CPLM-024153

Genbank Nucleotide ID

Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial

Protein Synonyms/Alias

GTP-specific succinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase beta-G chain; SCS-betaG

Mus musculus (Mouse)

Position	Peptide	Type	References
67	FFVANTAKEALEAAK	acetylation	[1, 2, 3, 4, 5]
67	FFVANTAKEALEAAK	succinylation	[4]
67	FFVANTAKEALEAAK	ubiquitination	[6]
74	KEALEAAKRLNAKEI	acetylation	[2, 3, 5]
79	AAKRLNAKEIVLKAQ	acetylation	[2, 3, 4]
79	AAKRLNAKEIVLKAQ	succinylation	[4]
84	NAKEIVLKAQILAGG	acetylation	[3]
94	ILAGGRGKGVFNSGL	acetylation	[4]
94	ILAGGRGKGVFNSGL	succinylation	[4]
94	ILAGGRGKGVFNSGL	ubiquitination	[6]
102	GVFNSGLKGGVHLTK	ubiquitination	[6]
109	KGGVHLTKDPKVVGE	acetylation	[2, 5, 7]
112	VHLTKDPKVVGELAQ	acetylation	[1, 2, 3, 5]
129	IGYNLATKQTPKEGV	ubiquitination	[6]
133	LATKQTPKEGVKVNK	acetylation	[2, 3, 5]
140	KEGVKVNKVMVAEAL	acetylation	[3, 5]
201	IDIFEGIKDSQAQRM	acetylation	[2, 3, 5]
201	IDIFEGIKDSQAQRM	ubiquitination	[6]
219	LGFLGSLKNQAADQI	acetylation	[3, 5]
219	LGFLGSLKNQAADQI	ubiquitination	[6]
228	QAADQITKLYHLFLK	acetylation	[1, 2, 3, 5]
272	DNAEFRQKDIFAMDD	acetylation	[1, 2, 3, 5, 8]
280	DIFAMDDKSENEPIE	acetylation	[2, 3, 5]
339	LDLGGGVKEAQVYEA	acetylation	[1, 3, 4]
339	LDLGGGVKEAQVYEA	succinylation	[4]
348	AQVYEAFKLLTSDPK	acetylation	[2, 3, 5]
387	ACRELELKVPLVVRL	acetylation	[3, 5]
387	ACRELELKVPLVVRL	ubiquitination	[6]
407	QEAQNILKSSGLPIT	acetylation	[3]
424	VDLEDAAKKAVASVA	acetylation	[1, 2, 3, 5]
432	KAVASVAKK******	acetylation	[2, 3]

[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] 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]
[3] 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]
[4] 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]
[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]
[6] 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]
[7] 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]
[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]

Functional Description

Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA (By similarity).

DOMAIN 47 275 ATP-grasp.
MOD_RES 228 228 N6-acetyllysine (By similarity).

Acetylation; Alternative splicing; Complete proteome; GTP-binding; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide; Tricarboxylic acid cycle.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005739; C:mitochondrion; IDA:MGI.
GO:0005524; F:ATP binding; IEA:InterPro.
GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO:0046872; F:metal ion binding; IEA:InterPro.
GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:EC.
GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; ISA:MGI.
GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.

IPR011761; ATP-grasp.
IPR013650; ATP-grasp_succ-CoA_synth-type.
IPR013815; ATP_grasp_subdomain_1.
IPR013816; ATP_grasp_subdomain_2.
IPR005811; CoA_ligase.
IPR017866; Succ-CoA_synthase_bsu_CS.
IPR005809; Succ_CoA_synthase_bsu.
IPR016102; Succinyl-CoA_synth-like.

PF08442; ATP-grasp_2
PF00549; Ligase_CoA

PS50975; ATP_GRASP
PS01217; SUCCINYL_COA_LIG_3