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Entry version 42 (13 Feb 2019)
Sequence version 1 (27 May 2015)
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Protein

Heat shock 70 kDa protein 1A

Gene

HSPA1A

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

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401).2 Publications7 Publications
(Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei71ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi12 – 15ATP4
Nucleotide bindingi202 – 204ATP3
Nucleotide bindingi268 – 275ATP8
Nucleotide bindingi339 – 342ATP4

<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

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, Host cell receptor for virus entry, Receptor
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-168330 Viral RNP Complexes in the Host Cell Nucleus
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-3371568 Attenuation phase
R-HSA-3371571 HSF1-dependent transactivation
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-6798695 Neutrophil degranulation

SIGNOR Signaling Network Open Resource

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SIGNORi
P0DMV8

<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 70 kDa protein 1AImported
Alternative name(s):
Heat shock 70 kDa protein 1
Short name:
HSP70-12 Publications
Short name:
HSP70.1
<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:HSPA1A
Synonyms:HSP721 Publication, HSPA1, HSX70
<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 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000204389.9

Human Gene Nomenclature Database

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HGNCi
HGNC:5232 HSPA1A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
140550 gene
603012 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P0DMV8

<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

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>Mutagenesisi10D → A: Reduces affinity for ADP. 1 Publication1
Mutagenesisi77K → Q: No loss of acetylation and ATPase activity. Exhibits normal protein refolding activity during the early phase but exhibits defects in ubiquitin-mediated protein degradation during the later phase. 1 Publication1
Mutagenesisi77K → R: Significant loss of acetylation and ATPase activity. Decreased binding to HOPX and HSP90 and increased binding to STUB1 and NAA10. Impaired capacity for protein refolding during the early phase after stress but shows normal protein degradation activity in the late phase. 1 Publication1
Mutagenesisi199D → A: Reduces affinity for ADP. 1 Publication1
Mutagenesisi561K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
3303
3304

Open Targets

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OpenTargetsi
ENSG00000204388
ENSG00000204389

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5460

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HSPA1A

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000782492 – 641Heat shock 70 kDa protein 1AAdd BLAST640

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 residuei2N-acetylalanineCombined sources1
Modified residuei77N6-acetyllysine1 Publication1
Modified residuei108N6-acetyllysineCombined sources1
Modified residuei246N6-acetyllysineCombined sources1
Modified residuei348N6-acetyllysineCombined sources1
Modified residuei469Omega-N-methylarginineCombined sources1
Modified residuei561N6,N6,N6-trimethyllysine; by METTL21A; alternateCombined sources2 Publications1
Modified residuei561N6,N6-dimethyllysine; alternateCombined sources1
Modified residuei631PhosphoserineCombined sources1
Modified residuei633PhosphoserineCombined sources1
Modified residuei636PhosphothreonineCombined 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

In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0DMV8

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

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PaxDbi
P0DMV8

PeptideAtlas

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PeptideAtlasi
P0DMV8

PRoteomics IDEntifications database

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PRIDEi
P0DMV8

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00304925

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P0DMV8

GlyConnect protein glycosylation platform

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GlyConnecti
1295

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P0DMV8

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

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PhosphoSitePlusi
P0DMV8

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P0DMV8

<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 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

By heat shock.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000204389 Expressed in 237 organ(s), highest expression level in endothelial cell

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P0DMV8 baseline and differential

