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

O00139 (KIF2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF2A
Alternative name(s):
Kinesin-2
Short name=hK2
Gene names
Name:KIF2A
Synonyms:KIF2, KNS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length706 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity. Ref.8 Ref.9 Ref.10

Subunit structure

Interacts with AURKA, PSRC1 and PLK1. Ref.10 Ref.11

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole. Cytoplasmcytoskeletonspindle. Note: Localized to the spindle microtubules and spindle poles from prophase to metaphase. Efficient targeting to spindle microtubules and spindle poles requires the kinase activity of PLK1. Recruited to mitotic spindles by interaction with PSRC1. Ref.10 Ref.11

Involvement in disease

Cortical dysplasia, complex, with other brain malformations 3 (CDCBM3) [MIM:615411]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include early-onset epilepsy, and various malformations of cortical development such as agyria, posterior or frontal pachygyria, subcortical band heterotopia, and thin corpus callosum.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Miscellaneous

HeLa cells lacking KIF2A show asymmetric or monopolar mitotic spindles. Osteosarcoma cells (U2OS) lacking KIF2A or KIF2B show disorganised or monopolar mitotic spindles.

Sequence similarities

Belongs to the kinesin-like protein family. MCAK/KIF2 subfamily.

Contains 1 kinesin-motor domain.

Sequence caution

The sequence AAP84320.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
Mitosis
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Motor protein
   PTMAcetylation
Phosphoprotein
   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 differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

metabolic process

Traceable author statement Ref.1. Source: GOC

microtubule-based movement

Traceable author statement. Source: Reactome

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic spindle organization

Inferred from direct assay Ref.10. Source: UniProtKB

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

kinesin complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule motor activity

Inferred from electronic annotation. Source: InterPro

motor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: O00139-3)

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 1 (identifier: O00139-1)

Also known as: HK2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
Isoform 2 (identifier: O00139-2)

Also known as: HK2s;

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
     134-153: GSVSDISPVQAAKKEFGPPS → A
Isoform 4 (identifier: O00139-4)

The sequence of this isoform differs from the canonical sequence as follows:
     552-552: E → EFGISPSDIPFSQGSGSRPDLSPSYEYDDFSPSVTRVKE
Note: Contains a phosphoserine at position 579 (By similarity). No experimental confirmation available.
Isoform 5 (identifier: O00139-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MATANFGKIQIGIYVEIKRSD → M
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 706706Kinesin-like protein KIF2A
PRO_0000125414

Regions

Domain218 – 552335Kinesin-motor
Nucleotide binding313 – 3208ATP
Region1 – 217217Globular Potential
Coiled coil660 – 69940 Potential

Amino acid modifications

Modified residue751Phosphoserine Ref.12
Modified residue781Phosphothreonine Ref.12
Modified residue1021N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 2727Missing in isoform 1 and isoform 2.
VSP_028374
Alternative sequence1 – 2121MATAN…IKRSD → M in isoform 5.
VSP_047373
Alternative sequence134 – 15320GSVSD…FGPPS → A in isoform 2.
VSP_028375
Alternative sequence5521E → EFGISPSDIPFSQGSGSRPD LSPSYEYDDFSPSVTRVKE in isoform 4.
VSP_028376
Natural variant3171S → N in CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein. Ref.15
VAR_070575
Natural variant3211H → D in CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein. Ref.15
VAR_070576

Experimental info

Sequence conflict1431Q → H in AAP84320. Ref.7
Sequence conflict1531S → SHLFFSA in AAP84320. Ref.7
Sequence conflict2951R → K in CAA69621. Ref.1

Secondary structure

...................................................... 706
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified October 2, 2007. Version 3.
Checksum: A407D84B6BD04ACF

FASTA70679,955
        10         20         30         40         50         60 
MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF 

        70         80         90        100        110        120 
SLNPDLVPDE EIEPSPETPP PPASSAKVNK IVKNRRTVAS IKNDPPSRDN RVVGSARARP 

       130        140        150        160        170        180 
SQFPEQSSSA QQNGSVSDIS PVQAAKKEFG PPSRRKSNCV KEVEKLQEKR EKRRLQQQEL 

       190        200        210        220        230        240 
REKRAQDVDA TNPNYEIMCM IRDFRGSLDY RPLTTADPID EHRICVCVRK RPLNKKETQM 

       250        260        270        280        290        300 
KDLDVITIPS KDVVMVHEPK QKVDLTRYLE NQTFRFDYAF DDSAPNEMVY RFTARPLVET 

       310        320        330        340        350        360 
IFERGMATCF AYGQTGSGKT HTMGGDFSGK NQDCSKGIYA LAARDVFLML KKPNYKKLEL 

       370        380        390        400        410        420 
QVYATFFEIY SGKVFDLLNR KTKLRVLEDG KQQVQVVGLQ EREVKCVEDV LKLIDIGNSC 

       430        440        450        460        470        480 
RTSGQTSANA HSSRSHAVFQ IILRRKGKLH GKFSLIDLAG NERGADTSSA DRQTRLEGAE 

       490        500        510        520        530        540 
INKSLLALKE CIRALGRNKP HTPFRASKLT QVLRDSFIGE NSRTCMIATI SPGMASCENT 

       550        560        570        580        590        600 
LNTLRYANRV KELTVDPTAA GDVRPIMHHP PNQIDDLETQ WGVGSSPQRD DLKLLCEQNE 

       610        620        630        640        650        660 
EEVSPQLFTF HEAVSQMVEM EEQVVEDHRA VFQESIRWLE DEKALLEMTE EVDYDVDSYA 

       670        680        690        700 
TQLEAILEQK IDILTELRDK VKSFRAALQE EEQASKQINP KRPRAL 

« Hide

Isoform 1 (HK2) [UniParc].

Checksum: ABB522C323822AF6
Show »

FASTA67976,955
Isoform 2 (HK2s) [UniParc].

Checksum: 8975B0872C83FED9
Show »

FASTA66075,043
Isoform 4 [UniParc].

Checksum: 9948FA52D473F3B0
Show »

FASTA74484,089
Isoform 5 [UniParc].

Checksum: A7845ECBC1EDA7D9
Show »

FASTA68677,749

References

« Hide 'large scale' references
[1]"Identification of a novel human kinesin-related gene (HK2) by the cDNA differential display technique."
Debernardi S., Fontanella E., de Gregorio L., Pierotti M.A., Delia D.
Genomics 42:67-73(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
Tissue: Fetal brain and Salivary gland.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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 1).
Tissue: Brain.
[7]Sha J.H., Zhou Z.M., Li J.M.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-706 (ISOFORMS 1/3).
Tissue: Testis.
[8]"Functional analysis of human microtubule-based motor proteins, the kinesins and dyneins, in mitosis/cytokinesis using RNA interference."
Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B., Abraham R.T., Jiang W.
Mol. Biol. Cell 16:3187-3199(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles during mitosis in human cells."
Manning A.L., Ganem N.J., Bakhoum S.F., Wagenbach M., Wordeman L., Compton D.A.
Mol. Biol. Cell 18:2970-2979(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"DDA3 recruits microtubule depolymerase Kif2a to spindle poles and controls spindle dynamics and mitotic chromosome movement."
Jang C.Y., Wong J., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
J. Cell Biol. 181:255-267(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PSRC1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a."
Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLK1 AND AURKA, SUBCELLULAR LOCATION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND THR-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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].
[14]"Crystal structure of the human KIF2 motor domain in complex with ADP."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 153-553 IN COMPLEX WITH ADP.
[15]"Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of cortical development and microcephaly."
Poirier K., Lebrun N., Broix L., Tian G., Saillour Y., Boscheron C., Parrini E., Valence S., Pierre B.S., Oger M., Lacombe D., Genevieve D., Fontana E., Darra F., Cances C., Barth M., Bonneau D., Bernadina B.D. expand/collapse author list , N'guyen S., Gitiaux C., Parent P., des Portes V., Pedespan J.M., Legrez V., Castelnau-Ptakine L., Nitschke P., Hieu T., Masson C., Zelenika D., Andrieux A., Francis F., Guerrini R., Cowan N.J., Bahi-Buisson N., Chelly J.
Nat. Genet. 45:639-647(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDCBM3 ASN-317 AND ASP-321, CHARACTERIZATION OF VARIANTS CDCBM3 ASN-317 AND ASP-321.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08319 mRNA. Translation: CAA69621.1.
AK302270 mRNA. Translation: BAG63616.1.
EF560716 mRNA. Translation: ABQ59026.1.
EF560728 mRNA. Translation: ABQ59038.1.
AC016637 Genomic DNA. No translation available.
AC034242 Genomic DNA. No translation available.
AC114982 Genomic DNA. No translation available.
CH471137 Genomic DNA. Translation: EAW51388.1.
CH471137 Genomic DNA. Translation: EAW51390.1.
BC031828 mRNA. Translation: AAH31828.1.
AY317140 mRNA. Translation: AAP84320.1. Different initiation.
RefSeqNP_001091981.1. NM_001098511.2.
NP_001230881.1. NM_001243952.1.
NP_004511.2. NM_004520.4.
UniGeneHs.558351.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GRYX-ray2.35A153-553[»]
ProteinModelPortalO00139.
SMRO00139. Positions 162-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109997. 6 interactions.
IntActO00139. 3 interactions.
MINTMINT-2997391.
STRING9606.ENSP00000385000.

PTM databases

PhosphoSiteO00139.

Proteomic databases

PaxDbO00139.
PRIDEO00139.

Protocols and materials databases

DNASU3796.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381103; ENSP00000370493; ENSG00000068796. [O00139-5]
ENST00000401507; ENSP00000385622; ENSG00000068796. [O00139-3]
ENST00000407818; ENSP00000385000; ENSG00000068796. [O00139-4]
ENST00000506857; ENSP00000423772; ENSG00000068796. [O00139-2]
GeneID3796.
KEGGhsa:3796.
UCSCuc003jsy.4. human. [O00139-3]
uc003jsz.4. human. [O00139-4]
uc010iwp.3. human. [O00139-2]

Organism-specific databases

CTD3796.
GeneCardsGC05P061601.
H-InvDBHIX0020778.
HGNCHGNC:6318. KIF2A.
HPAHPA004716.
MIM602591. gene.
615411. phenotype.
neXtProtNX_O00139.
PharmGKBPA162393356.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000231329.
HOVERGENHBG003875.
KOK10393.
OMANKKETVM.
OrthoDBEOG7K9K2C.
PhylomeDBO00139.
TreeFamTF105222.

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

ArrayExpressO00139.
BgeeO00139.
CleanExHS_KIF2A.
GenevestigatorO00139.

Family and domain databases

Gene3D3.40.850.10. 1 hit.
InterProIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO00139.
GeneWikiKIF2A.
GenomeRNAi3796.
NextBio14903.
PROO00139.
SOURCESearch...

Entry information

Entry nameKIF2A_HUMAN
AccessionPrimary (citable) accession number: O00139
Secondary accession number(s): A5YM42 expand/collapse secondary AC list , A5YM54, B4DY54, D3DW97, E9PB70, Q7Z5I3, Q8N5Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 125 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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