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Protein

Endoplasmic reticulum chaperone BiP

Gene

HSPA5

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

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating.By similarity7 Publications

Caution

AMPylation was initially reported to take place at Ser-365 and Thr-366 in vitro, and promote activation of HSPA5/BiP (PubMed:25601083). However, it was later shown that AMPylation takes place at Thr-518 and leads to inactivation of HSPA5/BiP.By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The chaperone activity is regulated by ATP-induced allosteric coupling of the nucleotide-binding (NBD) and substrate-binding (SBD) domains. In the ADP-bound and nucleotide-free (apo) states, the two domains have little interaction (PubMed:26655470). In contrast, in the ATP-bound state the two domains are tightly coupled, which results in drastically accelerated kinetics in both binding and release of polypeptide substrates (PubMed:26655470). J domain-containing co-chaperones (DNAJB9/ERdj4 or DNAJC10/ERdj5) stimulate the ATPase activity and are required for efficient substrate recognition by HSPA5/BiP (By similarity). Homooligomerization inactivates participating HSPA5/BiP protomers and probably act as reservoirs to store HSPA5/BiP molecules when they are not needed by the cell (By similarity).1 PublicationBy similarity1 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 sitei96ATP1 Publication1

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 bindingi36 – 39ATP1 Publication4
Nucleotide bindingi227 – 229ATP1 Publication3
Nucleotide bindingi293 – 300ATP1 Publication8
Nucleotide bindingi364 – 367ATP1 Publication4

<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

  • ATPase activity Source: AgBase
  • ATPase activity, coupled Source: GO_Central
  • ATP binding Source: GO_Central
  • cadherin binding Source: BHF-UCL
  • calcium ion binding Source: UniProtKB
  • chaperone binding Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • heat shock protein binding Source: GO_Central
  • misfolded protein binding Source: UniProtKB
  • protein binding involved in protein folding Source: GO_Central
  • protein domain specific binding Source: UniProtKB
  • ribosome binding Source: Ensembl
  • ubiquitin protein ligase binding Source: UniProtKB
  • unfolded protein binding Source: GO_Central

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, Hydrolase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114608 Platelet degranulation
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-381033 ATF6 (ATF6-alpha) activates chaperones
R-HSA-381042 PERK regulates gene expression
R-HSA-381070 IRE1alpha activates chaperones
R-HSA-381183 ATF6 (ATF6-alpha) activates chaperone genes
R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC

SIGNOR Signaling Network Open Resource

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SIGNORi
P11021

Protein family/group databases

Transport Classification Database

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TCDBi
1.A.33.1.6 the cation channel-forming heat shock protein-70 (hsp70) family

<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:
Endoplasmic reticulum chaperone BiPCurated (EC:3.6.4.101 Publication)
Alternative name(s):
78 kDa glucose-regulated protein1 Publication
Short name:
GRP-781 Publication
Binding-immunoglobulin protein1 Publication
Short name:
BiP1 Publication
Heat shock protein 70 family protein 5Curated
Short name:
HSP70 family protein 5Curated
Heat shock protein family A member 5Imported
Immunoglobulin heavy chain-binding protein1 Publication
<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:HSPA5Imported
Synonyms:GRP781 Publication
<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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000044574.7

Human Gene Nomenclature Database

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HGNCi
HGNC:5238 HSPA5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
138120 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P11021

<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, Endoplasmic reticulum

<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

Autoantigen in rheumatoid arthritis.1 Publication

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>Mutagenesisi229T → A: Impaired ATPase activity. 1 Publication1
Mutagenesisi585K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
3309

Open Targets

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OpenTargetsi
ENSG00000044574

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29504

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1781865

Drug and drug target database

More...
DrugBanki
DB00945 Acetylsalicylic acid
DB00025 Antihemophilic Factor (Recombinant)

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
HSPA5

Domain mapping of disease mutations (DMDM)

More...
DMDMi
14916999

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 182 PublicationsAdd BLAST18
<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_000001356619 – 654Endoplasmic reticulum chaperone BiPAdd BLAST636

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 residuei86PhosphoserineBy similarity1
Modified residuei125N6-acetyllysineBy similarity1
Modified residuei160Nitrated tyrosineBy similarity1
Modified residuei213N6-acetyllysineBy similarity1
Modified residuei271N6-acetyllysineBy similarity1
Modified residuei326N6-acetyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki352Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei353N6-acetyllysine; alternateBy similarity1
Cross-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei447N6-succinyllysineBy similarity1
Modified residuei492Omega-N-methylarginineBy similarity1
Modified residuei518O-AMP-threonine; alternateBy similarity1
Modified residuei518Phosphothreonine; alternateCombined sources1
Modified residuei585N6,N6,N6-trimethyllysine; by METTL21A; in vitroCombined sources2 Publications1
Modified residuei585N6,N6-dimethyllysine; alternateCombined sources1
Modified residuei585N6-methyllysine; alternateCombined sources1
Modified residuei591N6-methyllysineCombined sources1
Modified residuei643PhosphothreonineBy similarity1
Modified residuei648PhosphothreonineBy similarity1

<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

AMPylated by FICD (PubMed:25601083). In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins (By similarity). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P11021

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P11021

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

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PaxDbi
P11021

PeptideAtlas

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PeptideAtlasi
P11021

PRoteomics IDEntifications database

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PRIDEi
P11021

ProteomicsDB human proteome resource

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ProteomicsDBi
52688

Consortium for Top Down Proteomics

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TopDownProteomicsi
P11021

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P11021

USC-OGP 2-DE database

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OGPi
P11021

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
P11021

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

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SWISS-2DPAGEi
P11021

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P11021

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P11021

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

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PhosphoSitePlusi
P11021

SwissPalm database of S-palmitoylation events

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SwissPalmi
P11021

<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 endoplasmic reticulum stress.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000044574 Expressed in 243 organ(s), highest expression level in vena cava

CleanEx database of gene expression profiles

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CleanExi
HS_HSPA5

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P11021 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11021 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB005221
HPA038845
HPA038846

<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

Monomer and homooligomer; homooligomerization via the interdomain linker inactivates the chaperone activity and acts as a storage of HSPA5/BiP molecules (By similarity). Interacts with DNAJC1 (via J domain) (By similarity). Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity). Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (By similarity). Interacts with TMEM132A and TRIM21 (PubMed:12699405). May form a complex with ERLEC1, OS9, SEL1L and SYVN1 (PubMed:18264092,PubMed:18502753). Interacts with DNAJC10 (PubMed:12411443, PubMed:23769672). Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to ERN1/IRE1 (By similarity). Interacts with ERN1/IRE1; interaction takes place following interaction with DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1 (By similarity). Interacts with MX1 (By similarity). Interacts with METTL23 (PubMed:23349634). Interacts with CEMIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration (PubMed:23990668). Interacts with PCSK4 form; the interaction takes place in the endoplasmic reticulum (PubMed:21080038). Interacts with CIPC (PubMed:26657846). Interacts with CCDC88B (via C-terminus); the interaction opposes ERN1-mediated JNK activation, protecting against apoptosis (PubMed:21289099). Interacts with INPP5K; necessary for INPP5K localization at the endoplasmic reticulum (PubMed:26940976). Interacts with MANF; the interaction is direct (PubMed:22637475). Interacts with LOXL2; leading to activate the ERN1/IRE1-XBP1 pathway of the unfolded protein response (PubMed:28332555).By similarity13 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
109541, 593 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P11021

Database of interacting proteins

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DIPi
DIP-33189N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P11021

Protein interaction database and analysis system

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IntActi
P11021, 200 interactors

Molecular INTeraction database

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MINTi
P11021

STRING: functional protein association networks

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STRINGi
9606.ENSP00000324173

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P11021

<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

1654
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
3IUCX-ray2.40A/C26-410[»]
3LDLX-ray2.30A/B26-407[»]
3LDNX-ray2.20A/B26-407[»]
3LDOX-ray1.95A/B26-407[»]
3LDPX-ray2.20A/B26-407[»]
5E84X-ray2.99A/B/C/D/E/F25-633[»]
5E85X-ray2.57A418-637[»]
5E86X-ray2.68A418-637[»]
5EVZX-ray1.85A/B26-407[»]
5EX5X-ray1.90A/B26-407[»]
5EXWX-ray1.90A/B26-407[»]
5EY4X-ray1.86A/B26-407[»]
5F0XX-ray1.60A/B26-407[»]
5F1XX-ray1.90A/B26-407[»]
5F2RX-ray2.15A/B26-407[»]
6ASYX-ray1.85A/B25-633[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P11021

