UniProt Accession

 CH60_MOUSE; P63038; P19226; P19227; P97602; Q3KQP2; Q3UIP0; Q8C2C7; Q8VEF4 

Genbank Protein ID

 X55023; AK088844; AK143882; AK146831; BC016400; BC018545; BC106112; X53584 

Genbank Nucleotide ID

 CAA38762.1; BAC40607.1; BAE25581.1; BAE27466.1; AAH16400.1; AAH18545.1; AAI06113.1; CAA37653.1 

Protein Name

 60 kDa heat shock protein, mitochondrial 

Protein Synonyms/Alias

 60 kDa chaperonin; Chaperonin 60; CPN60; HSP-65; Heat shock protein 60; HSP-60; Hsp60; Mitochondrial matrix protein P1 

Gene Name

 Hspd1 

Gene Synonyms/Alias

 Hsp60 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
31	RAYAKDVKFGADARA	acetylation	[1]
31	RAYAKDVKFGADARA	ubiquitination	[2]
58	VAVTMGPKGRTVIIE	ubiquitination	[2]
72	EQSWGSPKVTKDGVT	ubiquitination	[2]
75	WGSPKVTKDGVTVAK	acetylation	[1]
75	WGSPKVTKDGVTVAK	ubiquitination	[2]
82	KDGVTVAKSIDLKDK	acetylation	[1]
82	KDGVTVAKSIDLKDK	ubiquitination	[2]
87	VAKSIDLKDKYKNIG	acetylation	[1]
89	KSIDLKDKYKNIGAK	acetylation	[1]
91	IDLKDKYKNIGAKLV	acetylation	[1]
96	KYKNIGAKLVQDVAN	ubiquitination	[2]
125	VLARSIAKEGFEKIS	acetylation	[1]
125	VLARSIAKEGFEKIS	ubiquitination	[2]
130	IAKEGFEKISKGANP	acetylation	[1]
133	EGFEKISKGANPVEI	acetylation	[1]
133	EGFEKISKGANPVEI	ubiquitination	[2]
156	DAVIAELKKQSKPVT	acetylation	[1]
191	NIISDAMKKVGRKGV	acetylation	[1]
191	NIISDAMKKVGRKGV	ubiquitination	[2]
202	RKGVITVKDGKTLND	acetylation	[1, 3, 4, 5, 6]
202	RKGVITVKDGKTLND	succinylation	[5]
205	VITVKDGKTLNDELE	acetylation	[1, 3, 4, 5, 6, 7]
205	VITVKDGKTLNDELE	succinylation	[5]
218	LEIIEGMKFDRGYIS	acetylation	[1, 4, 5, 6, 8]
218	LEIIEGMKFDRGYIS	succinylation	[5]
218	LEIIEGMKFDRGYIS	ubiquitination	[2]
233	PYFINTSKGQKCEFQ	acetylation	[1, 4, 5, 6]
233	PYFINTSKGQKCEFQ	succinylation	[5]
233	PYFINTSKGQKCEFQ	ubiquitination	[2]
236	INTSKGQKCEFQDAY	acetylation	[1, 3, 4, 5, 6, 9]
236	INTSKGQKCEFQDAY	succinylation	[5]
236	INTSKGQKCEFQDAY	ubiquitination	[2]
249	AYVLLSEKKISSVQS	acetylation	[1, 3, 4, 6, 7, 10]
250	YVLLSEKKISSVQSI	acetylation	[4, 5]
250	YVLLSEKKISSVQSI	succinylation	[5]
269	EIANAHRKPLVIIAE	acetylation	[4, 8]
292	TLVLNRLKVGLQVVA	acetylation	[4, 5]
292	TLVLNRLKVGLQVVA	succinylation	[5]
301	GLQVVAVKAPGFGDN	acetylation	[5]
301	GLQVVAVKAPGFGDN	succinylation	[5]
301	GLQVVAVKAPGFGDN	ubiquitination	[2]
314	DNRKNQLKDMAIATG	acetylation	[4, 6]
352	VGEVIVTKDDAMLLK	acetylation	[1, 3, 4, 5, 6, 8]
352	VGEVIVTKDDAMLLK	succinylation	[5]
352	VGEVIVTKDDAMLLK	ubiquitination	[2]
359	KDDAMLLKGKGDKAH	acetylation	[1, 3, 4, 5, 6, 7, 9]
359	KDDAMLLKGKGDKAH	succinylation	[5]
361	DAMLLKGKGDKAHIE	acetylation	[1]
364	LLKGKGDKAHIEKRI	acetylation	[1, 6]
369	GDKAHIEKRIQEITE	acetylation	[1, 6]
387	ITTSEYEKEKLNERL	acetylation	[6]
389	TSEYEKEKLNERLAK	acetylation	[3, 4, 8, 11]
396	KLNERLAKLSDGVAV	acetylation	[4, 5, 8, 9]
396	KLNERLAKLSDGVAV	succinylation	[5]
396	KLNERLAKLSDGVAV	ubiquitination	[2]
417	SDVEVNEKKDRVTDA	acetylation	[1, 6]
417	SDVEVNEKKDRVTDA	ubiquitination	[2]
418	DVEVNEKKDRVTDAL	acetylation	[8]
455	IPALDSLKPANEDQK	acetylation	[1, 3, 4, 5, 6, 8, 11]
455	IPALDSLKPANEDQK	succinylation	[5]
462	KPANEDQKIGIEIIK	acetylation	[3, 5, 6]
462	KPANEDQKIGIEIIK	succinylation	[5]
469	KIGIEIIKRALKIPA	acetylation	[1, 3, 4, 5, 6, 7, 8, 11]
469	KIGIEIIKRALKIPA	succinylation	[5]
473	EIIKRALKIPAMTIA	acetylation	[4, 5]
473	EIIKRALKIPAMTIA	succinylation	[5]
481	IPAMTIAKNAGVEGS	acetylation	[4, 5]
481	IPAMTIAKNAGVEGS	succinylation	[5]
481	IPAMTIAKNAGVEGS	ubiquitination	[2]
516	DFVNMVEKGIIDPTK	acetylation	[3]
523	KGIIDPTKVVRTALL	acetylation	[9]

Reference

 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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]
 [10] 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]
 [11] 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] 

Functional Description

 Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. 

Sequence Annotation

 MOD_RES 70 70 Phosphoserine (By similarity).
 MOD_RES 82 82 N6-acetyllysine (By similarity).
 MOD_RES 125 125 N6-acetyllysine (By similarity).
 MOD_RES 130 130 N6-acetyllysine (By similarity).
 MOD_RES 133 133 N6-malonyllysine (By similarity).
 MOD_RES 202 202 N6-acetyllysine (By similarity).
 MOD_RES 218 218 N6-acetyllysine (By similarity).
 MOD_RES 223 223 Phosphotyrosine.
 MOD_RES 269 269 N6-acetyllysine (By similarity).
 MOD_RES 352 352 N6-acetyllysine (By similarity).
 MOD_RES 359 359 N6-acetyllysine (By similarity).
 MOD_RES 396 396 N6-acetyllysine (By similarity).
 MOD_RES 469 469 N6-acetyllysine (By similarity).  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 573 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005905; C:coated pit; IEA:Compara.
 GO:0030135; C:coated vesicle; IEA:Compara.
 GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IEA:Compara.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005769; C:early endosome; IEA:Compara.
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0046696; C:lipopolysaccharide receptor complex; IEA:Compara.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:MGI.
 GO:0030141; C:secretory granule; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
 GO:0002368; P:B cell cytokine production; IEA:Compara.
 GO:0042100; P:B cell proliferation; IEA:Compara.
 GO:0048291; P:isotype switching to IgG isotypes; IEA:Compara.
 GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
 GO:0032727; P:positive regulation of interferon-alpha production; IDA:MGI.
 GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
 GO:0032733; P:positive regulation of interleukin-10 production; IEA:Compara.
 GO:0032735; P:positive regulation of interleukin-12 production; IEA:Compara.
 GO:0032755; P:positive regulation of interleukin-6 production; IEA:Compara.
 GO:0043032; P:positive regulation of macrophage activation; IEA:Compara.
 GO:0050870; P:positive regulation of T cell activation; IDA:BHF-UCL.
 GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IEA:Compara.
 GO:0042026; P:protein refolding; IEA:Compara.
 GO:0006986; P:response to unfolded protein; IEA:Compara.
 GO:0042110; P:T cell activation; IDA:MGI. 

Interpro

 IPR018370; Chaperonin_Cpn60_CS.
 IPR001844; Chaprnin_Cpn60.
 IPR002423; Cpn60/TCP-1.
 IPR027409; GroEL-like_apical_dom.
 IPR027413; GROEL-like_equatorial. 

Pfam

 PF00118; Cpn60_TCP1 

SMART

  

PROSITE

 PS00296; CHAPERONINS_CPN60 

PRINTS

 PR00298; CHAPERONIN60.