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Protein

78 kDa glucose-regulated protein

Gene

HSPA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei96ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 39ATP4
Nucleotide bindingi227 – 229ATP3
Nucleotide bindingi293 – 300ATP8
Nucleotide bindingi364 – 367ATP4

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • calcium ion binding Source: UniProtKB
  • chaperone binding Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • glycoprotein binding Source: UniProtKB
  • 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

  • activation of signaling protein activity involved in unfolded protein response Source: Ensembl
  • ATF6-mediated unfolded protein response Source: Reactome
  • cellular response to antibiotic Source: Ensembl
  • cellular response to glucose starvation Source: UniProtKB
  • cellular response to interleukin-4 Source: Ensembl
  • cellular response to manganese ion Source: Ensembl
  • cerebellar Purkinje cell layer development Source: Ensembl
  • cerebellum structural organization Source: Ensembl
  • endoplasmic reticulum unfolded protein response Source: BHF-UCL
  • ER-associated ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • ER overload response Source: Ensembl
  • IRE1-mediated unfolded protein response Source: Reactome
  • maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of protein homodimerization activity Source: ParkinsonsUK-UCL
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  • PERK-mediated unfolded protein response Source: Reactome
  • positive regulation of cell migration Source: UniProtKB
  • 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
  • protein folding in endoplasmic reticulum Source: ParkinsonsUK-UCL
  • 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
  • substantia nigra development Source: UniProtKB
  • toxin transport Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000044574-MONOMER.
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.

Names & Taxonomyi

Protein namesi
Recommended name:
78 kDa glucose-regulated protein
Short name:
GRP-78
Alternative name(s):
Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
Short name:
BiP
Gene namesi
Name:HSPA5
Synonyms:GRP78
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:5238. HSPA5.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cell surface Source: Ensembl
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum chaperone complex Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • integral component of endoplasmic reticulum membrane Source: BHF-UCL
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • midbody Source: UniProtKB
  • mitochondrion Source: Ensembl
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: Ensembl
  • smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Autoantigen in rheumatoid arthritis.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 – 65478 kDa glucose-regulated proteinAdd 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 residuei518PhosphothreonineCombined 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

Keywords - PTMi

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

Proteomic databases

EPDiP11021.
PaxDbiP11021.
PeptideAtlasiP11021.
PRIDEiP11021.
TopDownProteomicsiP11021.

2D gel databases

DOSAC-COBS-2DPAGEP11021.
OGPiP11021.
REPRODUCTION-2DPAGEP11021.
SWISS-2DPAGEP11021.
UCD-2DPAGEP11021.

PTM databases

iPTMnetiP11021.
PhosphoSitePlusiP11021.
SwissPalmiP11021.

Expressioni

Inductioni

By endoplasmic reticulum stress.1 Publication

Gene expression databases

BgeeiENSG00000044574.
CleanExiHS_HSPA5.
ExpressionAtlasiP11021. baseline and differential.
GenevisibleiP11021. HS.

Organism-specific databases

HPAiCAB005221.
HPA038845.
HPA038846.

Interactioni

Subunit structurei

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. 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 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).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q6T4243EBI-354921,EBI-7888150
AKT1P317492EBI-354921,EBI-296087
ATF6P188502EBI-354921,EBI-852157
DMKNQ6E0U43EBI-354921,EBI-7943171
DNAJB11Q9UBS43EBI-354921,EBI-713113
Dnajc3Q91YW32EBI-354921,EBI-8381770From a different organism.
EIF2AK3Q9NZJ54EBI-354921,EBI-766076
ERN1O754603EBI-354921,EBI-371750
PAWRQ96IZ08EBI-354921,EBI-595869
PawrQ626274EBI-354921,EBI-1187240From a different organism.
RAF1P040494EBI-354921,EBI-365996
SEC61A1P616193EBI-354921,EBI-358919

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • chaperone binding Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • misfolded protein binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109541. 462 interactors.
DIPiDIP-33189N.
IntActiP11021. 180 interactors.
MINTiMINT-1135308.
STRINGi9606.ENSP00000324173.

Chemistry databases

BindingDBiP11021.

Structurei

Secondary structure

1654
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 34Combined sources4
Beta strandi37 – 45Combined sources9
Beta strandi47 – 52Combined sources6
Beta strandi60 – 63Combined sources4
Beta strandi66 – 68Combined sources3
Beta strandi74 – 76Combined sources3
Helixi78 – 82Combined sources5
Helixi84 – 86Combined sources3
Helixi88 – 90Combined sources3
Beta strandi91 – 93Combined sources3
Helixi95 – 97Combined sources3
Turni98 – 100Combined sources3
Helixi106 – 114Combined sources9
Beta strandi116 – 122Combined sources7
Beta strandi125 – 131Combined sources7
Beta strandi137 – 140Combined sources4
Helixi142 – 161Combined sources20
Beta strandi167 – 172Combined sources6
Helixi178 – 190Combined sources13
Beta strandi194 – 200Combined sources7
Helixi201 – 208Combined sources8
Turni209 – 212Combined sources4
Beta strandi215 – 225Combined sources11
Beta strandi230 – 238Combined sources9
Beta strandi241 – 250Combined sources10
Helixi255 – 274Combined sources20
Helixi278 – 280Combined sources3
Helixi282 – 298Combined sources17
Turni299 – 301Combined sources3
Beta strandi302 – 313Combined sources12
Beta strandi316 – 323Combined sources8
Helixi324 – 337Combined sources14
Helixi339 – 348Combined sources10
Helixi353 – 355Combined sources3
Beta strandi358 – 363Combined sources6
Helixi364 – 367Combined sources4
Helixi369 – 378Combined sources10
Turni379 – 381Combined sources3
Turni390 – 392Combined sources3
Helixi393 – 405Combined sources13
Beta strandi415 – 419Combined sources5
Beta strandi424 – 428Combined sources5
Turni429 – 431Combined sources3
Beta strandi432 – 437Combined sources6
Beta strandi442 – 455Combined sources14
Beta strandi460 – 467Combined sources8
Helixi473 – 475Combined sources3
Beta strandi476 – 485Combined sources10
Beta strandi491 – 493Combined sources3
Beta strandi497 – 503Combined sources7
Beta strandi509 – 515Combined sources7
Turni516 – 518Combined sources3
Beta strandi521 – 526Combined sources6
Turni528 – 531Combined sources4
Helixi535 – 547Combined sources13
Helixi549 – 577Combined sources29
Turni579 – 581Combined sources3
Helixi582 – 585Combined sources4
Helixi590 – 606Combined sources17
Helixi613 – 634Combined sources22

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[»]
ProteinModelPortaliP11021.
SMRiP11021.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11021.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi651 – 654Prevents secretion from ER4

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP11021.
KOiK09490.
OMAiESHQDGD.
OrthoDBiEOG091G0352.
PhylomeDBiP11021.
TreeFamiTF105044.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

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 → H.1 PublicationCorresponds to variant rs35356639dbSNPEnsembl.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. Translation: CAQ08732.1.
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

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. Translation: CAQ08732.1.
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[»]
ProteinModelPortaliP11021.
SMRiP11021.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109541. 462 interactors.
DIPiDIP-33189N.
IntActiP11021. 180 interactors.
MINTiMINT-1135308.
STRINGi9606.ENSP00000324173.

Chemistry databases

BindingDBiP11021.
ChEMBLiCHEMBL1781865.
DrugBankiDB00945. Acetylsalicylic acid.
DB00025. Antihemophilic Factor (Recombinant).

PTM databases

iPTMnetiP11021.
PhosphoSitePlusiP11021.
SwissPalmiP11021.

Polymorphism and mutation databases

BioMutaiHSPA5.
DMDMi14916999.

2D gel databases

DOSAC-COBS-2DPAGEP11021.
OGPiP11021.
REPRODUCTION-2DPAGEP11021.
SWISS-2DPAGEP11021.
UCD-2DPAGEP11021.

Proteomic databases

EPDiP11021.
PaxDbiP11021.
PeptideAtlasiP11021.
PRIDEiP11021.
TopDownProteomicsiP11021.

Protocols and materials databases

DNASUi3309.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324460; ENSP00000324173; ENSG00000044574.
GeneIDi3309.
KEGGihsa:3309.

Organism-specific databases

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

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP11021.
KOiK09490.
OMAiESHQDGD.
OrthoDBiEOG091G0352.
PhylomeDBiP11021.
TreeFamiTF105044.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000044574-MONOMER.
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.

Miscellaneous databases

ChiTaRSiHSPA5. human.
EvolutionaryTraceiP11021.
GeneWikiiBinding_immunoglobulin_protein.
GenomeRNAii3309.
PROiP11021.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000044574.
CleanExiHS_HSPA5.
ExpressionAtlasiP11021. baseline and differential.
GenevisibleiP11021. HS.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGRP78_HUMAN
AccessioniPrimary (citable) accession number: P11021
Secondary accession number(s): B0QZ61
, Q2EF78, Q9NPF1, Q9UK02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 11, 2001
Last modified: November 30, 2016
This is version 197 of the entry and version 2 of the sequence. [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. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.