CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023524
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial 
Protein Synonyms/Alias
 Succinyl-CoA synthetase subunit alpha; SCS-alpha 
Gene Name
 Suclg1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
48GSYTASRKHIYIDKNacetylation[1]
54RKHIYIDKNTKIICQacetylation[1, 2, 3, 4, 5]
57IYIDKNTKIICQGFTacetylation[1, 2, 3, 5, 6]
57IYIDKNTKIICQGFTsuccinylation[6]
57IYIDKNTKIICQGFTubiquitination[7]
66ICQGFTGKQGTFHSQacetylation[1, 2, 3, 6]
66ICQGFTGKQGTFHSQsuccinylation[6]
66ICQGFTGKQGTFHSQubiquitination[7]
81QALEYGTKLVGGTTPacetylation[1, 3, 5]
90VGGTTPGKGGQKHLGubiquitination[7]
94TPGKGGQKHLGLPVFacetylation[1, 2, 3, 5, 6]
94TPGKGGQKHLGLPVFsuccinylation[6]
94TPGKGGQKHLGLPVFubiquitination[7]
105LPVFNTVKEAKEKTGacetylation[1, 2, 3, 5]
192IMPGHIHKKGRIGIVacetylation[1, 3, 5]
280HNSGPKAKPVVSFIAubiquitination[7, 8]
338QLGTTIYKEFEKRKMacetylation[6]
338QLGTTIYKEFEKRKMsuccinylation[6]
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 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] A proteomics approach to identify the ubiquitinated proteins in mouse heart.
 Jeon HB, Choi ES, Yoon JH, Hwang JH, Chang JW, Lee EK, Choi HW, Park ZY, Yoo YJ.
 Biochem Biophys Res Commun. 2007 Jun 8;357(3):731-6. [PMID: 17451654] 
Functional Description
 Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity). 
Sequence Annotation
 ACT_SITE 299 299 Tele-phosphohistidine intermediate (By
 MOD_RES 54 54 N6-acetyllysine (By similarity).
 CROSSLNK 280 280 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; GTP-binding; Isopeptide bond; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide; Tricarboxylic acid cycle; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 346 AA 
Protein Sequence
MTATVVAAAA TATMVSSSSG LAAARLLSRT FLLQQNGIRH GSYTASRKHI YIDKNTKIIC 60
QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGQKHLGLPV FNTVKEAKEK TGATASVIYV 120
PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ DMVRVKHRLT RQGTTRLIGP NCPGVINPGE 180
CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTDFIDCL 240
EVFLNDPATE GIILIGEIGG HAEENAAAFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA 300
GAIIAGGKGG AKEKISALQS AGVVVSMSPA QLGTTIYKEF EKRKML 346 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0045244; C:succinate-CoA ligase complex (GDP-forming); IEA:Compara.
 GO:0003878; F:ATP citrate synthase activity; IEA:InterPro.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0019003; F:GDP binding; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:EC.
 GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:EC.
 GO:0006105; P:succinate metabolic process; IEA:Compara.
 GO:0006104; P:succinyl-CoA metabolic process; IEA:Compara.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 
Interpro
 IPR017440; Cit_synth/succinyl-CoA_lig_AS.
 IPR003781; CoA-bd.
 IPR005810; CoA_lig_alpha.
 IPR005811; CoA_ligase.
 IPR016040; NAD(P)-bd_dom.
 IPR016102; Succinyl-CoA_synth-like. 
Pfam
 PF02629; CoA_binding
 PF00549; Ligase_CoA 
SMART
 SM00881; CoA_binding 
PROSITE
 PS01216; SUCCINYL_COA_LIG_1
 PS00399; SUCCINYL_COA_LIG_2 
PRINTS
 PR01798; SCOASYNTHASE.