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Protein

Heat shock protein beta-1

Gene

HSPB1

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 (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 homodimerization activity 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
  • 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: ProtInc
  • response to virus Source: UniProtKB
  • retina homeostasis Source: UniProtKB

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

Protein family/group databases

MoonDBiP04792 Predicted

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

EuPathDBiHostDB:ENSG00000106211.8
HGNCiHGNC:5246 HSPB1
MIMi602195 gene
neXtProtiNX_P04792

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, 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_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:rs28939681EnsemblClinVar.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)11 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_0781287P → S in HMN2B; induces hyperphosphorylation of neurofilaments; no effect on cytoplasmic location; no effect on dimerization. 1 Publication1
Natural variantiVAR_07748334G → R in HMN2B; increased aggregation; increased homooligomerization; changed function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07748541E → K in HMN2B; increased aggregation; increased homooligomerization; changed function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07812953G → D in HMN2B; no effect on dimerization; no effect on cytoplasmic location; no effect on dimerization. 1 PublicationCorresponds to variant dbSNP:rs375244209Ensembl.1
Natural variantiVAR_07748684G → R in HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; decreased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs770272088EnsemblClinVar.1
Natural variantiVAR_07748799L → M in HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; decreased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs121909113EnsemblClinVar.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. 4 PublicationsCorresponds to variant dbSNP:rs29001571EnsemblClinVar.1
Natural variantiVAR_078130128Q → R in HMN2B; unknown pathological significance; no effect on dimerization; no effect on cytoplasmic location; no effect on dimerization. 1 PublicationCorresponds to variant dbSNP:rs558882005EnsemblClinVar.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:rs121909112EnsemblClinVar.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. 3 PublicationsCorresponds to variant dbSNP:rs28937568EnsemblClinVar.1
Natural variantiVAR_078131175 – 205Missing in HMN2B. 1 PublicationAdd BLAST31
Natural variantiVAR_077492180T → I in HMN2B; unknown pathological significance. 3 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:rs28937569EnsemblClinVar.1
Natural variantiVAR_078132187S → L in HMN2B; formation of large cytoplasmic aggregates; no effect on dimerization. 1 Publication1

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
GeneReviewsiHSPB1
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
ProteomicsDBi51743
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 homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein kinase C binding Source: BHF-UCL
  • ubiquitin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109547, 417 interactors
DIPiDIP-412N
IntActiP04792, 327 interactors
MINTiP04792
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

ProteinModelPortaliP04792
SMRiP04792
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 184sHSPPROSITE-ProRule annotationAdd BLAST109

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
OMAiFDQSFGM
OrthoDBiEOG091G0USC
PhylomeDBiP04792
TreeFamiTF105049

Family and domain databases

CDDicd06475 ACD_HspB1_like, 1 hit
Gene3Di2.60.40.790, 1 hit
InterProiView protein in InterPro
IPR002068 A-crystallin/Hsp20_dom
IPR037876 ACD_HspB1
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.

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_0781287P → S in HMN2B; induces hyperphosphorylation of neurofilaments; no effect on cytoplasmic location; no effect on dimerization. 1 Publication1
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. 4 PublicationsCorresponds to variant dbSNP:rs557327165EnsemblClinVar.1
Natural variantiVAR_07748541E → K in HMN2B; increased aggregation; increased homooligomerization; changed function in chaperone-mediated protein folding. 2 Publications1
Natural variantiVAR_07812953G → D in HMN2B; no effect on dimerization; no effect on cytoplasmic location; no effect on dimerization. 1 PublicationCorresponds to variant dbSNP:rs375244209Ensembl.1
Natural variantiVAR_07748684G → R in HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; decreased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs770272088EnsemblClinVar.1
Natural variantiVAR_07748799L → M in HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; decreased function in chaperone-mediated protein folding. 2 PublicationsCorresponds to variant dbSNP:rs121909113EnsemblClinVar.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. 4 PublicationsCorresponds to variant dbSNP:rs29001571EnsemblClinVar.1
Natural variantiVAR_078130128Q → R in HMN2B; unknown pathological significance; no effect on dimerization; no effect on cytoplasmic location; no effect on dimerization. 1 PublicationCorresponds to variant dbSNP:rs558882005EnsemblClinVar.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:rs28939680EnsemblClinVar.1
Natural variantiVAR_077488136R → L in CMT2F and HMN2B. 1 PublicationCorresponds to variant dbSNP:rs863225022EnsemblClinVar.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:rs28939681EnsemblClinVar.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:rs121909112EnsemblClinVar.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. 3 PublicationsCorresponds to variant dbSNP:rs28937568EnsemblClinVar.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_078131175 – 205Missing in HMN2B. 1 PublicationAdd BLAST31
Natural variantiVAR_077492180T → I in HMN2B; unknown pathological significance. 3 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:rs28937569EnsemblClinVar.1
Natural variantiVAR_078132187S → L in HMN2B; formation of large cytoplasmic aggregates; no effect on dimerization. 1 Publication1
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

Similar proteinsi

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: July 18, 2018
This is version 222 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

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