Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O95235 (KI20A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF20A
Alternative name(s):
GG10_2
Mitotic kinesin-like protein 2
Short name=MKlp2
Rab6-interacting kinesin-like protein
Rabkinesin-6
Gene names
Name:KIF20A
Synonyms:MKLP2, RAB6KIFL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length890 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility. Ref.5

Subcellular location

Golgi apparatus By similarity. Cytoplasmcytoskeletonspindle Ref.5.

Post-translational modification

Phosphorylated by PLK1 at Ser-528 during mitosis, creating a docking site for PLK1 and recruiting PLK1 at central spindle. Ref.5

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.

Contains 1 kinesin motor domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Cytoskeleton
Golgi apparatus
Microtubule
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis

Inferred from direct assay Ref.5. Source: UniProtKB

microtubule bundle formation

Inferred from direct assay Ref.5. Source: UniProtKB

microtubule-based movement

Inferred from electronic annotation. Source: InterPro

mitotic cell cycle

Traceable author statement. Source: Reactome

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle-mediated transport

Traceable author statement PubMed 9438855. Source: ProtInc

   Cellular_componentGolgi apparatus

Traceable author statement PubMed 9438855. Source: ProtInc

kinesin complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoplasm

Traceable author statement. Source: Reactome

spindle

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule motor activity

Inferred from electronic annotation. Source: InterPro

protein kinase binding

Inferred from physical interaction Ref.5. Source: UniProtKB

transporter activity

Traceable author statement PubMed 9438855. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 890889Kinesin-like protein KIF20A
PRO_0000125460

Regions

Domain64 – 507444Kinesin motor
Nucleotide binding160 – 1678ATP By similarity
Region763 – 890128Globular Potential
Coiled coil611 – 762152 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.11
Modified residue71Phosphoserine Ref.11
Modified residue141Phosphoserine Ref.11
Modified residue211Phosphoserine Ref.11
Modified residue5281Phosphoserine; by PLK1 Ref.5 Ref.10
Modified residue5321Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue6621Phosphoserine Ref.5
Modified residue6681Phosphoserine Ref.5
Modified residue8251Phosphoserine Ref.11
Modified residue8571Phosphothreonine Ref.10
Modified residue8671Phosphoserine Ref.10

Natural variations

Natural variant631E → K.
Corresponds to variant rs3734116 [ dbSNP | Ensembl ].
VAR_049704
Natural variant8391P → L.
Corresponds to variant rs3172747 [ dbSNP | Ensembl ].
VAR_049705

Experimental info

Mutagenesis5281S → A: Impairs phosphorylation by PLK1 and recruitment of PLK1 to the spindle. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O95235 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 6620264615496051

FASTA890100,278
        10         20         30         40         50         60 
MSQGILSPPA GLLSDDDVVV SPMFESTAAD LGSVVRKNLL SDCSVVSTSL EDKQQVPSED 

        70         80         90        100        110        120 
SMEKVKVYLR VRPLLPSELE RQEDQGCVRI ENVETLVLQA PKDSFALKSN ERGIGQATHR 

       130        140        150        160        170        180 
FTFSQIFGPE VGQASFFNLT VKEMVKDVLK GQNWLIYTYG VTNSGKTHTI QGTIKDGGIL 

       190        200        210        220        230        240 
PRSLALIFNS LQGQLHPTPD LKPLLSNEVI WLDSKQIRQE EMKKLSLLNG GLQEEELSTS 

       250        260        270        280        290        300 
LKRSVYIESR IGTSTSFDSG IAGLSSISQC TSSSQLDETS HRWAQPDTAP LPVPANIRFS 

       310        320        330        340        350        360 
IWISFFEIYN ELLYDLLEPP SQQRKRQTLR LCEDQNGNPY VKDLNWIHVQ DAEEAWKLLK 

       370        380        390        400        410        420 
VGRKNQSFAS THLNQNSSRS HSIFSIRILH LQGEGDIVPK ISELSLCDLA GSERCKDQKS 

       430        440        450        460        470        480 
GERLKEAGNI NTSLHTLGRC IAALRQNQQN RSKQNLVPFR DSKLTRVFQG FFTGRGRSCM 

