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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: Ran-binding protein 3

UniprotKB/SwissProt ID: Q9H6Z4 (Q9H6Z4)

Gene Name: RANBP3

Organism: Homo sapiens (Human)

Function: Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011993 PH-like_dom_sf
IPR000156 Ran_bind_dom
IPR045255 RanBP1-like

The S-nitrosylation sites of Q9H6Z4

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 116 EDSDREDGNY C PPVKRERTSS   
2 203 GTNGVSLPAD C TGAVPAASPD   
3 228 RSPSEAADEV C ALEEKEPQKN