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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: Carbonyl reductase [NADPH] 1

UniprotKB/SwissProt ID: P16152 (P16152)

Gene Name: CBR1

Organism: Homo sapiens (Human)

Function: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol (PubMed:15799708, PubMed:17344335, PubMed:17912391, PubMed:18449627, PubMed:18826943, PubMed:1921984, PubMed:7005231). Can convert prostaglandin E to prostaglandin F2-alpha (By similarity). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione (PubMed:17344335, PubMed:18826943). In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue (PubMed:28878267)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR045313 CBR1-like
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam

The S-nitrosylation sites of P16152

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 122 KTNFFGTRDV C TELLPLIKPQ   
2 150 SIMSVRALKS C SPELQQKFRS   
3 226 RKGDKILLNA C CPGWVRTDMA   
4 227 KGDKILLNAC C PGWVRTDMAG