UniProtKB - P20029 (BIP_MOUSE)
Protein
Endoplasmic reticulum chaperone BiP
Gene
Hspa5
Organism
Mus musculus (Mouse)
Status
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
- EC:3.6.4.10By 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 | Graphical view | 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
- ATP binding Source: GO_Central
- enzyme binding Source: MGI
- heat shock protein binding Source: GO_Central
- misfolded protein binding Source: BHF-UCL
- protein domain specific binding Source: MGI
- protein folding chaperone Source: GO_Central
- ribosome binding Source: MGI
- ubiquitin protein ligase binding Source: MGI
- unfolded protein binding Source: MGI
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
- cellular response to interleukin-4 Source: MGI
- cellular response to manganese ion Source: Ensembl
- cellular response to nerve growth factor stimulus Source: Ensembl
- cellular response to unfolded protein Source: GO_Central
- cerebellar Purkinje cell layer development Source: BHF-UCL
- cerebellum structural organization Source: BHF-UCL
- chaperone cofactor-dependent protein refolding Source: GO_Central
- endoplasmic reticulum unfolded protein response Source: BHF-UCL
- ER overload response Source: MGI
- 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
- neuron apoptotic process Source: Ensembl
- neuron differentiation Source: Ensembl
- positive regulation of cell migration Source: UniProtKB
- positive regulation of embryonic development Source: BHF-UCL
- positive regulation of neuron projection development Source: MGI
- positive regulation of protein ubiquitination Source: BHF-UCL
- protein refolding Source: GO_Central
- proteolysis involved in cellular protein catabolic process Source: BHF-UCL
- response to cocaine Source: Ensembl
- response to endoplasmic reticulum stress Source: MGI
- response to methamphetamine hydrochloride Source: Ensembl
- response to unfolded protein Source: GO_Central
- stress response to metal ion Source: Ensembl
- toxin transport Source: MGI
- ubiquitin-dependent ERAD pathway Source: GO_Central
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 |
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 | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:95835 Hspa5 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum lumen PROSITE-ProRule annotation1 Publication
Other locations
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: UniProtKB
Endoplasmic reticulum
- endoplasmic reticulum Source: ParkinsonsUK-UCL
- endoplasmic reticulum chaperone complex Source: ParkinsonsUK-UCL
- endoplasmic reticulum lumen Source: BHF-UCL
- endoplasmic reticulum membrane Source: MGI
- integral component of endoplasmic reticulum membrane Source: MGI
- smooth endoplasmic reticulum Source: MGI
Extracellular region or secreted
- extracellular region Source: Reactome
Mitochondrion
- mitochondrion Source: UniProtKB
Nucleus
- COP9 signalosome Source: Ensembl
- nucleus Source: MGI
Plasma Membrane
- plasma membrane Source: MGI
Other locations
- cell surface Source: MGI
- cytoplasm Source: MGI
- endoplasmic reticulum-Golgi intermediate compartment Source: MGI
- intracellular membrane-bounded organelle Source: MGI
- membrane Source: MGI
- midbody Source: MGI
- myelin sheath Source: UniProtKB
- protein-containing complex Source: MGI
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulumPTM / 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 | Graphical view | 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 conjugationProteomic databases
EPDi | P20029 |
jPOSTi | P20029 |
MaxQBi | P20029 |
PaxDbi | P20029 |
PeptideAtlasi | P20029 |
PRIDEi | P20029 |
TopDownProteomicsi | P20029 |
2D gel databases
COMPLUYEAST-2DPAGEi | P20029 |
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 |
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
GO - Molecular functioni
- enzyme binding Source: MGI
- heat shock protein binding Source: GO_Central
- misfolded protein binding Source: BHF-UCL
- protein domain specific binding Source: MGI
- ubiquitin protein ligase binding Source: MGI
- unfolded protein binding Source: MGI
Protein-protein interaction databases
BioGridi | 200078, 44 interactors |
CORUMi | P20029 |
DIPi | DIP-32341N |
IntActi | P20029, 33 interactors |
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 | Graphical view | 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
SignalPhylogenomic databases
eggNOGi | KOG0101 Eukaryota COG0443 LUCA |
GeneTreei | ENSGT00940000154787 |
HOGENOMi | HOG000228135 |
HOVERGENi | HBG051845 |
InParanoidi | P20029 |
KOi | K09490 |
OMAi | CVGVMQK |
OrthoDBi | 288077at2759 |
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 |
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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
P20029-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A0A6YXF5 | A0A0A6YXF5_MOUSE | Endoplasmic reticulum chaperone BiP | Hspa5 | 42 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | 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 |
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 |
Genome annotation databases
Ensembli | ENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864 ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864 |
GeneIDi | 14828 |
KEGGi | mmu:14828 |
UCSCi | uc008jis.2 mouse |
Similar proteinsi
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 |
jPOSTi | P20029 |
MaxQBi | P20029 |
PaxDbi | P20029 |
PeptideAtlasi | P20029 |
PRIDEi | P20029 |
TopDownProteomicsi | P20029 |
Protocols and materials databases
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 | ENSGT00940000154787 |
HOGENOMi | HOG000228135 |
HOVERGENi | HBG051845 |
InParanoidi | P20029 |
KOi | K09490 |
OMAi | CVGVMQK |
OrthoDBi | 288077at2759 |
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 |
Miscellaneous databases
ChiTaRSi | Hspa5 mouse |
PROi | PR:P20029 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000026864 Expressed in 301 organ(s), highest expression level in prostate gland |
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: | February 13, 2019 | |
This is version 199 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 proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot