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Protein

Heat shock protein beta-1

Gene

HSPB1

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 (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742).4 Publications

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • protein binding involved in protein folding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein kinase C binding Source: BHF-UCL
  • protein kinase C inhibitor activity Source: BHF-UCL
  • RNA binding Source: UniProtKB
  • ubiquitin binding Source: BHF-UCL

GO - Biological processi

  • anterograde axonal protein transport Source: UniProtKB
  • cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  • chaperone-mediated protein folding Source: UniProtKB
  • intracellular signal transduction Source: BHF-UCL
  • movement of cell or subcellular component Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of protein kinase activity Source: BHF-UCL
  • platelet aggregation Source: UniProtKB
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of endothelial cell chemotaxis Source: BHF-UCL
  • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of interleukin-1 beta production Source: BHF-UCL
  • positive regulation of tumor necrosis factor biosynthetic process Source: BHF-UCL
  • regulation of autophagy Source: ParkinsonsUK-UCL
  • regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  • regulation of mRNA stability Source: Reactome
  • regulation of protein phosphorylation Source: UniProtKB
  • regulation of translational initiation Source: ProtInc
  • response to unfolded protein Source: UniProtKB
  • response to virus Source: UniProtKB
  • retina homeostasis Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome

Keywordsi

Molecular functionChaperone
Biological processStress response

Enzyme and pathway databases

ReactomeiR-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-5687128. MAPK6/MAPK4 signaling.
SIGNORiP04792.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein beta-1
Short name:
HspB1
Alternative name(s):
28 kDa heat shock protein
Estrogen-regulated 24 kDa protein
Heat shock 27 kDa protein
Short name:
HSP 27
Stress-responsive protein 27
Short name:
SRP27
Gene namesi
Name:HSPB1
Synonyms:HSP27, HSP28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:5246. HSPB1.

Subcellular locationi

GO - Cellular componenti

  • axon cytoplasm Source: GOC
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: Ensembl
  • proteasome complex Source: BHF-UCL
  • spindle Source: UniProtKB-SubCell
  • Z disc Source: Ensembl

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease 2F (CMT2F)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. Onset of Charcot-Marie-Tooth disease type 2F is between 15 and 25 years with muscle weakness and atrophy usually beginning in feet and legs (peroneal distribution). Upper limb involvement occurs later.
See also OMIM:606595
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07748439P → L in HMN2B and CMT2F; increased aggregation; increased homooligomerization; decreased phosphorylation by MAPKAPK2; changed function in chaperone-mediated protein folding. 3 PublicationsCorresponds to variant dbSNP:rs557327165Ensembl.1
Natural variantiVAR_018507135S → F in CMT2F and HMN2B; decreased homodimerization; increased client proteins binding; increased function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins; alters CDK5-mediated phosphorylation of neurofilament proteins and indirectly impairs their anterograde axonal transport. 4 PublicationsCorresponds to variant dbSNP:rs28939680Ensembl.1
Natural variantiVAR_077488136R → L in CMT2F and HMN2B. 1 PublicationCorresponds to variant dbSNP:rs863225022Ensembl.1
Natural variantiVAR_018508136R → W in CMT2F; decreased homodimerization only with the wild-type protein; increased client proteins binding; increased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs28939681Ensembl.1
Natural variantiVAR_067085164T → A in CMT2F. 1 Publication1
Natural variantiVAR_077493188R → W in CMT2F; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs772767500Ensembl.1
Neuronopathy, distal hereditary motor, 2B (HMN2B)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neuromuscular disorder. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.
See also OMIM:608634
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07748334G → R in HMN2B; increased aggregation; increased homooligomerization; changed function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07748439P → L in HMN2B and CMT2F; increased aggregation; increased homooligomerization; decreased phosphorylation by MAPKAPK2; changed function in chaperone-mediated protein folding. 3 PublicationsCorresponds to variant dbSNP:rs557327165Ensembl.1
Natural variantiVAR_07748541E → K in HMN2B; increased aggregation; increased homooligomerization; changed function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07748684G → R in HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; increased function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07748799L → M in HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; increased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs121909113Ensembl.1
Natural variantiVAR_018506127R → W in HMN2B; decreased homodimerization; increased client proteins binding; increased function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins and indirectly impairs their anterograde axonal transport. 3 PublicationsCorresponds to variant dbSNP:rs29001571Ensembl.1
Natural variantiVAR_018507135S → F in CMT2F and HMN2B; decreased homodimerization; increased client proteins binding; increased function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins; alters CDK5-mediated phosphorylation of neurofilament proteins and indirectly impairs their anterograde axonal transport. 4 PublicationsCorresponds to variant dbSNP:rs28939680Ensembl.1
Natural variantiVAR_077488136R → L in CMT2F and HMN2B. 1 PublicationCorresponds to variant dbSNP:rs863225022Ensembl.1
Natural variantiVAR_077489140R → G in HMN2B; decreased thermal stability; changed protein structure; changed homooligomerization; loss of heterooligomerization with HSPB6; decreased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs121909112Ensembl.1
Natural variantiVAR_077490141K → Q in HMN2B; decreased thermal stability; changed protein structure; no effect on homooligomerization; changed heterooligomerization with HSPB6; slightly decreased function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_018509151T → I in HMN2B; no effect on homodimerization; no effect on client proteins binding; no effect on function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs28937568Ensembl.1
Natural variantiVAR_077492180T → I in HMN2B; unknown pathological significance. 2 Publications1
Natural variantiVAR_018510182P → L in HMN2B; decreased protein abundance; no effect on oligomerization; increased client proteins binding; no effect on function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins; indirectly impairs their anterograde axonal transport. 3 PublicationsCorresponds to variant dbSNP:rs28937569Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-78 and D-82. 1 Publication1
Mutagenesisi78S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-82. 1 Publication1
Mutagenesisi82S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78. 1 Publication1

