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P06761

- GRP78_RAT

UniProt

P06761 - GRP78_RAT

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Protein
78 kDa glucose-regulated protein
Gene
Hspa5, Grp78
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Sites

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

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. ER overload response Source: Ensembl
  2. activation of signaling protein activity involved in unfolded protein response Source: Ensembl
  3. cellular response to antibiotic Source: RGD
  4. cellular response to glucose starvation Source: Ensembl
  5. cellular response to interleukin-4 Source: Ensembl
  6. cerebellar Purkinje cell layer development Source: Ensembl
  7. cerebellum structural organization 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
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. COP9 signalosome Source: Ensembl
  2. cell surface Source: Ensembl
  3. endoplasmic reticulum Source: MGI
  4. endoplasmic reticulum chaperone complex Source: Ensembl
  5. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  6. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  7. integral component of endoplasmic reticulum membrane Source: Ensembl
  8. melanosome Source: UniProtKB-SubCell
  9. membrane Source: MGI
  10. midbody Source: Ensembl
  11. mitochondrion Source: RGD
  12. 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 – 1818 By similarity
Add
BLAST
Chaini19 – 65463678 kDa glucose-regulated protein
PRO_0000013569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251N6-acetyllysine By similarity
Modified residuei160 – 1601Nitrated tyrosine By similarity
Modified residuei213 – 2131N6-acetyllysine By similarity
Modified residuei326 – 3261N6-acetyllysine By similarity
Modified residuei353 – 3531N6-acetyllysine By similarity
Modified residuei447 – 4471N6-succinyllysine By similarity
Modified residuei518 – 5181Phosphothreonine By similarity
Modified residuei585 – 5851N6,N6,N6-trimethyllysine; by METTL21A; in vitro By similarity
Modified residuei649 – 6491Phosphoserine By 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.1 Publication

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.

Family & Domainsi

Motif

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP06761.
KOiK09490.
OMAiDKRAVQK.
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

MKFTVVAAAL LLLCAVRAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV    50
EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG 100
RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL 150
TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN 200
EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD 250
THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS 300
SQHQARIEIE SFFEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD 350
LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV 400
QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI 450
FSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT 500
FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE 550
EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSPED KETMEKAVEE 600
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSGGP PPTGEEDTSE 650
KDEL 654
Length:654
Mass (Da):72,347
Last modified:April 1, 1988 - v1
Checksum:i9D686C6484150108
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291T → M in AAA41277. 1 Publication
Sequence conflicti649 – 6491S → D AA sequence 1 Publication
Sequence conflicti651 – 6511K → KK AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M14050 mRNA. Translation: AAA40817.1 .
BC062017 mRNA. Translation: AAH62017.1 .
M14866 Genomic DNA. Translation: AAA41277.1 .
PIRi A23948. HHRTGB.
RefSeqi NP_037215.1. NM_013083.2.
UniGenei Rn.11088.

3D structure databases

ProteinModelPortali P06761.
SMRi P06761. Positions 28-570.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247646. 8 interactions.
IntActi P06761. 16 interactions.
MINTi MINT-4575479.
STRINGi 10116.ENSRNOP00000025064.

PTM databases

PhosphoSitei P06761.

Proteomic databases

PaxDbi P06761.
PRIDEi P06761.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000025067 ; ENSRNOP00000025064 ; ENSRNOG00000018294 .
GeneIDi 25617.
KEGGi rno:25617.
UCSCi RGD:2843. rat.

Organism-specific databases

CTDi 3309.
RGDi 2843. Hspa5.

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00750000117237.
HOGENOMi HOG000228135.
HOVERGENi HBG051845.
InParanoidi P06761.
KOi K09490.
OMAi DKRAVQK.
OrthoDBi EOG780RKX.
PhylomeDBi P06761.
TreeFami TF105044.

Enzyme and pathway databases

Reactomei REACT_100458. ATF6-alpha activates chaperone genes.

Miscellaneous databases

NextBioi 607375.
PROi P06761.

Gene expression databases

Genevestigatori P06761.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 138 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

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