UniProt Accession

 GRP78_MOUSE; P20029; O35642; Q3UFF2; Q61630 

Genbank Protein ID

 AJ002387; M19351; D78645; AK076079; AK146647; AK148539; AK151647; AK152020; AK166739; AK169034; BC050927; U16277; M30779 

Genbank Nucleotide ID

 CAA05361.1; AAA37315.1; BAA11462.1; BAC36166.1; BAE27328.1; BAE28609.1; BAE30576.1; BAE30882.1; BAE38982.1; BAE40825.1; AAH50927.1; AAA76734.1; AAA37742.1 

Protein Name

 78 kDa glucose-regulated protein 

Protein Synonyms/Alias

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

Gene Name

 Hspa5 

Gene Synonyms/Alias

 Grp78 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
82	RLIGDAAKNQLTSNP	acetylation	[1, 2]
82	RLIGDAAKNQLTSNP	succinylation	[2]
82	RLIGDAAKNQLTSNP	ubiquitination	[3]
97	ENTVFDAKRLIGRTW	acetylation	[2, 4]
97	ENTVFDAKRLIGRTW	succinylation	[2]
97	ENTVFDAKRLIGRTW	ubiquitination	[3]
114	PSVQQDIKFLPFKVV	acetylation	[5]
114	PSVQQDIKFLPFKVV	ubiquitination	[3]
119	DIKFLPFKVVEKKTK	acetylation	[2, 4, 5]
119	DIKFLPFKVVEKKTK	succinylation	[2]
119	DIKFLPFKVVEKKTK	ubiquitination	[3]
126	KVVEKKTKPYIQVDI	acetylation	[2, 5]
153	ISAMVLTKMKETAEA	acetylation	[5]
164	TAEAYLGKKVTHAVV	ubiquitination	[3]
165	AEAYLGKKVTHAVVT	acetylation	[5]
165	AEAYLGKKVTHAVVT	ubiquitination	[3]
186	DAQRQATKDAGTIAG	acetylation	[2]
186	DAQRQATKDAGTIAG	succinylation	[2]
186	DAQRQATKDAGTIAG	ubiquitination	[3]
214	AIAYGLDKREGEKNI	acetylation	[2, 4, 5, 6, 7]
214	AIAYGLDKREGEKNI	succinylation	[2]
214	AIAYGLDKREGEKNI	ubiquitination	[3]
269	RVMEHFIKLYKKKTG	acetylation	[2, 5, 6, 8]
269	RVMEHFIKLYKKKTG	succinylation	[2]
295	KLRREVEKAKRALSS	acetylation	[6]
327	SETLTRAKFEELNMD	acetylation	[2, 5, 6, 7, 8]
327	SETLTRAKFEELNMD	ubiquitination	[3]
341	DLFRSTMKPVQKVLE	acetylation	[5]
345	STMKPVQKVLEDSDL	acetylation	[5]
353	VLEDSDLKKSDIDEI	acetylation	[4, 6]
353	VLEDSDLKKSDIDEI	ubiquitination	[3]
354	LEDSDLKKSDIDEIV	acetylation	[2]
354	LEDSDLKKSDIDEIV	succinylation	[2]
371	GGSTRIPKIQQLVKE	ubiquitination	[3]
377	PKIQQLVKEFFNGKE	acetylation	[5]
383	VKEFFNGKEPSRGIN	acetylation	[5]
447	RNTVVPTKKSQIFST	acetylation	[2]
447	RNTVVPTKKSQIFST	succinylation	[2]
448	NTVVPTKKSQIFSTA	acetylation	[2]
448	NTVVPTKKSQIFSTA	succinylation	[2]
448	NTVVPTKKSQIFSTA	ubiquitination	[3]
517	LRVTAEDKGTGNKNK	acetylation	[6]
524	KGTGNKNKITITNDQ	acetylation	[2, 4]
524	KGTGNKNKITITNDQ	succinylation	[2]
524	KGTGNKNKITITNDQ	ubiquitination	[3]
548	RMVNDAEKFAEEDKK	acetylation	[4]
548	RMVNDAEKFAEEDKK	ubiquitination	[3]
554	EKFAEEDKKLKERID	acetylation	[6]
574	ESYAYSLKNQIGDKE	ubiquitination	[3]
580	LKNQIGDKEKLGGKL	acetylation	[4, 6]
586	DKEKLGGKLSSEDKE	acetylation	[9]
602	MEKAVEEKIEWLESH	acetylation	[5]
618	DADIEDFKAKKKELE	acetylation	[2]

Reference

 [1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] 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]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [6] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [8] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [9] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753] 

Functional Description

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

Sequence Annotation

 MOTIF 652 655 Prevents secretion from ER.
 MOD_RES 161 161 Nitrated tyrosine.
 MOD_RES 167 167 Phosphothreonine.
 MOD_RES 519 519 Phosphothreonine (By similarity).
 MOD_RES 572 572 Phosphoserine.
 MOD_RES 586 586 N6,N6,N6-trimethyllysine; by METTL21A; in
 MOD_RES 650 650 Phosphoserine.  

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

 655 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IDA:MGI.
 GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Compara.
 GO:0005788; C:endoplasmic reticulum lumen; IDA:BHF-UCL.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Compara.
 GO:0005576; C:extracellular region; TAS:Reactome.
 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:0051787; F:misfolded protein binding; IDA:BHF-UCL.
 GO:0043022; F:ribosome binding; IDA:MGI.
 GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; IMP:BHF-UCL.
 GO:0042149; P:cellular response to glucose starvation; IEA:Compara.
 GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
 GO:0021680; P:cerebellar Purkinje cell layer development; IMP:BHF-UCL.
 GO:0021589; P:cerebellum structural organization; IMP:BHF-UCL.
 GO:0006983; P:ER overload response; IDA:MGI.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
 GO:0040019; P:positive regulation of embryonic development; TAS:BHF-UCL.
 GO:0031398; P:positive regulation of protein ubiquitination; IMP:BHF-UCL.
 GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL. 

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.