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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone
Biological processStress response

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

SIGNOR Signaling Network Open Resource

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SIGNORi
P04792

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P04792 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HSPB1
Synonyms:HSP27, HSP28
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000106211.8

Human Gene Nomenclature Database

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HGNCi
HGNC:5246 HSPB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602195 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P04792

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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. 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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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 PublicationsCorresponds to variant dbSNP:rs1393404971Ensembl.1
Natural variantiVAR_07812953G → D in HMN2B; no effect on dimerization; no effect on cytoplasmic location; no effect on dimerization. 1 PublicationCorresponds to variant dbSNP:rs375244209EnsemblClinVar.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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
3315

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
HSPB1

MalaCards human disease database

More...
MalaCardsi
HSPB1
MIMi606595 phenotype
608634 phenotype

Open Targets

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OpenTargetsi
ENSG00000106211

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
99940 Autosomal dominant Charcot-Marie-Tooth disease type 2F
139525 Distal hereditary motor neuropathy type 2

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29511

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5976

Drug and drug target database

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DrugBanki
DB06094 OGX-427

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HSPB1

Domain mapping of disease mutations (DMDM)

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DMDMi
19855073

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001259271 – 205Heat shock protein beta-1Add BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
P04792

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P04792

PeptideAtlas

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PeptideAtlasi
P04792

PRoteomics IDEntifications database

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PRIDEi
P04792

ProteomicsDB human proteome resource

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ProteomicsDBi
51743

Consortium for Top Down Proteomics

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TopDownProteomicsi
P04792

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P04792

USC-OGP 2-DE database

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OGPi
P04792

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00025512
P04792

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P04792

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P04792

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P04792

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P04792

SwissPalm database of S-palmitoylation events

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SwissPalmi
P04792

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000106211 Expressed in 230 organ(s), highest expression level in myometrium

CleanEx database of gene expression profiles

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CleanExi
HS_HSPB1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P04792 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P04792 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004439
CAB047330
CAB047331
CAB047332
HPA000497

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109547, 422 interactors

Database of interacting proteins

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DIPi
DIP-412N

Protein interaction database and analysis system

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IntActi
P04792, 320 interactors

Molecular INTeraction database

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MINTi
P04792

STRING: functional protein association networks

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STRINGi
9606.ENSP00000248553

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P04792

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P04792

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04792

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini76 – 184sHSPPROSITE-ProRule annotationAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni70 – 205Interaction with TGFB1I1By similarityAdd BLAST136

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3591 Eukaryota
ENOG410YERS LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155882

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG054766

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P04792

KEGG Orthology (KO)

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KOi
K04455

Identification of Orthologs from Complete Genome Data

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OMAi
FDQSFGM

Database of Orthologous Groups

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OrthoDBi
EOG091G0USC

Database for complete collections of gene phylogenies

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PhylomeDBi
P04792

TreeFam database of animal gene trees

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TreeFami
TF105049

Family and domain databases

Conserved Domains Database

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CDDi
cd06475 ACD_HspB1_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.790, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002068 A-crystallin/Hsp20_dom
IPR037876 ACD_HspB1
IPR001436 Alpha-crystallin/HSP
IPR031107 HSP20
IPR008978 HSP20-like_chaperone

The PANTHER Classification System

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PANTHERi
PTHR11527 PTHR11527, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00011 HSP20, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00299 ACRYSTALLIN

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49764 SSF49764, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01031 SHSP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

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

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1B4DC44A6F6606D5
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WE04F8WE04_HUMAN
Heat shock protein beta-1
HSPB1
186Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9J3N8C9J3N8_HUMAN
Heat shock protein beta-1
HSPB1
37Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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 PublicationsCorresponds to variant dbSNP:rs1393404971Ensembl.1
Natural variantiVAR_07812953G → D in HMN2B; no effect on dimerization; no effect on cytoplasmic location; no effect on dimerization. 1 PublicationCorresponds to variant dbSNP:rs375244209EnsemblClinVar.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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

The Consensus CDS (CCDS) project

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CCDSi
CCDS5583.1

Protein sequence database of the Protein Information Resource

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PIRi
S12102 HHHU27

NCBI Reference Sequences

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RefSeqi
NP_001531.1, NM_001540.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.520973

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000248553; ENSP00000248553; ENSG00000106211

Database of genes from NCBI RefSeq genomes

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GeneIDi
3315

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3315

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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, 422 interactors
DIPiDIP-412N
IntActiP04792, 320 interactors
MINTiP04792
STRINGi9606.ENSP00000248553

Chemistry databases

BindingDBiP04792
ChEMBLiCHEMBL5976
DrugBankiDB06094 OGX-427

Protein family/group databases

MoonDBiP04792 Predicted

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
ProteomicsDBi51743
TopDownProteomicsiP04792

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3315
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248553; ENSP00000248553; ENSG00000106211
GeneIDi3315
KEGGihsa:3315

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3315
DisGeNETi3315
EuPathDBiHostDB:ENSG00000106211.8

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HSPB1
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

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3591 Eukaryota
ENOG410YERS LUCA
GeneTreeiENSGT00940000155882
HOVERGENiHBG054766
InParanoidiP04792
KOiK04455
OMAiFDQSFGM
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
HSPB1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Hsp27

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
3315

Protein Ontology

More...
PROi
PR:P04792

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000106211 Expressed in 230 organ(s), highest expression level in myometrium
CleanExiHS_HSPB1
ExpressionAtlasiP04792 baseline and differential
GenevisibleiP04792 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHSPB1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04792
Secondary accession number(s): B2R4N8
, Q6FI47, Q96C20, Q96EI7, Q9UC31, Q9UC34, Q9UC35, Q9UC36
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: September 26, 2001
Last modified: December 5, 2018
This is version 226 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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