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Protein

Endoplasmic reticulum chaperone BiP

Gene

HSPA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Caution

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

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei96ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 39ATP1 Publication4
Nucleotide bindingi227 – 229ATP1 Publication3
Nucleotide bindingi293 – 300ATP1 Publication8
Nucleotide bindingi364 – 367ATP1 Publication4

GO - Molecular functioni

  • ATPase activity Source: AgBase
  • ATP binding Source: UniProtKB-KW
  • cadherin binding Source: BHF-UCL
  • calcium ion binding Source: UniProtKB
  • chaperone binding Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • misfolded protein binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • ribosome binding Source: Ensembl
  • ubiquitin protein ligase binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionChaperone, Hydrolase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Protein family/group databases

TCDBi1.A.33.1.6 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
Name:HSPA5Imported
Synonyms:GRP781 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000044574.7
HGNCiHGNC:5238 HSPA5
MIMi138120 gene
neXtProtiNX_P11021

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Autoantigen in rheumatoid arthritis.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi229T → A: Impaired ATPase activity. 1 Publication1
Mutagenesisi585K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications1

Organism-specific databases

DisGeNETi3309
OpenTargetsiENSG00000044574
PharmGKBiPA29504

Chemistry databases

ChEMBLiCHEMBL1781865
DrugBankiDB00945 Acetylsalicylic acid
DB00025 Antihemophilic Factor (Recombinant)

Polymorphism and mutation databases

BioMutaiHSPA5
DMDMi14916999

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 182 PublicationsAdd BLAST18
ChainiPRO_000001356619 – 654Endoplasmic reticulum chaperone BiPAdd BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei86PhosphoserineBy similarity1
Modified residuei125N6-acetyllysineBy similarity1
Modified residuei160Nitrated tyrosineBy similarity1
Modified residuei213N6-acetyllysineBy similarity1
Modified residuei271N6-acetyllysineBy similarity1
Modified residuei326N6-acetyllysineBy similarity1
Cross-linki352Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei353N6-acetyllysine; alternateBy similarity1
Cross-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei447N6-succinyllysineBy similarity1
Modified residuei492Omega-N-methylarginineBy similarity1
Modified residuei518O-AMP-threonine; alternateBy similarity1
Modified residuei518Phosphothreonine; alternateCombined sources1
Modified residuei585N6,N6,N6-trimethyllysine; by METTL21A; in vitroCombined sources2 Publications1
Modified residuei585N6,N6-dimethyllysine; alternateCombined sources1
Modified residuei585N6-methyllysine; alternateCombined sources1
Modified residuei591N6-methyllysineCombined sources1
Modified residuei643PhosphothreonineBy similarity1
Modified residuei648PhosphothreonineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

EPDiP11021
PaxDbiP11021
PeptideAtlasiP11021
PRIDEiP11021
ProteomicsDBi52688
TopDownProteomicsiP11021

2D gel databases

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

PTM databases

iPTMnetiP11021
PhosphoSitePlusiP11021
SwissPalmiP11021

Expressioni

Inductioni

By endoplasmic reticulum stress.1 Publication

Gene expression databases

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

Organism-specific databases

HPAiCAB005221
HPA038845
HPA038846

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, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (By similarity). Interacts with TMEM132A and TRIM21 (PubMed:12699405). May form a complex with ERLEC1, OS9, SEL1L and SYVN1 (PubMed:18264092,PubMed:18502753). Interacts with DNAJC10 (PubMed:12411443, PubMed:23769672). Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to ERN1/IRE1 (By similarity). Interacts with ERN1/IRE1; interaction takes place following interaction with DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1 (By similarity). Interacts with MX1 (By similarity). Interacts with METTL23 (PubMed:23349634). Interacts with CEMIP; the interaction induces calcium leakage from the endoplasmic reticulum and cell migration (PubMed:23990668). Interacts with PCSK4 form; the interaction takes place in the endoplasmic reticulum (PubMed:21080038). Interacts with CIPC (PubMed:26657846). Interacts with CCDC88B (via C-terminus); the interaction opposes ERN1-mediated JNK activation, protecting against apoptosis (PubMed:21289099). Interacts with INPP5K; necessary for INPP5K localization at the endoplasmic reticulum (PubMed:26940976). Interacts with MANF; the interaction is direct (PubMed:22637475). Interacts with LOXL2; leading to activate the ERN1/IRE1-XBP1 pathway of the unfolded protein response (PubMed:28332555).By similarity13 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109541, 572 interactors
CORUMiP11021
DIPiDIP-33189N
ELMiP11021
IntActiP11021, 196 interactors
MINTiP11021
STRINGi9606.ENSP00000324173

