SESN2
Sign in to saveAlso known as HI95, SES2, SEST2, sestrin 2
Sestrin-2 also known as Hi95 is a protein that in humans is encoded by the SESN2 gene.
Gene data
SESN2- Name
- sestrin 2
- Type
- protein-coding
- Position
- 28,259,473–28,282,491 (+)
- Aliases
- HI95, SES2, SEST2
- Ensembl
- ENSG00000285069
- RefSeq RNA
- NM_031459.5, XM_047431519.1, XM_054332156.1, XM_054338981.1
- RefSeq protein
- NP_113647.1, XP_047287475.1, XP_054188131.1, XP_054194956.1
This gene encodes a member of the sestrin family of PA26-related proteins. The encoded protein may function in the regulation of cell growth and survival. This protein may be involved in cellular response to different stress conditions. [provided by RefSeq, Jul 2008].
Gene Ontology
Biological process
Molecular function
Pathways
via MyGene.info
Gene · Ensembl
sestrin 2
- Symbol
- SESN2
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- 1:28,259,473-28,282,491
- Strand
- Forward (+)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
Show 5 more facts
- exact match
- identifiers.org/ncbigene/83667
- HomoloGene ID
- 12873
- genomic end
- 28609002
- genomic start
- 28259518
- cytogenetic location
- 1p35.3
Sources (4)
via Wikidata · CC0
~2 min read
Article
5 sectionsContents
- Function
- Ligands
- See also
- References
- Further reading
Sestrin-2 also known as Hi95 is a protein that in humans is encoded by the SESN2 gene.
==Function== This gene encodes a member of the sestrin family of PA26-related proteins. The encoded protein may function in the regulation of cell growth and survival. This protein may be involved in cellular response to different stress conditions. The Sestrins constitute a family of evolutionarily-conserved stress-inducible proteins that suppress oxidative stress and regulate adenosine monophosphate-dependent protein kinase (AMPK)-mammalian target of rapamycin (mTOR) signaling. By virtue of these activities, the Sestrins serve as important regulators of metabolic homeostasis. Accordingly, inactivation of Sestrin genes in invertebrates resulted in diverse metabolic pathologies, including oxidative damage, fat accumulation, mitochondrial dysfunction and muscle degeneration that resemble accelerated tissue aging.