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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 translation initiation factor 3 subunit D

UniprotKB/SwissProt ID: O15371 (O15371)

Gene Name: EIF3D

Organism: Homo sapiens (Human)

Function: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs (PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:18599441, PubMed:25849773). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs (PubMed:27462815) (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR007783 eIF3d

The S-nitrosylation sites of O15371

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 19 IQDNPSGWGP C AVPEQFRDMP   
2 195 LEVSEPQDIE C CGALEYYDKA   
3 196 EVSEPQDIEC C GALEYYDKAF   
4 258 TDAILATLMS C TRSVYSWDIV   
5 327 TYINHNFSQQ C LRMGKERYNF   
6 375 LGDDIDLIVR C EHDGVMTGAN   
7 404 KTLNEWDSRH C NGVDWRQKLD   
8 437 NNSYKLARWT C CALLAGSEYL   
9 493 SVENAWGILR C VIDICMKLEE