UniProtKB - P11021 (BIP_HUMAN)
Endoplasmic reticulum chaperone BiP
HSPA5
Functioni
Caution
Catalytic activityi
- EC:3.6.4.101 Publication
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 96 | ATP1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 36 – 39 | ATP1 Publication | 4 | |
Nucleotide bindingi | 227 – 229 | ATP1 Publication | 3 | |
Nucleotide bindingi | 293 – 300 | ATP1 Publication | 8 | |
Nucleotide bindingi | 364 – 367 | ATP1 Publication | 4 |
GO - Molecular functioni
- ATPase activity Source: UniProtKB
- ATP binding Source: UniProtKB
- 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 domain specific binding Source: UniProtKB
- protein folding chaperone Source: GO_Central
- ribosome binding Source: Ensembl
- ubiquitin protein ligase binding Source: UniProtKB
- unfolded protein binding Source: GO_Central
GO - Biological processi
- ATF6-mediated unfolded protein response Source: Reactome
- 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: UniProtKB
- cellular response to interleukin-4 Source: Ensembl
- 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: Ensembl
- cerebellum structural organization Source: Ensembl
- chaperone cofactor-dependent protein refolding Source: GO_Central
- endoplasmic reticulum unfolded protein response Source: GO_Central
- ER overload response Source: Ensembl
- IRE1-mediated unfolded protein response Source: Reactome
- luteolysis Source: Ensembl
- maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
- negative regulation of apoptotic process Source: UniProtKB
- negative regulation of IRE1-mediated unfolded protein response Source: UniProtKB
- negative regulation of protein-containing complex assembly Source: GO_Central
- negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
- neuron apoptotic process Source: Ensembl
- neuron differentiation Source: Ensembl
- PERK-mediated unfolded protein response Source: Reactome
- positive regulation of cell migration Source: UniProtKB
- positive regulation of neuron projection development Source: Ensembl
- positive regulation of protein ubiquitination Source: Ensembl
- positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
- posttranslational protein targeting to membrane, translocation Source: UniProtKB
- protein folding in endoplasmic reticulum Source: ParkinsonsUK-UCL
- protein refolding Source: GO_Central
- regulation of ATF6-mediated unfolded protein response Source: ParkinsonsUK-UCL
- regulation of IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
- regulation of PERK-mediated unfolded protein response Source: ParkinsonsUK-UCL
- regulation of protein folding in endoplasmic reticulum Source: BHF-UCL
- response to cocaine Source: Ensembl
- response to methamphetamine hydrochloride Source: Ensembl
- response to unfolded protein Source: GO_Central
- stress response to metal ion Source: Ensembl
- substantia nigra development Source: UniProtKB
- toxin transport Source: Ensembl
- ubiquitin-dependent ERAD pathway Source: GO_Central
Keywordsi
Molecular function | Chaperone, Hydrolase |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
PathwayCommonsi | P11021 |
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 |
SIGNORi | P11021 |
Protein family/group databases
TCDBi | 1.A.33.1.5, the cation channel-forming heat shock protein-70 (hsp70) family |
Names & Taxonomyi
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 |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:5238, HSPA5 |
MIMi | 138120, gene |
neXtProti | NX_P11021 |
VEuPathDBi | HostDB:ENSG00000044574.7 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum lumen 4 Publications
Other locations
- Melanosome 1 Publication
- Cytoplasm By similarity
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.1 Publication
Cytosol
- cytosol Source: UniProtKB
Endoplasmic reticulum
- endoplasmic reticulum Source: MGI
- endoplasmic reticulum chaperone complex Source: UniProtKB
- endoplasmic reticulum lumen Source: UniProtKB
- endoplasmic reticulum membrane Source: Reactome
- integral component of endoplasmic reticulum membrane Source: BHF-UCL
- smooth endoplasmic reticulum Source: Ensembl
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Mitochondrion
- mitochondrion Source: UniProtKB
Nucleus
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: Ensembl
Other locations
- cell surface Source: Ensembl
- cytoplasm Source: UniProtKB
- endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
- focal adhesion Source: UniProtKB
- intracellular membrane-bounded organelle Source: UniProtKB
- melanosome Source: UniProtKB-SubCell
- membrane Source: UniProtKB
- midbody Source: UniProtKB
- protein-containing complex Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulumPathology & Biotechi
Involvement in diseasei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 229 | T → A: Impaired ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 585 | K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications | 1 |
Organism-specific databases
DisGeNETi | 3309 |
OpenTargetsi | ENSG00000044574 |
PharmGKBi | PA29504 |
Miscellaneous databases
Pharosi | P11021, Tchem |
Chemistry databases
ChEMBLi | CHEMBL1781865 |
DrugBanki | DB00945, Acetylsalicylic acid DB00025, Antihemophilic factor, human recombinant DB09130, Copper DB13998, Lonoctocog alfa DB13999, Moroctocog alfa |
Genetic variation databases
BioMutai | HSPA5 |
DMDMi | 14916999 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | 2 PublicationsAdd BLAST | 18 | |
ChainiPRO_0000013566 | 19 – 654 | Endoplasmic reticulum chaperone BiPAdd BLAST | 636 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 86 | PhosphoserineBy similarity | 1 | |
Modified residuei | 125 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 160 | 3'-nitrotyrosineBy similarity | 1 | |
Modified residuei | 213 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 271 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 326 | N6-acetyllysineBy similarity | 1 | |
Cross-linki | 352 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 353 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 353 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources | ||
Modified residuei | 447 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 492 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 518 | O-AMP-threonine; alternateBy similarity | 1 | |
Modified residuei | 518 | Phosphothreonine; alternateCombined sources | 1 | |
Modified residuei | 585 | N6,N6,N6-trimethyllysine; by METTL21A; in vitroCombined sources2 Publications | 1 | |
Modified residuei | 585 | N6,N6-dimethyllysine; alternateCombined sources | 1 | |
Modified residuei | 585 | N6-methyllysine; alternateCombined sources | 1 | |
Modified residuei | 591 | N6-methyllysineCombined sources | 1 | |
Modified residuei | 643 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 648 | PhosphothreonineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugationProteomic databases
CPTACi | CPTAC-524 CPTAC-525 non-CPTAC-2616 |
EPDi | P11021 |
jPOSTi | P11021 |
MassIVEi | P11021 |
PaxDbi | P11021 |
PeptideAtlasi | P11021 |
PRIDEi | P11021 |
ProteomicsDBi | 52688 |
TopDownProteomicsi | P11021 |
2D gel databases
DOSAC-COBS-2DPAGEi | P11021 |
OGPi | P11021 |
REPRODUCTION-2DPAGEi | P11021 |
SWISS-2DPAGEi | P11021 |
UCD-2DPAGEi | P11021 |
PTM databases
GlyGeni | P11021, 1 site |
iPTMneti | P11021 |
MetOSitei | P11021 |
PhosphoSitePlusi | P11021 |
SwissPalmi | P11021 |
Expressioni
Inductioni
Gene expression databases
Bgeei | ENSG00000044574, Expressed in vena cava and 255 other tissues |
ExpressionAtlasi | P11021, baseline and differential |
Genevisiblei | P11021, HS |
Organism-specific databases
HPAi | ENSG00000044574, Low tissue specificity |
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) (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, UGGT1 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).
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 (PubMed:22689054).
Interacts with CCDC47 (By similarity).
Interacts with CLN3 (Probable).
Interacts with KIAA1324; may regulate the function of HSPA5 in apoptosis and cell proliferation (PubMed:26045166).
Interacts with CASP7 (PubMed:26045166).
