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Protein

Heat shock protein beta-1

Gene

Hspb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in stress resistance and actin organization.

GO - Molecular functioni

  • ubiquitin binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cellular response to butyrate Source: RGD
  • cellular response to hydrogen peroxide Source: RGD
  • cellular response to interleukin-11 Source: RGD
  • female pregnancy Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of oxidative stress-induced cell death Source: RGD
  • response to angiotensin Source: RGD
  • response to ischemia Source: RGD
  • response to muscle stretch Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61306. Hspb1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cytoplasmcytoskeletonspindle By similarity

  • Note: Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (By similarity).By similarity

GO - Cellular componenti

  • axon Source: RGD
  • cardiac myofibril Source: RGD
  • cytoplasm Source: UniProtKB
  • dendrite Source: RGD
  • I band Source: RGD
  • M band Source: RGD
  • nucleus Source: UniProtKB
  • perikaryon Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density membrane Source: RGD
  • proteasome complex Source: RGD
  • spindle Source: UniProtKB-SubCell
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Heat shock protein beta-1PRO_0000125930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei15 – 151Phosphoserine; by MAPKAPK2 and MAPKAPK3Combined sourcesCurated
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei86 – 861Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5Combined sources
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei127 – 1271N6-acetyllysineBy similarity
Modified residuei200 – 2001PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress leads to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair 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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP42930.
PRIDEiP42930.

PTM databases

iPTMnetiP42930.
PhosphoSiteiP42930.

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

Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 (By similarity). Interacts with HSPBAP1 and TGFB1I1.By similarity2 Publications

GO - Molecular functioni

  • ubiquitin binding Source: RGD

Protein-protein interaction databases

BioGridi246632. 4 interactions.
IntActiP42930. 4 interactions.
MINTiMINT-4542769.
STRINGi10116.ENSRNOP00000032902.

Structurei

3D structure databases

ProteinModelPortaliP42930.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni74 – 206133Interaction with TGFB1I1Add
BLAST

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

Gene3Di2.60.40.790. 2 hits.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491S → A AA sequence (PubMed:8282729).Curated
Sequence conflicti74 – 741R → A AA sequence (PubMed:8282729).Curated
Sequence conflicti76 – 761Missing in AAB29536 (PubMed:7916612).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP42930.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246632. 4 interactions.
IntActiP42930. 4 interactions.
MINTiMINT-4542769.
STRINGi10116.ENSRNOP00000032902.

PTM databases

iPTMnetiP42930.
PhosphoSiteiP42930.

Proteomic databases

PaxDbiP42930.
PRIDEiP42930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi61306. Hspb1.

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
HOGENOMiHOG000233955.
HOVERGENiHBG054766.
InParanoidiP42930.
PhylomeDBiP42930.

Miscellaneous databases

PROiP42930.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Variation in expression of hsp27 messenger ribonucleic acid during the cycle of the seminiferous epithelium and co-localization of hsp27 and microfilaments in Sertoli cells of the rat."
    Welsh M.J., Wu W., Parvinen M., Gilmont R.R.
    Biol. Reprod. 55:141-151(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
  3. "Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles."
    Inaguma Y., Goto S., Shinohara H., Hasegawa K., Ohshima K., Kato K.
    J. Biochem. 114:378-384(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 13-19; 21-31; 42-83; 104-123; 133-140 AND 190-206, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Skeletal muscle.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 29-38, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  5. "Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27."
    Liu C., Gilmont R.R., Benndorf R., Welsh M.J.
    J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPBAP1.
  6. "Identification and characterization of hic-5/ARA55 as an hsp27 binding protein."
    Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E.
    J. Biol. Chem. 276:39911-39918(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  7. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-86 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-15 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSPB1_RAT
AccessioniPrimary (citable) accession number: P42930
Secondary accession number(s): Q63922, Q9QWA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.