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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: Eukaryotic peptide chain release factor GTP-binding subunit ERF3B

UniprotKB/SwissProt ID: Q149F3 (Q149F3)

Gene Name: Gspt2

Organism: Mus musculus (Mouse)

Function: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA (PubMed:12354098). GSPT2/ERF3B mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (By similarity). GTP hydrolysis by GSPT2/ERF3B induces a conformational change that leads to its dissociation, permitting ETF1/ERF1 to accommodate fully in the A-site (By similarity). Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR004161 EFTu-like_2
IPR031157 G_TR_CS
IPR054696 GTP-eEF1A_C
IPR027417 P-loop_NTPase
IPR009818 PAM2_motif
IPR000795 T_Tr_GTP-bd_dom
IPR050100 TRAFAC_GTPase_members
IPR009000 Transl_B-barrel_sf
IPR009001 Transl_elong_EF1A/Init_IF2_C

The S-nitrosylation sites of Q149F3

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 586 RPRFVKQDQV C IARLRTAGTI   
2 597 IARLRTAGTI C LETFKDFPQM