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KI20A_HUMAN
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   03-AUG-2022, entry version 188.
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: FAM214B; 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}.
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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; 1041.
DR   IntAct; O95235; 43.
DR   MINT; O95235; -.
DR   STRING; 9606.ENSP00000378356; -.
DR   BindingDB; O95235; -.
DR   ChEMBL; CHEMBL2021753; -.
DR   iPTMnet; O95235; -.
DR   PhosphoSitePlus; O95235; -.
DR   BioMuta; KIF20A; -.
DR   EPD; O95235; -.
DR   jPOST; O95235; -.
DR   MassIVE; O95235; -.
DR   MaxQB; O95235; -.
DR   PaxDb; O95235; -.
DR   PeptideAtlas; O95235; -.
DR   PRIDE; O95235; -.
DR   ProteomicsDB; 4513; -.
DR   ProteomicsDB; 50732; -. [O95235-1]
DR   Antibodypedia; 26611; 322 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   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; DVREECW; -.
DR   OrthoDB; 314538at2759; -.
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; 281 hits in 1090 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 124 other tissues.
DR   ExpressionAtlas; O95235; baseline and differential.
DR   Genevisible; O95235; HS.
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:0005634; C:nucleus; IBA:GO_Central.
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   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR027326; KIF20A.
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; PTHR24115; 1.
DR   PANTHER; PTHR24115:SF352; PTHR24115:SF352; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
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)"
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
 
 
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