KIF2C_HUMAN
ID KIF2C_HUMAN Reviewed; 725 AA.
AC Q99661; B3ITR9; Q5JR88; Q6ICU1; Q96C18; Q96HB8; Q9BWV8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Kinesin-like protein KIF2C;
DE AltName: Full=Kinesin-like protein 6;
DE AltName: Full=Mitotic centromere-associated kinesin;
DE Short=MCAK;
GN Name=KIF2C; Synonyms=KNSL6;
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), VARIANT LEU-449, AND TISSUE
RP SPECIFICITY.
RC TISSUE=T-cell;
RX PubMed=9434124; DOI=10.1016/s0167-4889(97)00103-1;
RA Kim I.-G., Jun D.Y., Sohn U., Kim Y.H.;
RT "Cloning and expression of human mitotic centromere-associated kinesin
RT gene.";
RL Biochim. Biophys. Acta 1359:181-186(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-449, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=12383881; DOI=10.1016/s0024-3205(02)02079-9;
RA Cheng L.J., Zhou Z.M., Li J.M., Zhu H., Zhu H., Zhou Y.D., Wang L.R.,
RA Lin M., Sha J.H.;
RT "Expression of a novel HsMCAK mRNA splice variant, tsMCAK gene, in human
RT testis.";
RL Life Sci. 71:2741-2757(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-449.
RA Katagiri T., Shimo A.;
RT "MCAK/KIF2c V1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and 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 [9]
RP INTERACTION WITH CENPH.
RX PubMed=11092768; DOI=10.1093/hmg/9.19.2919;
RA Sugata N., Li S., Earnshaw W.C., Yen T.J., Yoda K., Masumoto H.,
RA Munekata E., Warburton P.E., Todokoro K.;
RT "Human CENP-H multimers colocalize with CENP-A and CENP-C at active
RT centromere-kinetochore complexes.";
RL Hum. Mol. Genet. 9:2919-2926(2000).
RN [10]
RP PHOSPHORYLATION AT SER-95 BY AURKB, AND SUBCELLULAR LOCATION.
RX PubMed=14960279; DOI=10.1016/s1534-5807(04)00025-5;
RA Andrews P.D., Ovechkina Y., Morrice N., Wagenbach M., Duncan K.,
RA Wordeman L., Swedlow J.R.;
RT "Aurora B regulates MCAK at the mitotic centromere.";
RL Dev. Cell 6:253-268(2004).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=17485487; DOI=10.1083/jcb.200701122;
RA Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D.,
RA Muschel R., Chan G.K., Yen T.J.;
RT "Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective
RT kinetochore attachments.";
RL J. Cell Biol. 177:413-424(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP 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 [14]
RP INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP
RP LOCALIZATION SIGNAL, AND MUTAGENESIS OF SER-95; 100-ILE-PRO-101; SER-109
RP AND SER-111.
RX PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
RA Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
RA Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
RA Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
RT "An EB1-binding motif acts as a microtubule tip localization signal.";
RL Cell 138:366-376(2009).
RN [15]
RP INTERACTION WITH MTUS2 AND MAPRE1.
RX PubMed=19543227; DOI=10.1038/embor.2009.94;
RA Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., Wang F.,
RA Yao X.;
RT "TIP150 interacts with and targets MCAK at the microtubule plus ends.";
RL EMBO Rep. 10:857-865(2009).
RN [16]
RP FUNCTION.
RX PubMed=19060894; DOI=10.1038/ncb1809;
RA Bakhoum S.F., Thompson S.L., Manning A.L., Compton D.A.;
RT "Genome stability is ensured by temporal control of kinetochore-microtubule
RT dynamics.";
RL Nat. Cell Biol. 11:27-35(2009).
RN [17]
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 [18]
RP UBIQUITINATION.
RX PubMed=20596523; DOI=10.1371/journal.pone.0011332;
RA Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B.,
RA Spruck C.;
RT "Development and validation of a method for profiling post-translational
RT modification activities using protein microarrays.";
RL PLoS ONE 5:E11332-E11332(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-621 AND SER-633, AND
RP IDENTIFICATION BY MASS 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 [20]
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 [21]
RP FUNCTION, INTERACTION WITH KIF18B, AND SUBCELLULAR LOCATION.
RX PubMed=21820309; DOI=10.1016/j.cub.2011.07.017;
RA Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A.,
RA Medema R.H.;
RT "A complex of Kif18b and MCAK promotes microtubule depolymerization and is
RT negatively regulated by Aurora kinases.";
RL Curr. Biol. 21:1356-1365(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23891108; DOI=10.1016/j.cub.2013.06.040;
RA Shrestha R.L., Draviam V.M.;
RT "Lateral to end-on conversion of chromosome-microtubule attachment requires
RT kinesins CENP-E and MCAK.";
RL Curr. Biol. 23:1514-1526(2013).
RN [24]
RP ERRATUM OF PUBMED:23891108.
RA Shrestha R.L., Draviam V.M.;
RL Curr. Biol. 23:2440-2441(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-22; SER-106; SER-115;
RP SER-166; SER-175; SER-187 AND SER-519, AND IDENTIFICATION BY MASS
RP 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 [26]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 225-593 IN COMPLEX WITH ADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the KIF2C motor domain.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: In complex with KIF18B, constitutes the major microtubule
CC plus-end depolymerizing activity in mitotic cells (PubMed:21820309).
CC Regulates the turnover of microtubules at the kinetochore and functions
CC in chromosome segregation during mitosis (PubMed:19060894). Plays a
CC role in chromosome congression and is required for the lateral to end-
CC on conversion of the chromosome-microtubule attachment
CC (PubMed:23891108). {ECO:0000269|PubMed:19060894,
CC ECO:0000269|PubMed:21820309, ECO:0000269|PubMed:23891108}.
CC -!- SUBUNIT: Interacts with CENPH. Interacts with MTUS2/TIP150; the
CC interaction is direct. Interacts with MAPRE1; the interaction is
CC direct, regulated by phosphorylation and is probably required for
CC targeting to growing microtubule plus ends. Interacts with KIF18B at
CC microtubule tips; this interaction increases the affinity of both
CC partners for microtubule plus ends and is required for robust
CC microtubule depolymerization. Phosphorylation by AURKA or AURKB
CC strongly reduces KIF18B-binding. {ECO:0000269|PubMed:11092768,
CC ECO:0000269|PubMed:19543227, ECO:0000269|PubMed:19632184,
CC ECO:0000269|PubMed:21820309, ECO:0000269|Ref.26}.
CC -!- INTERACTION:
CC Q99661; Q15691: MAPRE1; NbExp=7; IntAct=EBI-1642317, EBI-1004115;
CC Q99661; Q5JR59: MTUS2; NbExp=4; IntAct=EBI-1642317, EBI-742948;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21820309,
CC ECO:0000269|PubMed:23891108}. Nucleus {ECO:0000250|UniProtKB:P70096}.
CC Chromosome, centromere {ECO:0000269|PubMed:14960279,
CC ECO:0000269|PubMed:17485487}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:14960279, ECO:0000269|PubMed:17485487,
CC ECO:0000269|PubMed:23891108}. Note=Associates with the microtubule
CC network at the growing distal tip (the plus-end) of microtubules,
CC probably through interaction with MTUS2/TIP150 and MAPRE1 (By
CC similarity). Association with microtubule plus ends is also mediated by
CC interaction with KIF18B. Centromeric localization requires the presence
CC of BUB1 and SGO2. {ECO:0000250|UniProtKB:P70096,
CC ECO:0000269|PubMed:17485487, ECO:0000269|PubMed:21820309}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99661-1; Sequence=Displayed;
CC Name=2; Synonyms=tsMCAK;
CC IsoId=Q99661-2; Sequence=VSP_002866;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in thymus and testis, at
CC low levels in small intestine, the mucosal lining of colon, and
CC placenta, and at very low levels in spleen and ovary; expression is not
CC detected in prostate, peripheral blood Leukocytes, heart, brain, lung,
CC liver, skeletal muscle, kidney or pancreas. Isoform 2 is testis-
CC specific. {ECO:0000269|PubMed:12383881, ECO:0000269|PubMed:9434124}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed in fetal testis.
CC {ECO:0000269|PubMed:12383881}.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends. {ECO:0000269|PubMed:19632184}.
CC -!- PTM: Phosphorylation by AURKB, regulates association with centromeres
CC and kinetochores and the microtubule depolymerization activity.
CC {ECO:0000269|PubMed:14960279}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:20596523}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; U63743; AAC27660.1; -; mRNA.
DR EMBL; AY026505; AAK20168.1; -; mRNA.
DR EMBL; BT006759; AAP35405.1; -; mRNA.