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

DisGeNETi3315.
MalaCardsiHSPB1.
MIMi606595. phenotype.
608634. phenotype.
OpenTargetsiENSG00000106211.
Orphaneti99940. Autosomal dominant Charcot-Marie-Tooth disease type 2F.
139525. Distal hereditary motor neuropathy type 2.
PharmGKBiPA29511.

Chemistry databases

ChEMBLiCHEMBL5976.
DrugBankiDB06094. OGX-427.

Polymorphism and mutation databases

BioMutaiHSPB1.
DMDMi19855073.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001259271 – 205Heat shock protein beta-1Add BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12Omega-N-methylarginineCombined sources1
Modified residuei15Phosphoserine; by MAPKAPK2 and MAPKAPK3Combined sources3 Publications1
Modified residuei26PhosphoserineBy similarity1
Modified residuei65PhosphoserineCombined sources1
Modified residuei78Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5Combined sources6 Publications1
Modified residuei82Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5Combined sources7 Publications1
Modified residuei83PhosphoserineCombined sources1
Modified residuei86PhosphoserineCombined sources1
Modified residuei98PhosphoserineCombined sources1
Modified residuei123N6-acetyllysineCombined sources1
Modified residuei174PhosphothreonineCombined sources1
Modified residuei176PhosphoserineCombined sources1
Modified residuei199PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated upon exposure to protein kinase C activators and heat shock (PubMed:8325890). 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 (PubMed:1332886, PubMed:8093612, PubMed:19166925).4 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP04792.
PaxDbiP04792.
PeptideAtlasiP04792.
PRIDEiP04792.
TopDownProteomicsiP04792.

2D gel databases

DOSAC-COBS-2DPAGEiP04792.
OGPiP04792.
REPRODUCTION-2DPAGEiIPI00025512.
P04792.
SWISS-2DPAGEiP04792.
UCD-2DPAGEiP04792.

PTM databases

iPTMnetiP04792.
PhosphoSitePlusiP04792.
SwissPalmiP04792.