Chemistry databases

BindingDBiP11021

Structurei

Secondary structure

1654
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP11021
SMRiP11021
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11021

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni125 – 280Nucleotide-binding (NBD)1 PublicationAdd BLAST156
Regioni409 – 419Interdomain linkerBy similarityAdd BLAST11
Regioni420 – 500Substrate-binding (SBD)1 PublicationAdd BLAST81

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi651 – 654Prevents secretion from ERSequence analysis4

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

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00910000144045
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiP11021
KOiK09490
OMAiCVGVMQK
OrthoDBiEOG091G0352
PhylomeDBiP11021
TreeFamiTF105044

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00014 ER_TARGET, 1 hit
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

KDEL
Length:654
Mass (Da):72,333
Last modified:July 11, 2001 - v2
Checksum:i59B7D8D85BC32A00
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti297Missing in AAA52614 (PubMed:2840249).Curated1
Sequence conflicti297Missing in CAA61201 (Ref. 2) Curated1
Sequence conflicti418D → H in AAA52614 (PubMed:2840249).Curated1
Sequence conflicti418D → H in CAA61201 (Ref. 2) Curated1
Sequence conflicti439R → S in AAA52614 (PubMed:2840249).Curated1
Sequence conflicti439R → S in CAA61201 (Ref. 2) Curated1
Sequence conflicti447K → N in AAA52614 (PubMed:2840249).Curated1
Sequence conflicti447K → N in CAA61201 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025815543N → 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.
CCDSiCCDS6863.1
PIRiA29821
RefSeqiNP_005338.1, NM_005347.4
UniGeneiHs.743241

Genome annotation databases

EnsembliENST00000324460; ENSP00000324173; ENSG00000044574
GeneIDi3309
KEGGihsa:3309

Keywords - Coding sequence diversityi

Polymorphism

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.
CCDSiCCDS6863.1
PIRiA29821
RefSeqiNP_005338.1, NM_005347.4
UniGeneiHs.743241

3D structure databases

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

Protein-protein interaction databases

BioGridi109541, 572 interactors
CORUMiP11021
DIPiDIP-33189N
ELMiP11021
IntActiP11021, 196 interactors
MINTiP11021
STRINGi9606.ENSP00000324173

Chemistry databases

BindingDBiP11021
ChEMBLiCHEMBL1781865
DrugBankiDB00945 Acetylsalicylic acid
DB00025 Antihemophilic Factor (Recombinant)

Protein family/group databases

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

PTM databases

iPTMnetiP11021
PhosphoSitePlusiP11021
SwissPalmiP11021

Polymorphism and mutation databases

BioMutaiHSPA5
DMDMi14916999

2D gel databases

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

Proteomic databases

EPDiP11021
PaxDbiP11021
PeptideAtlasiP11021
PRIDEiP11021
ProteomicsDBi52688
TopDownProteomicsiP11021

Protocols and materials databases

DNASUi3309
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324460; ENSP00000324173; ENSG00000044574
GeneIDi3309
KEGGihsa:3309

Organism-specific databases

CTDi3309
DisGeNETi3309
EuPathDBiHostDB:ENSG00000044574.7
GeneCardsiHSPA5
HGNCiHGNC:5238 HSPA5
HPAiCAB005221
HPA038845
HPA038846
MIMi138120 gene
neXtProtiNX_P11021
OpenTargetsiENSG00000044574
PharmGKBiPA29504
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00910000144045
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiP11021
KOiK09490
OMAiCVGVMQK
OrthoDBiEOG091G0352
PhylomeDBiP11021
TreeFamiTF105044

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiHSPA5 human
EvolutionaryTraceiP11021
GeneWikiiBinding_immunoglobulin_protein
GenomeRNAii3309
PROiPR:P11021
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00014 ER_TARGET, 1 hit
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiBIP_HUMAN
AccessioniPrimary (citable) accession number: P11021
Secondary accession number(s): B0QZ61
, Q2EF78, Q9NPF1, Q9UK02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 11, 2001
Last modified: October 10, 2018
This is version 217 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
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