Kinesin-like protein KIF20A - Homo sapiens (Human)

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O95235 (KI20A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	890 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › spindle 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 kinesin-like protein family. Contains 1 kinesin-motor domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Cytoskeleton Golgi apparatus Microtubule
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	M phase of mitotic cell cycle Traceable author statement. Source: Reactome cytokinesis 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 protein transport Inferred from electronic annotation. Source: UniProtKB-KW vesicle-mediated transport Traceable author statement PubMed 9438855. Source: ProtInc
Cellular_component	Golgi apparatus Traceable author statement PubMed 9438855. Source: ProtInc microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Inferred from electronic annotation. Source: InterPro nucleoplasm Traceable author statement. Source: Reactome spindle Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule motor activity Inferred from electronic annotation. Source: InterPro transporter activity Traceable author statement PubMed 9438855. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.11

Chain

2 – 890

889

Kinesin-like protein KIF20A

PRO_0000125460

Regions

Domain

70 – 495

426

Kinesin-motor

Nucleotide binding

160 – 167

ATP By similarity

Region

763 – 890

128

Globular Potential

Coiled coil

611 – 762

152

Potential

Amino acid modifications

Modified residue

N-acetylserine Ref.11

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphoserine Ref.11

Modified residue

528

Phosphoserine; by PLK1 Ref.5 Ref.10

Modified residue

532

Phosphoserine Ref.10 Ref.11 Ref.12

Modified residue

662

Phosphoserine Ref.5

Modified residue

668

Phosphoserine

Modified residue

825

Phosphoserine Ref.11

Modified residue

857

Phosphothreonine Ref.10

Modified residue

867

Phosphoserine Ref.10

Natural variations

Natural variant

E → K.
Corresponds to variant rs3734116 [ dbSNP | Ensembl ].

VAR_049704

Natural variant

839

P → L.
Corresponds to variant rs3172747 [ dbSNP | Ensembl ].

VAR_049705

Experimental info

Mutagenesis

528

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

Sequences

Sequence

Length

Mass (Da)

Tools

O95235 [UniParc].

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

FASTA

890

100,278

        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' referencesShow '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. 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 AND SER-662, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00029422.
RefSeq	NP_005724.1. NM_005733.2.
UniGene	Hs.718626.
3D structure databases
ProteinModelPortal	O95235.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95235. 3 interactions.
MINT	MINT-4989469.
STRING	9606.ENSP00000378356.
PTM databases
PhosphoSite	O95235.
Proteomic databases
PaxDb	O95235.
PeptideAtlas	O95235.
PRIDE	O95235.
Protocols and materials databases
DNASU	10112.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000394894; ENSP00000378356; ENSG00000112984.
GeneID	10112.
KEGG	hsa:10112.
UCSC	uc003lcj.3. human.
Organism-specific databases
CTD	10112.
GeneCards	GC05P137542.
HGNC	HGNC:9787. KIF20A.
HPA	HPA036909. HPA036910.
MIM	605664. gene.
neXtProt	NX_O95235.
PharmGKB	PA34149.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5059.
HOGENOM	HOG000054207.
HOVERGEN	HBG052246.
InParanoid	O95235.
KO	K10402.
OMA	VKVYLRV.
OrthoDB	EOG4VT5WT.
PhylomeDB	O95235.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling.
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	O95235.
Bgee	O95235.
CleanEx	HS_KIF20A.
Genevestigator	O95235.
GermOnline	ENSG00000112984. Homo sapiens.
Family and domain databases
Gene3D	3.40.850.10. 2 hits.
InterPro	IPR027326. KIF20A. IPR019821. Kinesin_motor_CS. IPR001752. Kinesin_motor_dom. IPR027417. P-loop_NTPase. [Graphical view]
PANTHER	PTHR24115:SF227. PTHR24115:SF227. 1 hit.
Pfam	PF00225. Kinesin. 1 hit. [Graphical view]
PRINTS	PR00380. KINESINHEAVY.
SMART	SM00129. KISc. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
PROSITE	PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit. PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10112.
NextBio	38255.
SOURCE	Search...

Entry information

Entry name

KI20A_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 114 of the entry and version 1 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.

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents