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Protein

Heat shock protein beta-6

Gene

HSPB6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity.Curated4 Publications

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • structural constituent of eye lens Source: InterPro
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processStress response

Enzyme and pathway databases

SignaLinkiO14558.
SIGNORiO14558.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein beta-6
Short name:
HspB6
Alternative name(s):
Heat shock 20 kDa-like protein p20
Gene namesi
Name:HSPB6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:26511. HSPB6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular region Source: UniProtKB
  • nucleus Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3I → G: Increases homodimer-based self-association properties; increases chaperone activity; when associated with G-5. 1 Publication1
Mutagenesisi5V → G: Increases homodimer-based self-association properties; increases chaperone activity; when associated with G-3. 1 Publication1
Mutagenesisi67V → G: No effect on homodimer-based self-association properties; no effect on chaperone activity. 1 Publication1
Mutagenesisi134S → Q: Decreases heteromer formation with CRYAB. 1

Organism-specific databases

DisGeNETi126393.
OpenTargetsiENSG00000004776.
PharmGKBiPA134983584.

Polymorphism and mutation databases

BioMutaiHSPB6.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001259391 – 160Heat shock protein beta-6Add BLAST160

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16Phosphoserine; by PKACombined sources1 Publication1

Post-translational modificationi

The N-terminus is blocked.1 Publication
Phosphorylated at Ser-16 by PKA and probably PKD1K; required to protect cardiomyocytes from apoptosis.By similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO14558.
PeptideAtlasiO14558.
PRIDEiO14558.

2D gel databases

REPRODUCTION-2DPAGEO14558.
UCD-2DPAGEO14558.

PTM databases

iPTMnetiO14558.
PhosphoSitePlusiO14558.

Expressioni

Gene expression databases

BgeeiENSG00000004776.
CleanExiHS_HSPB6.
ExpressionAtlasiO14558. baseline and differential.
GenevisibleiO14558. HS.

Organism-specific databases

HPAiCAB001974.
HPA044153.
HPA054811.

Interactioni

Subunit structurei

Homodimer. Small heat shock proteins form high molecular mass oligomers containing variable number of monomers; these oligomers display a very flexible quaternary structure easily exchanging their subunits. Heterooligomer with HSPB1; formed through oligomerization of HSPB1:HSBP6 dimers; subunit exchange leads to formation of at least two different heterooligomeric complexes, differing in variable quantities of HSPB1 and HSPB6 homodimers in addition to HSPB1:HSPB6 heterodimers. Heterooligomer with CRYAB; large heterooligomers consist of CRYAB homodimers and HSPB5:HSPB6 heterodimers but lacking HSPB6 homodimers. Interacts with BAG3. Interacts (phosphorylated) with YWHAZ. Interacts with PDE4A and PDE4D; required for maintenance of the non-phosphorylated state of HSPB6 under basal conditions. Interacts with KDR. Interacts with PRKD1.10 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi125988. 9 interactors.
IntActiO14558. 51 interactors.
MINTiMINT-7002024.
STRINGi9606.ENSP00000004982.

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi69 – 71Combined sources3
Beta strandi74 – 79Combined sources6
Helixi85 – 87Combined sources3
Beta strandi88 – 93Combined sources6
Beta strandi96 – 107Combined sources12
Beta strandi109 – 122Combined sources14
Helixi129 – 131Combined sources3
Beta strandi133 – 136Combined sources4
Beta strandi140 – 146Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4JUSX-ray2.50A/B/C/D/E/F/G/H57-160[»]
4JUTX-ray2.20A/B/C/D/E/F/G/H57-160[»]
5LTWX-ray4.50C/D/G/H/K/L1-149[»]
5LU1X-ray2.40C/D/G/H13-20[»]
5LU2X-ray2.50C/D11-23[»]
5LUMX-ray2.60A/B/C/D/E72-149[»]
F/G/H/I/J2-10[»]
ProteinModelPortaliO14558.
SMRiO14558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 72Involved in stabilization of the HSPB1:HSBP6 heterodimer1 PublicationAdd BLAST72

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiO14558.
KOiK09545.
OMAiAFAPYYL.
OrthoDBiEOG091G0USC.
PhylomeDBiO14558.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiView protein in InterPro
IPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF229. PTHR11527:SF229. 1 hit.
PfamiView protein in Pfam
PF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiView protein in PROSITE
PS01031. HSP20. 1 hit.

