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Reviewed, UniProtKB/Swiss-Prot Q02241 (KIF23_HUMAN)

Last modified January 19, 2010. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

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

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Protein attributes

Sequence length960 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro. Localizes to the interzone of mitotic spindles.

Subunit structure

Interacts with PRC1. Interacts with ANXA11 during cytokinesis. Ref.4 Ref.5

Subcellular location

Nucleus. Cytoplasm › cytoskeleton › spindle Ref.5.

Sequence similarities

Belongs to the kinesin-like protein family.

Contains 1 kinesin-motor domain.

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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.

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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 residue291Phosphotyrosine Ref.7
Modified residue1551Phosphoserine Ref.8
Modified residue1601Phosphoserine Ref.10 Ref.14
Modified residue4501Phosphothreonine Ref.14 Ref.9
Modified residue6821Phosphoserine Ref.10 Ref.12 Ref.13
Modified residue6841Phosphoserine Ref.10 Ref.12 Ref.13 Ref.6
Modified residue6861Phosphoserine Ref.13 Ref.11
Modified residue7381Phosphothreonine Ref.14 Ref.9 Ref.15
Modified residue8141Phosphoserine Ref.8
Modified residue8611Phosphothreonine Ref.14
Modified residue8671Phosphoserine Ref.8 Ref.14 Ref.12 Ref.16
Modified residue9021Phosphoserine Ref.8 Ref.14
Modified residue9111Phosphoserine Ref.10 Ref.13
Modified residue9121Phosphoserine Ref.10 Ref.13
Modified residue9131Phosphothreonine Ref.13
Modified residue9341Phosphoserine Ref.12

Natural variations

Alternative sequence690 – 793104Missing in isoform 2.
VSP_021801
Natural variant5151F → L: dbSNP rs17310879.
VAR_049686

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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.

Checksum: DDE7CEB480ABE58A
Show »

FASTA85698,105

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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: 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]"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.
[5]"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.
[6]"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: Epithelium.
[7]"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.
[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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-814; SER-867 AND SER-902, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"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: Epithelium.
[10]"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: Epithelium.
[11]"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: Epithelium.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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: T-cell.
+Additional computationally mapped references.

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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.
NP_612565.1.
UniGeneHs.270845

3D structure databases

SMRQ02241. Positions 24-435.
ModBaseSearch...

Protein-protein interaction databases

IntActQ02241. 8 interactions.
STRINGQ02241.

PTM databases

PhosphoSiteQ02241.

Proteomic databases

PRIDEQ02241.

Genome annotation databases

EnsemblENST00000260363; ENSP00000260363; ENSG00000137807; Homo sapiens. [Genome view]
GeneID9493.
KEGGhsa:9493.
NMPDRfig|9606.3.peg.10905.
UCSCuc002asb.1. human.
uc002asc.1. human.

Organism-specific databases

CTD9493.
GeneCardsGC15P067493.
H-InvDBHIX0012389.
HGNCHGNC:6392. KIF23.
HPACAB010414.
MIM605064. gene.
PharmGKBPA30181.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04923.
HOGENOMHBG383437.
HOVERGENQ02241.
InParanoidQ02241.
OMAYNTPLNV.
OrthoDBEOG91RSFC.
PhylomeDBQ02241.

Enzyme and pathway databases

Pathway_Interaction_DBaurora_b_pathway. Aurora B signaling.
ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

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

Family and domain databases

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 Resources

NextBio35566.
SOURCESearch...

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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: January 19, 2010
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents