UniProt Accession

 ENPL_MOUSE; P08113; P11427 

Genbank Protein ID

 J03297; M29652; M16370 

Genbank Nucleotide ID

 AAA37573.1; AAA37743.1; AAA40023.1 

Protein Name

 Endoplasmin 

Protein Synonyms/Alias

 94 kDa glucose-regulated protein; GRP-94; Endoplasmic reticulum resident protein 99; ERp99; Heat shock protein 90 kDa beta member 1; Polymorphic tumor rejection antigen 1; Tumor rejection antigen gp96 

Gene Name

 Hsp90b1 

Gene Synonyms/Alias

 Grp94; Tra-1; Tra1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
72	QIRELREKSEKFAFQ	acetylation	[1]
75	ELREKSEKFAFQAEV	acetylation	[1]
75	ELREKSEKFAFQAEV	ubiquitination	[2]
87	AEVNRMMKLIINSLY	acetylation	[1]
95	LIINSLYKNKEIFLR	acetylation	[3]
95	LIINSLYKNKEIFLR	succinylation	[3]
95	LIINSLYKNKEIFLR	ubiquitination	[2]
97	INSLYKNKEIFLREL	acetylation	[4]
114	NASDALDKIRLISLT	ubiquitination	[2]
140	TVKIKCDKEKNLLHV	acetylation	[4]
161	MTREELVKNLGTIAK	acetylation	[1, 3, 5]
161	MTREELVKNLGTIAK	ubiquitination	[2]
168	KNLGTIAKSGTSEFL	acetylation	[1, 3]
168	KNLGTIAKSGTSEFL	succinylation	[3]
168	KNLGTIAKSGTSEFL	ubiquitination	[2]
265	YLELDTIKNLVRKYS	acetylation	[1]
265	YLELDTIKNLVRKYS	ubiquitination	[2]
270	TIKNLVRKYSQFINF	acetylation	[1]
320	EEEEEEKKPKTKKVE	acetylation	[4]
340	WELMNDIKPIWQRPS	acetylation	[3]
356	EVEEDEYKAFYKSFS	acetylation	[1]
360	DEYKAFYKSFSKESD	acetylation	[1, 3]
360	DEYKAFYKSFSKESD	succinylation	[3]
360	DEYKAFYKSFSKESD	ubiquitination	[2]
404	LFDEYGSKKSDYIKL	ubiquitination	[2]
434	PKYLNFVKGVVDSDD	ubiquitination	[2]
455	RETLQQHKLLKVIRK	acetylation	[4]
455	RETLQQHKLLKVIRK	ubiquitination	[2]
537	RMKEKQDKIYFMAGS	acetylation	[4]
597	NVAKEGVKFDESEKT	acetylation	[4]
603	VKFDESEKTKESREA	acetylation	[4]
663	GNMERIMKAQAYQTG	ubiquitination	[2]
671	AQAYQTGKDISTNYY	ubiquitination	[2]
682	TNYYASQKKTFEINP	ubiquitination	[2]
733	GYLLPDTKAYGDRIE	acetylation	[3]
733	GYLLPDTKAYGDRIE	succinylation	[3]

Reference

 [1] 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]
 [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]
 [3] 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]
 [4] 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]
 [5] 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] 

Functional Description

 Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). 

Sequence Annotation

 MOTIF 799 802 Prevents secretion from ER.
 BINDING 107 107 ATP (By similarity).
 BINDING 149 149 ATP (By similarity).
 BINDING 162 162 ATP (By similarity).
 BINDING 168 168 ATP (By similarity).
 BINDING 199 199 ATP; via amide nitrogen (By similarity).
 BINDING 448 448 ATP (By similarity).
 MOD_RES 306 306 Phosphoserine.
 CARBOHYD 62 62 N-linked (GlcNAc...) (Potential).
 CARBOHYD 107 107 N-linked (GlcNAc...) (Potential).
 CARBOHYD 217 217 N-linked (GlcNAc...).
 CARBOHYD 445 445 N-linked (GlcNAc...) (Potential).
 CARBOHYD 481 481 N-linked (GlcNAc...) (Potential).
 CARBOHYD 502 502 N-linked (GlcNAc...) (Potential).
 DISULFID 138 138 Interchain.  

Keyword

 ATP-binding; Calcium; Chaperone; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding; Phosphoprotein; Reference proteome; Signal. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 802 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005783; C:endoplasmic reticulum; IDA:MGI.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005886; C:plasma membrane; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
 GO:0019903; F:protein phosphatase binding; ISO:MGI.
 GO:0003723; F:RNA binding; IEA:Compara.
 GO:0046790; F:virion binding; IEA:Compara.
 GO:0031247; P:actin rod assembly; ISO:MGI.
 GO:0071318; P:cellular response to ATP; ISO:MGI.
 GO:0030433; P:ER-associated protein catabolic process; ISS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:MGI.
 GO:0001666; P:response to hypoxia; IEA:Compara. 

Interpro

 IPR015566; Endoplasmin.
 IPR003594; HATPase_ATP-bd.
 IPR019805; Heat_shock_protein_90_CS.
 IPR001404; Hsp90.
 IPR020575; Hsp90_N.
 IPR020568; Ribosomal_S5_D2-typ_fold. 

Pfam

 PF00183; HSP90 

SMART

 SM00387; HATPase_c 

PROSITE

 PS00014; ER_TARGET
 PS00298; HSP90 

PRINTS

 PR00775; HEATSHOCK90.