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Reviewed, UniProtKB/Swiss-Prot Q02241 (KIF23_HUMAN)

Last modified July 22, 2008. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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)
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.
Sequence processingThe displayed sequence is not processed.
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.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the kinesin-like protein family.

Contains 1 kinesin-motor domain.

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Ontologies

Keywords

   Biological processCell cycle
Cell division
Mitosis
   Cellular componentMicrotubule
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processmitotic spindle elongation Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentkinesin complex Ref.1

Traceable author statement. Source: ProtInc

nucleoplasm

Inferred from Experiment. Source: Reactome

spindle Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionmicrotubule motor activity Ref.1

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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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 view

Molecule processing

Chain1 – 960960Kinesin-like protein KIF23

Regions

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

Amino acid modifications

Modified residue291Phosphotyrosine
Modified residue1551Phosphoserine
Modified residue1601Phosphoserine
Modified residue4501Phosphothreonine
Modified residue6821Phosphoserine
Modified residue6841Phosphoserine
Modified residue6861Phosphoserine
Modified residue7381Phosphothreonine
Modified residue8141Phosphoserine
Modified residue8671Phosphoserine
Modified residue9021Phosphoserine
Modified residue9111Phosphoserine
Modified residue9121Phosphoserine
Modified residue9131Phosphothreonine

Natural variations

Alternative sequence690 – 793104Missing in isoform 2.

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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 [UniParc].

Checksum: DDE7CEB480ABE58A
Show »

85698,105

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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]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X67155 mRNA. Translation: CAA47628.2.
BC017705 mRNA. Translation: AAH17705.2.
BC051826 mRNA. Translation: AAH51826.1.
PIRS28262.
RefSeqNP_004847.2.
NP_612565.1.
UniGeneHs.270845

3D structure databases

HSSPHSSP built from PDB template 1F9W based on UniProtKB P17119.
ModBaseSearch...

Protein-protein interaction databases

IntActQ02241.

PTM databases

PhosphoSiteQ02241.

Genome annotation databases

EnsemblENSG00000137807. Homo sapiens. [Contig view]
GeneID9493.
KEGGhsa:9493.
NMPDRfig|9606.3.peg.10905.

Organism-specific databases

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

Phylogenomic databases

HOVERGENQ02241.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpressQ02241.
CleanExHS_KIF23.
GermOnlineENSG00000137807. Homo sapiens.

Family and domain databases

InterProIPR001752. Kinesin_motor.
[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]
ProDomQ02241.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubQ02241.
SOURCESearch...
ProtoNetSearch...

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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: July 22, 2008
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 15

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

MIM cross-references

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents