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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: Serine hydrolase RBBP9

UniprotKB/SwissProt ID: O75884 (O75884)

Gene Name: RBBP9

Organism: Homo sapiens (Human)

Function: Serine hydrolase (Probable) (PubMed:32196348). Catalyzes the hydrolytic activation of amino acid ester of the antiviral prodrug valacyclovir to its corresponding active drug, acyclovir (PubMed:32196348). May negatively regulate basal or autocrine TGF-beta signaling by suppressing SMAD2-SMAD3 phosphorylation (PubMed:20080647). May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta through interaction with RB1 and the subsequent displacement of E2F1 (PubMed:9697699)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization:

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR029058 AB_hydrolase_fold
IPR010662 Hydrolase_RBBP9/YdeN
IPR052581 RBBP9

The S-nitrosylation sites of O75884

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 39 KELEKIPGFQ C LAKNMPDPIT   
2 65 WLPFMETELH C DEKTIIIGHS