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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: NADH-quinone oxidoreductase subunit B

UniprotKB/SwissProt ID: NUOB_ECOLI (P0AFC7)

Gene Name: nuoB

Organism: Escherichia coli (strain K12).

Function: NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.

Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR006137
IPR006138
IPR014406

The S-nitrosylation sites of NUOB_ECOLI

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1102QADLMVVAGT C FTKMAPVIQR CCEEEEECCE E ECHHHHHHHH 3.89%EC0222178444-
2102QADLMVVAGT C FTKMAPVIQR CCEEEEECCE E ECHHHHHHHH 3.89%EC0219483679in vitro