CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022581
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; Renal carcinoma antigen NY-REN-39; Succinyl-CoA synthetase beta-A chain; SCS-betaA 
Gene Name
 SUCLA2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78VPKGYVAKSPDEAYAacetylation[1]
78VPKGYVAKSPDEAYAubiquitination[2]
89EAYAIAKKLGSKDVVubiquitination[3]
143IGKKLFTKQTGEKGRacetylation[1]
143IGKKLFTKQTGEKGRubiquitination[3]
417GTRVDDAKALIADSGubiquitination[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
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.
 MOD_RES 84 84 Phosphotyrosine.
 MOD_RES 143 143 N6-acetyllysine.
 MOD_RES 279 279 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Disease mutation; Ligase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transit peptide; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 463 AA 
Protein Sequence
MAASMFYGRL VAVATLRNHR PRTAQRAAAQ VLGSSGLFNN HGLQVQQQQQ RNLSLHEYMS 60
MELLQEAGVS VPKGYVAKSP DEAYAIAKKL GSKDVVIKAQ VLAGGRGKGT FESGLKGGVK 120
IVFSPEEAKA VSSQMIGKKL FTKQTGEKGR ICNQVLVCER KYPRREYYFA ITMERSFQGP 180
VLIGSSHGGV NIEDVAAESP EAIIKEPIDI EEGIKKEQAL QLAQKMGFPP NIVESAAENM 240
VKLYSLFLKY DATMIEINPM VEDSDGAVLC MDAKINFDSN SAYRQKKIFD LQDWTQEDER 300
DKDAAKANLN YIGLDGNIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG GATVHQVTEA 360
FKLITSDKKV LAILVNIFGG IMRCDVIAQG IVMAVKDLEI KIPVVVRLQG TRVDDAKALI 420
ADSGLKILAC DDLDEAARMV VKLSEIVTLA KQAHVDVKFQ LPI 463 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 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; TAS:UniProtKB.
 GO:0006105; P:succinate metabolic process; IEA:Compara.
 GO:0006781; P:succinyl-CoA pathway; NAS:UniProtKB.
 GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome. 
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