQAHGLSDAIPEDMCPAESTVHRNLLKEDSSLSTKEQDLSSVAVKPIEPANGQPPKERKRVRIVENENDNQDINKRNTNNCSVTSTSPRSASEESTSESKRFDEEQEKRKQERKSRLRAPPVLHVPSKPAATTQCPQQ', 611, 'B3DLE8;', 'KD00090', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'spdl1', '#Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041}#Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041}#Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041}', '-', '-', '100170491'),
(91, 'Q6QLM7', 'Kinesin heavy chain isoform 5A', 'GO:0003777', 116916, 'Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH; NFM and NFL). {ECO:0000250|UniProtKB:P33175}.', 'MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVIIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVRGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENIETEQKLSGKLYLADLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEDSALAAEICEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKEEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESEPQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQTVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDAEEVKKALELQMENHREAHHRQLARLRDEINEKQKTIDELKDLDQKLQLELEKLQADYERLKNEENEKSAKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTEVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNNLFQNYQNLHLQAAPSSTSDVYFASNGATSVAPLASYQKANTDNGNATDINDNRSDLPCGYEAEDPAKLFPLHQETAAS', 1027, 'Q6QLM7;', 'KD00091', 'Rattus norvegicus (Rat)', 'Kif5a', '#Kinesin heavy chain isoform 5A#Kinesin heavy chain neuron-specific 1#Neuronal kinesin heavy chain#NKHC', '-', '-', '314906'),
(92, 'Q874J6', 'Histone H3-like centromeric protein CSE4', 'GO:0000777', 28186, '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}.', 'MSTRQAVFERDVDEDRWPRSARGLAGVNTVFEGDSEINSKAMRLLEKTRHRRNLLNRREDRRRYLGGVKAKAIESDYYHRNQLPSSYDAGNDDFEPINNSHVESEEENKRLPEKYSLDKYVKRSRKQRDHRHIVAKPKEKRNFAPSKLAMYEIEKYQRSTALLIQKIPFAKLVKEVTEEFAGESQDLRWQSMAILALQEASEAYLVGLLEHTNLLALHAKRITIMKKDMQLARRIRGQFI', 240, 'Q874J6; Q6FIM9;', 'KD00092', 'Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622NRRL Y-65) (Yeast) (Torulopsis glabrata)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog', '-', '-', '2891205'),
(93, 'Q9NSK0', 'Kinesin light chain 4', 'GO:0003777', 68640, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity). {ECO:0000250}.', 'MSGLVLGQRDEPAGHRLSQEEILGSTRLVSQGLEALRSEHQAVLQSLSQTIECLQQGGHEEGLVHEKARQLRRSMENIELGLSEAQVMLALASHLSTVESEKQKLRAQVRRLCQENQWLRDELAGTQQRLQRSEQAVAQLEEEKKHLEFLGQLRQYDEDGHTSEEKEGDATKDSLDDLFPNEEEEDPSNGLSRGQGATAAQQGGYEIPARLRTLHNLVIQYAAQGRYEVAVPLCKQALEDLERTSGRGHPDVATMLNILALVYRDQNKYKEAAHLLNDALSIRESTLGPDHPAVAATLNNLAVLYGKRGKYKEAEPLCQRALEIREKVLGTNHPDVAKQLNNLALLCQNQGKYEAVERYYQRALAIYEGQLGPDNPNVARTKNNLASCYLKQGKYAEAETLYKEILTRAHVQEFGSVDDDHKPIWMHAEEREEMSKSRHHEGGTPYAEYGGWYKACKVSSPTVNTTLRNLGALYRRQGKLEAAETLEECALRSRRQGTDPISQTKVAELLGESDGRRTSQEGPGDSVKFEGGEDASVAVEWSGDGSGTLQRSGSLGKIRDVLRRSSELLVRKLQGTEPRPSSSNMKRAASLNYLNQPSAAPLQVSRGLSASTMDLSSSS', 619, 'Q9NSK0; B3KNY4; B3KPI3; B3KSQ3; B4DME9; Q66K28; Q96EG6;', 'KD00093', 'Homo sapiens (Human)', 'KLC4', '#Kinesin light chain 4#KLC 4#Kinesin-like protein 8', '-', 'ENSG00000137171', '-'),
(94, 'Q96DY7', 'Mdm2-binding protein', 'GO:0000776===GO:0034501', 102193, 'Inhibits cell migration in vitro and suppresses the invasive behavior of tumor cells (By similarity). May play a role in MDM2-dependent p53/TP53 homeostasis in unstressed cells. Inhibits autoubiquitination of MDM2; thereby enhancing MDM2 stability. This promotes MDM2-mediated ubiquitination of p53/TP53 and its subsequent degradation. {ECO:0000250; ECO:0000269|PubMed:15632057}.', 'MDRYLLLVIWGEGKFPSAASREAEHGPEVSSGEGTENQPDFTAANVYHLLKRSISASINPEDSTFPACSVGGIPGSKKWFFAVQAIYGFYQFCSSDWQEIHFDTEKDKIEDVLQTNIEECLGAVECFEEEDSNSRESLSLADLYEEAAENLHQLSDKLPAPGRAMVDIILLLSDKDPPKLKDYLPTVGALKHLREWYSAKITIAGNHCEINCQKIAEYLSANVVSLEDLRNVIDSKELWRGKIQIWERKFGFEISFPEFCLKGVTLKNFSTSNLNTDFLAKKIIPSKDKNILPKVFHYYGPALEFVQMIKLSDLPSCYMSDIEFELGLTNSTKQNSVLLLEQISSLCSKVGALFVLPCTISNILIPPPNQLSSRKWKEYIAKKPKTISVPDVEVKGECSSYYLLLQGNGNRRCKATLIHSANQINGSFALNLIHGKMKTKTEEAKLSFPFDLLSLPHFSGEQIVQREKQLANVQVLALEECLKRRKLAKQPETVSVAELKSLLVLTRKHFLDYFDAVIPKMILRKMDKIKTFNILNDFSPVEPNSSSLMETNPLEWPERHVLQNLETFEKTKQKMRTGSLPHSSEQLLGHKEGPRDSITLLDAKELLKYFTSDGLPIGDLQPLPIQKGEKTFVLTPELSPGKLQVLPFEKASVCHYHGIEYCLDDRKALERDGGFSELQSRLIRYETQTTCTRESFPVPTVLSPLPSPVVSSDPGSVPDGEVLQNELRTEVSRLKRRSKDLNCLYPRKRLVKSESSESLLSQTTGNSNHYHHHVTSRKPQTERSLPVTCPLVPIPSCETPKLATKTSSGQKSMHESKTSRQIKESRSQKHTRILKEVVTETLKKHSITETHECFTACSQRLFEISKFYLKDLKTSRGLFEEMKKTANNNAVQVIDWVLEKTSKK', 904, 'Q96DY7; B4DUR5; Q9HA89;', 'KD00094', 'Homo sapiens (Human)', 'MTBP', '#Mdm2-binding protein#hMTBP', '-', 'ENSG00000172167', '-'),
(95, 'P32597', 'Nuclear protein STH1/NPS1', 'k', 156743, 'Catalytic component of the chromatin structure- remodeling complex (RSC); which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation; DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes; RSC complex is required both for proper kinetochore function in chromosome segregation and; via a PKC1-dependent signaling pathway; for organization of the cellular cytoskeleton. This subunit is the essential ATPase of the complex. It is a DNA translocase capable of nucleosome remodeling. Required for full expression of early meiotic genes. Essential for mitotic growth and repression of CHA1 expression. Also involved in G2 phase control. {ECO:0000269|PubMed:10025404; ECO:0000269|PubMed:10320476; ECO:0000269|PubMed:10329629; ECO:0000269|PubMed:12072455; ECO:0000269|PubMed:12183366; ECO:0000269|PubMed:12697820; ECO:0000269|PubMed:8980231; ECO:0000269|PubMed:9799253}.', 'MLQEQSELMSTVMNNTPTTVAALAAVAAASETNGKLGSEEQPEITIPKPRSSAQLEQLLYRYRAIQNHPKENKLEIKAIEDTFRNISRDQDIYETKLDTLRKSIDKGFQYDEDLLNKHLVALQLLEKDTDVPDYFLDLPDTKNDNTTAIEVDYSEKKPIKISADFNAKAKSLGLESKFSNATKTALGDPDTEIRISARISNRINELERLPANLGTYSLDDCLEFITKDDLSSRMDTFKIKALVELKSLKLLTKQKSIRQKLINNVASQAHHNIPYLRDSPFTAAAQRSVQIRSKVIVPQTVRLAEELERQQLLEKRKKERNLHLQKINSIIDFIKERQSEQWSRQERCFQFGRLGASLHNQMEKDEQKRIERTAKQRLAALKSNDEEAYLKLLDQTKDTRITQLLRQTNSFLDSLSEAVRAQQNEAKILHGEEVQPITDEEREKTDYYEVAHRIKEKIDKQPSILVGGTLKEYQLRGLEWMVSLYNNHLNGILADEMGLGKTIQSISLITYLYEVKKDIGPFLVIVPLSTITNWTLEFEKWAPSLNTIIYKGTPNQRHSLQHQIRVGNFDVLLTTYEYIIKDKSLLSKHDWAHMIIDEGHRMKNAQSKLSFTISHYYRTRNRLILTGTPLQNNLPELWALLNFVLPKIFNSAKTFEDWFNTPFANTGTQEKLELTEEETLLIIRRLHKVLRPFLLRRLKKEVEKDLPDKVEKVIKCKLSGLQQQLYQQMLKHNALFVGAGTEGATKGGIKGLNNKIMQLRKICNHPFVFDEVEGVVNPSRGNSDLLFRVAGKFELLDRVLPKFKASGHRVLMFFQMTQVMDIMEDFLRMKDLKYMRLDGSTKTEERTEMLNAFNAPDSDYFCFLLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQKNEVRILRLITTDSVEEVILERAMQKLDIDGKVIQAGKFDNKSTAEEQEAFLRRLIESETNRDDDDKAELDDDELNDTLARSADEKILFDKIDKERMNQERADAKAQGLRVPPPRLIQLDELPKVFREDIEEHFKKEDSEPLGRIRQKKRVYYDDGLTEEQFLEAVEDDNMSLEDAIKKRREARERRRLRQNGTKENEIETLENTPEASETSLIENNSFTAAVDEETNADKETTASRSKRRSSRKKRTISIVTAEDKENTQEESTSQENGGAKVEEEVKSSSVEIINGSESKKKKPKLTVKIKLNKTTVLENNDGKRAEEKPESKSPAKKTAAKKTKTKSKSLGIFPTVEKLVEEMREQLDEVDSHPRTSIFEKLPSKRDYPDYFKVIEKPMAIDIILKNCKNGTYKTLEEVRQALQTMFENARFYNEEGSWVYVDADKLNEFTDEWFKEHSS', 1359, 'P32597; D6VVG1; Q45U09;', 'KD00095', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'STH1', '#Nuclear protein STH1/NPS1#3.6.4.12#ATP-dependent helicase STH1#Chromatin structure-remodeling complex protein STH1#SNF2 homolog', '-', '-', '854680'),
(96, 'P32598', 'Serine/threonine-protein phosphatase PP1-2', 'GO:0034501===GO:0000778', 35907, 'Involved in control of glycogen metabolism; meiosis; translation; chromosome segregation; cell polarity and G2/M cell cycle progression. PP1 may act in opposition to the IPL1 protein kinase in regulating chromosome segregation by dephosphorylating H3S10ph. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex.', 'MDSQPVDVDNIIDRLLEVRGSKPGQQVDLEENEIRYLCSKARSIFIKQPILLELEAPIKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFILRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIIDEKIFCMHGGLSPDLNSMEQIRRVMRPTDIPDVGLLCDLLWSDPDKDIVGWSENDRGVSFTFGPDVVNRFLQKQDMELICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGAMMSVDESLLCSFQILKPAQKSLPRQAGGRKKK', 312, 'P32598; D3DM39;', 'KD00096', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'GLC7', '#Serine/threonine-protein phosphatase PP1-2#3.1.3.16', '-', '-', '856870'),
(97, 'Q9QUR2', 'Dynactin subunit 4', 'GO:0005868', 53089, 'Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton.', 'MASLLQSERVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHAQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSQHTIHVVDKYSLGTRLQRPRAGASISTLAGLSLREGEDQKEVKIEPAQAVAEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDLQPVSASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLLECEEGDPDNINSTAKVVVPPKELILAGKDAAAEYDELAEPQDFQDDPDIVAFRKANKVGIFIKVTPQREEGDVTVCFKMKHDFKNLAAPIRPMEESDQGTEVIWLTQHVELSFGPLLP', 467, 'Q9QUR2; Q9QXP8;', 'KD00097', 'Rattus norvegicus (Rat)', 'Dctn4', '#Dynactin subunit 4#Dynactin subunit p62', '-', '-', '84428'),
(98, 'Q5CZ52', 'Bardet-Biedl syndrome 4 protein homolog', 'GO:0003777', 51511, 'May be required for microtubule anchoring at the centrosome. Required for ciliogenesis (By similarity). {ECO:0000250}.', 'MEASNQDEIIGTDVIPNEQDNPEEVVPEPTSLDVPPPPPERAPSAPKRVEILDCNSLNGLMYHYFAQGDYIECKSIIGEIQSKYLERNEAAFHVRGLIARNEGELEEAMECFHKAYELSGKNKRYFYETGRCNFLLGRHQIAVEQLTKASEVMKDNPKVWYWLARAIYHFPAEKVQGKTFNPVESARTILMKPDIAKDATLICFLGRLCEELGDTSGAIAAYKSSLKLQPDNTEVMNLLGLIYLRTGQVQEGFVQLGNCLAYDPANSQAILTIGSIMQNHSDHDVALNKYRVAADVSDYNGCLWNNIGIGLLARNKPAASHSALKKAAFINPLNYKISYNLGVLHDIMNLHCSALHYIKLCTELYPQNAKAVGAMAVILSHMNDDKNARLAYKKSIELKKNPSTILNYAIFEYRMKDVTAASNALKLYKDLQASGVKCSANNKETANLLESVLKQPDQSAEQ', 462, 'Q5CZ52; G3MTX0; G3MTX1;', 'KD00098', 'Caenorhabditis elegans', 'bbs-4', '#Bardet-Biedl syndrome 4 protein homolog', '-', '-', '3565681'),
(99, 'Q96IY1', 'Kinetochore-associated protein NSL1 homolog', 'GO:0000444===k', 32162, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. {ECO:0000269|PubMed:16585270}.', 'MAGSPELVVLDPPWDKELAAGTESQALVSATPREDFRVRCTSKRAVTEMLQLCGRFVQKLGDALPEEIREPALRDAQWTFESAVQENISINGQAWQEASDNCFMDSDIKVLEDQFDEIIVDIATKRKQYPRKILECVIKTIKAKQEILKQYHPVVHPLDLKYDPDPAPHMENLKCRGETVAKEISEAMKSLPALIEQGEGFSQVLRMQPVIHLQRIHQEVFSSCHRKPDAKPENFITQIETTPTETASRKTSDMVLKRKQTKDCPQRKWYPLRPKKINLDT', 281, 'Q96IY1; E7ETD5; Q5SY75; Q9H2M5; Q9NRN8; Q9Y415;', 'KD00099', 'Homo sapiens (Human)', 'NSL1', '#Kinetochore-associated protein NSL1 homolog', '-', 'ENSG00000117697', '-'),
(100, 'Q9UUB5', 'Kinetochore protein mis13', 'GO:0034501===GO:0000941===GO:0031617===GO:0000444===GO:0000779===k', 36798, 'Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Required for correct segregation of chromosomes and for maintaining the inner centromere structure.', 'MKRKPEEQEGFVFVRKGKEKAGSKRRKSSVEDDPDTSQTDGLVELPVSDTPIVKRNKELRKGKGRRSSLDQRGKRASSIGTGFEALPHADVPSHEYYRHISKDLSEPLRIKQLLLWASSKALEEQRKKYGETEEASEAAIARSIVQEVLNELLANKVSVSWYQRPPDAVIPNKPHPQNLKNAQLVDELSAKLTQLHNEEAAWRAVAANSVSSDKSILSFKKAVESIDSKQDLDKQDSPLPPDDAPELPNISKLKPKFHTLLDMLAENIHTLHSLTNAGPEVRSSYGRLAAQDFIAHRKSLLSFSKYVDTMNLLRLLSEASYKSSSNESV', 329, 'Q9UUB5;', 'KD00100', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mis13', '#Kinetochore protein mis13#NMS complex subunit mis13', '-', '-', '2541047'),
(101, 'Q9CWU9', 'Nucleoporin Nup37', 'GO:0000777', 36732, '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 (By similarity). {ECO:0000250}.', 'MKQDATRNAAYTVDCEDYVHVVEFNPFESGDSGNLIAYGGSNYVVVGMCTFQEEETDIEGIQYKTLRTFHHGVRVDGIAWSPETKLDSLPPVIKFCTSAADLKIRLFTSDLQDKNEYKVLEGHSDFINDLVFHPKEGQELASVSDDHTCRIWNLEGKQTAHFLLHSPGMSVCWHPEETFKLMVAEKNGTIRFYDLMAQQAILSLQSEQTPLMSAHWCLKNTFKVGAVAGNDWIIWDITRSSYPQETRPVHMDRAHLFRWSAISENLFATTGYPGKMASQFQIHHLGHSQPVLIGSVAVGSGLSWHRTLPLCAVGGDHKLLFWVTEI', 326, 'Q9CWU9; Q9CZ80;', 'KD00101', 'Mus musculus (Mouse)', 'Nup37', '#Nucleoporin Nup37#Nup107-160 subcomplex subunit Nup37', '-', '-', '69736'),
(102, 'Q3SZN0', 'Septin-6', 'GO:0000777', 48775, 'Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis (By similarity). {ECO:0000250}.', 'MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLRSNTYDLQESNVGLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHACLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKSDAISKSELTKFKIKITSELVNNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMKARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHSRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKN', 427, 'Q3SZN0;', 'KD00102', 'Bos taurus (Bovine)', 'SEPT6', '#Septin-6', '-', '-', '540783'),
(103, 'Q96EE3', 'Nucleoporin SEH1', 'GO:0000777===GO:0051315===k', 39649, '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. As a component of the GATOR2 complex; inhibits GATOR1 complex; an inhibitor of the amino acid-sensing branch of the TORC1 pathway. {ECO:0000269|PubMed:15146057; ECO:0000269|PubMed:17363900; ECO:0000269|PubMed:23723238}.', 'MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSESGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGIVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNAMAKVQIFEYNENTRKYAKAETLMTVTDPVHDIAFAPNLGRSFHILAIATKDVRIFTLKPVRKELTSSGGPTKFEIHIVAQFDNHNSQVWRVSWNITGTVLASSGDDGCVRLWKANYMDNWKCTGILKGNGSPVNGSSQQGTSNPSLGSTIPSLQNSLNGSSAGRKHS', 360, 'Q96EE3; A8K5B1; Q8NFU6; Q96MH3; Q9C069;', 'KD00103', 'Homo sapiens (Human)', 'SEH1L', '#Nucleoporin SEH1#Nup107-160 subcomplex subunit SEH1#SEC13-like protein', '-', 'ENSG00000085415', '-'),
(104, 'Q5U4T8', 'Centromere protein N-B', 'GO:0034508', 39713, 'Probable component of a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. {ECO:0000250}.', 'MDEWLAEFIKRTILKLPFSETATILKTWGFLTESELQTFTLRYPKEVTATEVVRFCEARNATLDHAAALDLVFNHAYSNKKTWTVYQMSKRLESENDLFDASEFKLQFKKSIHAVSKNVTINFKEFGEALWIRIAWGTHNSRPNQYKATFAVYHSQTPYVFITGLGKACQPLMCQALVIASKYSQIQEMELKSRCLESLKDIVFKRFNQPFSSHHSKPHEKALTPNIVDPRVTYENMREKDRVYHLTCETFGEGPLPKLELASYKLETMFKADSAMSGNLTAVNEPFRCVVKFSSPHLLEAIRSLAPAGIAEAPISTLLSCIPHKARNSFKITEKRSMHPSSSQPTNV', 348, 'Q5U4T8;', 'KD00104', 'Xenopus laevis (African clawed frog)', 'cenpn-b', '#Centromere protein N-B#CENP-N-B', '-', '-', '495435'),
(105, 'Q6CRN7', 'Central kinetochore subunit CTF19', 'GO:0000777', 30805, 'Component of the central kinetochore; which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle- microtubule attachments and proper chromosome segregation (By similarity). {ECO:0000250}.', 'MDFTSSSGVLDSERNTGSNDSDEPSSHSDVIETEELKLIKLQEHKNNLLRQRSELLDQLSQTRVVEPRSVQLDDKLLLKLLRRNDNAVSDSSQSSNNPLPRVLPSLNIEQRKKYLDITLNDVTVTCEKDMILLRKGSFTASFRIAVENESIRSMAIDLNAFEVELQPIIQYAEDTQNVNVAMMAVVQFLRIKELHEQMISKIVEASKFIRASNNTITLNDLEVSFHCYWNLPSPYPETLILTNKVQKILDFLIYQYGIQLGVIKYGSTII', 270, 'Q6CRN7;', 'KD00105', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'CTF19', '#Central kinetochore subunit CTF19#Chromosome transmission fidelity protein 19', '-', '-', '2893227'),
(106, 'Q9HAU4', 'E3 ubiquitin-protein ligase SMURF2', 'c;k;m', 86196, 'E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition; interaction with SMAD7 activates autocatalytic degradation; which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way; SMAD2 may recruit substrates; such as SNON; for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level. {ECO:0000269|PubMed:11389444; ECO:0000269|PubMed:12717440}.', 'MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPISGTNGATCGQSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPDSNIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE', 748, 'Q9HAU4; Q52LL1; Q9H260;', 'KD00106', 'Homo sapiens (Human)', 'SMURF2', '#E3 ubiquitin-protein ligase SMURF2#hSMURF2#6.3.2.-#SMAD ubiquitination regulatory factor 2#SMAD-specific E3 ubiquitin-protein ligase 2', '-', 'ENSG00000108854', '-'),
(107, 'Q80YF0', 'Mitotic spindle assembly checkpoint protein MAD1', 'GO:0000776===GO:0000777', 83152, 'Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression; possibly by interfering with MYC binding (By similarity). {ECO:0000250}.', 'MEDLGENTTVLSTLRSLNNFISQRVEGGSGLDVSTAAPGSLQLQYEQSMQLEERAEQIRSKSYLIQMEREKMQMELSHKRARVELERAANTSARNYEREVDRNQELLARIRQLQEREAAAEEKMQEQLERHRLCKQSLDAASQQLREREDGLAAARETISSLKGRVSEMQLNAMDQKVQVKRLESEKQELKEQLELQQRKCQEASQKIQELQASQEERADHEQKIKDLEQKLCLQEQDAAVVKNMKSELLRLPRMERELKRLREENTHLREMKETNGLLTEELEGLQRKLGRQEKMQEALVDLELEKEKLLAKLQSWEKLDQTMGVNLRTPEDLSRFVVELQQRELTLKEKNNTITSSARGLEKAQQQLQDEVRQVSAQLLEERKKREIHEALARRLQKRIVLLTKERDGMRAILGSYDSELTQAEYSAQLTQRMWEAEDMVQKVHAHSSEMETQLSQALEELGVQKQRADTLEMELKMLRAQTSSAETSFPFCKEEVDALRLKVEELEGERSRLEQEKQALEMQMERLTLQGDYNQSRTKVLHMSLNPASMARKRQQEDHARLQGECERLRGLVHALERGGPIPADLEVASSLPSSKEVAELRKQVESAELKNQRLKEVFQTKIQEFRKVCYTLTGYQIDVTTENQYRLTSRYAEHQSDCLIFKATGPSGSKMQLLETEFSRSVPELIELHLLQQDSIPAFLSALTIELFSRQTSI', 717, 'Q80YF0;', 'KD00107', 'Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)', 'MAD1L1', '#Mitotic spindle assembly checkpoint protein MAD1#Mitotic arrest deficient 1-like protein 1#MAD1-like protein 1', '-', '-', '100689352'),
(108, 'Q9PTR5', 'Lissencephaly-1 homolog', 'GO:0000776', 46664, 'Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein- mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity; the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. May be required for proliferation of neuronal precursors and neuronal migration. {ECO:0000255|HAMAP-Rule:MF_03141}.', 'MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHTGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSTISEATGSETKKSGKPGPFLLSGSRDKTIKMWDISTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDFKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR', 410, 'Q9PTR5;', 'KD00108', 'Gallus gallus (Chicken)', 'PAFAH1B1', '#Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141}', '-', '-', '374224'),
(109, 'O74957', 'Protein argonaute', 'k;t', 94439, 'Required for G1 arrest and mating in response to nitrogen starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints occurs downstream of dcr1. Required; indirectly; for regulated hyperphosphorylation of cdc2. Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation; accurate chromosome segregation; centromere cohesion and telomere function during mitosis and meiosis. Required for silencing at the centromeres and for initiation of transcriptionally silent heterochromatin at the mating type locus. Promotes histone H3K9 methylation necessary for centromere function. Required for recruitment of swi6 and cohesin to an ectopic dg repeat. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex. Has ribonuclease H-like cleavage (slicing) activity towards target messages complementary to siRNA and can direct site-specific cleavage of RNA substrates via siRNA. Slicing activity is required for both post-transcriptional and transcriptional gene silencing as well as for histone H3 ''Lys-10'' methylation spreading; conversion of double-stranded siRNA to single-stranded siRNA and siRNA-dependent association of ago1 with chromatin. A member of the argonaute siRNA chaperone (ARC) complex which is required for histone H3K9 methylation; heterochromatin assembly and siRNA generation. The ARC complex contains mostly double-stranded siRNA. {ECO:0000269|PubMed:12193640; ECO:0000269|PubMed:12215653; ECO:0000269|PubMed:12509501; ECO:0000269|PubMed:12733640; ECO:0000269|PubMed:14699070; ECO:0000269|PubMed:14704433; ECO:0000269|PubMed:15371329; ECO:0000269|PubMed:15607976; ECO:0000269|PubMed:16931764; ECO:0000269|PubMed:17310250}.', 'MSYKPSSEIALRPGYGGLGKQITLKANFFQIISLPNETINQYHVIVGDGSRVPRKQSQLIWNSKEVKQYFGSSWMNSVYDGRSMCWSKGDIADGTIKVNIGSESHPREIEFSIQKSSKINLHTLSQFVNSKYSSDPQVLSSIMFLDLLLKKKPSETLFGFMHSFFTGENGVSLGGGVEAWKGFYQSIRPNQGFMSVNVDISSSAFWRNDSLLQILMEYTDCSNVRDLTRFDLKRLSRKFRFLKVTCQHRNNVGTDLANRVYSIEGFSSKSASDSFFVRRLNGEEQKISVAEYFLENHNVRLQYPNLPCILVKNGAMLPIEFCFVVKGQRYTAKLNSDQTANMIRFAVQRPFERVQQIDDFVHQMDWDTDPYLTQYGMKIQKKMLEVPARVLETPSIRYGGDCIERPVSGRWNLRGKRFLDPPRAPIRSWAVMCFTSTRRLPMRGIENFLQTYVQTLTSLGINFVMKKPPVLYADIRGSVEELCITLYKKAEQVGNAPPDYLFFILDKNSPEPYGSIKRVCNTMLGVPSQCAISKHILQSKPQYCANLGMKINVKVGGINCSLIPKSNPLGNVPTLILGGDVYHPGVGATGVSIASIVASVDLNGCKYTAVSRSQPRHQEVIEGMKDIVVYLLQGFRAMTKQQPQRIIYFRDGTSEGQFLSVINDELSQIKEACHSLSPKYNPKILVCTTQKRHHARFFIKNKSDGDRNGNPLPGTIIEKHVTHPYQYDFYLISHPSLQGVSVPVHYTVLHDEIQMPPDQFQTLCYNLCYVYARATSAVSLVPPVYYAHLVSNLARYQDVTADDTFVETSEASMDQEVKPLLALSSKLKTKMWYM', 834, 'O74957;', 'KD00109', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ago1', '#Protein argonaute#Cell cycle control protein ago1#Eukaryotic translation initiation factor 2C 2-like protein ago1#PAZ Piwi domain protein ago1#Protein slicer#RNA interference pathway protein ago1', '-', '-', '2539403');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(110, 'P0C0S5', 'Histone H2A.Z', 'k', 13553, 'Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin; limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation; DNA repair; DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones; also called histone code; and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. {ECO:0000269|PubMed:15878876}.', 'MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV', 128, 'P0C0S5; B2RD56; P17317; Q6I9U0;', 'KD00110', 'Homo sapiens (Human)', 'H2AFZ', '#Histone H2A.Z#H2A/z', '-', 'ENSG00000164032', '-'),
(111, 'Q6C2T8', 'DASH complex subunit DAM1', 'GO:0005828===GO:0051315===GO:0051987===GO:0042729', 25253, '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}.', 'MQRPTTPLRRSNSRQSDHEEHYPIVESVLDMAIGEQMAELADGMSALDRNLKDLQVIHTNLNNFNESFSTLIYGLQMNAWCAEFHNGPRSCDFARRKEVEEMEERARRAQMQAERDRMAMQQIQETPTRLPSEPSDGDVTYMRNDNSFIIQPPSSYQSQLPSRIPQSSRASRIRPPNSLRPPRGRGLYLRGGSRGVTGGRGSYTGVGRGSGRPASEGTTRRWL', 223, 'Q6C2T8;', 'KD00111', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'DAM1', '#DASH complex subunit DAM1#Outer kinetochore protein DAM1', '-', '-', '2908164'),
(112, 'P42271', 'Tubulin gamma-2 chain', 'GO:0051316', 51296, 'Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome; suggesting that it is involved in the minus-end nucleation of microtubule assembly. Required for oocyte activation and consequently for organization of the female meiotic spindle. Essential for centrosome organization and assembly of biastral mitotic spindles in embryos. {ECO:0000269|PubMed:9155007; ECO:0000269|PubMed:9698447}.', 'MPSEIITLQLGQCGNQIGFEFWKRLCLEHGISPDGVLEDFATDGQDRKDVFFYQADDNHYIPRAVLIDLEPRVINNIMTSPYSKLYNQENVFLSKHGGGAGNNWASGFSQGEKVQEEVFDILDREADGSDSLEGFVLCHSIAGGTGSGMGSYVLERLSERFPKKLIQTYSVFPNQDEISDVVVQPYNSILTLKRLTKCADSVVVLDNTALNRIATERLHIQTPTFTQINNLVSTIMSLSTTTLRYPSYMNNNLIGLTASLIPTPQLHFLMTGYTPLMSDCETKTSVRKTTVLDVMRRLLQPKNMMVSALTDKQSRQCFVSILNIIQGEVDPSQVHKSLQRIRERKLANFIPWGPASIQVALPRSSPYVQSAHKVSGLMMANHTGISSLFKRALAQYDKLRKRNAFLDNFRRESMFQDDLTELDIARDTVDCLVQEYEAATQIDYPQWSPAVEASKAG', 457, 'P42271; O77160; Q9V476;', 'KD00112', 'Drosophila melanogaster (Fruit fly)', 'gammaTub37C', '#Tubulin gamma-2 chain#Gamma-2-tubulin', '-', '-', '35199'),
(113, 'Q8BZH4', 'Pogo transposable element with ZNF domain', 'GO:0051382', 154910, 'Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms (By similarity). {ECO:0000250}.', 'MADTDLFMECEEEELEPWQKISDVIEDSVVEDYNSVDKTTSVSVSQQPVSAPVPIAAHASVAGHLSTSTTVSNSGAQNSDSTKKTLVTLIANNNAGNTLVQQGGQPLILTQNPAPGLGTMVTQPVLRPVQVMQNANHVTSSPVASQPIFITTQGFPVRNVRPVQNAMNQVGIVLNVQQGQTVRPITLVPAPGTQFVKPTVGVPQVFSQMTPVRPGSTMPVRPTTNTFTTVIPATLTIRSTVPQSQSQQTKSTPSTSTTPTATQPTSLGQLAGQPPGQSNQTSNPKLAPSFPSPPAVSIASFVTVKRPGVTGENSNEVAKLVNTLNTVPSLGQSPGPVVVSNNSSAQRTSGPESSVKVTSSIPVFDLQDGGRKICPRCNAQFRVTEALRGHMCYCCPEMVEYQKKGKSLDAEPSVPSAAKPSSPEKTAPVTSTPSSTPIPALSPPTKVPEPNENAGDAVQTKLIMLVDDFYYGRDGGKAAQLTSFPKVATSFRCPHCTKRLKNNIRFMNHMKHHVELDQQNGEVDGHTICQHCYRQFSTPFQLQCHLENVHSPYESTTKCKICEWAFESEPLFLQHMKDTHKPGEMPYVCQVCQYRSSLYSEVDVHFRMIHEDTRHLLCPYCLKVFKNGNAFQQHYMRHQKRNVYHCNKCRLQFLFAKDKIEHKLQHHKTFRKPKQLEGLKPGTKVTIRASRGQPRTVPVSSNDAPSGTLQEAAALTSTDPLPVFLYPPVQRNIQKRAVRKMSVMGRQTCLECSFEIPDFPNHFPTYVHCSLCRYSTCCSRAYANHMINNHVPRKSPKYLALFKNSVSGIKLACTSCTFATSVGDAMAKHLVFNPSHRSSNILPRGLSWMSHLRPGQASERVFDWSMKNTYLPPPLVPNKAATVKPVGVTPAEPQELAGPVLQALPSPASTATPPATPTHPQPSALPPSATEGTECLNVSEQEEGSPVTQDPEPASGGGGGSGVGKKEQLSVKKLRVVLFALCCNTEQAAEHFRNPQRRIRRWLRRFQASQGENLEGKYLSFEAEEKLAEWVLIQREQQLPVNEETLFQKATKIGRSLEGGFKISYEWAVRFMLRHHLTPHARRAVAHTLPKHVAENAGLFIEFVQRQIHNQDLPLSMIVAIDEISLFLDTEVLSSDDRKENALQTVGTGEPWCDVVLAILADGTVLPTLVFFRGQANRFANVPDSILLEAKDSGYSDDEIMELWSTRVWKKHTACQHSKSMLVMDCHRTHLSEEVLALLSASSTLPAVVPAGCSSKIQPLDVCIKRTVKNFLHKKWKEQAREMADAACDSDVLLQLVLVWLGEVLGVIGDSPELVQRSFLVASVLPGPDGNVNSPTRNADMQEELIASLEEQLKLNGEQSEEHSASAPRPRSSPEETVEPESLHQLFEGESETESFYGFEEADLDLMEI', 1409, 'Q8BZH4; Q4VA94; Q80TZ8; Q8C0K1; Q8K294;', 'KD00113', 'Mus musculus (Mouse)', 'Pogz', '#Pogo transposable element with ZNF domain', '-', '-', '229584'),
(114, 'Q9Z1M9', 'Structural maintenance of chromosomes protein 1A', 'GO:0000776', 143205, 'Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase; the complex is cleaved and dissociates from chromatin; allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM; or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.', 'MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQALKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNRQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGGSQGEESVSGSQRTSSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ', 1233, 'Q9Z1M9;', 'KD00114', 'Rattus norvegicus (Rat)', 'Smc1a', '#Structural maintenance of chromosomes protein 1A#SMC protein 1A#SMC-1A', '-', '-', '63996'),
(115, 'A8WL28', 'Kinetochore null protein 1', 'GO:0000777', 105839, 'Proposed to be part of the KMN network incorporating the MIS12 complex and NDC80 complex that is required for establishing the kinetochore-microtubule interface that aids in chromosome segregation during meiotic and mitotic cell division. Appears to function downstream of hcp-3 (CENP-A) and hcp-4 (CENP-C) in the kinetochore assembly hierarchy. Has a role in the correct localization of spdl-1 and the RZZ complex that is composed of rod-1; czw-1 and zwl-1 (By similarity). {ECO:0000250|UniProtKB:P34278}.', 'MDNQRKKRNSILKVRQETNLMDVLEDTTVATSSGATNRRVSFHQLKQVKNYDRAGGQIIDATPIKEKAYDTMSSDGNSTSHTTRLDMDITGLNSTPVTPKTQTPFNGSMDMSVENYDETARLFDITRDKTICVYEKTVETTTTKVVERVVRVPEGSSGANNDTLALFNMTDRAEVDMSVDGGSEGALKVDDTISVFNQTNVEPVDMDITVQKPLDDTMGVFRSPAIPTSSRIQKTSASTMDSQNMSMSMDMDITSNEMMAAFKSPKIMSSVLVAAVKDSDDMDLTGLVNTAAEDVADDTMAVFRTPTRAQTTIQKTSGEIPESVDMEMTGIGNSDAPDDTMAVFRTPTRAQQTVQKTSGEIPESVDMEMTLLALLQPVSDVKDNFDDVAMDITQQTLVGVSDDTMAVFKNPAAEKKTPGKPLFDESMEIESTIVCPDNVTFSETAQPENPAYHSSMLMSMASEVSEDVVVQKTSESLQQSSMRMSTTITEDVTASKNPESSTISEVQKIPEVVQKTSNGVEDIQNASETPEDVSMEITSEVVEGERGTMYQMSTMDVDSLQKTSLASPKIQMTSFTDTSEKMGGVSETSLIQTMMIEASESMECSEAPEDVTASPEGLTMAPEDVTVASNVSGIVSVSSISRRRRSQLQESLHRESPRRMALEKNLSMMSQMGGASEALAEFRQNKLKNQTTLLNDSVNTTIGANTSESIGRDIFKMNTSIRSPAHRSSTAPSPMVSKTLPESPKFHVTPFDAAIVNVIYLTPEDAETQEPIPEAFEFEKVLSAEESNVHKEIDTANWSISGAIKSNLDAEVMNIARGQAEMKFLELRGKFAKESNVEIAQKIQELESQNLELAGKIRDSQNLRVLQKQIEELQKPQFSLEEAERIENEYHETKVELLRAQAASIRRQHELLMTIREERRRLIHEIEEKDELLARLEEEDRKKKEEMVERVRGVMRA', 957, 'A8WL28;', 'KD00115', 'Caenorhabditis briggsae', 'knl-1', '#Kinetochore null protein 1 {ECO:0000250|UniProtKB:P34278}', '-', '-', '8583307'),
