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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: Coatomer subunit gamma-1

UniprotKB/SwissProt ID: Q4AEF8 (Q4AEF8)

Gene Name: Copg1

Organism: Rattus norvegicus (Rat)

Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Golgi apparatus membrane. Cytoplasmic vesicle, COPI-coated vesicle membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR002553 Clathrin/coatomer_adapt-like_N
IPR013041 Clathrin_app_Ig-like_sf
IPR009028 Coatomer/calthrin_app_sub_C
IPR032154 Coatomer_g_Cpla
IPR017106 Coatomer_gsu
IPR013040 Coatomer_gsu_app_Ig-like_dom
IPR037067 Coatomer_gsu_app_sf
IPR012295 TBP_dom_sf

The S-nitrosylation sites of Q4AEF8

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 230 RHGLKSPFAY C MMIRVASKQL   
2 296 APAVSVLQLF C SSPKAALRYA   
3 706 RSLPYNQPGT C YTLVALPKED