SESN2 — Sestrin 2
SESN2 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.
SESN2's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Macrophages | Anti-inflammatory Response Inflammatory | AMPD2, ARRDC2, BHLHE40, CBX4, CDKN1B, CEBPD, CITED2, DENND3 +31 more | View in SCUBA |
| Monocytes | Inflammatory Autophagy Lysosomal & pahgocytosis | ATG2A, MAP1LC3B, RABGEF1, RELT, TOM1, UBALD2, UPP1 | View in SCUBA |
About the gene
| Synonyms | DKFZp761M0212, HI95, SES2, SEST2 |
|---|---|
| Chromosome | 1: 28259518-28282491 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Predicted intracellular proteins |
| Molecular function | Oxidoreductase |
Function
Functions as an intracellular leucine sensor that negatively regulates the mTORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents mTORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway. This stress-inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via mTORC1. May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1. May also mediate TP53 inhibition of TORC1 signaling upon genotoxic stress. Moreover, may prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N- terminal domain of the protein. Was originally reported to contribute to oxidative stress resistance by reducing PRDX1. However, this could not be confirmed.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.