Expressioni

Tissue specificityi

Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle.1 Publication

Inductioni

Up-regulated in response to environmental stresses such as heat shock (PubMed:8325890). Up-regulated by estrogen stimulation (PubMed:2743305).2 Publications
(Microbial infection) Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000106211.
CleanExiHS_HSPB1.
ExpressionAtlasiP04792. baseline and differential.
GenevisibleiP04792. HS.

Organism-specific databases

HPAiCAB004439.
CAB047330.
CAB047331.
CAB047332.
HPA000497.

Interactioni

Subunit structurei

Homooligomer (PubMed:10383393). Homodimer; becomes monomeric upon activation (PubMed:20178975). Heterooligomer; with HSPB6 (PubMed:23948568). Associates with alpha- and beta-tubulin (PubMed:10777697). Interacts with TGFB1I1 (By similarity). Interacts with CRYAB (PubMed:1560006). Interacts with HSPB8 (PubMed:11342557). Interacts with HSPBAP1 (PubMed:10751411).By similarity7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • protein binding involved in protein folding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein kinase C binding Source: BHF-UCL
  • ubiquitin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109547. 400 interactors.
DIPiDIP-412N.
IntActiP04792. 307 interactors.
MINTiMINT-1368692.
STRINGi9606.ENSP00000248553.

Chemistry databases

BindingDBiP04792.

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi86 – 88Combined sources3
Beta strandi94 – 100Combined sources7
Turni102 – 104Combined sources3
Beta strandi107 – 114Combined sources8
Beta strandi117 – 124Combined sources8
Beta strandi136 – 143Combined sources8
Turni145 – 147Combined sources3
Helixi150 – 152Combined sources3
Beta strandi154 – 157Combined sources4
Beta strandi161 – 168Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N3JNMR-A/B80-176[»]
3Q9PX-ray2.00A90-171[»]
3Q9QX-ray2.20A/B90-171[»]
4MJHX-ray2.60A/C84-176[»]
B/D179-186[»]
ProteinModelPortaliP04792.
SMRiP04792.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni70 – 205Interaction with TGFB1I1By similarityAdd BLAST136

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOVERGENiHBG054766.
InParanoidiP04792.
KOiK04455.
OMAiDQSFGMP.
OrthoDBiEOG091G0USC.
PhylomeDBiP04792.
TreeFamiTF105049.

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. HSP20. 1 hit.

Sequencei

Sequence statusi: Complete.

P04792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS
60 70 80 90 100
WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD
110 120 130 140 150
VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP
160 170 180 190 200
TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD

ETAAK
Length:205
Mass (Da):22,783
Last modified:September 26, 2001 - v2
Checksum:i1B4DC44A6F6606D5
GO