(116, 'Q5AZQ6', 'Probable kinetochore protein spc24', 'GO:0000777', 22688, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MLLDENPSTLIHHTIGNFNIAPDKQAVSRINDSLATLQQSRELRMREAESSLRKLSRHLQSLSTQHEEAVAAHDASKHAAAMVELDTKKFRIAKAASELEIESERLEGELEMLKERLADLEAQGLEGDEATRREREADDAILLRLKIYRALGIDIEPDEAGNFTKAVIRNSRKGDVHVVNLDPKFSRFFYANYFWSTMQG', 200, 'Q5AZQ6; C8V1S1;', 'KD00116', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'spc24', '#Probable kinetochore protein spc24', '-', '-', '2870790'),
(117, 'Q3UHX9', 'Putative methyltransferase C9orf114 homolog', 'GO:0000777', 42958, 'Required both for chromosome alignment and for association of the centrosomes with the poles of the bipolar spindle during metaphase. {ECO:0000250|UniProtKB:Q5T280}.', 'MAERPRKRPCGPGEHGQRVEWRKWKQQKKEEKKKWKDLKIMKKLERQRAQEEEAKRQEEEEEAAAQRSNQGRPYTLSVALPGSILDNAQSPELRTYLAGQIARACTIFCVDEIVVFDEEGQDTKSVEGEFRGVGKKGQACVQLARILQYLECPQYLRKAFFPKHQDLQFAGILNPLDSPHHMRQDEESEFREGVVVDRPTKAGHGSLVNCGMKKEVKIDKKLDPGLRVTVRLNQQQLPECKTYKGTVVSSQDPRTKAGLYWGYTVRLASCLSAVFAEAPFQDGYDLTIGTSERGSDVASAQLPSFRHALVVFGGLQGLEAAVDADPNLEVADPSVLFDFYVNTCLSQGSRTIRTEEAILISLAALQPGLTQVGSRPASPLSGPRM', 385, 'Q3UHX9; Q8BQY9;', 'KD00117', 'Mus musculus (Mouse)', 'D2Wsu81e', '#Putative methyltransferase C9orf114 homolog {ECO:0000305}#2.1.1.- {ECO:0000305}', '-', '-', '227695'),
(118, 'P59241', 'Aurora kinase A', 'GO:0032133===GO:0000780', 44874, '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 stabilizating 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}.', 'MDRCKENCVSRPVKSTVPFGPKRVLVTEQIPSQHPGSASSGQAQRVLCPSNSQRVPPQAQKPVAGQKPVLKQLPAASGPRPASRLSNPQKSEQPQPAASGNNSEKEQTSIQKTEDSKKRQWTLEDFDIGRPLGKGKFGNVYLAREKQSKFILALKVLFKVQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSNGELKIADFGWSVHAPSSRRTTLCGTLDYQPPEMIEGRMHDEKVDLWSLGVLCYEFLVGMPPFEAHTYQETYRRISRVEFTFPDFVTEGARDLISRLLKHNSSQRLTLAEVLEHPWIKANSSKPPTGHNSKEATSKSS', 397, 'P59241;', 'KD00118', 'Rattus norvegicus (Rat)', '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 6#Serine/threonine-protein kinase aurora-A#ratAurA', '-', '-', '-'),
(119, 'Q0V7M7', 'Spindle and kinetochore-associated protein 1', 'GO:0000940', 29412, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis; when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it mediates the interaction with microtubules (By similarity). {ECO:0000250}.', 'MASDLEQLCAHINEKIGNIKRTLSLRNCGQEPTLKTILNKIGDEIIVVNELLNKLELEIQYQEQTNSSLKELFESLEEDYKDVEHLKENIPPHLPQVTVTQNFVNGSDLDPEEPVKVEEPAPTKKPPKEQRSIKEMPFITSDEFNGIPAYMKSRLTYCHINDVIKEINKAVVSKYKILHQPKKSMSSVARNLYHRFIDEETKETKGHYFVVEADIKEFTTLKVDKRFHGILNILRHCRRLSEVRGKGLTRYVIT', 254, 'Q0V7M7;', 'KD00119', 'Bos taurus (Bovine)', 'SKA1', '#Spindle and kinetochore-associated protein 1', '-', '-', '507703'),
(120, 'Q2M1P5', 'Kinesin-like protein KIF7', 'GO:0003777', 150587, 'Essential for hedgehog signaling regulation: acts as both a negative and positive regulator of sonic hedgehog (Shh) and Indian hedgehog (Ihh) pathways; acting downstream of SMO; through both SUFU-dependent and -independent mechanisms (PubMed:21633164). Involved in the regulation of microtubular dynamics. Required for proper organization of the ciliary tip and control of ciliary localization of SUFU-GLI2 complexes (By similarity). Required for localization of GLI3 to cilia in response to Shh. Negatively regulates Shh signaling by preventing inappropriate activation of the transcriptional activator GLI2 in the absence of ligand. Positively regulates Shh signaling by preventing the processing of the transcription factor GLI3 into its repressor form. In keratinocytes; promotes the dissociation of SUFU-GLI2 complexes; GLI2 nuclear translocation and Shh signaling activation (By similarity). Involved in the regulation of epidermal differentiation and chondrocyte development (By similarity). {ECO:0000250; ECO:0000269|PubMed:21633164}.', 'MGLEAQRLPGAEEAPVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLLEDEQGIVPRAMAEAFKLIDENDLLDCLVHVSYLEVYKEEFRDLLEVGTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRLPRPAPGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWRPEAERPPEETASGARGPPRHRSETRIIHRGRRAPGPATASAAAAMRLGAECARYRACTDAAYSLLRELQAEPGLPGAAARKVRDWLCAVEGERSALSSASGPDSGIESASVEDQAAQGAGGRKEDEGAQQLLTLQNQVARLEEENRDFLAALEDAMEQYKLQSDRLREQQEEMVELRLRLELVRPGWGGPRLLNGLPPGSFVPRPHTAPLGGAHAHVLGMVPPACLPGDEVGSEQRGEQVTNGREAGAELLTEVNRLGSGSSAASEEEEEEEEPPRRTLHLRRNRISNCSQRAGARPGSLPERKGPELCLEELDAAIPGSRAVGGSKARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKLGGVNAVGHSRGGEKRSLCSEGRQAPGNEDELHLAPELLWLSPLTEGAPRTREETRDLVHAPLPLTWKRSSLCGEEQGSPEELRQREAAEPLVGRVLPVGEAGLPWNFGPLSKPRRELRRASPGMIDVRKNPL', 1343, 'Q2M1P5; Q3SXY0; Q6UXE9; Q8IW72;', 'KD00120', 'Homo sapiens (Human)', 'KIF7', '#Kinesin-like protein KIF7', '-', 'ENSG00000166813', '-'),
(121, 'Q4KLP8', 'Shugoshin-like 1', 'GO:0000777===SCL===k', 74638, 'Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase; when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the stag2 subunit of cohesin complex at the centromere; ensuring cohesin persistence at centromere until cohesin cleavage by espl1/separase at anaphase. May regulate kinetochore microtubule stability in mitosis; possibly to sense tension on mitotic chromosomes. {ECO:0000269|PubMed:15339662}.', 'MVKERCPKQAFQDSLEDIKERMKEKRIKKLAKVATVNKTLCTKVQILNSGSTAIKNYKANNTALALALEAEKLKTRQAQDLILGLKREHQRLIFEIFMLRRRLQSQQGRDTAESKLASLKDIIAKVTHNLLETASLLEPAHLLCSSANNNTPNPSKVEEKLSSGASAILRLPSHAPISDTLPKNVIPNRLEPEQRNFKDKVVLEANRNTAGVNRQSRGRRSHSNQPSFTSRLEECNNEDKTESGATMNKNVSLRRRASSLNICLEESLPLEDTNVNSEHTVVETERPFPTEEFSNESRTDREIDNVDNPASPLKVKCFPHANGSKMTGLASEAKQTSNKNKEEPRVGRERVKKGKAERVAVSQMKKPWENSKPRARSKSRDRSASKKSVAKEKMNSSLNSGDAFDFACEESIHVTPFRQNKQEESQNESSLEISSSEGELDDSLYKPYKDKSKNKNLKPDIAPVPLRSRSKRNTARKNSIAENELMSDVQAEANEKKITRNGLKRKSENSFTESAETYREKSFMPTCINTNNAIAENPEVKVFSDECNGGIIYTADEPSGASTPRISLSDVTNLPGNTDAKKHINLLFNEDEMKRSSTPSRKRRCKVSINYAEPKLSGKLRRGDPFTDSEFLQSPIFKNESKRNSLNRQSLSRYNEVFVGCRR', 663, 'Q4KLP8;', 'KD00121', 'Xenopus laevis (African clawed frog)', 'sgol1', '#Shugoshin-like 1#Xsgo', '-', '-', '735145'),
(122, 'P59235', 'Nucleoporin Nup43', 'GO:0000777', 41990, '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 (By similarity). {ECO:0000250}.', 'MEEIYAKFVSQKISKTRWRPVPSGSLQTTETFATGSWDNEENCVSLWSIGDFGNLDSDGGFEGDHQLLCDIRHHGDVMDLQFFDQERIVAASSTGCVTVFLHHPNNQTLSVNQQWPAAHYHTGPSSPSYSSAPCTGIVCDNPEIVTVGEDGRINLFRVDHKEAVRTIDNADSSTLHAVTFLRTPEIVTVNSIGQLKIWDFRQQGSEPCQILSLTGDRVPLHCVDRHPDQQHVVATGGQDGMLSIWDVRQGTMPVSLLKAHEAEMWEVHFHPSNPDHLFTCSEDGSLWHWDASTDAPEKSSLFHQGGRSSTFLSHSLSNQAGVHQSLVSSWLSTDPAKDRIEITSLLPSRTLSVNSLDVLGPCLVCGTDAEAIYVTRQLFS', 380, 'P59235; E9QPN3;', 'KD00122', 'Mus musculus (Mouse)', 'Nup43', '#Nucleoporin Nup43#Nup107-160 subcomplex subunit Nup43', '-', '-', '69912'),
(123, 'Q8BHK9', 'DNA excision repair protein ERCC-6-like', 'GO:0000777', 138854, '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}.', 'MEASQGLAEVETLSPQLAESYLRYVQEAKEAAKNGDLEESLKLFNLAKDIFPTKKVMSRIQKLQEALEQLAEEEDDDEFIDVCSSGLLLYRELYEKLFEHQKEGIAFLYSLYKDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVNEFAKWTPGMRVKTFHGSSKSERTRSLTRIQQRNGVVITTYQMLLNNWQQLASFNGQAFVWDYVILDEAHKIKSASTKSAVCARAIPASNRLLLTGTPVQNNLQELWSLFDFACQGSLLGTLKTFKMEYEHPIIRAREKDATPGEKALGLKISENLMEIIKPYFLRRTKEEVQTKKADNPEARLGEKNPAGEAICDMFSLARKNDLIVWIRLLPLQEEIYRKFVSLDHIKELLMETRSPLAELGVLKKLCDHPRLLSARACRLLNLGTATFSAQDENEQEDVSNMNSIDHLPDKTLIQESGKMIFLMSLLERLQDEGHQTLVFSQSIKILNIIERLLKNKHFKTLRIDGTVTHLWEREKRIQLFQQNKEYSVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFKDSLIRQTTGEKKNPFRYFTKQELKELFTVGDLQKSATQMQLQCLHAAQRRSDEKLDEHIAYLHLLGIAGISDHDLMFTRDLSVKEELDMLEDSQYIHQRVQKAQFLVESESQNTVQRQTTGIEETWLKAQEFPSQQKKKGTEFNKPQPQPSRLLTKPTQVEAISSQMASITICDQSAESEPQEHSEVHDVTSLQGSHHFNSTSDAGTIASLPQGAESIGEVSTDSLLSPAKGFAAENDAMQKKGLQASPGQEAPSENLGSFHYLPRESSKASLGPNLDLQDSVVLYHRSPTANENQNLESDVPMIEISDDLSEPPSALQGAQAIEAQLELKEDDPLKSPPQYACDFNLFLEDSADTRQNLSSKFLEHVEKEKSLQSPAANSRAKSALTLSLDSSPKSDEESEVISVKTKSKTRRILSDDEDEDEEDAFKGSHTNSINISPFPFSSVKQFDASTPQSGSNPSRRFFSPKTPGEVNTSLHSRRSLASRRSLINVVLDDVEDMEERLDNSSEEESEPGLSEENNEEEALACTEEQPSGATLASGNKSSNLTMSEPTSPAPQSSPCAPEPSSSDPMPDPPQDLAVEAGNDYESLVARGKELKECGKIQEALNCLVKALDIKSADPEVMLMTLSLYKQLNI', 1240, 'Q8BHK9; Q8BGN1; Q8BRC9; Q8CE49;', 'KD00123', 'Mus musculus (Mouse)', 'Ercc6l', '#DNA excision repair protein ERCC-6-like#3.6.4.12#ATP-dependent helicase ERCC6-like', '-', '-', '236930'),
(124, 'Q2TBQ9', 'Kinesin light chain 3', 'GO:0003777', 55583, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. {ECO:0000250}.', 'MSVQVAAPGGLGLGLERPSPEELVRQTRQVVKGLEALRAEHRGLAGHLAEALAAQGPAAGLELLEEKQQVVSHSLEAIELGLGEAQVLLALSAHVGALEAEKQRLRAQARRLAQENAWLREELEETQRRLRASEEAVAQLEEEKSHLEFLGQLRQYDPPAESQQPESPPRRDSLASLFPSEEEERRGPEAVGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATDLLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFEEVERHYARALSIYEALGGPHDPNVAKTKNNLASAYLKQNKYQQAEELYKEILHREALPAPLGAPNTGTTSDTQQQTLSRSSSFSKLRESIRRGSEKLVSRLRGEGAAGAAGMKRAMSLSMLNTDGSRAPENQFPRQHLSEASRTLSTSTQDLGPR', 505, 'Q2TBQ9;', 'KD00124', 'Bos taurus (Bovine)', 'KLC3', '#Kinesin light chain 3', '-', '-', '517633'),
(125, 'A1L4U8', 'At5g04320Shugoshin C terminus protein', 'k', 47738, '', 'MTLMKALAHRNKLVELSGIEIQKLRINLRSVQEKNLQLAQANSQMLAELNTNRDRLKDLQHELGCKNALLKVKKHLEEQVLPRTHHESKDKVSASASDGDCKSFQVHDIKHKDTKRKRTTRIKSSVSADVKPIPVNDSNSKANRKRRVSGVIDTTGIPEEICQTEDDIDKGVVSRGVNQDIDNVVNKKFVPDAANPVKESVHRKRQCTRRQSTRFDVQETKQTEKLLEMDGAKESKETASFSLRRRSARLRHEEAEPCKSLHEGDEVRETIKRRRVSLRLSARFDIQEPHVTETSNADDARSIVIEESAGSRSESVEPSESRHETKEITRKRSFSTRRQSTKGKSQTDEAIKEIATDPSLVNTIVQECDQETESKDKPKADENEGMTRRSSVGRPSRHAAEKVQSYREVSLRVKMRRKC', 419, 'A1L4U8;', 'KD00125', 'Arabidopsis thaliana (Mouse-ear cress)', 'At5g04320', '#At5g04320 {ECO:0000313|EMBL:ABM06005.1}#Shugoshin C terminus protein {ECO:0000313|EMBL:AED90726.1}', '-', '-', '830311'),
(126, 'Q2UL45', 'Probable kinetochore protein ndc80', 'GO:0034501===GO:0000778===GO:0051315===GO:0051455===GO:0031617===GO:0031262', 83600, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSQDTGLFSIKRPRESLAHFSALPQPSSALKRTSSIGAFGNPPTAQHTRMSLLNSASRPQQPNFQRSSSGGAFGADAGLSSVRRSVSSNIFHGASAGRQSYAPGSFSSNPASQNLQRRSSVFSRPSAGVGGAMGHQSFFTQVPNAAGVPRDPRPLRDRSFQARIGQELLEYLTHNNFELEMKHTLGQNTLRSPTQKDFNYIFQWLYHRIDPGYRFQKSMDAEVPPILKQLRYPYEKGITKSQIAAVGGQNWPTFLGMLHWLMQLAQMMDRFIMGEYDEACAEAGVDVSGDRIIFRFLTGAYHDWLQGGEDEDDETAGQRLVPHIEMMAQEFERGNEKYVQEVQALEAENRALRDQIEEMEKSAPDMAKLDKHFRILEDDKRKFEDYNQNVQGKIEKYENRIKFLEDELQKTEADLQAAEDERAGLQSSVDRQGITIQDIDRMNTERDRLQKILDDTMGRLEETHSRVMEKEKEASEKLEALEEVVKAYNTLGYQTSLIPSSAVNAKGQDYELSLNVNESNFSASQIGSAPSRISPEGDRLLAEPFTGYHPAHLLSLDLRGTVRSSLQTLRKDINERRKRAADDDLDRRNLLDNIKEAMDEKRSEVEALEHRRRAAEEEFERTKEITTTQKLASDAQIEKMEKELAKMRATMSESVQLMEQREMNTNIEYEQLTLRANALREELHTNVESMLNDVIRFKVHVQKGLEDYEGFVVDEVEQELGGDMVPADDIPPEEEL', 736, 'Q2UL45;', 'KD00126', 'Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)', 'ndc80', '#Probable kinetochore protein ndc80', '-', '-', '5991705'),
(127, 'Q9XWH0', 'BUB-3', 'k', 38127, '', 'MSTYQAATIVAAPNEFRVPFPPFVQISKVQFQREAGSRLLAASGWDGTCRVYEVGKLGDISEKLVFTHGKPLLTCTFAGYNKVAFGGVDHNVKLADIETGNGTQLGSHALAVRCMEFNPMSSLIVSGGWDSSVKLWDARSYGNGAIESVNVSSSVYAMDVLKHTILVGTKDRKIFMYDSRKLREPLQVRDSPLKYQTRAVQFFPTGEAFVVSSIEGRVAVEYVDQSGEEMMKRKYAFKCHREKDTDGTELIHPVHTVAFHPKYGTFATGGADGIVNIWDPFNRKRIIQLHKFETSISSLSFNEDGSQLAIATSYQYEKEIDPSPLPNNSITIRHITDPESRPK', 343, 'Q9XWH0;', 'KD00127', 'Caenorhabditis elegans', 'bub-3', '#BUB-3 {ECO:0000313|EMBL:CAA21698.1}', '-', '-', '175018'),
(128, 'P11388', 'DNA topoisomerase 2-alpha', 'c;k', 174385, 'Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity). {ECO:0000250|UniProtKB:Q01320; ECO:0000269|PubMed:18790802; ECO:0000269|PubMed:22013166; ECO:0000269|PubMed:22323612}.', 'MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSSLARLLFPPKDDHTLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREIVNNIRRLMDGEEPLPMLPSYKNFKGTIEELAPNQYVISGEVAILNSTTIEISELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDNEKETEKSDSVTDSGPTFNYLLDMPLWYLTKEKKDELCRLRNEKEQELDTLKRKSPSDLWKEDLATFIEELEAVEAKEKQDEQVGLPGKGGKAKGKKTQMAEVLPSPRGQRVIPRITIEMKAEAEKKNKKKIKNENTEGSPQEDGVELEGLKQRLEKKQKREPGTKTKKQTTLAFKPIKKGKKRNPWSDSESDRSSDESNFDVPPRETEPRRAATKTKFTMDLDSDEDFSDFDEKTDDEDFVPSDASPPKTKTSPKLSNKELKPQKSVVSDLEADDVKGSVPLSSSPPATHFPDETEITNPVPKKNVTVKKTAAKSQSSTSTTGAKKRAAPKGTKRDPALNSGVSQKPDPAKTKNRRKRKPSTSDDSDSNFEKIVSKAVTSKKSKGESDDFHMDFDSAVAPRAKSVRAKKPIKYLEESDEDDLF', 1531, 'P11388; B2RTS1; Q71UN1; Q71UQ5; Q9HB24; Q9HB25; Q9HB26; Q9UP44;Q9UQP9;', 'KD00128', 'Homo sapiens (Human)', 'TOP2A', '#DNA topoisomerase 2-alpha#5.99.1.3#DNA topoisomerase II; alpha isozyme', '-', 'ENSG00000131747', '-'),
(129, 'P30776', 'Cohesin subunit rad21', 'k', 67854, 'Cleavable component of the cohesin complex; involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition; this protein is cleaved by cut1 and dissociates from chromatin; allowing sister chromatids to segregate. Also involved in the DNA double-strand-break (DSB) repair system. {ECO:0000269|PubMed:11069892; ECO:0000269|PubMed:1480481}.', 'MFYSEAILSKKGPLAKVWLAAHWEKKLSKVQTLHTSIEQSVHAIVTEETAPMALRLSGQLMLGVVRIYSRKARYLLEDCTEALMRLKMSFQPGQVDMIEPATALQSLKGKDAVTQSANLTLPETITEFDLLVPDSTFDFQWSQLLRTPSRSSNTLELHSLPISSSPSFPSSQLSIEAGRNAQVESGFSLGESFAHVGNDMQFHLPISNSGAATPRSVHSDNQSQISIEVGRDAPAAAATDLSGIIGPQMTKSPASSVTHFSTPSMLPIGGTSLDDELLAPVDDLNLDLGLDDLLGDEQGANAPAIEADEQAETSSIHLPSDIMEDDSSRPAAAGVEEGQVVESATAPQQEKINPQKTVRRQRAIIDPVTELSSKQMKKQLADTSSITSPLCLNTSSIVFNATVNFTRNGKFNTSIFSSNLNPKVNELLQADFKQAILRKRKNESPEEVEPAKHQRTDTSTENQETAEVLDPEEIAAAELANITEAAIATLPQETVVQPEGEAPELGSPMGFPVTALESADDSLFDAPPVMLDEADLLGSERLDSSVSEALPSSQTAKDSLRNKWDPYTEGEKVSFQTLSAGCNREEAVQLFFDVLVLATKDVISVKQDVAIQNEITLTAKRGMLLSSL', 628, 'P30776;', 'KD00129', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'rad21', '#Cohesin subunit rad21#Double-strand-break repair protein rad21#SCC1 homolog', '-', '-', '2539447'),
(130, 'Q8SUE9', 'Probable kinetochore protein NDC80', 'GO:0000777', 63097, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MTRRFTMTPNSRNPVKTPVSGMKVAPFPRHSIATEEVRRRDMRVVREKGYRQQCVDGILRFLVENGYDGQVSQKILHNPSSKDFQSIFKFLYGFVDDFTFSSRFEDEVVNVMKNLKYPYCGEITKSQLSAITPHTWPVILSMCSWLVDLISHGTSLLQQEEERSVESCFFEYVCDGYMRFMEGDEDDTALEEEFERRVTEIYTGIFKEIDRKKEELRRIEEMISEARKMSEGREELDRKKRELTDDLNMLIASEKQLEGKKRKYLGAISRLSEEIVKVEEEIESLRAQEDGLRAQITKQRINPEDVKEMNAEKIELFKELERMKPEKESLMKVVGEQEREAQERAEEVEKLFFDLKGLRDEISLRIVKDGKGVPRVANEVSGEVFSGMSGVIVRLEEELNSKSDVLVTAEMNKSILEEARGEKESITSELNSRLGYYSDKLVMAGKLYLEKKEISENEQRKSKTEMELLENELLKLNLESNTSLLMSEQKLQKARIVLDRTLNSINYEREEINKMIFGFYNAAMDIHASIQSQVGDLRALLNK', 543, 'Q8SUE9;', 'KD00130', 'Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '859845'),
(131, 'Q76PC4', 'UPF0649 protein C1442.02', 'GO:0000778', 64175, '', 'MDWKEAIPGAAKVAIETKDYITYSTLLELILEEARIKDIDEQRELIKCLHEELKQEKNDHITREISWDIIGMVLPYVGKVQNEADEFVDFLAKNGNPREVFLKCCELLINGGFESPQQFISLNSAILSALHRISTKRPVLFVNNFLISLFSGLANILQIDSDELYCVWKISISSIQDAMHRFPVSECYLACLKACSILAQLFLSKETLMLSFRSLLQTKDQYAEFREELSGATTNCDKLDTLSKSIINIFDYLLSHLPESWSIITEHMAQELTKATYVSQSSSISSEDEEIAKNADVPAEVDNNSTKADDKRDEIEFDTKGCLALLTIKSFYQSGNFFLDFLKEKFPSTILETLQQLVSWEIQLDSVGFKDIAVYQGYLLDLPHFQVPDSELEHLSSLLHGYHFMASSTELPWLRVTCNAIVTKCLDSQLPSVRLSYILDTLEECPLLNIKTAILNYYQKQCSLVKDSNEEGLKNFVSPNTLLDVFKVFDAMEDVELDSQSLSYIHQTLVFLYSLEIQNLLSQNQFPTVYFTKISDQINNYEGELPTDGLKYYIELLNSRNK', 562, 'Q76PC4;', 'KD00131', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'SPCC1442.02', '#UPF0649 protein C1442.02', '-', '-', '2538698'),
(132, 'Q4V7H8', 'Borealin-2', 'GO:0032133', 32372, 'Component of the chromosomal passenger complex (CPC); a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Contributes to CPC function by facilitating loading of the CPC onto chromosomes. {ECO:0000269|PubMed:15260989; ECO:0000269|PubMed:17199039}.', 'MPPKRNRNRLGTRGEGSGDSGVGMFERNDAVQEHKKEKIRLFMQDFVQQGKDRLAELKKDLESLSTTADKALEVELLKMPLAIRHMKVQDYLSLMGGDKSAVAAAAVKLDCSVDELSEPKLVRKNSKKVKVTTNVEYQDDVRTKVMTTSTKNRTVQKVPKSKSMLSLTGKNGKKTTALTRSVSATPLDKASKKLLVTNSSSKPAQRSSRTAMTPLTRSARSDTMFTFGDGAFLDEGVPFVKIPLADGKTVFSAGDDLDSLNVELLRGDTVQHIHNLVGQLTSLCAKASIQHHGNTL', 296, 'Q4V7H8; Q693P3;', 'KD00132', 'Xenopus laevis (African clawed frog)', 'cdca9', '#Borealin-2#Cell division cycle-associated protein 8.2#Cell division cycle-associated protein 9#Dasra-A#DasraA#xDasraA', '-', '-', '444883'),
(133, 'Q18508', 'MEL-28', 'k', 200846, '', 'MDNENSSIFKSYQGYECWRGEKQIILKDSIGRQLPYIVNFKKNTCQIFDIEWERVTHSFVFPEGCALIDADYFPTEEGKLGILVGVEDPRQSCGAEHFVLALAVDPDSPAMTITHSLEVPSKITVVKTLFSSADMADETQRTVLKLYHRLMTWQHIVAIGCKETQCYLARLVAVETPSSPVITVHSEKKYLINLMNAYVSGSVLQYTLDDGAYREYPTAAVYISALSLMPRSRTLLVGLSMGGILAASLNPSNQMMLLELRHERLVRKIAPLEPEDDPDKFEYFIATVDCSPRHPIMIQLWRGSFKTLEDVDGEEKYDRPSFSVCLEHKILFGERWLAVNPIVTERDHMMLTRKRGTEDSMHNVSQTFGSTSNRNSVLLAYERKKMVIGTEDPNAEPEYIVEAAIFDIDSWYYKRVPGRVSTDGTVLKQCAFLSTIKSNIRSEDVNDIGILTNEATDVSSFSSMVSDADQLFYPSALSFERVFVAKNTRIDWMKIQNIQDTILNKCAVKLPALIRNPEMISSVVMAAGLVRKNILSGSPNSSAAEINELQLSSDQKVLLNVIVYYGKIEEFCQLASRPDISDTLKRELAEWALHEAVDYKRTISDKMVSLFQGRSLALSPLAEESIAQGIKLFRVVYEYLKACSKALKDDRLRNLAHSVICMRNHTKLTSQFINFAIIPVDPIRQQRMKDLHSKRKNMARKNSSSLPVQSVVRKMNRQAPNAQFWNDIPHDEWYPPTPLDLLECLLNVSISESIKRELVVQYVIDWISTSPEDSEHSEKQLALETIKIMTNQMLNVNLEKIYYILDQGKKALTSSKTSDDMRALGEKVFSMKDDEISYEKLWGKDAPMTVTIGKHDLQRFEQRMKMQMEGGKVRLPVLDPESEILYQMFLFENEKFEAMSSEAISSNKLLSAFLPGMIKKDGRGRQKTAKEQEIEISVKKMFERKVQNDDEDMPEVFASVNDKTERKRKSSQFGEDDESSVSSSQYVPPTAKRIQQWKSAVESVANNSSINSITSPDSHQNAEINMMIATPARYYKRHNEEENVQDGFLSPAGNRPPPVSAHNSILKTAKGGQSASRGRIRFRADVPRGADESIEDNGRKGLALNFAILEDEEEETMTIRKSRSMGKHDEEKDSEKNVVDEMEEVKDQEQENDECIESEKTFENQDDFEVLEDTSAPEAANTENGSETPPMEDTFEVRDDDVMPPTDETYLSHLQTDKTGILEEEGEDEDIWDGVQRSFEVQMDEDCEAVPTIDVADDLESKSEEVNEEEVVESEEVQQDAKEPEKTEKRQEEPEPEVMQPVIPEEPQNESLESSIKLQEELQEEPDIVPTGDEDTADKVQEQAVEEDRPPSRNTRSSSVQKSTSQVEDRDPKELVEEERPPSRNTRSASVQKSSNQEKTSESGEVTEEDRPPSRNTRSASVQKSSSKVKDQKPEELIEEDRPPSRNTRSASAQKTVAANKSVLESEIPSRSASRRTRSTSLRNDTVAEPDETSVAMTTRRRTRATSEVVSKQSSEDDGRSTPKTGRTPTKKAAASTSSSRAGSVTRGKKSIIQKMPSPLEVTMEVQEEEEEEAEEERPASRSTRSASVKNTTVDPSSSALASTKRTTSRKRGNSETIDFNQDDKSAPTTPKRGRPAKKDAGSPKVGSKARGTKPKSIFENQEDEEDRSSSPDIEQPATPTRSSKRTARSRANSESIDDDSKQKTPKKKNAAVNEAGTSKQSRSVTRSRASSIDVQQEVEEPTTPKRGRGRPPKTVLENIEEGEEERKETAATPLLRSARRAKQ', 1784, 'Q18508;', 'KD00133', 'Caenorhabditis elegans', 'mel-28', '#MEL-28 {ECO:0000313|EMBL:CAA86316.2}', '-', '-', '175634'),
(134, 'Q9HFF5', 'Sister chromatid cohesion protein pds5', 'GO:0034501===GO:0072356===GO:0051455===GO:2000817', 138875, 'Required for the establishment and maintenance of sister chromatid cohesion during S phase. Prevents their formation until eso1 is present. May also have a role during meiosis. {ECO:0000269|PubMed:11598020; ECO:0000269|PubMed:11861765}.', 'MIKLQFQRNIVPTHDNPLTTSEILKRLRDLLGELTSLSQDTIDRDSVLPVARSLVNNNLLHHKDKGIRSYTLCCIVELLRLCAPDAPFTLSQLEDIFQVILKILSGLMNQESTYYPQIYEILESLSNVKSAVLIVDLPNAEEFLVNIFRLFFDLARKGTTKNVEFYMLDIINQLINEINTIPAAALNILFAQLISGKGVRQTIGSSDSTNHGPAFQLARNIFHDSADRLQRYVCQYFSDIIFDSRDSLSDSMTTPEFIFSHNLVLQLWKYAPTTLLNIIPQFENELQAEQTSVRLVAIETVGLMLQDNAIWSDYPRVWSAFCGRLNDKSVACRIKCIEVASNALQNSLATSEIIENVVQMLQSKLADTDEKVRVATLKTIEQLTFETFKMQFSVQALKLMGDRLRDRKLNVRLQAIRTLSQIYNRAYQDLIDGVEYSIQMFSWIPSSLLEVFYVNDETTNAAVEICMAELVLQYLSSDTQTRLNRLFLSIKYFSEKAMRVFILLLQRQVKYSELLNYYIECCKNYNGGVMDNDEESITNKLKKVIDIISSKSSNPTLTEATFRKFAELNDRQSYKMLLQTFSIKSEYQVVLKSIKYLFKRVSETLSTASLECFRIFVYRSALFAFNKSNVHEIIQLLNEPVKYHNFLKPSEALLQHLPLIHPNIYGEVVIEVENIIVSSGIESDPKVIKALSQFSKRKKNFSIQTTTAEILRKLCLHGTQEQAKQAATIIAITETKEFKLDMITNIVENLEYNGGLPVRLMTLGQLFLYTLEEVEKVADQVTEFLVKKVIQRFPEKYDDTHNDEEWCTYEKLDNLTMCKVLAIRVLVNRLRAAAGGTEALNIGAPIIKLLKVLLMADGELSPFKNTPKISRAYLRLTASKYFLKLCSIPFYAEHIDFSSYVQISLLCQDENFDVRNLFLTKLQKQLQLKKLPISYYPLLFLTAVDPEEEIKTKASIWIRSQVAFFQKTHDFTMEYVATYLIHLLSHHPDISSIESENSLDFIAYIRFYVDTVVNSENVPIVFHLMQRIKQSYDVIEDGNNYIYVLSDMAQKILQVKSQNFGWSLTTYPKQIKLPYEILRPIPSIDEKKRIFNKIFITPKMESQIEHAIRTPVSSFAKQTTNKHANLKQKKTHSSKSDKKSSRRRKNEKRRKLNEQNPNIRNVPERSSSRFQGIRINYSEAPSSSEEISEEEEEISEEDFDEIEDL', 1205, 'Q9HFF5; O94237;', 'KD00134', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'pds5', '#Sister chromatid cohesion protein pds5#Precocious dissociation of sisters protein 5', '-', '-', '2541628'),
(135, 'Q8AYS7', 'Centromere protein I', 'GO:0000776===GO:0034508', 86894, 'Component of the CENPA-HI complex; a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. Required for the localization of CENPC but not CENPA to the centromere. It however may be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. {ECO:0000269|PubMed:11970896}.', 'MQRRQSSKHSKRPLQVHHSNQTDLSAWRKGGTVDTEKSAQNRQSLSDQKNDNEQDSLEQALSYFEKIQDRVSLKKSEVLQKHLSTMESIALKRGLPPEGFDVLLDVALSGKLADTVNTRLLKSLIPASAIPESSIVSSVSWFCVSKCSSNIQLLFLRWLITMFDFIDHKEQVHALYGIFFSFLNDEKLCPYICHVLYLLTRKENVKPFRVRRLLDLQSKMGMQPHLQALLSLYKLFCPELVSITLPQKMKTYFKNADGPWKAAINAVRQRNQANSTVPQPLLLGTAQPHSRKRKWNTQLIVPASSANAQNLVVGGKMSRADSYSANESFPVEQLRTFPQLLQNIHRLEFPSQMGSVLTNPLLLHYMNCSKDESVYLRLYYWMGQTLQEECTWCVVDNNQYEEEFRGFLETVYKAECFLQEGFPSCEEFLYRSLPLWDGVSCRSQILQLVSWIPLSTFSEMKSQLCDPLAQLFFTSSLYFKCSVLESLKELLQNWLNWHVVQLDSESDSQFSSLNTTLSGLVNGVAELINFVGRISTAALHLEKSHTFLLYFILDFYETVCDIYLKYKLPLLIMPPAGVFYPALLSMDSVNLNQLCYIMYRYRTNLIAAKENEMSKKKIQQFKFSSQTYQEYNQYIIAMVGCLWTSSAFQKDNHPEGIRLDDELLKKTGVREYKNSFNIVYHPALMCYAVDFLQQAWPDDTTFNFNLIKGKKWNWYLRYLYGQGLEGLKLFIESSINRVSKASQSKAEDEDEKV', 753, 'Q8AYS7;', 'KD00135', 'Gallus gallus (Chicken)', 'CENPI', '#Centromere protein I#CENP-I', '-', '-', '395207'),
(136, 'Q2N2K6', 'Histone H3-like centromeric protein CNA1', 'GO:0000777', 21703, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. {ECO:0000269|PubMed:16738316}.', 'MARKAYQPKRRSNSNQNQQRSDSLKKNKQDNLRSKSAGNQQGNEKNKKDIQDQRNKASTKKKRESSGEKYESARDKVIRRFRPGDNALKQLRQYNQTPSLLIRKLPFQRLIREISTRMTEEDSLRWTSFALVLLQTVVEDYMVSFFEDANACALHAKRVTLMSKDLALAARIRGQKNVTGIFIPTKK', 187, 'Q2N2K6;', 'KD00136', 'Tetrahymena thermophila (strain SB210)', 'CNA1', '#Histone H3-like centromeric protein CNA1', '-', '-', '7840155'),
(137, 'Q9BS16', 'Centromere protein K', 'GO:0000777===k', 31655, 'Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Acts in coordination with CASC5/KNL1 to recruit the NDC80 complex to the outer kinetochore. {ECO:0000269|PubMed:16622420; ECO:0000269|PubMed:16716197; ECO:0000269|PubMed:18045986}.', 'MNQEDLDPDSTTDVGDVTNTEEELIRECEEMWKDMEECQNKLSLIGTETLTDSNAQLSLLIMQVKCLTAELSQWQKKTPETIPLTEDVLITLGKEEFQKLRQDLEMVLSTKESKNEKLKEDLEREQRWLDEQQQIMESLNVLHSELKNKVETFSESRIFNELKTKMLNIKEYKEKLLSTLGEFLEDHFPLPDRSVKKKKKNIQESSVNLITLHEMLEILINRLFDVPHDPYVKISDSFWPPYVELLLRNGIALRHPEDPTRIRLEAFHQ', 269, 'Q9BS16; Q9H4L0;', 'KD00137', 'Homo sapiens (Human)', 'CENPK', '#Centromere protein K#CENP-K#Interphase centromere complex protein 37#Protein AF-5alpha#p33', '-', 'ENSG00000123219', '-'),
(138, 'P28743', 'Kinesin-like protein KIP2', 'GO:0003777', 78378, 'Required for assembly of the mitotic spindle.', 'MIQKMSPSLRRPSTRSSSGSSNIPQSPSVRSTSSFSNLTRNSIRSTSNSGSQSISASSTRSNSPLRSVSAKSDPFLHPGRIRIRRSDSINNNSRKNDTYTGSITVTIRPKPRSVGTSRDHVGLKSPRYSQPRSNSHHGSNTFVRDPWFITNDKTIVHEEIGEFKFDHVFASHCTNLEVYERTSKPMIDKLLMGFNATIFAYGMTGSGKTFTMSGNEQELGLIPLSVSYLFTNIMEQSMNGDKKFDVIISYLEIYNERIYDLLESGLEESGSRISTPSRLYMSKSNSNGLGVELKIRDDSQYGVKVIGLTERRCESSEELLRWIAVGDKSRKIGETDYNARSSRSHAIVLIRLTSTNVKNGTSRSSTLSLCDLAGSERATGQQERRKEGSFINKSLLALGTVISKLSADKMNSVGSNIPSPSASGSSSSSGNATNNGTSPSNHIPYRDSKLTRLLQPALSGDSIVTTICTVDTRNDAAAETMNTLRFASRAKNVALHVSKKSIISNGNNDGDKDRTIELLRRQLEEQRRMISELKNRSNIGEPLTKSSNESTYKDIKATGNDGDPNLALMRAENRVLKYKLENCEKLLDKDVVDLQDSEIMEIVEMLPFEVGTLLETKFQGLESQIRQYRKYTQKLEDKIMALEKSGHTAMSLTGCDGTEVIELQKMLERKDKMIEALQSAKRLRDRALKPLINTQQSPHPVVDNDK', 706, 'P28743; D6W3L3;', 'KD00138', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'KIP2', '#Kinesin-like protein KIP2', '-', '-', '855948'),
(139, 'P28742', 'Kinesin-like protein KIP1', 'GO:0003777===c;k', 125795, 'Required for assembly of the mitotic spindle. Interact with spindle microtubules to produce an outwardly directed force acting upon the poles. Following spindle assembly; CIN8 and KIP1 apparently act to oppose a force that draws separated poles back together. This force seems to be mediate by KAR3.', 'MARSSLPNRRTAQFEANKRRTIAHAPSPSLSNGMHTLTPPTCNNGAATSDSNIHVYVRCRSRNKREIEEKSSVVISTLGPQGKEIILSNGSHQSYSSSKKTYQFDQVFGAESDQETVFNATAKNYIKEMLHGYNCTIFAYGQTGTGKTYTMSGDINILGDVQSTDNLLLGEHAGIIPRVLVDLFKELSSLNKEYSVKISFLELYNENLKDLLSDSEDDDPAVNDPKRQIRIFDNNNNNSSIMVKGMQEIFINSAHEGLNLLMQGSLKRKVAATKCNDLSSRSHTVFTITTNIVEQDSKDHGQNKNFVKIGKLNLVDLAGSENINRSGAENKRAQEAGLINKSLLTLGRVINALVDHSNHIPYRESKLTRLLQDSLGGMTKTCIIATISPAKISMEETASTLEYATRAKSIKNTPQVNQSLSKDTCLKDYIQEIEKLRNDLKNSRNKQGIFITQDQLDLYESNSILIDEQNLKIHNLREQIKKFKENYLNQLDINNLLQSEKEKLIAIIQNFNVDFSNFYSEIQKIHHTNLELMNEVIQQRDFSLENSQKQYNTNQNMQLKISQQVLQTLNTLQGSLNNYNSKCSEVIKGVTEELTRNVNTHKAKHDSTLKSLLNITTNLLMNQMNELVRSISTSLEIFQSDSTSHYRKDLNEIYQSHQQFLKNLQNDIKSCLDSIGSSILTSINEISQNCTTNLNSMNVLIENQQSGSSKLIKEQDLEIKKLKNDLINERRISNQFNQQLAEMKRYFQDHVSRTRSEFHDELNKCIDNLKDKQSKLDQDIWQKTASIFNETDIVVNKIHSDSIASLAHNAENTLKTVSQNNESFTNDLISLSRGMNMDISSKLRSLPINEFLNKISQTICETCGDDNTIASNPVLTSIKKFQNIICSDIALTNEKIMSLIDEIQSQIETISNENNINLIAINENFNSLCNFILTDYDENIMQISKTQDEVLSEHCEKLQSLKILGMDIFTAHSIEKPLHEHTRPEASVIKALPLLDYPKQFQIYRDAENKSKDDTSNSRTCIPNLSTNENFPLSQFSPKTPVPVPDQPLPKVLIPKSINSAKSNRSKTLPNTEGTGRESQNNLKRRFTTEPILKGEETENNDILQNKKLHQ', 1111, 'P28742; D6VPT7;', 'KD00139', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'KIP1', '#Kinesin-like protein KIP1#Chromosome instability protein 9', '-', '-', '852216'),
(140, 'P28741', 'Kinesin-like protein KIF3A', 'GO:0003777', 80170, 'Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation. {ECO:0000269|PubMed:21670265}.', 'MPINKSEKPESCDNVKVVVRCRPLNEREKSMCYRQAVSVDEMRGTITVHKTDSSNEPPKTFTFDTVFGPESKQLDVYNLTARPIIDSVLEGYNGTIFAYGQTGTGKTFTMEGVRAVPGLRGVIPNSFAHIFGHIAKAEGDTRFLVRVSYLEIYNEEVRDLLGKDQTQRLEVKERPDVGVYIKDLSAYVVNNADDMDRIMTLGHKNRSVGATNMNEHSSRSHAIFTITIECSEKGVDGNMHVRMGKLHLVDLAGSERQAKTGATGQRLKEATKINLSLSTLGNVISALVDGKSTHVPYRNSKLTRLLQDSLGGNSKTMMCANIGPADYNYDETISTLRYANRAKNIKNKARINEDPKDALLRQFQKEIEELKKKLEEGEEVSGSDISGSEEDDEEGELGEDGEKKKKRRDQAGKKKVSPDKMVEMQAKIDEERKALETKLDMEEEERNKARAELERREKDLLKAQQEHQSLLEKLSALEKKVIVGGVDLLAKAEEQEKLLEESNMELEERRRRAEQLRKELEEKEQERLDIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELRLQMLIIDNFIPQDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKERDPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKMGRRKRSAKPETVIDSLLQ', 701, 'P28741; Q7TSZ7;', 'KD00140', 'Mus musculus (Mouse)', 'Kif3a', '#Kinesin-like protein KIF3A#Microtubule plus end-directed kinesin motor 3A', '-', '-', '16568'),
(141, 'P28740', 'Kinesin-like protein KIF2A', 'GO:0003777', 79756, 'Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity (By similarity). {ECO:0000250}.', 'MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEDIEPSPELPPPSSSSKVNKIVKNRRTVAAVKNDPPPRDNRVVGSARARPSQLPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTVNPAAAGDVHPIMHHPPSQIDDLETQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWIEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL', 705, 'P28740; O54744; Q91W03;', 'KD00141', 'Mus musculus (Mouse)', 'Kif2a', '#Kinesin-like protein KIF2A#Kinesin-2', '-', '-', '16563'),
(142, 'Q4IBU5', 'Probable kinetochore protein SPC24', 'GO:0000778===GO:0051455===GO:0031617', 22765, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MLLSEEPATLIHHTIENFNIAPDKTAVARVTESLATLQQARDLRVREAESSLKKLSRQLATHTSRHDDLVTSHSSADHASNIARLDTLKFRTAKAAADAETDAERLALTAADLKARLRELELQGVEGDAAANARRRDPVDDEVLLRLKVYRSLGIDIERDERDGEWSKAVIRNDRKGDVHVVNMDKKFSRFFYANYFWQTL', 201, 'Q4IBU5;', 'KD00142', 'Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084(Wheat head blight fungus) (Fusarium graminearum)', 'SPC24', '#Probable kinetochore protein SPC24', '-', '-', '2786593'),
(143, 'Q5PQM2', 'Kinesin light chain 4', 'GO:0003777', 68964, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity). {ECO:0000250}.', 'MSGLVLGQRDEPAGHRLSQEEILGSTRLVSQGLESLHSEHQAVLQSLSHTIECLQQGGHEEGLVHEKARQLRRSMENIELGLSEAQVMLALASHLSTVESEKQKLRAQVRRLCQENQWLRDELAGTQQRLQRSEQAVAQLEEEKKHLEFLRQLRQYDEDGHSMEEKEGDASKDSLDDLFPNEEEEDSSNDLSRGQGAAAAQQGGYEIPARLRTLHNLVIQYAAQGRYEVAVPLCKQALEDLERTSGRGHPDVATMLNILALVYRDQNKYKEAAHLLNDALSIRESTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCQRALEIREKVLGTDHPDVAKQLNNLALLCQNQGKYEAVERYYQRALAIYERQLGPDNPNVARTKNNLASCYLKQGKYSEAETLYKEILTRAHVQEFGSVDDDHKPIWMHAEEREEMSRSRSRESGTPYAEYGGWYKACRVSSPTVNTTLRNLGALYRRQGKLEAAETLEECALRSRKQGTDPISQTKVAELLGEGDGRKTMQEGPGDSVKFEGGEDASVAVEWSGDGSGTLQRSGSLGKIRDVLRRSSELLVRKLQGTEPRPSSSNMKRAASLNYLNQPNAAPLQTSRGLSASTVDLSSSS', 619, 'Q5PQM2;', 'KD00143', 'Rattus norvegicus (Rat)', 'Klc4', '#Kinesin light chain 4#KLC 4#Kinesin-like protein 8', '-', '-', '316226'),
(144, 'P07199', 'Major centromere autoantigen B', 'k', 65171, 'Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA; called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.', 'MGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVSCSGVARARARNAAPRTPAAPASPAAVPSEGSGGSTTGWRAREEQPPSVAEGYASQDVFSATETSLWYDFLPDQAAGLCGGDGRPRQATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQAGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLAAQSLDTSGLRHVQLAFFPPGTVHPLERGVVQQVKGHYRQAMLLKAMAALEGQDPSGLQLGLTEALHFVAAAWQAVEPSDIAACFREAGFGGGPNATITTSLKSEGEEEEEEEEEEEEEEGEGEEEEEEGEEEEEEGGEGEELGEEEEVEEEGDVDSDEEEEEDEESSSEGLEAEDWAQGVVEAGGSFGAYGAQEEAQCPTLHFLEGGEDSDSDSEEEDDEEEDDEDEDDDDDEEDGDEVPVPSFGEAMAYFAMVKRYLTSFPIDDRVQSHILHLEHDLVHVTRKNHARQAGVRGLGHQS', 599, 'P07199; Q96EI4;', 'KD00144', 'Homo sapiens (Human)', 'CENPB', '#Major centromere autoantigen B#Centromere protein B#CENP-B', '-', 'ENSG00000177946', '-'),
(145, 'Q753N1', 'Probable kinetochore protein NDC80', 'GO:0034501===GO:0000778===GO:0051315===GO:0051455===GO:0031617===GO:0031262', 75839, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MAERRGSSGANGVLNSLNPQRFTSQIPSIGGNTNKKGVPGTNAALTDMINKSLARNGRSSLSRPVPEVRKSLRRSLRSSQRPSIVPGGGPSAYGALQSTRDPRPLRDKNYQAVLQQEIFDYLQSRKFDIETGHAISLKSLKQPTQKDFICIFRWLYRRLDPGYSFKRSLETEVYSILKTIQYPFLDTINKSQISAVGGSNWHKFLGMLHWLMNTSQRLDSCLHKLDESKTMQLTQDITILNQPVTTLDEQDEKHEQYELMVERLFIEYISKCYKSFINMEDDFSPFKEELEIGFDRFVHIIETDINNLGRQEEMLQQDCEMFAARCEGLKLARSKHQALKGDLVKFQNYINAMKNKAEDWPRKLNQMVEEINEKKGLIKDIHAEIDKLRQALSQEDIQEIDQMNQQRDTFSKMLDTVSSKLDNLTGSVKSQKLNLESSSKVFLDTLEKFNASINGFVLARNNLQHPINPAELLIPVKANITLTDSTAITPSTILEGCTDILSSIKPNLLKVNKEIDERISALQTENNQLEKELRGLRDTITSKGHMLESMENELSNIKSEYDEYQQVSHSKLLSQRIEIEKLERKIQNDRHKTQQRVAQAEQEIEDAAFKLKELTLKIQQERVVLHRKLIKVIEYVVSFKMDVQGSIEALHDFSVEQLESL', 661, 'Q753N1;', 'KD00145', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '4622091'),
(146, 'Q9VA00', 'Protein zwilch', 'GO:0000776===GO:0000777===GO:0005828===GO:1990423===SCL===k', 72442, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin; Mad2 complexes and spindly/CG15415 onto kinetochores. {ECO:0000269|PubMed:12686595; ECO:0000269|PubMed:15886105; ECO:0000269|PubMed:17576797}.', 'MSASANLANVYAELMRRCGESYTITYGAPPTYLVSMVGAAEAGKKIVLVFKEDRNGAVARLRTTPTRAAPKKEGSADLDLTGSPLKDDCLVDAIADLSIDLQLDHSNPWKLEEEYQRGIPVDKARSIVCSEFLQLAEGLGSVWFLCDGSDLGQTQLLQYEFNPTHFSRGILSYQGVRPAYLVTSQALVRHHGKTPDETLIENSYQVNPHMRLRCSWTSSAALPLLVNLNDCDVALNHTFRVGDCGPLTQDFMNQLRILVYIREDIVSYHTDVKQGVSRDPTYRCGSGIDMDELRESINQTMTDVSGLIGRYSISNAEFDIEDVVQRAKVRQLTDLTDKLWELLKCCHSYKDLKIAFSMLFQCAARCNIVNTPTNKNRLAKIITELANRRLAMPCLSGAEPLELLLEIGLEKLYKDYEFIYTESKMCSTNLLKDDSSGASMDDGSPQNLPQLRKSLHNAVRGDPTPGAGMRKTLLHHHGAVNSRSTKYAGSDDDAGFKNSHFDEHESTERISKLFQIHCTLEHLLMMHIHLNLANVYNDVCSELLKKPPKLVESIDDQLSDVMDIRLSAHYVRDHLDGKDPYSRHITMRSHNKFRELKTTFYFNSENICPPNLAQCFQCDDKEMVKERTYHSWIYHKIRSLK', 641, 'Q9VA00; Q95TU6;', 'KD00146', 'Drosophila melanogaster (Fruit fly)', 'zwilch', '#Protein zwilch', '-', '-', '59247'),
(147, 'Q9H081', 'Protein MIS12 homolog', 'GO:0051382===GO:0000444===k', 24140, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis. {ECO:0000269|PubMed:12515822; ECO:0000269|PubMed:15502821; ECO:0000269|PubMed:16585270}.', 'MSVDPMTYEAQFFGFTPQTCMLRIYIAFQDYLFEVMQAVEQVILKKLDGIPDCDISPVQIRKCTEKFLCFMKGHFDNLFSKMEQLFLQLILRIPSNILLPEDKCKETPYSEEDFQHLQKEIEQLQEKYKTELCTKQALLAELEEQKIVQAKLKQTLTFFDELHNVGRDHGTSDFRESLVSLVQNSRKLQNIRDNVEKESKRLKIS', 205, 'Q9H081; Q96N24;', 'KD00147', 'Homo sapiens (Human)', 'MIS12', '#Protein MIS12 homolog', '-', 'ENSG00000117697', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(148, 'Q80TV8', 'CLIP-associating protein 1', 'GO:0000776===GO:0000777===GO:0043515===GO:0005828', 169227, '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 (By similarity). {ECO:0000250}.', 'MEPRMESCLAQVLQKDVGKRLQVGQELIDYFSDRQKSADLEHDQTLLDKLVDGLATSWVNSSNYKVVLLGMDILSALVTRLQDRFKAQIGTVLPSLIDRLGDAKDSVREQDQTLLLKIMDQAANPQYVWDRMLGGFKHKNFRTREGICLCLIATLNASGAQTLTLSKIVPHICNLLGDPNSQVRDAAINSLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGNMIQSANEKNFDDEDSVDGNRPSSASSSSSKAPSSSRRNVNLGTTRRLMSSSLGSKSSAAKEGAGAVDEEDFIKAFDDVPVVQIYSSRDLEESINKIREILSDDKHDWEQRVNALKKIRSLLLAGAAEYDNFFQHLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAIMPTIFNLIPNSAKIMATSGVVAVRLIIRHTHIPRLIPVITSNCTSKSVAVRRRCFEFLDLLLQEWQTHSLERHISVLAETIKKGIHDADSEARIEARKCYWGFHSHFSREAEHLYHTLESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTASRGSTVSTKSVSTTGSLQRSRSDIDVNAAASAKSKVSSSSGSPAFSSAAALPPGSYASLGRIRTRRQSSGSTTNVASTPDSRGRSRAKVVSQSQRSRSANPAGAGSRSSSPGKLLGSGLAGGSSRGPPVTPSSEKRSKIPRSQGCSRETSPNRIGLARSSRIPRPSMSQGCSRDTSRESSRDTSPARGFTPLDRFGLGQSGRIPGSVNAMRVLSTSTDLEAAVADALKKPVRRRYEPYGMYSDDDANSDASSVCSERSYGSRNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLLGLQNLLKSQRTLSRVELKRLCEIFTRMFADPHSKRVFSMFLETLVDFIIIHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQIVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNTGVGSPSNTIGRTPSRHPSSRTSPLTSPTNCSHGGLSPSRLWGWSADGLSKPPPPFSQPNSIPTAPSHKTLRRSYSPSMLDYDTENLNSEEIYSSLRGVTEAIEKFSFRSQEDLNEPIKRDGKKDCDIVSRDGGAASPATEGRGGSEIEGGRMALDNKTSLLNTQPPRAFPGPRAREYNPYPYSDTINTYDKTALKEAVFDDDMEQLRDVPIDHSDLVADLLKELSNHNERVEERKGALLELLKITREDSLGVWEEHFKTILLLLLETLGDKDHSIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLASSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVVERITKESLLQLLVDIIPGLLQGYDNTESSVRKASVFCLVAIYSVIGEDLKPHLAQLTGSKMKLLNLYIKRAQTTNSNSSSSSDVSTHS', 1535, 'Q80TV8; Q505G6; Q6DI75; Q6PG14; Q8BNS4; Q99JH5; Q99JI2; Q9CVU1;', 'KD00148', 'Mus musculus (Mouse)', 'Clasp1', '#CLIP-associating protein 1#Cytoplasmic linker-associated protein 1', '-', '-', '76707'),
(149, 'Q5RJQ4', 'NAD-dependent protein deacetylase sirtuin-2', 'GO:0051987', 39319, 'NAD-dependent protein deacetylase; which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. Participates in the modulation of multiple and diverse biological processes such as cell cycle control; genomic integrity; microtubule dynamics; cell differentiation; metabolic networks; and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents; and hence allowing proper inheritance of chromosomes. Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1; then allowing progression through mitosis. Associates with both chromatin at transcriptional start sites (TSSs) and enhancers of active genes. Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 ''Lys-20'' methylation (H4K20me1) during early mitosis. Specifically deacetylates histone H4 at ''Lys-16'' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by SETD8 leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle; and mitotic S-phase progression. Deacetylates SETD8 modulating SETD8 chromatin localization during the mitotic stress response. Deacetylates also histone H3 at ''Lys- 57'' (H3K56ac) during the mitotic G2/M transition. During oocyte meiosis progression; may deacetylate histone H4 at ''Lys-16'' (H4K16ac) and alpha-tubulin; regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function. Deacetylates alpha-tubulin at ''Lys-40'' and hence controls neuronal motility; oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells. Phosphorylation at Ser-330 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation; negatively regulating cell adhesion; cell migration and neurite outgrowth during neuronal differentiation. Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination. Involved in several cellular metabolic pathways. Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability. Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme; and therefore; stimulates the production of cytosolic NADPH to counteract oxidative damage. Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis. Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity. Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells. Deacetylates FOXO1 in response to oxidative stress or serum deprivation; thereby negatively regulating FOXO1-mediated autophagy. Deacetylates a broad range of transcription factors and co- regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation. Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation. Inhibits transcriptional activation by deacetylating p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions. Plays a role as tumor suppressor. {ECO:0000269|PubMed:17344398; ECO:0000269|PubMed:21949390; ECO:0000269|PubMed:22943040}.', 'MDFLRNLFTQTLGLGSQKERLLDELTLEGVTRYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYANLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFIRLLKEKGLLLRCYTQNIDTLERVAGLEPQDLVEAHGTFYTSHCVNTSCGKEYTMSWMKEKIFSEATPKCEKCQNVVKPDIVFFGENLPPRFFSCMQSDFSKVDLLIIMGTSLQVQPFASLISKAPLATPRLLINKEKTGQTDPFLGMMMGLGGGMDFDSKKAYRDVAWLGDCDQGCLALADLLGWKELEDLVRREHANIDAQSGSQASNPSATVSPRKSPPPAKEAARTKEKEEH', 350, 'Q5RJQ4;', 'KD00149', 'Rattus norvegicus (Rat)', 'Sirt2', '#NAD-dependent protein deacetylase sirtuin-2#3.5.1.-#Regulatory protein SIR2 homolog 2#SIR2-like protein 2', '-', '-', '361532'),
(150, 'P28738', 'Kinesin heavy chain isoform 5C', 'GO:0003777', 109275, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Mediates dendritic trafficking of mRNAs. {ECO:0000269|PubMed:19608740}.', 'MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKALKSVLQHLEMELNRWRNGEAVPEDEQISAKDQKSLEPCDNTPIIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAVRGGGGGSSNSTHYQK', 956, 'P28738; Q6NXI9; Q9Z2F8;', 'KD00150', 'Mus musculus (Mouse)', 'Kif5c', '#Kinesin heavy chain isoform 5C#Kinesin heavy chain neuron-specific 2', '-', '-', '16574'),
(151, 'P39731', 'Kinetochore-associated protein MTW1', 'GO:0034501===GO:0000818===c;k', 33243, 'Acts as essential component of the kinetochore MIND complex; which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules. {ECO:0000269|PubMed:14602074; ECO:0000269|PubMed:14633972}.', 'MSAPTMRSTSILTEHLGYPPISLVDDIINAVNEIMYKCTAAMEKYLLSKSKIGEEDYGEEIKSGVAKLESLLENSVDKNFDKLELYVLRNVLRIPEEYLDANVFRLENQKDLVIVDENELKKSEEKLREKVNDVELAFKKNEMLLKRVTKVKRLLFTIRGFKQKLNELLKCKDDVQLQKILESLKPIDDTMTLLTDSLRKLYVDSESTSSTEEVEALLQRLKTNGKQNNKDFRTRYIDIRTNNVLRKLGLLGDKEDEKQSAKPDARTQAGDIVSIDIEEPQLDLLDDVL', 289, 'P39731; D6VPI3;', 'KD00151', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MTW1', '#Kinetochore-associated protein MTW1#Mis12-like protein', '-', '-', '851197'),
(152, 'Q3ZCF0', 'Dynactin subunit 2', 'GO:0000776', 44294, 'Modulates cytoplasmic dynein binding to an organelle; and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development (By similarity). {ECO:0000250}.', 'MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELTSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGEYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLTDPDGALAKRLLLQLEATKNSKGTGSGGKTTSGTPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQGACLMDTVELLQAKVGALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQSKVHQLYETIQRWSPIAASLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMIACSLKDNATLLTQVQTTMCENLSTIEGNFANIDERMKKLGK', 403, 'Q3ZCF0;', 'KD00152', 'Bos taurus (Bovine)', 'DCTN2', '#Dynactin subunit 2', '-', '-', '527201'),
(153, 'Q29RT6', 'Kinesin-like protein KIF20A', 'GO:0003777', 100044, 'Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1; involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility.', 'MSQGILSPPAGLLSDEEVVVSPMFESTAADLGSVIRKDLLSDCSVISTSLEDKQVPSEDGTEKVKVYLRVRPLLPSELERQEDQGCVCIENMETLALQAPKDSFAQKSNERGIGQATHRFTFSQIFGPEVGQASFFNLTVKEMVKDVLKGQNWLIYTYGVTNSGKTYTIQGTIKDGGILPRSLALIFNSLQGQLHPTPNLKPLFSNEVMWLDSKQIRQEELKKLALLNGGLQEEELSTSLKKSVYIDSRMGTSTSFDSGIAGLSSSSQFPSSSQLDEMSHRWAQPDTVPVSVPADLRFSIWISFFEIYNELLYDLLEPPSQQRKRQTLRLCEDQNGNPYVKDLNWIHVQDAEEAWKLLKVGRKNQSFASTHLNQNSSRSHSIFSIRILHLQGEGDIIPKISELSLCDLAGSERCKDQKSGERLKEAGNINTSLHTLGRCIAALRQNQQNRSKQNLVPFRDSKLTRVFQGFFTGRGRSCMIVNVNPCASTYDETLHVAKFSAIASQLVHAPPVQLGFPSIHSFLKEHSLRASPSLETGAKTDPGLGDDIENEVDISTYGKEELLQVVEAMKALLLKERQEKLRLEVQLRDEICNEMVEQMQQREQWCSEHLDTQKELLEELYEDKLTILKESLTSFYQEELQERDEKIKELEALLQEARQQQVAHQPSGSELSLRRSQRLTSVSTQQFHEIKAKLEQCKAELNSTTEELQKYQKMLEPPPSAKPFIVDVDKKLEEGQKNIRLLRTELQKLGESLQSAERACCHNTGAGKLRQALATCDDILIKQDQTLAELQNNMTLVKLDLRKKAACIAEQYHTVLKLQGQASTKKRLGANQENQQPNQQPPGKKPFLRNLLPRTPTCQSSTDCSPYARILRSRRSPLLKSGPFGKKY', 888, 'Q29RT6;', 'KD00153', 'Bos taurus (Bovine)', 'KIF20A', '#Kinesin-like protein KIF20A', '-', '-', '527854'),
(154, 'P29295', 'Casein kinase I homolog HRR25', 'GO:0051455===GO:0033551===c;k;m', 57340, 'Associated with repair of damaged DNA and meiosis. Phosphorylates serine and threonine. Can use casein as a substrate.', 'MDLRVGRKFRIGRKIGSGSFGDIYHGTNLISGEEVAIKLESIRSRHPQLDYESRVYRYLSGGVGIPFIRWFGREGEYNAMVIDLLGPSLEDLFNYCHRRFSFKTVIMLALQMFCRIQYIHGRSFIHRDIKPDNFLMGVGRRGSTVHVIDFGLSKKYRDFNTHRHIPYRENKSLTGTARYASVNTHLGIEQSRRDDLESLGYVLIYFCKGSLPWQGLKATTKKQKYDRIMEKKLNVSVETLCSGLPLEFQEYMAYCKNLKFDEKPDYLFLARLFKDLSIKLEYHNDHLFDWTMLRYTKAMVEKQRDLLIEKGDLNANSNAASASNSTDNKSETFNKIKLLAMKKFPTHFHYYKNEDKHNPSPEEIKQQTILNNNAASSLPEELLNALDKGMENLRQQQPQQQVQSSQPQPQPQQLQQQPNGQRPNYYPEPLLQQQQRDSQEQQQQVPMATTRATQYPPQINSNNFNTNQASVPPQMRSNPQQPPQDKPAGQSIWL', 494, 'P29295; D6W3G5;', 'KD00154', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'HRR25', '#Casein kinase I homolog HRR25#2.7.11.1', '-', '-', '855897'),
(155, 'Q96EA4', 'Protein Spindly', 'GO:0043515===GO:0034501===GO:0000940===c;k', 70172, 'Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. {ECO:0000255|HAMAP-Rule:MF_03041; ECO:0000269|PubMed:17576797; ECO:0000269|PubMed:19468067}.', 'MEADIITNLRCRLKEAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENMKLRAKLDELKLKYEPEETVEVPVLKKRREVLPVDITTAKDACVNNSALGGEVYRLPPQKEETQSCPNSLEDNNLQLEKSVSIYTPVVSLSPHKNLPVDMQLKKEKKCVKLIGVPADAEALSERSGNTPNSPRLAAESKLQTEVKEGKETSSKLEKETCKKLHPILYVSSKSTPETQCPQQ', 605, 'Q96EA4; B4E393; C9JS47; Q8TEC8; Q9HD44; Q9NX97;', 'KD00155', 'Homo sapiens (Human)', 'SPDL1', '#Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041}#hSpindly#Arsenite-related gene 1 protein#Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041}#Rhabdomyosarcoma antigen MU-RMS-40.4A#Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041}', '-', 'ENSG00000040275', '-'),
(156, 'Q3E829', 'MHF histone-fold complex subunit 2', 'GO:0051382', 9050, 'DNA-binding component of a FANCM-MHF complex involved in DNA damage repair and genome maintenance (PubMed:20347428). FANCM- MHF promotes gene conversion at blocked replication forks (By similarity). {ECO:0000250|UniProtKB:O74896; ECO:0000269|PubMed:20347428}.', 'MLSKEALIKILSQNEGGNDMKIADEVVPMIQKYLDIFIDEAVLRSLQSHKDINGERGDKSPLELSHQDLERIVGLLLMDM', 80, 'Q3E829; D6VRI9;', 'KD00156', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MHF2', '#MHF histone-fold complex subunit 2 {ECO:0000305|PubMed:20347428}#MPH1-associated histone-fold protein 2 {ECO:0000303|PubMed:20347428}', '-', '-', '1466431'),
(157, 'Q5U4X5', 'Kinetochore protein NDC80 homolog', 'GO:0000776===GO:0000777===GO:0031262', 74637, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MRRSSVTNRQSLLPLRVQDANRMGLTTPQSKDRQGFGKLSMSKPHSGTSERKTSFFGKRMSNGTARTSQYGAFGGTEKIKDPRPLHDKAFIQQCIRQLCEFLNENGYSQTLTVKSLQGPSTKDFLKIFAFIYTFICPNYENPESKFEEEIPRIFKELGYPFALSKSSMYTVGAPHTWPQIVAALVWLIDCVKLCCVLRSENPVFEEPQMGEQSENGIDFNQLFLDYTVRCYDQFMEGRDTFEEYDADMCIRLKEAYHVDESNLEALQQESRRLLEEIERLEKEKENEPDRLASMRKLKVSLQADIQKYQNYLTEIESHSTLLEQRVSSVSEDLEATELESRAVQQENLRLKNILDNQKYSVADIERIKYEENELQQTIAKLTKDLDEDKQQLWSEELKYAKMKESVETQLSEFHKIGRKVRLIPPTAEYANGYDFQIQCNLDSEQSSLIHYRNKINVPLVEILSQSEGQIAGATNKKMGVEDMVEQLNTLIGEKKNEVKVQKDEAQKLEETYQQKVEEAEEDEKRWISEIESLEKHRQLLESGVNKSLDEALKDLQKEQQELQLVEHQTEEEMRQVENKLVRVVHAVANHVAVIEKHLEEKRLKVEREYEEFMKEDLLLDLRELLDKYKEKARVLDSPPY', 640, 'Q5U4X5;', 'KD00157', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'ndc80', '#Kinetochore protein NDC80 homolog#Kinetochore protein Hec1#Kinetochore-associated protein 2', '-', '-', '496580'),
(158, 'Q9C107', 'Minichromosome loss protein 1', 'k', 90986, 'Has a role in regulating DNA replication complexes. Acts as a regulator of post DNA replication initiation. Associates with chromatin during G1 and S phases of mitosis. Required for the transcriptional repression of the outer repeats of the centromeric region. Acts as a polymerase alpha replication accessory factor and is important for S-phase DNA damage survival. Plays a role in lagging-strand synthesis and Ozaki fragment processing; in addition to DNA repair. {ECO:0000269|PubMed:12455694; ECO:0000269|PubMed:15643072; ECO:0000269|PubMed:15915339; ECO:0000269|PubMed:16997270}.', 'MAGNRLVPRYAHTDGLTRLAYTRDGKFLLTVGSNQVIRKFQVGSDEEPDSIDNHQDPITGIAVAENYFCTCSEDATVCVYPIDSPTEHTLLARTTLPIRDVAYSVDGNWIAIASDETAVKVVSSTDSSQIFSLRPAKASNKHVTYSPNGNFLAVSSCNGILYFYDTQTRELIKFLTNTIASLEAESEICSKAAWHPKNGTFAVASTDHFVSVISPDDWLPLYKLLPKENHSGVTDISWSSNGMYIAASFKKGGILIWDTQSHEVVVELPYSTVVALAWQPFENVLSFTTNQGILYSCPDVIPKSILKEENDPTKPLTSSKSKNRTSKELDDLFGSDDEQSQNVNDLDGNSANEENEFINHDGLDSSLDLDGDSYMVDENDLNLAKKRKQKALIDRTTTIENGSSKRRLLQASIHKPVHTGSTPWQGNRRYLCLNLVGFIWTVQQDAEHNTITVEFHDETTHRKYHFVDDQKFEMACLDHEGALYASPATESSPGVIYYKAHVDWSRKSEWAMALPMENESPVTISLSSSVVLVCTSAGYVRVFSRQGFPISIHRSKHLPFVACSSFQDTIITIANDGLSSDGNSRLVYSIEDISRDEMLQTGDGVALPPQGTLESVFFSDVGDPYIYDSTGVLLVLMHWRIPGQAKWIPVLDTNELERRKSRQESYWPVTVADNQFHCILLKGASRYPYFPRPMFTEFDFRIPCNTNNPDASTSVPVLEELQLRNKLFLTLLEDSIGDGDVTEDEKISIARLEANIDKALLQLIQKACLEERIERVYELTKTLRRTTSIAAAQKIALHHSLTNVAEKIGNLLSNV', 815, 'Q9C107;', 'KD00158', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'mcl1', '#Minichromosome loss protein 1#DNA polymerase alpha accessory factor Mcl1', '-', '-', '2543387'),
(159, 'P47074', 'Spindle assembly checkpoint component MAD3', 'k', 59521, 'Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20. {ECO:0000269|PubMed:10704439}.', 'MKAYAKKRISYMPSSPSQNVINFEEIETQKENILPLKEGRSAAALSKAIHQPLVEINQVKSSFEQRLIDELPALSDPITLYLEYIKWLNNAYPQGGNSKQSGMLTLLERCLSHLKDLERYRNDVRFLKIWFWYIELFTRNSFMESRDIFMYMLRNGIGSELASFYEEFTNLLIQKEKFQYAVKILQLGIKNKARPNKVLEDRLNHLLRELGENNIQLGNEISMDSLESTVLGKTRSEFVNRLELANQNGTSSDVNLTKNNVFVDGEESDVELFETPNRGVYRDGWENFDLKAERNKENNLRISLLEANTNLGELKQHEMLSQKKRPYDEKLPIFRDSIGRSDPVYQMINTKDQKPEKIDCNFKLIYCEDEESKGGRLEFSLEEVLAISRNVYKRVRTNRKHPREANLGQEESANQKEAEAQSKRPKISRKALVSKSLTPSNQGRMFSGEEYINCPMTPKGRSTETSDIISAVKPRQLTPILEMRESNSFSQSKNSEIISDDDKSSSSFISYPPQR', 515, 'P47074; D6VWG4;', 'KD00159', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'MAD3', '#Spindle assembly checkpoint component MAD3#Mitotic MAD3 protein', '-', '-', '853439'),
(160, 'Q9VQ69', 'CG31672-PALD22825p', 'k', 63440, '', 'MSSMAKSPDMRTPGCCSPLRTKELLERQRSSRCTPAKGYLTPRNCQSPKHPEMRIPSIFVTDADYGLERPKQLLQRLERSLYRSSSASKVPPKHSLLASQNRQRTWEGPKTPEFRRTNKTIPASEPRPRRAKELLEDLRSKHQGTPATKIPSQRNPKENQELSKSHTCIPSSEPQPIRPKLILERERQESITNRLASTSIDRLKTKPPRSSFTSSRLLVPQMGFSYPKDPKRLHESDKGIKLTTSKRKLDFKTELGTDWLRRELEKIGKEWRKKTDYQLRQLISGFVKQLVRLLPFNGITFSHLSRDCYVQQMVEALQQLQYTKKVNKSWLQTPNSTQAIAHVLELLNFLLDVLEHRKGEGMCALPVVSEKQRIEQLASASGTSYDVMSLQQKFENIKIEKERLNNYQESLMPESPVSKDMDKVTERDGNQDFVRLLDFQKETLHELQLQRLRLQEFSELVSLAKIKLKRCCKANKQCIEAFNDQIQDLADCVVLRNRNIGLLTQLHLNDNPKEEELHERMKQLQRLYEDNYSNLLQLNIKPPQGSP', 547, 'Q9VQ69; Q961C7;', 'KD00160', 'Drosophila melanogaster (Fruit fly)', 'Kebab', '#CG31672-PA {ECO:0000313|EMBL:AAF51310.2}#LD22825p {ECO:0000313|EMBL:AAK93101.1}', '-', '-', '48440'),
(161, 'Q9W1U4', 'Kinesin-like protein Klp59C', 'GO:0000777===GO:0005828===GO:0003777===SCL===k', 70053, 'Required during anaphase to drive sister chromatid separation to actively depolymerize kinetochore microtubules at their kinetochore-associated plus ends; thereby contributing to chromatid mobility through a "Pac-man" mechanism. {ECO:0000269|PubMed:14681690}.', 'MDKLSIEQKIFIRRSDGRVHLAEIIKLEGGDSKLITVEWPEGHTVRGKELPLELVVLMNPHIFDSPRCSGGNAASANQTASISPRSMKQRIATGSLSPVLATAPPRQQTAPPVREDEVVHQAERMRKERERRREAQARTRLDREQGKNEDPGNPNWEVARMIRLQREQMESQRVRSGTTNERINCHQIMVCVRKRPLRRKELADREQDVVSIPSKHTLVVHEPRKHVNLVKFLENHSFRFDYVFDEECSNATVYEFTARPLIKHIFDGGMATCFAYGQTGSGKTYTMGGQFPGRHQSSMDGIYAMAAKDVFSTLKTVPYNKLNLKVYCSFFEIYGTRVFDLLMPGKPQLRVLEDRNQQVQVVGLTQNPVQNTAEVLDLLELGNSVRTSGHTSANSKSSRSHAVFQIVLRSAAGEKLHGKFSLIDLAGNERGADNSSADRQTRLEGSEINKSLLVLKECIRALGRQSSHLPFRGSKLTQVLRDSFIGGKKVKTCMIAMISPCLHSVEHTLNTLRYADRVKELSVESIPSKRMPDANLGSTSMSDIVCQSSTQRLFPCASSTSMPGGGNQAQQHTNTANDLNRSQKPTSKPTYPTSGQQLVQRKGSSQREASMMLTKSLAQFRGRNFP', 626, 'Q9W1U4;', 'KD00161', 'Drosophila melanogaster (Fruit fly)', 'Klp59C', '#Kinesin-like protein Klp59C#Kinesin-like protein at cytological position 59C', '-', '-', '37671'),
(162, 'Q92624', 'Amyloid protein-binding protein 2', 'GO:0003777', 66853, 'May play a role in intracellular protein transport. May be involved in the translocation of APP along microtubules toward the cell surface. {ECO:0000269|PubMed:9843960}.', 'MAAVELEWIPETLYNTAISAVVDNYIRSRRDIRSLPENIQFDVYYKLYQQGRLCQLGSEFCELEVFAKVLRALDKRHLLHHCFQALMDHGVKVASVLAYSFSRRCSYIAESDAAVKEKAIQVGFVLGGFLSDAGWYSDAEKVFLSCLQLCTLHDEMLHWFRAVECCVRLLHVRNGNCKYHLGEETFKLAQTYMDKLSKHGQQANKAALYGELCALLFAKSHYDEAYKWCIEAMKEITAGLPVKVVVDVLRQASKACVVKREFKKAEQLIKHAVYLARDHFGSKHPKYSDTLLDYGFYLLNVDNICQSVAIYQAALDIRQSVFGGKNIHVATAHEDLAYSSYVHQYSSGKFDNALFHAERAIGIITHILPEDHLLLASSKRVKALILEEIAIDCHNKETEQRLLQEAHDLHLSSLQLAKKAFGEFNVQTAKHYGNLGRLYQSMRKFKEAEEMHIKAIQIKEQLLGQEDYEVALSVGHLASLYNYDMNQYENAEKLYLRSIAIGKKLFGEGYSGLEYDYRGLIKLYNSIGNYEKVFEYHNVLSNWNRLRDRQYSVTDALEDVSTSPQSTEEVVQSFLISQNVEGPSC', 585, 'Q92624; A8K862; O95095; Q8WVC9;', 'KD00162', 'Homo sapiens (Human)', 'APPBP2', '#Amyloid protein-binding protein 2#Amyloid beta precursor protein-binding protein 2#APP-BP2#Protein interacting with APP tail 1', '-', 'ENSG00000062725', '-'),
(163, 'Q8VYZ0', 'E3 ubiquitin-protein ligase ORTHRUS 2', 'k', 71467, 'E3 ubiquitin-protein ligase. Participates in CpG methylation-dependent transcriptional regulation and epigenetic transcriptional silencing. Mediates ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. Promotes methylation-mediated gene silencing leading; for example; to early flowering. Associates with methylated DNA; and can bind to CpG; CpNpG; and CpNpN DNA motifs; with a strong preference for methylated forms; and with highest affinity for CpG substrate. Probably acts at the DNA methylation?histone interface to maintain centromeric heterochromatin. {ECO:0000269|PubMed:17239600; ECO:0000269|PubMed:17242155; ECO:0000269|PubMed:18643997; ECO:0000269|PubMed:18704160}.', 'MARDIQLPCDGDGVCMRCKSNPPPEESLTCGTCVTPWHVSCLSSPPKTLASTLQWHCPDCSGEIDPLPVSGGATGFESAGSDLVAAIRAIEADESLSTEEKAKMRQRLLSGKGVEEDDEEEKRKKKGKGKNPNLDVLSALGDNLMCSFCMQLPERPVTKPCGHNACLKCFEKWMGQGKRTCGKCRSIIPEKMAKNPRINSSLVAAIRLAKVSKSAAATTSKVFHFISNQDRPDKAFTTERAKKTGKANAASGKIYVTIPPDHFGPIPAENDPVRNQGLLVGESWEDRLECRQWGAHFPHVAGIAGQSTYGAQSVALSGGYKDDEDHGEWFLYTGSGGRDLSGNKRTNKEQSFDQKFEKSNAALKLSCKLGYPVRVVRSHKEKRSAYAPEEGVRYDGVYRIEKCWRKVGVQGSFKVCRYLFVRCDNEPAPWTSDENGDRPRPIPNIPELNMATDLFERKETPSWDFDEGEGCWKWMKPPPASKKSVNVLAPEERKNLRKAIKAAHSNTMRARLLKEFKCQICQQVLTLPVTTPCAHNFCKACLEAKFAGKTLVRERSTGGRTLRSRKNVLNCPCCPTDISDFLQNPQVNREVAEVIEKLKTQEEDTAELEDEDEGECSGTTPEEDSEQPKKRIKLDTDATVSATIR', 645, 'Q8VYZ0; Q3ECM8; Q9FVS3;', 'KD00163', 'Arabidopsis thaliana (Mouse-ear cress)', 'ORTH2', '#E3 ubiquitin-protein ligase ORTHRUS 2#6.3.2.-#Protein VARIANT IN METHYLATION 1', '-', '-', '842157'),
(164, 'Q1MTQ7', 'Kinesin-like motor protein 9', 'GO:0003777', 71452, 'Kinesin-like motor protein ionvolved in anaphase B spindle elongation. {ECO:0000269|PubMed:19686686}.', 'MIQIFLRVKKAQPSSDASNKYGFLTVLNDYEILLESPEDSHAYRVSKSKTLEKASFTKVFPPSCTQLDVFSTICAPLIADSLVNMNDTLLFTLGVSGAGKTYTLFGPSDRPGVAFLALDALFYAIKGREASPQTVEFLRSQLEKCKIVEASKFLRGEAPLDIKVPNTEYYASHFPKIEEKNYQYAIYLSFAEIYNDRIFDLLEKASFFGHRHALSLKKSSTSDKKSIAGIQKVFVSNTTEAYKLIQKVLQLRKSTSTKSNSVSSRSHLIMSIELFKVCTKSNKFESCQIDLVDLAGSERTRSAETSGLLLREGASINRSLLTLGQCLEALRRKHEGKQHIIPFRQSKLTELLFHSGHLSGLAGINMLVNIDPFGSFDENAQVMRYSANAREILPPPLNENSGSQSPSHSLLQKSKNTSSTKALTSHLEQLQQENQQLRMLLADADSEMMNLEYEIRQQMTREMEERVSEVERTFLTKLLEESAQGIEYTDQKLEKMGGWMKKLQDENSEKTETIAQLEQIIEELHEELRSLEEESIKESSATQQNENQHKRSSRKLLYEDKQAIQEAHTINTKRKLWPQSTLIQAPNSDDEENVPSPSPKKKVVSPIKPLSPSRRPPLTSLYSGTTDIDINEL', 633, 'Q1MTQ7;', 'KD00164', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'klp9', '#Kinesin-like motor protein 9', '-', '-', '2539778'),
(165, 'Q9VLW2', 'Kinesin-like protein CG14535', 'GO:0003777', 120722, '', 'MATTSTSNMSRNGGFCGALQRAPPPMPPTLIRRLSSRECYGVGKVKVMLRVADRDRNSGGTEPDFMALDKKKRQVTLTDPRTACPPPQAAQERAPMVAAPKMFAFDNLFTGEDKQSDVCASALSEVIPAVLEGSDGCLLAMGYPATGQAQTVLGELGGGSGSGSASGSGVACSLGAAPCAIAWLYKGIQERRQKSGARFSVRVSAVGVSATKPDALSQDLLISHAAESDDSPGIYLRDDFLGGPTELRAPTAERAALFLDSALAGRLKSSGSTASGSSGCAAPLESALIFTLHVYQYSLSRKGGVAGGRSRLHIIDLGGCANRNGGLPLSGIGNILLAILSGQRHPPHKDHPLTPLLKDCLAPITCHVAIVAHVRPEQSYQDALSTIQIASRIHRLRRRKHRVPMPLAVGLAQGLGGNGSSAGSGADPSSSEISADTVIYMGPNDDATDGEHPPVYLPSLTAGDNRGVMSKALKGSGLEKPPSKSASNSPMMMKKAMAAEKAKKLPGSHTGSLKRQAGAGACSSPMIPHEQPQIQAMGSPIPIPRHMVSKGSMVPSPKGSPMRRAHPGAALEQLEAGMRKITEEQWIDGPRVSRAKVAEARHLMREVNHVKQCETWVDGPKSQSCRSLTACNLPAAGGSQTQGYGFMDAHKKTMIRQWVENQTTQVFQSTVSASNSPTALHWKLSQLKQKSLDLPDRPAFNPEPSLDLNQPCFESLPLLDPAPPDGDEDEDSGPSEVPPALPLLDDPLGSRDISQDNLHRMLSRHVSREQLHEAELVASRASSSHHPSQRSIDCGLQVTEEEIARTMSRDRDHDPSAHPLSALSHCDNISFVSSFNMACESFSECGERARQQFDQLARLHEIFTSQLAMAEVTPSAALFRTDIGSVFSEPVYHFNVGQSSVCSEPAYRLTPSPPKQPSHSPSQGSLPSLNGIMEIAGMDDYALLRQPDGASDPNLQKGEKRFTPQHDDICELDEKSMAAAVGKGNSLEDAQHKLNEITNILPLAAQSRLPLLPLNTSSEAYDSGHDSNSTPRTSKHSGISRRAESGYHSVATVRDSDESSFASGMSKGQRHRITVSGTGAVTSAGIGNYQRQCHKKRHRQDQAGNNKGLCNWLLTPFSCTYPETEGEISDF', 1131, 'Q9VLW2;', 'KD00165', 'Drosophila melanogaster (Fruit fly)', 'CG14535', '#Kinesin-like protein CG14535', '-', '-', '34073'),
(166, 'Q9WVC0', 'Septin-7', 'GO:0000777', 50508, 'Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements (By similarity). {ECO:0000250}.', 'MSVSARSAAAEERSVNCSTMAQPKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQGHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEEEKANWEAQQRILEQQNSSRTLEKNKKKGKIF', 436, 'Q9WVC0;', 'KD00166', 'Rattus norvegicus (Rat)', 'Sept7', '#Septin-7#CDC10 protein homolog', '-', '-', '64551'),
(167, 'Q12769', 'Nuclear pore complex protein Nup160', 'c;k', 162121, 'Involved in poly(A)+ RNA transport. {ECO:0000269|PubMed:11684705}.', 'MLHLSAAPPAPPPEVTATARPCLCSVGRRGDGGKMAAAGALERSFVELSGAERERPRHFREFTVCSIGTANAVAGAVKYSESAGGFYYVESGKLFSVTRNRFIHWKTSGDTLELMEESLDINLLNNAIRLKFQNCSVLPGGVYVSETQNRVIILMLTNQTVHRLLLPHPSRMYRSELVVDSQMQSIFTDIGKVDFTDPCNYQLIPAVPGISPNSTASTAWLSSDGEALFALPCASGGIFVLKLPPYDIPGMVSVVELKQSSVMQRLLTGWMPTAIRGDQSPSDRPLSLAVHCVEHDAFIFALCQDHKLRMWSYKEQMCLMVADMLEYVPVKKDLRLTAGTGHKLRLAYSPTMGLYLGIYMHAPKRGQFCIFQLVSTESNRYSLDHISSLFTSQETLIDFALTSTDIWALWHDAENQTVVKYINFEHNVAGQWNPVFMQPLPEEEIVIRDDQDPREMYLQSLFTPGQFTNEALCKALQIFCRGTERNLDLSWSELKKEVTLAVENELQGSVTEYEFSQEEFRNLQQEFWCKFYACCLQYQEALSHPLALHLNPHTNMVCLLKKGYLSFLIPSSLVDHLYLLPYENLLTEDETTISDDVDIARDVICLIKCLRLIEESVTVDMSVIMEMSCYNLQSPEKAAEQILEDMITIDVENVMEDICSKLQEIRNPIHAIGLLIREMDYETEVEMEKGFNPAQPLNIRMNLTQLYGSNTAGYIVCRGVHKIASTRFLICRDLLILQQLLMRLGDAVIWGTGQLFQAQQDLLHRTAPLLLSYYLIKWGSECLATDVPLDTLESNLQHLSVLELTDSGALMANRFVSSPQTIVELFFQEVARKHIISHLFSQPKAPLSQTGLNWPEMITAITSYLLQLLWPSNPGCLFLECLMGNCQYVQLQDYIQLLHPWCQVNVGSCRFMLGRCYLVTGEGQKALECFCQAASEVGKEEFLDRLIRSEDGEIVSTPRLQYYDKVLRLLDVIGLPELVIQLATSAITEAGDDWKSQATLRTCIFKHHLDLGHNSQAYEALTQIPDSSRQLDCLRQLVVVLCERSQLQDLVEFPYVNLHNEVVGIIESRARAVDLMTHNYYELLYAFHIYRHNYRKAGTVMFEYGMRLGREVRTLRGLEKQGNCYLAALNCLRLIRPEYAWIVQPVSGAVYDRPGASPKRNHDGECTAAPTNRQIEILELEDLEKECSLARIRLTLAQHDPSAVAVAGSSSAEEMVTLLVQAGLFDTAISLCQTFKLPLTPVFEGLAFKCIKLQFGGEAAQAEAWAWLAANQLSSVITTKESSATDEAWRLLSTYLERYKVQNNLYHHCVINKLLSHGVPLPNWLINSYKKVDAAELLRLYLNYDLLEEAVDLVSEYVDAVLGKGHQYFGIEFPLSATAPMVWLPYSSIDQLLQALGENSANSHNIALSQKILDKLEDYQQKVDKATRDLLYRRTL', 1436, 'Q12769; B4DYE8; B4E2J9; Q08AD3; Q7Z5X6; Q96GB3; Q9H660;', 'KD00167', 'Homo sapiens (Human)', 'NUP160', '#Nuclear pore complex protein Nup160#160 kDa nucleoporin#Nucleoporin Nup160', '-', 'ENSG00000030066', '-'),
(168, 'Q80U96', 'Exportin-1', 'GO:0000776', 123039, 'Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus; in association with RANBP3; binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm; disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1; respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap (By similarity). {ECO:0000250}.', 'MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFETLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLLEKRLNLREALMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDIPPRRQLYLTVLSKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTEIIMTKKLQNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTPLNPGSPVSNQMFIQDYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEERETALRQAQEEKHKLQMSVPGILNPHEIPEEMCD', 1071, 'Q80U96;', 'KD00168', 'Rattus norvegicus (Rat)', 'Xpo1', '#Exportin-1#Exp1#Chromosome region maintenance 1 protein homolog', '-', '-', '85252'),
(169, 'Q3ZCC9', 'Protein SEC13 homolog', 'GO:0000776', 35472, 'Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum; SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). As a component of the GATOR2 complex; inhibits GATOR1 complex; an inhibitor of the amino acid-sensing branch of the TORC1 pathway (By similarity). {ECO:0000250}.', 'MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILVADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWKEENGTWEKTHEHTGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGLGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDQPSGQKPNYIKKFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFVWTCDDASGNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGPVSTSVTEGQQNDQ', 322, 'Q3ZCC9;', 'KD00169', 'Bos taurus (Bovine)', 'SEC13', '#Protein SEC13 homolog#SEC13-like protein 1', '-', '-', '512530'),
(170, 'P13405', 'Retinoblastoma-associated protein', 'GO:0031134', 105367, 'Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated; active form of RB1 interacts with E2F1 and represses its transcription activity; leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and; in particular; that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1; SUV420H1 and SUV420H2; leading to epigenetic transcriptional repression. Controls histone H4 ''Lys-20'' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons; transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx; RB1 is dephosphorylated by calcineurin; which leads to release of the repressor complex (By similarity). {ECO:0000250}.', 'MPPKAPRRAAAAEPPPPPPPPPREDDPAQDSGPEELPLARLEFEEIEEPEFIALCQKLKVPDHVRERAWLTWEKVSSVDGILEGYIQKKKELWGICIFIAAVDLDEMPFTFTELQKSIETSVYKFFDLLKEIDTSTKVDNAMSRLLKKYNVLCALYSKLERTCELIYLTQPSSALSTEINSMLVLKISWITFLLAKGEVLQMEDDLVISFQLMLCVVDYFIKFSPPALLREPYKTAAIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFINSLGIVSSNGLPEVESLSKRYEEVYLKNKDLDARLFLDHDKTLQTDPIDSFETERTPRKNNPDEEANVVTPHTPVRTVMNTIQQLMVILNSASDQPSENLISYFNNCTVNPKENILKRVKDVGHIFKEKFANAVGQGCVDIGVQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTLQHLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKVEANLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDGEGPDNLEPACPLSLPLQGNHTAADMYLSPLRSPKKRTSTTRVNSAANTETQAASAFHTQKPLKSTSLALFYKKVYRLAYLRLNTLCARLLSDHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGADEADGSKHLPAESKFQQKLAEMTSTRTRMQKQRMNESKDVSNKEEK', 921, 'P13405; Q4VA62;', 'KD00170', 'Mus musculus (Mouse)', 'Rb1', '#Retinoblastoma-associated protein#pRb#Rb#pp105', 'BIOMD0000000242,Bai2003_G1phaseRegulation;BIOMD0000000568,Mueller2015 - Hepatocyte proliferation - T160 phosphorylation of CDK2;', '-', '19645'),
(171, 'F1M5M3', 'Inactive serine/threonine-protein kinase TEX14', 'GO:0000776===GO:0000777===GO:0008608', 162407, 'Required both for the formation of intercellular bridges during meiosis and for kinetochore-microtubule attachment during mitosis. Intercellular bridges are evolutionarily conserved structures that connect differentiating germ cells and are required for spermatogenesis and male fertility. Acts by promoting the conversion of midbodies into intercellular bridges via its interaction with CEP55: interaction with CEP55 inhibits the interaction between CEP55 and PDCD6IP/ALIX and TSG101; blocking cell abscission and leading to transform midbodies into intercellular bridges. Also plays a role during mitosis: recruited to kinetochores by PLK1 during early mitosis and regulates the maturation of the outer kinetochores and microtubule attachment. Has no protein kinase activity in vitro (By similarity). {ECO:0000250}.', 'MSRAVHFPVPCPVLLGTLTDDSLEAQLHEYAKQGNYVKVKKILKKGVCVDAVNTLGQSALFVAALLGYVKLVDVLVDYGSDPNHRCFDGSTPVHAAAFSGNQWILSKVLTAGGDLRLHDEKGRNPQAWALAAGKDRSTQMVEFMQRCASHMKAVIQGFSYDLLKKIDSPQRLIGSPPWFGGLIQGSPNSSPNRQPKPGIISAQNIYSFGFGKFYLTSGMQLTYPGSLPVIGEKEVIQADDEPTFSFFSGPYMVMTNLVWNRSRVTVKELNLPTHPHCSRLRLADLLIAEQEHSSNLRHPSLLQLMAVCLSRDLEKIRLVYERITVGTLFSVLHERRSQFPVLHMEMIVHLLLQIADALIYLHSRGFIHRSLSSYAVHIVSAGEARLTNLEYMMESQDSGAHRDMTRVPLPAQLYNWAAPEVVLQKTATVKSDIYSFSMIIQEILTDNIPWNGLDGSLVKETIALGNYLEADVRLPEPYYDIVKSGIHAKQKNRTMNLQDIRYILKNDLKEFIGAQKTQTTESPRGQRYEPHPDINICLGLTSEYQKDPPDLDIKELKETGSQPHSPTDHSFLTEKTLAPQTLDSSLSAQEPDNPNVPSASRLAEEVRSPTPSEASLYSFEINEIYSGCLTLGTDKEEECPGTASSPEGDKANQVDELPSLEEELDKMERELHCFCEEDKSFSDVDTDLSFEDGDWQSDSLSSLSLPEPTREAKGKTSSWSKTDEYVSKCVLNLKISQVMMQQSAEWLRKLEQEVDELEWAQKELDNQCRSLWDASLRFANTKFLSAVGPPSLTYLPPVMQLSEPKQPENGGNWLTLARPPGNERDFQEGNFSKKSEKLSACDWNPFTQASEESRGYCSEPNNQPPTLCGPGKQNTGEQLPSTEEAKESLERNTNQNIRRMESVSSEVCDTKSRNNEDAGEARSKWRLAVKEMAEKAVSGQLLVPPWNLQSSFESKVENESTPLPRPPIRGPESTDWQYILEYQREKDELKGNMKFGKMENSDCDKNKHSSWTGLQRFTSIIYPFFRNHEQPEHNEASQASCDTXCGEKFYSTSSPIEDDFERIQSSFAQPQGYVEENFQIREIFGKNAEILTKPQFQAVQCAEDEQEETLEETPKELKEKNISLTDIQDLSSITYEQDGCFKETSCKTPKLKHAPTSASTPLSPESISSAASHYEDCLENTFHVKRGSTFCWNGQEAMRTLSTKFTTVRERAKSLESLLASSKTLPAKLTDPKRLCMFGGACSSNISTAFVTSTHSTKRKSLPGELAEATSQHHIDELPPPAQELLDEIEQLKQQQVSSMVSLENTAHDLNVTENDKKHLEEQETNSSKDSSFLSSREIQDLEDTERAHSSLDEDLERLLQLPEENMTLLDPTKGSTREKKTKDQDMVEQKRKKKEGIKPERRKSDSFLGTLEEDELKPCFWKRLGWSEPSRIIVLDQSDLSD', 1443, 'F1M5M3;', 'KD00171', 'Rattus norvegicus (Rat)', 'Tex14', '#Inactive serine/threonine-protein kinase TEX14#Testis-expressed sequence 14#Testis-expressed sequence 14 protein', '-', '-', '-'),
(172, 'A1A4L0', 'Sorting nexin-4', 'GO:0005868', 52194, 'May be involved in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation (By similarity). {ECO:0000250}.', 'MEQAAPDPERLWQPAPLEPLSHPDAGLESMVGEETKGARDEGPGDGTMTENNFSLKKIEISVSEAEKRTGRNAMNMQETYTAYLIETRSVEHNDGQSVLTDSLWRRYSEFELLRNYLLVYYPHIVVPPLPEKRAEFVWHKLSADNMDPDFVERRRIGLENFLLRVASHPILCRDKIFYLFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFIELKHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRKHELMQYDLEMAAQDLASKKQQCEELATGTVRTFSLKGMTTKLFGQETPEQREARIKMLEEQIKEGEQQLKSKNLEGREFVRNAWADIERFKEQKNHDLKEALISYAVMQISMCKKGIQVWTNAKECFSKM', 450, 'A1A4L0;', 'KD00172', 'Bos taurus (Bovine)', 'SNX4', '#Sorting nexin-4', '-', '-', '519597'),
(173, 'P38650', 'Cytoplasmic dynein 1 heavy chain 1', 'GO:0003777', 532252, 'Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.', 'MSETGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGDAPAALEAALEEKSALEQMRKFLSDPQVHTVLVERSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRAPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPFFKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPIITNVAKQCYERGEKPKVTDFGDKVEDPTFLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDTGLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRKLMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVIVRVLRPQVTAVAQQNQGEAPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRDLPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTIESARVRGRSGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNTISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNRVQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVHELRITNQVIYLNPPIEECRYKLYQEMFAWKMIVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRSRDGPVALEESYSAVMGIVTEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLSKWQALLVQIRRARGTFDNAETKKEFGPVVIDYGKVQSKVNLKYDSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQRFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQALTIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLRQNLDGLLNQLKNFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQKNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDALSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRSLERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDSSVVLGISSREGEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSENVENALSNVGGGGNVGPLQSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLSQMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCELLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQSHYDFGLRALKSVLVSPGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSFCETMVPKLVAEDIPLLFSLLSDVFPGVQYHRGEMTDLREELKKVCKEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKALERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDNVRGELQKRQWIVFDGDVDPEWVENLNSVLDDNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDLLSTDMIFNNFLARLRTIPLDEGEDEAQRRRKGKEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFKLEHIMDLTRLRCLGSLFSMLHQGCRNVAQYNANHPDFPMQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETHKVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDMVALKHFPNIDKEKAMSRPILYSNWLSKDYIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNYIVPDYMPVVYDKLPQPPTHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRALRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEISDAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQVHFLYQYSLQFFLDIYHNVLYENPNLKGATDHTQRLSVITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTMGEPTYDAEFQHFLRGKEIVLSAGSTPKVQGLTVEQAEAVARLSCLPAFKDLIAKVQADEQFGIWLESSSPEQTVPYLWTEETPATPIGQAIHRLLLIQAFRPDRLLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQADKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPRVPVNLLRAGRIFVFEPPPGVKANMLRTFSSIPVSRMCKSPNERARLYFLLAWFHAVIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPWSALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDAQTPSWLGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDFTSDGRPAWMRTLHTTASNWLHLIPQTLSPLKRTVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQLQNISQAAAAGGAKELKNIHVCLGALFVPEAYITATRQYVAQANSWSLEELCLEVNVTASQSTTLDACSFGVTGLKLQGATCSNNKLSLSNAISTVLPLTQLRWGKQTSAEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGVAVLCTE', 4644, 'P38650; Q63178;', 'KD00173', 'Rattus norvegicus (Rat)', 'Dync1h1', '#Cytoplasmic dynein 1 heavy chain 1#Cytoplasmic dynein heavy chain 1#Dynein heavy chain; cytosolic#MAP 1C', '-', '-', '29489'),
(174, 'Q6P7W0', 'Sentrin-specific protease 6', 'GO:0090234', 127013, 'Protease that deconjugates SUMO1; SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly- SUMO3 chains; but does not efficiently process SUMO1; SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA; leading to transcriptional activation. Involved in chromosome alignment and spindle assembly; by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI; protecting them from degradation by the ubiquitin ligase RNF4; which targets polysumoylated proteins for proteasomal degradation. Desumoylates also RPA1; thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination.', 'MAAGKSGGSAGALFLKALDRSESKRDGGFKNNWSFDHEEESEGDADKDGANLLSVEDEDSEISKGKKLNRRSEIVATSSGDFILKTYVRRSKTDGFKTLKGNPIGLNMLSNNKKLSESTAGTALCSGTVVHGRRFHHAHSQTPGIRTAAQRKEYPPYVHKAENSPVMLSHGQGGDHIMKKTEESESYVESEIKRKVQQKRHCSTYQLSPLSPASKKCLTHLEVSEQREYCPKCGKEKENQTKCQSCGIVFHNDLQRNCRQAVTLNEPTGPLLRTSIHQNSGGQKSQNTGLTAKKFYGNSVDKIPIDILVTCDDSRHNYIQTNGKVILPGGKIPKLTNPKERKISVSDLNDPIILSSDDDDDDDDRTKRRESTSPKPADSACSSPVPSTGKVEAALNADACRAEQEPRSSPAEPELNTIVIPRKARMKDQLGNSISTPLKRRKVNSHAAFIHPMSLSCQNFESVILNCRSIRVGTLFRLLVEPVIFSLESITIHLDGPESDPVDIILNTSDLTKCEWCNVRKLPVVFLQAIPAVYQKLSMQLQMSKEDKVWNDCKGINRITSLEEQYIILIFQTGLDHQAEVVFESIITDIGIRNNVPNFFAKILFDEANSRLVACTRSYEESIKGNCAQKENKVKTVSFESKIQLRSKQELQFFDDDEEAGESHTIFIGPVEKLIVYPPPPAKGGISVTNEDLHCLSEGEFLNDVIIDFYLKYLVLEKLKKEDADRIHIFSSFFYKRLNQRERRNPETTNLSIQQKRHGRVKTWTRHVDIFEKDFIFVPLNEAAHWFLAVVCFPGLEKPKYEPNPHYHENAVMQKTPSAEDSCVSSASEMGACSQNSAAKPVIKKMLNRKHCLAVTDSSAAQEESEPCYRRNAYSVKCSMKKKNHAINENEEPSNGESTCQDICDRTQSENGLRDECFSSVHHPDALSKIRLNYGDQSADGGKLLEDELIDFSEDQDDPDDSSDDGLLADENYSSEIGQWHLKPTVCKQPCILLMDSLRGPSRSNVVKILREYLEVEWEVKKGSKRSFSKDVMKGSNPKVPQQNNFSDCGVYVLQYVESFFENPVLNFELPMNLMNWFPPPRMKTKREEIRNIILKLQESQSKDKKLLKDSLAETSLGDGAEQYASASGGSE', 1132, 'Q6P7W0; E9QN09; Q6ZQ43; Q8BK94; Q8BUL4;', 'KD00174', 'Mus musculus (Mouse)', 'Senp6', '#Sentrin-specific protease 6#3.4.22.68#SUMO-1-specific protease 1#Sentrin/SUMO-specific protease SENP6', '-', '-', '215351'),
(175, 'Q503N2', 'Kinetochore protein Spc24', 'GO:0000777===GO:0031262', 23398, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSHSISMHDDDLEKLGESLNEIIMSSKAESVLQAARKKKQEFFDHYIKTKKTLTELLNDLVHTEEVVGQKLLDLDQQKSQMMQEIMKMEQEVQRSQSKSQNLDSELEFLQKELERLRDAEQEIQTLQQEVDEDTTEVIPSAIYVAQLYSKVTKIKLEFDTEPHILKGVHYGADVVTPINIDTSTRTPCEVSDELWSLVKTEW', 202, 'Q503N2; Q6DG65;', 'KD00175', 'Danio rerio (Zebrafish) (Brachydanio rerio)', 'spc24', '#Kinetochore protein Spc24', '-', '-', '554147'),
(176, 'Q00664', 'Nuclear distribution protein nudF', 'GO:2000574', 48841, 'Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein- mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs. {ECO:0000255|HAMAP-Rule:MF_03141; ECO:0000269|PubMed:11369237; ECO:0000269|PubMed:15930134; ECO:0000269|PubMed:16467375; ECO:0000269|PubMed:18390647; ECO:0000269|PubMed:20876661}.', 'MSQILTAPQAEALHKAMLAYLSVINAPQTAETLREELHFDESYNEATCKKFEGVLEKKWTGIARLQRRINDLEAEVRSLQAELEASPSAARAKNQDPTNWLPKPSSTHTLTSHRDAVTCVAFHPVFTSLASGSEDCTIKIWDWELGEIERTLKGHIRGVSGLDYGGQKGNTLLASCSSDLTIKLWDPSKDYANIRTLSGHDHSVSSVRFLTSNDNHLISASRDGTLRIWDVSTGFCVKVIKSATESWIRDVSPSFDGKWLVSGGRDQAITVWEVSSAEPKAALLGHENFIECCVFAPPASYEHLATLAGLKKPPPATSSCEFVATGARDKTIKLWEARGRLIKTLHGHDNWVRGLVFHPGGKYLFSVSDDKTIRCWDLSQEGRLVKTISGAHEHFVSCIRWAPSPNTDNPDPAGEKAGKKDAVKPSYRCVIATGCADNSVRVFS', 444, 'Q00664; C8V209; Q5AZT3;', 'KD00176', 'Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRR194 / M139) (Aspergillus nidulans)', 'nudF', '#Nuclear distribution protein nudF {ECO:0000255|HAMAP-Rule:MF_03141}#Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141}#LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141}#Nuclear migration protein nudF', '-', '-', '2870783'),
(177, 'Q8WVM7', 'Cohesin subunit SA-1', 'k', 144427, 'Component of cohesin complex; a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase; the complex is cleaved and dissociates from chromatin; allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis.', 'MITSELPVLQDSTNETTAHSDAGSELEETEVKGKRKRGRPGRPPSTNKKPRKSPGEKSRIEAGIRGAGRGRANGHPQQNGEGEPVTLFEVVKLGKSAMQSVVDDWIESYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRNMQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKMYSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSMTLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLVYSAHRPVAVAAGEFLHKKLFSRHDPQAEEALAKRRGRNSPNGNLIRMLVLFFLESELHEHAAYLVDSLWESSQELLKDWECMTELLLEEPVQGEEAMSDRQESALIELMVCTIRQAAEAHPPVGRGTGKRVLTAKERKTQIDDRNKLTEHFIITLPMLLSKYSADAEKVANLLQIPQYFDLEIYSTGRMEKHLDALLKQIKFVVEKHVESDVLEACSKTYSILCSEEYTIQNRVDIARSQLIDEFVDRFNHSVEDLLQEGEEADDDDIYNVLSTLKRLTSFHNAHDLTKWDLFGNCYRLLKTGIEHGAMPEQIVVQALQCSHYSILWQLVKITDGSPSKEDLLVLRKTVKSFLAVCQQCLSNVNTPVKEQAFMLLCDLLMIFSHQLMTGGREGLQPLVFNPDTGLQSELLSFVMDHVFIDQDEENQSMEGDEEDEANKIEALHKRRNLLAAFSKLIIYDIVDMHAAADIFKHYMKYYNDYGDIIKETLSKTRQIDKIQCAKTLILSLQQLFNELVQEQGPNLDRTSAHVSGIKELARRFALTFGLDQIKTREAVATLHKDGIEFAFKYQNQKGQEYPPPNLAFLEVLSEFSSKLLRQDKKTVHSYLEKFLTEQMMERREDVWLPLISYRNSLVTGGEDDRMSVNSGSSSSKTSSVRNKKGRPPLHKKRVEDESLDNTWLNRTDTMIQTPGPLPAPQLTSTVLRENSRPMGDQIQEPESEHGSEPDFLHNPQMQISWLGQPKLEDLNRKDRTGMNYMKVRTGVRHAVRGLMEEDAEPIFEDVMMSSRSQLEDMNEEFEDTMVIDLPPSRNRRERAELRPDFFDSAAIIEDDSGFGMPMF', 1258, 'Q8WVM7; O00539; Q6P275;', 'KD00177', 'Homo sapiens (Human)', 'STAG1', '#Cohesin subunit SA-1#SCC3 homolog 1#Stromal antigen 1', '-', 'ENSG00000118007', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(178, 'Q9H8V3', 'Protein ECT2', 'GO:0051988', 103505, 'Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases; like RHOA; RHOC; RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)- induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells; thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. {ECO:0000269|PubMed:10579713; ECO:0000269|PubMed:14645260; ECO:0000269|PubMed:15254234; ECO:0000269|PubMed:15545273; ECO:0000269|PubMed:15642749; ECO:0000269|PubMed:16103226; ECO:0000269|PubMed:16170345; ECO:0000269|PubMed:16236794; ECO:0000269|PubMed:16495035; ECO:0000269|PubMed:19129481; ECO:0000269|PubMed:19468300; ECO:0000269|PubMed:19617897; ECO:0000269|PubMed:21189248; ECO:0000269|PubMed:21373644}.', 'MAENSVLTSTTGRTSLADSSIFDSKVTEISKENLLIGSTSYVEEEMPQIETRVILVQEAGKQEELIKALKTIKIMEVPVIKIKESCPGKSDEKLIKSVINMDIKVGFVKMESVEEFEGLDSPEFENVFVVTDFQDSVFNDLYKADCRVIGPPVVLNCSQKGEPLPFSCRPLYCTSMMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQDFYAAVDDFRNEFKVPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDARAGETMYLYEKANTPELKKSVSMLSLNTPNSNRKRRRLKETLAQLSRETDVSPFPPRKRPSAEHSLSIGSLLDISNTPESSINYGDTPKSCTKSSKSSTPVPSKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRGGPILAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESKSIGDIFLKYSKDLVKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLGEHPCDRGEQVTLFLFNDCLEIARKRHKVIGTFRSPHGQTRPPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSDELPKENWLKMLCRHVANTICKADAENLIYTADPESFEVNTKDMDSTLSRASRAIKKTSKKVTRAFSFSKTPKRALRRALMTSHGSVEGRSPSSNDKHVMSRLSSTSSLAGIPSPSLVSLPSFFERRSHTLSRSTTHLI', 914, 'Q9H8V3; Q0MT80; Q2M269; Q6U836; Q9NSV8; Q9NVW9;', 'KD00178', 'Homo sapiens (Human)', 'ECT2', '#Protein ECT2#Epithelial cell-transforming sequence 2 oncogene', '-', 'ENSG00000114346', '-'),
(179, 'Q3UHU5', 'Microtubule cross-linking factor 1', 'GO:2000576', 213862, 'Microtubule-associated factor involved in the late phase of epithelial polarization and microtubule dynamics regulation. Plays a role in the development and maintenance of non-centrosomal microtubule bundles at the lateral membrane in polarized epithelial cells. {ECO:0000269|PubMed:23902687}.', 'METLNGPAGGGAPDTKPQPAGQHHRHHHLHPLAERRRLHRAPSPARPFLKDLHTRPATATPSAGRAPTPAAPRSPSLAGKAPPSPGPPAAPGRLSRRSGVVPGAKDKPPPGAGARSAGGAKAVPGTRRAARAGPAEPLSRVGRPTGAEPPPAVAKGRKTKRGPGTPPARAVVPPARASRVPAVTLSVTSVAGCRINHTDSSSDLSDCASEPLSDEQRLLPAASSDAESGTGSSDREPIRGAPTPSSGSRGPPPGSPEPPILLAAPPVASACLGGRSSPGGASTGSPGPGSQEDVGGRAPPERTILGTSKEPSLGEQPRLLVVAEEEELLREMEELRSENDYLKDELDELRAEMEEMRDSYLEEDGYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELETVEEKRAKAEDDNETLRQQMIEVEVSRQALQNEVERLRESSLKRRGSREMYKEKKLVNQDDSADLKCQLQFVKEEASLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEASILGRKIVELEVENRGLKAEMEDIRVQHEREGTGRDHVPSTPTSPFGDSMESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPHQESGWLGDGVSKGPAASVPLQEELKSARLQIDELSGKVLKLQCENRLLLSNAQRGDLAAHLGLRAPSPRDSDAESDAGKKESDGEEGRLPQPKREGPVGGESDSEDMFEKTSGFGSGKPSEASEPCPAELLRVREDTECLVTIKLEAQRLERTVERLISDTDGFIHDSGLRGNGLASPGVQGGGGEGNSPSEPHLLETINVRMKAFRKELQAFLEQMSRIVDGLSPLSHLTESSSFLSTVTSVSRDSPIGTLGKELGPDLQSKLREQLEWQLNQDRGDEREGLRLRATRELHRRADGDSGSHHGLGGQSCFNLEMEEDHLYALRWKELEMHSLALQNTLHKRTWSDEKNLLQQELRSLKQNIFLFYVKLRWLLKHWRQGKQMEEGGEDLEESEHPENVPGLAELGVQGVHQTDGIDQEDADQGCSLPMGEHAPHSLVQISEHGSRLQSSDGGPLNKQVVENQQLFRALKALLEDFRSELREDEHARLRLQQQYASDKAAWDVEWAVLKCRLEQLEEKTEKSLGELDSSAEGKGALKKEREVHQKLLADSHSLVMDLRWQIHHREKNWNREKVELLERLDSERQEWGRQKEELLWRVEQLQKEKSPRRSGSFLCSRREDDTRPYPHQGSLHSSRPVSMWPCEDADSIPFEDRPLSKLKESDRCSASENLYLDALSLDDDPGDPPPLRNCLAEEEESRKGNLQRAVSVSCMSEFQRLMDVSPFLPEKGLPSAGSKEDVTPPLSPDDLKYIEEFHSNDWDYASPRAEADRPPDPWADRTEMGRVGHEATTEPCPDPSWYLTTSVTMTTDTMTSPEHCQKQPLRTHVLTEQSGVHVLHSPPAIRRVDSIASGGEGRSRADPEGPFPMSRARGNLADAKGGHPEPVLNRWPCTPPRHPRDCVEGSLRPLDRPICPSLGFASPLNSLDMSKNMSDDMKEVAFSVRNAICAGPAEPHVRDMACQTNGSRTAGTQTIQTISVGLQTEALRASGVTSSPHKCLTPKAGGGTTPVSSPSRSLRSRQVAPAIEKVQAKFERTCCSPKYGSPKLQRKPLSKADQPNSRTSPGIPQKGFSESAWARSTTTRESPVHTTINDGLSSLFNIIDHSPIGVRAGSRSRSAEPRQELGPGQETGTSSRGRSPSPLGVGSETFREEGGESTPVRQDLSAPPGYTLTENVARILNKKLLEHALKEERKQASHGSSGLTSDSHTGEPVPAEPGSMEELPCSALAPSLEPCFSRPERPANRRLPSRWAPPSPTASQSQSPGHPMSMEEHGEEDPPEEKPHL', 1945, 'Q3UHU5; Q6PAM2; Q80TR7;', 'KD00179', 'Mus musculus (Mouse)', 'Mtcl1', '#Microtubule cross-linking factor 1#Coiled-coil domain-containing protein 165#PAR-1-interacting protein#SOGA family member 2', '-', '-', '68617'),
(180, 'Q6BHU0', 'DASH complex subunit SPC19', 'GO:0008608===GO:0042729', 19783, '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}.', 'MSHTYNSLSNCISSLSASVALLNDSLKTIDNATKDIPRLKKVLSTNKVFGLVPESDLESAKRNIQNEIQPQINALVIKIEKELSKLKRKKTNLASKVDLQQVRLENAAKSNRDSLSGIKGITANRISKGDIDESKLARLKLLQNKKERLKYSLSRLNLQDKRARLSTIPSLPPHRDS', 177, 'Q6BHU0;', 'KD00180', 'Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBR0083 / IGC 2968) (Yeast) (Torulaspora hansenii)', 'SPC19', '#DASH complex subunit SPC19#Outer kinetochore protein SPC19', '-', '-', '2905155'),
(181, 'Q8IXJ6', 'NAD-dependent protein deacetylase sirtuin-2', 'GO:0051987', 43182, 'Isoform 2: Deacetylates EP300; alpha-tubulin and histone H3 and H4.', 'MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQSGAGVPNPSTSASPKKSPPPAKDEARTTEREKPQ', 389, 'Q8IXJ6; A8K3V1; B2RB45; O95889; Q924Y7; Q9P0G8; Q9UNT0; Q9Y6E9;U5TP13;', 'KD00181', 'Homo sapiens (Human)', 'SIRT2', '#NAD-dependent protein deacetylase sirtuin-2#3.5.1.-#Regulatory protein SIR2 homolog 2#SIR2-like protein 2', '-', 'ENSG00000068903', '-'),
(182, 'Q68CP9', 'AT-rich interactive domain-containing protein 2', 'k', 197391, 'Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes. {ECO:0000269|PubMed:16782067}.', 'MANSTGKAPPDERRKGLAFLDELRQFHHSRGSPFKKIPAVGGKELDLHGLYTRVTTLGGFAKVSEKNQWGEIVEEFNFPRSCSNAAFALKQYYLRYLEKYEKVHHFGEDDDEVPPGNPKPQLPIGAIPSSYNYQQHSVSDYLRQSYGLSMDFNSPNDYNKLVLSLLSGLPNEVDFAINVCTLLSNESKHVMQLEKDPKIITLLLANAGVFDDTLGSFSTVFGEEWKEKTDRDFVKFWKDIVDDNEVRDLISDRNKSHEGTSGEWIWESLFHPPRKLGINDIEGQRVLQIAVILRNLSFEEGNVKLLAANRTCLRFLLLSAHSHFISLRQLGLDTLGNIAAELLLDPVDFKTTHLMFHTVTKCLMSRDRFLKMRGMEILGNLCKAEDNGVLICEYVDQDSYREIICHLTLPDVLLVISTLEVLYMLTEMGDVACTKIAKVEKSIDMLVCLVSMDIQMFGPDALAAVKLIEHPSSSHQMLSEIRPQAIEQVQTQTHVASAPASRAVVAQHVAPPPGIVEIDSEKFACQWLNAHFEVNPDCSVSRAEMYSEYLSTCSKLARGGILTSTGFYKCLRTVFPNHTVKRVEDSSSNGQAHIHVVGVKRRAIPLPIQMYYQQQPVSTSVVRVDSVPDVSPAPSPAGIPHGSQTIGNHFQRTPVANQSSNLTATQMSFPVQGVHTVAQTVSRIPQNPSPHTHQQQNAPVTVIQSKAPIPCEVVKATVIQNSIPQTGVPVSIAVGGGPPQSSVVQNHSTGPQPVTVVNSQTLLHHPSVIPQQSPLHTVVPGQIPSGTPVTVIQQAVPQSHMFGRVQNIPACTSTVSQGQQLITTSPQPVQTSSQQTSAGSQSQDTVIIAPPQYVTTSASNIVSATSVQNFQVATGQMVTIAGVPSPQASRVGFQNIAPKPLPSQQVSSTVVQQPIQQPQQPTQQSVVIVSQPAQQGQTYAPAIHQIVLANPAALPAGQTVQLTGQPNITPSSSPSPVPATNNQVPTAMSSSSTPQSQGPPPTVSQMLSVKRQQQQQHSPAPPPQQVQVQVQQPQQVQMQVQPQQSNAGVGQPASGESSLIKQLLLPKRGPSTPGGKLILPAPQIPPPNNARAPSPQVVYQVASNQAAGFGVQGQTPAQQLLVGQQNVQLVPSAMPPSGGVQTVPISNLQILPGPLISNSPATIFQGTSGNQVTITVVPNTSFAPATVSQGNATQLIAPAGITMSGTQTGVGLPVQTLPATQASPAGQSSCTTATPPFKGDKIICQKEEEAKEATGLHVHERKIEVMENPSCRRGATNTSNGDTKENEMHVGSLLNGRKYSDSSLPPSNSGKIQSETNQCSLISNGPSLELGENGASGKQNSEQIDMQDIKSDLRKPLVNGICDFDKGDGSHLSKNIPNHKTSNHVGNGEISPMEPQGTLDITQQDTAKGDQLERISNGPVLTLGGSSVSSIQEASNAATQQFSGTDLLNGPLASSLNSDVPQQRPSVVVSPHSTTSVIQGHQIIAVPDSGSKVSHSPALSSDVRSTNGTAECKTVKRPAEDTDRETVAGIPNKVGVRIVTISDPNNAGCSATMVAVPAGADPSTVAKVAIESAVQQKQQHPPTYVQNVVPQNTPMPPSPAVQVQGQPNSSQPSPFSGSSQPGDPMRKPGQNFMCLWQSCKKWFQTPSQVFYHAATEHGGKDVYPGQCLWEGCEPFQRQRFSFITHLQDKHCSKDALLAGLKQDEPGQAGSQKSSTKQPTVGGTSSTPRAQKAIVNHPSAALMALRRGSRNLVFRDFTDEKEGPITKHIRLTAALILKNIGKYSECGRRLLKRHENNLSVLAISNMEASSTLAKCLYELNFTVQSKEQEKDSEMLQ', 1835, 'Q68CP9; Q15KG9; Q5EB51; Q645I3; Q6ZRY5; Q7Z3I5; Q86T28; Q96SJ6;Q9HCL5;', 'KD00182', 'Homo sapiens (Human)', 'ARID2', '#AT-rich interactive domain-containing protein 2#ARID domain-containing protein 2#BRG1-associated factor 200#BAF200#Zinc finger protein with activation potential#Zipzap/p200', '-', 'ENSG00000189079', '-'),
(183, 'P62152', 'Calmodulin', 'GO:0051383', 16811, 'Calmodulin mediates the control of a large number of enzymes; ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.', 'MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTSK', 149, 'P62152; P07181; Q9V3T4;', 'KD00183', 'Drosophila melanogaster (Fruit fly)', 'Cam', '#Calmodulin#CaM', '-', '-', '36329'),
(184, 'B2W0D9', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 34013, 'Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). {ECO:0000250}.', 'MNVQYQAFTPPHLLNNTRRSPTRNISSLSSTMSGRKRKAEDDGSAGDDDRMSASPSASPAVLPRPAPRGMKRMRTNISGRPLPLPRLLETLSPDDMRNLLQSICQRHPDISNEIVTTAPRPSIQSTLEVLAKYEASFQAAFPFGGRASSDYAYNRVRQQLDELLDSLKDFTPHFLPPNEQQPATSLTFLDGATNIIHRLPNWDTFQHNRHKQEAYEEMAKAWAMVIQEAAKKAGGIQLQYGGWDEKIAKHNEISGGKMQEAVNELRGGLGWMGAETSNSAAGAPADAMSIRQQLLSGNYGAGSPASIGAW', 310, 'B2W0D9;', 'KD00184', 'Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spofungus) (Drechslera tritici-repentis)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '6342160'),
(185, 'Q78PB6', 'Nuclear distribution protein nudE-like 1', 'GO:0000776===GO:0000777', 38366, 'Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity; the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. 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). Plays a role; together with DISC1; in the regulation of neurite outgrowth. {ECO:0000250; ECO:0000269|PubMed:17035248}.', 'MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYVPGSVNCGVMNSNGPECPRSGRATFFHKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV', 345, 'Q78PB6; Q6IRI4;', 'KD00185', 'Rattus norvegicus (Rat)', 'Ndel1', '#Nuclear distribution protein nudE-like 1#Protein Nudel', '-', '-', '170845'),
(186, 'P42208', 'Septin-2', 'GO:0000777', 41526, '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 (By similarity). 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. {ECO:0000250; ECO:0000269|PubMed:20558667; ECO:0000269|PubMed:22179047; ECO:0000269|PubMed:9203580}.', 'MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERIIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHSIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDSDSGALGQHV', 361, 'P42208; B2RRZ2; Q3U9Y5;', 'KD00186', 'Mus musculus (Mouse)', 'Sept2', '#Septin-2#Neural precursor cell expressed developmentally down-regulated protein 5#NEDD-5', '-', '-', '18000'),
(187, 'Q75ED7', 'DASH complex subunit DUO1', 'GO:0008608===GO:0051987===GO:0042729', 21501, '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}.', 'MNANGEANGGVDSAALDELIPQIFDQMRTNQLDGSGAAAWGTAAVSTATLLKEMEQLDQIIPVLQQLNESLRRSTGENLSRIRRTCEAVNRVLDTWIKIQSQAGYVGELMDDSEYLSYMEKTRGDEGQQQAYMESLRKQVEELRRKVDERRAVEAAAAAPRAPERTRGASGIPRGGSRITKRGGTTVRGRRMFR', 194, 'Q75ED7;', 'KD00187', 'Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRY-1056) (Yeast) (Eremothecium gossypii)', 'DUO1', '#DASH complex subunit DUO1#Outer kinetochore protein DUO1', '-', '-', '4618740'),
(188, 'O74518', 'Poly(A) RNA polymerase cid12', 'GO:0031134', 38558, 'Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-induced transcriptional silencing (RITS) complex. RITS acts as a priming complex for dsRNA synthesis at the site of non-coding centromeric RNA. {ECO:0000269|PubMed:15607976}.', 'MGKVLLELHSVPWNEEGLSDNARLYSFLEFVSPKIEELKYRKLLLEKLQTHIREVVLDAELQVYGSMYIGTTLSISDVDVSLKSPRVGELEKRRVTMVLRKYLDADADFHSSARVPRINLVDVSGIGVDLTFGNDKACRTAELQKAYNEEHPIFGRLLMLLKHWLFERDLENVHHGGIASCALSYMLIGWLEMRFHKKGIDSEVQPIRALLQKFFYFWGVEWTYELFVLRPLTGQIVPKLQKGWLNEVQPNLLSIEDPIDRNNDIGKQSFQISMIKAAFVASANELLSDKTWFSTFAITEDEMFLCKQFENVINTKRSLVEGYDSDTESDELQAGG', 336, 'O74518;', 'KD00188', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'cid12', '#Poly(A) RNA polymerase cid12#PAP#2.7.7.19#Caffeine-induced death protein 12#Polynucleotide adenylyltransferase cid12', '-', '-', '2539423'),
(189, 'Q8R060', 'Protein zwilch homolog', 'GO:0000776===GO:0000777', 66839, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores (By similarity). {ECO:0000250}.', 'MWSRMNRAAEEFYARLRQEFNEEKKGASKDPFIYEADVQVQLISKGQPSLLKTILNENDSVFLVEKVVLEKEETSQVEELQSEETAISDLSAGENIRPLALPVGRARQLIGLYTMAHNPNMTHLKIKQPVTALPPLWVRCDGSDPEGTCWLGAELITTNDIIAGVILYVLTCKADKNYSEDLENLKTSHKKRHHVSAVTARGFAQYELFKSDDLDDTVAPSQTTVTLDLSWSPVDEMLQTPPLSSTAALNIRVQSGESRGCLSHLHRELKFLLVLADGIRTGVTEWLEPLETKSALEFVQEFLNDLNKLDEFDDSTKKDKQKEAVNHDAAAVVRSMLLTVRGDLDFAEQLWCRMSSSVVSYQDLVKCFTLILQSLQRGDIQPWLHSGSNSLLSKLIHQSYHGAMDSVPLSGTTPLQMLLEIGLDKLKKDYISFFVSQELASLNHLEYFISPSVSTQEQVCRVQKLHHILEILVICMLFIKPQHELLFSLTQSCIKYYKQNPLDEQHIFQLPVRPAAVKNLYQSEKPQKWRVELSNSQKRVKTVWQLSDSSPVDHSSFHRPEFPELTLNGSLEERTAFVNMLTCSQVHFK', 589, 'Q8R060; Q9D2E4; Q9D761;', 'KD00189', 'Mus musculus (Mouse)', 'Zwilch', '#Protein zwilch homolog', '-', '-', '68014'),
(190, 'Q5XI06', 'Histone acetyltransferase KAT8', 'GO:0000776', 52632, 'Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at ''Lys-120''. {ECO:0000250|UniProtKB:Q9H7Z6}.', 'MAAQGATAAVAATTSGIVGEGEPGPGENTSVEGPARSPGRVSPPTPARGEPEVTVEIGETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKFEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPKHKQVKLSKK', 458, 'Q5XI06;', 'KD00190', 'Rattus norvegicus (Rat)', 'Kat8', '#Histone acetyltransferase KAT8#2.3.1.48 {ECO:0000250|UniProtKB:Q9H7Z6}#Lysine acetyltransferase 8#MOZ; YBF2/SAS3; SAS2 and TIP60 protein 1#MYST-1', '-', '-', '310194'),
(191, 'Q29RQ3', 'Cytoplasmic dynein 1 intermediate chain 1', 'GO:0000777===GO:0005868', 68556, '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) DCTN1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores (By similarity). {ECO:0000250}.', 'MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVPDDSDLDRKRRETEALLQSIGISPEPPLVPTPMSPSSKSVSTPSEAGSQDSGDLGPLTRRRLHKLGVSKITQVDFLPREVVSYSKETQTPLATHQSEEDEDDEEMVEPKGDQDSEQENEDKKQEVKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYNNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNNDTEVPTASVAIEGASALNRVRWAQGGKEVAVGDSEGRIWIYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGAVELSA', 608, 'Q29RQ3;', 'KD00191', 'Bos taurus (Bovine)', 'DYNC1I1', '#Cytoplasmic dynein 1 intermediate chain 1#Cytoplasmic dynein intermediate chain 1#Dynein intermediate chain 1; cytosolic#DH IC-1', '-', '-', '613724'),
(192, 'F1NPG5', 'Centromere protein T', 'GO:0000777===GO:0051382', 70670, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere; as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins; with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. {ECO:0000250; ECO:0000269|PubMed:19070575; ECO:0000269|PubMed:22304917}.', 'MDGRVGLRASRRAAPTPRVAVRSSPRHRARVREQEPVVSAMSGSGLGKENKAGSSTPLRHRPNAFSELDNATPRVMLRKIIQNQPQVSPLALQTVQLEETEDARPEPPSQRTSSTVELQLPDLVPEDASVTTFRMTRKRKKLSISEFERAADKRLPQNQAHSTLDSTLVRSLRMSVGSVMAPDTVEKRGLLRRPQNHKAIDIAAFEGGVEQNMLQIKAQDYLVDLQTSSMTGTTTIRTDAEVVLNNTELFVEPQLGEQNLLAVEPQLSDSKTSAQRSNTSYPAHEKARLEGLVSRVSTDERRTLRFSEKDLITDHEHVDGITQKTPAKQGEEEQDHSQQNDPMEQFSESEEMAGTTEHHADAEYSEHSEKKLSRKAVSQLTAAQDAGVEMEMTPSEGGVAEGTEHQDSPKAELQMAGSPGGHSPASYSLEKPGAKPLKEAVEQTGEIERGTITGVLDAAEEEATDDESDKEDHESEEISMKTPMFVHAAAYRPQPVLSPPHPVKSASPELPPQPVRAKPVPKSSGAAQRKTREPEIASSLIKQIFSHYVKTPVTRDAYKIVEKCSERYFKQISSDLEAYSQHAGRKTVEMADVELLMRRQGLVTDKMPLHVLVERHLPLEYRKLLIPIAVSGNKVIPCK', 639, 'F1NPG5;', 'KD00192', 'Gallus gallus (Chicken)', 'CENPT', '#Centromere protein T#CENP-T', '-', '-', '415654'),
(193, 'Q2TBR7', 'Centromere protein S', 'GO:0000777', 15951, 'DNA-binding component of the FA core complex involved in DNA damage repair and genome maintenance. Required for optimal chromatin association of the FA core complex. Required for efficient damage-induced monoubiquitination and focus formation of FANCD2. Stabilizes FAAD24; FANCM and APITD1/CENPS in the FA core complex. Plays a role in DNA interstrand cross-linking (ICL) repair and in recovery of replication forks stalled by topoisomerase I-DNA cleavage intermediates induced by camptothecin. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA; and plays an important role in kinetochore assembly. Component of the APITD1/CENPS complex that is essential for the stable assembly of the outer kinetochore. Plays an important role in mitotic progression and chromosome segregation. Component of the CENPA-CAD (nucleosome distal) complex; a complex recruited to centromeres which is involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation (By similarity). {ECO:0000250}.', 'MEEEEWSEEQQRFSYLQRLKAAVHYTVGCLCEEVASDKDMQFSKQTIAAISEVTFGQCENFAKDLEMFARHAKRSTINTEDVKLLARRSHSLLKYITEKNEDIAQLNLEKKAKKKKKLEDENRNSVESAEAGVEESEN', 138, 'Q2TBR7;', 'KD00193', 'Bos taurus (Bovine)', 'APITD1', '#Centromere protein S#CENP-S#Apoptosis-inducing TAF9-like domain-containing protein 1 homolog#FANCM-interacting histone fold protein 1', '-', '-', '613732'),
(194, 'O74511', 'Extragenic suppressor of kinetochore protein 1', 'k', 94967, 'Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. {ECO:0000269|PubMed:12773390}.', 'MFWRLGQGFGFQSSSAIEAILDKPEDEINLKELLEENGVLDECKSHNPKLLEYLCKPEVLSQLIDYILEVDETEIPSADGGYEEPEHTRLSYIASEILSSDVWSICEACVENKTLMVKLWSFLDSEGPLNPLQASYFAKVNEHFLDKKTEETVAFIQSIDNFVEKILRHAETSAIMDLLLKFISMDRCNTAIGIADWLYSQGLIQSLLRLLSPYVDPDVQFTVADVIKAIIAISANSNEPGVIGPNSLSRELVSRQTITTLTDYMTDSKAPHSATSLINGVSIVIELIRKNNSDYDVTPVLQMPLDTHPPTTRDPIYLGTMLRLFAEKIPVFQKILLKPSTESDLMPTSFGKIKPLGFERFRICELYAELLHCSNMSLLSDPNGEAMVMQRDHLRDYLFRHNSCARDLVMSDEDDDDSTFSDKNSKDFKETEDMNGAEDMHGRAPQITKDNLNLTTTDSPMSEAEPVSEEEYKDVMETAKALHHGDDDAASDTSYEPLPESVIEDAKKLPVIGDFLKIEFIQNNVIPTILDHFFDYPWNNFLHNVVYDVVQQVLNAPMDKDQNYALAVDMFKQGKITEKIVYGQELNDKKVAKPSGFRAGYMGHLTIIADEVVKFVEHYSSTFDQELLNLINDEKWQNFVNKTLVETRNRDNQLLGGLEPSMVGYLEDMDEGEMLDANNLPEMQFALEQELESNSSDDDVVEVHRELSHNSSSNDEDDGNDEDPLSREMSRRLSFESANDSDQDNRDHFAQYMSQQISDNNANQFSSSDEDDDDDDEVVEWVSRGNENKYPRSNFFINGSDREDFSDSEEEDGNDSSDDDRGFAEEEYSDGLVLNHGK', 838, 'O74511; O74554;', 'KD00194', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'ekc1', '#Extragenic suppressor of kinetochore protein 1', '-', '-', '2539511'),
(195, 'Q9VYX4', 'CG1558-RA proteinKinetochore Mis12-Ndc80 network component 1RE03006p', 'k', 21391, '', 'MEPAESPEKLMKFVRRSDVLEYVGNTSAVDLSSGDLSDIDLKDVPAQLEATLKPRRYEASTLFNIDLDDIWDPSCQEDEVQQYKERAQKEQQKFFDFVMHAALDTDNRKVSFKPNKEQQRYLDQGPNLQNFVRSSLAFTNAAIRFQAEHEDMMELQCNMDDHYLFMRNTMINNAIHQNMANQR', 183, 'Q9VYX4;', 'KD00195', 'Drosophila melanogaster (Fruit fly)', 'Kmn1', '#CG1558-RA protein {ECO:0000313|EMBL:ACC38324.1}#Kinetochore Mis12-Ndc80 network component 1 {ECO:0000313|EMBL:AAF48059.1}#RE03006p {ECO:0000313|EMBL:AAL48547.1}', '-', '-', '32102'),
(196, 'O19175', 'Casein kinase I isoform alpha', 'GO:0000777', 14633, '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}.', 'GEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKY', 125, 'O19175;', 'KD00196', 'Sus scrofa (Pig)', 'CSNK1A1', '#Casein kinase I isoform alpha#CKI-alpha#2.7.11.1#CK1', '-', '-', '-'),
(197, 'Q8K305', 'Kinetochore-associated protein NSL1 homolog', 'GO:0000444', 31739, 'Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. {ECO:0000250}.', 'MAAVSETVLVSAPQDHDAQAASDPQATAADSPLEDFRVRCTLKRAVMEVMEMCGRFVQELGAVLPEDVRELALRDAQWTFESAVQENVSFNGQAWEEAKEHGLMDSDIKVLEDEFDELIVDVATKRRQYPRRILESVIKTLKAQHASLKQYHPVVHPLDLKCDPDPASRVEDLKCRGEAIAKEMSEAMKALPVLIEQGEGFSQVLKMRPVIQLQRINQEVFSSLYRKADFKPDTCVTHVETTPAETGARKASNIVLKRKKAPDCAQRKRYPLRLQRINLDM', 281, 'Q8K305;', 'KD00197', 'Mus musculus (Mouse)', 'Nsl1', '#Kinetochore-associated protein NSL1 homolog', '-', '-', '-'),
(198, 'Q9VM45', 'Nuf2', 'k', 45699, '', 'MALSVEIERVMDQGNCLMPDINICQSDLANPTEPIVTKIMVHYLRSFGFRLEPPYKIGTELGHSSREARVFLIRVCRQVERIVQISFPNKTYTYMDIIKPAVKKTLATLSYLFNHLAYYKVFKKKVLGPVEEAIKLKDSLTAEVKAKSQQLEQCSQKTKDCEVAINKLKKDLQDTQAKLLPLKKSCSEHENTLELIEQQQGELDKRIGHWEQLVVEDSQVTELREKIKSASSHVESCKTELASKKQVTNEHRRMIENSQHIATALEKATAVLSLCKVDDYKESFKQLEAVEKQLPTCKVNYQKLLQDAEAKKQELALCAHRYEERNQENDAENHKVQNELKKLQVDVEDRKKRLEDLNNHLIELDQQNLEQDQLYAILNEQIHEVLGQNWQMNST', 395, 'Q9VM45;', 'KD00198', 'Drosophila melanogaster (Fruit fly)', 'Nuf2', '#Nuf2 {ECO:0000313|EMBL:AAF52482.2}', '-', '-', '33992'),
(199, 'Q12748', 'Central kinetochore subunit CTF3', 'GO:0000778===k', 84252, '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.', 'MSLILDDIILSLTNANERTPPQALKTTLSLLYEKSKQYGLSSPQLQALVRLLCETSIIDTVTKVYIVENCFLPDGYLTKELLLEIINHLGTPTVFSRYRIQTPPVLQSALCKWLVHVYFLFPVHSEREHNISSSIWLHLWQFSFLQKWITPLVIWQATTPVDVKPWKLSIIKRCAMHPGYRDAPGSATLILQRFQCLVGASSQITESIITINCNRKTLKSHRNLKLDAHFLSILKRILSRAHPANFPADTVQNTIDMYLSEIHQLGADSIYPLRLQSLPEYVPSDSTVSLWDVTSLEQLAQNWPQLHIPNDVDYMMKPSLNSNVLLPRKVMSRDSLKHLYSSIILIKNSRDESSSPYEWCIWQLKRCFAHQIETPQEVIPIIISVSSMDNKLSSRIIQTFCNLKYLKLDELTLKKVCGGILPLWKPELISGTREFFVKFMASIFMWSTRDGHDNNCTFSETCFYVLQMITNWVLDDKLIALGLTLLHDMQSLLTLDKIFNNATSNRFSTMAFISSLDILTQLSKQTKSDYAIQYLIVGPDIMNKVFSSDDPLLLSAACRYLVATKNKLMQYPSTNKFVRMQNQYIMDLTNYLYRNKVLSSKSLFGVSPDFFKQILENLYIPTADFKNAKFFTITGIPALSYICIIILRRLETAENTKIKFTSGIINEETFNNFFRVHHDEIGQHGWIKGVNNIHDLRVKILMHLSNTANPYRDIAAFLFTYLKSLSKYSVQNS', 733, 'Q12748; D6VZ16; Q7LHY6;', 'KD00199', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'CTF3', '#Central kinetochore subunit CTF3#Chromosome loss protein 3#Chromosome transmission fidelity protein 3', '-', '-', '851097'),
(200, 'Q6CEY7', 'Probable kinetochore protein NDC80', 'GO:0034501===GO:0000778===GO:0051315===GO:0051455===GO:0031617===GO:0031262', 72294, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MNASAHKKRLSMMPGTSSASRPSMAGLPQRNNPPPQREPATPAVSELMRSSRRSMAFGRNPRQSSFGLVPQTPMAPMHTRDPRPVRDRHYQQQISQQIYEYLVTNHFEQETRHPLNQRTLSNPTQKDFKTMFEWIFRRIDPGYPFHKSIENEVHAVLRAAKYPWLDSITKSQIVAVGGQSWAYFSGMLHWMVELNTTIEKYHNHDYSGDDGPSLVDEIFNRHARESYFAYLQGDDRFARPDAELCLAEENAEFQEILAEQRAQNPLPEGEDDELDEELSRLEAKWGKIEEAKLLGKNLADDIVKLGAFVDARKEHNARYASQMSQATAEEDNVTSEVESLSRQKLKLQQTIQDQGLSPAELDKLHLDMERQQKALNSLDEIIDEGRQVVSNKESTALAVFDALDRVIKEYTSSVLSYNAWVASDNDLPEIPESVYLIDLREPLSEENLGRHPSVILGGVDPRNQIRPEIVRICNMVTSKVKALQEEALRLQEEIETNQEKLVSQKRHIGELEAKSRRLRETRNALEDSASMNENENSQNTERLENQFVQAQSETALAQSQLKGLQVRLQDAEHERNKLSVEVQQARERLSQDILKQAEVMVAFKAMVQTKLQDFEMFVRANVEEEIRGDHN', 631, 'Q6CEY7;', 'KD00200', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'NDC80', '#Probable kinetochore protein NDC80', '-', '-', '2907301'),
(201, 'Q9WVA3', 'Mitotic checkpoint protein BUB3', 'GO:0000776===GO:0000777===GO:0008608===SCL===k', 36955, 'Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1 (By similarity). Regulates chromosome segregation during oocyte meiosis. {ECO:0000250; ECO:0000269|PubMed:19888327}.', 'MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMVTGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAETKPKST', 326, 'Q9WVA3; P97397; Q6ZWM5;', 'KD00201', 'Mus musculus (Mouse)', 'Bub3', '#Mitotic checkpoint protein BUB3#WD repeat type I transmembrane protein A72.5', '-', '-', '12237'),
(202, 'Q5U4Y8', 'Nucleoporin seh1', 'GO:0000777===GO:0051315', 39679, 'Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment; mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (By similarity). {ECO:0000250}.', 'MFVARSIAADHKDLIHDVSFDFHGRRMATCSSDQSVKVWDKSENGDWHCTASWKTHSGSVWRVTWAHPEFGQVLASCSFDRTAAVWEEIVGESNDKLRGQSHWVKRTTLVDSRTSVTDVKFAPKHMGLMLATCSADGVVRIYEAPDVMNLSQWSLQHEISCKLSCSCISWNPSSSRAHSPMIAVGSDDSSPNIMGKVQIYEYNENTRKYAKAETLMSVSDPVHDIAFAPNLGRSFHILAVATKDVRIFTMKPLRKELSSSGGVTKFEIHTVAQFDNHNSQVWRVSWNITGTVLASSGDDGTVRLWKANYMDNWKCIGVLKGDGNPVGNSCQGIFGSSVGSAIQSLQNSVNGTSSSGRKHS', 360, 'Q5U4Y8;', 'KD00202', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'seh1l', '#Nucleoporin seh1#Nup107-160 subcomplex subunit seh1', '-', '-', '496570'),
(203, 'Q9W1U1', 'FI21273p1Kinesin-like protein at 59D', 'c;k', 81917, '', 'MDRIKIGEQLLFQRSDGRVHQVVCTAKNLERDSITGEWTEGTVVKGKEVPLSTLIGINHHIFAENQPPISKPPSSLLPKPRGSSPTGGPKTHTGNPYAERMRVQDGRSKIATRKTDPAAVGAGNHELGRAHTPRVPAGRPDRDASPTQGRKSQGGNNSNQRFSSVVREVNRMKEQREKRRARQAEQLQEKDALRRNNPGNPNWEVSVMLRQYRSTLIFSPLRCLDPNGGTVQQITVCVRKRPMSRKEENSKNLDIITVPSADSLIVHELRLKVDLTKFLEHHKFRFDYTFDEECSNALVYDHTARPLIRTMFEGGNATCFAYGQTGSGKTHTMGGEFFGKVQDCGTGIYAMAARDVFEEVSRPEYRQMGAKITCSFFEIYGTKVFDLLLPNKPMLRVLEDARQQVVVVGLTEMPVTKVEDVLRLIEHGSKERTSGQTSANAKSSRSHAVFQIALHFPDSWGPHGKCSFVDLAGNERGADTQSADRQTRIEGAEINKSLLALKECIRALSRQSSHLPFRGSKLTQVLRDSFVGGKKNKTCMIAMISPSMSCVENTLNTLRYADRVKELIAKEDEHLQSVEGDGEKSPDLNEESEPEMMADEEGDEEPEDEDNQHLTISSEEASSYNNMSYDMSFNHTLNILGPSRNVDIQEVAEQHALLVENLETYAHNFRQLKTDKEIEQYTQNSESALMKLLAMVNRTRDVTHNYNTQKLLKEENQNAYKKGELDESE', 729, 'Q9W1U1;', 'KD00203', 'Drosophila melanogaster (Fruit fly)', 'Klp59D', '#FI21273p1 {ECO:0000313|EMBL:AGW25613.1}#Kinesin-like protein at 59D {ECO:0000313|EMBL:AAF46962.2}', '-', '-', '37674'),
(204, 'Q7S8M2', 'Probable kinetochore protein spc24', 'GO:0000778===GO:0051455===GO:0031617', 24728, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MLLEEDPSTLIAHTTQNFNITPDRHAVSRVAESLSTLQQARDLRLRESETNLKKLARTLNTLQSQHQEVTSSHSSAEHASLISRLDTQKFRVAKNVSDLEMETERLQTQLAELQARLQELELQGVDGGDASAAGGATSTGENNGNGSAGNGGQVRSVEDEVLLRLKVYRSLGIEIEREEQDGGEFTRAVVRNDRRGDVCVVNVDRHRFSRFFYANYFWQTL', 221, 'Q7S8M2;', 'KD00204', 'Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DS1257 / FGSC 987)', 'kpr-3', '#Probable kinetochore protein spc24#Kinetochore protein 3', '-', '-', '3878077'),
(205, 'Q9CQA0', 'Centromere protein M', 'GO:0000777', 20039, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). {ECO:0000250}.', 'MSVLRSMDKLPDLNRATVLLVSTEDALLQQLAESMLKDDCASELRVHLANSLPLPSNVNRPRIDLIVFVINLHSKYSLQKVEEFLQHVDSSFFLGKVCFLVTGAGQESHCSVHQNTVIKLAHTYRSPLLLCDLQVESFRAAMARRLVRILQICAGHVPGVSALNLMSLLRSPENPPSKEL', 180, 'Q9CQA0; Q3THN3; Q91VS6;', 'KD00205', 'Mus musculus (Mouse)', 'Cenpm', '#Centromere protein M#CENP-M#Proliferation-associated nuclear element protein 1', '-', '-', '66570'),
(206, 'Q1MTN3', 'Inner centromere protein-related protein pic1', 'GO:0000941===GO:0032133===k', 114476, 'Required for chromosome segregation and cytokinesis. Has a role in sister chromatid cohesion and condensation. {ECO:0000269|PubMed:16199877}.', 'MGSNGSELWFNKELEYSQQLTNGKMKEFFFLVSETMDWLNEHMLEVSKLQLESDIYELVRTPTKIKEKYSTPRLSPVHRCALPTPRMRLTSIQHQLEEAAVEGYKSGESNTVKEPKELHTATNTETQFDDDRDSTKLSSEYVKDDIVNKSTKGGVSPIKETRLPTNLPAFSPTSVERRFTEWNVPLRETSPSPSETADSPNKLPKQKHPAYSFVTLPKREEILKRPASLHSRVESTNSFINQLNRRRTKDNLTNNPEISLDEPIKALPSTTSDAPSSLLNTNVSSSPSKFRKFLSSVIPAKTDLSAKESLTSSTRLSTSYKTRKRSSGVAFSSETVTSSSKERKRSVENEMLKPHPTIFESPPEITSFDKSNAVEAEALTAKLKSNEERLPVSSQPGSDAKSQEFDFFEAKIPDSIAKLNELTASNENHYELKTYDRAERLRQKIQEVSSNKRLIPSTPPTKKPINAVLDAAKNSAAKDLHLAKMKLNNKNDESSLSPAKSHAVITQAPKIPLISTFTRLSTRKSSNDFNSSNSRPSSNALKSDANENTDSSLPPSKKEFIEKSLHKLSEPLHDDSRQNSDHNFAPHSRPIAIRVATASQRELEQTEKRKAKNGAANASNMESRSSENETHRFKKFYGKERELSNNEFPSRQTKTVTSANSSNIRDMEHTISDKPRSEPDAIPSSKSMHSNKPFEEKSEKPTTKRLVTNPSNVNASWHSNMLKRQEDLRKKKPLTDNGATSRHMLKSGLTRVTSKPTQRFANELAEDMSLAFHSTIPKKMEPDSVTSVTQPSVGSLRNNFDIGTTNSQNEDRKKKIAAQKNKNPVHGNVGLTNQHGFKTMHHNVNPFTKQNGIMKGKLPSSSTSQSNKPFIEKASMHAPAKGRNSSMQEPSSKSPLLKTPKSNYFPGYGSLSPNTSVELPEINSDYSDDSDDEGNKKKVNLPSWAESPELREQLKRQQKWDPDKIFGMIKPLQMDEYFRSKDRSKIRFRPRSSSADWSSQDRLTQAEIDNYKKNMGFL', 1018, 'Q1MTN3; Q9UST0; Q9Y7L3;', 'KD00206', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'pic1', '#Inner centromere protein-related protein pic1#INCENP-related protein pic1', '-', '-', '2540250'),
(207, 'Q6DF39', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262', 26858, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSALKMDEEQSLNVYMQEFRTRFINRSSEEVTSQALKESYKDSAQTDAWFKKYRDGELMIEKVLEFRNEITLQNKRIEEKQKNILQEAAKQGEHEQIKEELTERIQRLREELNKKREVALANRKANKERIKELQKSATLFRERLGLEIRKLRGDKLQFVFRCINPKDLDQPYSCIISLNAEGEYEVTGCDPPLECIAEFQEKVRETRNFSALLANLRKSFTALGSQVK', 228, 'Q6DF39;', 'KD00207', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'spc25', '#Kinetochore protein Spc25', '-', '-', '448571'),
(208, 'B1H1S4', 'Spindle and kinetochore-associated protein 3', 'GO:0000940', 62718, 'Component of the SKA1 complex; a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex; it mediates the microtubule-stimulated oligomerization (By similarity). {ECO:0000250}.', 'MSVTGNFFSKLRSLALTLEKETAQLEQVFGNEDNEYEEESPMRVLHDLRSDIMVLKGDFQSTLDKKLTRGQELSAFIKACRVLHERSAADIEQIKETFQTYGYKPLCNDNSENEQTQESEKPKDNDVSPRKADAEDLPILEKAASTSWDLLRAPQLSDFGLSHYQLPTAWEPPKVKPCPKNPEEEKPRIMYKDPEPINVAKTPKCALRLEEDFSQIQHFGISDCSTNLNDDYTIALINKNFQKKQNDTENETCQAKNLKSLLATPSHLSHRMDCVDSPLPPVFFTPGLKVHKKETISLPGKTGERQGLNAADTDSTLLSGTCDRKDSDNAHLEDVHECTAMKPAMDLKSISAAPPYLSLGSNFDSVYSPRPPVFCTPGLKTHKKETSSVLVEPKEVTGCSDTPPLPSFQTNWLKNDTTEKALDITEPVPRPELSYRQYLEEPPSLVLNSNKYEAPAMTEYDIGTPTRPEMTVSLTEDLFKYNVKPSSPPKMSEYEKMLWTPIRPEMTSCITEDISQILSKYCDNNTNVADKEMWNKAGASFGKISSEYEDKENRQY', 556, 'B1H1S4;', 'KD00208', 'Xenopus laevis (African clawed frog)', 'ska3', '#Spindle and kinetochore-associated protein 3', '-', '-', '100158292'),
(209, 'Q8SQK7', 'Probable kinetochore protein NUF2', 'GO:0000777', 50906, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MQKRNVYAVPDLPVKEIMQYFSEMEINIKASDILKPTPQSTQRIYEVLLEVYCGVKTSDLLPRINSGESIEAFEESLSCILLQKRMSGFLKRIGIDNFGLRDLVPDSRRLIGILSVVVNFSMFRDNKRHVYERVCQMNDEKLLLKNEIDEKVHNAKKELERCERDARKSIEEAKGVEEEISLLESELKDFYRHQRALVQETERSKTERNEYSDKLSSLKLMVLNLNQEITCLKTQIVSDPTKLMELLDEMRCLIAKESEIMKGLEVKRVGLKEKIEFMQVLKEDTMKAITLAISNREADKTIDKTNREISELEVQMKNLDSGINALKIRLNHVSRQISHIESKIFNLQDNDKRCSEEISAKLEKLKSNYGVVSDERNSIRGKIEENVRLTKSIEYELVKRRNEHANDITAIQSALCRLKDDVFNYFAEAKGIIDKTMSD', 439, 'Q8SQK7;', 'KD00209', 'Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '860508'),
(210, 'B8N9X2', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 34193, 'Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). {ECO:0000250}.', 'MNSLVATPPVPPHFYEYSRLSSSRPMSTPTYTPNSRKRKADDDGNDHDGRMSASPTSSPAFTPRSLPSRNMKRARPNVSGRPLSLPRLLETLDTDALRGVLRSMCERHPGLVDEVVHTAPRPSVSSALQVLRNYQSTLQSSFPLGGNPASDYAYNRVRQPLSNLLDALSDFTPHFLPPNEIQPSLSLNYLDGATEIIHALPRWHTPQNNIERDSAYDEICKAWILVIREAAKRGGGIQLQYGGWDQKLAKHNQNSGGKLQAAVNELGASLGWMHGPETQSHASPGGNDFGSIREQLLSGTYGLGTPVKVGPW', 312, 'B8N9X2;', 'KD00210', 'Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JC12722 / SRRC 167)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '7912769'),
(211, 'O13710', 'Structural maintenance of chromosomes protein 5', 'k', 124261, '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.', 'MDGLRPSKRRKSNPLYSDYALGSIVRIKLVNFVTYDYCELFPGPYLNLIIGPNGTGKSTIVSAICIGLGWPPKLLGRAKEAREFIKYGKNTATIEIEMKYRDDETVTITRQISQDKSSSFSINREACATSSITSLMDTFNVQLNNLCHFLPQDRVAEFAQLDPYSRLMETERAIDHEGLLPAHEKLIDLRKREREILQNKNQGQSTLNSLKDRQQALEKEVNIFKEREKIKSYIEMLGLAKMLVIYREKTNVFNQLRADKKKLKKDLKDLVEEFQPILDKGEELRSDLKLKDDTFNDYSSASMELNTSNLRARASFSNFMENEKKLYEKVNTNRTLLRNANLTLNEAQQSVKSLTERQGPRPSDNGVQDLQEKMQEVNAEKLQHENEKLESSHELGSIRTLKAQKLIDLDNIKRELSYYNDATKRKLDFMSSAPGWEDAYQTYQLLKEYESAFEAPAYGPIYMNLKCKEKGFAALIEGFFRTDTFRTFIMSNYNDYLKLMDLITSKTKYTPTIREFSSERKKKIEDFEPPCSREKLQSFGFDGYVIDFLEGPEVVLVALCHMLKIHQIPIAKRELPPASVNALNNFRLANGDPVLKTYLAGSSIHLVFRSAYGDREITRRTDPLPSRSIYFSENVEMDLVKRKEEQLNAQLSQLENLQNEERKLQEKVNEHESLLSRTNDILSTLRKERDEKLIPIHEWQQLQERIEHQTLLLRQREKVPEQFAAEIEKNEDIRKENFEALMNSVLKVKENSIKATNNFEKMLGSRLNVIEAKYKLEKHEMDANQVNARLTEVQDRLKDITDKLASAREDAMSLYGSVVDSLQTQSSDRQTAITELNEEFATSSEVDNKISIEETKLKFMNVNSYVMEQYDARKKEIEELESKMSDFDQSVEELQDEMNSIKEDWVSKLEENVQCISDRFSKGMSGMGYAGEVRLGKSDDYDKWYIDILVQFREEEGLQKLTGQRQSGGERSVSTIMYLLSLQGLAIAPFRIVDEINQGMDPRNERVVHRHIVNSVCDNAVSQYFLVTPKLLPDLTYHRNLKVLCICNGAWLPATFRTSLSTYFEKLKKSALISSS', 1076, 'O13710;', 'KD00211', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'smc5', '#Structural maintenance of chromosomes protein 5#DNA repair protein spr18#SMC partner of rad18', '-', '-', '2541587'),
(212, 'P43034', 'Platelet-activating factor acetylhydrolase IB subunit alpha', 'GO:0000776===c;k', 46638, 'Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet- activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity; the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis; whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. {ECO:0000250; ECO:0000269|PubMed:15173193}.', 'MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR', 410, 'P43034; B2R7Q7; Q8WZ88; Q8WZ89;', 'KD00212', 'Homo sapiens (Human)', 'PAFAH1B1', '#Platelet-activating factor acetylhydrolase IB subunit alpha {ECO:0000255|HAMAP-Rule:MF_03141}#Lissencephaly-1 protein {ECO:0000255|HAMAP-Rule:MF_03141}#LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141}#PAF acetylhydrolase 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141}#PAF-AH 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141}#PAF-AH alpha {ECO:0000255|HAMAP-Rule:MF_03141}#PAFAH alpha {ECO:0000255|HAMAP-Rule:MF_03141}', '-', 'ENSG00000007168', '-'),
(213, 'Q92674', 'Centromere protein I', 'GO:0000776===k', 86720, '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. {ECO:0000269|PubMed:12640463; ECO:0000269|PubMed:16622420}.', 'MSPQKRVKNVQAQNRTSQGSSSFQTTLSAWKVKQDPSNSKNISKHGQNNPVGDYEHADDQAEEDALQMAVGYFEKGPIKASQNKDKTLEKHLKTVENVAWKNGLASEEIDILLNIALSGKFGNAVNTRILKCMIPATVISEDSVVKAVSWLCVGKCSGSTKVLFYRWLVAMFDFIDRKEQINLLYGFFFASLQDDALCPYVCHLLYLLTKKENVKPFRVRKLLDLQAKMGMQPHLQALLSLYKFFAPALISVSLPVRKKIYFKNSENLWKTALLAVKQRNRGPSPEPLKLMLGPANVRPLKRKWNSLSVIPVLNSSSYTKECGKKEMSLSDCLNRSGSFPLEQLQSFPQLLQNIHCLELPSQMGSVLNNSLLLHYINCVRDEPVLLRFYYWLSQTLQEECIWYKVNNYEHGKEFTNFLDTIIRAECFLQEGFYSCEAFLYKSLPLWDGLCCRSQFLQLVSWIPFSSFSEVKPLLFDHLAQLFFTSTIYFKCSVLQSLKELLQNWLLWLSMDIHMKPVTNSPLETTLGGSMNSVSKLIHYVGWLSTTAMRLESNNTFLLHFILDFYEKVCDIYINYNLPLVVLFPPGIFYSALLSLDTSILNQLCFIMHRYRKNLTAAKKNELVQKTKSEFNFSSKTYQEFNHYLTSMVGCLWTSKPFGKGIYIDPEILEKTGVAEYKNSLNVVHHPSFLSYAVSFLLQESPEERTVNVSSIRGKKWSWYLDYLFSQGLQGLKLFIRSSVHHSSIPRAEGINCNNQY', 756, 'Q92674; Q5JWZ9; Q96ED0;', 'KD00213', 'Homo sapiens (Human)', 'CENPI', '#Centromere protein I#CENP-I#FSH primary response protein 1#Follicle-stimulating hormone primary response protein#Interphase centromere complex protein 19#Leucine-rich primary response protein 1', '-', 'ENSG00000102384', '-'),
(214, 'Q9YHB5', 'Condensin complex subunit 3', 'k', 115815, 'Regulatory subunit of the condensin complex; a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerase. {ECO:0000269|PubMed:10428035; ECO:0000269|PubMed:9774278}.', 'MVKEGKAMEIKEAFDLSQKAHQNHAKLVSSLRAAYNKTEDKSIFLEEFIHFLKFPLIVYRREPAVERVMDFVAKFVTSFHNSGGENEEEADEENSPVNCLFNFLLQSHGASSMAVRFRVCQLINKLLVNLPENAQIDDDLFDKIHDAMLIRLKDRVPNVRIQAVLALARLQDPSDPDCPVSNAYVHLLENDSNPEVRRAVLTCIAPSAKSLPKIVGRTMDVKEPVRKLAYQVLSEKVHIRALTIAQRVKLLQQGLNDRSAAVKDVIQKKLIQAWLQYSEGDVLDLLHRLDVENSPEVSLSALNALFSVSPVGELVQNCKNLDERKLIPVETLTPENVLYWRALCEHLKSKGDEGEAALENILPEPAVYARYLSSYLQTLPVLSEDQRADMTKIEDLMTKEFIGQQLILTIGCLDTSEEGGRKRLLAVLQEILVMQNTPTSLISSLAELLLFVLKDDDKRIQTVAEIISELREPIVTVDNPKDAAQSRKLQLKLADVKVQLIEAKQALEDSLTNEDYSRASELKEKVKELESLKTQLIKEAEEPEMKEIRVEKNDPETLLKCLIMCNELLKHLSLSKGLGGTLNEICESLILPGITNVHPSVRNMAVLCIGCCALQNKDFARQHLPLLLQILQLDEVKVKNSALNAVFDMLLLFGMDILKSKPTNPDDSQCKAQENADEDISEQEKPGSVDENLTNEEVQEETATVNGILHLFSGFLDSEIAEIRTETAEGLVKLMFSGRLISAKLLSRLILLWYNPVTEEDTKLRHCLGVFFPIFAYSCRSNQECFAEAFLPTLQTLFNAPASSPLADVDVANVAELLVDLTRPSGLNPQNKQSQDYQAAMVHDGLAIKICNEILKDPTAPDVRIYAKALCSLELSRENSTDLLPLLDCAVEDVTDKVCERAIEKVRSQLRSGREEHRVSKETEPQVSKETEDRTNLQENEEGKQKDEANCDENTDTVKEKAARGKATKGRRKGPAAAATRRKASKAEEAEAEMERQEESQCVPVNTRPSRRAKTAALEKTKKNLSKLLNEEAN', 1034, 'Q9YHB5; Q8AVZ4;', 'KD00214', 'Xenopus laevis (African clawed frog)', 'ncapg', '#Condensin complex subunit 3#Chromosome assembly protein xCAP-G#Chromosome-associated protein G#Condensin subunit CAP-G#Non-SMC condensin I complex subunit G', '-', '-', '398088');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(215, 'O43293', 'Death-associated protein kinase 3', 'c;k;m', 52536, 'Serine/threonine kinase which is involved in the regulation of apoptosis; autophagy; transcription; translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase- dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal; depending on the cellular setting. Involved in regulation of starvation-induced autophagy. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle; regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin; PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on ''Ser-77'' upon interferon-gamma activation which is causing RPL13A release from the ribosome; RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor. {ECO:0000269|PubMed:10356987; ECO:0000269|PubMed:11384979; ECO:0000269|PubMed:11781833; ECO:0000269|PubMed:12917339; ECO:0000269|PubMed:15096528; ECO:0000269|PubMed:15367680; ECO:0000269|PubMed:16219639; ECO:0000269|PubMed:17126281; ECO:0000269|PubMed:17158456; ECO:0000269|PubMed:18084323; ECO:0000269|PubMed:18995835; ECO:0000269|PubMed:21169990; ECO:0000269|PubMed:21408167; ECO:0000269|PubMed:21454679; ECO:0000269|PubMed:21487036; ECO:0000269|PubMed:23454120}.', 'MSTFRQEDVEDHYEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIRHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKAIRRRNVRGEDSGRKPERRRLKTTRLKEYTIKSHSSLPPNNSYADFERFSKVLEEAAAAEEGLRELQRSRRLCHEDVEALAAIYEEKEAWYREESDSLGQDLRRLRQELLKTEALKRQAQEEAKGALLGTSGLKRRFSRLENRYEALAKQVASEMRFVQDLVRALEQEKLQGVECGLR', 454, 'O43293; A0AVN4; B3KQE2; Q05JY4;', 'KD00215', 'Homo sapiens (Human)', 'DAPK3', '#Death-associated protein kinase 3#DAP kinase 3#2.7.11.1 {ECO:0000269|PubMed:10356987; ECO:0000269|PubMed:11384979; ECO:0000269|PubMed:11781833; ECO:0000269|PubMed:15096528; ECO:0000269|PubMed:17126281; ECO:0000269|PubMed:18995835}#DAP-like kinase#Dlk#MYPT1 kinase#Zipper-interacting protein kinase#ZIP-kinase', '-', 'ENSG00000167657', '-'),
(216, 'Q2TBH1', 'Centromere protein M', 'GO:0000777', 19635, 'Component of the CENPA-NAC (nucleosome-associated) complex; a complex that plays a central role in assembly of kinetochore proteins; mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres (By similarity). {ECO:0000250}.', 'MSALRPLDKLPGLNTATILLVGTEDALLQQLADSMLKADCTSELKVHLARSLPLPCSVNRPRIDLIVFVVNLHSKLSLQSVEESLCHLDAAFFLGKVAFLATGAGRDSHCSIHRNTVVKLAHTYRSPLLFCDLEIEDFRAAMAQRLVRLLQICAGHVPGVSALNLLSLMRGSENPSLEDL', 180, 'Q2TBH1;', 'KD00216', 'Bos taurus (Bovine)', 'CENPM', '#Centromere protein M#CENP-M', '-', '-', '615953'),
(217, 'Q2TBH8', 'ZW10 interactor', 'GO:0000777', 32629, 'Part of the MIS12 complex; which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase (By similarity). {ECO:0000250}.', 'MGAAESEVETAAREVLAKVADIQEPVGFQEEAELPAQILAEFVMDSRKKDKLLCSQLQVVDFLQNFLVQEGTAQDQNPLASEDTSRQKALEAKEQWKELKATYQEHVEVITNSLTEALPKVEEAQIKQAQLQEALKQLQAKKQMAMEKLRIAQKQWQLEQEKHLQNLAEASSEVRERQTGAQQELQRLYQELGTLKQQAGQEKDKLQRHQTFLQLLYTLQGKQLFNEAEAEIPQELDLPKDKLQQVTQPQEQNTQDTMGREADNPQPVGDAGLPWLPGRQQHKEES', 286, 'Q2TBH8;', 'KD00217', 'Bos taurus (Bovine)', 'ZWINT', '#ZW10 interactor#ZW10-interacting protein 1#Zwint-1', '-', '-', '514564'),
(218, 'O76755', 'Mitotic checkpoint control protein kinase BUB1', 'k', 165455, '', 'MDFDNAKENIQPLASGRNVSLLQASLSQDSTHGQELLAQRKQMEEEVRTYKGADPLGAWYTFICWIEQSYPAGGSGSGLQTVLHQCLTKFEDDERYRQDKRLIKLFIKFMEKQKDKIEFYQQMYNNGIGTMLADFYIAWAYSYDLSGNMRKADEIFRLGLECRAEPLEDLKEAHHHFGYTVGQRMLYSTGEEANAVNQELNERRLALQSLHGRRQQISNSITVGSIRTGAAVKSGLPGVVQVEPSTTTSRRNVGRNVEVFNDENSEGNIPISNSETEVKSSLRSIIDSACSQENIKEPVAWNKANAKRHKHGKIFGSNASPDLGFDIHVDEQAMPPITNYDVRLEQPFRFPTNFVAKNRPQEPWVTPVTIEDEPNASGLPCYNKCLLYPRPNIEFSPEEYRAYSFLKHRNPQHPFIHRNDDWWGTGRVIRGIRCYPNFARYSKPQDLDELDKFWKPPLVPGLQVVFDKIYNEVEQKEYQPEELLAAKWMEKRNVTVHGDFDMEETVCLPGNKMPRRKSFFPSSFRKSIMPRRVSSVQEEDEKKEDEATLIVKDIPSQVAPKIPESPCDQIDEPKIKIFEDSGSPRDNFAVPAVPVPKIEIYEDSEEPQPTPKTRPFYDGDETCSTQMFNMFIKSQAVSTPKGTQKQAPVTSIWNPCSKNYRYQRRLLIPSNLQWRLVLQLCESNLSTILETSEHGTQSLATSGTTTKSTITSTSSPGSNAVSKLGSKIEENTPGQMRLQRVISAGVSAVLSEPEKPGGDNFLRRELWEPNAPSVPMLKSLRFQEDKTETIPRPLACFQEDKTETLPQMPIALPENSMDHGSLGAENCFSAPQLPTLEDESDLCGLFGKTPPKTNIFGSSKRNFDPTSQLFKSTQGDRRSFAVTGNKLEAAPSISNLQDSFMCDLSFVPETQPEAVAKSGAIQKFDIFLDDTQPKLTKSKPVALMVSSFDLDCTLPETQQVAIKEPGTQQENIGHSHMIASFMKDCTEIGSCPSQMPASVVKTNISSTSNKIKFSNDSMSESSRKAPVNENVGISKQPDEFFELNAATEMFATNISMIKNSTLLIPNAKVAEASELSIYYKTTPLTPKQSHRSWSQSDLETPPRENFVHPTSNGDQTVLNETLADANKNPFNVELISSLLESIDFSMYIEKLPHCQLVGHVKRLHPNTHLEVHNEKFEVSKMIGKGAYGSVYVGKHLKSGKKVALKQERPTNYWEFYICLEIHSRLTSEQMIPSYAHIDYALVGNNSSVYISEFSDYGSLIGVCNKVKSVTNRNMDEYVVMHLSCQMLDIVDHLHAMGIIHADIKPDNFLLMKPICADPNEVSLQLIDFGVSIDMKLFPDNQTFNYVHHDDLFKCIEMRTGRPWTYQLDLYGLVSVMHVLLFGRYMEVVQRSPSTIWMPKTNVPRYFQRTMWENIFRTLLNIRDCRTMPNLQQLRTQLKCALAEKEKYVAEAISKFNTILQK', 1461, 'O76755;', 'KD00218', 'Drosophila melanogaster (Fruit fly)', 'BubR1', '#Mitotic checkpoint control protein kinase BUB1 {ECO:0000313|EMBL:AAC32190.1}', '-', '-', '-'),
(219, 'Q6CER3', 'DASH complex subunit DAD1', 'GO:0042729', 10306, '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}.', 'MSRVSMFPTEDKRSYFERQRDQYIKNISASMEDVLNNLNALNRSLEHTVGLSQKSEELAEMWSHFYNTVNEDLVKTEDGDIEVDTTKE', 88, 'Q6CER3;', 'KD00219', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'DAD1', '#DASH complex subunit DAD1#Outer kinetochore protein DAD1', '-', '-', '2907311'),
(220, 'Q6CER9', 'Histone H3-like centromeric protein CSE4', 'GO:0034501===GO:0000941', 16550, '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}.', 'MARISLASSSAGVAGKPRGGGGLHPLGQTRKTLPGERRDTTQKITKPRYKPGQKALKEIRRYQRGTELLIAKLPFARVVREVALNYLGSEYGNLQWQSMALLALQEAAEAFLVHLFEDVNLCAIHAKRVTIMQKDMQLARRIRGAWGGAG', 150, 'Q6CER9;', 'KD00220', 'Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candidlipolytica)', 'CSE4', '#Histone H3-like centromeric protein CSE4#CENP-A homolog', '-', '-', '2907440'),
(221, 'Q6CJ49', 'DASH complex subunit SPC34', 'GO:0008608===GO:0042729', 31796, '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}.', 'MSGSLDYCLDQISKSAESISTLYFKPPGIFRNAIVPGNSKVYSDLIVKLIRDGDSIEEMSLYSTDNDGNMKRKDGKVGIYDHLLEREATLKRNRALCLPDPRPITYIPKGFYLSQNDHVIRKKQKPARDFIFEGSNSDELGIYDVLLKKFSKDEQIKQFLHALRNGSVITGEDVSRRKTLFVEDFPISIILSVFREIIDQWPLTEYKEKFEKLMQIYNGLQADINELQKKVEIQELDFQHEALPEKTSISSLIDKEEKEIQKLEKQLDLLEGRNK', 275, 'Q6CJ49;', 'KD00221', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'SPC34', '#DASH complex subunit SPC34#Outer kinetochore protein SPC34', '-', '-', '2895447'),
(222, 'Q2KJY2', 'Kinesin-like protein KIF26B', 'GO:0003777', 223883, 'Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds; possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8; which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules (By similarity). {ECO:0000250}.', 'MNSVAGNKERLAVSTRGKKYGVNEVCSPTKPAAPFSPESWYRKAYEESRAGSRPTPEGAGSALGSSGTPSPGSGTSSPSSFTGSPGPASPGIGTSSPGSLGGSPGFGTGSPGSGSGGGSSPGSDRGVWCENCNARLVELKRQALRLLLPGPFPGKDPAFSAVIHDKLQVPNTIRKAWNDRDNRCDICATHLNQLKQEAIQMVLTLEQAAGSEHYDASPCSPPPLSNIPTLVGSRHVGGLQQPRDWAFVPAPCATSNYTGFANKHGSKPSSLGVSNGAEKKSGSPTHQAKVSLQMATSPSNGNILNSVAIQAHQYLDGTWSLSRTNGVTLYPYQISQLMTESSREGLTEAVLNRYNADKPSACSVPASQGSCVASETSTGTSVAASFFARAAQKLNLSSKKKKHRPSTSSAAEPPLFATSFSGILQTSPPPAPPCLLRAVNKVKDTPGLGKVKVMLRICSTLARDTSESSSFLKVDPRKKQITLYDPLTCGGQNAFQKRGNQVPPKMFAFDAVFPQDASQAEVCAGTVAEVIQSVVNGADGCVFCFGHAKLGKSYTMIGKDDSMQNLGIIPCAISWLFKLINERKEKTGARFSVRVSAVEVWGKEENLRDLLSEVATGSLQDGQSPGVYLCEDPICGTQLQNQSELRAPTAEKAAFFLDAAIASRRSHQQDCDEDDHRNSHVFFTLHIYQYRMEKSGKGGMSGGRSRLHLIDLGSCVKALSKNREGGSGLCLSLSALGNVILALVNGSKHIPYKESKLAMLLRESLGNMNCRTTMIAHISAAVGSYAETLSTIQIASRVLRMKKKKTKYTSSSSGGESSCEEGRMRRPTQLRPFHTRATVDPDFPIAHLSSDPDYSSSSEQSCDTVIYIGPNGTALSDKELTDNEGPPDFVPIVPALQKTRGDSRPAEAGEAAAGKSERDCLKCNTFAELQERLDCIDGSEEPSSFPFEELPAQFGPEQASRGPRLSQAAGASPLSESDKEDNGSEGQLTNREGPELPASKMQRSHSPVPAAAPAHSPSPASPRSVPGSSSQHSASPLVQSPSLQSSRESLNSCGFVEGKPRPMGSPRLGIASLSKTSEYKPPSSPSQRCKVYTQKGVLPSPAPLPPSSKDSGVASRESLLQPEVRTPPVGMSPQVLKKSMSAGSEGFPETPVDDEQQAATPSESKKEILSTTMVTVQQPLELNGEDELVFTLVEELTISGVLDSGRPTSIISFNSDCSARALASGSRPVSIISSISEDLECYSSTAPVSEVSITQFLPLPKMSLDEKAQDAGSRRSSISSWLSEMSAGSEGEQSCHSFIAQTCFGHGEAMAEPVASEFVSSLQNTAVVCREKPKASPDNLLILSEMGDDSFNKAAPIKGCKISTVSKAMVTISNTANLSSCEGYIPMKTNITVYPCIAMSPRNIQEPEAPTATPKAGPTLAQSRESKENSAKKEMKFEDPWLKREEEVKKETAHPNEEGMMRCETATGPSNAETRAEQEQDGKPSPGDRLSSSSGEVSASPVTDNFRRVVDGCEMALPGLATQSPVHPNKSVKSSSLPRAFQKASRQEEPDSLSYYCAAETNGVGAASGTPPSKATLEGKVASPKHCVLARPKGTPPLPPVRKSSLDQKNRASPQHSASGSGTSSPLNQPAAFPAGLPDEPSGKTKDASSSSKLFSAKLEQLASRSNSLGRATVSHYECLSLERAESLSSVSSRLHAGKDGTMPRAGRSLGRSAGTSPPSSGASPKAGQSKISAVSRLLLASPRARGPSASTTKTLSFSTKSLPQAVGQGSSSPPGGKHTPWSTQSLSRNRSSGLASKLPLRAVSGRISELLQGGAGARGLQLRAGPEAEARGGALAEDEPAAAHLLPSPYSKITPPRRPHRCSSGHGSDNSSVLSGELPPAMGKTALFYHSGGSSGYESVMRDSEATGSASSAQDSTSENSSSVGGRCRSLKTPKKRSNPGSQRRRLIPALSLDTSSPVRKPPNSTGVRWVDGPLRSSPRGLGEPFEIKVYEIDDVERLQRRRGGASKEAMCFNAKLKILEHRQQRIAEVRAKYEWLMKELEATKQYLMLDPNKWLSEFDLEQVWELDSLEYLEALECVTERLESRVNFCKAHLMMITCFDITSRRR', 2108, 'Q2KJY2; Q6ZQR9; Q6ZUZ0; Q8IUN3; Q8IVR1; Q9NWB4;', 'KD00222', 'Homo sapiens (Human)', 'KIF26B', '#Kinesin-like protein KIF26B', '-', 'ENSG00000162849', '-'),
(223, 'C4R591', 'Tethering factor for nuclear proteasome STS1', 'GO:0061638', 33421, 'Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). {ECO:0000250}.', 'MSSLQTSFPWGFKKAVISKPTKNKRKIQEDIDTLGDAKSRTKFHPNNSNSTSRKHRTHAIMGTKLPLNTLIETLDHESLQKLVKSLVEQRPDVQEALYNAAPTVTVQVCIDKLTDKVENIKCNLPYKVDTECDYTYLRVKALVHEFFQALSDYMLNFLPPQEYDVSKSIEFLNGFLLKVLLKMPMFSHMEFKYYYKLTLDKLNTVYVNLIADFIQQKPTNILLLKDSDLAEKLLEINKHYEDYFEQVSQLLSQDEGSDIPERLQGLSNLLNFSSENNPLNGGVVSSVKGSW', 291, 'C4R591;', 'KD00223', 'Komagataella pastoris (strain GS115 / ATCC 20864) (Yeast) (Pichipastoris)', 'STS1', '#Tethering factor for nuclear proteasome STS1', '-', '-', '8200378'),
(224, 'Q08581', 'Kinetochore protein SLK19', 'GO:0000776===GO:0000778===GO:0098653===k', 95380, 'Has a role in spindle assembly and stability. Required to ensure a timely exit form mitosis. Essential to maintain pre- anaphase spindle polarity. Associates to the plus ends of the microtubules at the kinetochore and spindle midzone. A component of the FEAR (CDC14 Early Anaphase Release) network which promotes CDC14 release from the nucleolus during early anaphase. Required for proper chromosome segregation during meiosis I where it prevents premature sister chromatid seperation. {ECO:0000269|PubMed:10427094; ECO:0000269|PubMed:10835382; ECO:0000269|PubMed:11050386; ECO:0000269|PubMed:11533655; ECO:0000269|PubMed:11832211; ECO:0000269|PubMed:12354097; ECO:0000269|PubMed:12737807}.', 'MNEVPTTPVRLILGQAQQREQNSENCSQERNPRTFNSEPDSSFNSPGSSQFVIHPHEPLEKEKDEKQDLDRSIDYGRSSALNNKNNANPLENIDINKMFDDKKSDSGTNDDKGGASTSDKHVLALNYSPIRVEMNSSEKRSDKNVDVDENDKEGSHINKKLKLQLESVPDLKQSSTKDIINDKEEIMSSPMAIDMIETNISPNKFIINDGVERNDSFNINTDTLKLENDINEKQQEEDFIKSNSNNVVNIDNAYKEKEDEENDITNSHINRLTPLYETSARESNSNEEGRNDYDDDNQLDIRHDNFQIVAKRNEELTDQIYHLNQMLNSLISKNESLSFQYEKLNKNHQLLIDLTNEKLDKLNTERESDIAKVEKFKKRIKELNTEIKVLNSNQKILQEKFDASITEVNHIKGEHENTVNTLQQNEKILNDKNVELENMKAELKGNNDKLSEYETTLNDLNSRIVQLNDKIESTDIVLKSKENELDNLKLSLKETLSISKDFNDSDLIGQINELISTKNNLQQKMDDLNNLNDDNLKVVQDKLIKNEETLKLKEAEIDSLNSEMDELKKQITSKDDEFKMWQSKYETVEDEAKIRNAEVTELNGDIEDLKESKLHLEETITELENKVHKLENECELEKQKFEKTSLELESLQLKNSNIQAEHIKELENLHENLISLQNELKISSDRITTLTKENEVLMEQNNNNNNSVTLSNDQKDRDDEKIKSLGKQVQDWKEKYEAKEKDTNKRLKLLAEDLYIQYSSKHEQKVKLLKKGYENKYQNKFDQLNLENKTLSEEIEQLNKQLSSEREEKQELLKLLENEKK', 821, 'Q08581; D6W2Q4;', 'KD00224', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SLK19', '#Kinetochore protein SLK19#Synthetic lethal KAR3 protein 19', '-', '-', '854370'),
(225, 'Q9WVM1', 'Rac GTPase-activating protein 1', 'GO:0051988', 70158, 'Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells. {ECO:0000269|PubMed:10235109; ECO:0000269|PubMed:10493933; ECO:0000269|PubMed:10979956; ECO:0000269|PubMed:11287179}.', 'MDTTMVNLWTLFEQLVRRMEIINEGNESIEFIQVVKDFEDFRKKYQRTNQELEKFKDLLLKAETGRSALDVKLKHARNQVDVEIKRRQRAEAECAKLEQQIQLIRDILMCDTSGSIQLSEEQKSALAFLNRGQASSGHAGNNRLSTIDESGSILSDISFDKTDESLDWDSSLVKNFKMKKREKRRSNSRQFIDGPPGPVKKTCSIGSTVDQANESIVAKTTVTVPSDGGPIEAVSTIETLPSWTRSRGKSGPLQPVNSDSALNSRPLEPRTDTDNLGTPQNTGGMRLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRLVSHPECRDRCPLPCIPPLVGTPVKIGEGMLADFVSQASPMIPAIVVSCVNEIEQRGLTEAGLYRISGCDRTVKELKEKFLKVKTVPLLSKVDDIHVICSLLKDFLRNLKEPLLTFWLSKAFMEAAEITDEDNSTAAMYQAVSELPQANRDTLAFLMIHLQRVSQSPDTKMDIANLAKVFGPTIVAHTVPNPDPVTMFQDIKRQLKVVERLLSLPLEYWNQFMMVDQENIDSQRGNGNSTPRTPDVKVSLLGPVTTPEFQLVKTPLSSSLSQRLYNLSKSTPRFGNKSKSATNLGQQGKFFPAPYLK', 628, 'Q9WVM1; Q3THR5; Q3TI41; Q3TM81;', 'KD00225', 'Mus musculus (Mouse)', 'Racgap1', '#Rac GTPase-activating protein 1#Male germ cell RacGap#MgcRacGAP', '-', '-', '26934'),
(226, 'G5EDA3', 'CENP-C-like protein HCP-4HCP-4', 'k', 97423, '', 'MNRKPRTRSTIVPGRKMITEIVALREAGLDDTRPSYLEEPTVIVDESMMNDSANLEEREWRKQGLSEKQMFAILEKRKQTQLNNARKRLEKEMYGAKTFKELIACREYSECESDSENTVNQNVRSASVFAIPALPKHISEKSMMGSPIANSRGSGKAGLSCSTPKSSSDTSMRSLRSLDISHVVNTDRLDAERVTVHTKSVVIPTILEERESTLQKTLTIEKNHSSQLQKTFTVAEDAPEELQKTVTIEKNQSSEMQRTFTVAKDASKEQSQLQRTVTIEKNQSSQLQGNFTVAKDAPEELQKTVTIEKNQSSEMQGTVTVAKDAEHSSLQKTFTKPTEKDESSLQRTFNVANRDENNDSTLQKTFIIEERDAYEQGTTSVGVKPPVLAQNTMEGGEKRRTSKVTSDERERRNASISNPLHNSMLEKEEIQSPGANFFKHPRKKIRPVVQTPPRIKATSRLSTESNKERTIEMESVAEERTMEADSIGSSYISPTFNASRVSPVPEVPEKVEPMHVSKAATPKSIRHTDNSIRNIGPTNNVECARAALLSTPTRMDIVDSVNRVTPARRYEQPTFASLVKRMNMKDANRLLEETSRKNTPAKTTATTSSAAVRMVLEDDEEDQATEVIEKRSENGGVIVDGEDEAADSSNRSLNIELNALTVNEEPAHDISAIDFPEDDTNEMRSSSDEEEMEARPDPRKKSSRRLGLLSDSIALGLASSSRRRPNDTFVDETWYPEPNSKGNRRPRTHRGMKLKEHQLMKPEDAPDGVRRSTRVRVKPVRSWLGEQPVYVNSPISGCKRLTGVTAVVIKDPRLCYYRTADVRTATERELKDKANKRALAQEKKQQRQNARSGRRHDSDDDEEDDM', 866, 'G5EDA3;', 'KD00226', 'Caenorhabditis elegans', 'hcp-4', '#CENP-C-like protein HCP-4 {ECO:0000313|EMBL:AAK07638.1}#HCP-4 {ECO:0000313|EMBL:CCD67794.1}', '-', '-', '171964'),
(227, 'P09874', 'Poly [ADP-ribose] polymerase 1', 'c;k', 113084, 'Involved in the base excision repair (BER) pathway; by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP- ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK; forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription; and is thus involved importantly in Th1 cytokine production. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1; UIMC1/RAP80; and BRCA1 to DNA damage sites. {ECO:0000269|PubMed:17177976; ECO:0000269|PubMed:18172500; ECO:0000269|PubMed:19344625; ECO:0000269|PubMed:19661379; ECO:0000269|PubMed:23230272}.', 'MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW', 1014, 'P09874; B1ANJ4; Q8IUZ9;', 'KD00227', 'Homo sapiens (Human)', 'PARP1', '#Poly [ADP-ribose] polymerase 1#PARP-1#2.4.2.30#ADP-ribosyltransferase diphtheria toxin-like 1#ARTD1#NAD(+) ADP-ribosyltransferase 1#ADPRT 1#Poly[ADP-ribose] synthase 1', 'BIOMD0000000220,Albeck2008_extrinsic_apoptosis;BIOMD0000000407,Schliemann2011_TNF_ProAntiApoptosis;', 'ENSG00000185480', '-'),
(228, 'Q28BZ7', 'Centrosomal protein cep57l1', 'GO:0000777', 54747, 'Required for spindle microtubule attachment to both kinetochores and centrosomes. Also functions to tether minus-ends of spindle microtubules to centrosomes. May act by forming ring- like structures around microtubules; or by serving as a cross- linker or scaffold at the attachment site (By similarity). {ECO:0000250}.', 'MESLSKESYLSSFHQFPSYAPLPDHIKFESVSSKKIQCSALENISPHQYDILQAPNSRALISALKTLQEKICRLELEKTHARDRLTNLTRVAGEHKKVLESEKQSAELAAKEATNQQNDIGKQLNNAKQRCSLLEKQLDYMKEMMENADTQKTTIHEHQMLTQKEQKEIQSKLKKLEVLEKMCTRLSATHKSAETKIQHLEEKLSVEEQNRKALQDKAAQVQTSLEVNRILLSSASAQNSTQRKVKKKKQSKLKNSVSKEPPSKCFYPKAGELPFVAGKSTTSSHSLSANVQNVLHMMKHHSPQVSQKNPKTAEHKPSVLPGGSRTIPTRLISSFTGDNLSDILLALQDELGQMSFEHQELLRHINETKNTDMREDLERELDYVVKQMEIKSDQIMKLKRHQLNVNKLKKTAKLLKEQPRPTSVTKLAADKQNTGAKDPSTPRRKGDLADGSGTPNSKASLELLKSVRKIQMTLKKDDIMWEK', 483, 'Q28BZ7; A9ULF2; Q0VFM8;', 'KD00228', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'cep57l1', '#Centrosomal protein cep57l1#Centrosomal protein 57kDa-like protein 1#Centrosomal protein of 57 kDa#Cep57#Cep57-related protein#Cep57R', '-', '-', '733970'),
(229, 'O43264', 'Centromere/kinetochore protein zw10 homolog', 'GO:0000776===GO:0000777===GO:0005828===GO:0034501===k', 88829, 'Essential component of the mitotic checkpoint; which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum. {ECO:0000269|PubMed:11590237; ECO:0000269|PubMed:15029241; ECO:0000269|PubMed:15094189; ECO:0000269|PubMed:15485811; ECO:0000269|PubMed:15824131}.', 'MASFVTEVLAHSGRLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPSMQSAQGLITQVDKLSEDIDLLKSRIESEVRRDLHVSTGEFTDLKQQLERDSVVLSLLKQLQEFSTAIEEYNCALTEKKYVTGAQRLEEAQKCLKLLKSRKCFDLKILKSLSMELTIQKQNILYHLGEEWQKLIVWKFPPSKDTSSLESYLQTELHLYTEQSHKEEKTPMPPISSVLLAFSVLGELHSKLKSFGQMLLKYILRPLASCPSLHAVIESQPNIVIIRFESIMTNLEYPSPSEVFTKIRLVLEVLQKQLLDLPLDTDLENEKTSTVPLAEMLGDMIWEDLSECLIKNCLVYSIPTNSSKLQQYEEIIQSTEEFENALKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARNLMTSEIHNTVKIIPDSKINVPELPTPDEDNKLEVQKVSNTQYHEVMNLEPENTLDQHSFSLPTCRISESVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLQKLPQLAAIHHNNCMYIAHHLLTLGHQFRLRLAPILCDGTATFVDLVPGFRRLGTECFLAQMRAQKGELLERLSSARNFSNMDDEENYSAASKAVRQVLHQLKRLGIVWQDVLPVNIYCKAMGTLLNTAISEVIGKITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSEESKNKKYQEEVPVYVPKWMPFKELMMMLQASLQEIGDRWADGKGPLAAAFSSSEVKALIRALFQNTERRAAALAKIK', 779, 'O43264; A1A528;', 'KD00229', 'Homo sapiens (Human)', 'ZW10', '#Centromere/kinetochore protein zw10 homolog', '-', 'ENSG00000086827', '-'),
(230, 'Q61768', 'Kinesin-1 heavy chain', 'GO:0003777', 109551, 'Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. May be involved in the mechanisms of growth arrest induced by exposure to DNA-damaging drugs or by cellular senescence. {ECO:0000269|PubMed:9657148}.', 'MADPAECNIKVMCRFRPLNESEVNRGDKYVAKFQGEDTVMIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKTLRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTADKDIAITSDKPAAAVGMAGSFTDAERRKCEEELAKLYKQLDDKDEEINQQSQLVEKLKTQMLDQEELLASTRRDQDNMQAELNRLQAENDASKEEVKEVLQALEELAVNYDQKSQEVEDKTKEYELLSDELNQKSATLASIDAELQKLKEMTNHQKKRAAEMMASLLKDLAEIGIAVGNNDVKQPEGTGMIDEEFTVARLYISKMKSEVKTMVKRCKQLESTQTESNKKMEENEKELAACQLRISQHEAKIKSLTEYLQNVEQKKRQLEESVDSLGEELVQLRAQEKVHEMEKEHLNKVQTANEVKQAVEQQIQSHRETHQKQISSLRDEVEAKEKLITDLQDQNQKMVLEQERLRVEHERLKATDQEKSRKLHELTVMQDRREQARQDLKGLEETVAKELQTLHNLRKLFVQDLATRVKKSAEVDSDDTGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENASRDRKRYQQEVDRIKEAVRSKNMARRGHSAQIAKPIRPGQHPAASPTHPGTVRGGGSFVQNNQPVGLRGGGGKQS', 963, 'Q61768; O08711; Q5BL10; Q61580;', 'KD00230', 'Mus musculus (Mouse)', 'Kif5b', '#Kinesin-1 heavy chain#Conventional kinesin heavy chain#Ubiquitous kinesin heavy chain#UKHC', '-', '-', '16573'),
(231, 'Q9UR05', 'Dynein light chain 1; cytoplasmic', 'GO:0005868===k', 9822, 'Acts as one of several non-catalytic accessory components of the cytoplasmic dynein complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). {ECO:0000250}.', 'MAVIKAVDMSEKMQQEAIHAAVQAMEKFTIEKDIAAFIKREFDKKFSPTWHCIVGRNFGSFVTHESRHFIYFYLGTVAFLLFKSG', 85, 'Q9UR05;', 'KD00231', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'dlc2', '#Dynein light chain 1; cytoplasmic', '-', '-', '2543530'),
(232, 'Q02956', 'Protein kinase C zeta type', 'c;k', 67682, 'Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade; and is involved in NF-kappa-B activation; mitogenic signaling; cell proliferation; cell polarity; inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages; or following mitogenic stimuli; functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3; but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells; binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62; functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase; which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes; forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1; stimulates neuronal differentiation in PC12 cells. In the inflammatory response; is required for the T-helper 2 (Th2) differentiation process; including interleukin production; efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma); a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response; can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at ''Ser-311''. Necessary and sufficient for LTP maintenance in hippocampal CA1 pyramidal cells. In vein endothelial cells treated with the oxidant peroxynitrite; phosphorylates STK11 leading to nuclear export of STK11; subsequent inhibition of PI3K/Akt signaling; and increased apoptosis. {ECO:0000269|PubMed:15987782; ECO:0000269|PubMed:21131967}.', 'MPSRTDPKMDRSGGRVRLKAHYGGDILITSVDAMTTFKDLCEEVRDMCGLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLVCQGRDEVLIIHVFPSIPEQPGMPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRGAYCGQCSERIWGLSRQGYRCINCKLLVHKRCHVLVPLTCRRHMDSVMPSQEPPVDDKNDGVDLPSEETDGIAYISSSRKHDNIKDDSEDLKPVIDGVDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQTLPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSAEESV', 592, 'Q02956; A2AD76;', 'KD00232', 'Mus musculus (Mouse)', 'Prkcz', '#Protein kinase C zeta type#2.7.11.13#nPKC-zeta', '-', '-', '18762'),
(233, 'Q99P69', 'Kinetochore protein Nuf2', 'GO:0000776===GO:0000777===GO:0008608===GO:0031262', 54594, '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}.', 'METLSFPRYNVAELVVHIRNKLLTGADGKNLSKSDFLPNPKSDVLYMIYMKALQLVYGVRLEHFYMMPMNIEVTYPHLMEGFLPVRSLFFYMDSFMPICRVNDFEIVDILNPRTNRTSRFLSGIINFIHFRETCLEKCEEFLLQNKSSMVRMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQHLLNEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIEKVAEERSAKLEEKTAELKKRMVRMV', 463, 'Q99P69; Q8BTK7; Q8VE05; Q9CST5;', 'KD00233', 'Mus musculus (Mouse)', 'Nuf2', '#Kinetochore protein Nuf2#Cell division cycle-associated protein 1', '-', '-', '66977'),
(234, 'Q9HBM1', 'Kinetochore protein Spc25', 'GO:0000777===GO:0031262===k', 26153, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. {ECO:0000269|PubMed:14699129; ECO:0000269|PubMed:14738735}.', 'MVEDELALFDKSINEFWNKFKSTDTSCQMAGLRDTYKDSIKAFAEKLSVKLKEEERMVEMFLEYQNQISRQNKLIQEKKDNLLKLIAEVKGKKQELEVLTANIQDLKEEYSRKKETISTANKANAERLKRLQKSADLYKDRLGLEIRKIYGEKLQFIFTNIDPKNPESPFMFSLHLNEARDYEVSDSAPHLEGLAEFQENVRKTNNFSAFLANVRKAFTATVYN', 224, 'Q9HBM1; A8K4X8; D3DPC0;', 'KD00234', 'Homo sapiens (Human)', 'SPC25', '#Kinetochore protein Spc25#hSpc25', '-', 'ENSG00000262452', '-'),
(235, 'P36162', 'DASH complex subunit DAD2', 'GO:0008608===GO:0051987===GO:0042729===SCL===k', 15072, '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}.', 'MDSIDEQIAIKRKELQSLQKITSLTDGLKIQLTELNEQIKEMGMNADSVAQLMNNWDSIINNISQASLGLLQYAEGDYEIGPWKDSKKKESEQSNETGLEAQENDKNDEDNDEDEDLVPLPETMVRIRVDGNE', 133, 'P36162; D6VXE3;', 'KD00235', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'DAD2', '#DASH complex subunit DAD2#DUO1 and DAM1-interacting protein 2#Helper of ASK1 protein 1#Outer kinetochore protein DAD2', '-', '-', '853958'),
(236, 'Q03954', 'DASH complex subunit SPC19', 'GO:0008608===GO:0051987===GO:0042729===SCL===c;k', 18910, '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}.', 'MTDALEQSVLALEGTVSVLKDSVESLKCANEPSTNLASTMLQTKRVFRLVPEYDVERSKLDLIEEVEPLVRTLGDKLRKSMGRMQRELDTLQQTYELNDLRLKKNISMDDDDALNSPDMGQEYEGRDADDVVMMASSTNEELEELKKLKEKKKQLENKLEILKQK', 165, 'Q03954; D6VSI3;', 'KD00236', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SPC19', '#DASH complex subunit SPC19#19 kDa spindle pole component protein#Outer kinetochore protein SPC19', '-', '-', '851782'),
(237, 'Q7XPJ0', 'Kinesin-like calmodulin-binding protein homolog', 'GO:0003777', 141786, 'Minus-end microtubule-dependent motor protein involved in the regulation of cell division. {ECO:0000250}.', 'MNGGGASGGDGYDSDGYSFAPPTPTTLSMSIPPELAGAIPLIDRFQVEGFLKAMQKQIHSAGKRGFFSKKSVGPHVREKFTLEDMLCFQKDPIPTSLLKISSDLVSRSIKLFHVILKYMGIDSPAIISLDERIELVAKLYKHTLKRSELRDELFAQISKQTRNNPDRAWLIRAWELMYLCASSMPPSKDIGAYLSEYVHYIAHGATTDSDVRVLALNTLNALKRSVKAGPRVTIPAREEIEALLSSRKLTTIVFFLDETFEEITYDMATTVADAVEELAGIIKLSVYSSFSLFECRKVVNGSKSSDVGNEEYIGLDDNKYIGDLLSEFKAAKDRNKGEILHCKLVFKKRLFRESDEAITDPMFVQLSYVQLQHDYILGNYPVGRDDAAQLSALQILVEIGFVDNPESCVEWISLLERFLPRQVAITRAKRDWELDIVSRYQLMEHLSKDDARQQFLRILRTLPYGNSVFFSVRKIDDPIGLLPGRIILGINKRGVHFFRPVPKEYLHSAELRDIMQFGSSNTAVFFKMRVAGVLHIFQFETKQGEEICVALQTHINDVMLRRYSKARSATSAVSQNDVSQTYKPPNIEIYEKRVQELSKAVEESERKADLLNEELQKKTKQERDMQKELEGLRDTLQSERQSIKEVTNDLDKLKSLCDEKDSSLQASLMEKTRLETRLKSGQGQESSNRTGVSGNHFERDTLPTVGTVNNSIEMLAKLEEELKSCKKELDASKELSKKLTMENNLLDQKVQRLERAKSEEKSNMERVYEDECCKLKSRIAELEQKLESRTRSLNVTESTLALRNAEVDTLQNSLKELDELREFKADVDRKNQQTAEILKRQGAQLIELENLYKQEQVLRKRYYNTIEDMKGKIRVFCRLRPLNDKELIEKDKNIVCSPDEFTVAHPWKDDKSKQHIYDRVFDANTTQEEVFEDTKYLVQSAVDGYNVCIFAYGQTGSGKTFTIYGSENNPGLTPRATSELFRVIKRDGHKYSFSLKAYMVELYQDNLVDLLLAKNATHQKLEIKKDSKGVVTVENVTVVNISSFEELRAIILRGSERRHTAGTNMNVESSRSHLILSIIIESTNLQTQSYARGKLSFVDLAGSERVKKSGSAGKQLKEAQSINKSLSALADVIGALSSDGQHIPYRNHKLTMLMSDSLGGNAKTLMFVNVSPAESNLEETYNSLMYASRVRCIVNDTSKHVAPKEIMRLKKLIAYWKEQAGKRSEDDDLEEIQEERTPKEKADNRLTS', 1248, 'Q7XPJ0; Q84VE4;', 'KD00237', 'Oryza sativa subsp. japonica (Rice)', 'Os04g0666900', '#Kinesin-like calmodulin-binding protein homolog', '-', '-', '4337322'),
(238, 'Q5XH29', 'Centromere protein N-A', 'GO:0034508', 39729, 'Probable component of a centromeric complex involved in assembly of kinetochore proteins; mitotic progression and chromosome segregation. {ECO:0000250}.', 'MDEWLAEFIKRTILKLPFSETVTILKAWGFLTESELQTFTFRYPKDVTATEVVRLCEAKNATVDHAAALDLVFNHAYSNKKSWTVYQMSKPSESENDLFDASEFKLQFKKSIHAVSKNVTLNFKQFGEALWIRIAWGTHNTRPNQYKATFAVYHSQTPYVFITGLGKACRPLMCQALVIAAKYSQIQEMELKSRCLESLKDIVFKRFNQPFSSHHSIPHEKALIPKIVDPRVIYENMREKDRVSHLTRETFGEGPLPKLELASYKLETMFRAESIMDGNLTAVNEPFRCVVKFSSPHLLEAIRSLAPAGIAEAPISTLLSCIPHKARNSFKITEKRGMHPTSSQTTNF', 348, 'Q5XH29;', 'KD00238', 'Xenopus laevis (African clawed frog)', 'cenpn-a', '#Centromere protein N-A#CENP-N-A', '-', '-', '495081'),
(239, 'O60333', 'Kinesin-like protein KIF1B', 'GO:0003777', 204476, 'Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. Isoform 2 is required for induction of neuronal apoptosis. {ECO:0000269|PubMed:18334619}.', 'MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQNRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKHDNETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLIDDYSGSGSKYLKDFQNNKHRYLLASENQRPGHFSTASMGSLTSSPSSCSLSSQVGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERSNSGEVIVTLEPCERSETYVNGKRVSQPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKKEKEEADLLLEQQRLDYESKLQALQKQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPLPPELLPTEMEKTHEDRPFPRTVVAVEVQDLKNGATHYWSLEKLKQRLDLMREMYDRAGEMASSAQDESETTVTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDEMEDFDDEAFVDDAGSDAGTEEGSDLFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFSSVAMTRSGLSLEELRIVEGQGQSSEVITPPEEISRINDLDLKSSTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLAFYHVQNIAVEITESFVDYIKTKPIVFEVFGHYQQHPLHLQGQELNSPPQPCRRFFPPPMPLSKPVPATKLNTMSKTSLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAILSLNIISAKYLKSSHNSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRSLFGSGYSKSPDSNRVTGIYELSLCKMSDTGSPGMQRRRRKILDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSIPKSLSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSGDIESLVDREKELATKCLQLLTHTFNREFSQVHGSVSDCKLSDISPIGRDPSESSFSSATLTPSSTCPSLVDSRSNSLDQKTPEANSRASSPCPEFEQFQIVPAVETPYLARAGKNEFLNLVPDIEEIRPSSVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQSKY', 1816, 'O60333; A6NFS8; A6NKQ4; Q4VXC3; Q4VXC4; Q4VXC5; Q4VXC6; Q96Q94;Q9BV80; Q9P280;', 'KD00239', 'Homo sapiens (Human)', 'KIF1B', '#Kinesin-like protein KIF1B#Klp', '-', 'ENSG00000054523', '-'),
(240, 'P38200', 'Mitotic spindle-associated protein SHE1', 'GO:2000575', 38015, 'May have a role related to the spindle integrity function of the DAM1 complex; which is essential for proper chromosome segregation. Causes growth arrest when highly overexpressed. {ECO:0000269|PubMed:17634282; ECO:0000269|PubMed:7762298}.', 'MNDKLQEEHNEKDTTSQINGFTPPHMSIDFHSNNNSNIIETIGVSKRLGNSVLSELDSRASSKFEFLKDQSEQQYNGDKNNEPKSGSYNINEFFQAKHDSQFGQMESLDTHYTLLHTPKRKSQHAIPQDRSDSMKRSRPSRSIPYTTPVVNDITRRIRRLKLRNSLVNGNDIVARARSMQANSNINSIKNTPLSKPKPFMHKPNFLMPTTNSLNKINSAHRNTSSSSTASSIPRSKVHRSISIRDLHAKTKPVERTPVAQGTNSQLKNSVSVFDRLYKQTTFSRSTSMNNLSSGTSAKSKEHTNVKTRLVKSKTSGSLSSNLKQSTATGTKSDRPIWR', 338, 'P38200; D6VPW8;', 'KD00240', 'Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker''s yeast)', 'SHE1', '#Mitotic spindle-associated protein SHE1#Sensitive to high expression protein 1', '-', '-', '852249'),
(241, 'Q9D1M0', 'Protein SEC13 homolog', 'GO:0000776', 35566, 'Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum; SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). As a component of the GATOR2 complex; inhibits GATOR1 complex; an inhibitor of the amino acid-sensing branch of the TORC1 pathway (By similarity). {ECO:0000250}.', 'MVSVMNTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWKEENGTWEKTHEHSGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDQPSGQKPNYIKKFASGGCDNLIKLWREEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASGNMWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASITEGQQNEQ', 322, 'Q9D1M0; Q99M12; Q9D712;', 'KD00241', 'Mus musculus (Mouse)', 'Sec13', '#Protein SEC13 homolog#SEC13-like protein 1#SEC13-related protein', '-', '-', '110379'),
(242, 'Q03565', 'Barrier-to-autointegration factor 1', 'GO:0000779', 9954, 'DNA-binding protein which plays an essential role in nuclear envelope formation. Required for normal chromosome segregation during mitosis. Associates with the nuclear lamina via its interaction with LEM domain containing proteins emr-1 and lem- 2. {ECO:0000269|PubMed:12684533; ECO:0000269|PubMed:17170708}.', 'MSTSVKHREFVGEPMGDKEVTCIAGIGPTYGTKLTDAGFDKAYVLFGQYLLLKKDEDLFIEWLKETAGVTANHAKTAFNCLNEWADQFM', 89, 'Q03565; Q9BMU1;', 'KD00242', 'Caenorhabditis elegans', 'baf-1', '#Barrier-to-autointegration factor 1', '-', '-', '176330'),
(243, 'Q03569', 'G-protein regulator 2', 'GO:0005818', 60129, '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}.', 'MDVSYYDGPKDEVIEAMLKSAVTAMKLGQYEDGKGRLEDTMEFGTSNFQLLGTIYMYYGRVCRHLNHDAKALEFFEHELNMFKLIFNYPEACDSTRRIVQQALKMEKFSKARRFAEDLIDYTSNKKNGEKYIGQARILFASVCLEGCERDVESNQDEKKKLLSICAEQIAAVKLFNENNTEGAVSETKIMLIEAKCLSLDEKYEESRRKYQECIDFAIKTDQFEAVHIAYYDKALYAETYLLFFIIRDLRSALFYATKFGKERDVVKYKSKLSEEMLRNGEFHEAYLYGLEALVSIRKLGLNEHIGDVLLTIAKCLIALGKRRQAAYFIILGSVLTINQSSFKLFYEQIDVAMNQERSETATDQDACLAIDSSPDPTSSNDMINKFVVKLEHATNVETWEMIVNGIIEDQKKPVAIEKKENEEPVDMMDLIFSMSSRMDDQRTELSAARFIPPRPVSSASKKTTKSHRILPGLRANWTKVQSMKFDGHTMNRILKRSKKSKSSLDSTNSIQGDDTRSDDVTMTSK', 525, 'Q03569;', 'KD00243', 'Caenorhabditis elegans', 'gpr-2', '#G-protein regulator 2', '-', '-', '176318'),
(244, 'Q9QZB9', 'Dynactin subunit 5', 'GO:0000777', 20141, '', 'MELGELLYNKSEYIETASGNKVSRQSVLCGSQNIVLNGKTIIMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQELMIDVTKSYYQKFLPLTQV', 182, 'Q9QZB9; Q3U9A4; Q8BPE5; Q91XC6; Q99J17;', 'KD00244', 'Mus musculus (Mouse)', 'Dctn5', '#Dynactin subunit 5#Dynactin subunit p25', '-', '-', '59288'),
(245, 'Q5R8E2', 'Kinesin light chain 3', 'GO:0003777', 55445, 'Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. {ECO:0000250}.', 'MSVQVAAPGSAGLGPERLSPEELVRQTRQVVQGLEALRAEHHGLVGHLAEALAGQGPVTGLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHVGALEAEKQRLRSQARRLAQENVWLREELEETQRRLRASEEAVAQLEEEKRHLEFLGQLRQYDPPAESQQSESPPRRDSLASLFPSEEEERKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATDLLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFEDVERHYARALSIYEALGGPHDPNVAKTKNNLASAYLKQNKYQQAEELYKEILHKEDLPAPLGAPNTGTAGDAEQALRRSSSLSKIRESIRRGSEKLVSRLRGEGAAGAAGMKRAMSLNTLNVDAPRALGTQFPSWHLDKAPRTLSASTHDLSPH', 504, 'Q5R8E2;', 'KD00245', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'KLC3', '#Kinesin light chain 3', '-', '-', '100173098'),
(246, 'P13496', 'Dynactin subunit 1', 'GO:0000776===GO:0005828===GO:0051383===GO:0034501===GO:0005818===c;k', 141218, 'Required for the cytoplasmic dynein-driven retrograde movement of vesicles and organelles along microtubules. Dynein- dynactin interaction is a key component of the mechanism of axonal transport of vesicles and organelles.', 'MSEKNLKVGARVELTGKDLLGTVAYVGMTSFAVGKWVGVVLDEPKGKNSGSIKGQQYFQCDENCGMFVRPTQLRLLEAAPGSRRSIEDVSGATPTAAQPTKARLSSSRTSLSSSRQSLLGSRTQLTTSLSERTASSSSIGPRKSLAPQNSKDKESPSTSLAEGAPAASGGNGAASHASSKRASFVETGFLEILKPQFTPSQPLRSPSFTMPSNSGAEDKVALLEAQKTSAELQAQLADLTEKLETLKQRRNEDKERLREFDKMKIQFEQLQEFRTKIMGAQASLQKELLRAKQEAKDAIEAKEQHAQEMADLADNVEMITLDKEMAEEKADTLQLELESSKERIEELEVDLELLRSEMQNKAESAIGNISGGGDSPGLSTYEFKQLEQQNIRLKETLVRLRDLSAHDKHDIQKLSKELEMKRSEVTELERTKEKLSAKIDELEAIVADLQEQVDAALGAEEMVEQLAEKKMELEDKVKLLEEEIAQLEALEEVHEQLVESNHELELDLREELDLANGAKKEVLRERDAAIETIYDRDQTIVKFRELVQKLNDQLTELRDRNSSNEKESLQDPSLKMVTETIDYKQMFAESKAYTRAIDVQLRQIELSQANEHVQMLTAFMPESFMSRGGDHDSILVILLISRIVFKCDIVVSQTRERFPPVDAITREAVTQGHAVQQYAFKCRLLHYVHSLQCALHQILYGLNSCQPDTLLRAGSSLPEMVAQEKIVDGIIELLKSNQLDENSTTDNIEKCVAFFNAMNSVLLAGEQLLNEIQMIRDCVASLGAACESILSDTAIAKVIIQEAGATSDSVLLIQFLNENMESVRQQVKLIKRRLPSDQHVIKSGLSQHKVEAMRGLAQNISRIMSAMHQATKQSLAAIVSTIESDNAAEHTLPQEKYWALLTASCERIYEQDDRGPTQNFKTLLAQANSDLQLIAQHLLDKEYDIISAANNASNQQKSGAHSTPITQRAQLIKKQLEQKNVLAATLENREADVKQLKVAAKMKQNELSEMQIRKDLAEKKLSVLQNEYEHAVDKWKQKYEETSLQLQLKEKEFEETMDHLQSDIDALESEKSDLRDKLKLNSTTGKVQPGSESHSPHNISLSGNTSTAPGISNVSYSAPAGTAPVVAEEVELLKNAFNQERNQRLRLQAQDMRAKLSQFEPLHVPQPQDQRITALESELTRMKHAWVLSLLQVRSQDSVNSGTRIDAVALQRRNQPVPLKGEISSKASQLASDILTEYLQRKPHRATHGQFASFPTVDVKRVLQI', 1265, 'P13496; B5X0J0; Q8MT52; Q9VUA1;', 'KD00246', 'Drosophila melanogaster (Fruit fly)', 'Gl', '#Dynactin subunit 1#150 kDa dynein-associated polypeptide#DAP-150#DP-150#Protein glued', '-', '-', '39536'),
(247, 'Q9NS87', 'Kinesin-like protein KIF15', 'GO:0003777', 160160, 'Plus-end directed kinesin-like motor enzyme involved in mitotic spindle assembly. {ECO:0000250}.', 'MAPGCKTELRSVTNGQSNQPSNEGDAIKVFVRIRPPAERSGSADGEQNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESDNFSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKESRGGFLPEEQDRLLSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLKIITTPTKAYQLHSRPVPKLSPEMGSFGSLYTQNSSILDNDILNEPVPPEMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRSES', 1388, 'Q9NS87; Q17RV9; Q69YL6; Q96JX7; Q9H280;', 'KD00247', 'Homo sapiens (Human)', 'KIF15', '#Kinesin-like protein KIF15#Kinesin-like protein 2#hKLP2#Kinesin-like protein 7#Serologically defined breast cancer antigen NY-BR-62', '-', 'ENSG00000163808', '-'),
(248, 'F4JGP4', 'Kinesin-5', 'GO:0003777', 89194, 'Kinesin that supports microtubule movement in an ATP- dependent manner and that functions as a minus-end directed motor as well as a plus-end tracking protein. During mitosis; is involved in early spindle assembly. Participates in the capture of antiparallel interpolar microtubules and helps in generating force to coalign microtubules. {ECO:0000269|PubMed:15659646; ECO:0000269|PubMed:17220198}.', 'MPLRNQNRAPLPSPNVKKEALSSIPFDKRRKETQGTGRRQVLSTVNRQDANSDVGSTEECGKVEFTKDEVLALLNERAKAGKFDTKGKIEQMTDIIKKLKVCVRWYQQVDETHVQDKENLSSSLQSAEKRYSDKELDAKTKEEELRATITEMKENIESLQEKLSKEKLSKLDAIENHRREKDCRVVAEKLQVSLREELDKVKEEKMAAKQKVTSLEDMYKRLQEYNTSLQQYNTKLQTDLEVAREAHTRAEKEKSSILENLTTLRGHSKSLQDQLASSRVSQDEAVKQKDSLLMEVNNLQSELQQVRDDRDRHVVQSQKLAGEILMYKESVGKSSHELDILIAKSGSLEETCSLQKERIKMLEQELAFAKEKLKMVDLSMSHTMTEFEEQKQCMHELQDRLADTERQLFEGELLRKKLHNTILELKGNIRVFCRVRPLLPDDGGRQEASVIAYPTSTESLGRGIDVVQSGNKHPFTFDKVFDHGASQEEVFFEISQLVQSALDGYKVCIFAYGQTGSGKTYTMMGRPETPEQKGLIPRSLEQIFKTSQSLSTQGWKYKMQVSMLEIYNESIRDLLSTSRTIAIESVRADSSTSGRQYTITHDVNGNTHVSDLTIVDVCSIGQISSLLQQAAQSRSVGKTHMNEQSSRSHFVFTLRISGVNESTEQQVQGVLNLIDLAGSERLSRSGATGDRLKETQAINKSLSALSDVIFALAKKEDHVPFRNSKLTYLLQPCLGGDSKTLMFVNISPDPSSTGESLCSLRFAARVNACEIGIPRRQTSAKLLDSRLSYG', 790, 'F4JGP4; Q6NQ77; Q9M0X6;', 'KD00248', 'Arabidopsis thaliana (Mouse-ear cress)', 'ATK5', '#Kinesin-5', '-', '-', '825867'),
(249, 'Q9UM13', 'Anaphase-promoting complex subunit 10', 'c;k;m', 21252, '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}.', 'MTTPNKTPPGADPKQLERTGTVREIGSQAVWSLSSCKPGFGVDQLRDDNLETYWQSDGSQPHLVNIQFRRKTTVKTLCIYADYKSDESYTPSKISVRVGNNFHNLQEIRQLELVEPSGWIHVPLTDNHKKPTRTFMIQIAVLANHQNGRDTHMRQIKIYTPVEESSIGKFPRCTTIDFMMYRSIR', 185, 'Q9UM13; D3DNZ7; Q2V500; Q9UG51; Q9Y5R0;', 'KD00249', 'Homo sapiens (Human)', 'ANAPC10', '#Anaphase-promoting complex subunit 10#APC10#Cyclosome subunit 10', 'BIOMD0000000186,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Dissociation variant;BIOMD0000000187,Ibrahim2008 - Mitotic Spindle Assembly Checkpoint - Convey variant;', 'ENSG00000164162', '-');
INSERT INTO `protein` (`ProteinID`, `UniprotID`, `Name`, `Evidence`, `MolecularWeight`, `Function`, `Sequence`, `Length`, `altUniprotACC`, `DBid`, `Organism`, `Gene`, `allNames`, `BioModel`, `1000Gene`, `GeneAnnotation`) VALUES
(250, 'Q9Y448', 'Small kinetochore-associated protein', 'GO:0000776===GO:0000777===GO:0051988===SCL===k', 35438, 'Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase (PubMed:19667759). Promotes the metaphase-to-anaphase transition and is required for chromosome alignment; normal timing of sister chromatid segregation; and maintenance of spindle pole architecture (PubMed:19667759; PubMed:22110139). The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule- kinetochore attachments (PubMed:21402792). Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis; possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division (PubMed:23035123). May be involved in UV- induced apoptosis via its interaction with PRPF19; however; these results need additional evidences (PubMed:24718257). {ECO:0000269|PubMed:19667759; ECO:0000269|PubMed:21402792; ECO:0000269|PubMed:22110139; ECO:0000269|PubMed:23035123; ECO:0000305|PubMed:24718257}.', 'MAAPEAPPLDRVFRTTWLSTECDSHPLPPSYRKFLFETQAADLAGGTTVAAGNLLNESEKDCGQDRRAPGVQPCRLVTMTSVVKTVYSLQPPSALSGGQPADTQTRATSKSLLPVRSKEVDVSKQLHSGGPENDVTKITKLRRENGQMKATDTATRRNVRKGYKPLSKQKSEEELKDKNQLLEAVNKQLHQKLTETQGELKDLTQKVELLEKFRDNCLAILESKGLDPALGSETLASRQESTTDHMDSMLLLETLQEELKLFNETAKKQMEELQALKVKLEMKEERVRFLEQQTLCNNQVNDLTTALKEMEQLLEM', 316, 'Q9Y448; B4DXA7; Q147U5; Q32Q57; Q5ISJ0; Q6P2S5; Q6PJM0; Q86XB4;', 'KD00250', 'Homo sapiens (Human)', 'KNSTRN', '#Small kinetochore-associated protein {ECO:0000303|PubMed:19667759}#SKAP {ECO:0000303|PubMed:19667759}#Kinetochore-localized astrin-binding protein {ECO:0000303|PubMed:21402792}#Kinastrin {ECO:0000303|PubMed:21402792}#Kinetochore-localized astrin/SPAG5-binding protein#TRAF4-associated factor 1', '-', 'ENSG00000128944', '-'),
(251, 'Q15019', 'Septin-2', 'GO:0000777===SCL', 41487, '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. May play a role in the internalization of 2 intracellular microbial pathogens; Listeria monocytogenes and Shigella flexneri. {ECO:0000269|PubMed:15774761; ECO:0000269|PubMed:17803907; ECO:0000269|PubMed:18209106; ECO:0000269|PubMed:19145258}.', 'MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDGDGGALGHHV', 361, 'Q15019; B4DGE8; Q14132; Q53QU3; Q8IUK9; Q96CB0;', 'KD00251', 'Homo sapiens (Human)', 'SEPT2', '#Septin-2#Neural precursor cell expressed developmentally down-regulated protein 5#NEDD-5', '-', 'ENSG00000168385', '-'),
(252, 'Q9V6Q2', 'Histone H3-like centromeric protein cid', 'GO:0000776===GO:0051382===GO:0051383===GO:0000941===GO:0003777===GO:0000780===k', 25968, 'Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins; mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. {ECO:0000269|PubMed:11483958; ECO:0000269|PubMed:16839185}.', 'MPRHSRAKRAPRPSANNSKSPNDDDTAFRSPEPEDGTDYGLEFTTSQLTLQDNNRRSSTLRRDAGRRQPAARDSSTSGEEEDQENRYPTTRSPQTRRMTVQQESKTRAAGPVAAQNQTRRRKAANPMSRAKRMDREIRRLQHHPGTLIPKLPFSRLVREFIVKYSDDEPLRVTEGALLAMQESCEMYLTQRLADSYMLTKHRNRVTLEVRDMALMAYICDRGRQF', 225, 'Q9V6Q2; Q7YUD4; Q7YUD5; Q8MQP5; Q9NG62;', 'KD00252', 'Drosophila melanogaster (Fruit fly)', 'cid', '#Histone H3-like centromeric protein cid#CENP-A homolog#Centromere identifier protein', '-', '-', '36495'),
(253, 'O43237', 'Cytoplasmic dynein 1 light intermediate chain 2', 'GO:0003777===GO:0005868===c;k;m;s', 54099, '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.', 'MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEEGCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSSPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPGAGGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA', 492, 'O43237; A8K6V1; B4DZP4; Q8TAT3;', 'KD00253', 'Homo sapiens (Human)', 'DYNC1LI2', '#Cytoplasmic dynein 1 light intermediate chain 2#Dynein light intermediate chain 2; cytosolic#LIC-2#LIC53/55', '-', 'ENSG00000135720', '-'),
(254, 'Q96IK1', 'Biorientation of chromosomes in cell division protein 1', 'GO:0000777===SCL===k', 19196, 'Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. {ECO:0000269|PubMed:17938248}.', 'MADGGGGGGTGAVGGGGTSQASAGAATGATGASGGGGPINPASLPPGDPQLIALIVEQLKSRGLFDSFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNPTMNKNQLRNGLRQSVVQSGMLEAGVDRIISQVVDPKLNHIFRPQIERAIHEFLAAQKKAAVPAPPPEPEGQDPPAPSQDTS', 185, 'Q96IK1; B4DXH8; Q9BTW1;', 'KD00254', 'Homo sapiens (Human)', 'BOD1', '#Biorientation of chromosomes in cell division protein 1#Biorientation defective protein 1#Protein FAM44B', '-', 'ENSG00000145919', '-'),
(255, 'Q99KJ8', 'Dynactin subunit 2', 'GO:0000776', 44117, 'Modulates cytoplasmic dynein binding to an organelle; and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development. {ECO:0000269|PubMed:14983524}.', 'MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGDYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLADPDGALAKRLLLQLEATKSSKGSSGGKATAGAPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQNKVHQLYETIQRWSPVASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMMASSLKDNTALLTQVQTTMRENLATVEGNFASIDARMKRLGK', 402, 'Q99KJ8;', 'KD00255', 'Mus musculus (Mouse)', 'Dctn2', '#Dynactin subunit 2#50 kDa dynein-associated polypeptide#Dynactin complex 50 kDa subunit#DCTN-50#Growth cone membrane protein 23-48K#GMP23-48K#p50 dynamitin', '-', '-', '69654'),
(256, 'P62627', '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.', 'MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYANLMHNFILKARSTVREIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE', 96, 'P62627; A2AVR8; O88567; Q4FZJ8; Q9D812;', 'KD00256', 'Mus musculus (Mouse)', 'Dynlrb1', '#Dynein light chain roadblock-type 1#Dynein light chain 2A; cytoplasmic', '-', '-', '67068'),
(257, 'A1A5G0', 'CLIP-associating protein 1', 'GO:0000777===GO:0005828', 160245, 'Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules during anaphase. Plays a crucial role in chromatin-induced microtubule formation. May also act at microtubule minus ends. May be involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN) (By similarity). {ECO:0000250}.', 'MEQGMDYWLGQIQQKDVGKRLQVGPDLMEYLSDRQKSIDLEQDQTVLDRMVDGLATSWVNSSNYKVALLGMDILSALVTRLQDRFRSQIGTVLPSLMDRLGDAKDSVREQDQNLLIKIMEQASNPQYVWERMFSGFKHKNFRTREGVCLCLIATLNVYGAHSLTLSKIVPHICNLLGDPNSQVRDAAINCLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGTMILSSADKNFDDEDSVDGNRPSSASSSASSKAPQAARRGVSLGTARRPGTSSAAPKPGGTAKEGAGGVDEEDFIRGFEDVPTVQIYSSRDLEESLNKIREILSDDKHDWEQRISALKKIRSLLLAGAAEYDTFFPQLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAIMPTVFNLVPNSAKIMATSGVVAIRLIIRQTHVPRLIPIITSNCTSKSVAVRRRCYEFLDLLLQEWQTHSLERHVSVLAETIKKGIHDADSEARIVARKCYWGFHSHFSKEAEQLFHTLESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTVSRASTATSKSTPGSLQRSRSDIDVNAATCAKSKATSGASAAPFSSVAALPPGSYASLGRIRTRRQSSGSTTSTASTPADTRGRSRAKVVSQSQPGSRSSSPGKLLGSGYGGIASGPQRVPQMPSSEKRSKIPRSQGCSRETSPSRIGLDRFGISQPGRIPSAMRVLSSSTDLEAAVADALKKPVRRRYEPYGMYSDDDANSDASSACSERSYSSKNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLIGLQNLLKSQRTLSRVELKRLCEIFTRMFADPHSKRVFSMFLETLVDFVIIHKDDLQDWLFILLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQVVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNSSMGSPSNTIGRTPSRHSSSRASPLTSPTNCSHGGLSPSMLDYDTENLNSDEIYSSLRGVTEAIEKFSFRSQVDLNEPVRREGKKESELGSCDVGIASPASDLRGGTDMVEGGRMALDNKTSLLNTQPPRAFTGPRGREYNPYAYSDSINSYDKTALKEAVFDDDMDQLRDVPIDHSDLVADLLKELSNHNERVEERKGALCELLKITREDSLAVWEEHFKTILLLLLETLGDKDHAIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLAGSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERISKESLHQILPDIIPGLLQGYDNTESSVRKASVFCLVAIYSVIGEELKPYLAQLTGGKMKLLNLYIKRAQTTNSNSSSSSDVSTHS', 1452, 'A1A5G0;', 'KD00257', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'clasp1', '#CLIP-associating protein 1 {ECO:0000250|UniProtKB:Q7Z460}#Cytoplasmic linker-associated protein 1 {ECO:0000312|Xenbase:XB-GENE-6049805}', '-', '-', '100036688'),
(258, 'Q6CJ06', 'Probable kinetochore protein NUF2', 'GO:0000777', 52887, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MSKDVFPLLELSELVTCLQSCDFSLAVEENISKPSSQYVITLYKQIIDTFMGVSPDTLLSNEALFDNSGSNDIQQNPAYTETVKVLALNKICFKFFQDIGVSDFNMMDLYKPDSLRTRRLLSAVVNYARFREERMFDCDKFMSKTEFLLNQLRSKFDDYNYLQQQINKHRNEIELREGETFETLQQQNKHLDQQISRLKGLQETLNIDYNAYKSRKQSLLHDLEKFGFELIELEFERNKLEKHSKTDFNELNLNIEKLSTLLATQQTNLNNLEQKHRKLRISMNTFQTLTHELYDVLQLISTDLQESHLREANLIDMREQLLQTDQKLNNILSSGVMVKMKILQSQLDNQKKKLHQLEGETKAKQIENSETLQLLQRQYTDEVVPDLRAAEEQVENDLANGTIKNYDYEISQLKQAFQTEIDAIDLEYSLLSSHINRYMEEMLRVMVEVTS', 451, 'Q6CJ06;', 'KD00258', 'Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBR1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '2895393'),
(259, 'Q4IBX0', 'Probable kinetochore protein NUF2', 'GO:0000778===GO:0051455===GO:0031617===GO:0031262', 54047, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MAYNPRMSIIPTSQQNSRTRKKEEEADAFMRLPDREIVGCITDIGITFTVADLQKPNAAHVQQIFEWFAELLLNATRETVEPAMRAAAEDIAGEYADIIPSDTRNLMGFYVSLRRLLFECGITDFSFNDLYKPTYDRLVKIFSYLINFVRFRESQTAVIDQHYNKAESTKTRIETLYGENQENEGRLEDMKRNRKAMEAQVQQKTMRNEELKKRLLELRRNQERVAARLEEAKQKKGELTTALEQKTHEKVTLKQESTKLRPYVLQSASDLQENLAELRDILNNDKSHIDALDRRARALQTSTDSFSVVSTDVASCIKILDEIASELAKEEEELARNAKQRDALSERSNNAREVERTETMLKRQLSKWMERTEKLREQSNHKAHEAKEKMHELRAIHRQLTEEHTEKGKEMEVRRVRIEQTEKKMLDLKENIENEVHSAHEEYRKMEAHIKLYIAEMEQAIA', 462, 'Q4IBX0; V6R9D0;', 'KD00259', 'Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084(Wheat head blight fungus) (Fusarium graminearum)', 'NUF2', '#Probable kinetochore protein NUF2', '-', '-', '2787102'),
(260, 'P62628', '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, 'P62628; O88567; Q9D812;', 'KD00260', 'Rattus norvegicus (Rat)', 'Dynlrb1', '#Dynein light chain roadblock-type 1#Bithoraxoid-like protein#BLP#robl/LC7-like protein#Dynein light chain 2A; cytoplasmic#Dynein-associated protein Km23', '-', '-', '170714'),
(261, 'Q5RAH9', 'Baculoviral IAP repeat-containing protein 5', 'GO:0000777===GO:0032133', 16389, 'Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). {ECO:0000250}.', 'MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD', 142, 'Q5RAH9;', 'KD00261', 'Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)', 'BIRC5', '#Baculoviral IAP repeat-containing protein 5#Apoptosis inhibitor survivin', '-', '-', '100172652'),
(262, 'Q2UGF7', 'Tethering factor for nuclear proteasome sts1', 'GO:0061638', 34193, 'Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). {ECO:0000250}.', 'MNSLVATPPVPPHFYEYSRLSSSRPMSTPTYTPNSRKRKADDDGNDHDGRMSASPTSSPAFTPRSLPSRNMKRARPNVSGRPLSLPRLLETLDTDALRGVLRSMCERHPGLVDEVVHTAPRPSVSSALQVLRNYQSTLQSSFPLGGNPASDYAYNRVRQPLSNLLDALSDFTPHFLPPNEIQPSLSLNYLDGATEIIHALPRWHTPQNNIERDSAYDEICKAWILVIREAAKRGGGIQLQYGGWDQKLAKHNQNSGGKLQAAVNELGASLGWMHGPETQSHASPGGNDFGSIREQLLSGTYGLGTPVKVGPW', 312, 'Q2UGF7;', 'KD00262', 'Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)', 'sts1', '#Tethering factor for nuclear proteasome sts1', '-', '-', '5993362'),
(263, 'A1C9U5', 'E3 ubiquitin ligase complex SCF subunit sconC', 'GO:0051382===GO:0031518', 18156, 'Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes; which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression; probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}.', 'MSTTVTLTSSDGVDLTVDRDVAERSVLIKNMLEDLGESGEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE', 159, 'A1C9U5;', 'KD00263', 'Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCT3887 / NRRL 1)', 'sconC', '#E3 ubiquitin ligase complex SCF subunit sconC#Sulfur controller C#Sulfur metabolite repression control protein C', '-', '-', '4706645'),
(264, 'O94716', 'Kinetochore protein fta4', 'GO:0000776', 27149, 'The Sim4 complex is required for loading the DASH complex onto the kinetochore via interaction with dad1. Fta2; fta3 and fta4 associate with the central core (cnt) and inner repeat (inr) region of the centromere. {ECO:0000269|PubMed:16079914}.', 'MDIYEHKKSFMERQIRLLNRPMRPPKDWKLPLKSGQLSESVVETVFQRLQLRIQKHAKLNYSHQATQHVAAQIRKLYEQNSAIEDITFLNPLFYGEIDLSNLDSVKSLPHPWPFQKESRPVEKDEEQEKFNRLTGELLGLLTTLSELEQERSELEQIEKMLEPFEDGPSSIHTNMWKKNPELISTLNSTNTMVAKINSLLRGVSFPSLNNDNQEASLEDEIRSQLFEKTISDD', 233, 'O94716;', 'KD00264', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'fta4', '#Kinetochore protein fta4#Sim4 complex subunit fta4#Sim4-mal2-associated protein 4', '-', '-', '2538719'),
(265, 'O13351', 'Ubiquitin-like protein pmt3/smt3', 'c;k', 12935, 'Required for chromosome segregation where it may be involved in microtubule assembly. Loss of smt3 leads to an increase in telomere length. {ECO:0000269|PubMed:10567589}.', 'MSESPSANISDADKSAITPTTGDTSQQDVKPSTEHINLKVVGQDNNEVFFKIKKTTEFSKLMKIYCARQGKSMNSLRFLVDGERIRPDQTPAELDMEDGDQIEAVLEQLGGCTHLCL', 117, 'O13351; O74186;', 'KD00265', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'pmt3', '#Ubiquitin-like protein pmt3/smt3', '-', '-', '2540927'),
(266, 'Q17BU3', 'Kinesin-like protein unc-104', 'GO:0003777', 185610, 'Required for presynaptic maturation; has a role in axonal transport of dense-core vesicles carrying synaptic vesicle precursors; components required for the morphological transformation of axonal growth cones to mature boutons. {ECO:0000250|UniProtKB:A1ZAJ2}.', 'MSSVKVAVRVRPFNSREISRESKCIIEMSGNTTCITNPKVPPGTSDSIKRFNYDYSYWSHDPRDAEFSTQSMVYADIGEEMLQHSFDGYNVCIFAYGQTGAGKSYTMMGKQEESQEGVIPMICKDLFRRIQETEGVDLKYSVEVSYMEIYCERVRDLLNPKNKGNLKVREHPLLGPYVEDLSKLAVTSYQDIHDLIDEGNKARTVAATNMNETSSRSHAVFTIFFTQRRVDKMTSLETEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVASKSKKSKKADFIPYRDSVLTWLLRENLGGNSKTAMIAAISPADINYDETLSTLRYADRAKQIVCKAVVNEDANAKLIRELKEEIQKLRELLKAEGIEVQEGNRRTPTPMICSPNRLRKRTGSSTEMAVDQLQASEKLIAELNETWEEKLKRTEQIRLQREAVFAEMGVAVKEDGITVGVFSPKKSPHLVNLNEDPTLSECLLYYIKDGLTRLGTSEANVPQDIQLSGSHILKEHCVFENKDGVVTLVPHKDALVYLNGRKLVEPEVLQTGSRVILGKNHVFRFTHPEQAREKREKPKDKDVGENPGGNAEAADWNFAQCELLEKQGIDLKAEMQKRLCALEEQFKREKLAADQEFEEQRKTYEARIDALQKQVEEQSMTMSMYSSYSPEDFHQEEDIFVNPLFESCWTAREAGLAAWAFRKWRYHQFTSLRDDLWGNAIFLKEANAISVELKKKVQFQFTLLTDTLYSPLPPELAPSPIIGGALTNGQEDEFGQSPIPRTIVAVEVTDTKNGATHHWSLDKLRQRLELMREMYHNEAELSPTSPDYNVESLTGGDPFYDRFPWFRMVGRSFVYLSNLLYPVPLVHKVAIVNERGDVRGYLRVAVQPVMDEENADFNNGVKQSARIVFDEEQNGGHKIPKIRTIHDKDEKYIEGSNDIMKLEELEQEDADSGRGDSSVASELHESNEHEPGEHLQPGKEFTFRVTVLQATGIAAEYADIFCQFNFLHRHEEAFSTEPVKNSGSGAPLGFYHVQNITVPVTKSFIEYLKTQPIVFKVFGHYQNHPLHKDAKQDCQITRPPPRRMLPPSIPISQPVRSPKFGPLPCPPSSTVLAKHDVLVWFEICELAPNGEYVPAVVDHSDDLPCRGLYLLHQGIQRRIRITIVHEPTAEVKWKDIRELVVGRIRNQPEPADELDDSDSCVLSLGLFPGEVLEVPGDDRSFFRFEAAWDSSLHNSALLNRVTQTGEQIFITLSAYLELENCARPAIITKDLSMIIYGRDARTGPRSLKHLFSGQYRNPEANRLSGVYELSLRRASEAGSPGVQRRQRRVLDTSSTYVRGEENLHGWRPRGDSLIFDHQWELEKLTRLEEVGRVRHLLMLRERLGMDTTPNPTTKTEKDVCNLAQRASASPVHMVIPPSPQTPVKDQQTPTLPERELTPRETELVWKCVKLIQGRIGGKGDPSDTSNQLAVDASPGDEGCADMNASYISGNSIELCSPDRVDIPNGWEAPAPVPQSQEVSLRLYVPELEEIRVSPVVARKGYLNVLEHGGSGWKKRWVTVRRPYVFIFRSDKDPVERAVLNLATAQVECSEDQAAMVKVPNTFSVVTKHRGYLLQTLGDKEVHDWLYAINPLLAGQIR', 1644, 'Q17BU3;', 'KD00266', 'Aedes aegypti (Yellowfever mosquito) (Culex aegypti)', 'unc-104', '#Kinesin-like protein unc-104', '-', '-', '5565492'),
