Hspa5

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.By similarity2 Publications

Catalytic activityⁱ

ATP + H₂O = ADP + phosphate.By similarity

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 key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	97	ATPBy similarity		1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	37 – 40	ATPBy similarity	4
Nucleotide bindingⁱ	228 – 230	ATPBy similarity	3
Nucleotide bindingⁱ	294 – 301	ATPBy similarity	8
Nucleotide bindingⁱ	365 – 368	ATPBy similarity	4

GO - Molecular functionⁱ

ATPase activity Source: UniProtKB
ATPase activity, coupled
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
ATP binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
enzyme binding Source: MGI
heat shock protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
misfolded protein binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18923430
protein binding involved in protein folding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein domain specific binding Source: MGI
ribosome binding
Source: MGI
Inferred from direct assayⁱ
- 12065409
ubiquitin protein ligase binding Source: MGI
unfolded protein binding Source: MGI

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to antibiotic Source: Ensembl
cellular response to calcium ion Source: Ensembl
cellular response to cAMP Source: Ensembl
cellular response to drug Source: Ensembl
cellular response to gamma radiation Source: Ensembl
cellular response to glucose starvation Source: MGI
cellular response to heat
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to interleukin-4
Source: MGI
Inferred from direct assayⁱ
- 9798653
cellular response to manganese ion Source: Ensembl
cellular response to nerve growth factor stimulus Source: Ensembl
cellular response to unfolded protein
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cerebellar Purkinje cell layer development
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 19816510
cerebellum structural organization
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 19816510
chaperone cofactor-dependent protein refolding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
endoplasmic reticulum unfolded protein response
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 19816510
ER overload response
Source: MGI
Inferred from direct assayⁱ
- 11854325
luteolysis Source: Ensembl
maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
negative regulation of apoptotic process Source: MGI
negative regulation of IRE1-mediated unfolded protein response Source: UniProtKB
negative regulation of protein homodimerization activity Source: UniProtKB
negative regulation of transforming growth factor beta receptor signaling pathway
Source: MGI
Inferred from genetic interactionⁱ
- 17991893
neuron apoptotic process Source: Ensembl
neuron differentiation Source: Ensembl
positive regulation of cell migration Source: UniProtKB
positive regulation of embryonic development
Source: BHF-UCL
Traceable author statementⁱ
- 19816510
positive regulation of neuron projection development Source: MGI
positive regulation of protein ubiquitination
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 19816510
protein refolding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
proteolysis involved in cellular protein catabolic process
Source: BHF-UCL
Inferred from direct assayⁱ
- 18923430
response to cocaine Source: Ensembl
response to endoplasmic reticulum stress
Source: MGI
Inferred from sequence orthologyⁱ
- 23444373
response to methamphetamine hydrochloride Source: Ensembl
response to unfolded protein
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
stress response to metal ion Source: Ensembl
toxin transport
Source: MGI
Inferred from mutant phenotypeⁱ
- 23716698
ubiquitin-dependent ERAD pathway
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chaperone, Hydrolase
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

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

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:Hspa5Imported Synonyms:Grp781 Publication
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 2

Organism-specific databases

MGIⁱ	MGI:95835 Hspa5

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 19	2 PublicationsAdd BLAST		19
ChainⁱPRO_0000013568	20 – 655	Endoplasmic reticulum chaperone BiPAdd BLAST		636

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	87	PhosphoserineBy similarity	1
Modified residueⁱ	126	N6-acetyllysineCombined sources	1
Modified residueⁱ	161	Nitrated tyrosineCombined sources	1
Modified residueⁱ	214	N6-acetyllysineCombined sources	1
Modified residueⁱ	272	N6-acetyllysineBy similarity	1
Modified residueⁱ	327	N6-acetyllysineCombined sources	1
Cross-linkⁱ	353	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	354	N6-acetyllysine; alternateCombined sources	1
Cross-linkⁱ	354	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residueⁱ	448	N6-succinyllysineCombined sources	1
Modified residueⁱ	493	Omega-N-methylarginineBy similarity	1
Modified residueⁱ	519	O-AMP-threonine; alternateBy similarity	1
Modified residueⁱ	519	Phosphothreonine; alternateBy similarity	1
Modified residueⁱ	586	N6,N6,N6-trimethyllysine; by METTL21A; in vitro1 Publication	1
Modified residueⁱ	586	N6,N6-dimethyllysine; alternateBy similarity	1
Modified residueⁱ	586	N6-methyllysine; alternateBy similarity	1
Modified residueⁱ	592	N6-methyllysineBy similarity	1
Modified residueⁱ	644	PhosphothreonineCombined sources	1
Modified residueⁱ	649	PhosphothreonineCombined sources	1
Modified residueⁱ	650	PhosphoserineCombined sources	1

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

EPDⁱ	P20029
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P20029
PaxDbⁱ	P20029
PeptideAtlas More...PeptideAtlasⁱ	P20029
PRIDEⁱ	P20029
TopDownProteomicsⁱ	P20029

2D gel databases

COMPLUYEAST-2DPAGEⁱ	P20029
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00319992 P20029
SWISS-2DPAGEⁱ	P20029
UCD-2DPAGEⁱ	P20029

PTM databases

CarbonylDBⁱ	P20029
iPTMnetⁱ	P20029
PhosphoSitePlusⁱ	P20029
SwissPalmⁱ	P20029

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000026864 Expressed in 301 organ(s), highest expression level in prostate gland
CleanExⁱ	MM_HSPA5
ExpressionAtlasⁱ	P20029 baseline and differential
Genevisibleⁱ	P20029 MM

Interactionⁱ

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, UGT1A1 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).By similarity6 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Atf6b	O35451	2	EBI-772325,EBI-8361741
Dnajb11	Q99KV1	4	EBI-772325,EBI-8328260
ERN1	O75460	2	EBI-772325,EBI-371750	From Homo sapiens.
SOD1	P00441	7	EBI-772325,EBI-990792	From Homo sapiens.

GO - Molecular functionⁱ

enzyme binding Source: MGI
heat shock protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
misfolded protein binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18923430
protein binding involved in protein folding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein domain specific binding Source: MGI
ubiquitin protein ligase binding Source: MGI
unfolded protein binding Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	200078, 44 interactors
CORUMⁱ	P20029
Database of interacting proteins More...DIPⁱ	DIP-32341N
IntActⁱ	P20029, 33 interactors
Molecular INTeraction database More...MINTⁱ	P20029
STRINGⁱ	10090.ENSMUSP00000028222

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P20029
SMRⁱ	P20029
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	126 – 281	Nucleotide-binding (NBD)By similarityAdd BLAST	156
Regionⁱ	410 – 420	Interdomain linkerBy similarityAdd BLAST	11
Regionⁱ	421 – 501	Substrate-binding (SBD)By similarityAdd BLAST	81

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	652 – 655	Prevents secretion from ER		4

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

Sequence similaritiesⁱ

Belongs to the heat shock protein 70 family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	KOG0101 Eukaryota COG0443 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00930000150862
HOGENOMⁱ	HOG000228135
HOVERGENⁱ	HBG051845
InParanoidⁱ	P20029
KEGG Orthology (KO) More...KOⁱ	K09490
OMAⁱ	CVGVMQK
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0352
PhylomeDBⁱ	P20029
TreeFamⁱ	TF105044

Family and domain databases

Gene3Dⁱ	1.20.1270.10, 1 hit 2.60.34.10, 1 hit
InterProⁱ	View protein in InterPro IPR018181 Heat_shock_70_CS IPR029048 HSP70_C_sf IPR029047 HSP70_peptide-bd_sf IPR013126 Hsp_70_fam
PANTHERⁱ	PTHR19375 PTHR19375, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00012 HSP70, 1 hit
PRINTSⁱ	PR00301 HEATSHOCK70
SUPFAMⁱ	SSF100920 SSF100920, 1 hit SSF100934 SSF100934, 1 hit
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

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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 all Align All

P20029-1 [UniParc]FASTA Add 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

Checksum:ⁱAFB795D15E20FAC2

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A0A6YXF5	A0A0A6YXF5_MOUSE		Endoplasmic reticulum chaperone BiP Endoplasmic reticulum chaperone BiP	Hspa5	42	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	43	V → F in BAA11462 (PubMed:8645260).Curated	1
Sequence conflictⁱ	245	V → W in BAA11462 (PubMed:8645260).Curated	1
Sequence conflictⁱ	329	E → G in BAA11462 (PubMed:8645260).Curated	1
Sequence conflictⁱ	361	V → A in BAA11462 (PubMed:8645260).Curated	1
Sequence conflictⁱ	474	T → R in CAA05361 (PubMed:2895472).Curated	1
Sequence conflictⁱ	591	D → G in AAA37742 (PubMed:2583523).Curated	1
Sequence conflictⁱ	596	E → K AA sequence (PubMed:2559088).Curated	1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS15950.1
PIRⁱ	A37048
NCBI Reference Sequences More...RefSeqⁱ	NP_001156906.1, NM_001163434.1 NP_071705.3, NM_022310.3
UniGeneⁱ	Mm.330160 Mm.470180 Mm.474909

Genome annotation databases

Ensemblⁱ	ENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864 ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864
GeneIDⁱ	14828
KEGGⁱ	mmu:14828
UCSC genome browser More...UCSCⁱ	uc008jis.2 mouse

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P20029	Heat shock 70 kDa protein cognate		Daphnia magna		655	UniRef100_P20029
Uncharacterized protein (Fragment)		MOUSE		619
UPI000A3128E8		MUSPA		654

Protein	Similar proteins		Species	Score	Length	Source
P20029	Endoplasmic reticulum chaperone BiP	)	HUMAN		654	UniRef90_P11021
Endoplasmic reticulum chaperone BiP		XENLA		658
Endoplasmic reticulum chaperone BiP		BOVIN		655
Endoplasmic reticulum chaperone BiP	)	CRIGR		654
Endoplasmic reticulum chaperone BiP		MESAU		654
+329

Protein	Similar proteins		Species	Score	Length	Source
P20029	Heat shock 70 kDa protein 1A	)	HUMAN		641	UniRef50_P0DMV8
Heat shock 70 kDa protein 1		PONAB		641
Heat shock 70 kDa protein 1B		MOUSE		642
Heat shock 70 kDa protein 1B		BOVIN		641
Heat shock 70 kDa protein 1B		BOSMU		641
+2027

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
CCDSⁱ	CCDS15950.1
PIRⁱ	A37048
RefSeqⁱ	NP_001156906.1, NM_001163434.1 NP_071705.3, NM_022310.3
UniGeneⁱ	Mm.330160 Mm.470180 Mm.474909

3D structure databases

ProteinModelPortalⁱ	P20029
SMRⁱ	P20029
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	200078, 44 interactors
CORUMⁱ	P20029
DIPⁱ	DIP-32341N
IntActⁱ	P20029, 33 interactors
MINTⁱ	P20029
STRINGⁱ	10090.ENSMUSP00000028222

PTM databases

CarbonylDBⁱ	P20029
iPTMnetⁱ	P20029
PhosphoSitePlusⁱ	P20029
SwissPalmⁱ	P20029

2D gel databases

COMPLUYEAST-2DPAGEⁱ	P20029
REPRODUCTION-2DPAGEⁱ	IPI00319992 P20029
SWISS-2DPAGEⁱ	P20029
UCD-2DPAGEⁱ	P20029

Proteomic databases

EPDⁱ	P20029
MaxQBⁱ	P20029
PaxDbⁱ	P20029
PeptideAtlasⁱ	P20029
PRIDEⁱ	P20029
TopDownProteomicsⁱ	P20029

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864 ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864
GeneIDⁱ	14828
KEGGⁱ	mmu:14828
UCSCⁱ	uc008jis.2 mouse

Organism-specific databases

CTDⁱ	3309
MGIⁱ	MGI:95835 Hspa5

Phylogenomic databases

eggNOGⁱ	KOG0101 Eukaryota COG0443 LUCA
GeneTreeⁱ	ENSGT00930000150862
HOGENOMⁱ	HOG000228135
HOVERGENⁱ	HBG051845
InParanoidⁱ	P20029
KOⁱ	K09490
OMAⁱ	CVGVMQK
OrthoDBⁱ	EOG091G0352
PhylomeDBⁱ	P20029
TreeFamⁱ	TF105044

Enzyme and pathway databases

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

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

Miscellaneous databases

ChiTaRSⁱ	Hspa5 mouse
Protein Ontology More...PROⁱ	PR:P20029
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000026864 Expressed in 301 organ(s), highest expression level in prostate gland
CleanExⁱ	MM_HSPA5
ExpressionAtlasⁱ	P20029 baseline and differential
Genevisibleⁱ	P20029 MM

Family and domain databases

Gene3Dⁱ	1.20.1270.10, 1 hit 2.60.34.10, 1 hit
InterProⁱ	View protein in InterPro IPR018181 Heat_shock_70_CS IPR029048 HSP70_C_sf IPR029047 HSP70_peptide-bd_sf IPR013126 Hsp_70_fam
PANTHERⁱ	PTHR19375 PTHR19375, 1 hit
Pfamⁱ	View protein in Pfam PF00012 HSP70, 1 hit
PRINTSⁱ	PR00301 HEATSHOCK70
SUPFAMⁱ	SSF100920 SSF100920, 1 hit SSF100934 SSF100934, 1 hit
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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BIP_MOUSE
Accessionⁱ	P20029Primary (citable) accession number: P20029 Secondary accession number(s): O35642, Q3UFF2, Q61630
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
	Last sequence update:	November 1, 1997
	Last modified:	November 7, 2018
	This is version 196 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P20029 (BIP_MOUSE)

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Endoplasmic reticulum chaperone BiP

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<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

Sites

Regions

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Endoplasmic reticulum

Other locations

Endoplasmic reticulum

Extracellular region or secreted

Mitochondrion

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<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

<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

GO - Molecular functioni

Protein-protein interaction databases

<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

<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

Motif

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