CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013289
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acyl-CoA synthetase family member 3, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 ACSF3 
Gene Synonyms/Alias
 PSEC0197 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
162LLSPVVRKLGVPLLPubiquitination[1]
324LRAVCEEKIRLMVSGubiquitination[1]
342LPLPVLEKWKNITGHubiquitination[1]
344LPVLEKWKNITGHTLubiquitination[1]
413EGDERGTKVTPGFEEubiquitination[1]
421VTPGFEEKEGELLVRubiquitination[1]
439VFREYWNKPEETKSAacetylation[2]
439VFREYWNKPEETKSAubiquitination[1]
444WNKPEETKSAFTLDGubiquitination[1]
462TGDTVVFKDGQYWIRubiquitination[1]
478RTSVDIIKTGGYKVSubiquitination[1]
534SLSHRELKEWARNVLubiquitination[1]
566NQMGKIDKKALIRHFubiquitination[1]
567QMGKIDKKALIRHFHubiquitination[1]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates. 
Sequence Annotation
 NP_BIND 202 210 ATP (By similarity).
 BINDING 457 457 ATP (By similarity).
 BINDING 471 471 ATP (By similarity).
 BINDING 563 563 ATP (By similarity).  
Keyword
 ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Mitochondrion; Nucleotide-binding; Polymorphism; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 576 AA 
Protein Sequence
MLPHVVLTFR RLGCALASCR LAPARHRGSG LLHTAPVARS DRSAPVFTRA LAFGDRIALV 60
DQHGRHTYRE LYSRSLRLSQ EICRLCGCVG GDLREERVSF LCANDASYVV AQWASWMSGG 120
VAVPLYRKHP AAQLEYVICD SQSSVVLASQ EYLELLSPVV RKLGVPLLPL TPAIYTGAVE 180
EPAEVPVPEQ GWRNKGAMII YTSGTTGRPK GVLSTHQNIR AVVTGLVHKW AWTKDDVILH 240
VLPLHHVHGV VNALLCPLWV GATCVMMPEF SPQQVWEKFL SSETPRINVF MAVPTIYTKL 300
MEYYDRHFTQ PHAQDFLRAV CEEKIRLMVS GSAALPLPVL EKWKNITGHT LLERYGMTEI 360
GMALSGPLTT AVRLPGSVGT PLPGVQVRIV SENPQREACS YTIHAEGDER GTKVTPGFEE 420
KEGELLVRGP SVFREYWNKP EETKSAFTLD GWFKTGDTVV FKDGQYWIRG RTSVDIIKTG 480
GYKVSALEVE WHLLAHPSIT DVAVIGVPDM TWGQRVTAVV TLREGHSLSH RELKEWARNV 540
LAPYAVPSEL VLVEEIPRNQ MGKIDKKALI RHFHPS 576 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0090409; F:malonyl-CoA synthetase activity; IDA:UniProtKB.
 GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
 GO:0090410; P:malonate catabolic process; IDA:UniProtKB. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS