CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022612
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxisomal acyl-coenzyme A oxidase 2 
Protein Synonyms/Alias
 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase; 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase; Trihydroxycoprostanoyl-CoA oxidase; THCA-CoA oxidase; THCCox 
Gene Name
 Acox2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
66RDPVFNLKHLYFMTRacetylation[1]
66RDPVFNLKHLYFMTRubiquitination[2]
137GSDEQIAKWGQLGKNubiquitination[2]
244TVGDIGPKMGFENIDubiquitination[2]
303TRVQLLYKGFLPTLQacetylation[3]
303TRVQLLYKGFLPTLQsuccinylation[3]
303TRVQLLYKGFLPTLQubiquitination[2]
453QVARFLMKSYLQAQVacetylation[3]
453QVARFLMKSYLQAQVsuccinylation[3]
556FLTVRNFKEAVEKLDacetylation[3]
556FLTVRNFKEAVEKLDsuccinylation[3]
556FLTVRNFKEAVEKLDubiquitination[2]
561NFKEAVEKLDNEPEIacetylation[3]
561NFKEAVEKLDNEPEIsuccinylation[3]
655RLFEWAQKSPANTQEacetylation[1, 4]
667TQENPAYKKYIRPLMacetylation[3, 5]
667TQENPAYKKYIRPLMsuccinylation[3]
678RPLMQSWKPKL****acetylation[1]
680LMQSWKPKL******acetylation[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] 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]
 [3] 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]
 [4] 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]
 [5] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647
Functional Description
 Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycoprostanic acids (By similarity). 
Sequence Annotation
 MOTIF 679 681 Microbody targeting signal (Potential).
 MOD_RES 667 667 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 681 AA 
Protein Sequence
MGNPGDRVSL GETWSREVHP DIDSERHSPS FSVERLTNIL DGGIPNTELR RRVESLIQRD 60
PVFNLKHLYF MTRDELYEDA VQKRFHLEKL AWSLGWSEDG PERIYADRVL AGYNNLNLHG 120
IAMNAIRSLG SDEQIAKWGQ LGKNFQIITT YAQTELGHGT YLQGLETEAT YDATTQEFVI 180
HSPTMTSIKW WPGDLGRTVT HAVVLAHLIC LGARHGMHAF IVPIRSLEDH TPLPGITVGD 240
IGPKMGFENI DNGFLRLNHV RVPRENMLSR FAEVLPDGTY QRLGTPQSNY LGMLVTRVQL 300
LYKGFLPTLQ KACTIAVRYA VIRHQSRLRP SDPEAKILEY QTQQQKLLPQ LAVSYALHFM 360
TTSLLQFFHS SYSDILKRDF SLLPELHALS TGMKAMSSDF CAQGTEICRR ACGGHGYSKL 420
SGLPTLVTQA IASCTYEGEN TVLYLQVARF LMKSYLQAQV SPGSIPQKPL PQSVMYLATP 480
RPARCPAQTA ADFRCPEVYT TAWAYVSARL IRDATQHTQT LMRSGVDQYD AWNQTSVIHL 540
QAAKAHCYFL TVRNFKEAVE KLDNEPEIQR VLQNLCDLYA LNGILTNSGD FLHDGFLSGA 600
QVDMARTAFL DLLPLIRKDA ILLTDAFDFS DHCLNSALGC YDGHVYQRLF EWAQKSPANT 660
QENPAYKKYI RPLMQSWKPK L 681 
Gene Ontology
 GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
 GO:0033791; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity; IEA:EC.
 GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
 GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro. 
Interpro
 IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
 IPR012258; Acyl-CoA_oxidase.
 IPR002655; Acyl-CoA_oxidase_C.
 IPR009075; AcylCo_DH/oxidase_C.
 IPR013786; AcylCoA_DH/ox_N.
 IPR009100; AcylCoA_DH/oxidase. 
Pfam
 PF01756; ACOX 
SMART
  
PROSITE
  
PRINTS