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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: Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

UniprotKB/SwissProt ID: ODB2_MOUSE (P53395)

Gene Name: Dbt

Organism: Mus musculus (Mouse).

Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion matrix.

Network with metabolic pathway:
Kegg map ID Pathway Link
map00280"Valine, leucine and isoleucine degradation"
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR000089
IPR001078
IPR003016
IPR004167
IPR011053
IPR015761

The S-nitrosylation sites of ODB2_MOUSE

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1279AALKIPHFGY C DEIDLTQLVK HHCCCCEEEE E EECCHHHHHH 3.76%MC0121278135in vitro
2279AALKIPHFGY C DEIDLTQLVK HHCCCCEEEE E EECCHHHHHH 3.76%MC0122865876in vivo
3333PILNASVDEN C QNITYKASHN CCEEEEECCC C CEEEECCCEE 2.85%MC0221278135in vitro
4333PILNASVDEN C QNITYKASHN CCEEEEECCC C CEEEECCCEE 2.85%MC0222865876in vivo