Q02241 (KIF23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin-like protein KIF23

Alternative name(s):
Kinesin-like protein 5
Mitotic kinesin-like protein 1

Gene names

Name:	KIF23
Synonyms:	KNSL5, MKLP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	960 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro. Ref.8 Ref.11
Subunit structure	Heteretetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Interacts with RACGAP1; the interaction is direct. Interacts with ECT2 and PRC1. Interacts with ANXA11 during cytokinesis. Ref.4 Ref.5 Ref.6 Ref.8 Ref.11 Ref.19
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › spindle. Note: Localizes to the interzone of mitotic spindles. Ref.6 Ref.11
Sequence similarities	Belongs to the kinesin-like protein family. Contains 1 kinesin-motor domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome cell cycle cytokinesis Inferred from mutant phenotype Ref.11. Source: UniProtKB microtubule-based movement Traceable author statement. Source: Reactome mitotic spindle elongation Traceable author statement. Source: ProtInc positive regulation of cell cycle cytokinesis Inferred from mutant phenotype Ref.8. Source: UniProtKB spindle midzone assembly involved in mitosis Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular component	centralspindlin complex Inferred from direct assay Ref.4Ref.11. Source: UniProtKB cytosol Traceable author statement. Source: Reactome kinesin complex Traceable author statement. Source: ProtInc microtubule Inferred from electronic annotation. Source: UniProtKB-KW midbody Inferred from direct assay Ref.4Ref.6. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from direct assay Ref.4. Source: UniProtKB microtubule motor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIRC6	Q9NR09	4	EBI-306852,EBI-1765160

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q02241-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q02241-2)

The sequence of this isoform differs from the canonical sequence as follows:
     690-793: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 960	960	Kinesin-like protein KIF23		PRO_0000125434
Regions
	Domain	1 – 352	352	Kinesin-motor
	Nucleotide binding	112 – 119	8	ATP By similarity
	Coiled coil	535 – 620	86	Potential
	Motif	7 – 11	5	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	29	1	Phosphotyrosine Ref.9
	Modified residue	155	1	Phosphoserine Ref.10
	Modified residue	160	1	Phosphoserine Ref.13 Ref.17
	Modified residue	450	1	Phosphothreonine Ref.12 Ref.17
	Modified residue	682	1	Phosphoserine Ref.13 Ref.15 Ref.16
	Modified residue	684	1	Phosphoserine Ref.7 Ref.13 Ref.15 Ref.16
	Modified residue	686	1	Phosphoserine Ref.14 Ref.16
	Modified residue	738	1	Phosphothreonine Ref.12 Ref.17 Ref.18
	Modified residue	814	1	Phosphoserine Ref.10
	Modified residue	861	1	Phosphothreonine Ref.17
	Modified residue	867	1	Phosphoserine Ref.10 Ref.15 Ref.17 Ref.20
	Modified residue	902	1	Phosphoserine Ref.10 Ref.17
	Modified residue	911	1	Phosphoserine Ref.13 Ref.16
	Modified residue	912	1	Phosphoserine Ref.13 Ref.16
	Modified residue	913	1	Phosphothreonine Ref.16
	Modified residue	934	1	Phosphoserine Ref.15
Natural variations
	Alternative sequence	690 – 793	104	Missing in isoform 2.		VSP_021801
	Natural variant	515	1	F → L. Corresponds to variant rs17310879 [ dbSNP | Ensembl ].		VAR_049686

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2006. Version 3. Checksum: B2AA784D2D236A90	FASTA	960	110,059
	10 20 30 40 50 60 MKSARAKTPR KPTVKKGSQT NLKDPVGVYC RVRPLGFPDQ ECCIEVINNT TVQLHTPEGY 70 80 90 100 110 120 RLNRNGDYKE TQYSFKQVFG THTTQKELFD VVANPLVNDL IHGKNGLLFT YGVTGSGKTH 130 140 150 160 170 180 TMTGSPGEGG LLPRCLDMIF NSIGSFQAKR YVFKSNDRNS MDIQCEVDAL LERQKREAMP 190 200 210 220 230 240 NPKTSSSKRQ VDPEFADMIT VQEFCKAEEV DEDSVYGVFV SYIEIYNNYI YDLLEEVPFD 250 260 270 280 290 300 PIKPKPPQSK LLREDKNHNM YVAGCTEVEV KSTEEAFEVF WRGQKKRRIA NTHLNRESSR 310 320 330 340 350 360 SHSVFNIKLV QAPLDADGDN VLQEKEQITI SQLSLVDLAG SERTNRTRAE GNRLREAGNI 370 380 390 400 410 420 NQSLMTLRTC MDVLRENQMY GTNKMVPYRD SKLTHLFKNY FDGEGKVRMI VCVNPKAEDY 430 440 450 460 470 480 EENLQVMRFA EVTQEVEVAR PVDKAICGLT PGRRYRNQPR GPVGNEPLVT DVVLQSFPPL 490 500 510 520 530 540 PSCEILDIND EQTLPRLIEA LEKRHNLRQM MIDEFNKQSN AFKALLQEFD NAVLSKENHM 550 560 570 580 590 600 QGKLNEKEKM ISGQKLEIER LEKKNKTLEY KIEILEKTTT IYEEDKRNLQ QELETQNQKL 610 620 630 640 650 660 QRQFSDKRRL EARLQGMVTE TTMKWEKECE RRVAAKQLEM QNKLWVKDEK LKQLKAIVTE 670 680 690 700 710 720 PKTEKPERPS RERDREKVTQ RSVSPSPVPL SSNYIAQISN GQQLMSQPQL HRRSNSCSSI 730 740 750 760 770 780 SVASCISEWE QKIPTYNTPL KVTSIARRRQ QEPGQSKTCI VSDRRRGMYW TEGREVVPTF 790 800 810 820 830 840 RNEIEIEEDH CGRLLFQPDQ NAPPIRLRHR RSRSAGDRWV DHKPASNMQT ETVMQPHVPH 850 860 870 880 890 900 AITVSVANEK ALAKCEKYML THQELASDGE IETKLIKGDI YKTRGGGQSV QFTDIETLKQ 910 920 930 940 950 960 ESPNGSRKRR SSTVAPAQPD GAESEWTDVE TRCSVAVEMR AGSQLGPGYQ HHAQPKRKKP
	Isoform 2 [UniParc]. Checksum: DDE7CEB480ABE58A	FASTA	856	98,105
	10 20 30 40 50 60 MKSARAKTPR KPTVKKGSQT NLKDPVGVYC RVRPLGFPDQ ECCIEVINNT TVQLHTPEGY 70 80 90 100 110 120 RLNRNGDYKE TQYSFKQVFG THTTQKELFD VVANPLVNDL IHGKNGLLFT YGVTGSGKTH 130 140 150 160 170 180 TMTGSPGEGG LLPRCLDMIF NSIGSFQAKR YVFKSNDRNS MDIQCEVDAL LERQKREAMP 190 200 210 220 230 240 NPKTSSSKRQ VDPEFADMIT VQEFCKAEEV DEDSVYGVFV SYIEIYNNYI YDLLEEVPFD 250 260 270 280 290 300 PIKPKPPQSK LLREDKNHNM YVAGCTEVEV KSTEEAFEVF WRGQKKRRIA NTHLNRESSR 310 320 330 340 350 360 SHSVFNIKLV QAPLDADGDN VLQEKEQITI SQLSLVDLAG SERTNRTRAE GNRLREAGNI 370 380 390 400 410 420 NQSLMTLRTC MDVLRENQMY GTNKMVPYRD SKLTHLFKNY FDGEGKVRMI VCVNPKAEDY 430 440 450 460 470 480 EENLQVMRFA EVTQEVEVAR PVDKAICGLT PGRRYRNQPR GPVGNEPLVT DVVLQSFPPL 490 500 510 520 530 540 PSCEILDIND EQTLPRLIEA LEKRHNLRQM MIDEFNKQSN AFKALLQEFD NAVLSKENHM 550 560 570 580 590 600 QGKLNEKEKM ISGQKLEIER LEKKNKTLEY KIEILEKTTT IYEEDKRNLQ QELETQNQKL 610 620 630 640 650 660 QRQFSDKRRL EARLQGMVTE TTMKWEKECE RRVAAKQLEM QNKLWVKDEK LKQLKAIVTE 670 680 690 700 710 720 PKTEKPERPS RERDREKVTQ RSVSPSPVPL LFQPDQNAPP IRLRHRRSRS AGDRWVDHKP 730 740 750 760 770 780 ASNMQTETVM QPHVPHAITV SVANEKALAK CEKYMLTHQE LASDGEIETK LIKGDIYKTR 790 800 810 820 830 840 GGGQSVQFTD IETLKQESPN GSRKRRSSTV APAQPDGAES EWTDVETRCS VAVEMRAGSQ 850 LGPGYQHHAQ PKRKKP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles." Nislow C., Lombillo V.A., Kuriyama R., McIntosh J.R. Nature 359:543-547(1992) [PubMed: 1406973] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	Gryka M.A. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-960 (ISOFORM 1). Tissue: Lymph and Uterus.
[4]	"Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity." Mishima M., Kaitna S., Glotzer M. Dev. Cell 2:41-54(2002) [PubMed: 11782313] [Abstract] Cited for: IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, ASSOCIATION TO MICROTUBULES, INTERACTION WITH RACGAP1.
[5]	"Essential roles of KIF4 and its binding partner PRC1 in organized central spindle midzone formation." Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K. EMBO J. 23:3237-3248(2004) [PubMed: 15297875] [Abstract] Cited for: INTERACTION WITH PRC1.
