CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019337
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 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 
Gene Name
 SUCLG2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73NEALEAAKRLNAKEIacetylation[1]
118NVVGQLAKQMIGYNLubiquitination[2, 3]
227QAADQITKLYNLFLKacetylation[1]
291PIENEAAKYDLKYIGacetylation[1, 4]
338LDLGGGVKEAQVYQAacetylation[1, 4]
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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA (By similarity). 
Sequence Annotation
 DOMAIN 46 274 ATP-grasp.
 MOD_RES 227 227 N6-acetyllysine.
 MOD_RES 291 291 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; GTP-binding; Ligase; Mitochondrion; Nucleotide-binding; Polymorphism; Reference proteome; Transit peptide; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 432 AA 
Protein Sequence
MASPVAAQAG KLLRALALRP RFLAAGSQAV QLTSRRWLNL QEYQSKKLMS DNGVRVQRFF 60
VADTANEALE AAKRLNAKEI VLKAQILAGG RGKGVFNSGL KGGVHLTKDP NVVGQLAKQM 120
IGYNLATKQT PKEGVKVNKV MVAEALDISR ETYLAILMDR SCNGPVLVGS PQGGVDIEEV 180
AASNPELIFK EQIDIFEGIK DSQAQRMAEN LGFVGPLKSQ AADQITKLYN LFLKIDATQV 240
EVNPFGETPE GQVVCFDAKI NFDDNAEFRQ KDIFAMDDKS ENEPIENEAA KYDLKYIGLD 300
GNIACFVNGA GLAMATCDII FLNGGKPANF LDLGGGVKEA QVYQAFKLLT ADPKVEAILV 360
NIFGGIVNCA IIANGITKAC RELELKVPLV VRLEGTNVQE AQKILNNSGL PITSAIDLED 420
AAKKAVASVA KK 432 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; NAS:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006104; P:succinyl-CoA metabolic process; NAS:UniProtKB.
 GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome. 
Interpro
 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