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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: Bifunctional glutamate/proline--tRNA ligase

UniprotKB/SwissProt ID: Q8CGC7 (Q8CGC7)

Gene Name: Eprs1

Organism: Mus musculus (Mouse)

Function: Multifunctional protein which primarily functions within the aminoacyl-tRNA synthetase multienzyme complex, also known as multisynthetase complex. Within the complex it catalyzes the attachment of both L-glutamate and L-proline to their cognate tRNAs in a two-step reaction where the amino acid is first activated by ATP to form a covalent intermediate with AMP. Subsequently, the activated amino acid is transferred to the acceptor end of the cognate tRNA to form L-glutamyl-tRNA(Glu) and L-prolyl-tRNA(Pro) (By similarity). Upon interferon-gamma stimulation, EPRS1 undergoes phosphorylation, causing its dissociation from the aminoacyl-tRNA synthetase multienzyme complex. It is recruited to form the GAIT complex, which binds to stem loop-containing GAIT elements found in the 3'-UTR of various inflammatory mRNAs, such as ceruloplasmin. The GAIT complex inhibits the translation of these mRNAs, allowing interferon-gamma to redirect the function of EPRS1 from protein synthesis to translation inhibition in specific cell contexts (PubMed:23071094). Furthermore, it can function as a downstream effector in the mTORC1 signaling pathway, by promoting the translocation of SLC27A1 from the cytoplasm to the plasma membrane where it mediates the uptake of long-chain fatty acid by adipocytes. Thereby, EPRS1 also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR002314 aa-tRNA-synt_IIb
IPR001412 aa-tRNA-synth_I_CS
IPR006195 aa-tRNA-synth_II
IPR045864 aa-tRNA-synth_II/BPL/LPL
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR053836 Arc1-like_N
IPR004526 Glu-tRNA-synth_arc/euk
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR036282 Glutathione-S-Trfase_C_sf
IPR004499 Pro-tRNA-ligase_IIa_arc-type
IPR016061 Pro-tRNA_ligase_II_C
IPR017449 Pro-tRNA_synth_II
IPR033721 ProRS_core_arch_euk
IPR020056 Rbsml_bL25/Gln-tRNA_synth_N
IPR011035 Ribosomal_bL25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold
IPR049437 tRNA-synt_1c_C2
IPR009068 uS15_NS1_RNA-bd_sf
IPR000738 WHEP-TRS_dom

The S-nitrosylation sites of Q8CGC7

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 105 LTSAINELNH C LSLRTYLVGN  CCEEEEEECC C CCCHHHHHHE  2.41% 20925432
2 1377 LEVGPRDMKS C QFVAVRRDTG  CCEEEEEECC C CCCHHHHHHE  2.8% 24926564
3 336 MKKGSQFGQS C CLRAKIDMSS  CCEEEEEECC C CCCHHHHHHE  1.62%
4 337 KKGSQFGQSC C LRAKIDMSSN  CCEEEEEECC C CCCHHHHHHE  3.31% 24926564
5 381 YNVYPTYDFA C PIVDSIEGVT  CCEEEEEECC C CCCHHHHHHE  2.09%
6 660 KHEELMLGDP C LKDLKKGDII  CCEEEEEECC C CCCHHHHHHE  9.8% 24926564
7 744 ERPAPAVSST C ATAEDSSVLY  CCEEEEEECC C CCCHHHHHHE  3.24% 21278135
8 856 PKAKVTEAVE C LLSLKAEYKE  CCEEEEEECC C CCCHHHHHHE  3.58%