[6]	"Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis." Tomas A., Futter C., Moss S.E. J. Cell Biol. 165:813-822(2004) [PubMed: 15197175] [Abstract] Cited for: INTERACTION WITH ANXA11, SUBCELLULAR LOCATION.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"An ECT2-centralspindlin complex regulates the localization and function of RhoA." Yuce O., Piekny A., Glotzer M. J. Cell Biol. 170:571-582(2005) [PubMed: 16103226] [Abstract] Cited for: FUNCTION, INTERACTION WITH RACGAP1.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, MASS SPECTROMETRY.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-814; SER-867 AND SER-902, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Dissecting the role of Rho-mediated signaling in contractile ring formation." Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T. Mol. Biol. Cell 17:43-55(2006) [PubMed: 16236794] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH ECT2 AND RACGAP1, SUBCELLULAR LOCATION.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450 AND THR-738, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-682; SER-684; SER-911 AND SER-912, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682; SER-684; SER-867 AND SER-934, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682; SER-684; SER-686; SER-911; SER-912 AND THR-913, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-450; THR-738; THR-861; SER-867 AND SER-902, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-738, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation." Wolfe B.A., Takaki T., Petronczki M., Glotzer M. PLoS Biol. 7:E1000110-E1000110(2009) [PubMed: 19468300] [Abstract] Cited for: INTERACTION WITH ECT2.
[20]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X67155 mRNA. Translation: CAA47628.2. BC017705 mRNA. Translation: AAH17705.2. BC051826 mRNA. Translation: AAH51826.1.
IPI	IPI00291579. IPI00293884.
PIR	S28262.
RefSeq	NP_004847.2. NM_004856.5. NP_612565.1. NM_138555.2.
UniGene	Hs.270845.
3D structure databases
ProteinModelPortal	Q02241.
SMR	Q02241. Positions 23-443.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-40359N.
IntAct	Q02241. 10 interactions.
MINT	MINT-1631617.
STRING	Q02241.
PTM databases
PhosphoSite	Q02241.
Polymorphism databases
DMDM	118572664.
Proteomic databases
PRIDE	Q02241.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260363; ENSP00000260363; ENSG00000137807.
GeneID	9493.
KEGG	hsa:9493.
NMPDR	fig|9606.3.peg.10905.
UCSC	uc002asb.1. human. uc002asc.1. human.
Organism-specific databases
CTD	9493.
GeneCards	GC15P069706.
HGNC	HGNC:6392. KIF23.
HPA	CAB010414.
MIM	605064. gene.
neXtProt	NX_Q02241.
PharmGKB	PA30181.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04923.
GeneTree	ENSGT00530000063172.
HOGENOM	HBG383437.
HOVERGEN	HBG052253.
InParanoid	Q02241.
OMA	RDSKITH.
PhylomeDB	Q02241.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling.
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q02241.
Bgee	Q02241.
CleanEx	HS_KIF23.
Genevestigator	Q02241.
GermOnline	ENSG00000137807. Homo sapiens.
Family and domain databases
InterPro	IPR019821. Kinesin_motor_CS. IPR001752. Kinesin_motor_dom. [Graphical view]
Gene3D	G3DSA:3.40.850.10. kinesin_motor. 2 hits.
KO	K10402.
Pfam	PF00225. Kinesin. 1 hit. [Graphical view]
PRINTS	PR00380. KINESINHEAVY.
SMART	SM00129. KISc. 1 hit. [Graphical view]
PROSITE	PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit. PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35566.
SOURCE	Search...

Entry information

Entry name

KIF23_HUMAN

Accession

Primary (citable) accession number: Q02241
Secondary accession number(s): Q8WVP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 28, 2006
Last modified:	January 25, 2012
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.