RRAGB
Sign in to saveAlso known as RAGB, bA465E19.1, Ras related GTP binding B
Ras-related GTP-binding protein B is a protein that in humans is encoded by the RRAGB gene.
Gene data
RRAGB- Name
- Ras related GTP binding B
- Type
- protein-coding
- Chromosome
- X
- Aliases
- RAGB, bA465E19.1
Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified. [provided by RefSeq, Jul 2008].
via MyGene.info
Gene · Ensembl
Ras related GTP binding B
- Symbol
- RRAGB
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- Chr X:55,717,612-55,758,777
- Strand
- Forward (+)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
Show 2 more facts
- HomoloGene ID
- 48396
- exact match
- identifiers.org/ncbigene/10325
via Wikidata · CC0
~1 min read
Article
2 sectionsContents
- References
- Further reading
Ras-related GTP-binding protein B is a protein that in humans is encoded by the RRAGB gene.
Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified. MTORC1 responds to amino acids via interaction with RAGB.