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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: Spliceosome RNA helicase DDX39B

UniprotKB/SwissProt ID: Q13838 (Q13838)

Gene Name: DDX39B

Organism: Homo sapiens (Human)

Function: Involved in nuclear export of spliced and unspliced mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). The TREX complex 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). The THOC1-THOC2-THOC3 core complex alone is sufficient to promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). Associates with SARNP/CIP29, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export (PubMed:37578863). May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC4 and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2; the effect of ALYREF/THOC4 is reported conflictingly with [PubMed:23299939] reporting a stimulatory effect (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: Nucleus. Nucleus speckle. Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011545 DEAD/DEAH_box_helicase_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C-like
IPR027417 P-loop_NTPase
IPR014014 RNA_helicase_DEAD_Q_motif

The S-nitrosylation sites of Q13838

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 120 VTGQVSVLVM C HTRELAFQIS  CCCCCCCCCC C CCCCCCCCCC  2.01%
2 165 KKDEEVLKKN C PHIVVGTPGR  CCCCCCCCCC C CCCCCCCCCC  3.4% 22178444
18335467
37478858
3 198 KHIKHFILDE C DKMLEQLDMR  CCCCCCCCCC C CCCCCCCCCC  6.43%
4 239 ATLSKEIRPV C RKFMQDPMEI  CCCCCCCCCC C CCCCCCCCCC  4.31%
5 300 VVIFVKSVQR C IALAQLLVEQ  CCCCCCCCCC C CCCCCCCCCC  0.89%