KIF23_HUMAN
ID KIF23_HUMAN Reviewed; 960 AA.
AC Q02241; B4E1K0; Q8WVP0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Kinesin-like protein KIF23;
DE AltName: Full=Kinesin-like protein 5;
DE AltName: Full=Mitotic kinesin-like protein 1;
GN Name=KIF23; Synonyms=KNSL5, MKLP1;
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 2).
RX PubMed=1406973; DOI=10.1038/359543a0;
RA Nislow C., Lombillo V.A., Kuriyama R., McIntosh J.R.;
RT "A plus-end-directed motor enzyme that moves antiparallel microtubules in
RT vitro localizes to the interzone of mitotic spindles.";
RL Nature 359:543-547(1992).
RN [2]
RP SEQUENCE REVISION.
RA Gryka M.A.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Trachea;
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 5-960 (ISOFORM 1).
RC TISSUE=Lymph, 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 [6]
RP IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, ASSOCIATION TO MICROTUBULES,
RP AND INTERACTION WITH RACGAP1.
RX PubMed=11782313; DOI=10.1016/s1534-5807(01)00110-1;
RA Mishima M., Kaitna S., Glotzer M.;
RT "Central spindle assembly and cytokinesis require a kinesin-like
RT protein/RhoGAP complex with microtubule bundling activity.";
RL Dev. Cell 2:41-54(2002).
RN [7]
RP INTERACTION WITH PRC1.
RX PubMed=15297875; DOI=10.1038/sj.emboj.7600347;
RA Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.;
RT "Essential roles of KIF4 and its binding partner PRC1 in organized central
RT spindle midzone formation.";
RL EMBO J. 23:3237-3248(2004).
RN [8]
RP INTERACTION WITH ANXA11, AND SUBCELLULAR LOCATION.
RX PubMed=15197175; DOI=10.1083/jcb.200311054;
RA Tomas A., Futter C., Moss S.E.;
RT "Annexin 11 is required for midbody formation and completion of the
RT terminal phase of cytokinesis.";
RL J. Cell Biol. 165:813-822(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
RA Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
RA Guha M., Sillibourne J., Doxsey S.J.;
RT "Centriolin anchoring of exocyst and SNARE complexes at the midbody is
RT required for secretory-vesicle-mediated abscission.";
RL Cell 123:75-87(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH RACGAP1.
RX PubMed=16103226; DOI=10.1083/jcb.200501097;
RA Yuce O., Piekny A., Glotzer M.;
RT "An ECT2-centralspindlin complex regulates the localization and function of
RT RhoA.";
RL J. Cell Biol. 170:571-582(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-814; SER-867 AND
RP SER-902, AND 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 [12]
RP FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH
RP ECT2 AND RACGAP1, AND SUBCELLULAR LOCATION.
RX PubMed=16236794; DOI=10.1091/mbc.e05-06-0569;
RA Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.;
RT "Dissecting the role of Rho-mediated signaling in contractile ring
RT formation.";
RL Mol. Biol. Cell 17:43-55(2006).
RN [13]
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 [14]
RP UBIQUITINATION, DEUBIQUITINATION, AND INTERACTION WITH BIRC6/BRUCE AND
RP USP8/UBPY.
RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
RA Pohl C., Jentsch S.;
RT "Final stages of cytokinesis and midbody ring formation are controlled by
RT BRUCE.";
RL Cell 132:832-845(2008).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-738; SER-867 AND
RP SER-902, 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP INTERACTION WITH ECT2.
RX PubMed=19468300; DOI=10.1371/journal.pbio.1000110;
RA Wolfe B.A., Takaki T., Petronczki M., Glotzer M.;
RT "Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF
RT complex to initiate cleavage furrow formation.";
RL PLoS Biol. 7:E1000110-E1000110(2009).
RN [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867, AND IDENTIFICATION BY
RP 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 [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-738; SER-867; SER-902;
RP SER-911 AND THR-927, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-741, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-586 AND LYS-877, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-571; LYS-586; LYS-624; LYS-647;
RP LYS-662; LYS-665; LYS-741; LYS-823; LYS-854; LYS-874; LYS-877; LYS-899 AND
RP LYS-956, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 794-911 IN COMPLEX WITH ARF6,
RP INTERACTION WITH ARF6, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22522702; DOI=10.1038/emboj.2012.89;
RA Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A.,
RA Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M.,
RA Kawasaki M., Kato R., Wakatsuki S., Nakayama K.;
RT "Structural basis for Arf6-MKLP1 complex formation on the Flemming body
RT responsible for cytokinesis.";
RL EMBO J. 31:2590-2603(2012).
CC -!- FUNCTION: Component of the centralspindlin complex that serves as a
CC microtubule-dependent and Rho-mediated signaling required for the
CC myosin contractile ring formation during the cell cycle cytokinesis.
CC Essential for cytokinesis in Rho-mediated signaling. Required for the
CC localization of ECT2 to the central spindle. Plus-end-directed motor
CC enzyme that moves antiparallel microtubules in vitro.
CC {ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794,
CC ECO:0000269|PubMed:22522702}.
CC -!- SUBUNIT: Heterotetramer of two molecules each of RACGAP1 and KIF23.
CC Found in the centralspindlin complex. Interacts with RACGAP1; the
CC interaction is direct. Interacts with ECT2 and PRC1. Interacts with
CC ANXA11 during cytokinesis. Interacts with BIRC6/bruce and USP8/UBPY.
CC Interacts with ARF6, forming heterodimers and heterotetramers.
CC {ECO:0000269|PubMed:11782313, ECO:0000269|PubMed:15197175,
CC ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:16103226,
CC ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:18329369,
CC ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:22522702}.
CC -!- INTERACTION:
CC Q02241; P62330: ARF6; NbExp=23; IntAct=EBI-306852, EBI-638181;
CC Q02241; Q9NR09: BIRC6; NbExp=4; IntAct=EBI-306852, EBI-1765160;
CC Q02241; Q9H8V3: ECT2; NbExp=2; IntAct=EBI-306852, EBI-1054039;
CC Q02241; Q7RTP6-1: MICAL3; NbExp=8; IntAct=EBI-306852, EBI-13945605;
CC Q02241; Q9H0H5: RACGAP1; NbExp=12; IntAct=EBI-306852, EBI-717233;
CC Q02241; P61981: YWHAG; NbExp=3; IntAct=EBI-306852, EBI-359832;
CC Q02241; P63104: YWHAZ; NbExp=6; IntAct=EBI-306852, EBI-347088;
CC Q02241; P62331: Arf6; Xeno; NbExp=10; IntAct=EBI-306852, EBI-988682;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Note=Localizes to
CC the interzone of mitotic spindles. Detected at the midbody during later
CC stages of mitotic cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q02241-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02241-2; Sequence=VSP_021801;
CC Name=3;
CC IsoId=Q02241-3; Sequence=VSP_057348, VSP_057349, VSP_021801;
CC -!- PTM: Ubiquitinated. Deubiquitinated by USP8/UBPY.
CC {ECO:0000269|PubMed:18329369}.
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; X67155; CAA47628.2; -; mRNA.
DR EMBL; AK303874; BAG64812.1; -; mRNA.
DR EMBL; AC027237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017705; AAH17705.2; -; mRNA.
DR EMBL; BC051826; AAH51826.1; -; mRNA.
DR CCDS; CCDS32278.1; -. [Q02241-1]
DR CCDS; CCDS32279.1; -. [Q02241-2]
DR PIR; S28262; S28262.
DR RefSeq; NP_004847.2; NM_004856.6. [Q02241-2]
DR RefSeq; NP_612565.1; NM_138555.3. [Q02241-1]
DR PDB; 3VHX; X-ray; 2.81 A; B/D/F/H=794-911.
DR PDBsum; 3VHX; -.
DR AlphaFoldDB; Q02241; -.
DR SMR; Q02241; -.
DR BioGRID; 114873; 979.
DR CORUM; Q02241; -.
DR DIP; DIP-40359N; -.
DR IntAct; Q02241; 56.
DR MINT; Q02241; -.
DR STRING; 9606.ENSP00000260363; -.
DR BindingDB; Q02241; -.
DR ChEMBL; CHEMBL5899; -.
DR iPTMnet; Q02241; -.
DR MetOSite; Q02241; -.
DR PhosphoSitePlus; Q02241; -.
DR SwissPalm; Q02241; -.
DR BioMuta; KIF23; -.
DR DMDM; 118572664; -.
DR EPD; Q02241; -.
DR jPOST; Q02241; -.
DR MassIVE; Q02241; -.
DR MaxQB; Q02241; -.
DR PaxDb; Q02241; -.
DR PeptideAtlas; Q02241; -.
DR PRIDE; Q02241; -.
DR ProteomicsDB; 5765; -.
DR ProteomicsDB; 58066; -. [Q02241-1]
DR ProteomicsDB; 58067; -. [Q02241-2]
DR Antibodypedia; 4171; 196 antibodies from 29 providers.
DR DNASU; 9493; -.
DR Ensembl; ENST00000260363.9; ENSP00000260363.4; ENSG00000137807.16. [Q02241-1]
DR Ensembl; ENST00000352331.8; ENSP00000304978.6; ENSG00000137807.16. [Q02241-2]
DR Ensembl; ENST00000647715.1; ENSP00000497065.1; ENSG00000137807.16. [Q02241-1]
DR GeneID; 9493; -.
DR KEGG; hsa:9493; -.
DR UCSC; uc002asb.5; human. [Q02241-1]
DR CTD; 9493; -.
DR DisGeNET; 9493; -.
DR GeneCards; KIF23; -.
DR HGNC; HGNC:6392; KIF23.
DR HPA; ENSG00000137807; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; KIF23; -.
DR MIM; 605064; gene.
DR neXtProt; NX_Q02241; -.
DR OpenTargets; ENSG00000137807; -.
DR Orphanet; 98870; Congenital dyserythropoietic anemia type III.
DR PharmGKB; PA30181; -.
DR VEuPathDB; HostDB:ENSG00000137807; -.
DR eggNOG; KOG0247; Eukaryota.
DR GeneTree; ENSGT00940000155837; -.
DR HOGENOM; CLU_001485_13_0_1; -.
DR InParanoid; Q02241; -.
DR OrthoDB; 314538at2759; -.
DR PhylomeDB; Q02241; -.
DR TreeFam; TF105232; -.
DR PathwayCommons; Q02241; -.
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; Q02241; -.
DR SIGNOR; Q02241; -.
DR BioGRID-ORCS; 9493; 798 hits in 1087 CRISPR screens.
DR GeneWiki; KIF23; -.
DR GenomeRNAi; 9493; -.
DR Pharos; Q02241; Tbio.
DR PRO; PR:Q02241; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q02241; protein.
DR Bgee; ENSG00000137807; Expressed in ventricular zone and 121 other tissues.
DR ExpressionAtlas; Q02241; baseline and differential.
DR Genevisible; Q02241; HS.
DR GO; GO:0097149; C:centralspindlin complex; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0090543; C:Flemming body; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
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:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0000022; P:mitotic spindle elongation; TAS:ProtInc.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR Gene3D; 2.60.40.4330; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR032384; Kif23_Arf-bd.
DR InterPro; IPR038105; Kif23_Arf-bd_sf.
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 Pfam; PF16540; MKLP1_Arf_bdg; 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; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Microtubule;
KW Mitosis; Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..960
FT /note="Kinesin-like protein KIF23"
FT /id="PRO_0000125434"
FT DOMAIN 25..436
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..911
FT /note="Interaction with ARF6"
FT /evidence="ECO:0000269|PubMed:22522702"
FT REGION 898..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 535..620
FT /evidence="ECO:0000255"
FT MOTIF 7..11
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 659..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q5G3"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q5G3"
FT MOD_RES 738
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 927
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 571
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 586
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 662
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 665
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 741
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 823
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 854
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 874
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 877
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 899
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 956
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..197
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057348"
FT VAR_SEQ 245
FT /note="K -> KWNSCSTPMRNTDFV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057349"
FT VAR_SEQ 690..793
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:1406973,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_021801"
FT VARIANT 515
FT /note="F -> L (in dbSNP:rs17310879)"
FT /id="VAR_049686"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:3VHX"
FT STRAND 819..822
FT /evidence="ECO:0007829|PDB:3VHX"
FT STRAND 833..836
FT /evidence="ECO:0007829|PDB:3VHX"
FT STRAND 841..846
FT /evidence="ECO:0007829|PDB:3VHX"
FT HELIX 849..854
FT /evidence="ECO:0007829|PDB:3VHX"
FT STRAND 856..865
FT /evidence="ECO:0007829|PDB:3VHX"
FT STRAND 871..882
FT /evidence="ECO:0007829|PDB:3VHX"
FT STRAND 888..901
FT /evidence="ECO:0007829|PDB:3VHX"
SQ SEQUENCE 960 AA; 110059 MW; B2AA784D2D236A90 CRC64;
MKSARAKTPR KPTVKKGSQT NLKDPVGVYC RVRPLGFPDQ ECCIEVINNT TVQLHTPEGY
RLNRNGDYKE TQYSFKQVFG THTTQKELFD VVANPLVNDL IHGKNGLLFT YGVTGSGKTH
TMTGSPGEGG LLPRCLDMIF NSIGSFQAKR YVFKSNDRNS MDIQCEVDAL LERQKREAMP
NPKTSSSKRQ VDPEFADMIT VQEFCKAEEV DEDSVYGVFV SYIEIYNNYI YDLLEEVPFD
PIKPKPPQSK LLREDKNHNM YVAGCTEVEV KSTEEAFEVF WRGQKKRRIA NTHLNRESSR
SHSVFNIKLV QAPLDADGDN VLQEKEQITI SQLSLVDLAG SERTNRTRAE GNRLREAGNI
NQSLMTLRTC MDVLRENQMY GTNKMVPYRD SKLTHLFKNY FDGEGKVRMI VCVNPKAEDY
EENLQVMRFA EVTQEVEVAR PVDKAICGLT PGRRYRNQPR GPVGNEPLVT DVVLQSFPPL
PSCEILDIND EQTLPRLIEA LEKRHNLRQM MIDEFNKQSN AFKALLQEFD NAVLSKENHM
QGKLNEKEKM ISGQKLEIER LEKKNKTLEY KIEILEKTTT IYEEDKRNLQ QELETQNQKL
QRQFSDKRRL EARLQGMVTE TTMKWEKECE RRVAAKQLEM QNKLWVKDEK LKQLKAIVTE
PKTEKPERPS RERDREKVTQ RSVSPSPVPL SSNYIAQISN GQQLMSQPQL HRRSNSCSSI
SVASCISEWE QKIPTYNTPL KVTSIARRRQ QEPGQSKTCI VSDRRRGMYW TEGREVVPTF
RNEIEIEEDH CGRLLFQPDQ NAPPIRLRHR RSRSAGDRWV DHKPASNMQT ETVMQPHVPH
AITVSVANEK ALAKCEKYML THQELASDGE IETKLIKGDI YKTRGGGQSV QFTDIETLKQ
ESPNGSRKRR SSTVAPAQPD GAESEWTDVE TRCSVAVEMR AGSQLGPGYQ HHAQPKRKKP
