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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: Envelope glycoprotein gp95

UniprotKB/SwissProt ID: P03396 (P03396)

Gene Name: env

Organism: Rous sarcoma virus subgroup C (strain Prague) (RSV-Pr-C)

Function: The surface protein (SU) attaches the virus to the host cell entry receptor TVC (PubMed:16051833). This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate on Cys-100 to activate its fusogenic potential. Fusion occurs at the host cell plasma membrane (By similarity) The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Virion membrane. Host cell membrane. Virion membrane. Host cell membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR005166 RSV_p95_env
IPR018154 TLV/ENV_coat_polyprotein