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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Peroxisomal acyl-coenzyme A oxidase 1

UniprotKB/SwissProt ID: Q15067 (Q15067)

Gene Name: ACOX1

Organism: Homo sapiens (Human)

Function: Involved in the initial and rate-limiting step of peroxisomal beta-oxidation of straight-chain saturated and unsaturated very-long-chain fatty acids (PubMed:15060085, PubMed:17458872, PubMed:17603022, PubMed:32169171, PubMed:33234382, PubMed:7876265). Catalyzes the desaturation of fatty acyl-CoAs such as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-CoAs) such as (2E)-hexadecenoyl-CoA, and donates electrons directly to molecular oxygen (O(2)), thereby producing hydrogen peroxide (H(2)O(2)) (PubMed:17458872, PubMed:17603022, PubMed:7876265) Shows highest activity against medium-chain fatty acyl-CoAs. Shows optimum activity with a chain length of 10 carbons (decanoyl-CoA) in vitro Is active against a much broader range of substrates and shows activity towards long-chain fatty acyl-CoAs

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Peroxisome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR034171 ACO
IPR055060 ACOX_C_alpha1
IPR029320 Acyl-CoA_ox_N
IPR006091 Acyl-CoA_Oxase/DH_mid-dom
IPR046373 Acyl-CoA_Oxase/DH_mid-dom_sf
IPR012258 Acyl-CoA_oxidase
IPR002655 Acyl-CoA_oxidase_C
IPR036250 AcylCo_DH-like_C
IPR037069 AcylCoA_DH/ox_N_sf
IPR009100 AcylCoA_DH/oxidase_NM_dom_sf

The S-nitrosylation sites of Q15067

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 199 VLAQLITKGK C YGLHAFIVPI   
2 449 YDQVHSGKLV C GMVSYLNDLP