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O15066 (KIF3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 KIF3B
Alternative name(s):
HH0048
Microtubule plus end-directed kinesin motor 3B
Gene names
Name:KIF3B
Synonyms:KIAA0359
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro By similarity.

Subunit structure

Heterodimer of KIF3A and KIF3B. Interacts directly with IFT20 By similarity. Interacts with the SMC3 subunit of the cohesin complex. Ref.5

Subcellular location

Cytoplasmcytoskeleton Probable.

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 BAA20815.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterograde axon cargo transport

Traceable author statement PubMed 7559760. Source: ProtInc

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

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

determination of left/right symmetry

Traceable author statement PubMed 9865700. Source: ProtInc

membrane organization

Traceable author statement. Source: Reactome

metabolic process

Traceable author statement PubMed 7559760PubMed 9865700. Source: GOC

microtubule-based movement

Traceable author statement. Source: Reactome

mitotic centrosome separation

Traceable author statement PubMed 16298999. Source: BHF-UCL

mitotic spindle organization

Traceable author statement PubMed 16298999. Source: BHF-UCL

plus-end-directed vesicle transport along microtubule

Traceable author statement PubMed 16298999. Source: BHF-UCL

spindle assembly involved in mitosis

Inferred from mutant phenotype PubMed 19635168. Source: BHF-UCL

   Cellular_componentcentrosome

Non-traceable author statement 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

midbody

Inferred from electronic annotation. Source: Ensembl

plus-end kinesin complex

Traceable author statement PubMed 7559760. Source: ProtInc

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Rho GTPase binding

Inferred from physical interaction PubMed 19635168. Source: BHF-UCL

microtubule motor activity

Traceable author statement PubMed 9865700. Source: ProtInc

plus-end-directed microtubule motor activity

Traceable author statement PubMed 7559760. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 19635168. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARHGEF10O150133EBI-3931791,EBI-2515636

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 747747Kinesin-like protein KIF3B
PRO_0000125395
Initiator methionine11Removed; alternate Ref.7
Chain2 – 747746Kinesin-like protein KIF3B, N-terminally processed
PRO_0000424495

Regions

Domain9 – 340332Kinesin motor
Nucleotide binding96 – 1038ATP
Region580 – 747168Globular
Coiled coil346 – 579234 Potential
Compositional bias386 – 3938Poly-Gly
Compositional bias394 – 40613Poly-Glu
Compositional bias723 – 7308Poly-Ser

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7
Modified residue21N-acetylserine; in Kinesin-like protein KIF3B, N-terminally processed Ref.7

Secondary structure

.......................................................... 747
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15066 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 97FA4573AFA87023

FASTA74785,125
        10         20         30         40         50         60 
MSKLKSSESV RVVVRCRPMN GKEKAASYDK VVDVDVKLGQ VSVKNPKGTA HEMPKTFTFD 

        70         80         90        100        110        120 
AVYDWNAKQF ELYDETFRPL VDSVLQGFNG TIFAYGQTGT GKTYTMEGIR GDPEKRGVIP 

       130        140        150        160        170        180 
NSFDHIFTHI SRSQNQQYLV RASYLEIYQE EIRDLLSKDQ TKRLELKERP DTGVYVKDLS 

       190        200        210        220        230        240 
SFVTKSVKEI EHVMNVGNQN RSVGATNMNE HSSRSHAIFV ITIECSEVGL DGENHIRVGK 

       250        260        270        280        290        300 
LNLVDLAGSE RQAKTGAQGE RLKEATKINL SLSALGNVIS ALVDGKSTHI PYRDSKLTRL 

       310        320        330        340        350        360 
LQDSLGGNAK TVMVANVGPA SYNVEETLTT LRYANRAKNI KNKPRVNEDP KDALLREFQE 

       370        380        390        400        410        420 
EIARLKAQLE KRSIGRRKRR EKRREGGGSG GGGEEEEEEG EEGEEEGDDK DDYWREQQEK 

       430        440        450        460        470        480 
LEIEKRAIVE DHSLVAEEKM RLLKEKEKKM EDLRREKDAA EMLGAKIKAM ESKLLVGGKN 

       490        500        510        520        530        540 
IVDHTNEQQK ILEQKRQEIA EQKRREREIQ QQMESRDEET LELKETYSSL QQEVDIKTKK 

       550        560        570        580        590        600 
LKKLFSKLQA VKAEIHDLQE EHIKERQELE QTQNELTREL KLKHLIIENF IPLEEKSKIM 

       610        620        630        640        650        660 
NRAFFDEEED HWKLHPITRL ENQQMMKRPV SAVGYKRPLS QHARMSMMIR PEARYRAENI 

       670        680        690        700        710        720 
VLLELDMPSR TTRDYEGPAI APKVQAALDA ALQDEDEIQV DASSFESTAN KKSKARPKSG 

       730        740 
RKSGSSSSSS GTPASQLYPQ SRGLVPK 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Brain and Testis.
[5]"Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide."
Shimizu K., Shirataki H., Honda T., Minami S., Takai Y.
J. Biol. Chem. 273:6591-6594(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH SMC3 AND KIFAP3B.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Motor domain of human kinesin family member 3B in complex with ADP."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-359IN COMPLEX WITH ADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002357 mRNA. Translation: BAA20815.2. Different initiation.
AL121897 Genomic DNA. Translation: CAC16425.1.
CH471077 Genomic DNA. Translation: EAW76381.1.
CH471077 Genomic DNA. Translation: EAW76382.1.
BC136310 mRNA. Translation: AAI36311.1.
BC136311 mRNA. Translation: AAI36312.1.
CCDSCCDS13200.1.
RefSeqNP_004789.1. NM_004798.3.
UniGeneHs.369670.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B6UX-ray1.80A/B6-359[»]
ProteinModelPortalO15066.
SMRO15066. Positions 7-358.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114772. 11 interactions.
IntActO15066. 3 interactions.
MINTMINT-1185610.
STRING9606.ENSP00000364864.

Chemistry

BindingDBO15066.
ChEMBLCHEMBL6109.

PTM databases

PhosphoSiteO15066.

Proteomic databases

MaxQBO15066.
PaxDbO15066.
PeptideAtlasO15066.
PRIDEO15066.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375712; ENSP00000364864; ENSG00000101350.
GeneID9371.
KEGGhsa:9371.
UCSCuc002wxq.3. human.

Organism-specific databases

CTD9371.
GeneCardsGC20P030865.
HGNCHGNC:6320. KIF3B.
HPAHPA007119.
MIM603754. gene.
neXtProtNX_O15066.
PharmGKBPA30103.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000116164.
HOVERGENHBG052255.
InParanoidO15066.
KOK10394.
OMADNQQMMK.
OrthoDBEOG7WX086.
PhylomeDBO15066.
TreeFamTF105223.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressO15066.
BgeeO15066.
CleanExHS_KIF3B.
GenevestigatorO15066.

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

ChiTaRSKIF3B. human.
EvolutionaryTraceO15066.
GeneWikiKIF3B.
GenomeRNAi9371.
NextBio35098.
PROO15066.
SOURCESearch...

Entry information

Entry nameKIF3B_HUMAN
AccessionPrimary (citable) accession number: O15066
Secondary accession number(s): B2RMP4, E1P5M5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 123 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

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 chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM