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 27-MAR-2024, entry version 223. 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). RN [28] RP VARIANT CDAN3A ARG-916, CHARACTERIZATION OF VARIANT CDAN3A ARG-916, RP INVOLVEMENT IN CDAN3A, TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=23570799; DOI=10.1182/blood-2012-10-461392; RA Liljeholm M., Irvine A.F., Vikberg A.L., Norberg A., Month S., RA Sandstroem H., Wahlin A., Mishima M., Golovleva I.; RT "Congenital dyserythropoietic anemia type III (CDA III) is caused by a RT mutation in kinesin family member, KIF23."; RL Blood 121:4791-4799(2013). RN [29] RP INVOLVEMENT IN CDAN3A. RX PubMed=33159567; DOI=10.1007/s00277-020-04319-5; RA Mendez M., Moreno-Carralero M.I., Peri V.L., Camacho-Galan R., RA Bosch-Benitez J.M., Huerta-Aragones J., Sanchez-Calero-Guilarte J., RA Moreno-Risco M.B., Alonso-Dominguez J.M., Moran-Jimenez M.J.; RT "Congenital dyserythropoietic anemia types Ib, II, and III: novel variants RT in the CDIN1 gene and functional study of a novel variant in the KIF23 RT gene."; RL Ann. Hematol. 100:353-364(2021). 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, ECO:0000269|PubMed:23570799}. 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; P31947: SFN; NbExp=4; IntAct=EBI-306852, EBI-476295; CC Q02241; P61981: YWHAG; NbExp=6; IntAct=EBI-306852, EBI-359832; CC Q02241; P63104: YWHAZ; NbExp=8; 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 -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:23570799}. CC -!- PTM: Ubiquitinated. Deubiquitinated by USP8/UBPY. CC {ECO:0000269|PubMed:18329369}. CC -!- DISEASE: Anemia, congenital dyserythropoietic, 3A (CDAN3A) CC [MIM:105600]: An autosomal dominant blood disorder characterized by CC ineffective erythropoiesis, hemolytic anemia, macrocytosis in the CC peripheral blood, intravascular hemolysis, and giant multinucleated CC erythroblasts in the bone marrow. {ECO:0000269|PubMed:23570799, CC ECO:0000269|PubMed:33159567}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 1020. DR CORUM; Q02241; -. DR DIP; DIP-40359N; -. DR IntAct; Q02241; 60. DR MINT; Q02241; -. DR STRING; 9606.ENSP00000260363; -. DR BindingDB; Q02241; -. DR ChEMBL; CHEMBL5899; -. DR GlyGen; Q02241; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000260363; -. DR PeptideAtlas; Q02241; -. DR ProteomicsDB; 5765; -. DR ProteomicsDB; 58066; -. [Q02241-1] DR ProteomicsDB; 58067; -. [Q02241-2] DR Pumba; Q02241; -. DR Antibodypedia; 4171; 261 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 AGR; HGNC:6392; -. 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; 105600; phenotype. 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; 5403873at2759; -. 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; 834 hits in 1165 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 123 other cell types or tissues. DR ExpressionAtlas; Q02241; baseline and differential. 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:HPA. 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 CDD; cd01368; KISc_KIF23_like; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 2.60.40.4330; Kinesin-like protein Kif23, Arf6-interacting domain; 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:SF600; KINESIN-LIKE PROTEIN KIF23; 1. DR PANTHER; PTHR24115; KINESIN-RELATED; 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; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR Genevisible; Q02241; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division; KW Coiled coil; Congenital dyserythropoietic anemia; Cytoplasm; Cytoskeleton; KW Disease variant; Hereditary hemolytic anemia; 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 VARIANT 916 FT /note="P -> R (in CDAN3A; results in loss of function; does FT not rescue defective cytokinesis when expressed in FT KIF3-deficient cells)" FT /evidence="ECO:0000269|PubMed:23570799" FT /id="VAR_086957" 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 //