       490        500        510        520        530        540 
IVNVNPCAST YDETLHVAKF SAIASQLVHA PPMQLGFPSL HSFIKEHSLQ VSPSLEKGAK 

       550        560        570        580        590        600 
ADTGLDDDIE NEADISMYGK EELLQVVEAM KTLLLKERQE KLQLEMHLRD EICNEMVEQM 

       610        620        630        640        650        660 
QQREQWCSEH LDTQKELLEE MYEEKLNILK ESLTSFYQEE IQERDEKIEE LEALLQEARQ 

       670        680        690        700        710        720 
QSVAHQQSGS ELALRRSQRL AASASTQQLQ EVKAKLQQCK AELNSTTEEL HKYQKMLEPP 

       730        740        750        760        770        780 
PSAKPFTIDV DKKLEEGQKN IRLLRTELQK LGESLQSAER ACCHSTGAGK LRQALTTCDD 

       790        800        810        820        830        840 
ILIKQDQTLA ELQNNMVLVK LDLRKKAACI AEQYHTVLKL QGQVSAKKRL GTNQENQQPN 

       850        860        870        880        890 
QQPPGKKPFL RNLLPRTPTC QSSTDCSPYA RILRSRRSPL LKSGPFGKKY 

« Hide

References

« Hide 'large scale' references
[1]"Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes."
Horrevoets A.J.G., Fontijn R.D., van Zonneveld A.J., de Vries C.J.M., ten Cate J.W., Pannekoek H.
Blood 93:3418-3431(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endothelial cell.
[2]"cDNA cloning, expression pattern, genomic structure and chromosomal location of RAB6KIFL, a human kinesin-like gene."
Lai F., Fernald A.A., Zhao N., Le Beau M.M.
Gene 248:117-125(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Uterus.
[5]"Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis."
Neef R., Preisinger C., Sutcliffe J., Kopajtich R., Nigg E.A., Mayer T.U., Barr F.A.
J. Cell Biol. 162:863-875(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-528; SER-662 AND SER-668, MUTAGENESIS OF SER-528, FUNCTION.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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.
[8]"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.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-528; SER-532; THR-857 AND SER-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-14; SER-21; SER-532 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-532, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF070672 mRNA. Translation: AAC83230.1.
AF153329 mRNA. Translation: AAD37806.1.
CH471062 Genomic DNA. Translation: EAW62157.1.
CH471062 Genomic DNA. Translation: EAW62158.1.
BC012999 mRNA. Translation: AAH12999.1.
CCDSCCDS4199.1.
RefSeqNP_005724.1. NM_005733.2.
XP_006714577.1. XM_006714514.1.
UniGeneHs.718626.

3D structure databases

ProteinModelPortalO95235.
SMRO95235. Positions 56-516.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115418. 11 interactions.
IntActO95235. 3 interactions.
MINTMINT-4989469.
STRING9606.ENSP00000378356.

Chemistry

ChEMBLCHEMBL2021753.

PTM databases

PhosphoSiteO95235.

Proteomic databases

MaxQBO95235.
PaxDbO95235.
PeptideAtlasO95235.
PRIDEO95235.

Protocols and materials databases

DNASU10112.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394894; ENSP00000378356; ENSG00000112984.
GeneID10112.
KEGGhsa:10112.
UCSCuc003lcj.3. human.

Organism-specific databases

CTD10112.
GeneCardsGC05P137542.
HGNCHGNC:9787. KIF20A.
HPAHPA036909.
HPA036910.
MIM605664. gene.
neXtProtNX_O95235.
PharmGKBPA34149.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000054207.
HOVERGENHBG052246.
InParanoidO95235.
KOK10402.
OMARLCEDQN.
OrthoDBEOG74BJR9.
PhylomeDBO95235.
TreeFamTF105232.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressO95235.
BgeeO95235.
CleanExHS_KIF20A.
GenevestigatorO95235.

Family and domain databases

Gene3D3.40.850.10. 2 hits.
InterProIPR027326. KIF20A.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PTHR24115:SF352. PTHR24115:SF352. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKIF20A.
GenomeRNAi10112.
NextBio38255.
PROO95235.
SOURCESearch...

Entry information

Entry nameKI20A_HUMAN
AccessionPrimary (citable) accession number: O95235
Secondary accession number(s): D3DQB6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 126 of the entry and version 1 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM