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P33176 (KINH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. 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-1 heavy chain
Alternative name(s):
Conventional kinesin heavy chain
Ubiquitous kinesin heavy chain
Short name=UKHC
Gene names
Name:KIF5B
Synonyms:KNS, KNS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length963 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes By similarity.

Subunit structure

Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and PPP1R42 By similarity. Interacts with SYBU. Interacts with JAKMIP1. Interacts with PLEKHM2. Interacts with ECM29. Ref.4 Ref.5 Ref.7 Ref.9

Subcellular location

Cytoplasmcytoskeleton By similarity. Note: Uniformly distributed between soma and neurites in hippocampal neurons By similarity.

Domain

Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.

Sequence similarities

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

Contains 1 kinesin motor domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

cytoplasm organization

Inferred from electronic annotation. Source: Ensembl

microtubule-based movement

Traceable author statement PubMed 7514426. Source: ProtInc

positive regulation of establishment of protein localization to plasma membrane

Inferred from direct assay PubMed 19675065. Source: BHF-UCL

positive regulation of potassium ion transport

Inferred from direct assay PubMed 19675065. Source: BHF-UCL

regulation of membrane potential

Inferred from direct assay PubMed 19675065. Source: BHF-UCL

stress granule disassembly

Inferred from sequence or structural similarity. Source: BHF-UCL

vesicle transport along microtubule

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentciliary rootlet

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

kinesin complex

Traceable author statement Ref.1. Source: ProtInc

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from direct assay. Source: HPA

neuron projection

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: HGNC

vesicle

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from sequence or structural similarity. Source: HGNC

microtubule motor activity

Inferred from sequence or structural similarity. Source: HGNC

protein binding

Inferred from physical interaction PubMed 19164528. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VACWR159P686193EBI-355878,EBI-7133540From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 963962Kinesin-1 heavy chain
PRO_0000125351

Regions

Domain8 – 325318Kinesin motor
Nucleotide binding85 – 928ATP
Region915 – 96349Globular
Coiled coil329 – 914586

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.12 Ref.13
Modified residue9331Phosphoserine Ref.10

Secondary structure

................................................................. 963
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33176 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: A1FE5760C3250C8B

FASTA963109,685
        10         20         30         40         50         60 
MADLAECNIK VMCRFRPLNE SEVNRGDKYI AKFQGEDTVV IASKPYAFDR VFQSSTSQEQ 

        70         80         90        100        110        120 
VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH DPEGMGIIPR IVQDIFNYIY 

       130        140        150        160        170        180 
SMDENLEFHI KVSYFEIYLD KIRDLLDVSK TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM 

       190        200        210        220        230        240 
DTIDEGKSNR HVAVTNMNEH SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK 

       250        260        270        280        290        300 
TGAEGAVLDE AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI 

       310        320        330        340        350        360 
CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK NKILRNTIQW 

       370        380        390        400        410        420 
LENELNRWRN GETVPIDEQF DKEKANLEAF TVDKDITLTN DKPATAIGVI GNFTDAERRK 

       430        440        450        460        470        480 
CEEEIAKLYK QLDDKDEEIN QQSQLVEKLK TQMLDQEELL ASTRRDQDNM QAELNRLQAE 

       490        500        510        520        530        540 
NDASKEEVKE VLQALEELAV NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL 

       550        560        570        580        590        600 
KEMTNHQKKR AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE 

       610        620        630        640        650        660 
VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL QNVEQKKRQL 

       670        680        690        700        710        720 
EESVDALSEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA VEQQIQSHRE THQKQISSLR 

       730        740        750        760        770        780 
DEVEAKAKLI TDLQDQNQKM MLEQERLRVE HEKLKATDQE KSRKLHELTV MQDRREQARQ 

       790        800        810        820        830        840 
DLKGLEETVA KELQTLHNLR KLFVQDLATR VKKSAEIDSD DTGGSAAQKQ KISFLENNLE 

       850        860        870        880        890        900 
QLTKVHKQLV RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD 

       910        920        930        940        950        960 
RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPSAI RGGGAFVQNS QPVAVRGGGG 


KQV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells."
Navone F., Niclas J., Hom-Booher N., Sparks L., Bernstein H.D., McCaffrey G., Vale R.D.
J. Cell Biol. 117:1263-1275(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
[4]"Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons."
Su Q., Cai Q., Gerwin C., Smith C.L., Sheng Z.-H.
Nat. Cell Biol. 6:941-953(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYBU.
[5]"The intracellular fate of Salmonella depends on the recruitment of kinesin."
Boucrot E., Henry T., Borg J.-P., Gorvel J.-P., Meresse S.
Science 308:1174-1178(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLEKHM2.
[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]"Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton and regulate receptor transport."
Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S., Couve A.
Mol. Cell. Neurosci. 35:501-512(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH JAKMIP1.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ECM29.
[10]"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-933, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Crystal structure of the kinesin motor domain reveals a structural similarity to myosin."
Kull F.J., Sablin E.P., Lau R., Fletterick R.J., Vale R.D.
Nature 380:550-555(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP.
[15]"Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy."
Sindelar C.V., Budny M.J., Rice S., Naber N., Fletterick R., Cooke R.
Nat. Struct. Biol. 9:844-848(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP.
[16]"The beginning of kinesin's force-generating cycle visualized at 9-A resolution."
Sindelar C.V., Downing K.H.
J. Cell Biol. 177:377-385(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 1-325.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65873 mRNA. Translation: CAA46703.1.
AL161932 Genomic DNA. Translation: CAH71618.1.
BC126279 mRNA. Translation: AAI26280.1.
BC126281 mRNA. Translation: AAI26282.1.
CCDSCCDS7171.1.
PIRA41919.
RefSeqNP_004512.1. NM_004521.2.
UniGeneHs.327736.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG2X-ray1.80A1-325[»]
1MKJX-ray2.70A1-349[»]
2P4Nelectron microscopy9.00K1-325[»]
4HNAX-ray3.19K1-349[»]
ProteinModelPortalP33176.
SMRP33176. Positions 3-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110000. 64 interactions.
DIPDIP-29244N.
IntActP33176. 22 interactions.
MINTMINT-4999704.
STRING9606.ENSP00000307078.

Chemistry

BindingDBP33176.
ChEMBLCHEMBL5864.

PTM databases

PhosphoSiteP33176.

Polymorphism databases

DMDM417216.

Proteomic databases

MaxQBP33176.
PaxDbP33176.
PRIDEP33176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302418; ENSP00000307078; ENSG00000170759.
GeneID3799.
KEGGhsa:3799.
UCSCuc001iwe.4. human.

Organism-specific databases

CTD3799.
GeneCardsGC10M032340.
HGNCHGNC:6324. KIF5B.
HPACAB009846.
HPA037589.
HPA037590.
MIM602809. gene.
neXtProtNX_P33176.
PharmGKBPA30108.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOVERGENHBG006210.
InParanoidP33176.
KOK10396.
OMALAECNIK.
OrthoDBEOG7T4MJD.
PhylomeDBP33176.
TreeFamTF105225.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP33176.
BgeeP33176.
CleanExHS_KIF5B.
GenevestigatorP33176.

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

ChiTaRSKIF5B. human.
EvolutionaryTraceP33176.
GeneWikiKIF5B.
GenomeRNAi3799.
NextBio14917.
PROP33176.
SOURCESearch...

Entry information

Entry nameKINH_HUMAN
AccessionPrimary (citable) accession number: P33176
Secondary accession number(s): A0AVB2, Q5VZ85
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 144 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 10

Human chromosome 10: entries, gene names and cross-references to MIM