Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heat shock protein beta-1

Gene

HSPB1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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

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
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

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

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001259251 – 209Heat shock protein beta-1Add BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Omega-N-methylarginineBy similarity1
Modified residuei13PhosphoserineBy similarity1
Modified residuei15Phosphoserine; by MAPKAPK2 and MAPKAPK3By similarity1
Modified residuei27PhosphoserineBy similarity1
Modified residuei82Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5By similarity1
Modified residuei86Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5By similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei90PhosphoserineBy similarity1
Modified residuei102PhosphoserineBy similarity1
Modified residuei127N6-acetyllysineBy similarity1
Modified residuei178PhosphothreonineBy similarity1
Modified residuei180PhosphoserineBy similarity1
Modified residuei203PhosphoserineBy 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

PaxDbiP42929.
PRIDEiP42929.

PTM databases

iPTMnetiP42929.

Interactioni

Subunit structurei

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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000019945.

Structurei

3D structure databases

ProteinModelPortaliP42929.
SMRiP42929.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni74 – 209Interaction with TGFB1I1By similarityAdd BLAST136

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
HOGENOMiHOG000233955.
HOVERGENiHBG054766.
InParanoidiP42929.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiView protein in InterPro
IPR002068. A-crystallin/Hsp20_dom.
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.

P42929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTERRVPFSL LRSPSWDPFR DWYPAHSRLF DQAFGLPRLP EEWAQWFGHS
60 70 80 90 100
GWPGYVRPIP PAVEGPAAAA AAAAPAYSRA LSRQLSSGVS EIRQTADRWR
110 120 130 140 150
VSLDVNHFAP EELTVKTKDG VVEITGKHEE RQDEHGYISR RLTPKYTLPP
160 170 180 190 200
GVDPTLVSSS LSPEGTLTVE APMPKPATQS AEITIPVTFE ARAQIGGPEA

GKSEQSGAK
Length:209
Mass (Da):22,939
Last modified:November 1, 1995 - v1
Checksum:i7E59F696D8C7F1BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19368 mRNA. Translation: AAA87172.1.
PIRiJC4244.
UniGeneiCfa.3849.

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.

Entry informationi

Entry nameiHSPB1_CANLF
AccessioniPrimary (citable) accession number: P42929
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 10, 2017
This is version 105 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families