ID KI20A_HUMAN Reviewed; 890 AA. AC O95235; B4DL79; D3DQB6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=Kinesin-like protein KIF20A; DE AltName: Full=GG10_2; DE AltName: Full=Mitotic kinesin-like protein 2; DE Short=MKlp2; DE AltName: Full=Rab6-interacting kinesin-like protein; DE AltName: Full=Rabkinesin-6; GN Name=KIF20A; Synonyms=MKLP2, RAB6KIFL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Endothelial cell; RX PubMed=10233894; RA Horrevoets A.J.G., Fontijn R.D., van Zonneveld A.J., de Vries C.J.M., RA ten Cate J.W., Pannekoek H.; RT "Vascular endothelial genes that are responsive to tumor necrosis factor- RT alpha in vitro are expressed in atherosclerotic lesions, including RT inhibitor of apoptosis protein-1, stannin, and two novel genes."; RL Blood 93:3418-3431(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10806357; DOI=10.1016/s0378-1119(00)00135-9; RA Lai F., Fernald A.A., Zhao N., Le Beau M.M.; RT "cDNA cloning, expression pattern, genomic structure and chromosomal RT location of RAB6KIFL, a human kinesin-like gene."; RL Gene 248:117-125(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP SUBCELLULAR LOCATION, INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-528; RP SER-662 AND SER-668, MUTAGENESIS OF SER-528, AND FUNCTION. RX PubMed=12939256; DOI=10.1083/jcb.200306009; RA Neef R., Preisinger C., Sutcliffe J., Kopajtich R., Nigg E.A., Mayer T.U., RA Barr F.A.; RT "Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is RT required for cytokinesis."; RL J. Cell Biol. 162:863-875(2003). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-532; THR-857 AND RP SER-867, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-7; SER-14; SER-21; SER-532 AND SER-825, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532; SER-685; SER-878 AND RP SER-883, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP VARIANT RCM6 TRP-182, INVOLVEMENT IN RCM6, CHARACTERIZATION OF VARIANT RCM6 RP TRP-182, AND SUBCELLULAR LOCATION. RX PubMed=29357359; DOI=10.1371/journal.pgen.1007138; RA Louw J.J., Nunes Bastos R., Chen X., Verdood C., Corveleyn A., Jia Y., RA Breckpot J., Gewillig M., Peeters H., Santoro M.M., Barr F., Devriendt K.; RT "Compound heterozygous loss-of-function mutations in KIF20A are associated RT with a novel lethal congenital cardiomyopathy in two siblings."; RL PLoS Genet. 14:e1007138-e1007138(2018). CC -!- FUNCTION: Mitotic kinesin required for chromosome passenger complex CC (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved CC in recruitment of PLK1 to the central spindle. Interacts with guanosine CC triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor CC required for the retrograde RAB6 regulated transport of Golgi membranes CC and associated vesicles along microtubules. Has a microtubule plus end- CC directed motility. {ECO:0000269|PubMed:12939256}. CC -!- INTERACTION: CC O95235; Q7L5A3: ATOSB; NbExp=4; IntAct=EBI-2551319, EBI-745689; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000269|PubMed:12939256, CC ECO:0000269|PubMed:29357359}. Note=Localizes to the spindle midzone CC during anaphase and telophase. {ECO:0000269|PubMed:29357359}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95235-1; Sequence=Displayed; CC Name=2; CC IsoId=O95235-2; Sequence=VSP_056007; CC -!- PTM: Phosphorylated by PLK1 at Ser-528 during mitosis, creating a CC docking site for PLK1 and recruiting PLK1 at central spindle. CC {ECO:0000269|PubMed:12939256}. CC -!- DISEASE: Cardiomyopathy, familial restrictive 6 (RCM6) [MIM:619433]: A CC heart disorder characterized by impaired filling of the ventricles with CC reduced diastolic volume, in the presence of normal or near normal wall CC thickness and systolic function. RCM6 is an autosomal recessive, severe CC form characterized by prenatal onset, irreversible heart failure and CC early death. {ECO:0000269|PubMed:29357359}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF070672; AAC83230.1; -; mRNA. DR EMBL; AF153329; AAD37806.1; -; mRNA. DR EMBL; AK296879; BAG59441.1; -; mRNA. DR EMBL; AC106752; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC109442; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW62157.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62158.1; -; Genomic_DNA. DR EMBL; BC012999; AAH12999.1; -; mRNA. DR CCDS; CCDS4199.1; -. [O95235-1] DR RefSeq; NP_005724.1; NM_005733.2. [O95235-1] DR PDB; 6YIP; X-ray; 1.43 A; A/B=596-668. DR PDBsum; 6YIP; -. DR AlphaFoldDB; O95235; -. DR SMR; O95235; -. DR BioGRID; 115418; 1060. DR IntAct; O95235; 45. DR MINT; O95235; -. DR STRING; 9606.ENSP00000378356; -. DR BindingDB; O95235; -. DR ChEMBL; CHEMBL2021753; -. DR iPTMnet; O95235; -. DR PhosphoSitePlus; O95235; -. DR SwissPalm; O95235; -. DR BioMuta; KIF20A; -. DR EPD; O95235; -. DR jPOST; O95235; -. DR MassIVE; O95235; -. DR MaxQB; O95235; -. DR PaxDb; 9606-ENSP00000378356; -. DR PeptideAtlas; O95235; -. DR ProteomicsDB; 4513; -. DR ProteomicsDB; 50732; -. [O95235-1] DR Pumba; O95235; -. DR Antibodypedia; 26611; 370 antibodies from 28 providers. DR DNASU; 10112; -. DR Ensembl; ENST00000394894.8; ENSP00000378356.3; ENSG00000112984.12. [O95235-1] DR Ensembl; ENST00000508792.5; ENSP00000420880.1; ENSG00000112984.12. [O95235-2] DR GeneID; 10112; -. DR KEGG; hsa:10112; -. DR MANE-Select; ENST00000394894.8; ENSP00000378356.3; NM_005733.3; NP_005724.1. DR UCSC; uc003lcj.4; human. [O95235-1] DR AGR; HGNC:9787; -. DR CTD; 10112; -. DR DisGeNET; 10112; -. DR GeneCards; KIF20A; -. DR HGNC; HGNC:9787; KIF20A. DR HPA; ENSG00000112984; Tissue enhanced (bone marrow, lymphoid tissue, testis). DR MalaCards; KIF20A; -. DR MIM; 605664; gene. DR MIM; 619433; phenotype. DR neXtProt; NX_O95235; -. DR OpenTargets; ENSG00000112984; -. DR Orphanet; 75249; Familial isolated restrictive cardiomyopathy. DR PharmGKB; PA34149; -. DR VEuPathDB; HostDB:ENSG00000112984; -. DR eggNOG; KOG0247; Eukaryota. DR GeneTree; ENSGT00940000156931; -. DR HOGENOM; CLU_001485_2_5_1; -. DR InParanoid; O95235; -. DR OMA; NRHPQKA; -. DR OrthoDB; 5403873at2759; -. DR PhylomeDB; O95235; -. DR TreeFam; TF105232; -. DR BRENDA; 5.6.1.3; 2681. DR PathwayCommons; O95235; -. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-68884; Mitotic Telophase/Cytokinesis. DR Reactome; R-HSA-983189; Kinesins. DR SignaLink; O95235; -. DR SIGNOR; O95235; -. DR BioGRID-ORCS; 10112; 303 hits in 1170 CRISPR screens. DR ChiTaRS; KIF20A; human. DR GeneWiki; KIF20A; -. DR GenomeRNAi; 10112; -. DR Pharos; O95235; Tchem. DR PRO; PR:O95235; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O95235; Protein. DR Bgee; ENSG00000112984; Expressed in ventricular zone and 125 other cell types or tissues. DR ExpressionAtlas; O95235; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0045171; C:intercellular bridge; IDA:HPA. DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB. DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central. DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB. DR CDD; cd01368; KISc_KIF23_like; 1. DR CDD; cd21787; RBD_KIF20A; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR InterPro; IPR027640; Kinesin-like_fam. DR InterPro; IPR019821; Kinesin_motor_CS. DR InterPro; IPR001752; Kinesin_motor_dom. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR24115:SF352; KINESIN-LIKE PROTEIN KIF20A; 1. DR PANTHER; PTHR24115; KINESIN-RELATED; 1. DR Pfam; PF00225; Kinesin; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR Genevisible; O95235; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cardiomyopathy; Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; KW Golgi apparatus; Microtubule; Motor protein; Nucleotide-binding; KW Phosphoprotein; Protein transport; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:20068231" FT CHAIN 2..890 FT /note="Kinesin-like protein KIF20A" FT /id="PRO_0000125460" FT DOMAIN 64..507 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT REGION 763..890 FT /note="Globular" FT /evidence="ECO:0000255" FT REGION 832..865 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 611..762 FT /evidence="ECO:0000255" FT BINDING 160..167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 528 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000269|PubMed:12939256, FT ECO:0007744|PubMed:18669648" FT MOD_RES 532 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 662 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12939256" FT MOD_RES 668 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12939256" FT MOD_RES 685 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 825 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 857 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 867 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 878 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 883 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 65..82 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056007" FT VARIANT 63 FT /note="E -> K (in dbSNP:rs3734116)" FT /id="VAR_049704" FT VARIANT 182 FT /note="R -> W (in RCM6; loss-of-function variant unable to FT rescue cardiac defects in zebrafish morphants; results in FT greatly reduced microtubule activated motor activity; does FT not localize to the spindle midzone; dbSNP:rs771130761)" FT /evidence="ECO:0000269|PubMed:29357359" FT /id="VAR_086018" FT VARIANT 839 FT /note="P -> L (in dbSNP:rs3172747)" FT /id="VAR_049705" FT MUTAGEN 528 FT /note="S->A: Impairs phosphorylation by PLK1 and FT recruitment of PLK1 to the spindle." FT /evidence="ECO:0000269|PubMed:12939256" FT HELIX 596..663 FT /evidence="ECO:0007829|PDB:6YIP" SQ SEQUENCE 890 AA; 100278 MW; 6620264615496051 CRC64; MSQGILSPPA GLLSDDDVVV SPMFESTAAD LGSVVRKNLL SDCSVVSTSL EDKQQVPSED SMEKVKVYLR VRPLLPSELE RQEDQGCVRI ENVETLVLQA PKDSFALKSN ERGIGQATHR FTFSQIFGPE VGQASFFNLT VKEMVKDVLK GQNWLIYTYG VTNSGKTHTI QGTIKDGGIL PRSLALIFNS LQGQLHPTPD LKPLLSNEVI WLDSKQIRQE EMKKLSLLNG GLQEEELSTS LKRSVYIESR IGTSTSFDSG IAGLSSISQC TSSSQLDETS HRWAQPDTAP LPVPANIRFS IWISFFEIYN ELLYDLLEPP SQQRKRQTLR LCEDQNGNPY VKDLNWIHVQ DAEEAWKLLK VGRKNQSFAS THLNQNSSRS HSIFSIRILH LQGEGDIVPK ISELSLCDLA GSERCKDQKS GERLKEAGNI NTSLHTLGRC IAALRQNQQN RSKQNLVPFR DSKLTRVFQG FFTGRGRSCM IVNVNPCAST YDETLHVAKF SAIASQLVHA PPMQLGFPSL HSFIKEHSLQ VSPSLEKGAK ADTGLDDDIE NEADISMYGK EELLQVVEAM KTLLLKERQE KLQLEMHLRD EICNEMVEQM QQREQWCSEH LDTQKELLEE MYEEKLNILK ESLTSFYQEE IQERDEKIEE LEALLQEARQ QSVAHQQSGS ELALRRSQRL AASASTQQLQ EVKAKLQQCK AELNSTTEEL HKYQKMLEPP PSAKPFTIDV DKKLEEGQKN IRLLRTELQK LGESLQSAER ACCHSTGAGK LRQALTTCDD ILIKQDQTLA ELQNNMVLVK LDLRKKAACI AEQYHTVLKL QGQVSAKKRL GTNQENQQPN QQPPGKKPFL RNLLPRTPTC QSSTDCSPYA RILRSRRSPL LKSGPFGKKY //