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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: Polyadenylate-binding protein 1

UniprotKB/SwissProt ID: P11940 (P11940)

Gene Name: PABPC1

Organism: Homo sapiens (Human)

Function: Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability (PubMed:11051545, PubMed:17212783, PubMed:25480299). Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2 (PubMed:11051545, PubMed:20573744). Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). Involved in translationally coupled mRNA turnover (PubMed:11051545). Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (PubMed:11051545). Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (PubMed:18447585). By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (PubMed:25480299) (Microbial infection) Positively regulates the replication of dengue virus (DENV)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Cytoplasm, Stress granule. Nucleus. Cell projection, lamellipodium

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR036053 PABP-dom
IPR006515 PABP_1234
IPR002004 PABP_HYD_C
IPR034364 PABP_RRM1
IPR035979 RBD_domain_sf
IPR045305 RRM2_I_PABPs
IPR000504 RRM_dom
IPR003954 RRM_dom_euk

The S-nitrosylation sites of P11940

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 128 TFSAFGNILS C KVVCDENGSK   
2 132 FGNILSCKVV C DENGSKGYGF   
3 339 GGRSKGFGFV C FSSPEEATKA