(267, 'O13734', 'Shugoshin-2', 'GO:0000778===GO:0072356===GO:0000780===k', 72485, 'Involved in chromosome cohesion during mitosis and meiosis by preventing premature dissociation of cohesin complex from centromeres after prophase; when most of cohesin complex dissociates from chromosomes arms. Required for faithful mitotic chromosome segregation and proper kinetochore orientation during meiosis I. In contrast to sgo1; it is dispensable for centromeric protection of rec8 during meiosis I as well as protection of rad21 during mitosis. Required to sense the lack of tension at centromeres during mitosis. {ECO:0000269|PubMed:14730319; ECO:0000269|PubMed:14972679; ECO:0000269|PubMed:16229998}.', 'MSKASLSPNVEDLKKKQIRQYKEIIRISKAQSIRIKELQLENERLLSENIDLRTTAINLEEQLETVQNENEENKTKLAALLNRFHEETDNFLSKLSLCQQEIQDTFKPVEANLAYDVDTDSEDLDEESVVKDTEEIIEQAQHDVSLRNLSGIEDENIIDDGETAINEQKKREANVFSDTQSAPQLKSGKALPADFENPYNLSNSKPVNNNNEDRVEAVTSENKSIDSAPQEKNHEYEIVSPKSLSNKINNQAAAQRRTEEDNANGVAQEENEGSQEAHFHSRIQSDTVIQSTPTKRKWDVDIQNKQINLASAATNVTGYVSETDSRPNRANSLDSAVLLVQSSNKSNRNGHHISDPNLNSSISLKFAPEDTAHNSLTSQENVGPQVTTTSLSNMTVAESPRTDTPREINGLVDSSVTNGNEKFSVEIMNDSNKIGLNPKSFTDEEREILTLFRNPPMRLSSEPPSSNGFSIAHPNNSPLRPPSLQGILNAEDRPYEIEPSRSSFATNDTGSYNNLELLSSVTNLKSPNENDRVTKTQSRRETKVKRRRKARIQETSEESTVVNEPNEKPDGRSRRERKKVNYALPGLRTKLRRNFDLPSDHVKAKKTRRAPKNSENDSATKTETANITSEAPTTSEVTLENSETLNL', 647, 'O13734; Q9UU02;', 'KD00267', 'Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)', 'sgo2', '#Shugoshin-2', '-', '-', '2542788'),
(268, 'Q61315', 'Adenomatous polyposis coli protein', 'GO:0000776===GO:0051988', 311089, 'Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration (By similarity). Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2- dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity). {ECO:0000250}.', 'MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDETMTSGQIDLLERLKEFNLDSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRTFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRAAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRVRQLLQSQAAEAERSSQSRHDAASHEAGRQHEGHGVAESNTAASSSGQSPATRVDHETASVLSSSGTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEQGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSVTLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQNLYGDYAFDANRHDDSRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLSAYHPTTENAGTSSKRGLQITTTAAQIAKVMEEVSAIHTSQDDRSSASTTEFHCVADDRSAARRSSASHTHSNTYNFTKSENSNRTCSMPYAKVEYKRSSNDSLNSVTSSDGYGKRGQMKPSVESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHVIEDEIKQNEQRQARSQNTSYPVYSENTDDKHLKFQPHFGQQECVSPYRSRGTSGSETNRMGSSHAINQNVNQSLCQEDDYEDDKPTNYSERYSEEEQHEEEEERPTNYSIKYNEEKHHVDQPIDYSLKYATDISSSQKPSFSFSKNSSAQSTKPEHLSPSSENTAVPPSNAKRQNQLRPSSAQRNGQTQKGTTCKVPSINQETIQTYCVEDTPICFSRCSSLSSLSSADDEIGCDQTTQEADSANTLQTAEVKENDVTRSAEDPATEVPAVSQNARAKPSRLQASGLSSESTRHNKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLVFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTVQAKREVPKSKVPAAEKRESGPKQTAVNAAVQRVQVLPDVDTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPEESNENQDKEVEKPDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKLAQTASKLPPPVARKPSQLPVYKLLPAQNRLQAQKHVSFTPGDDVPRVYCVEGTPINFSTATSLSDLTIESPPNELATGDGVRAGIQSGEFEKRDTIPTEGRSTDDAQRGKISSIVTPDLDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASSTSSGANKNQVDTKKKKPTSPVKPMPQNTEYRTRVRKNTDSKVNVNTEETFSDNKDSKKPSLQTNAKAFNEKLPNNEDRVRGTFALDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKGKESKDSEAKVTCRPEPNSSQQAASKSQASIKHPANRAQSKPVLQKQPTFPQSSKDGPDRGAATDEKLQNLAIENTPVCFSRNSSLSSLSDIDQENNNNKESEPIKEAEPANSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKRPSRLKSESEKQSPRKVGGILAEDLTLDLKDLQRPDSEHAFSPGSENFDWKAIQEGANSIVSSLHQAAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLEAKKIESENKGIKGGKKVYKSLITGKIRSNSEISSQMKQPLPTNMPSISRGRTMIHIPGLRNSSSSTSPVSKKGPPLKTPASKSPSEGPGATTSPRGTKPAGKSELSPITRQTSQISGSNKGSSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLTKQASLSKNASSIPRSESASKGLNQMSNGNGSNKKVELSRMSSTKSSGSESDSSERPALVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSVQAGGWRKLPPNLSPTIEYNDGRPTKRHDIARSHSESPSRLPINRAGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDERHVSSMPAPRQMKENQVPTKGTWRKIKESDISPTGMASQSASSGAASGAESKPLIYQMAPPVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKGSSSIKDSKDSKDTHGKQSVGSGSPVQTVGLETRLNSFVQVEAPEQKGTEAKPGQSNPVSIAETAETCIAERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVSTNTKKRDSKTDITESSGAQSPKRHSGSYLVTSV', 2845, 'Q61315; Q62044;', 'KD00268', 'Mus musculus (Mouse)', 'Apc', '#Adenomatous polyposis coli protein#Protein APC#mAPC', '-', '-', '-'),
(269, 'Q9DAJ5', 'Dynein light chain roadblock-type 2', 'GO:0005868', 10876, '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.', 'MTEVEETLKRIQSHKGVIGTMVVNAEGIPIRTTLDNSTTVQYAGLLHQLTMKAKSTVRDIDPQNDLTFLRIRSKKHEIMVAPDKEYLLIVIQNPCE', 96, 'Q9DAJ5;', 'KD00269', 'Mus musculus (Mouse)', 'Dynlrb2', '#Dynein light chain roadblock-type 2#Dynein light chain 2B; cytoplasmic', '-', '-', '75465'),
(270, 'P78527', 'DNA-dependent protein kinase catalytic subunit', 'c;k;m', 469089, 'Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes; suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates ''Ser-139'' of histone variant H2AX/H2AFX; thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C; c-Abl/ABL1; histone H1; HSPCA; c-jun/JUN; p53/TP53; PARP1; POU2F1; DHX9; SRF; XRCC1; XRCC1; XRCC4; XRCC5; XRCC6; WRN; MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 ''Ser-588'' and increasing CRY1 protein stability; most likely through an indirect machanism. Interacts with CRY1 and CRY2; negatively regulates CRY1 phosphorylation. {ECO:0000269|PubMed:12649176; ECO:0000269|PubMed:14734805; ECO:0000269|PubMed:15574326; ECO:0000269|PubMed:9679063}.', 'MAGSGAGVRCSLLRLQETLSAADRCGAALAGHQLIRGLGQECVLSSSPAVLALQTSLVFSRDFGLLVFVRKSLNSIEFRECREEILKFLCIFLEKMGQKIAPYSVEIKNTCTSVYTKDRAAKCKIPALDLLIKLLQTFRSSRLMDEFKIGELFSKFYGELALKKKIPDTVLEKVYELLGLLGEVHPSEMINNAENLFRAFLGELKTQMTSAVREPKLPVLAGCLKGLSSLLCNFTKSMEEDPQTSREIFNFVLKAIRPQIDLKRYAVPSAGLRLFALHASQFSTCLLDNYVSLFEVLLKWCAHTNVELKKAALSALESFLKQVSNMVAKNAEMHKNKLQYFMEQFYGIIRNVDSNNKELSIAIRGYGLFAGPCKVINAKDVDFMYVELIQRCKQMFLTQTDTGDDRVYQMPSFLQSVASVLLYLDTVPEVYTPVLEHLVVMQIDSFPQYSPKMQLVCCRAIVKVFLALAAKGPVLRNCISTVVHQGLIRICSKPVVLPKGPESESEDHRASGEVRTGKWKVPTYKDYVDLFRHLLSSDQMMDSILADEAFFSVNSSSESLNHLLYDEFVKSVLKIVEKLDLTLEIQTVGEQENGDEAPGVWMIPTSDPAANLHPAKPKDFSAFINLVEFCREILPEKQAEFFEPWVYSFSYELILQSTRLPLISGFYKLLSITVRNAKKIKYFEGVSPKSLKHSPEDPEKYSCFALFVKFGKEVAVKMKQYKDELLASCLTFLLSLPHNIIELDVRAYVPALQMAFKLGLSYTPLAEVGLNALEEWSIYIDRHVMQPYYKDILPCLDGYLKTSALSDETKNNWEVSALSRAAQKGFNKVVLKHLKKTKNLSSNEAISLEEIRIRVVQMLGSLGGQINKNLLTVTSSDEMMKSYVAWDREKRLSFAVPFREMKPVIFLDVFLPRVTELALTASDRQTKVAACELLHSMVMFMLGKATQMPEGGQGAPPMYQLYKRTFPVLLRLACDVDQVTRQLYEPLVMQLIHWFTNNKKFESQDTVALLEAILDGIVDPVDSTLRDFCGRCIREFLKWSIKQITPQQQEKSPVNTKSLFKRLYSLALHPNAFKRLGASLAFNNIYREFREEESLVEQFVFEALVIYMESLALAHADEKSLGTIQQCCDAIDHLCRIIEKKHVSLNKAKKRRLPRGFPPSASLCLLDLVKWLLAHCGRPQTECRHKSIELFYKFVPLLPGNRSPNLWLKDVLKEEGVSFLINTFEGGGCGQPSGILAQPTLLYLRGPFSLQATLCWLDLLLAALECYNTFIGERTVGALQVLGTEAQSSLLKAVAFFLESIAMHDIIAAEKCFGTGAAGNRTSPQEGERYNYSKCTVVVRIMEFTTTLLNTSPEGWKLLKKDLCNTHLMRVLVQTLCEPASIGFNIGDVQVMAHLPDVCVNLMKALKMSPYKDILETHLREKITAQSIEELCAVNLYGPDAQVDRSRLAAVVSACKQLHRAGLLHNILPSQSTDLHHSVGTELLSLVYKGIAPGDERQCLPSLDLSCKQLASGLLELAFAFGGLCERLVSLLLNPAVLSTASLGSSQGSVIHFSHGEYFYSLFSETINTELLKNLDLAVLELMQSSVDNTKMVSAVLNGMLDQSFRERANQKHQGLKLATTILQHWKKCDSWWAKDSPLETKMAVLALLAKILQIDSSVSFNTSHGSFPEVFTTYISLLADTKLDLHLKGQAVTLLPFFTSLTGGSLEELRRVLEQLIVAHFPMQSREFPPGTPRFNNYVDCMKKFLDALELSQSPMLLELMTEVLCREQQHVMEELFQSSFRRIARRGSCVTQVGLLESVYEMFRKDDPRLSFTRQSFVDRSLLTLLWHCSLDALREFFSTIVVDAIDVLKSRFTKLNESTFDTQITKKMGYYKILDVMYSRLPKDDVHAKESKINQVFHGSCITEGNELTKTLIKLCYDAFTENMAGENQLLERRRLYHCAAYNCAISVICCVFNELKFYQGFLFSEKPEKNLLIFENLIDLKRRYNFPVEVEVPMERKKKYIEIRKEAREAANGDSDGPSYMSSLSYLADSTLSEEMSQFDFSTGVQSYSYSSQDPRPATGRFRRREQRDPTVHDDVLELEMDELNRHECMAPLTALVKHMHRSLGPPQGEEDSVPRDLPSWMKFLHGKLGNPIVPLNIRLFLAKLVINTEEVFRPYAKHWLSPLLQLAASENNGGEGIHYMVVEIVATILSWTGLATPTGVPKDEVLANRLLNFLMKHVFHPKRAVFRHNLEIIKTLVECWKDCLSIPYRLIFEKFSGKDPNSKDNSVGIQLLGIVMANDLPPYDPQCGIQSSEYFQALVNNMSFVRYKEVYAAAAEVLGLILRYVMERKNILEESLCELVAKQLKQHQNTMEDKFIVCLNKVTKSFPPLADRFMNAVFFLLPKFHGVLKTLCLEVVLCRVEGMTELYFQLKSKDFVQVMRHRDDERQKVCLDIIYKMMPKLKPVELRELLNPVVEFVSHPSTTCREQMYNILMWIHDNYRDPESETDNDSQEIFKLAKDVLIQGLIDENPGLQLIIRNFWSHETRLPSNTLDRLLALNSLYSPKIEVHFLSLATNFLLEMTSMSPDYPNPMFEHPLSECEFQEYTIDSDWRFRSTVLTPMFVETQASQGTLQTRTQEGSLSARWPVAGQIRATQQQHDFTLTQTADGRSSFDWLTGSSTDPLVDHTSPSSDSLLFAHKRSERLQRAPLKSVGPDFGKKRLGLPGDEVDNKVKGAAGRTDLLRLRRRFMRDQEKLSLMYARKGVAEQKREKEIKSELKMKQDAQVVLYRSYRHGDLPDIQIKHSSLITPLQAVAQRDPIIAKQLFSSLFSGILKEMDKFKTLSEKNNITQKLLQDFNRFLNTTFSFFPPFVSCIQDISCQHAALLSLDPAAVSAGCLASLQQPVGIRLLEEALLRLLPAELPAKRVRGKARLPPDVLRWVELAKLYRSIGEYDVLRGIFTSEIGTKQITQSALLAEARSDYSEAAKQYDEALNKQDWVDGEPTEAEKDFWELASLDCYNHLAEWKSLEYCSTASIDSENPPDLNKIWSEPFYQETYLPYMIRSKLKLLLQGEADQSLLTFIDKAMHGELQKAILELHYSQELSLLYLLQDDVDRAKYYIQNGIQSFMQNYSSIDVLLHQSRLTKLQSVQALTEIQEFISFISKQGNLSSQVPLKRLLNTWTNRYPDAKMDPMNIWDDIITNRCFFLSKIEEKLTPLPEDNSMNVDQDGDPSDRMEVQEQEEDISSLIRSCKFSMKMKMIDSARKQNNFSLAMKLLKELHKESKTRDDWLVSWVQSYCRLSHCRSRSQGCSEQVLTVLKTVSLLDENNVSSYLSKNILAFRDQNILLGTTYRIIANALSSEPACLAEIEEDKARRILELSGSSSEDSEKVIAGLYQRAFQHLSEAVQAAEEEAQPPSWSCGPAAGVIDAYMTLADFCDQQLRKEEENASVIDSAELQAYPALVVEKMLKALKLNSNEARLKFPRLLQIIERYPEETLSLMTKEISSVPCWQFISWISHMVALLDKDQAVAVQHSVEEITDNYPQAIVYPFIISSESYSFKDTSTGHKNKEFVARIKSKLDQGGVIQDFINALDQLSNPELLFKDWSNDVRAELAKTPVNKKNIEKMYERMYAALGDPKAPGLGAFRRKFIQTFGKEFDKHFGKGGSKLLRMKLSDFNDITNMLLLKMNKDSKPPGNLKECSPWMSDFKVEFLRNELEIPGQYDGRGKPLPEYHVRIAGFDERVTVMASLRRPKRIIIRGHDEREHPFLVKGGEDLRQDQRVEQLFQVMNGILAQDSACSQRALQLRTYSVVPMTSRLGLIEWLENTVTLKDLLLNTMSQEEKAAYLSDPRAPPCEYKDWLTKMSGKHDVGAYMLMYKGANRTETVTSFRKRESKVPADLLKRAFVRMSTSPEAFLALRSHFASSHALICISHWILGIGDRHLNNFMVAMETGGVIGIDFGHAFGSATQFLPVPELMPFRLTRQFINLMLPMKETGLMYSIMVHALRAFRSDPGLLTNTMDVFVKEPSFDWKNFEQKMLKKGGSWIQEINVAEKNWYPRQKICYAKRKLAGANPAVITCDELLLGHEKAPAFRDYVAVARGSKDHNIRAQEPESGLSEETQVKCLMDQATDPNILGRTWEGWEPWM', 4128, 'P78527; P78528; Q13327; Q13337; Q14175; Q59H99; Q7Z611; Q96SE6;Q9UME3;', 'KD00270', 'Homo sapiens (Human)', 'PRKDC', '#DNA-dependent protein kinase catalytic subunit#DNA-PK catalytic subunit#DNA-PKcs#2.7.11.1#DNPK1#p460', 'BIOMD0000000581,DallePezze2012 - TSC-independent mTORC2 regulation;', 'ENSG00000253729', '-'),
(271, 'A1CZG3', 'E3 ubiquitin ligase complex SCF subunit sconC', 'GO:0051382===GO:0031518', 18141, 'Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes; which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression; probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). {ECO:0000250}.', 'MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE', 158, 'A1CZG3;', 'KD00271', 'Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRR181) (Aspergillus fischerianus)', 'sconC', '#E3 ubiquitin ligase complex SCF subunit sconC#Sulfur controller C#Sulfur metabolite repression control protein C', '-', '-', '4592491'),
(272, 'Q15058', 'Kinesin-like protein KIF14', 'GO:0003777', 186492, 'Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division; cytokinesis and also in cell proliferation and apoptosis (PubMed:24784001; PubMed:16648480). During cytokinesis; targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation; resulting in positive regulation of cyclins; including CCNE1; CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis; regulates the cerebellar; cerebral cortex and olfactory bulb development through regulation of apoptosis; cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading; focal adhesion dynamics; and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302). {ECO:0000250|UniProtKB:L0N7N1; ECO:0000269|PubMed:15843429; ECO:0000269|PubMed:16431929; ECO:0000269|PubMed:16648480; ECO:0000269|PubMed:23209302; ECO:0000269|PubMed:24784001; ECO:0000269|PubMed:24854087}.', 'MSLHSTHNRNNSGDILDIPSSQNSSSLNALTHSSRLKLHLKSDMSECENDDPLLRSAGKVRDINRTYVISASRKTADMPLTPNPVGRLALQRRTTRNKESSLLVSELEDTTEKTAETRLTLQRRAKTDSAEKWKTAEIDSVKMTLNVGGETENNGVSKESRTNVRIVNNAKNSFVASSVPLDEDPQVIEMMADKKYKETFSAPSRANENVALKYSSNRPPIASLSQTEVVRSGHLTTKPTQSKLDIKVLGTGNLYHRSIGKEIAKTSNKFGSLEKRTPTKCTTEHKLTTKCSLPQLKSPAPSILKNRMSNLQVKQRPKSSFLANKQERSAENTILPEEETVVQNTSAGKDPLKVENSQVTVAVRVRPFTKREKIEKASQVVFMSGKEITVEHPDTKQVYNFIYDVSFWSFDECHPHYASQTTVYEKLAAPLLERAFEGFNTCLFAYGQTGSGKSYTMMGFSEEPGIIPRFCEDLFSQVARKQTQEVSYHIEMSFFEVYNEKIHDLLVCKDENGQRKQPLRVREHPVYGPYVEALSMNIVSSYADIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEFVEGEEHDHRITSRINLIDLAGSERCSTAHTNGDRLKEGVSINKSLLTLGKVISALSEQANQRSVFIPYRESVLTWLLKESLGGNSKTAMIATISPAASNIEETLSTLRYANQARLIVNIAKVNEDMNAKLIRELKAEIAKLKAAQRNSRNIDPERYRLCRQEITSLRMKLHQQERDMAEMQRVWKEKFEQAEKRKLQETKELQKAGIMFQMDNHLPNLVNLNEDPQLSEMLLYMIKEGTTTVGKYKPNSSHDIQLSGVLIADDHCTIKNFGGTVSIIPVGEAKTYVNGKHILEITVLRHGDRVILGGDHYFRFNHPVEVQKGKRPSGRDTPISEGPKDFEFAKNELLMAQRSQLEAEIKEAQLKAKEEMMQGIQIAKEMAQQELSSQKAAYESKIKALEAELREESQRKKMQEINNQKANHKIEELEKAKQHLEQEIYVNKKRLEMETLATKQALEDHSIRHARILEALETEKQKIAKEVQILQQNRNNRDKTFTVQTTWSSMKLSMMIQEANAISSKLKTYYVFGRHDISDKSSSDTSIRVRNLKLGISTFWSLEKFESKLAAMKELYESNGSNRGEDAFCDPEDEWEPDITDAPVSSLSRRRSRSLMKNRRISGCLHDIQVHPIKNLHSSHSSGLMDKSSTIYSNSAESFLPGICKELIGSSLDFFGQSYDEERTIADSLINSFLKIYNGLFAISKAHEEQDEESQDNLFSSDRAIQSLTIQTACAFEQLVVLMKHWLSDLLPCTNIARLEDELRQEVKKLGGYLQLFLQGCCLDISSMIKEAQKNAIQIVQQAVKYVGQLAVLKGSKLHFLENGNNKAASVQEEFMDAVCDGVGLGMKILLDSGLEKAKELQHELFRQCTKNEVTKEMKTNAMGLIRSLENIFAESKIKSFRRQVQEENFEYQDFKRMVNRAPEFLKLKHCLEKAIEIIISALKGCHSDINLLQTCVESIRNLASDFYSDFSVPSTSVGSYESRVTHIVHQELESLAKSLLFCFESEESPDLLKPWETYNQNTKEEHQQSKSSGIDGSKNKGVPKRVYELHGSSPAVSSEECTPSRIQWV', 1648, 'Q15058; Q14CI8; Q4G0A5; Q5T1W3;', 'KD00272', 'Homo sapiens (Human)', 'KIF14', '#Kinesin-like protein KIF14 {ECO:0000305}', '-', 'ENSG00000118193', '-'),
(273, 'B2GU58', 'Kinesin-like protein KIF11', 'GO:0003777', 119832, 'Plus end-directed motor protein required for establishing a bipolar spindle. Associates with both interphase and mitotic spindle microtubules. May be involved in nuclear divisions taking place during the development of unfertilized eggs (By similarity). {ECO:0000250}.', 'MSSQNSFMSSKKDDKGKNIQVVVRCRPFNQLERKASSHSVLECDAPRKEVCVRTGGINDKLGKKTYTFDMVFGPAAKQIDVYRSVVCPILDEVIMGYNCTVFAYGQTGTGKTFTMEGERSADEEFTWEQDPLAGIIPRTLHQIFEKLSENGTEFSVKVSLLEIYNEELFDLLSPSPDVGERLQMFDDPRNKRGVIIKGLEEVSVHNKDEVYHILERGAARRKTASTLMNAYSSRSHSVFSVTIHMKETTVDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHIPYRESKLTRILQDSLGGRTKTSIIATVSPASINLEETVSTLEYANRAKNIMNKPEVNQKLTKRALIKEYTEEIERLKRDLATAREKNGVYLSNENYEQLQGKVLSQEEIITEYTEKITAMEEEIKRINELFAENKKELEECTTILQCKEKELEETQKNLHESKEQLAQEAFVVTALETTEKKLHGTANKLLTTVRETSKDVSGLHAKLDRKRAVDQHNTQVHENFAEQMDKRFSVIERSVDEYSVKQQGMLDFYTNSIDNLLGASSAALSVTATAVAKSFTSVQETVSEKVSHSVDEILKQETLSSQAKDDLQKLMAAHRTGLEQALRTDLLPVVTAVLNLNSHLSHCLQNFQAVADKIDSHKEEMNSFFTEHSRSLHRLRLDSGSALSSIQSEYESLKVEIETAQSMHSEGVNNLIGSLQNQLNLLAMETQQNFSGFLAKGGKLQKSVGCLQQDLDSISSDAIEHTSSHHDKFAGQSQDIAVEIRQLAASNMGTLEESSKQCEKLTGSINAISRESQHWCESASQQIDSLLEEQVCYLRTSKKHLQSLQKDVEVGCGASVVEITEHVNAQRQAEEKALTSLVEQVRDDKEMLGEQRLELHEQVQSGQNKVNSYLNEELRNDVPTGTTPQRRDYVYPSLLVRTKPRDVLLEQFRQQQQEYLESISSVISEAVEPPVEQDSLEDEPPVAVNDSVMSEKSCIDLSMVCQENGGVPFFQQKKALRKEKENRANTTLLERSKIMDEAEQSLPKSKLPLRMQN', 1067, 'B2GU58; D0PPG2;', 'KD00273', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'kif11', '#Kinesin-like protein KIF11 {ECO:0000250|UniProtKB:P52732; ECO:0000312|EMBL:AAI66147.1}#Costal2 {ECO:0000250|UniProtKB:P52732; ECO:0000312|EMBL:ABX55790.1}', '-', '-', '548870'),
(274, 'P62205', 'Serine/threonine-protein kinase PLK1', 'GO:0000776', 68121, 'Plays multiple essential roles during mitosis. Phosphorylates the N-terminal domain of cdc25; which leads to cyclin b-cdc2 activation and mitotic entry. Also required for organization of bipolar spindles; and for exit from mitosis. Phosphorylates tpx2 (By similarity). {ECO:0000250}.', 'MAQVAGKKLTVAPEAGKPPGIPGSSSSVKEIPEILVDPRTRRRYLRGRFLGKGGFAKCYEITDLESREVFAGKIVPKTMLLKPHQKDKMTMEIAIQRSLDHRHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRRKAVTEPEARYYLKQTILGCQYLHSNRVIHRDLKLGNLFLNDEMEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLGKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYMRIKKNEYSVPKHINPMATALIQKMLRSEPTSRPTIDDLLNDEFFTTGYIPSRLPTTCLTVPPRFSIAPSTIDQSLRKPLTAINKGQDSPLVEKQSVPAKEEEMQQPESTEPADCYLSEMLQQLTCVNAVKPSERAVIRQEEAEDPASVPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLIMYNDGDSLQYIERNNSESYLNVRSYPAALTKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPFLRTWFRTRSAIILHLSNGTVQINFFQDHTKIILCPLMAAVSYIDEKREFHTYKLSLIQEFGCCKELASRLRYARTMVEKLQSSKSGVAHVKASA', 598, 'P62205;', 'KD00274', 'Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)', 'plk1', '#Serine/threonine-protein kinase PLK1#2.7.11.21#Plx1#Polo-like kinase 1#PLK-1', '-', '-', '407937'),
(275, 'Q3ZC98', 'Nuclear pore complex protein Nup85', 'GO:0000777', 74710, 'Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP98/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2- activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl- inositol 3-kinase-Rac-lammellipodium protrusion cascade (By similarity). {ECO:0000250}.', 'MEEFDGEPTVTWIPGVNSQKKQMCFDWGPGEMLVCETSFNKKEKSEMVAGCPFIHIIRKDIDVYSKILRKLFNESHGIFVGLQRIEEELTGKSRKAQLVRVSKNYRSVIRACMEEMHQFAVADKDSAIGRQFSSQVSILSAVELIWNLCEILFIEVAPAGPLLLYLLDWVRLHVCEVDSLSADVLGSENPSKHESFWNLVTTLVLQGRLDEARQMLSKEADSNPTSAGMCRVLGDLMRTMPILSPGNTQTLTELELRWQHWHEECERHLQDGTFASNPHLESLCKVLLGDDAALLEHKELLSNWYHFLVTRLLYSQPTVKPMDLHLYAQSSLDLFLGGESSPEPLDNILMAAFEFDIHQVIKECSIALSNWWFVAHLTDLLDHCKLLQSHNLYFGSNMREFLLLEYASGLFAHHSLWQLGVDYCDHCPELGRVSLELHIERIPLTTEQKALKVLRVCEQRQMTEQVRSICKVLAMKAVRNNRLGSALSWSIRAKDAAFATLVSDRFLRDYCERGCFSDLDLIDNLGPAMMLSDRLTFLGKYREFHRLYGEKCFVDAASLLLSLMTSQIAPRSFWMTLLTDALPLLEQKQVIFSAEQTYELLRCLEDLTSGRPLCGEPDAQQLQDDDIETTKVEILRLALARNLARSIIKEGSLEGS', 656, 'Q3ZC98; A7E3X3;', 'KD00275', 'Bos taurus (Bovine)', 'NUP85', '#Nuclear pore complex protein Nup85#85 kDa nucleoporin#Nucleoporin Nup85', '-', '-', '510540'),
(276, 'Q2UPH5', 'Probable kinetochore protein spc25', 'GO:0000778===GO:0051455===GO:0031617', 30709, 'Acts as a component of the essential kinetochore- associated NDC80 complex; which is required for chromosome segregation and spindle checkpoint activity. {ECO:0000250}.', 'MASSFEPSLSTSGMRPPLTSADAPSMADSLPSINFGFEDLRNRMAQFTARFDAFIEKGRKQILEERNQFKIGLAELQEDQRMKQRDIEILNLKSQTHDQTIQKEAAEAAEMHGTIASVTMERDSRLAKRDRLKQQINETQKAINQKLEAQKAHARHLDAQARLNIPELEFWQDYLCLRIEGAGREDRLKFIFSHLLEKDWEAEAWFELGTSSRDYDVFHTRPKVDRDALNGELDILNEDRDFGAFLKRMRRLLVEKMQQKRPTI', 264, 'Q2UPH5;', 'KD00276', 'Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)', 'spc25', '#Probable kinetochore protein spc25', '-', '-', '5990487'),
(277, 'Q9LPC6', 'Armadillo repeat-containing kinesin-like protein 2', 'GO:0003777', 98423, 'Involved in the control of epidermal-cell morphogenesis in roots and helical growth of roots by promoting microtubule depolymerization and limiting the accumulation of endoplasmic microtubules. Seems to be involved in the control of cell-file rotation (or twisting). {ECO:0000269|PubMed:17971038}.', 'MAMASSRNGAVRGSMRPVSGANSSNLRSSSFKSRIPSSAPAPRRSSSASIGAADNGVPGRVRVAVRLRPRNADESVADADFADCVELQPELKRLKLRKNNWDTETYEFDEVLTEAASQKRVYEVVAKPVVESVLEGYNGTVMAYGQTGTGKTFTLGRLGDEDTAARGIMVRSMEDIIGGTSLDTDSISVSYLQLYMETIQDLLDPTNDNIAIVEDPRTGDVSLPGATHVEIRNQQNFLELLQLGETHRVAANTKLNTESSRSHAILMVHVKRSVVENEFPVSNEMESSSHFVRPSKPLVRRSKLVLVDLAGSERVHKSGSEGHMLEEAKSINLSLSALGKCINAIAENSPHVPLRDSKLTRLLRDSFGGTARTSLIVTIGPSPRHRGETTSTILFGQRAMKVENMLKIKEEFDYKSLSKKLEVQLDKVIAENERQLKAFDDDVERINRQAQNRISEVEKNFAEALEKEKLKCQMEYMESVKKLEEKLISNQRNHENGKRNGEVNGVVTASEFTRLKESLENEMKLRKSAEEEVSKVKSQSTLKTRSGEGEDAGITRLQKLLEDEALQKKKLEEEVTILRSQLVQLTFEADQMRRCLDRGAPGNSYSGTDSLPSRHSQARESVNGQKAPFATLCEQVGLQKILQLLESDDANIRIHAVKVVANLAAEEANQEKIVEAGGLTSLLMLLRSYEDETVRRVAAGAIANLAMNEVSQQLIVDQGGISLLSLTAADAEDPQTLRMVAGAIANLCGNDKLQARLWSDGGIKALLGMVRCGHPDVLAQVARGIANFAKCESRATTQGVKSGRSLLIEDGALPWIVQHANDEAAPIRRHIELALCHLAQHEVNAKEMISGGALWELVRISKECSREDIRSLAHRTLSSSPVFRSEIRRLGIQF', 894, 'Q9LPC6; A9CP40; Q0WMY6;', 'KD00277', 'Arabidopsis thaliana (Mouse-ear cress)', 'ARK2', '#Armadillo repeat-containing kinesin-like protein 2', '-', '-', '839306'),
(278, 'Q804H7', 'Baculoviral IAP repeat-containing protein 5.2-B', 'GO:0000777===GO:0032133', 18341, 'Does not appear to exhibit anti-apoptotic activity. Plays a role in increasing blood vessel size during development (By similarity). 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. {ECO:0000250|UniProtKB:Q50L39; ECO:0000269|PubMed:15853809; ECO:0000269|PubMed:16344111; ECO:0000269|PubMed:17199039}.', 'MLSISPIVSLRRCDNEPSMPDEWRLYNLATRLRTFSNWPFTEDCACTPERMAEAGFVHCPTDNSPDVVKCFFCLKELEGWQPEDDPMDEHKKHSPSCLFIALKKKAEELTLSEFLKLDLEHMKIKMQKQMNLHIERFQAKANEVRGHLEKLDADETQ', 157, 'Q804H7; B7ZQC9;', 'KD00278', 'Xenopus laevis (African clawed frog)', 'birc5.2-b', '#Baculoviral IAP repeat-containing protein 5.2-B#Survivin in Xenopus {ECO:0000303|PubMed:12535669}#SIX {ECO:0000312|EMBL:AAO20085.1}#Survivin2-B {ECO:0000303|PubMed:15853809}#XSurvivin2B {ECO:0000312|EMBL:BAE02679.1}', '-', '-', '398454'),
(279, 'Q9VHP9', 'Cenp-C; isoform AFI18815p1', 'c;k', 157699, '', 'MSKPQNNDTLELDDILSQPVKDKERFAAFMMRKLAENKPAQNDNLFGNFKLDFDLDFEVPLIKKSQAKPKSKLPEVQPLGELVSKNSAATEKVNEPPVDQAPNENVPPRRSPTLSPNNRRSMRRSGNVPGSDKLRRHAIRRRSRSCGRQLLPEFEETVNLTRSISSPVNFLPEISSTPCTEKQKEEVAKNTTRVETDKPAEKPMELSQEPEPENPLQTKVTSPARNPILAAEIEQICKERQSSFHKNVLQLDYSGRAPYSRPPTPSSPSVAGLRRTYTMEKGPAPGQLLLSPSHRYDTPSKMPVVKAKRFNQELMVPDTPERQSHDPAWQSEPQPEFVVPETQPQDLGELVQTLSRSAISPIVVINTSNSNRSVRRDAVAMKSVPTSPVTALSSPPIAPSPRRSAAASPQKSIAQLPRVEENMDAIMTDDESDEHPSTVPLNLAPSGGNTTRQRRLRSSNRARATIESQESSMRLLNLHKSVNAKKSKPRKTAIPLNKAPSAPINGEQFARELTRMSNYEILDLRKRNSLNEIYPLNGHRNHRSEKLILEEEIQRELLRRNLMDEAEGLPKQQSSDDSNEDYIPVPPKTQSLRTKSNDRSQGRGRPRSTRRDLPMTTELVNYLGLSQTLETRRKSSKDGKRCLYTKGSSDHEDNDSLSPVKLPRLSKSIQIVPPPPVSLRYSQSLQNLPCSGKFDFDNVVMAAPPDFHDSVNSDAIEIAPPPPEYVVNTRGRSTSGRKSNKNDLVLPPPGYEGGQEEEHDERPSQPRCTAKELQQSTQNGRRAMENELVPPPIEYVEEENRNNEQSRRSTKNGNLVDRNTHNAVEYCEPPEPPEYDDSDHGQASILRRSGKKLQHSKQSVQKSNKEQIIAPSYENNEDYDSDEEPIYNEEYGKEESQNKNVTRRKSDKDEMASHTLECIEGPDPNWNSSCNKQNRNHQNASKSKENDKLANRSSKSQKLSNPRQNAVGTEKSVALSNRGEECTEKSSDVMESLRVNTPTPPIDQNSDDVPSRNPSPSRTLLSDDVPSTSRAALEFLQRSQNMSKSRPPDESSADVVFKKPLAPAPRAKSKKGKSEVDKLKLAKMPVEAEELNTTGIRRSKRGQVPLQMSWCHTMDPSKFNFMSGFIEPRSKNSKTKKGNLSKAKKASATKPKPTVEKNLPDNRGPLCSSTPRISEKLPGAIPHSESLGLSTLTWEETEVQAEAEKVPKKRGRPKKAVGGVQTDTEAEPEPEPEPMISSVAPLTSDQEEPDVPDEQAPYTEAALGPVVFSTPLRDEQEEASTKLMQWLRGVGDAPPSASMSDENASVSSANELIFCQVDGIDYAFYNTKEKAMLGYMRFKPYQKRSMKQAKVHPLKLLVQFGEFNVETLAVGEEKEVHSVLRVGDMIEIDRGTRYSIQNAIDKVSVLMCIRS', 1411, 'Q9VHP9; Q9VHP8;', 'KD00279', 'Drosophila melanogaster (Fruit fly)', 'Cenp-C', '#Cenp-C; isoform A {ECO:0000313|EMBL:AAF54252.4}#FI18815p1 {ECO:0000313|EMBL:AFC88881.1}', '-', '-', '41014'),
(280, 'Q8NCD3', 'Holliday junction recognition protein', 'GO:0000777', 83539, '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. {ECO:0000269|PubMed:19410544; ECO:0000269|PubMed:19410545}.', 'MLGTLRAMEGEDVEDDQLLQKLRASRRRFQRRMQRLIEKYNQPFEDTPVVQMATLTYETPQGLRIWGGRLIKERNEGEIQDSSMKPADRTDGSVQAAAWGPELPSHRTVLGADSKSGEVDATSDQEESVAWALAPAVPQSPLKNELRRKYLTQVDILLQGAEYFECAGNRAGRDVRVTPLPSLASPAVPAPGYCSRISRKSPGDPAKPASSPREWDPLHPSSTDMALVPRNDSLSLQETSSSSFLSSQPFEDDDICNVTISDLYAGMLHSMSRLLSTKPSSIISTKTFIMQNWNSRRRHRYKSRMNKTYCKGARRSQRSSKENFIPCSEPVKGTGALRDCKNVLDVSCRKTGLKLEKAFLEVNRPQIHKLDPSWKERKVTPSKYSSLIYFDSSATYNLDEENRFRTLKWLISPVKIVSRPTIRQGHGENRQREIEIRFDQLHREYCLSPRNQPRRMCLPDSWAMNMYRGGPASPGGLQGLETRRLSLPSSKAKAKSLSEAFENLGKRSLEAGRCLPKSDSSSSLPKTNPTHSATRPQQTSDLHVQGNSSGIFRKSVSPSKTLSVPDKEVPGHGRNRYDEIKEEFDKLHQKYCLKSPGQMTVPLCIGVSTDKASMEVRYQTEGFLGKLNPDPHFQGFQKLPSSPLGCRKSLLGSTAIEAPSSTCVARAITRDGTRDHQFPAKRPRLSEPQGSGRQGNSLGASDGVDNTVRPGDQGSSSQPNSEERGENTSYRMEEKSDFMLEKLETKSV', 748, 'Q8NCD3; A8IRH5; B4DWR0; B4DZV4; Q9BUT2; Q9NSL8;', 'KD00280', 'Homo sapiens (Human)', 'HJURP', '#Holliday junction recognition protein#14-3-3-associated AKT substrate#Fetal liver-expressing gene 1 protein#Up-regulated in lung cancer 9', '-', 'ENSG00000123485', '-'),
(281, 'P52948', 'Nuclear pore complex protein Nup98-Nup96', 'k', 197579, 'Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Nup98 and Nup96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. {ECO:0000269|PubMed:15229283}.', 'MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFGFGTSTGTANTLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGLFSSSTTNSGFAYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTQNTGFSFGNTSTIGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQTNTGFGAVGSTLFGNNKLTTFGSSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNTSGNSIFGSKPAPGTLGTGLGAGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTTTATLGFGAPQAPVALTDPNASAAQQAVLQQHINSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNRDSENLASPSEYPENGERFSFLSKPVDENHQQDGDEDSLVSHFYTNPIAKPIPQTPESAGNKHSNSNSVDDTIVALNMRAALRNGLEGSSEETSFHDESLQDDREEIENNSYHMHPAGIILTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVVVYLDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHFSKYGLQDSDEEEEEHPSKTSTKKLKTAPLPPASQTTPLQMALNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVLDTMLEESMPEDQEPVSASTHIASSLGINPHVLQIMKASLLTDEEDVDMALDQRFSRLPSKADTSQEICSPRLPISASHSSKTRSLVGGLLQSKFTSGAFLSPSVSVQECRTPRAASLMNIPSTSSWSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPREKSVTYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLNGSHELENHQIADSMEFGFLPNPVAVKPLTESPFKVHLEKLSLRQRKPDEDMKLYQTPLELKLKHSTVHVDELCPLIVPNLGVAVIHDYADWVKEASGDLPEAQIVKHWSLTWTLCEALWGHLKELDSQLNEPREYIQILERRRAFSRWLSCTATPQIEEEVSLTQKNSPVEAVFSYLTGKRISEACSLAQQSGDHRLALLLSQFVGSQSVRELLTMQLVDWHQLQADSFIQDERLRIFALLAGKPVWQLSEKKQINVCSQLDWKRSLAIHLWYLLPPTASISRALSMYEEAFQNTSDSDRYACSPLPSYLEGSGCVIAEEQNSQTPLRDVCFHLLKLYSDRHYDLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSAQCEGVLQASYAGQLESEGLWEWAIFVLLHIDNSGIREKAVRELLTRHCQLLETPESWAKETFLTQKLRVPAKWIHEAKAVRAHMESDKHLEALCLFKAEHWNRCHKLIIRHLASDAIINENYDYLKGFLEDLAPPERSSLIQDWETSGLVYLDYIRVIEMLRHIQQVDCSGNDLEQLHIKVTSLCSRIEQIQCYSAKDRLAQSDMAKRVANLLRVVLSLHHPPDRTSDSTPDPQRVPLRLLAPHIGRLPMPEDYAMDELRSLTQSYLRELAVGSL', 1817, 'P52948; Q8IUT2; Q8WYB0; Q96E54; Q9H3Q4; Q9NT02; Q9UF57; Q9UHX0;Q9Y6J4; Q9Y6J5;', 'KD00281', 'Homo sapiens (Human)', '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', '-', 'ENSG00000206535', '-');
