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Q61768 (KINH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Khcs, Kns1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. May be involved in the mechanisms of growth arrest induced by exposure to DNA-damaging drugs or by cellular senescence. Ref.5

Subunit structure

Interacts with SYBU By similarity. Interacts with PLEKHM2 By similarity. Interacts with ECM29 By similarity. Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1. Interacts with JAKMIP1 and PPP1R42. Ref.6 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.

Disruption phenotype

Mice are embryonic lethal. They show perinuclear clustering of mitochondria and impaired lysosomal dispersion. Ref.5

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 termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcytoplasm organization

Inferred from mutant phenotype Ref.5. Source: MGI

metabolic process

Inferred from sequence or structural similarity. Source: GOC

microtubule-based process

Traceable author statement PubMed 11486041. Source: MGI

mitochondrial transport

Traceable author statement PubMed 11486041. Source: MGI

positive regulation of establishment of protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

positive regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

stress granule disassembly

Inferred from mutant phenotype PubMed 19825938. Source: BHF-UCL

vesicle transport along microtubule

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentciliary rootlet

Inferred from direct assay PubMed 16018997. Source: MGI

cytoplasm

Inferred from direct assay PubMed 16018997. Source: MGI

cytosol

Traceable author statement. Source: Reactome

kinesin complex

Traceable author statement PubMed 10964943. Source: MGI

membrane-bounded organelle

Inferred from direct assay PubMed 12805290. Source: MGI

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from direct assay PubMed 16301330. Source: MGI

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: HGNC

vesicle

Inferred from sequence or structural similarity. 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 Ref.9PubMed 9624122. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dync1i1O884853EBI-776129,EBI-492834
NudcO356854EBI-776129,EBI-911192

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 963962Kinesin-1 heavy chain
PRO_0000125352

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue9331Phosphoserine By similarity
Modified residue9451Phosphoserine Ref.8

Experimental info

Sequence conflict20 – 212ES → AT in AAA20133. Ref.3
Sequence conflict401M → V in AAB53940. Ref.1
Sequence conflict751E → G in AAA20133. Ref.3
Sequence conflict1911H → D in AAA20133. Ref.3
Sequence conflict2551N → K in AAA20133. Ref.3
Sequence conflict3961I → T in AAA20133. Ref.3
Sequence conflict4031P → G in AAB53940. Ref.1
Sequence conflict4511T → I in AAA20132. Ref.3
Sequence conflict5201S → T in AAB53940. Ref.1
Sequence conflict5231L → F in AAB53940. Ref.1
Sequence conflict6531V → D in AAB53940. Ref.1
Sequence conflict6641V → L in AAB53940. Ref.1
Sequence conflict7441Q → T in AAB53940. Ref.1
Sequence conflict8141S → R in AAA20133. Ref.3
Sequence conflict8651K → F in AAB53940. Ref.1
Sequence conflict8811L → R in AAA20133. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q61768 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: C3D3461A0C314901

FASTA963109,551
        10         20         30         40         50         60 
MADPAECNIK VMCRFRPLNE SEVNRGDKYV AKFQGEDTVM 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 NKTLRNTIQW 

       370        380        390        400        410        420 
LENELNRWRN GETVPIDEQF DKEKANLEAF TADKDIAITS DKPAAAVGMA GSFTDAERRK 

       430        440        450        460        470        480 
CEEELAKLYK 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 
EESVDSLGEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA VEQQIQSHRE THQKQISSLR 

       730        740        750        760        770        780 
DEVEAKEKLI TDLQDQNQKM VLEQERLRVE HERLKATDQE KSRKLHELTV MQDRREQARQ 

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

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

       910        920        930        940        950        960 
RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPGTV RGGGSFVQNN QPVGLRGGGG 


KQS 

« Hide

References

« Hide 'large scale' references
[1]"Suppression of the expression of a pancreatic beta-cell form of the kinesin heavy chain by antisense oligonucleotides inhibits insulin secretion from primary cultures of mouse beta-cells."
Meng Y.X., Wilson G.W., Avery M.C., Varden C.H., Balczon R.
Endocrinology 138:1979-1987(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"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].
Strain: C57BL/6.
Tissue: Brain.
[3]"Cloning mammalian genes by expression selection of genetic suppressor elements: association of kinesin with drug resistance and cell immortalization."
Gudkov A.V., Kazarov A.R., Thimmapaya R., Axenovich S.A., Mazo I.A., Roninson I.B.
Proc. Natl. Acad. Sci. U.S.A. 91:3744-3748(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-881.
Strain: BALB/c.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 132-141 AND 490-505, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria."
Tanaka Y., Kanai Y., Okada Y., Nonaka S., Takeda S., Harada A., Hirokawa N.
Cell 93:1147-1158(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites."
Setou M., Seog D.-H., Tanaka Y., Kanai Y., Takei Y., Kawagishi M., Hirokawa N.
Nature 417:83-87(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIP1.
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-945, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"TLRR (lrrc67) interacts with PP1 and is associated with a cytoskeletal complex in the testis."
Wang R., Kaul A., Sperry A.O.
Biol. Cell 102:173-189(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R42.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U86090 mRNA. Translation: AAB53940.1.
BC090841 mRNA. Translation: AAH90841.1.
L27153 mRNA. Translation: AAA20133.1.
L29223 mRNA. Translation: AAA20132.2.
CCDSCCDS37724.1.
PIRI84737.
RefSeqNP_032474.2. NM_008448.3.
UniGeneMm.223744.

3D structure databases

ProteinModelPortalQ61768.
SMRQ61768. Positions 3-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200946. 8 interactions.
IntActQ61768. 13 interactions.
MINTMINT-236764.

PTM databases

PhosphoSiteQ61768.

Proteomic databases

MaxQBQ61768.
PaxDbQ61768.
PRIDEQ61768.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025083; ENSMUSP00000025083; ENSMUSG00000006740.
GeneID16573.
KEGGmmu:16573.
UCSCuc008dzf.2. mouse.

Organism-specific databases

CTD3799.
MGIMGI:1098268. Kif5b.

Phylogenomic databases

eggNOGCOG5059.
GeneTreeENSGT00730000110208.
HOGENOMHOG000216718.
HOVERGENHBG006210.
InParanoidQ5BL10.
KOK10396.
OMADQNQKMV.
OrthoDBEOG7T4MJD.
TreeFamTF105225.

Gene expression databases

ArrayExpressQ61768.
BgeeQ61768.
CleanExMM_KIF5B.
GenevestigatorQ61768.

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

NextBio290095.
PROQ61768.
SOURCESearch...

Entry information

Entry nameKINH_MOUSE
AccessionPrimary (citable) accession number: Q61768
Secondary accession number(s): O08711, Q5BL10, Q61580
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot