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UniProtKB - P20029 (BIP_MOUSE)

Entry version 211 (12 Aug 2020)
Sequence version 3 (01 Nov 1997)
Previous versions | rss
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Protein

Endoplasmic reticulum chaperone BiP

Gene

Hspa5

Organism
Mus musculus (Mouse)
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:12411443, PubMed:12475965). 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 (PubMed:12411443). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). 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. May also play a role in apoptosis and cell proliferation (By similarity).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 (By similarity). In the ADP-bound and nucleotide-free (apo) states, the two domains have little interaction (By similarity). 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 (By similarity). J domain-containing co-chaperones (DNAJB9/ERdj4 or DNAJC10/ERdj5) stimulate the ATPase activity and are required for efficient substrate recognition by HSPA5/BiP. 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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei97ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi37 – 40ATPBy similarity4
Nucleotide bindingi228 – 230ATPBy similarity3
Nucleotide bindingi294 – 301ATPBy similarity8
Nucleotide bindingi365 – 368ATPBy similarity4

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

More...Reactomei		R-MMU-3371453, Regulation of HSF1-mediated heat shock response
R-MMU-983170, Antigen Presentation: Folding, assembly and peptide loading of class I MHC

<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%5Fand%5Ftaxonomy%5Fsection">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:3.6.4.10By similarity)
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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:95835, Hspa5

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

<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 – 192 PublicationsAdd BLAST19
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001356820 – 655Endoplasmic 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 residuei87PhosphoserineBy similarity1
Modified residuei126N6-acetyllysineCombined sources1
Modified residuei1613'-nitrotyrosineCombined sources1
Modified residuei214N6-acetyllysineCombined sources1
Modified residuei272N6-acetyllysineBy similarity1
Modified residuei327N6-acetyllysineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei354N6-acetyllysine; alternateCombined sources1
Cross-linki354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei448N6-succinyllysineCombined sources1
Modified residuei493Omega-N-methylarginineBy similarity1
Modified residuei519O-AMP-threonine; alternateBy similarity1
Modified residuei519Phosphothreonine; alternateBy similarity1
Modified residuei586N6,N6,N6-trimethyllysine; by METTL21A; in vitro1 Publication1
Modified residuei586N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei586N6-methyllysine; alternateBy similarity1
Modified residuei592N6-methyllysineBy similarity1
Modified residuei644PhosphothreonineCombined sources1
Modified residuei649PhosphothreonineCombined sources1
Modified residuei650PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 unstressed cells, AMPylation at Thr-519 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins. In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity.By similarity

Keywords - PTMi

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

Proteomic databases

The CPTAC Assay portal

More...CPTACi		non-CPTAC-3387
non-CPTAC-3388

Encyclopedia of Proteome Dynamics

More...EPDi		P20029

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P20029

MaxQB - The MaxQuant DataBase

More...MaxQBi		P20029

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

More...PaxDbi		P20029

PeptideAtlas

More...PeptideAtlasi		P20029

PRoteomics IDEntifications database

More...PRIDEi		P20029

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P20029

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...COMPLUYEAST-2DPAGEi		P20029

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00319992
P20029

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

More...SWISS-2DPAGEi		P20029

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P20029

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P20029

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P20029

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

More...PhosphoSitePlusi		P20029

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P20029

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000026864, Expressed in prostate gland and 316 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P20029, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P20029, MM

<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%5Fsection">'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%5Fsection">'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) (PubMed:12065409).

Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (PubMed:16931514).

Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (PubMed:12475965).

Interacts with TMEM132A and TRIM21 (By similarity). May form a complex with ERLEC1, OS9, SEL1L and SYVN1 (By similarity).

Interacts with DNAJC10 (PubMed:12411443).

Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to ERN1/IRE1 (PubMed:11836248).

Interacts with ERN1/IRE1; interaction takes place following interaction with DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1 (By similarity).

Interacts with MX1 (PubMed:21992152).

Interacts with METTL23 (By similarity).

Interacts with CEMIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration (By similarity).

Interacts with PCSK4 form; the interaction takes place in the endoplasmic reticulum (By similarity).

Interacts with CIPC (By similarity).

Interacts with CCDC88B (via C-terminus); the interaction opposes ERN1-mediated JNK activation, protecting against apoptosis (By similarity).

