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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: Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

UniprotKB/SwissProt ID: P11310 (P11310)

Gene Name: ACADM

Organism: Homo sapiens (Human)

Function: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:1970566, PubMed:21237683, PubMed:2251268, PubMed:8823175). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (PubMed:2251268). Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:15159392, PubMed:25416781). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains (PubMed:1970566, PubMed:21237683, PubMed:2251268, PubMed:8823175)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion matrix

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR050741 Acyl-CoA_dehydrogenase
IPR006089 Acyl-CoA_DH_CS
IPR006091 Acyl-CoA_Oxase/DH_mid-dom
IPR046373 Acyl-CoA_Oxase/DH_mid-dom_sf
IPR036250 AcylCo_DH-like_C
IPR009075 AcylCo_DH/oxidase_C
IPR013786 AcylCoA_DH/ox_N
IPR037069 AcylCoA_DH/ox_N_sf
IPR009100 AcylCoA_DH/oxidase_NM_dom_sf
IPR034180 MCAD

The S-nitrosylation sites of P11310

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 156 LGRMTEEPLM C AYCVTEPGAG   
2 159 MTEEPLMCAY C VTEPGAGSDV