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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: Importin-9

UniprotKB/SwissProt ID: Q96P70 (Q96P70)

Gene Name: IPO9

Organism: Homo sapiens (Human)

Function: Nuclear transport receptor that mediates nuclear import of proteins, such as histones, proteasome and actin (PubMed:11823430, PubMed:30855230, PubMed:34711951). Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:11823430). Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:11823430). At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran (PubMed:11823430). The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:11823430). Mediates the import of pre-assembled proteasomes into the nucleus; AKIRIN2 acts as a molecular bridge between IPO9 and the proteasome complex (PubMed:11823430, PubMed:34711951). Mediates the nuclear import of histones H2A, H2B, H4 and H4 (PubMed:11823430, PubMed:30855230). In addition to nuclear import, also acts as a chaperone for histones by preventing inappropriate non-nucleosomal interactions (PubMed:30855230). Mediates the nuclear import of actin (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR056840 HEAT_IPO9_central
IPR001494 Importin-beta_N

The S-nitrosylation sites of Q96P70

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 450 TEHWWKIHEA C MLALGSVKAI   
2 545 ISAVRAIWGY C DQLKVSESTH   
3 639 IFKELSQIEA C QGPMQMRLIP   
4 864 YEGKVSSVAL C KLLQHGINAD   
5 90 ILKQYVETHW C AQSEKFRPPE