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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: Elongation factor G, mitochondrial

UniprotKB/SwissProt ID: Q96RP9 (Q96RP9)

Gene Name: GFM1

Organism: Homo sapiens (Human)

Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Mitochondrion

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR041095 EFG_II
IPR009022 EFG_III
IPR035647 EFG_III/V
IPR047872 EFG_IV
IPR035649 EFG_V
IPR000640 EFG_V-like
IPR004161 EFTu-like_2
IPR031157 G_TR_CS
IPR027417 P-loop_NTPase
IPR020568 Ribosomal_Su5_D2-typ_SF
IPR014721 Ribsml_uS5_D2-typ_fold_subgr
IPR005225 Small_GTP-bd
IPR000795 T_Tr_GTP-bd_dom
IPR009000 Transl_B-barrel_sf
IPR004540 Transl_elong_EFG/EF2
IPR005517 Transl_elong_EFG/EF2_IV

The S-nitrosylation sites of Q96RP9

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 256 ATDHRQELIE C VANSDEQLGE   
2 514 YAQRLEREYG C PCITGKPKVA   
3 594 PAVEKGFLDA C EKGPLSGHKL   
4 723 YTMEYSRYQP C LPSTQEDVIN