Sequencei

Sequence statusi: Complete.

O14558-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIPVPVQPS WLRRASAPLP GLSAPGRLFD QRFGEGLLEA ELAALCPTTL
60 70 80 90 100
APYYLRAPSV ALPVAQVPTD PGHFSVLLDV KHFSPEEIAV KVVGEHVEVH
110 120 130 140 150
ARHEERPDEH GFVAREFHRR YRLPPGVDPA AVTSALSPEG VLSIQAAPAS
160
AQAPPPAAAK
Length:160
Mass (Da):17,136
Last modified:August 2, 2002 - v2
Checksum:i3BFB1FFB5877F2E7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64 – 66Missing in AAB81196 (PubMed:15057824).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07781820P → L Decreases phosphorylation at Ser-16; abolishes cardioprotective effects. 1 PublicationCorresponds to variant dbSNP:rs11549029Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056951 mRNA. Translation: BAB71323.1.
AC002398 Genomic DNA. Translation: AAB81196.1.
BC068046 mRNA. Translation: AAH68046.1.
CCDSiCCDS12475.1.
PIRiB53814.
T00703.
RefSeqiNP_653218.1. NM_144617.2.
UniGeneiHs.534538.
Hs.744178.

Genome annotation databases

EnsembliENST00000004982; ENSP00000004982; ENSG00000004776.
ENST00000592984; ENSP00000468057; ENSG00000004776.
GeneIDi126393.
KEGGihsa:126393.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056951 mRNA. Translation: BAB71323.1.
AC002398 Genomic DNA. Translation: AAB81196.1.
BC068046 mRNA. Translation: AAH68046.1.
CCDSiCCDS12475.1.
PIRiB53814.
T00703.
RefSeqiNP_653218.1. NM_144617.2.
UniGeneiHs.534538.
Hs.744178.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4JUSX-ray2.50A/B/C/D/E/F/G/H57-160[»]
4JUTX-ray2.20A/B/C/D/E/F/G/H57-160[»]
5LTWX-ray4.50C/D/G/H/K/L1-149[»]
5LU1X-ray2.40C/D/G/H13-20[»]
5LU2X-ray2.50C/D11-23[»]
5LUMX-ray2.60A/B/C/D/E72-149[»]
F/G/H/I/J2-10[»]
ProteinModelPortaliO14558.
SMRiO14558.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125988. 9 interactors.
IntActiO14558. 51 interactors.
MINTiMINT-7002024.
STRINGi9606.ENSP00000004982.

PTM databases

iPTMnetiO14558.
PhosphoSitePlusiO14558.

Polymorphism and mutation databases

BioMutaiHSPB6.

2D gel databases

REPRODUCTION-2DPAGEO14558.
UCD-2DPAGEO14558.

Proteomic databases

PaxDbiO14558.
PeptideAtlasiO14558.
PRIDEiO14558.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000004982; ENSP00000004982; ENSG00000004776.
ENST00000592984; ENSP00000468057; ENSG00000004776.
GeneIDi126393.
KEGGihsa:126393.

Organism-specific databases

CTDi126393.
DisGeNETi126393.
GeneCardsiHSPB6.
HGNCiHGNC:26511. HSPB6.
HPAiCAB001974.
HPA044153.
HPA054811.
MIMi610695. gene.
neXtProtiNX_O14558.
OpenTargetsiENSG00000004776.
PharmGKBiPA134983584.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiO14558.
KOiK09545.
OMAiAFAPYYL.
OrthoDBiEOG091G0USC.
PhylomeDBiO14558.

Enzyme and pathway databases

SignaLinkiO14558.
SIGNORiO14558.

Miscellaneous databases

GeneWikiiHSPB6.
GenomeRNAii126393.
PROiO14558.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000004776.
CleanExiHS_HSPB6.
ExpressionAtlasiO14558. baseline and differential.
GenevisibleiO14558. HS.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiView protein in InterPro
IPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF229. PTHR11527:SF229. 1 hit.
PfamiView protein in Pfam
PF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiView protein in PROSITE
PS01031. HSP20. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHSPB6_HUMAN
AccessioniPrimary (citable) accession number: O14558
Secondary accession number(s): O14551, Q6NVI3, Q96MG9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 2, 2002
Last modified: March 15, 2017
This is version 142 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.