GIGYF2 — GRB10 interacting GYF protein 2
GIGYF2 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
GIGYF2's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Macrophages | Ubiquitin-Proteasome Regulation Housekeeping | ABCA1, AVL9, EHMT1, HUWE1, LCORL, PAXBP1, PPP2R2D, PPP2R5C +4 more | View in SCUBA |
| Mucosal-associated invariant T cell | Nuclear regulatory housekeeping Housekeeping | ATXN2, BAZ1B, CCDC90B, CD164, CREB1, HELB, HNRNPA2B1, PHIP +6 more |
About the gene
| Synonyms | GYF2, KIAA0642, PARK11, PERQ2, PERQ3, TNRC15 |
|---|---|
| Chromosome | 2: 232697299-232860605 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Disease related genes, Human disease related genes, Predicted intracellular proteins |
Function
Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation. In the 4EHP-GYF2 complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay. 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. May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors. 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. 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. (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 infection, the interaction with non-structural protein 2 (nsp2) enhances GIGYF2 binding to EIF4E2 and increases repression of translation initiation of genes involved in antiviral innate immune response such as IFNB1
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.