\
logo
  Home | Contact us | Browse | Quick Search by UniProtKB ID, Keyword, PDBID

Menu:

Latest news:

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.

Read more...


Protein Name: Eukaryotic translation initiation factor 1A, X-chromosomal

UniprotKB/SwissProt ID: P47813 (P47813)

Gene Name: EIF1AX

Organism: Homo sapiens (Human)

Function: Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:9732867). This protein enhances formation of the cap-proximal complex (PubMed:9732867). Together with EIF1, facilitates scanning, start codon recognition, promotion of the assembly of 48S complex at the initiation codon (43S PIC becomes 48S PIC after the start codon is reached), and dissociation of aberrant complexes (PubMed:9732867). After start codon location, together with EIF5B orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex (PubMed:35732735). Is released after 80S initiation complex formation, just after GTP hydrolysis by EIF5B, and before release of EIF5B (PubMed:35732735). Its globular part is located in the A site of the 40S ribosomal subunit (PubMed:35732735). Its interaction with EIF5 during scanning contribute to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994). In contrast to yeast orthologs, does not bind EIF1 (PubMed:24319994)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR012340 NA-bd_OB-fold
IPR006196 RNA-binding_domain_S1_IF1
IPR001253 TIF_eIF-1A
IPR018104 TIF_eIF-1A_CS

The S-nitrosylation sites of P47813

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 51 MLGNGRLEAM C FDGVKRLCHI