A0A097HUC9 · A0A097HUC9_CANLF

Function

function

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.

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 Componentcytoplasm
Cellular Componentnucleus
Cellular Componentspindle

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Heat shock protein beta-1
  • Alternative names
    • Heat shock 27 kDa protein

Gene names

    • Name
      HSP27

Organism names

Accessions

  • Primary accession
    A0A097HUC9

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homooligomer. Homodimer; becomes monomeric upon activation. Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin. Interacts with TGFB1I1. Interacts with CRYAB. Interacts with HSPB8. Interacts with HSPBAP1.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain77-185SHSP

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    206
  • Mass (Da)
    22,784
  • Last updated
    2015-01-07 v1
  • Checksum
    B9A5FF96E7E15484
MTERRVPFSLLRSPSWDPFRDWYPAHSRLFDQAFGLPRLPEEWAQWFGHSGWPGYVRPIPPAVEGPAAAAAPAYSRALSRQLSSGVSEIRQTADRWRVSMDVNHFAPEELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPMPKPATQSAEITIPVTFEARAQIGGPEAGKSEQSGAK

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue206

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KJ947842
EMBL· GenBank· DDBJ
AIT52079.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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