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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
 
 
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