CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012488
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxisomal acyl-coenzyme A oxidase 1 
Protein Synonyms/Alias
 AOX; Palmitoyl-CoA oxidase; Straight-chain acyl-CoA oxidase; SCOX 
Gene Name
 ACOX1 
Gene Synonyms/Alias
 ACOX 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29ILDGSPEKTRRRREIubiquitination[1]
122GTTAQKEKWLLSSKGubiquitination[1]
198AQLITKGKCYGLHAFacetylation[2]
216IREIGTHKPLPGITVacetylation[3]
216IREIGTHKPLPGITVubiquitination[1, 2]
255PRENMLMKYAQVKPDacetylation[3, 4, 5]
267KPDGTYVKPLSNKLTacetylation[2, 3, 4, 5]
295EAARALSKACTIAIRubiquitination[1, 2]
437QTARFLMKSYDQVHSacetylation[2, 3, 4, 5]
500RLVEIAAKNLQKEVIacetylation[3, 4, 5]
504IAAKNLQKEVIHRKSacetylation[2, 3, 4]
651AEVHESYKHLKSLQSacetylation[4]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] 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]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
 Catalyzes the desaturation of acyl-CoAs to 2-trans- enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy- palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl- CoA. 
Sequence Annotation
 MOTIF 658 660 Microbody targeting signal.
 ACT_SITE 421 421 Proton acceptor (By similarity).
 BINDING 139 139 FAD (By similarity).
 BINDING 178 178 FAD; via amide nitrogen (By similarity).
 MOD_RES 26 26 Phosphoserine.
 MOD_RES 255 255 N6-acetyllysine.
 MOD_RES 267 267 N6-acetyllysine.
 MOD_RES 310 310 Phosphoserine (By similarity).
 MOD_RES 437 437 N6-acetyllysine.
 MOD_RES 500 500 N6-acetyllysine.
 MOD_RES 504 504 N6-acetyllysine.
 MOD_RES 643 643 N6-acetyllysine (By similarity).
 MOD_RES 649 649 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Disease mutation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 660 AA 
Protein Sequence
MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED LNFLTRSQRY 60
EVAVRKSAIM VKKMREFGIA DPDEIMWFKK LHLVNFVEPV GLNYSMFIPT LLNQGTTAQK 120
EKWLLSSKGL QIIGTYAQTE MGHGTHLRGL ETTATYDPET QEFILNSPTV TSIKWWPGGL 180
GKTSNHAIVL AQLITKGKCY GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYDEIDNGYL 240
KMDNHRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGEAA RALSKACTIA 300
IRYSAVRHQS EIKPGEPEPQ ILDFQTQQYK LFPLLATAYA FQFVGAYMKE TYHRINEGIG 360
QGDLSELPEL HALTAGLKAF TSWTANTGIE ACRMACGGHG YSHCSGLPNI YVNFTPSCTF 420
EGENTVMMLQ TARFLMKSYD QVHSGKLVCG MVSYLNDLPS QRIQPQQVAV WPTMVDINSP 480
ESLTEAYKLR AARLVEIAAK NLQKEVIHRK SKEVAWNLTS VDLVRASEAH CHYVVVKLFS 540
EKLLKIQDKA IQAVLRSLCL LYSLYGISQN AGDFLQGSIM TEPQITQVNQ RVKELLTLIR 600
SDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKNSP LNKAEVHESY KHLKSLQSKL 660 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005782; C:peroxisomal matrix; TAS:Reactome.
 GO:0005778; C:peroxisomal membrane; IEA:Compara.
 GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
 GO:0003997; F:acyl-CoA oxidase activity; IDA:UniProtKB.
 GO:0071949; F:FAD binding; IDA:UniProtKB.
 GO:0005504; F:fatty acid binding; IEA:Compara.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0016401; F:palmitoyl-CoA oxidase activity; IDA:UniProtKB.
 GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
 GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IMP:BHF-UCL.
 GO:0019395; P:fatty acid oxidation; IGI:UniProtKB.
 GO:0006091; P:generation of precursor metabolites and energy; IMP:UniProtKB.
 GO:0055088; P:lipid homeostasis; IDA:UniProtKB.
 GO:0016559; P:peroxisome fission; IGI:UniProtKB.
 GO:2000189; P:positive regulation of cholesterol homeostasis; IGI:UniProtKB.
 GO:0006693; P:prostaglandin metabolic process; IMP:UniProtKB.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0000038; P:very long-chain fatty acid metabolic process; IMP:BHF-UCL. 
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
 PF02770; Acyl-CoA_dh_M 
SMART
  
PROSITE
  
PRINTS