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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: THO complex subunit 7

UniprotKB/SwissProt ID: Q6I9Y2 (Q6I9Y2)

Gene Name: THOC7

Organism: Homo sapiens (Human)

Function: Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA (PubMed:23222130). Plays a key structural role in the oligomerization of the THO-DDX39B complex (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602) (Microbial infection) The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus. Nucleus speckle

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR008501 THOC7/Mft1

The S-nitrosylation sites of Q6I9Y2

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 38 NLLVKSFIKW C NSGSQEEGYS