P37285 · KLC1_RAT

  • Protein
    Kinesin light chain 1
  • Gene
    Klc1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport (PubMed:19861499).
The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (PubMed:19861499).

Caution

It is uncertain whether Met-1 or Met-5 is the initiator.

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
Cellular Componentciliary rootlet
Cellular Componentcytoplasm
Cellular Componentcytoplasmic vesicle
Cellular Componentcytosol
Cellular Componentgrowth cone
Cellular Componentkinesin complex
Cellular Componentmembrane
Cellular Componentmembrane-bounded organelle
Cellular Componentmicrotubule
Cellular Componentneuron projection
Cellular Componentneuronal cell body
Cellular Componentvesicle
Molecular Functionkinesin binding
Molecular Functiontubulin binding
Biological Processaxo-dendritic transport
Biological Processcell adhesion
Biological Processintracellular protein transport
Biological Processmicrotubule-based movement
Biological Processprotein localization to synapse
Biological Processstress granule disassembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Kinesin light chain 1
  • Short names
    KLC 1

Gene names

    • Name
      Klc1
    • Synonyms
      Klc, Kns2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P37285

Proteomes

Organism-specific databases

Phenotypes & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002150941-560Kinesin light chain 1
Modified residue162Phosphoserine
Modified residue449Phosphotyrosine
Modified residue460Phosphoserine
Modified residue521Phosphoserine
Modified residue524Phosphoserine

Post-translational modification

Phosphorylation at Ser-460 by ERK inhibits interaction with CLSTN1 and localization to cytoplasmic vesicles.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in brain (at protein level).

Gene expression databases

Interaction

Subunit

Oligomeric complex composed of two heavy chains and two light chains (Probable). Interacts with SPAG9 (By similarity).
Interacts with ATCAY; may link mitochondria to KLC1 and regulate mitochondria localization into neuron projections (PubMed:19861499).
Interacts (via TPR repeats) with TOR1A; the interaction associates TOR1A with the kinesin oligomeric complex (PubMed:14970196).
Interacts with BORCS5 (By similarity).
Interacts with MAPK8IP3/JIP3 and NTRK2/TRKB; interaction with NTRK2/TRKB is mediated by MAPK8IP3/JIP3 (PubMed:21775604).
Interacts with CLSTN1; phosphorylation at Ser-460 inhibits interaction with CLSTN1 (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO P37285OPG164 P686194EBI-917396, EBI-7133540

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for coiled coil, compositional bias, region, repeat.

TypeIDPosition(s)Description
Coiled coil27-156
Compositional bias156-178Basic and acidic residues
Region156-203Disordered
Compositional bias187-201Polar residues
Repeat213-246TPR 1
Repeat255-288TPR 2
Repeat297-330TPR 3
Repeat339-372TPR 4
Repeat381-414TPR 5
Repeat464-497TPR 6

Sequence similarities

Belongs to the kinesin light chain family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing. Additional isoforms seem to exist.

P37285-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    560
  • Mass (Da)
    63,745
  • Last updated
    2008-11-25 v2
  • Checksum
    24D0C4CF9E304366
MHDNMSTMVYMKEEKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSSMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDSDSSKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGSSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAALRSRKQGLDNVHKQRVAEVLNDPENVEKRRSRESLNVDVVKYESGPDGGEEVSMSVEWNGMRKMKLGLVK

P37285-2

  • Name
    A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 542-560: VSMSVEWNGMRKMKLGLVK → A

P37285-3

  • Name
    B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8L2RC24A0A8L2RC24_RATKlc1565
A0A140TAB3A0A140TAB3_RATKlc1552
A0A8L2QTG3A0A8L2QTG3_RATKlc1551
A0A8I5ZN87A0A8I5ZN87_RATKlc1593
A0A8I5ZU72A0A8I5ZU72_RATKlc1585

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias156-178Basic and acidic residues
Compositional bias187-201Polar residues
Alternative sequenceVSP_002871542-550in isoform B
Alternative sequenceVSP_002872542-560in isoform A

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M75146
EMBL· GenBank· DDBJ
-mRNA No translation available.
M75147
EMBL· GenBank· DDBJ
-mRNA No translation available.
M75148
EMBL· GenBank· DDBJ
-mRNA No translation available.

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.
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