KIF2A_HUMAN
ID KIF2A_HUMAN Reviewed; 706 AA.
AC O00139; A5YM42; A5YM54; B4DY54; D3DW97; E9PB70; Q7Z5I3; Q8N5Q7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Kinesin-like protein KIF2A;
DE AltName: Full=Kinesin-2;
DE Short=hK2;
GN Name=KIF2A; Synonyms=KIF2, KNS2;
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] (ISOFORMS 1 AND 2).
RX PubMed=9177777; DOI=10.1006/geno.1997.4720;
RA Debernardi S., Fontanella E., de Gregorio L., Pierotti M.A., Delia D.;
RT "Identification of a novel human kinesin-related gene (HK2) by the cDNA
RT differential display technique.";
RL Genomics 42:67-73(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Fetal brain, and Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 60-706 (ISOFORMS 1/3).
RC TISSUE=Testis;
RA Sha J.H., Zhou Z.M., Li J.M.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=15843429; DOI=10.1091/mbc.e05-02-0167;
RA Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B.,
RA Abraham R.T., Jiang W.;
RT "Functional analysis of human microtubule-based motor proteins, the
RT kinesins and dyneins, in mitosis/cytokinesis using RNA interference.";
RL Mol. Biol. Cell 16:3187-3199(2005).
RN [9]
RP FUNCTION.
RX PubMed=17538014; DOI=10.1091/mbc.e07-02-0110;
RA Manning A.L., Ganem N.J., Bakhoum S.F., Wagenbach M., Wordeman L.,
RA Compton D.A.;
RT "The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles
RT during mitosis in human cells.";
RL Mol. Biol. Cell 18:2970-2979(2007).
RN [10]
RP FUNCTION, INTERACTION WITH PSRC1, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=18411309; DOI=10.1083/jcb.200711032;
RA Jang C.Y., Wong J., Coppinger J.A., Seki A., Yates J.R. III, Fang G.;
RT "DDA3 recruits microtubule depolymerase Kif2a to spindle poles and controls
RT spindle dynamics and mitotic chromosome movement.";
RL J. Cell Biol. 181:255-267(2008).
RN [11]
RP INTERACTION WITH PLK1 AND AURKA, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19351716; DOI=10.1242/jcs.044321;
RA Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.;
RT "Plk1 and Aurora A regulate the depolymerase activity and the cellular
RT localization of Kif2a.";
RL J. Cell Sci. 122:1334-1341(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND THR-78, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-97; SER-100; SER-135 AND
RP SER-140, 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 153-553 IN COMPLEX WITH ADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the human KIF2 motor domain in complex with ADP.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [16]
RP VARIANTS CDCBM3 ASN-317 AND ASP-321, AND CHARACTERIZATION OF VARIANTS
RP CDCBM3 ASN-317 AND ASP-321.
RX PubMed=23603762; DOI=10.1038/ng.2613;
RA Poirier K., Lebrun N., Broix L., Tian G., Saillour Y., Boscheron C.,
RA Parrini E., Valence S., Pierre B.S., Oger M., Lacombe D., Genevieve D.,
RA Fontana E., Darra F., Cances C., Barth M., Bonneau D., Bernadina B.D.,
RA N'guyen S., Gitiaux C., Parent P., des Portes V., Pedespan J.M., Legrez V.,
RA Castelnau-Ptakine L., Nitschke P., Hieu T., Masson C., Zelenika D.,
RA Andrieux A., Francis F., Guerrini R., Cowan N.J., Bahi-Buisson N.,
RA Chelly J.;
RT "Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of
RT cortical development and microcephaly.";
RL Nat. Genet. 45:639-647(2013).
CC -!- FUNCTION: Plus end-directed microtubule-dependent motor required for
CC normal brain development. May regulate microtubule dynamics during
CC axonal growth. Required for normal progression through mitosis.
CC Required for normal congress of chromosomes at the metaphase plate.
CC Required for normal spindle dynamics during mitosis. Promotes spindle
CC turnover. Implicated in formation of bipolar mitotic spindles. Has
CC microtubule depolymerization activity. {ECO:0000269|PubMed:15843429,
CC ECO:0000269|PubMed:17538014, ECO:0000269|PubMed:18411309}.
CC -!- SUBUNIT: Interacts with AURKA, PSRC1 and PLK1.
CC {ECO:0000269|PubMed:18411309, ECO:0000269|PubMed:19351716,
CC ECO:0000269|Ref.15}.
CC -!- INTERACTION:
CC O00139; Q8NE31: FAM13C; NbExp=4; IntAct=EBI-2692369, EBI-751248;
CC O00139; Q659C4: LARP1B; NbExp=3; IntAct=EBI-2692369, EBI-3940258;
CC O00139; Q96EL3: MRPL53; NbExp=3; IntAct=EBI-2692369, EBI-2513715;
CC O00139-1; P25791-3: LMO2; NbExp=3; IntAct=EBI-12197879, EBI-11959475;
CC O00139-1; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-12197879, EBI-11742507;
CC O00139-1; Q96EL3: MRPL53; NbExp=3; IntAct=EBI-12197879, EBI-2513715;
CC O00139-1; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12197879, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Cytoplasm, cytoskeleton,
CC spindle pole. Cytoplasm, cytoskeleton, spindle. Note=Localized to the
CC spindle microtubules and spindle poles from prophase to metaphase.
CC Efficient targeting to spindle microtubules and spindle poles requires
CC the kinase activity of PLK1. Recruited to mitotic spindles by
CC interaction with PSRC1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=3;
CC IsoId=O00139-3; Sequence=Displayed;
CC Name=1; Synonyms=HK2;
CC IsoId=O00139-1; Sequence=VSP_028374;
CC Name=2; Synonyms=HK2s;
CC IsoId=O00139-2; Sequence=VSP_028374, VSP_028375;
CC Name=4;
CC IsoId=O00139-4; Sequence=VSP_028376;
CC Name=5;
CC IsoId=O00139-5; Sequence=VSP_047373;
CC -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 3
CC (CDCBM3) [MIM:615411]: A disorder of aberrant neuronal migration and
CC disturbed axonal guidance. Clinical features include early-onset
CC epilepsy, and various malformations of cortical development such as
CC agyria, posterior or frontal pachygyria, subcortical band heterotopia,
CC and thin corpus callosum. {ECO:0000269|PubMed:23603762}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: HeLa cells lacking KIF2A show asymmetric or monopolar
CC mitotic spindles. Osteosarcoma cells (U2OS) lacking KIF2A or KIF2B show
CC disorganised or monopolar mitotic spindles.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP84320.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y08319; CAA69621.1; -; mRNA.
DR EMBL; AK302270; BAG63616.1; -; mRNA.
DR EMBL; EF560716; ABQ59026.1; -; mRNA.
DR EMBL; EF560728; ABQ59038.1; -; mRNA.
DR EMBL; AC016637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471137; EAW51388.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51390.1; -; Genomic_DNA.
DR EMBL; BC031828; AAH31828.1; -; mRNA.
DR EMBL; AY317140; AAP84320.1; ALT_INIT; mRNA.
DR CCDS; CCDS3980.2; -. [O00139-3]
DR CCDS; CCDS47216.1; -. [O00139-4]
DR CCDS; CCDS58949.1; -. [O00139-1]
DR RefSeq; NP_001091981.1; NM_001098511.2. [O00139-4]
DR RefSeq; NP_001230881.1; NM_001243952.1. [O00139-1]
DR RefSeq; NP_004511.2; NM_004520.4. [O00139-3]
DR PDB; 2GRY; X-ray; 2.35 A; A=153-553.
DR PDB; 6BBN; X-ray; 3.51 A; E=153-553.
DR PDBsum; 2GRY; -.
DR PDBsum; 6BBN; -.
DR AlphaFoldDB; O00139; -.
DR SASBDB; O00139; -.
DR SMR; O00139; -.
DR BioGRID; 109997; 186.
DR DIP; DIP-56112N; -.
DR IntAct; O00139; 69.
DR MINT; O00139; -.
DR STRING; 9606.ENSP00000385000; -.
DR GlyGen; O00139; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00139; -.
DR PhosphoSitePlus; O00139; -.
DR BioMuta; KIF2A; -.
DR EPD; O00139; -.
DR jPOST; O00139; -.
DR MassIVE; O00139; -.
DR MaxQB; O00139; -.
DR PeptideAtlas; O00139; -.
DR PRIDE; O00139; -.
DR ProteomicsDB; 19159; -.
DR ProteomicsDB; 47722; -. [O00139-3]
DR ProteomicsDB; 47723; -. [O00139-1]
DR ProteomicsDB; 47724; -. [O00139-2]
DR ProteomicsDB; 47725; -. [O00139-4]
DR Antibodypedia; 1353; 217 antibodies from 28 providers.
DR DNASU; 3796; -.
DR Ensembl; ENST00000381103.7; ENSP00000370493.3; ENSG00000068796.19. [O00139-1]
DR Ensembl; ENST00000401507.7; ENSP00000385622.3; ENSG00000068796.19. [O00139-3]
DR Ensembl; ENST00000407818.8; ENSP00000385000.3; ENSG00000068796.19. [O00139-4]
DR Ensembl; ENST00000506857.5; ENSP00000423772.1; ENSG00000068796.19. [O00139-2]
DR Ensembl; ENST00000676413.1; ENSP00000502125.1; ENSG00000068796.19. [O00139-1]
DR GeneID; 3796; -.
DR KEGG; hsa:3796; -.
DR MANE-Select; ENST00000407818.8; ENSP00000385000.3; NM_001098511.3; NP_001091981.1. [O00139-4]
DR UCSC; uc003jsx.5; human. [O00139-3]
DR CTD; 3796; -.
DR DisGeNET; 3796; -.
DR GeneCards; KIF2A; -.
DR HGNC; HGNC:6318; KIF2A.
DR HPA; ENSG00000068796; Low tissue specificity.
DR MalaCards; KIF2A; -.
DR MIM; 602591; gene.
DR MIM; 615411; phenotype.
DR neXtProt; NX_O00139; -.
DR OpenTargets; ENSG00000068796; -.
DR PharmGKB; PA162393356; -.
DR VEuPathDB; HostDB:ENSG00000068796; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000155570; -.
DR HOGENOM; CLU_001485_19_1_1; -.
DR InParanoid; O00139; -.
DR OMA; XDVDATN; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; O00139; -.
DR TreeFam; TF105222; -.
DR PathwayCommons; O00139; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; O00139; -.
DR SIGNOR; O00139; -.
DR BioGRID-ORCS; 3796; 46 hits in 1085 CRISPR screens.
DR ChiTaRS; KIF2A; human.
DR EvolutionaryTrace; O00139; -.
DR GeneWiki; KIF2A; -.
DR GenomeRNAi; 3796; -.
DR Pharos; O00139; Tbio.
DR PRO; PR:O00139; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O00139; protein.
DR Bgee; ENSG00000068796; Expressed in cortical plate and 196 other tissues.
DR ExpressionAtlas; O00139; baseline and differential.
DR Genevisible; O00139; HS.
DR GO; GO:0120103; C:centriolar subdistal appendage; IDA:GO_Central.
DR GO; GO:0005814; C:centriole; IDA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:ProtInc.
DR GO; GO:0008017; F:microtubule binding; IDA:ARUK-UCL.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:ARUK-UCL.
DR GO; GO:0007019; P:microtubule depolymerization; TAS:ARUK-UCL.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0030334; P:regulation of cell migration; IGI:ARUK-UCL.
DR Gene3D; 3.40.850.10; -; 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; PTHR24115; 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; Cell cycle;
KW Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Disease variant; Lissencephaly; Microtubule; Mitosis;
KW Motor protein; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..706
FT /note="Kinesin-like protein KIF2A"
FT /id="PRO_0000125414"
FT DOMAIN 223..553
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..217
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 66..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 660..699
FT /evidence="ECO:0000255"
FT COMPBIAS 120..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313..320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28740"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9177777"
FT /id="VSP_028374"
FT VAR_SEQ 1..21
FT /note="MATANFGKIQIGIYVEIKRSD -> M (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047373"
FT VAR_SEQ 134..153
FT /note="GSVSDISPVQAAKKEFGPPS -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9177777"
FT /id="VSP_028375"
FT VAR_SEQ 552
FT /note="E -> EFGISPSDIPFSQGSGSRPDLSPSYEYDDFSPSVTRVKE (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028376"
FT VARIANT 317
FT /note="S -> N (in CDCBM3; results in abnormal cellular
FT localization with predominant decoration of microtubules
FT rather than diffuse punctiform cytoplasmic and nuclear
FT distribution as observed for wild-type protein;
FT dbSNP:rs587777034)"
FT /evidence="ECO:0000269|PubMed:23603762"
FT /id="VAR_070575"
FT VARIANT 321
FT /note="H -> D (in CDCBM3; results in abnormal cellular
FT localization with predominant decoration of microtubules
FT rather than diffuse punctiform cytoplasmic and nuclear
FT distribution as observed for wild-type protein;
FT dbSNP:rs587777033)"
FT /evidence="ECO:0000269|PubMed:23603762"
FT /id="VAR_070576"
FT CONFLICT 143
FT /note="Q -> H (in Ref. 7; AAP84320)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="S -> SHLFFSA (in Ref. 7; AAP84320)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="R -> K (in Ref. 1; CAA69621)"
FT /evidence="ECO:0000305"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 250..261
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:2GRY"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:2GRY"
FT TURN 377..381
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 407..421
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 434..457
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 472..497
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 508..512
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 514..518
FT /evidence="ECO:0007829|PDB:2GRY"
FT STRAND 522..530
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:2GRY"
FT HELIX 537..548
FT /evidence="ECO:0007829|PDB:2GRY"
FT MOD_RES O00139-4:556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28740"
FT MOD_RES O00139-4:573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28740"
SQ SEQUENCE 706 AA; 79955 MW; A407D84B6BD04ACF CRC64;
MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF
SLNPDLVPDE EIEPSPETPP PPASSAKVNK IVKNRRTVAS IKNDPPSRDN RVVGSARARP
SQFPEQSSSA QQNGSVSDIS PVQAAKKEFG PPSRRKSNCV KEVEKLQEKR EKRRLQQQEL
REKRAQDVDA TNPNYEIMCM IRDFRGSLDY RPLTTADPID EHRICVCVRK RPLNKKETQM
KDLDVITIPS KDVVMVHEPK QKVDLTRYLE NQTFRFDYAF DDSAPNEMVY RFTARPLVET
IFERGMATCF AYGQTGSGKT HTMGGDFSGK NQDCSKGIYA LAARDVFLML KKPNYKKLEL
QVYATFFEIY SGKVFDLLNR KTKLRVLEDG KQQVQVVGLQ EREVKCVEDV LKLIDIGNSC
RTSGQTSANA HSSRSHAVFQ IILRRKGKLH GKFSLIDLAG NERGADTSSA DRQTRLEGAE
INKSLLALKE CIRALGRNKP HTPFRASKLT QVLRDSFIGE NSRTCMIATI SPGMASCENT
LNTLRYANRV KELTVDPTAA GDVRPIMHHP PNQIDDLETQ WGVGSSPQRD DLKLLCEQNE
EEVSPQLFTF HEAVSQMVEM EEQVVEDHRA VFQESIRWLE DEKALLEMTE EVDYDVDSYA
TQLEAILEQK IDILTELRDK VKSFRAALQE EEQASKQINP KRPRAL
