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Q9Y496 (KIF3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF3A
Alternative name(s):
Microtubule plus end-directed kinesin motor 3A
Gene names
Name:KIF3A
Synonyms:KIF3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation By similarity.

Subunit structure

Heterodimer of KIF3A and KIF3B. Interacts with PIFO. Interacts with CLN3. Ref.6 Ref.9

Subcellular location

Cytoplasmcytoskeleton Probable. Cell projectioncilium By similarity.

Sequence similarities

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

Contains 1 kinesin motor domain.

Sequence caution

The sequence AAC04475.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAD93017.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCell projection
Cilium
Cytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cilium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

determination of left/right symmetry

Inferred from electronic annotation. Source: Ensembl

dorsal/ventral neural tube patterning

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

membrane organization

Traceable author statement. Source: Reactome

metabolic process

Traceable author statement PubMed 16298999. Source: GOC

microtubule-based movement

Traceable author statement. Source: Reactome

organelle organization

Traceable author statement PubMed 1447303. Source: ProtInc

plus-end-directed vesicle transport along microtubule

Traceable author statement PubMed 16298999. Source: BHF-UCL

positive regulation of receptor-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from direct assay PubMed 16298999. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

kinesin II complex

Inferred from direct assay PubMed 16298999. Source: BHF-UCL

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule cytoskeleton

Inferred from direct assay PubMed 16298999. Source: BHF-UCL

neuron projection

Inferred from electronic annotation. Source: Ensembl

photoreceptor connecting cilium

Inferred from electronic annotation. Source: Ensembl

primary cilium

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

plus-end-directed microtubule motor activity

Traceable author statement PubMed 16298999. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.6Ref.9. Source: UniProtKB

spectrin binding

Inferred from direct assay PubMed 23704327. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DISC1Q9NRI53EBI-1104844,EBI-529989

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 699699Kinesin-like protein KIF3A
PRO_0000125393

Regions

Domain14 – 345332Kinesin motor
Nucleotide binding100 – 1078ATP By similarity
Region697 – 6993Globular
Coiled coil355 – 590236 Potential

Amino acid modifications

Modified residue6871Phosphoserine Ref.5 Ref.7

Natural variations

Natural variant1721K → I. Ref.4
Corresponds to variant rs17854353 [ dbSNP | Ensembl ].
VAR_055319

Experimental info

Sequence conflict1511E → G in AAH45542. Ref.4
Sequence conflict1701E → A in AAC72294. Ref.1
Sequence conflict4091R → RDQA in BAD93017. Ref.2
Sequence conflict4091R → RDQT in AAH45542. Ref.4
Sequence conflict4091R → RIQI in AAC72294. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y496 [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: A0BF5BB1F699DF12

FASTA69980,041
        10         20         30         40         50         60 
MPINKSEKPE SCDNVKVVVR CRPLNEREKS MCYKQAVSVD EMRGTITVHK TDSSNEPPKT 

        70         80         90        100        110        120 
FTFDTVFGPE SKQLDVYNLT ARPIIDSVLE GYNGTIFAYG QTGTGKTFTM EGVRAIPELR 

       130        140        150        160        170        180 
GIIPNSFAHI FGHIAKAEGD TRFLVRVSYL EIYNEEVRDL LGKDQTQRLE VKERPDVGVY 

       190        200        210        220        230        240 
IKDLSAYVVN NADDMDRIMT LGHKNRSVGA TNMNEHSSRS HAIFTITIEC SEKGIDGNMH 

       250        260        270        280        290        300 
VRMGKLHLVD LAGSERQAKT GATGQRLKEA TKINLSLSTL GNVISALVDG KSTHVPYRNS 

       310        320        330        340        350        360 
KLTRLLQDSL GGNSKTMMCA NIGPADYNYD ETISTLRYAN RAKNIKNKAR INEDPKDALL 

       370        380        390        400        410        420 
RQFQKEIEEL KKKLEEGEEI SGSDISGSEE DDDEEGEVGE DGEKRKKRRG KKKVSPDKMI 

       430        440        450        460        470        480 
EMQAKIDEER KALETKLDME EEERNKARAE LEKREKDLLK AQQEHQSLLE KLSALEKKVI 

       490        500        510        520        530        540 
VGGVDLLAKA EEQEKLLEES NMELEERRKR AEQLRRELEE KEQERLDIEE KYTSLQEEAQ 

       550        560        570        580        590        600 
GKTKKLKKVW TMLMAAKSEM ADLQQEHQRE IEGLLENIRQ LSRELRLQML IIDNFIPRDY 

       610        620        630        640        650        660 
QEMIENYVHW NEDIGEWQLK CVAYTGNNMR KQTPVPDKKE KDPFEVDLSH VYLAYTEESL 

       670        680        690 
RQSLMKLERP RTSKGKARPK TGRRKRSAKP ETVIDSLLQ 

« Hide

References

« Hide 'large scale' references
[1]"Photoreceptor localization of the KIF3A and KIF3B subunits of the heterotrimeric microtubule motor kinesin II in vertebrate retina."
Whitehead J.L., Wang S.Y., Bost-Usinger L., Hoang E., Frazer K.A., Burnside B.
Exp. Eye Res. 69:491-503(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"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].
[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], VARIANT ILE-172.
Tissue: Testis.
[5]"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-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIFO.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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].
[9]"Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments."
Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K., Neefjes J., Olkkonen V.M., Jalanko A.
Cell. Mol. Life Sci. 69:2075-2089(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLN3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041853 mRNA. Translation: AAC72294.1.
AB209780 mRNA. Translation: BAD93017.1. Different initiation.
AC004039 Genomic DNA. No translation available.
AC004237 Genomic DNA. Translation: AAC04475.1. Sequence problems.
BC045542 mRNA. Translation: AAH45542.1.
CCDSCCDS34235.1.
RefSeqNP_008985.3. NM_007054.5.
UniGeneHs.43670.

3D structure databases

ProteinModelPortalQ9Y496.
SMRQ9Y496. Positions 13-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116300. 19 interactions.
DIPDIP-33237N.
IntActQ9Y496. 10 interactions.
STRING9606.ENSP00000368020.

Chemistry

ChEMBLCHEMBL5544.

PTM databases

PhosphoSiteQ9Y496.

Polymorphism databases

DMDM296439481.

Proteomic databases

MaxQBQ9Y496.
PaxDbQ9Y496.
PRIDEQ9Y496.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378746; ENSP00000368020; ENSG00000131437.
GeneID11127.
KEGGhsa:11127.
UCSCuc003kxo.3. human.

Organism-specific databases

CTD11127.
GeneCardsGC05M132059.
H-InvDBHIX0024788.
HGNCHGNC:6319. KIF3A.
HPACAB037085.
MIM604683. gene.
neXtProtNX_Q9Y496.
PharmGKBPA30102.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000116164.
HOVERGENHBG052255.
KOK10394.
OrthoDBEOG7WX086.
PhylomeDBQ9Y496.
TreeFamTF105223.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9Y496.
BgeeQ9Y496.
CleanExHS_KIF3A.
GenevestigatorQ9Y496.

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_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKIF3A. human.
GeneWikiKIF3A.
GenomeRNAi11127.
NextBio42288.
PROQ9Y496.
SOURCESearch...

Entry information

Entry nameKIF3A_HUMAN
AccessionPrimary (citable) accession number: Q9Y496
Secondary accession number(s): A8MSW9 expand/collapse secondary AC list , Q59EN1, Q86XE9, Q9Y6V4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 117 of the entry and version 4 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