By similarity1 Publication15 PublicationsBinary interactionsi
Hide detailsP11021
GO - Molecular functioni
- cadherin binding Source: BHF-UCL
- chaperone binding Source: BHF-UCL
- enzyme binding Source: BHF-UCL
- heat shock protein binding Source: GO_Central
- misfolded protein binding Source: UniProtKB
- protein domain specific binding Source: UniProtKB
- ubiquitin protein ligase binding Source: UniProtKB
- unfolded protein binding Source: GO_Central
Protein-protein interaction databases
BioGRIDi | 109541, 793 interactors |
CORUMi | P11021 |
DIPi | DIP-33189N |
ELMi | P11021 |
IntActi | P11021, 401 interactors |
MINTi | P11021 |
STRINGi | 9606.ENSP00000324173 |
Chemistry databases
BindingDBi | P11021 |
Miscellaneous databases
RNActi | P11021, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P11021 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P11021 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 80 | Required for interaction with KIAA13241 PublicationAdd BLAST | 80 | |
Regioni | 125 – 280 | Nucleotide-binding (NBD)1 PublicationAdd BLAST | 156 | |
Regioni | 409 – 419 | Interdomain linkerBy similarityAdd BLAST | 11 | |
Regioni | 420 – 500 | Substrate-binding (SBD)1 PublicationAdd BLAST | 81 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 651 – 654 | Prevents secretion from ERSequence analysis | 4 |
Domaini
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG0100, Eukaryota |
GeneTreei | ENSGT00940000154787 |
HOGENOMi | CLU_005965_3_0_1 |
InParanoidi | P11021 |
OMAi | CVGVMQK |
OrthoDBi | 288077at2759 |
PhylomeDBi | P11021 |
TreeFami | TF105044 |
Family and domain databases
CDDi | cd10241, HSPA5-like_NBD, 1 hit |
DisProti | DP01938 |
Gene3Di | 1.20.1270.10, 1 hit 2.60.34.10, 1 hit |
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 |
PANTHERi | PTHR19375, PTHR19375, 1 hit |
Pfami | View protein in Pfam PF00012, HSP70, 1 hit |
SUPFAMi | SSF100920, SSF100920, 1 hit SSF100934, SSF100934, 1 hit SSF53067, SSF53067, 2 hits |
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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 297 | Missing in AAA52614 (PubMed:2840249).Curated | 1 | |
Sequence conflicti | 297 | Missing in CAA61201 (Ref. 2) Curated | 1 | |
Sequence conflicti | 418 | D → H in AAA52614 (PubMed:2840249).Curated | 1 | |
Sequence conflicti | 418 | D → H in CAA61201 (Ref. 2) Curated | 1 | |
Sequence conflicti | 439 | R → S in AAA52614 (PubMed:2840249).Curated | 1 | |
Sequence conflicti | 439 | R → S in CAA61201 (Ref. 2) Curated | 1 | |
Sequence conflicti | 447 | K → N in AAA52614 (PubMed:2840249).Curated | 1 | |
Sequence conflicti | 447 | K → N in CAA61201 (Ref. 2) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_025815 | 543 | N → H1 PublicationCorresponds to variant dbSNP:rs35356639Ensembl. | 1 |
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. |
CCDSi | CCDS6863.1 |
PIRi | A29821 |
RefSeqi | NP_005338.1, NM_005347.4 |
Genome annotation databases
Ensembli | ENST00000324460; ENSP00000324173; ENSG00000044574 |
GeneIDi | 3309 |
KEGGi | hsa:3309 |
Similar proteinsi
Cross-referencesi
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. |
CCDSi | CCDS6863.1 |
PIRi | A29821 |
RefSeqi | NP_005338.1, NM_005347.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3IUC | X-ray | 2.40 | A/C | 26-410 | [»] | |
3LDL | X-ray | 2.30 | A/B | 26-407 | [»] | |
3LDN | X-ray | 2.20 | A/B | 26-407 | [»] | |
3LDO | X-ray | 1.95 | A/B | 26-407 | [»] | |
3LDP | X-ray | 2.20 | A/B | 26-407 | [»] | |
5E84 | X-ray | 2.99 | A/B/C/D/E/F | 25-633 | [»] | |
5E85 | X-ray | 2.57 | A | 418-637 | [»] | |
5E86 | X-ray | 2.68 | A | 418-637 | [»] | |
5EVZ | X-ray | 1.85 | A/B | 26-407 | [»] | |
5EX5 | X-ray | 1.90 | A/B | 26-407 | [»] | |
5EXW | X-ray | 1.90 | A/B | 26-407 | [»] | |
5EY4 | X-ray | 1.86 | A/B | 26-407 | [»] | |
5F0X | X-ray | 1.60 | A/B | 26-407 | [»] | |
5F1X | X-ray | 1.90 | A/B | 26-407 | [»] | |
5F2R | X-ray | 2.15 | A/B | 26-407 | [»] | |
6ASY | X-ray | 1.85 | A/B | 25-633 | [»] | |
6CZ1 | X-ray | 1.68 | A/B | 26-407 | [»] | |
6DFM | X-ray | 2.14 | A/B | 26-407 | [»] | |
6DFO | X-ray | 2.54 | A/B | 26-407 | [»] | |
6DO2 | X-ray | 1.70 | A/B | 26-407 | [»] | |
6DWS | X-ray | 1.90 | A/B | 26-407 | [»] | |
SMRi | P11021 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109541, 793 interactors |
CORUMi | P11021 |
DIPi | DIP-33189N |
ELMi | P11021 |
IntActi | P11021, 401 interactors |
MINTi | P11021 |
STRINGi | 9606.ENSP00000324173 |
Chemistry databases
BindingDBi | P11021 |
ChEMBLi | CHEMBL1781865 |
DrugBanki | DB00945, Acetylsalicylic acid DB00025, Antihemophilic factor, human recombinant DB09130, Copper DB13998, Lonoctocog alfa DB13999, Moroctocog alfa |
Protein family/group databases
TCDBi | 1.A.33.1.5, the cation channel-forming heat shock protein-70 (hsp70) family |
PTM databases
GlyGeni | P11021, 1 site |
iPTMneti | P11021 |
MetOSitei | P11021 |
PhosphoSitePlusi | P11021 |
SwissPalmi | P11021 |
Genetic variation databases
BioMutai | HSPA5 |
DMDMi | 14916999 |
2D gel databases
DOSAC-COBS-2DPAGEi | P11021 |
OGPi | P11021 |
REPRODUCTION-2DPAGEi | P11021 |
SWISS-2DPAGEi | P11021 |
UCD-2DPAGEi | P11021 |
Proteomic databases
CPTACi | CPTAC-524 CPTAC-525 non-CPTAC-2616 |
EPDi | P11021 |
jPOSTi | P11021 |
MassIVEi | P11021 |
PaxDbi | P11021 |
PeptideAtlasi | P11021 |
PRIDEi | P11021 |
ProteomicsDBi | 52688 |
TopDownProteomicsi | P11021 |
Protocols and materials databases
ABCDi | P11021, 16 sequenced antibodies |
Antibodypediai | 3926, 1672 antibodies |
DNASUi | 3309 |
Genome annotation databases
Ensembli | ENST00000324460; ENSP00000324173; ENSG00000044574 |
GeneIDi | 3309 |
KEGGi | hsa:3309 |
Organism-specific databases
CTDi | 3309 |
DisGeNETi | 3309 |
GeneCardsi | HSPA5 |
HGNCi | HGNC:5238, HSPA5 |
HPAi | ENSG00000044574, Low tissue specificity |
MIMi | 138120, gene |
neXtProti | NX_P11021 |
OpenTargetsi | ENSG00000044574 |
PharmGKBi | PA29504 |
VEuPathDBi | HostDB:ENSG00000044574.7 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0100, Eukaryota |
GeneTreei | ENSGT00940000154787 |
HOGENOMi | CLU_005965_3_0_1 |
InParanoidi | P11021 |
OMAi | CVGVMQK |
OrthoDBi | 288077at2759 |
PhylomeDBi | P11021 |
TreeFami | TF105044 |
Enzyme and pathway databases
PathwayCommonsi | P11021 |
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 |
SIGNORi | P11021 |
Miscellaneous databases
BioGRID-ORCSi | 3309, 641 hits in 878 CRISPR screens |
ChiTaRSi | HSPA5, human |
EvolutionaryTracei | P11021 |
GeneWikii | Binding_immunoglobulin_protein |
GenomeRNAii | 3309 |
Pharosi | P11021, Tchem |
PROi | PR:P11021 |
RNActi | P11021, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000044574, Expressed in vena cava and 255 other tissues |
ExpressionAtlasi | P11021, baseline and differential |
Genevisiblei | P11021, HS |
Family and domain databases
CDDi | cd10241, HSPA5-like_NBD, 1 hit |
DisProti | DP01938 |
Gene3Di | 1.20.1270.10, 1 hit 2.60.34.10, 1 hit |
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 |
PANTHERi | PTHR19375, PTHR19375, 1 hit |
Pfami | View protein in Pfam PF00012, HSP70, 1 hit |
SUPFAMi | SSF100920, SSF100920, 1 hit SSF100934, SSF100934, 1 hit SSF53067, SSF53067, 2 hits |
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... |
MobiDBi | Search... |
Entry informationi
Entry namei | BIP_HUMAN | |
Accessioni | P11021Primary (citable) accession number: P11021 Secondary accession number(s): B0QZ61 Q9UK02 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | July 11, 2001 | |
Last modified: | February 10, 2021 | |
This is version 236 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families