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Protein

78 kDa glucose-regulated protein

Gene

Hspa5

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 394ATPBy similarity
Nucleotide bindingi227 – 2293ATPBy similarity
Nucleotide bindingi293 – 3008ATPBy similarity
Nucleotide bindingi364 – 3674ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. misfolded protein binding Source: MGI
  3. ribosome binding Source: Ensembl
  4. unfolded protein binding Source: RGD

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Ensembl
  2. cellular response to antibiotic Source: RGD
  3. cellular response to glucose starvation Source: Ensembl
  4. cellular response to interleukin-4 Source: Ensembl
  5. cerebellar Purkinje cell layer development Source: Ensembl
  6. cerebellum structural organization Source: Ensembl
  7. ER overload response Source: Ensembl
  8. maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
  9. negative regulation of apoptotic process Source: Ensembl
  10. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  11. positive regulation of cell migration Source: UniProtKB
  12. positive regulation of protein ubiquitination Source: Ensembl
  13. proteolysis involved in cellular protein catabolic process Source: Ensembl
  14. response to endoplasmic reticulum stress Source: MGI
  15. substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_100458. ATF6-alpha activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
78 kDa glucose-regulated protein
Short name:
GRP-78
Alternative name(s):
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
Short name:
BiP
Steroidogenesis-activator polypeptide
Gene namesi
Name:Hspa5
Synonyms:Grp78
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi2843. Hspa5.

Subcellular locationi

Endoplasmic reticulum lumen. Melanosome By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. COP9 signalosome Source: Ensembl
  3. endoplasmic reticulum Source: MGI
  4. endoplasmic reticulum chaperone complex Source: Ensembl
  5. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  6. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  7. extracellular vesicular exosome Source: Ensembl
  8. integral component of endoplasmic reticulum membrane Source: Ensembl
  9. melanosome Source: UniProtKB-SubCell
  10. membrane Source: MGI
  11. midbody Source: Ensembl
  12. mitochondrion Source: RGD
  13. smooth endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 65463678 kDa glucose-regulated proteinPRO_0000013569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei160 – 1601Nitrated tyrosineBy similarity
Modified residuei213 – 2131N6-acetyllysineBy similarity
Modified residuei326 – 3261N6-acetyllysineBy similarity
Modified residuei353 – 3531N6-acetyllysineBy similarity
Modified residuei447 – 4471N6-succinyllysineBy similarity
Modified residuei518 – 5181PhosphothreonineBy similarity
Modified residuei585 – 5851N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity
Modified residuei649 – 6491PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Methylation, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP06761.
PRIDEiP06761.

PTM databases

PhosphoSiteiP06761.

Expressioni

Gene expression databases

GenevestigatoriP06761.

Interactioni

Subunit structurei

May form a complex with ERLEC1, OS9, SEL1L and SYVN1 (By similarity). Interacts with DNAJC1 (via J domain). Interacts with TRIM21 (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. Interacts with TMEM132A. Interacts with MX1. Interacts with METTL23 and DNAJC10. Interacts with CEMIP; the interaction induces calcium leakage from the endoplamic reticulum and cell migration (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Sigmar1Q9R0C93EBI-916036,EBI-1557826
TgP068826EBI-916036,EBI-1549657

Protein-protein interaction databases

BioGridi247646. 8 interactions.
IntActiP06761. 16 interactions.
MINTiMINT-4575479.
STRINGi10116.ENSRNOP00000025064.

Structurei

3D structure databases

ProteinModelPortaliP06761.
SMRiP06761. Positions 28-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi651 – 6544Prevents secretion from ER

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP06761.
KOiK09490.
OMAiESHQDGD.
OrthoDBiEOG780RKX.
PhylomeDBiP06761.
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.

P06761-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFTVVAAAL LLLCAVRAEE 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 SFFEGEDFSE 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 KLGGKLSPED KETMEKAVEE
610 620 630 640 650
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSGGP PPTGEEDTSE

KDEL
Length:654
Mass (Da):72,347
Last modified:April 1, 1988 - v1
Checksum:i9D686C6484150108
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291T → M in AAA41277. (PubMed:3468506)Curated
Sequence conflicti649 – 6491S → D AA sequence (PubMed:3563495)Curated
Sequence conflicti651 – 6511K → KK AA sequence (PubMed:3563495)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14050 mRNA. Translation: AAA40817.1.
BC062017 mRNA. Translation: AAH62017.1.
M14866 Genomic DNA. Translation: AAA41277.1.
PIRiA23948. HHRTGB.
RefSeqiNP_037215.1. NM_013083.2.
UniGeneiRn.11088.

Genome annotation databases

EnsembliENSRNOT00000025067; ENSRNOP00000025064; ENSRNOG00000018294.
GeneIDi25617.
KEGGirno:25617.
UCSCiRGD:2843. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14050 mRNA. Translation: AAA40817.1.
BC062017 mRNA. Translation: AAH62017.1.
M14866 Genomic DNA. Translation: AAA41277.1.
PIRiA23948. HHRTGB.
RefSeqiNP_037215.1. NM_013083.2.
UniGeneiRn.11088.

3D structure databases

ProteinModelPortaliP06761.
SMRiP06761. Positions 28-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247646. 8 interactions.
IntActiP06761. 16 interactions.
MINTiMINT-4575479.
STRINGi10116.ENSRNOP00000025064.

PTM databases

PhosphoSiteiP06761.

Proteomic databases

PaxDbiP06761.
PRIDEiP06761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025067; ENSRNOP00000025064; ENSRNOG00000018294.
GeneIDi25617.
KEGGirno:25617.
UCSCiRGD:2843. rat.

Organism-specific databases

CTDi3309.
RGDi2843. Hspa5.

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP06761.
KOiK09490.
OMAiESHQDGD.
OrthoDBiEOG780RKX.
PhylomeDBiP06761.
TreeFamiTF105044.

Enzyme and pathway databases

ReactomeiREACT_100458. ATF6-alpha activates chaperone genes.

Miscellaneous databases

NextBioi607375.
PROiP06761.

Gene expression databases

GenevestigatoriP06761.

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...

Publicationsi

« Hide 'large scale' publications
  1. "An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein."
    Munro S., Pelham H.R.B.
    Cell 46:291-300(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression."
    Chang S.C., Wooden S.K., Nakaki T., Kim Y.K., Lin A.Y., Kung L., Attenello J.W., Lee A.S.
    Proc. Natl. Acad. Sci. U.S.A. 84:680-684(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
  4. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 50-60; 165-181; 307-324; 475-492 AND 533-540, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  5. "Steroidogenesis-activator polypeptide isolated from a rat Leydig cell tumor."
    Pedersen R.C., Brownie A.C.
    Science 236:188-190(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 626-654.
  6. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
    Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
    Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF A CHAPERONE COMPLEX.
  7. "Cloning and characterization of a novel GRP78-binding protein in the rat brain."
    Oh-hashi K., Naruse Y., Amaya F., Shimosato G., Tanaka M.
    J. Biol. Chem. 278:10531-10537(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM132A.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiGRP78_RAT
AccessioniPrimary (citable) accession number: P06761
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 1, 1988
Last modified: January 7, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.