Search Results
Overview
| Uniprot ID | P57772 |
|---|---|
| Protein Name | Selenocysteine-specific elongation factor |
| Gene Name | EEFSEC |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 38 | ASTAAFDKQPQSRER |
| 397 | DNDEADKKAGQATEG |
| 549 | KILTPALKKRARAGR |
Function
Translation factor required for the incorporation of the rare amino acid selenocysteine encoded by UGA codons (PubMed:27708257, PubMed:35709277). Replaces the eRF1-eRF3-GTP ternary complex for the insertion of selenocysteine directed by the UGA codon (PubMed:27708257, PubMed:35709277). Insertion of selenocysteine at UGA codons is mediated by SECISBP2 and EEFSEC: SECISBP2 (1) specifically binds the SECIS sequence once the 80S ribosome encounters an in-frame UGA codon and (2) contacts the RPS27A/eS31 of the 40S ribosome before ribosome stalling (PubMed:35709277). (3) GTP-bound EEFSEC then delivers selenocysteinyl-tRNA(Sec) to the 80S ribosome and adopts a preaccommodated state conformation (PubMed:35709277). (4) After GTP hydrolysis, EEFSEC dissociates from the assembly, selenocysteinyl-tRNA(Sec) accommodates, and peptide bond synthesis and selenoprotein elongation occur (PubMed:35709277)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0043021 | ribonucleoprotein complex binding |
| Molecular Function | GO:0035368 | selenocysteine insertion sequence binding |
| Molecular Function | GO:0003746 | translation elongation factor activity |
| Molecular Function | GO:0000049 | tRNA binding |
| Biological Process | GO:0001514 | selenocysteine incorporation |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.