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Q02241 (KIF23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF23
Alternative name(s):
Kinesin-like protein 5
Mitotic kinesin-like protein 1
Gene names
Name:KIF23
Synonyms:KNSL5, MKLP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length960 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7 Ref.9

Subunit structure

Heterotetramer 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. Interacts with BIRC6/bruce and USP8/UBPY. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.11 Ref.14

Subcellular location

Nucleus. Cytoplasm › cytoskeleton › spindle. Note: Localizes to the interzone of mitotic spindles. Ref.6 Ref.9

Post-translational modification

Ubiquitinated. Deubiquitinated by USP8/UBPY. Ref.11

Sequence similarities

Belongs to the kinesin-like protein family.

Contains 1 kinesin-motor domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell cycle cytokinesis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

microtubule-based movement

Traceable author statement. Source: Reactome

mitotic spindle elongation

Traceable author statement Ref.1. Source: ProtInc

positive regulation of cell cycle cytokinesis

Inferred from mutant phenotype Ref.7. Source: UniProtKB

spindle midzone assembly involved in mitosis

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentcentralspindlin complex

Inferred from direct assay Ref.4Ref.9. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 20186884. Source: MGI

cytosol

Traceable author statement. Source: Reactome

intercellular bridge

Inferred from electronic annotation. Source: Compara

kinesin complex

Traceable author statement Ref.1. 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_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from direct assay Ref.4. Source: UniProtKB

microtubule motor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BIRC6Q9NR094EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 960960Kinesin-like protein KIF23
PRO_0000125434

Regions

Domain1 – 352352Kinesin-motor
Nucleotide binding112 – 1198ATP By similarity
Coiled coil535 – 62086 Potential
Motif7 – 115Nuclear localization signal Potential

Amino acid modifications

Modified residue1551Phosphoserine Ref.8
Modified residue1601Phosphoserine Ref.13
Modified residue6051Phosphoserine Ref.18
Modified residue7381Phosphothreonine Ref.13
Modified residue8141Phosphoserine Ref.8
Modified residue8671Phosphoserine Ref.8 Ref.13 Ref.16
Modified residue9021Phosphoserine Ref.8 Ref.13

Natural variations

Alternative sequence690 – 793104Missing in isoform 2.
VSP_021801
Natural variant5151F → L.
Corresponds to variant rs17310879 [ dbSNP | Ensembl ].
VAR_049686

Secondary structure

1 ................. 960
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 3.
Checksum: B2AA784D2D236A90

FASTA960110,059
        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

« Hide

Isoform 2 [UniParc].

Checksum: DDE7CEB480ABE58A
Show »

FASTA85698,105

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANXA11, SUBCELLULAR LOCATION.
[7]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RACGAP1.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-814; SER-867 AND SER-902, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH ECT2 AND RACGAP1, SUBCELLULAR LOCATION.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
Pohl C., Jentsch S.
Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION, INTERACTION WITH BIRC6/BRUCE AND USP8/UBPY.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-738; SER-867 AND SER-902, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ECT2.
[15]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, MASS SPECTROMETRY.
+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.
IPIIPI00291579.
IPI00293884.
PIRS28262.
RefSeqNP_004847.2. NM_004856.5.
NP_612565.1. NM_138555.2.
UniGeneHs.270845.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VHXX-ray2.81B/D/F/H794-911[»]
ProteinModelPortalQ02241.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-40359N.
IntActQ02241. 10 interactions.
MINTMINT-1631617.
STRING9606.ENSP00000260363.

PTM databases

PhosphoSiteQ02241.

Polymorphism databases

DMDM118572664.

Proteomic databases

PaxDbQ02241.
PRIDEQ02241.

Protocols and materials databases

DNASU9493.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260363; ENSP00000260363; ENSG00000137807.
ENST00000352331; ENSP00000304978; ENSG00000137807.
ENST00000559279; ENSP00000453386; ENSG00000137807.
GeneID9493.
KEGGhsa:9493.
UCSCuc002asb.3. human.
uc002asc.3. human.

Organism-specific databases

CTD9493.
GeneCardsGC15P069706.
HGNCHGNC:6392. KIF23.
HPACAB010414.
MIM605064. gene.
neXtProtNX_Q02241.
PharmGKBPA30181.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000273893.
HOVERGENHBG052253.
InParanoidQ02241.
KOK10402.
OMAIHESSID.
PhylomeDBQ02241.

Enzyme and pathway databases

Pathway_Interaction_DBaurora_b_pathway. Aurora B signaling.
ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ02241.
BgeeQ02241.
CleanExHS_KIF23.
GenevestigatorQ02241.
GermOnlineENSG00000137807. Homo sapiens.

Family and domain databases

Gene3D3.40.850.10. 2 hits.
InterProIPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
[Graphical view]
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ02241.
ChEMBLCHEMBL5899.
GenomeRNAi9493.
NextBio35566.
SOURCESearch...

Entry information

Entry nameKIF23_HUMAN
AccessionPrimary (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: May 1, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

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Human chromosome 15: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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