CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024154
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial 
Protein Synonyms/Alias
 ATP-specific succinyl-CoA synthetase subunit beta; Succinyl-CoA synthetase beta-A chain; SCS-betaA 
Gene Name
 Sucla2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
78VPKGFVAKSSDEAYAacetylation[1, 2, 3]
78VPKGFVAKSSDEAYAubiquitination[4]
88DEAYAIAKKLGSKDVacetylation[1, 2, 3, 5, 6, 7, 8, 9]
88DEAYAIAKKLGSKDVsuccinylation[9]
88DEAYAIAKKLGSKDVubiquitination[4]
93IAKKLGSKDVVIKAQacetylation[1, 2, 9]
93IAKKLGSKDVVIKAQsuccinylation[9]
108VLAGGRGKGTFTSGLacetylation[9]
108VLAGGRGKGTFTSGLsuccinylation[9]
120SGLKGGVKIVFSPEEacetylation[1, 2, 3]
129VFSPEEAKAVSSQMIacetylation[1, 2, 3, 6]
139SSQMIGQKLITKQTGacetylation[1, 2, 3]
139SSQMIGQKLITKQTGubiquitination[4]
143IGQKLITKQTGEKGRacetylation[2]
216DIVEGIKKEQAVTLAacetylation[2]
267MVEDSDGKVLCMDAKacetylation[3]
368FKLITSDKKVQAILVacetylation[1, 2, 3]
417GTRVDDAKALIADSGacetylation[3]
417GTRVDDAKALIADSGubiquitination[4]
426LIADSGLKILACDDLacetylation[3]
438DDLDEAAKMVVKLSEacetylation[1, 2, 3, 6]
451SEIVTLAKEAHVDVKacetylation[1]
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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
 Catalyzes the ATP-dependent ligation of succinate and CoA to form succinyl-CoA (By similarity). 
Sequence Annotation
 DOMAIN 61 288 ATP-grasp.
 MOD_RES 78 78 N6-acetyllysine (By similarity).
 MOD_RES 84 84 Phosphotyrosine (By similarity).
 MOD_RES 143 143 N6-acetyllysine (By similarity).
 MOD_RES 279 279 Phosphoserine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 463 AA 
Protein Sequence
MAASMFYGRQ LAAAALRSHR PQTTLRAAAQ VLGNSGLFNK HGLQVQQQQQ RTLSLHEYLS 60
MELLQEAGVS VPKGFVAKSS DEAYAIAKKL GSKDVVIKAQ VLAGGRGKGT FTSGLKGGVK 120
IVFSPEEAKA VSSQMIGQKL ITKQTGEKGR ICNQVLVCER KYPRREYYFA ITMERSFQGP 180
VLIGSAQGGV NIEDVAAENP EAIVKEPIDI VEGIKKEQAV TLAQKMGFPS NIVDSAAENM 240
IKLYNLFLKY DATMVEINPM VEDSDGKVLC MDAKINFDSN SAYRQKKIFD LQDWSQEDER 300
DKEAANADIN YIGLDGSIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG GATVQQVTEA 360
FKLITSDKKV QAILVNIFGG IMRCDVIAQG IVMAVKDLEI RIPVVVRLQG TRVDDAKALI 420
ADSGLKILAC DDLDEAAKMV VKLSEIVTLA KEAHVDVKFQ LPI 463 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:EC.
 GO:0004774; F:succinate-CoA ligase activity; ISS:MGI.
 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
 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. 
Pfam
 PF08442; ATP-grasp_2
 PF00549; Ligase_CoA 
SMART
  
PROSITE
 PS50975; ATP_GRASP
 PS01217; SUCCINYL_COA_LIG_3 
PRINTS