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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: Polypyrimidine tract-binding protein 1

UniprotKB/SwissProt ID: P17225 (P17225)

Gene Name: Ptbp1

Organism: Mus musculus (Mouse)

Function: Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. Binds to polypyrimidine-rich controlling element (PCE) of CFTR and promotes exon skipping of CFTR exon 9, thereby antagonizing TIA1 and its role in exon inclusion of CFTR exon 9. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to a polypyrimidine tract flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR006536 HnRNP-L/PTB
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR021790 PTBP1-like_RRM2
IPR035000 PTBP1_RRM1
IPR035001 PTBP1_RRM3
IPR035979 RBD_domain_sf
IPR000504 RRM_dom

The S-nitrosylation sites of P17225

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 249 SLDGQNIYNA C CTLRIDFSKL   
2 250 LDGQNIYNAC C TLRIDFSKLT