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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: Exportin-5

UniprotKB/SwissProt ID: Q9HAV4 (Q9HAV4)

Gene Name: XPO5

Organism: Homo sapiens (Human)

Function: Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in a RanGTP-dependent manner Mediates the nuclear export of micro-RNA precursors, which form short hairpins (PubMed:14631048, PubMed:14681208, PubMed:15613540). Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs (PubMed:19965479). Binding is dependent on Ran-GTP (PubMed:19965479) (Microbial infection) Mediates the nuclear export of adenovirus VA1 dsRNA

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR013598 Exportin-1/Importin-b-like
IPR045478 Exportin-5_C
IPR001494 Importin-beta_N
IPR045065 XPO1/5

The S-nitrosylation sites of Q9HAV4

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1044 NSLAWKDTLS C QRTTSQLCWP   
2 1131 IQKDSLDQFD C KLLNPSLQKV   
3 419 GFPSKTDSPS C EYSRFDFDSD   
4 50 FKEKCPICVP C GLRLAEKTQV   
5 605 RAVRNVRRHA C SSIIKMCRDY   
6 714 KSCDPGLEDP C GLNRARMSFC   
7 736 YSILGVVKRT C WPTDLEEAKA   
8 765 SSGNPIFRNP C TEQILKLLDN   
9 941 WQVINQRSLL C GEDEAADENP