DR EMBL; CR450302; CAG29298.1; -; mRNA.
DR EMBL; AB264115; BAG50306.1; -; mRNA.
DR EMBL; AL592166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07025.1; -; Genomic_DNA.
DR EMBL; BC008764; AAH08764.1; -; mRNA.
DR EMBL; BC014924; AAH14924.1; -; mRNA.
DR CCDS; CCDS512.1; -. [Q99661-1]
DR CCDS; CCDS72774.1; -. [Q99661-2]
DR RefSeq; NP_001284584.1; NM_001297655.1.
DR RefSeq; NP_001284585.1; NM_001297656.1. [Q99661-2]
DR RefSeq; NP_001284586.1; NM_001297657.1.
DR RefSeq; NP_006836.2; NM_006845.3. [Q99661-1]
DR PDB; 2HEH; X-ray; 2.15 A; A=225-593.
DR PDB; 4UBF; X-ray; 3.00 A; A/B/C/D=225-593, P=709-720.
DR PDB; 4Y05; X-ray; 2.59 A; A=216-599.
DR PDB; 5MIO; X-ray; 3.19 A; C=216-598.
DR PDBsum; 2HEH; -.
DR PDBsum; 4UBF; -.
DR PDBsum; 4Y05; -.
DR PDBsum; 5MIO; -.
DR AlphaFoldDB; Q99661; -.
DR SMR; Q99661; -.
DR BioGRID; 116195; 146.
DR ELM; Q99661; -.
DR IntAct; Q99661; 62.
DR MINT; Q99661; -.
DR STRING; 9606.ENSP00000361298; -.
DR BindingDB; Q99661; -.
DR ChEMBL; CHEMBL5967; -.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR GlyGen; Q99661; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99661; -.
DR MetOSite; Q99661; -.
DR PhosphoSitePlus; Q99661; -.
DR SwissPalm; Q99661; -.
DR BioMuta; KIF2C; -.
DR DMDM; 20141607; -.
DR EPD; Q99661; -.
DR jPOST; Q99661; -.
DR MassIVE; Q99661; -.
DR MaxQB; Q99661; -.
DR PaxDb; Q99661; -.
DR PeptideAtlas; Q99661; -.
DR PRIDE; Q99661; -.
DR ProteomicsDB; 78382; -. [Q99661-1]
DR ProteomicsDB; 78383; -. [Q99661-2]
DR Antibodypedia; 1212; 393 antibodies from 34 providers.
DR CPTC; Q99661; 3 antibodies.
DR DNASU; 11004; -.
DR Ensembl; ENST00000372217.5; ENSP00000361291.1; ENSG00000142945.13. [Q99661-2]
DR Ensembl; ENST00000372224.9; ENSP00000361298.4; ENSG00000142945.13. [Q99661-1]
DR GeneID; 11004; -.
DR KEGG; hsa:11004; -.
DR MANE-Select; ENST00000372224.9; ENSP00000361298.4; NM_006845.4; NP_006836.2.
DR UCSC; uc001cmg.5; human. [Q99661-1]
DR CTD; 11004; -.
DR DisGeNET; 11004; -.
DR GeneCards; KIF2C; -.
DR HGNC; HGNC:6393; KIF2C.
DR HPA; ENSG00000142945; Group enriched (bone marrow, lymphoid tissue, testis).
DR MIM; 604538; gene.
DR neXtProt; NX_Q99661; -.
DR OpenTargets; ENSG00000142945; -.
DR PharmGKB; PA30182; -.
DR VEuPathDB; HostDB:ENSG00000142945; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000154046; -.
DR HOGENOM; CLU_001485_19_1_1; -.
DR InParanoid; Q99661; -.
DR OMA; RTTLECH; -.
DR PhylomeDB; Q99661; -.
DR TreeFam; TF105222; -.
DR BRENDA; 5.6.1.3; 2681.
DR PathwayCommons; Q99661; -.
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; Q99661; -.
DR SIGNOR; Q99661; -.
DR BioGRID-ORCS; 11004; 175 hits in 1095 CRISPR screens.
DR ChiTaRS; KIF2C; human.
DR EvolutionaryTrace; Q99661; -.
DR GeneWiki; KIF2C; -.
DR GenomeRNAi; 11004; -.
DR Pharos; Q99661; Tbio.
DR PRO; PR:Q99661; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99661; protein.
DR Bgee; ENSG00000142945; Expressed in secondary oocyte and 130 other tissues.
DR ExpressionAtlas; Q99661; baseline and differential.
DR Genevisible; Q99661; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0019237; F:centromeric DNA binding; TAS:ProtInc.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:HGNC-UCL.
DR GO; GO:0051310; P:metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; IMP:UniProtKB.
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; Centromere; Chromosome; Chromosome partition; Coiled coil;
KW Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..725
FT /note="Kinesin-like protein KIF2C"
FT /id="PRO_0000125418"
FT DOMAIN 258..588
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 2..254
FT /note="Globular"
FT /evidence="ECO:0000255"
FT REGION 89..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..238
FT /note="Negative regulator of microtubule-binding"
FT /evidence="ECO:0000250"
FT COILED 618..658
FT /evidence="ECO:0000255"
FT MOTIF 98..101
FT /note="Microtubule tip localization signal"
FT MOTIF 415..418
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 348..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:14960279"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70096"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..55
FT /note="MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATK
FT GKE -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12383881"
FT /id="VSP_002866"
FT VARIANT 449
FT /note="I -> L (in dbSNP:rs4342887)"
FT /evidence="ECO:0000269|PubMed:12383881,
FT ECO:0000269|PubMed:9434124, ECO:0000269|Ref.5"
FT /id="VAR_049683"
FT MUTAGEN 95
FT /note="S->E: Alters interaction with MAPRE1 and association
FT with microtubule growing ends; when associated with E-109
FT and E-111."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 100..101
FT /note="IP->NN: Loss of interaction with MAPRE1 and
FT association with microtubule growing ends."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 109
FT /note="S->E: Alters interaction with MAPRE1 and association
FT with microtubule growing ends; when associated with E-95
FT and E-111."
FT /evidence="ECO:0000269|PubMed:19632184"
FT MUTAGEN 111
FT /note="S->E: Alters interaction with MAPRE1 and association
FT with microtubule growing ends; when associated with E-95
FT and E-109."
FT /evidence="ECO:0000269|PubMed:19632184"
FT CONFLICT 698
FT /note="R -> P (in Ref. 8; AAH08764)"
FT /evidence="ECO:0000305"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:5MIO"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 285..296
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:4Y05"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 373..385
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2HEH"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 396..405
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2HEH"
FT TURN 412..416
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:5MIO"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 442..455
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 470..492
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:5MIO"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:4UBF"
FT HELIX 514..531
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 543..547
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:2HEH"
FT STRAND 557..565
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:2HEH"
FT HELIX 572..585
FT /evidence="ECO:0007829|PDB:2HEH"
SQ SEQUENCE 725 AA; 81313 MW; 5BDECC133AB4B55C CRC64;
MAMDSSLQAR LFPGLAIKIQ RSNGLIHSAN VRTVNLEKSC VSVEWAEGGA TKGKEIDFDD
VAAINPELLQ LLPLHPKDNL PLQENVTIQK QKRRSVNSKI PAPKESLRSR STRMSTVSEL
RITAQENDME VELPAAANSR KQFSVPPAPT RPSCPAVAEI PLRMVSEEME EQVHSIRGSS
SANPVNSVRR KSCLVKEVEK MKNKREEKKA QNSEMRMKRA QEYDSSFPNW EFARMIKEFR
ATLECHPLTM TDPIEEHRIC VCVRKRPLNK QELAKKEIDV ISIPSKCLLL VHEPKLKVDL
TKYLENQAFC FDFAFDETAS NEVVYRFTAR PLVQTIFEGG KATCFAYGQT GSGKTHTMGG
DLSGKAQNAS KGIYAMASRD VFLLKNQPCY RKLGLEVYVT FFEIYNGKLF DLLNKKAKLR
VLEDGKQQVQ VVGLQEHLVN SADDVIKMID MGSACRTSGQ TFANSNSSRS HACFQIILRA
KGRMHGKFSL VDLAGNERGA DTSSADRQTR MEGAEINKSL LALKECIRAL GQNKAHTPFR
ESKLTQVLRD SFIGENSRTC MIATISPGIS SCEYTLNTLR YADRVKELSP HSGPSGEQLI
QMETEEMEAC SNGALIPGNL SKEEEELSSQ MSSFNEAMTQ IRELEEKAME ELKEIIQQGP
DWLELSEMTE QPDYDLETFV NKAESALAQQ AKHFSALRDV IKALRLAMQL EEQASRQISS
KKRPQ
