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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

  • ATPase activity Source: Ensembl
  • ATP binding Source: UniProtKB-KW
  • misfolded protein binding Source: MGI
  • ribosome binding Source: Ensembl
  • unfolded protein binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2843. Hspa5.

Subcellular locationi

GO - Cellular componenti

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 residuei86 – 861PhosphoserineCombined sources
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei160 – 1601Nitrated tyrosineBy similarity
Modified residuei213 – 2131N6-acetyllysineBy similarity
Modified residuei271 – 2711N6-acetyllysineBy similarity
Modified residuei326 – 3261N6-acetyllysineBy similarity
Cross-linki352 – 352Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei353 – 3531N6-acetyllysine; alternateBy similarity
Cross-linki353 – 353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei447 – 4471N6-succinyllysineBy similarity
Modified residuei518 – 5181PhosphothreonineBy similarity
Modified residuei585 – 5851N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity
Modified residuei643 – 6431PhosphothreonineBy similarity
Modified residuei648 – 6481PhosphothreonineCombined sources
Modified residuei649 – 6491PhosphoserineCombined sources

Keywords - PTMi

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

Proteomic databases

PaxDbiP06761.
PRIDEiP06761.

PTM databases

iPTMnetiP06761.
PhosphoSiteiP06761.

Expressioni

Gene expression databases

BgeeiENSRNOG00000018294.
GenevisibleiP06761. RN.

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

GO - Molecular functioni

  • misfolded protein binding Source: MGI
  • unfolded protein binding Source: RGD

Protein-protein interaction databases

BioGridi247646. 7 interactions.
IntActiP06761. 17 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

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP06761.
KOiK09490.
OMAiESHQDGD.
OrthoDBiEOG091G0352.
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. 7 interactions.
IntActiP06761. 17 interactions.
MINTiMINT-4575479.
STRINGi10116.ENSRNOP00000025064.

PTM databases

iPTMnetiP06761.
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

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP06761.
KOiK09490.
OMAiESHQDGD.
OrthoDBiEOG091G0352.
PhylomeDBiP06761.
TreeFamiTF105044.

Miscellaneous databases

PROiP06761.

Gene expression databases

BgeeiENSRNOG00000018294.
GenevisibleiP06761. RN.

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_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 7, 2016
This is version 156 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

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.