UniProt Accession

 GRP75_MOUSE; P38647; Q3TW93; Q3UVN1; Q3V015; Q7TSZ0; Q9CQ05 

Genbank Protein ID

 D11089; L06896; D17666; D17556; AK004946; AK002634; AK133501; AK137109; AK145965; AK159791; AK165958; AK167856; AC114820; AC131675; CH466557; BC052727; BC057343 

Genbank Nucleotide ID

 BAA01862.2; BAA04548.1; BAA04493.1; BAB23690.1; BAB22248.1; BAE21690.1; BAE23238.1; BAE26790.1; BAE35373.1; BAE38486.1; BAE39874.1; EDK97122.1; AAH52727.1; AAH57343.1 

Protein Name

 Stress-70 protein, mitochondrial 

Protein Synonyms/Alias

 75 kDa glucose-regulated protein; GRP-75; Heat shock 70 kDa protein 9; Mortalin; Peptide-binding protein 74; PBP74; p66 MOT 

Gene Name

 Hspa9 

Gene Synonyms/Alias

 Grp75; Hsp74; Hspa9a 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
76	VMEGKQAKVLENAEG	acetylation	[1]
121	NNTFYATKRLIGRRY	acetylation	[2, 3]
121	NNTFYATKRLIGRRY	ubiquitination	[4]
135	YDDPEVQKDTKNVPF	acetylation	[1, 2, 3, 5, 6, 7, 8, 9, 10]
135	YDDPEVQKDTKNVPF	succinylation	[10]
138	PEVQKDTKNVPFKIV	acetylation	[1, 2, 3, 5, 8, 10]
138	PEVQKDTKNVPFKIV	succinylation	[10]
143	DTKNVPFKIVRASNG	acetylation	[1, 3, 8, 11]
159	AWVEAHGKLYSPSQI	acetylation	[1, 3, 5, 8, 11]
175	AFVLMKMKETAENYL	acetylation	[1, 3, 8, 10]
175	AFVLMKMKETAENYL	succinylation	[10]
187	NYLGHTAKNAVITVP	acetylation	[10]
187	NYLGHTAKNAVITVP	succinylation	[10]
206	DSQRQATKDAGQISG	acetylation	[1, 3, 5, 7, 8, 10]
206	DSQRQATKDAGQISG	succinylation	[10]
234	ALAYGLDKSEDKVIA	acetylation	[1, 3, 6, 10, 11]
234	ALAYGLDKSEDKVIA	ubiquitination	[4]
265	QKGVFEVKSTNGDTF	acetylation	[3]
288	ALLRHIVKEFKRETG	acetylation	[1, 2, 3, 5, 6, 7, 8, 10, 11, 12]
288	ALLRHIVKEFKRETG	succinylation	[10]
291	RHIVKEFKRETGVDL	acetylation	[8]
300	ETGVDLTKDNMALQR	acetylation	[1, 2, 3, 5, 6, 7, 8, 9, 10, 11, 12]
300	ETGVDLTKDNMALQR	succinylation	[10]
300	ETGVDLTKDNMALQR	ubiquitination	[4]
314	RVREAAEKAKCELSS	acetylation	[8]
345	GPKHLNMKLTRAQFE	acetylation	[3, 8, 10]
345	GPKHLNMKLTRAQFE	succinylation	[10]
360	GIVTDLIKRTIAPCQ	acetylation	[1, 2, 3, 5, 6, 7, 8, 10, 11, 12]
360	GIVTDLIKRTIAPCQ	succinylation	[10]
360	GIVTDLIKRTIAPCQ	ubiquitination	[4]
368	RTIAPCQKAMQDAEV	acetylation	[10]
368	RTIAPCQKAMQDAEV	succinylation	[10]
377	MQDAEVSKSDIGEVI	acetylation	[3, 8, 11]
394	GGMTRMPKVQQTVQD	acetylation	[2, 7, 10, 11]
394	GGMTRMPKVQQTVQD	succinylation	[10]
467	RNTTIPTKKSQVFST	acetylation	[1]
468	NTTIPTKKSQVFSTA	acetylation	[10]
468	NTTIPTKKSQVFSTA	succinylation	[10]
468	NTTIPTKKSQVFSTA	ubiquitination	[4]
555	QSSGGLSKDDIENMV	acetylation	[3, 11]
563	DDIENMVKNAEKYAE	acetylation	[1]
567	NMVKNAEKYAEEDRR	acetylation	[1, 2, 3, 5, 6, 8, 10]
567	NMVKNAEKYAEEDRR	succinylation	[10]
600	ETKMEEFKDQLPADE	acetylation	[1, 2, 3, 7, 8, 9, 10]
600	ETKMEEFKDQLPADE	succinylation	[10]
610	LPADECNKLKEEISK	acetylation	[3, 8, 10]
610	LPADECNKLKEEISK	succinylation	[10]
612	ADECNKLKEEISKMR	acetylation	[1, 2, 3, 5, 8]
617	KLKEEISKMRALLAG	acetylation	[3, 8]
625	MRALLAGKDSETGEN	acetylation	[3, 8, 11]
625	MRALLAGKDSETGEN	ubiquitination	[4]
646	SLQQASLKLFEMAYK	acetylation	[1, 2, 3, 10]
646	SLQQASLKLFEMAYK	succinylation	[10]
653	KLFEMAYKKMASERE	acetylation	[1, 2, 8]
671	SSGTGEQKEDQKEEK	acetylation	[1, 8]
675	GEQKEDQKEEKQ***	acetylation	[1, 8]
678	KEDQKEEKQ******	acetylation	[1]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [7] 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]
 [8] 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]
 [9] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [10] 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]
 [11] 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]
 [12] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647] 

Functional Description

 Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. 

Sequence Annotation

 MOD_RES 135 135 N6-acetyllysine (By similarity).
 MOD_RES 138 138 N6-acetyllysine (By similarity).
 MOD_RES 143 143 N6-acetyllysine (By similarity).
 MOD_RES 206 206 N6-malonyllysine (By similarity).
 MOD_RES 234 234 N6-acetyllysine (By similarity).
 MOD_RES 288 288 N6-acetyllysine.
 MOD_RES 300 300 N6-acetyllysine.
 MOD_RES 360 360 N6-acetyllysine.
 MOD_RES 567 567 N6-acetyllysine (By similarity).
 MOD_RES 646 646 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; ATP-binding; Chaperone; Complete proteome; Direct protein sequencing; Mitochondrion; Nucleotide-binding; Nucleus; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 679 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006611; P:protein export from nucleus; IDA:MGI.
 GO:0006457; P:protein folding; IEA:InterPro. 

Interpro

 IPR012725; Chaperone_DnaK.
 IPR018181; Heat_shock_70_CS.
 IPR013126; Hsp_70_fam. 

Pfam

 PF00012; HSP70 

SMART

  

PROSITE

 PS00297; HSP70_1
 PS00329; HSP70_2
 PS01036; HSP70_3 

PRINTS

 PR00301; HEATSHOCK70.