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Protein

Heat shock protein beta-6

Gene

HSPB6

Organism
Homo sapiens (Human)
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. 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

EuPathDBiHostDB:ENSG00000004776.11
HGNCiHGNC:26511 HSPB6
MIMi610695 gene
neXtProtiNX_O14558

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, 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
ProteomicsDBi48083

2D gel databases

REPRODUCTION-2DPAGEiO14558
UCD-2DPAGEiO14558

PTM databases

iPTMnetiO14558
PhosphoSitePlusiO14558

Expressioni

Gene expression databases

BgeeiENSG00000004776 Expressed in 175 organ(s), highest expression level in heart left ventricle
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

WithEntry#Exp.IntActNotes
HSPB8Q9UJY12EBI-739095,EBI-739074

GO - Molecular functioni

Protein-protein interaction databases

BioGridi125988, 9 interactors
IntActiO14558, 4 interactors
MINTiO14558
STRINGi9606.ENSP00000004982

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO14558
SMRiO14558
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 160sHSPPROSITE-ProRule annotationAdd BLAST106

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
OMAiPVQPTWL
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
IPR003090 Alpha-crystallin_N
IPR031107 HSP20
IPR008978 HSP20-like_chaperone
PANTHERiPTHR11527 PTHR11527, 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 SHSP, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EP04K7EP04_HUMAN
Heat shock protein beta-6
HSPB6
137Annotation score:
A0A1X7SC65A0A1X7SC65_HUMAN
Heat shock protein beta-6
HSPB6
122Annotation score:

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
GeneIDi126393
KEGGihsa:126393

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

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[»]
5OK9X-ray2.35A/B/E/F12-19[»]
5OKFX-ray3.20A/B/C/D12-19[»]
ProteinModelPortaliO14558
SMRiO14558
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125988, 9 interactors
IntActiO14558, 4 interactors
MINTiO14558
STRINGi9606.ENSP00000004982

PTM databases

iPTMnetiO14558
PhosphoSitePlusiO14558

Polymorphism and mutation databases

BioMutaiHSPB6

2D gel databases

REPRODUCTION-2DPAGEiO14558
UCD-2DPAGEiO14558

Proteomic databases

PaxDbiO14558
PeptideAtlasiO14558
PRIDEiO14558
ProteomicsDBi48083

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000004982; ENSP00000004982; ENSG00000004776
GeneIDi126393
KEGGihsa:126393

Organism-specific databases

CTDi126393
DisGeNETi126393
EuPathDBiHostDB:ENSG00000004776.11
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
OMAiPVQPTWL
OrthoDBiEOG091G0USC
PhylomeDBiO14558

Enzyme and pathway databases

SignaLinkiO14558
SIGNORiO14558

Miscellaneous databases

ChiTaRSiHSPB6 human
GeneWikiiHSPB6
GenomeRNAii126393
PROiPR:O14558
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000004776 Expressed in 175 organ(s), highest expression level in heart left ventricle
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
IPR003090 Alpha-crystallin_N
IPR031107 HSP20
IPR008978 HSP20-like_chaperone
PANTHERiPTHR11527 PTHR11527, 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 SHSP, 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: November 7, 2018
This is version 154 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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