Sequence cautioni

The sequence AAA62175 differs from that shown. Reason: Frameshift at position 194.Curated
The sequence AAB20722 differs from that shown. Reason: Frameshift at position 194.Curated
The sequence CAA34498 differs from that shown. Reason: Frameshift at position 194.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10L → I AA sequence (PubMed:2295696).Curated1
Sequence conflicti109L → R in AAH12292 (PubMed:15489334).Curated1
Sequence conflicti121T → S in AAH12292 (PubMed:15489334).Curated1
Sequence conflicti127R → L in AAH12292 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07748334G → R in HMN2B; increased aggregation; increased homooligomerization; changed function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07748439P → L in HMN2B and CMT2F; increased aggregation; increased homooligomerization; decreased phosphorylation by MAPKAPK2; changed function in chaperone-mediated protein folding. 3 PublicationsCorresponds to variant dbSNP:rs557327165Ensembl.1
Natural variantiVAR_07748541E → K in HMN2B; increased aggregation; increased homooligomerization; changed function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07748684G → R in HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; increased function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07748799L → M in HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; increased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs121909113Ensembl.1
Natural variantiVAR_018506127R → W in HMN2B; decreased homodimerization; increased client proteins binding; increased function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins and indirectly impairs their anterograde axonal transport. 3 PublicationsCorresponds to variant dbSNP:rs29001571Ensembl.1
Natural variantiVAR_018507135S → F in CMT2F and HMN2B; decreased homodimerization; increased client proteins binding; increased function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins; alters CDK5-mediated phosphorylation of neurofilament proteins and indirectly impairs their anterograde axonal transport. 4 PublicationsCorresponds to variant dbSNP:rs28939680Ensembl.1
Natural variantiVAR_077488136R → L in CMT2F and HMN2B. 1 PublicationCorresponds to variant dbSNP:rs863225022Ensembl.1
Natural variantiVAR_018508136R → W in CMT2F; decreased homodimerization only with the wild-type protein; increased client proteins binding; increased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs28939681Ensembl.1
Natural variantiVAR_077489140R → G in HMN2B; decreased thermal stability; changed protein structure; changed homooligomerization; loss of heterooligomerization with HSPB6; decreased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs121909112Ensembl.1
Natural variantiVAR_077490141K → Q in HMN2B; decreased thermal stability; changed protein structure; no effect on homooligomerization; changed heterooligomerization with HSPB6; slightly decreased function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_018509151T → I in HMN2B; no effect on homodimerization; no effect on client proteins binding; no effect on function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs28937568Ensembl.1
Natural variantiVAR_077491156S → Y Rare polymorphism; no effect on oligomerization; no effect on client proteins binding; no effect on function in chaperone-mediated protein folding. 1 Publication1
Natural variantiVAR_067085164T → A in CMT2F. 1 Publication1
Natural variantiVAR_077492180T → I in HMN2B; unknown pathological significance. 2 Publications1
Natural variantiVAR_018510182P → L in HMN2B; decreased protein abundance; no effect on oligomerization; increased client proteins binding; no effect on function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins; indirectly impairs their anterograde axonal transport. 3 PublicationsCorresponds to variant dbSNP:rs28937569Ensembl.1
Natural variantiVAR_077493188R → W in CMT2F; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs772767500Ensembl.1
Natural variantiVAR_077494190Q → H Found in a patient with sporadic amyotrophic lateral sclerosis; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs764297134Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39370 Genomic DNA. Translation: AAA62175.1. Frameshift.
X54079 mRNA. Translation: CAA38016.1.
Z23090 mRNA. Translation: CAA80636.1.
AB020027 mRNA. Translation: BAB17232.1.
U90906 mRNA. Translation: AAB51056.1.
CR407614 mRNA. Translation: CAG28542.1.
CR536489 mRNA. Translation: CAG38728.1.
BT019888 mRNA. Translation: AAV38691.1.
AK311894 mRNA. Translation: BAG34835.1.
DQ379985 Genomic DNA. Translation: ABC88475.1.
AC006388 Genomic DNA. No translation available.
CH471220 Genomic DNA. Translation: EAW71803.1.
BC000510 mRNA. Translation: AAH00510.1.
BC012292 mRNA. Translation: AAH12292.1.
BC012768 mRNA. Translation: AAH12768.1.
BC014920 mRNA. Translation: AAH14920.1.
BC073768 mRNA. Translation: AAH73768.1.
X16477 mRNA. Translation: CAA34498.1. Frameshift.
S74571 mRNA. Translation: AAB20722.1. Frameshift.
CCDSiCCDS5583.1.
PIRiS12102. HHHU27.
RefSeqiNP_001531.1. NM_001540.3.
UniGeneiHs.520973.

Genome annotation databases

EnsembliENST00000248553; ENSP00000248553; ENSG00000106211.
GeneIDi3315.
KEGGihsa:3315.

