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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: Protein CASC3

UniprotKB/SwissProt ID: O15234 (O15234)

Gene Name: CASC3

Organism: Homo sapiens (Human)

Function: Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homomer

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Cytoplasm, perinuclear region. Nucleus. Nucleus speckle. Cytoplasm, Stress granule. Cytoplasm, Cytoplasmic ribonucleoprotein granule. Cell projection, dendrite

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR018545 Btz_dom
IPR028544 CASC3

The S-nitrosylation sites of O15234

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 36 GGSPLRGGGS C SGSAGGGGSG