UniProt Accession

 GRP78_RAT; P06761 

Genbank Protein ID

 M14050; BC062017; M14866 

Genbank Nucleotide ID

 AAA40817.1; AAH62017.1; AAA41277.1 

Protein Name

 78 kDa glucose-regulated protein 

Protein Synonyms/Alias

 GRP-78; Heat shock 70 kDa protein 5; Immunoglobulin heavy chain-binding protein; BiP; Steroidogenesis-activator polypeptide 

Gene Name

 Hspa5 

Gene Synonyms/Alias

 Grp78 

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
81	RLIGDAAKNQLTSNP	acetylation	[1]
81	RLIGDAAKNQLTSNP	ubiquitination	[2]
96	ENTVFDAKRLIGRTW	ubiquitination	[2]
113	PSVQQDIKFLPFKVV	acetylation	[1]
113	PSVQQDIKFLPFKVV	ubiquitination	[2]
118	DIKFLPFKVVEKKTK	acetylation	[1]
118	DIKFLPFKVVEKKTK	ubiquitination	[2]
123	PFKVVEKKTKPYIQV	acetylation	[1]
125	KVVEKKTKPYIQVDI	acetylation	[1]
154	AMVLTKMKETAEAYL	acetylation	[1]
163	TAEAYLGKKVTHAVV	acetylation	[1]
163	TAEAYLGKKVTHAVV	ubiquitination	[2]
164	AEAYLGKKVTHAVVT	acetylation	[1]
164	AEAYLGKKVTHAVVT	ubiquitination	[2]
185	DAQRQATKDAGTIAG	ubiquitination	[2]
213	AIAYGLDKREGEKNI	acetylation	[1]
213	AIAYGLDKREGEKNI	ubiquitination	[2]
268	RVMEHFIKLYKKKTG	acetylation	[1]
287	KDNRAVQKLRREVEK	acetylation	[1]
326	SETLTRAKFEELNMD	acetylation	[1]
326	SETLTRAKFEELNMD	ubiquitination	[2]
352	VLEDSDLKKSDIDEI	acetylation	[1]
352	VLEDSDLKKSDIDEI	ubiquitination	[2]
370	GGSTRIPKIQQLVKE	ubiquitination	[2]
376	PKIQQLVKEFFNGKE	acetylation	[1]
382	VKEFFNGKEPSRGIN	acetylation	[1]
447	NTVVPTKKSQIFSTA	ubiquitination	[2]
523	KGTGNKNKITITNDQ	ubiquitination	[2]
547	RMVNDAEKFAEEDKK	acetylation	[1]
547	RMVNDAEKFAEEDKK	ubiquitination	[2]
553	EKFAEEDKKLKERID	acetylation	[1]
573	ESYAYSLKNQIGDKE	acetylation	[1]
601	MEKAVEEKIEWLESH	acetylation	[1]

Reference

 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

Functional Description

 Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. 

Sequence Annotation

 MOTIF 651 654 Prevents secretion from ER.
 MOD_RES 160 160 Nitrated tyrosine (By similarity).
 MOD_RES 166 166 Phosphothreonine (By similarity).
 MOD_RES 518 518 Phosphothreonine (By similarity).
 MOD_RES 571 571 Phosphoserine (By similarity).
 MOD_RES 585 585 N6,N6,N6-trimethyllysine; by METTL21A; in
 MOD_RES 649 649 Phosphoserine (By similarity).  

Keyword

 ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Methylation; Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome; Signal. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 654 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005783; C:endoplasmic reticulum; IDA:MGI.
 GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Compara.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Compara.
 GO:0030176; C:integral to endoplasmic reticulum membrane; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IEA:Compara.
 GO:0008180; C:signalosome; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0043022; F:ribosome binding; IEA:Compara.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; IEA:Compara.
 GO:0071236; P:cellular response to antibiotic; IEP:RGD.
 GO:0042149; P:cellular response to glucose starvation; IEA:Compara.
 GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Compara.
 GO:0021589; P:cerebellum structural organization; IEA:Compara.
 GO:0006983; P:ER overload response; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Compara.
 GO:0031398; P:positive regulation of protein ubiquitination; IEA:Compara.
 GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:Compara. 

Interpro

 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 

Pfam

 PF00012; HSP70 

SMART

  

PROSITE

 PS00014; ER_TARGET
 PS00297; HSP70_1
 PS00329; HSP70_2
 PS01036; HSP70_3 

PRINTS

 PR00301; HEATSHOCK70.