Cross-referencesi

Web resourcesi

Inherited peripheral neuropathies mutation db
NIEHS SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39370 Genomic DNA. Translation: AAA62175.1. Frameshift.
X54079 mRNA. Translation: CAA38016.1.
Z23090 mRNA. Translation: CAA80636.1.
AB020027 mRNA. Translation: BAB17232.1.
U90906 mRNA. Translation: AAB51056.1.
CR407614 mRNA. Translation: CAG28542.1.
CR536489 mRNA. Translation: CAG38728.1.
BT019888 mRNA. Translation: AAV38691.1.
AK311894 mRNA. Translation: BAG34835.1.
DQ379985 Genomic DNA. Translation: ABC88475.1.
AC006388 Genomic DNA. No translation available.
CH471220 Genomic DNA. Translation: EAW71803.1.
BC000510 mRNA. Translation: AAH00510.1.
BC012292 mRNA. Translation: AAH12292.1.
BC012768 mRNA. Translation: AAH12768.1.
BC014920 mRNA. Translation: AAH14920.1.
BC073768 mRNA. Translation: AAH73768.1.
X16477 mRNA. Translation: CAA34498.1. Frameshift.
S74571 mRNA. Translation: AAB20722.1. Frameshift.
CCDSiCCDS5583.1.
PIRiS12102. HHHU27.
RefSeqiNP_001531.1. NM_001540.3.
UniGeneiHs.520973.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N3JNMR-A/B80-176[»]
3Q9PX-ray2.00A90-171[»]
3Q9QX-ray2.20A/B90-171[»]
4MJHX-ray2.60A/C84-176[»]
B/D179-186[»]
ProteinModelPortaliP04792.
SMRiP04792.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109547. 400 interactors.
DIPiDIP-412N.
IntActiP04792. 307 interactors.
MINTiMINT-1368692.
STRINGi9606.ENSP00000248553.

Chemistry databases

BindingDBiP04792.
ChEMBLiCHEMBL5976.
DrugBankiDB06094. OGX-427.

PTM databases

iPTMnetiP04792.
PhosphoSitePlusiP04792.
SwissPalmiP04792.

Polymorphism and mutation databases

BioMutaiHSPB1.
DMDMi19855073.

2D gel databases

DOSAC-COBS-2DPAGEiP04792.
OGPiP04792.
REPRODUCTION-2DPAGEiIPI00025512.
P04792.
SWISS-2DPAGEiP04792.
UCD-2DPAGEiP04792.

Proteomic databases

EPDiP04792.
PaxDbiP04792.
PeptideAtlasiP04792.
PRIDEiP04792.
TopDownProteomicsiP04792.

Protocols and materials databases

DNASUi3315.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248553; ENSP00000248553; ENSG00000106211.
GeneIDi3315.
KEGGihsa:3315.

Organism-specific databases

CTDi3315.
DisGeNETi3315.
GeneCardsiHSPB1.
GeneReviewsiHSPB1.
HGNCiHGNC:5246. HSPB1.
HPAiCAB004439.
CAB047330.
CAB047331.
CAB047332.
HPA000497.
MalaCardsiHSPB1.
MIMi602195. gene.
606595. phenotype.
608634. phenotype.
neXtProtiNX_P04792.
OpenTargetsiENSG00000106211.
Orphaneti99940. Autosomal dominant Charcot-Marie-Tooth disease type 2F.
139525. Distal hereditary motor neuropathy type 2.
PharmGKBiPA29511.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOVERGENiHBG054766.
InParanoidiP04792.
KOiK04455.
OMAiDQSFGMP.
OrthoDBiEOG091G0USC.
PhylomeDBiP04792.
TreeFamiTF105049.

Enzyme and pathway databases

ReactomeiR-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-5687128. MAPK6/MAPK4 signaling.
SIGNORiP04792.

Miscellaneous databases

ChiTaRSiHSPB1. human.
GeneWikiiHsp27.
GenomeRNAii3315.
PROiPR:P04792.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106211.
CleanExiHS_HSPB1.
ExpressionAtlasiP04792. baseline and differential.
GenevisibleiP04792. HS.

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. HSP20. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHSPB1_HUMAN
AccessioniPrimary (citable) accession number: P04792
Secondary accession number(s): B2R4N8
, Q6FI47, Q96C20, Q96EI7, Q9UC31, Q9UC34, Q9UC35, Q9UC36
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: September 26, 2001
Last modified: April 12, 2017
This is version 209 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 7
    Human chromosome 7: 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.