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB017451
CAB032815
HPA052504

<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

Component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2 (PubMed:21081504, PubMed:12853476, PubMed:18620420, PubMed:17233114, PubMed:15383005, PubMed:15963462). Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed (PubMed:11274138). Interacts with TRIM5 (via B30.2/SPRY domain) (PubMed:20053985). Interacts with METTL21A (PubMed:23921388). Interacts with DNAAF2 (By similarity). Interacts with PRKN (PubMed:24270810). Interacts with FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction enhances NOD2 stability (PubMed:24790089). Interacts with DNAJC9 (via J domain) (PubMed:17182002). Interacts with ATF5; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes (PubMed:22528486). Interacts with RNF207 (via the C-terminus); this interaction additively increases KCNH2 expression (PubMed:25281747). Interacts with HSF1 (via transactivation domain); this interaction results in the inhibition of heat shock- and HSF1-induced transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:7935376, PubMed:9499401). Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and the non-acetylated form interact with HOPX and STUB1 respectively (PubMed:27708256). Interacts with NEDD1 (PubMed:27137183). Interacts (via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105 (PubMed:24318877). Interacts with SMAD3 (PubMed:24613385). Interacts with DNAJC8 (PubMed:27133716).By similarity27 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

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P0DMV8

Protein interaction database and analysis system

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IntActi
P0DMV8, 60 interactors

Molecular INTeraction database

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MINTi
P0DMV8

STRING: functional protein association networks

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STRINGi
9606.ENSP00000364802

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0DMV8

<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

1641
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1HJOX-ray2.30A3-382[»]
1S3XX-ray1.84A1-382[»]
1XQSX-ray2.90C/D184-371[»]
2E88X-ray1.80A1-388[»]
2E8AX-ray1.77A1-388[»]
2LMGNMR-A537-610[»]
3A8YX-ray2.30A/B1-388[»]
3ATUX-ray1.65A1-388[»]
3ATVX-ray1.58A1-388[»]
3AY9X-ray1.75A1-388[»]
3D2EX-ray2.35B/D1-382[»]
3D2FX-ray2.30B/D1-382[»]
3JXUX-ray2.14A1-387[»]
3LOFX-ray2.40A/B/C/D/E/F534-641[»]
3Q49X-ray1.54C634-641[»]
4IO8X-ray2.58A1-382[»]
4J8FX-ray2.70A1-382[»]
4PO2X-ray2.00A/B386-613[»]
4WV5X-ray2.04A/B395-543[»]
4WV7X-ray2.42A/B395-543[»]
5AQWX-ray1.53A1-380[»]
5AQXX-ray2.12A1-380[»]
5AQYX-ray1.56A1-380[»]
5AQZX-ray1.65A1-380[»]
5AR0X-ray1.90A1-380[»]
5BN8X-ray1.34A1-388[»]
5BN9X-ray1.69A1-388[»]
5BPLX-ray1.93A1-388[»]
5BPMX-ray1.83A1-388[»]
5BPNX-ray2.10A1-388[»]
5GJJNMR-A385-641[»]
5MKRX-ray1.87A1-380[»]
5MKSX-ray1.99A1-380[»]
5XI9NMR-A381-564[»]
5XIRNMR-A381-564[»]
6FHKX-ray1.66A/B1-381[»]
6G3RX-ray1.40A3-382[»]
6G3SX-ray2.30A3-382[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0DMV8

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

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SMRi
P0DMV8

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

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>Regioni2 – 386Nucleotide-binding domain (NBD)By similarityAdd BLAST385
Regioni394 – 509Substrate-binding domain (SBD)By similarityAdd BLAST116

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.2 Publications

<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 heat shock protein 70 family.Curated

Phylogenomic databases

KEGG Orthology (KO)

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KOi
K03283

Identification of Orthologs from Complete Genome Data

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OMAi
FRGEEKQ

Database of Orthologous Groups

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OrthoDBi
288077at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P0DMV8

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1270.10, 1 hit
2.60.34.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam

The PANTHER Classification System

More...
PANTHERi
PTHR19375 PTHR19375, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00012 HSP70, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00301 HEATSHOCK70

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 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>Sequences (2+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: P0DMV8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK
110 120 130 140 150
PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF
160 170 180 190 200
NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK
260 270 280 290 300
KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
310 320 330 340 350
RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL
360 370 380 390 400
QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS
410 420 430 440 450
LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490 500
KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK
510 520 530 540 550
ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK
560 570 580 590 600
SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
610 620 630 640
QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
Length:641
Mass (Da):70,052
Last modified:May 27, 2015 - v1
<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:i78F513118C96DE66
GO
Isoform 2 (identifier: P0DMV8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-150: Missing.

Show »
Length:586
Mass (Da):63,937
Checksum:i6FBA863FEACE9DF1
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
V9GZ37V9GZ37_HUMAN
Heat shock 70 kDa protein 1A
HSPA1A
476Annotation 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>

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 conflicti7I → V in AAA52697 (PubMed:3931075).Curated1
Sequence conflicti7I → V in CAA28381 (PubMed:3786141).Curated1
Sequence conflicti355N → D in BAG65428 (PubMed:14702039).Curated1
Sequence conflicti370A → G in AAA52697 (PubMed:3931075).Curated1
Sequence conflicti469Missing in AAA52697 (PubMed:3931075).Curated1
Sequence conflicti497K → N in BAG65428 (PubMed:14702039).Curated1

Natural variant

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_029053110E → D2 PublicationsCorresponds to variant dbSNP:rs562047Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_04442796 – 150Missing in isoform 2. 1 PublicationAdd BLAST55

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M11717 Genomic DNA Translation: AAA52697.1
M59828 Genomic DNA Translation: AAA63226.1
BA000025 Genomic DNA Translation: BAB63300.1
AF134726 Genomic DNA Translation: AAD21816.1
AK304652 mRNA Translation: BAG65428.1
DQ451402 Genomic DNA Translation: ABD96830.1
AL671762 Genomic DNA No translation available.
BC002453 mRNA Translation: AAH02453.1
M24743 Genomic DNA Translation: AAA59844.1
X04676 Genomic DNA Translation: CAA28381.1
X04677 Genomic DNA Translation: CAA28382.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS34414.1 [P0DMV8-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A29160
A45871
I59139
I79540

NCBI Reference Sequences

More...
RefSeqi
NP_005336.3, NM_005345.5 [P0DMV8-1]
NP_005337.2, NM_005346.4 [P0DMV8-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.274402
Hs.702139
Hs.719966
Hs.743411

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000375651; ENSP00000364802; ENSG00000204389 [P0DMV8-1]
ENST00000400040; ENSP00000382915; ENSG00000215328
ENST00000430065; ENSP00000404524; ENSG00000235941 [P0DMV8-1]
ENST00000433487; ENSP00000408907; ENSG00000234475 [P0DMV8-1]
ENST00000441618; ENSP00000406359; ENSG00000237724 [P0DMV8-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3303
3304

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3303
hsa:3304

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11717 Genomic DNA Translation: AAA52697.1
M59828 Genomic DNA Translation: AAA63226.1
BA000025 Genomic DNA Translation: BAB63300.1
AF134726 Genomic DNA Translation: AAD21816.1
AK304652 mRNA Translation: BAG65428.1
DQ451402 Genomic DNA Translation: ABD96830.1
AL671762 Genomic DNA No translation available.
BC002453 mRNA Translation: AAH02453.1
M24743 Genomic DNA Translation: AAA59844.1
X04676 Genomic DNA Translation: CAA28381.1
X04677 Genomic DNA Translation: CAA28382.1
CCDSiCCDS34414.1 [P0DMV8-1]
PIRiA29160
A45871
I59139
I79540
RefSeqiNP_005336.3, NM_005345.5 [P0DMV8-1]
NP_005337.2, NM_005346.4 [P0DMV8-1]
UniGeneiHs.274402
Hs.702139
Hs.719966
Hs.743411

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HJOX-ray2.30A3-382[»]
1S3XX-ray1.84A1-382[»]
1XQSX-ray2.90C/D184-371[»]
2E88X-ray1.80A1-388[»]
2E8AX-ray1.77A1-388[»]
2LMGNMR-A537-610[»]
3A8YX-ray2.30A/B1-388[»]
3ATUX-ray1.65A1-388[»]
3ATVX-ray1.58A1-388[»]
3AY9X-ray1.75A1-388[»]
3D2EX-ray2.35B/D1-382[»]
3D2FX-ray2.30B/D1-382[»]
3JXUX-ray2.14A1-387[»]
3LOFX-ray2.40A/B/C/D/E/F534-641[»]
3Q49X-ray1.54C634-641[»]
4IO8X-ray2.58A1-382[»]
4J8FX-ray2.70A1-382[»]
4PO2X-ray2.00A/B386-613[»]
4WV5X-ray2.04A/B395-543[»]
4WV7X-ray2.42A/B395-543[»]
5AQWX-ray1.53A1-380[»]
5AQXX-ray2.12A1-380[»]
5AQYX-ray1.56A1-380[»]
5AQZX-ray1.65A1-380[»]
5AR0X-ray1.90A1-380[»]
5BN8X-ray1.34A1-388[»]
5BN9X-ray1.69A1-388[»]
5BPLX-ray1.93A1-388[»]
5BPMX-ray1.83A1-388[»]
5BPNX-ray2.10A1-388[»]
5GJJNMR-A385-641[»]
5MKRX-ray1.87A1-380[»]
5MKSX-ray1.99A1-380[»]
5XI9NMR-A381-564[»]
5XIRNMR-A381-564[»]
6FHKX-ray1.66A/B1-381[»]
6G3RX-ray1.40A3-382[»]
6G3SX-ray2.30A3-382[»]
ProteinModelPortaliP0DMV8
SMRiP0DMV8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP0DMV8
IntActiP0DMV8, 60 interactors
MINTiP0DMV8
STRINGi9606.ENSP00000364802

Chemistry databases

BindingDBiP0DMV8
ChEMBLiCHEMBL5460

PTM databases

CarbonylDBiP0DMV8
GlyConnecti1295
iPTMnetiP0DMV8
PhosphoSitePlusiP0DMV8
SwissPalmiP0DMV8

Polymorphism and mutation databases

BioMutaiHSPA1A

2D gel databases

REPRODUCTION-2DPAGEiIPI00304925

Proteomic databases

jPOSTiP0DMV8
PaxDbiP0DMV8
PeptideAtlasiP0DMV8
PRIDEiP0DMV8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375651; ENSP00000364802; ENSG00000204389 [P0DMV8-1]
ENST00000400040; ENSP00000382915; ENSG00000215328
ENST00000430065; ENSP00000404524; ENSG00000235941 [P0DMV8-1]
ENST00000433487; ENSP00000408907; ENSG00000234475 [P0DMV8-1]
ENST00000441618; ENSP00000406359; ENSG00000237724 [P0DMV8-1]
GeneIDi3303
3304
KEGGihsa:3303
hsa:3304

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3303
3304
DisGeNETi3303
3304
EuPathDBiHostDB:ENSG00000204389.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HSPA1A
HGNCiHGNC:5232 HSPA1A
HPAiCAB017451
CAB032815
HPA052504
MIMi140550 gene
603012 gene
neXtProtiNX_P0DMV8
OpenTargetsiENSG00000204388
ENSG00000204389

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

KOiK03283
OMAiFRGEEKQ
OrthoDBi288077at2759
PhylomeDBiP0DMV8

Enzyme and pathway databases

ReactomeiR-HSA-168330 Viral RNP Complexes in the Host Cell Nucleus
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-3371568 Attenuation phase
R-HSA-3371571 HSF1-dependent transactivation
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-6798695 Neutrophil degranulation
SIGNORiP0DMV8

Miscellaneous databases

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

More...
ChiTaRSi
HSPA1A human

Protein Ontology

More...
PROi
PR:P0DMV8

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000204389 Expressed in 237 organ(s), highest expression level in endothelial cell
ExpressionAtlasiP0DMV8 baseline and differential

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 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 nameiHS71A_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: P0DMV8
Secondary accession number(s): B4E3B6
, P08107, P19790, Q5JQI4, Q5SP17, Q9UQL9, Q9UQM0
<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: May 27, 2015
Last sequence update: May 27, 2015
Last modified: February 13, 2019
This is version 42 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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