Search Results
Overview
| Uniprot ID | Q6Y7W6 |
|---|---|
| Protein Name | GRB10-interacting GYF protein 2 |
| Gene Name | GIGYF2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1103 | KNNASLSKSVGVSNR |
| 175 | RFEKPGRKDVGRPNF |
| 985 | QQQQQQQKLSGWGNV |
Function
Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931, PubMed:31439631, PubMed:35878012). In the 4EHP-GYF2 complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay (PubMed:31439631). Also recruits and bridges the association of the 4EHP complex with the decapping effector protein DDX6, which is required for the ZFP36/TTP-mediated down-regulation of AU-rich mRNA (PubMed:31439631). May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors (PubMed:12771153). In association with EIF4E2, assists ribosome-associated quality control (RQC) by sequestering the mRNA cap, blocking ribosome initiation and decreasing the translational load on problematic messages. Part of a pathway that works in parallel to RQC-mediated degradation of the stalled nascent polypeptide (PubMed:32726578). GIGYF2 and EIF4E2 work downstream and independently of ZNF598, which seems to work as a scaffold that can recruit them to faulty mRNA even if alternative recruitment mechanisms may exist (PubMed:32726578)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0010494 | cytoplasmic stress granule |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005768 | endosome |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0043204 | perikaryon |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:1990635 | proximal dendrite |
| Cellular Component | GO:0031982 | vesicle |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Molecular Function | GO:0000900 | mRNA regulatory element binding translation repressor activity |
| Molecular Function | GO:0070064 | proline-rich region binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0048009 | insulin-like growth factor receptor signaling pathway |
| Biological Process | GO:0061157 | mRNA destabilization |
| Biological Process | GO:0017148 | negative regulation of translation |
| Biological Process | GO:0045947 | negative regulation of translational initiation |
| Biological Process | GO:0060339 | negative regulation of type I interferon-mediated signaling pathway |
| Biological Process | GO:0016441 | post-transcriptional gene silencing |
| Biological Process | GO:1990261 | pre-mRNA catabolic process |
| Biological Process | GO:0072344 | rescue of stalled cytosolic ribosome |
Reference
[1] 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.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.