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Protein

Heat shock protein beta-1

Gene

Hspb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • anterograde axonal protein transport Source: UniProtKB
  • cellular response to butyrate Source: RGD
  • cellular response to hydrogen peroxide Source: RGD
  • cellular response to interleukin-11 Source: RGD
  • chaperone-mediated protein folding Source: UniProtKB
  • female pregnancy Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of oxidative stress-induced cell death Source: RGD
  • positive regulation of neuron projection development Source: ParkinsonsUK-UCL
  • regulation of protein phosphorylation Source: UniProtKB
  • response to angiotensin Source: RGD
  • response to ischemia Source: RGD
  • response to muscle stretch Source: RGD

Keywordsi

Molecular functionChaperone
Biological processStress response

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein beta-1
Short name:
HspB1
Alternative name(s):
Heat shock 27 kDa protein
Short name:
HSP 27
Gene namesi
Name:Hspb1
Synonyms:Hsp27
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61306 Hspb1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001259301 – 206Heat shock protein beta-1Add BLAST206

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Omega-N-methylarginineBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei15Phosphoserine; by MAPKAPK2 and MAPKAPK3Combined sourcesCurated1
Modified residuei27PhosphoserineCombined sources1
Modified residuei86Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5Combined sources1
Modified residuei87PhosphoserineBy similarity1
Modified residuei90PhosphoserineCombined sources1
Modified residuei102PhosphoserineBy similarity1
Modified residuei127N6-acetyllysineBy similarity1
Modified residuei178PhosphothreonineBy similarity1
Modified residuei180PhosphoserineBy similarity1
Modified residuei200PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated upon exposure to protein kinase C activators and heat shock. Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP42930
PRIDEiP42930

PTM databases

iPTMnetiP42930
PhosphoSitePlusiP42930

Expressioni

Tissue specificityi

Expressed in a variety of tissues. High levels in lung, adrenal, xiphoid, adipose tissue, heart and striated and smooth muscle, lower levels in the CNS. Adult levels are much higher in the slow-twitch soleus muscle than in the fast-twitch rectus femoris and extensor digitorum muscles.1 Publication

Developmental stagei

Expressed in the soleus and rectus femoris muscles at prenatal day 2, increasing to a maximum at postnatal day 3. Expression in the rectus femoris muscle then decreases reaching adult levels within a few weeks.1 Publication

Interactioni

Subunit structurei

Homooligomer. Homodimer; becomes monomeric upon activation. Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin (By similarity). Interacts with TGFB1I1 (PubMed:11546764). Interacts with CRYAB (By similarity). Interacts with HSPB8 (By similarity). Interacts with HSPBAP1 (PubMed:10751411).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi246632, 5 interactors
IntActiP42930, 4 interactors
MINTiP42930
STRINGi10116.ENSRNOP00000032902

Structurei

3D structure databases

ProteinModelPortaliP42930
SMRiP42930
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 188sHSPPROSITE-ProRule annotationAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni74 – 206Interaction with TGFB1I11 PublicationAdd BLAST133

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3591 Eukaryota
ENOG410YERS LUCA
HOGENOMiHOG000233955
HOVERGENiHBG054766
InParanoidiP42930
PhylomeDBiP42930

Family and domain databases

CDDicd06475 ACD_HspB1_like, 1 hit
Gene3Di2.60.40.790, 1 hit
InterProiView protein in InterPro
IPR002068 A-crystallin/Hsp20_dom
IPR037876 ACD_HspB1
IPR001436 Alpha-crystallin/HSP
IPR031107 HSP20
IPR008978 HSP20-like_chaperone
PANTHERiPTHR11527 PTHR11527, 1 hit
PfamiView protein in Pfam
PF00011 HSP20, 1 hit
PRINTSiPR00299 ACRYSTALLIN
SUPFAMiSSF49764 SSF49764, 1 hit
PROSITEiView protein in PROSITE
PS01031 SHSP, 1 hit

Sequencei

Sequence statusi: Complete.

P42930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRFP DEWSQWFSSA
60 70 80 90 100
GWPGYVRPLP AATAEGPAAV TLARPAFSRA LNRQLSSGVS EIRQTADRWR
110 120 130 140 150
VSLDVNHFAP EELTVKTKEG VVEITGKHEE RQDEHGYISR CFTRKYTLPP
160 170 180 190 200
GVDPTLVSSS LSPEGTLTVE APLPKAVTQS AEITIPVTFE ARAQIGGPES

EQSGAK
Length:206
Mass (Da):22,893
Last modified:November 1, 1995 - v1
Checksum:i1CEC75582E5E34B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49S → A AA sequence (PubMed:8282729).Curated1
Sequence conflicti74R → A AA sequence (PubMed:8282729).Curated1
Sequence conflicti76Missing in AAB29536 (PubMed:7916612).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86389 mRNA Translation: AAA41353.1
S67755 Genomic DNA Translation: AAB29536.2
PIRiJN0924
UniGeneiRn.3841

Similar proteinsi

Entry informationi

Entry nameiHSPB1_RAT
AccessioniPrimary (citable) accession number: P42930
Secondary accession number(s): Q63922, Q9QWA8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 138 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health