KIF23_MOUSE
ID KIF23_MOUSE Reviewed; 953 AA.
AC E9Q5G3; Q80V30; Q99PT8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Kinesin-like protein KIF23;
GN Name=Kif23;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-340, AND TISSUE SPECIFICITY.
RX PubMed=11416179; DOI=10.1073/pnas.111145398;
RA Miki H., Setou M., Kaneshiro K.;
RT "All kinesin superfamily protein, KIF, genes in mouse and human.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7004-7011(2001).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19020301; DOI=10.1095/biolreprod.108.070649;
RA Greenbaum M.P., Iwamori N., Agno J.E., Matzuk M.M.;
RT "Mouse TEX14 is required for embryonic germ cell intercellular bridges but
RT not female fertility.";
RL Biol. Reprod. 80:449-457(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-683; SER-685;
RP SER-860 AND THR-920, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH ARF6.
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 (By similarity).
CC {ECO:0000250}.
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 (By
CC similarity). Interacts with ARF6, forming heterodimers and
CC heterotetramers. {ECO:0000250, ECO:0000269|PubMed:22522702}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Midbody, Midbody ring
CC {ECO:0000269|PubMed:19020301}. Note=Localizes to the interzone of
CC mitotic spindles (By similarity). Detected at the midbody during later
CC stages of mitotic cytokinesis. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in testis and ovary from newborn mice (at
CC protein level). Detected in brain, spinal cord and small intestine.
CC {ECO:0000269|PubMed:11416179, ECO:0000269|PubMed:19020301}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by USP8/UBPY (By similarity).
CC {ECO:0000250}.
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; AC151969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047273; AAH47273.1; -; mRNA.
DR EMBL; AB054027; BAB32491.1; -; Genomic_DNA.
DR CCDS; CCDS40662.1; -.
DR RefSeq; NP_077207.3; NM_024245.4.
DR AlphaFoldDB; E9Q5G3; -.
DR SMR; E9Q5G3; -.
DR BioGRID; 214951; 31.
DR IntAct; E9Q5G3; 16.
DR MINT; E9Q5G3; -.
DR STRING; 10090.ENSMUSP00000034815; -.
DR iPTMnet; E9Q5G3; -.
DR PhosphoSitePlus; E9Q5G3; -.
DR EPD; E9Q5G3; -.
DR jPOST; E9Q5G3; -.
DR MaxQB; E9Q5G3; -.
DR PaxDb; E9Q5G3; -.
DR PeptideAtlas; E9Q5G3; -.
DR PRIDE; E9Q5G3; -.
DR ProteomicsDB; 263530; -.
DR Antibodypedia; 4171; 196 antibodies from 29 providers.
DR DNASU; 71819; -.
DR Ensembl; ENSMUST00000034815; ENSMUSP00000034815; ENSMUSG00000032254.
DR GeneID; 71819; -.
DR KEGG; mmu:71819; -.
DR UCSC; uc009pzu.2; mouse.
DR CTD; 9493; -.
DR MGI; MGI:1919069; Kif23.
DR VEuPathDB; HostDB:ENSMUSG00000032254; -.
DR eggNOG; KOG0247; Eukaryota.
DR GeneTree; ENSGT00940000155837; -.
DR HOGENOM; CLU_001485_13_0_1; -.
DR InParanoid; E9Q5G3; -.
DR OMA; INPRIED; -.
DR OrthoDB; 314538at2759; -.
DR PhylomeDB; E9Q5G3; -.
DR TreeFam; TF105232; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68884; Mitotic Telophase/Cytokinesis.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 71819; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Kif23; mouse.
DR PRO; PR:E9Q5G3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; E9Q5G3; protein.
DR Bgee; ENSMUSG00000032254; Expressed in animal zygote and 204 other tissues.
DR ExpressionAtlas; E9Q5G3; baseline and differential.
DR Genevisible; E9Q5G3; MM.
DR GO; GO:0097149; C:centralspindlin complex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0090543; C:Flemming body; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; IDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
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; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; ISO:MGI.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
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 ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Microtubule; Mitosis; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..953
FT /note="Kinesin-like protein KIF23"
FT /id="PRO_0000425085"
FT DOMAIN 25..436
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 658..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 542..618
FT /evidence="ECO:0000255"
FT MOTIF 7..11
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 658..681
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:0000250|UniProtKB:Q02241"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 739
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT MOD_RES 920
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 587
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 625
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 663
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 666
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 816
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 847
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 867
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 870
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 892
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CROSSLNK 949
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02241"
FT CONFLICT 464
FT /note="V -> I (in Ref. 2; AAH47273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 108776 MW; DE6E050D59A18513 CRC64;
MKSAKAKTVR KPVIKKGSQT NLKDPVGVYC RVRPLSFPDQ ECCVEVINST TLQLHTPEGY
RLNRNGDYKE TQYSFKRVFG THTTQKELFD VVANPLVDDL IHGKNGLLFT YGVTGSGKTY
TMTGSPGSGG LLPRCLNMIF NSIGSFQAKR YVFKSNDRNS MEIQCEVDAL LERQKREALP
IPKTPSSKRQ ADPEFADMIN VQEFCKAEEV DEDSVYGVFV SYIEIYNNYI YDLLEEVQFD
PIKPKLPQSK TLREDKNHNM YVAGCTEVEV KSTEEAFEVF WRGQKKRRIA NTHLNRESSR
SHSVFSIKLV QAPLDADGDN VLQEKEQITI SQLSLVDLAG SERTNRTKAE GNRLREAGNI
NQSLMTLRTC MEVLRENQTY GTNKMVPYRD SKLTHLFKNY FDGEGKVRMI VCVNPKAEDY
EESLQVMRFA EVTQEVEVAR PVDKVICGLT PGRRYRNLPR GGPVGDEPLV PEVILQSFPP
LPPCKLLDIN DEETLPKLAD TLEKRHHLRQ LMTEDLNKKC LAFKALLKEF DNSLSNKENY
VQEKLNEREK VISGQKLEIE RLEKKNKTLE YKIEILEKTT TIYEEDKRNL QQELESQNQK
LQRQFSDKRR LEARLQGMVT ETSMKWQKEC ERRVAATQLE MQNKLWVKDE KLKQLKAIVT
EPKPEKPERP SRERDREKII PRSVSPSPLP LSSNNIAQIS NGQQLMSQPQ LHRRSNSCSS
ISVASCISEW EQKLSPFSTP VNVTSLARHR QQEPGQSKTC IVSDRRRGMC WTEGREMVPT
FSSEIGVEED HCRRNTPIPV RHRRSRSAGS RWVDHKPASN VQTETVMQPH VPHAITVSVA
NEKALAKCEK YMLTHQELAS DGEIQTKVIK GDVYKTRGGG QSVQFTDIET LKQELPTGSR
KRRSSTLAPA QPDGTESEWT DVETRCSVAV EMRAGSQLGP GYQHHAQPKR KKP