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

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SMRi
P11021

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P11021

<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>Regioni125 – 280Nucleotide-binding (NBD)1 PublicationAdd BLAST156
Regioni409 – 419Interdomain linkerBy similarityAdd BLAST11
Regioni420 – 500Substrate-binding (SBD)1 PublicationAdd BLAST81

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi651 – 654Prevents secretion from ERSequence analysis4

<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 interdomain linker regulates the chaperone activity by mediating the formation of homooligomers. Homooligomers are formed by engagement of the interdomain linker of one HSPA5/BiP molecule as a typical substrate of an adjacent HSPA5/BiP molecule. HSPA5/BiP oligomerization inactivates participating HSPA5/BiP protomers. HSPA5/BiP oligomers probably act as reservoirs to store HSPA5/BiP molecules when they are not needed by the cell. When the levels of unfolded proteins rise, cells can rapidly break up these oligomers to make active monomers.By similarity

<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

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0101 Eukaryota
COG0443 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154787

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000228135

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051845

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P11021

KEGG Orthology (KO)

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KOi
K09490

Identification of Orthologs from Complete Genome Data

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OMAi
CVGVMQK

Database of Orthologous Groups

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OrthoDBi
288077at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P11021

TreeFam database of animal gene trees

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TreeFami
TF105044

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.1270.10, 1 hit
2.60.34.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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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
PS00014 ER_TARGET, 1 hit
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>Sequencei

<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.

P11021-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV
60 70 80 90 100
EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG
110 120 130 140 150
RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL
160 170 180 190 200
TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN
210 220 230 240 250
EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD
260 270 280 290 300
THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS
310 320 330 340 350
SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD
360 370 380 390 400
LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV
410 420 430 440 450
QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI
460 470 480 490 500
FSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT
510 520 530 540 550
FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE
560 570 580 590 600
EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE
610 620 630 640 650
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE

KDEL
Length:654
Mass (Da):72,333
Last modified:July 11, 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:i59B7D8D85BC32A00
GO

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 conflicti297Missing in AAA52614 (PubMed:2840249).Curated1
Sequence conflicti297Missing in CAA61201 (Ref. 2) Curated1
Sequence conflicti418D → H in AAA52614 (PubMed:2840249).Curated1
Sequence conflicti418D → H in CAA61201 (Ref. 2) Curated1
Sequence conflicti439R → S in AAA52614 (PubMed:2840249).Curated1
Sequence conflicti439R → S in CAA61201 (Ref. 2) Curated1
Sequence conflicti447K → N in AAA52614 (PubMed:2840249).Curated1
Sequence conflicti447K → N in CAA61201 (Ref. 2) 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_025815543N → H1 PublicationCorresponds to variant dbSNP:rs35356639Ensembl.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

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DDBJi
Links Updated
M19645 Genomic DNA Translation: AAA52614.1
X87949 mRNA Translation: CAA61201.1
AJ271729 mRNA Translation: CAB71335.1
AF216292 mRNA Translation: AAF42836.1
DQ385847 Genomic DNA Translation: ABD04090.1
AL354710 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW87620.1
BC020235 mRNA Translation: AAH20235.1
X59969 Genomic DNA Translation: CAA42595.1
AF188611 mRNA Translation: AAF13605.1 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6863.1

Protein sequence database of the Protein Information Resource

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PIRi
A29821

NCBI Reference Sequences

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RefSeqi
NP_005338.1, NM_005347.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.743241

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000324460; ENSP00000324173; ENSG00000044574

Database of genes from NCBI RefSeq genomes

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GeneIDi
3309

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3309

Keywords - Coding sequence diversityi

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
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19645 Genomic DNA Translation: AAA52614.1
X87949 mRNA Translation: CAA61201.1
AJ271729 mRNA Translation: CAB71335.1
AF216292 mRNA Translation: AAF42836.1
DQ385847 Genomic DNA Translation: ABD04090.1
AL354710 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW87620.1
BC020235 mRNA Translation: AAH20235.1
X59969 Genomic DNA Translation: CAA42595.1
AF188611 mRNA Translation: AAF13605.1 Sequence problems.
CCDSiCCDS6863.1
PIRiA29821
RefSeqiNP_005338.1, NM_005347.4
UniGeneiHs.743241

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IUCX-ray2.40A/C26-410[»]
3LDLX-ray2.30A/B26-407[»]
3LDNX-ray2.20A/B26-407[»]
3LDOX-ray1.95A/B26-407[»]
3LDPX-ray2.20A/B26-407[»]
5E84X-ray2.99A/B/C/D/E/F25-633[»]
5E85X-ray2.57A418-637[»]
5E86X-ray2.68A418-637[»]
5EVZX-ray1.85A/B26-407[»]
5EX5X-ray1.90A/B26-407[»]
5EXWX-ray1.90A/B26-407[»]
5EY4X-ray1.86A/B26-407[»]
5F0XX-ray1.60A/B26-407[»]
5F1XX-ray1.90A/B26-407[»]
5F2RX-ray2.15A/B26-407[»]
6ASYX-ray1.85A/B25-633[»]
ProteinModelPortaliP11021
SMRiP11021
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109541, 593 interactors
CORUMiP11021
DIPiDIP-33189N
ELMiP11021
IntActiP11021, 200 interactors
MINTiP11021
STRINGi9606.ENSP00000324173

Chemistry databases

BindingDBiP11021
ChEMBLiCHEMBL1781865
DrugBankiDB00945 Acetylsalicylic acid
DB00025 Antihemophilic Factor (Recombinant)

Protein family/group databases

TCDBi1.A.33.1.6 the cation channel-forming heat shock protein-70 (hsp70) family

PTM databases

iPTMnetiP11021
PhosphoSitePlusiP11021
SwissPalmiP11021

Polymorphism and mutation databases

BioMutaiHSPA5
DMDMi14916999

2D gel databases

DOSAC-COBS-2DPAGEiP11021
OGPiP11021
REPRODUCTION-2DPAGEiP11021
SWISS-2DPAGEiP11021
UCD-2DPAGEiP11021

Proteomic databases

EPDiP11021
jPOSTiP11021
PaxDbiP11021
PeptideAtlasiP11021
PRIDEiP11021
ProteomicsDBi52688
TopDownProteomicsiP11021

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3309
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324460; ENSP00000324173; ENSG00000044574
GeneIDi3309
KEGGihsa:3309

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3309
DisGeNETi3309
EuPathDBiHostDB:ENSG00000044574.7

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HSPA5
HGNCiHGNC:5238 HSPA5
HPAiCAB005221
HPA038845
HPA038846
MIMi138120 gene
neXtProtiNX_P11021
OpenTargetsiENSG00000044574
PharmGKBiPA29504

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00940000154787
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiP11021
KOiK09490
OMAiCVGVMQK
OrthoDBi288077at2759
PhylomeDBiP11021
TreeFamiTF105044

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-381033 ATF6 (ATF6-alpha) activates chaperones
R-HSA-381042 PERK regulates gene expression
R-HSA-381070 IRE1alpha activates chaperones
R-HSA-381183 ATF6 (ATF6-alpha) activates chaperone genes
R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC
SIGNORiP11021

Miscellaneous databases

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

More...
ChiTaRSi
HSPA5 human
EvolutionaryTraceiP11021

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Binding_immunoglobulin_protein

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

More...
GenomeRNAii
3309

Protein Ontology

More...
PROi
PR:P11021

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000044574 Expressed in 243 organ(s), highest expression level in vena cava
CleanExiHS_HSPA5
ExpressionAtlasiP11021 baseline and differential
GenevisibleiP11021 HS

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
PS00014 ER_TARGET, 1 hit
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 nameiBIP_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: P11021
Secondary accession number(s): B0QZ61
, Q2EF78, Q9NPF1, Q9UK02
<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: July 1, 1989
Last sequence update: July 11, 2001
Last modified: January 16, 2019
This is version 220 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
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