Interacts with INPP5K; necessary for INPP5K localization at the endoplasmic reticulum (By similarity).

Interacts with MANF; the interaction is direct (By similarity).

Interacts with LOXL2; leading to activate the ERN1/IRE1-XBP1 pathway of the unfolded protein response (By similarity).

Interacts with CLU under stressed condition; interaction increases CLU protein stability; facilitates its retrotranslocation and redistribution to the mitochondria; cooperatively suppress stress-induced apoptosis by stabilizing mitochondrial membrane integrity (By similarity).

Interacts with CCDC47 (PubMed:25009997).

Interacts with CLN3 (By similarity).

Interacts with KIAA1324; may regulate the function of HSPA5 in apoptosis and cell proliferation.

Interacts with CASP7 (By similarity).

By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		200078, 89 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P20029

Database of interacting proteins

More...DIPi		DIP-32341N

Protein interaction database and analysis system

More...IntActi		P20029, 39 interactors

Molecular INTeraction database

More...MINTi		P20029

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000097747

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P20029, protein

<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

3D structure databases

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

More...SMRi		P20029

Database of comparative protein structure models

More...ModBasei		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>Regioni1 – 81Required for interaction with KIAA1324By similarityAdd BLAST81
Regioni126 – 281Nucleotide-binding (NBD)By similarityAdd BLAST156
Regioni410 – 420Interdomain linkerBy similarityAdd BLAST11
Regioni421 – 501Substrate-binding (SBD)By similarityAdd 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>Motifi652 – 655Prevents secretion from ER4

<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

More...eggNOGi		KOG0100, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154787

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_005965_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P20029

KEGG Orthology (KO)

More...KOi		K09490

Identification of Orthologs from Complete Genome Data

More...OMAi		CVGVMQK

Database of Orthologous Groups

More...OrthoDBi		288077at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P20029

TreeFam database of animal gene trees

More...TreeFami		TF105044

Family and domain databases

Conserved Domains Database

More...CDDi		cd10241, HSPA5-like_NBD, 1 hit

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
IPR043129, ATPase_NBD
IPR042050, BIP_NBD
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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF100920, SSF100920, 1 hit
SSF100934, SSF100934, 1 hit
SSF53067, SSF53067, 2 hits

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P20029-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMKFTVVAAA LLLLGAVRAE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR 
        60         70         80         90        100
VEIIANDQGN RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI 
       110        120        130        140        150
GRTWNDPSVQ QDIKFLPFKV VEKKTKPYIQ VDIGGGQTKT FAPEEISAMV 
       160        170        180        190        200
LTKMKETAEA YLGKKVTHAV VTVPAYFNDA QRQATKDAGT IAGLNVMRII 
       210        220        230        240        250
NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN GVFEVVATNG 
       260        270        280        290        300
DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL 
       310        320        330        340        350
SSQHQARIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS 
       360        370        380        390        400
DLKKSDIDEI VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA 
       410        420        430        440        450
VQAGVLSGDQ DTGDLVLLDV CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ 
       460        470        480        490        500
IFSTASDNQP TVTIKVYEGE RPLTKDNHLL GTFDLTGIPP APRGVPQIEV 
       510        520        530        540        550
TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE RMVNDAEKFA 
       560        570        580        590        600
EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE 
       610        620        630        640        650
EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSGG PPPTGEEDTS 

EKDEL
Length:655
Mass (Da):72,422
Last modified:November 1, 1997 - v3
<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:iAFB795D15E20FAC2
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
A0A0A6YXF5A0A0A6YXF5_MOUSE
Endoplasmic reticulum chaperone BiP
Hspa5
42Annotation 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 conflicti43V → F in BAA11462 (PubMed:8645260).Curated1
Sequence conflicti245V → W in BAA11462 (PubMed:8645260).Curated1
Sequence conflicti329E → G in BAA11462 (PubMed:8645260).Curated1
Sequence conflicti361V → A in BAA11462 (PubMed:8645260).Curated1
Sequence conflicti474T → R in CAA05361 (PubMed:2895472).Curated1
Sequence conflicti591D → G in AAA37742 (PubMed:2583523).Curated1
Sequence conflicti596E → K AA sequence (PubMed:2559088).Curated1

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
AJ002387 mRNA Translation: CAA05361.1
M19351 mRNA Translation: AAA37315.1
D78645 mRNA Translation: BAA11462.1
AK076079 mRNA Translation: BAC36166.1
AK146647 mRNA Translation: BAE27328.1
AK148539 mRNA Translation: BAE28609.1
AK151647 mRNA Translation: BAE30576.1
AK152020 mRNA Translation: BAE30882.1
AK166739 mRNA Translation: BAE38982.1
AK169034 mRNA Translation: BAE40825.1
BC050927 mRNA Translation: AAH50927.1
U16277 Genomic DNA Translation: AAA76734.1
M30779 mRNA Translation: AAA37742.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS15950.1

Protein sequence database of the Protein Information Resource

More...PIRi		A37048

NCBI Reference Sequences

More...RefSeqi		NP_001156906.1, NM_001163434.1
NP_071705.3, NM_022310.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864
ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864

Database of genes from NCBI RefSeq genomes

More...GeneIDi		14828

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:14828

UCSC genome browser

More...UCSCi		uc008jis.2, mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002387 mRNA Translation: CAA05361.1
M19351 mRNA Translation: AAA37315.1
D78645 mRNA Translation: BAA11462.1
AK076079 mRNA Translation: BAC36166.1
AK146647 mRNA Translation: BAE27328.1
AK148539 mRNA Translation: BAE28609.1
AK151647 mRNA Translation: BAE30576.1
AK152020 mRNA Translation: BAE30882.1
AK166739 mRNA Translation: BAE38982.1
AK169034 mRNA Translation: BAE40825.1
BC050927 mRNA Translation: AAH50927.1
U16277 Genomic DNA Translation: AAA76734.1
M30779 mRNA Translation: AAA37742.1
CCDSiCCDS15950.1
PIRiA37048
RefSeqiNP_001156906.1, NM_001163434.1
NP_071705.3, NM_022310.3

3D structure databases

SMRiP20029
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi200078, 89 interactors
CORUMiP20029
DIPiDIP-32341N
IntActiP20029, 39 interactors
MINTiP20029
STRINGi10090.ENSMUSP00000097747

PTM databases

CarbonylDBiP20029
iPTMnetiP20029
PhosphoSitePlusiP20029
SwissPalmiP20029

2D gel databases

COMPLUYEAST-2DPAGEiP20029
REPRODUCTION-2DPAGEiIPI00319992
P20029
SWISS-2DPAGEiP20029
UCD-2DPAGEiP20029

Proteomic databases

CPTACinon-CPTAC-3387
non-CPTAC-3388
EPDiP20029
jPOSTiP20029
MaxQBiP20029
PaxDbiP20029
PeptideAtlasiP20029
PRIDEiP20029
TopDownProteomicsiP20029

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3926, 1672 antibodies

Genome annotation databases

EnsembliENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864
ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864
GeneIDi14828
KEGGimmu:14828
UCSCiuc008jis.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3309
MGIiMGI:95835, Hspa5

Phylogenomic databases

eggNOGiKOG0100, Eukaryota
GeneTreeiENSGT00940000154787
HOGENOMiCLU_005965_3_0_1
InParanoidiP20029
KOiK09490
OMAiCVGVMQK
OrthoDBi288077at2759
PhylomeDBiP20029
TreeFamiTF105044

Enzyme and pathway databases

ReactomeiR-MMU-3371453, Regulation of HSF1-mediated heat shock response
R-MMU-983170, Antigen Presentation: Folding, assembly and peptide loading of class I MHC

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		14828, 10 hits in 18 CRISPR screens

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

More...ChiTaRSi		Hspa5, mouse

Protein Ontology

More...PROi		PR:P20029
RNActiP20029, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000026864, Expressed in prostate gland and 316 other tissues
ExpressionAtlasiP20029, baseline and differential
GenevisibleiP20029, MM

Family and domain databases

CDDicd10241, HSPA5-like_NBD, 1 hit
Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR043129, ATPase_NBD
IPR042050, BIP_NBD
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
SUPFAMiSSF100920, SSF100920, 1 hit
SSF100934, SSF100934, 1 hit
SSF53067, SSF53067, 2 hits
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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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_MOUSE
<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: P20029
Secondary accession number(s): O35642, Q3UFF2, Q61630
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1997
Last modified: August 12, 2020
This is version 211 of the entry and version 3 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

<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

Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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