CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021494
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acyl-CoA dehydrogenase family member 9, mitochondrial 
Protein Synonyms/Alias
 ACAD-9 
Gene Name
 ACAD9 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41PPVRAFAKELFLGKIacetylation[1]
599ENLDEQIKKVSQQILubiquitination[2]
608VSQQILEKRAYICAHacetylation[1]
608VSQQILEKRAYICAHubiquitination[2, 3]
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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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
 Has a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA than on stearoyl-CoA. Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0). 
Sequence Annotation
 ACT_SITE 426 426 Proton acceptor (By similarity).
 MOD_RES 41 41 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Polymorphism; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 621 AA 
Protein Sequence
MSGCGLFLRT TAAARACRGL VVSTANRRLL RTSPPVRAFA KELFLGKIKK KEVFPFPEVS 60
QDELNEINQF LGPVEKFFTE EVDSRKIDQE GKIPDETLEK LKSLGLFGLQ VPEEYGGLGF 120
SNTMYSRLGE IISMDGSITV TLAAHQAIGL KGIILAGTEE QKAKYLPKLA SGEHIAAFCL 180
TEPASGSDAA SIRSRATLSE DKKHYILNGS KVWITNGGLA NIFTVFAKTE VVDSDGSVKD 240
KITAFIVERD FGGVTNGKPE DKLGIRGSNT CEVHFENTKI PVENILGEVG DGFKVAMNIL 300
NSGRFSMGSV VAGLLKRLIE MTAEYACTRK QFNKRLSEFG LIQEKFALMA QKAYVMESMT 360
YLTAGMLDQP GFPDCSIEAA MVKVFSSEAA WQCVSEALQI LGGLGYTRDY PYERILRDTR 420
ILLIFEGTNE ILRMYIALTG LQHAGRILTT RIHELKQAKV STVMDTVGRR LRDSLGRTVD 480
LGLTGNHGVV HPSLADSANK FEENTYCFGR TVETLLLRFG KTIMEEQLVL KRVANILINL 540
YGMTAVLSRA SRSIRIGLRN HDHEVLLANT FCVEAYLQNL FSLSQLDKYA PENLDEQIKK 600
VSQQILEKRA YICAHPLDRT C 621 
Gene Ontology
 GO:0030425; C:dendrite; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IDA:LIFEdb.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. 
Interpro
 IPR006089; Acyl-CoA_DH_CS.
 IPR006092; Acyl-CoA_DH_N.
 IPR006090; Acyl-CoA_Oxase/DH_1.
 IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
 IPR009075; AcylCo_DH/oxidase_C.
 IPR013786; AcylCoA_DH/ox_N.
 IPR009100; AcylCoA_DH/oxidase. 
Pfam
 PF00441; Acyl-CoA_dh_1
 PF02770; Acyl-CoA_dh_M
 PF02771; Acyl-CoA_dh_N 
SMART
  
PROSITE
 PS00072; ACYL_COA_DH_1
 PS00073; ACYL_COA_DH_2 
PRINTS