P28738 · KIF5C_MOUSE

  • Protein
    Kinesin heavy chain isoform 5C
  • Gene
    Kif5c
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Microtubule-associated force-producing protein that may play a role in organelle transport. Has ATPase activity (By similarity).
Involved in synaptic transmission (By similarity).
Mediates dendritic trafficking of mRNAs (PubMed:19608740).
Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (By similarity).

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site87ATP (UniProtKB | ChEBI)
Binding site89ATP (UniProtKB | ChEBI)
Binding site90ATP (UniProtKB | ChEBI)
Binding site91ATP (UniProtKB | ChEBI)
Binding site92ATP (UniProtKB | ChEBI)
Binding site93ATP (UniProtKB | ChEBI)
Binding site94ATP (UniProtKB | ChEBI)
Binding site99ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentaxon cytoplasm
Cellular Componentaxonal growth cone
Cellular Componentciliary rootlet
Cellular Componentcytoplasm
Cellular Componentdendrite
Cellular Componentdendrite cytoplasm
Cellular Componentdistal axon
Cellular Componentkinesin complex
Cellular Componentmicrotubule
Cellular Componentneuron projection
Cellular Componentneuronal cell body
Cellular Componentpostsynaptic cytosol
Molecular Functionapolipoprotein receptor binding
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule motor activity
Molecular Functionplus-end-directed microtubule motor activity
Biological Processanterograde axonal protein transport
Biological Processanterograde dendritic transport of messenger ribonucleoprotein complex
Biological Processanterograde dendritic transport of neurotransmitter receptor complex
Biological Processaxon guidance
Biological Processintracellular mRNA localization
Biological Processmotor neuron axon guidance
Biological ProcessmRNA transport
Biological Processsynaptic vesicle transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Kinesin heavy chain isoform 5C
  • EC number
  • Alternative names
    • Kinesin heavy chain neuron-specific 2
    • Kinesin-1

Gene names

    • Name
      Kif5c
    • Synonyms
      Nkhc2

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P28738
  • Secondary accessions
    • Q6NXI9
    • Q9Z2F8

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001253561-956Kinesin heavy chain isoform 5C
Modified residue403Phosphothreonine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Oligomer composed of two heavy chains and two light chains (PubMed:15286375).
Interacts with GRIP1 (PubMed:11986669).
Interacts with KLC3 and TRAK1 (By similarity).
Interacts with ZFYVE27 (PubMed:21976701).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P28738Mapk8ip3 Q9ESN98EBI-2506834, EBI-301496

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, coiled coil.

TypeIDPosition(s)Description
Domain8-327Kinesin motor
Region174-315Microtubule-binding
Coiled coil406-923
Region859-956Globular
Region910-956Disordered

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    956
  • Mass (Da)
    109,275
  • Last updated
    2011-07-27 v3
  • Checksum
    A36BC903603D8748
MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKALKSVLQHLEMELNRWRNGEAVPEDEQISAKDQKSLEPCDNTPIIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQMDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAVRGGGGGSSNSTHYQK

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A2ARD4A2ARD4_MOUSEKif5c243

Sequence caution

The sequence CAA43677.1 differs from that shown. Reason: Miscellaneous discrepancy Chimeric cDNA. The C-terminus (up to position 300) corresponds to KIF5C sequence.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict387in Ref. 2; AAC79804
Sequence conflict792in Ref. 2; AAC79804

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X61435
EMBL· GenBank· DDBJ
CAA43677.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AF067180
EMBL· GenBank· DDBJ
AAC79804.1
EMBL· GenBank· DDBJ
mRNA
AL845332
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL929069
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH466519
EMBL· GenBank· DDBJ
EDL26880.1
EMBL· GenBank· DDBJ
Genomic DNA
BC067051
EMBL· GenBank· DDBJ
AAH67051.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp