RRAGC

Protein-coding gene in the species Homo sapiens
RRAGC
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3LLU

Identifiers
AliasesRRAGC, GTR2, RAGC, TIB929, Ras related GTP binding C
External IDsOMIM: 608267; MGI: 1858751; HomoloGene: 39141; GeneCards: RRAGC; OMA:RRAGC - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for RRAGC
Genomic location for RRAGC
Band1p34.3Start38,838,198 bp[1]
End38,859,772 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for RRAGC
Genomic location for RRAGC
Band4|4 D2.2Start123,811,239 bp[2]
End123,830,790 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • islet of Langerhans

  • monocyte

  • skin of leg

  • tibial arteries

  • smooth muscle tissue

  • skin of abdomen

  • ventricular zone

  • gastric mucosa

  • stromal cell of endometrium

  • right coronary artery
Top expressed in
  • secondary oocyte

  • primary oocyte

  • stroma of bone marrow

  • calvaria

  • zygote

  • brown adipose tissue

  • endothelial cell of lymphatic vessel

  • motor neuron

  • decidua

  • white adipose tissue
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GTP binding
  • protein binding
  • GTPase activity
  • magnesium ion binding
  • GDP binding
  • protein heterodimerization activity
  • GTPase binding
Cellular component
  • cytoplasm
  • cytosol
  • intracellular membrane-bounded organelle
  • lysosome
  • nucleus
  • Gtr1-Gtr2 GTPase complex
Biological process
  • regulation of TOR signaling
  • small GTPase mediated signal transduction
  • cellular response to amino acid starvation
  • transcription, DNA-templated
  • cell growth
  • RNA splicing
  • apoptotic process
  • regulation of TORC1 signaling
  • response to amino acid
  • regulation of autophagy
  • regulation of macroautophagy
  • positive regulation of TOR signaling
  • cellular response to amino acid stimulus
  • cellular response to starvation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

64121

54170

Ensembl

ENSG00000116954

ENSMUSG00000028646

UniProt

Q9HB90

Q99K70

RefSeq (mRNA)

NM_022157
NM_001271851

NM_017475

RefSeq (protein)

NP_001258780
NP_071440

NP_059503

Location (UCSC)Chr 1: 38.84 – 38.86 MbChr 4: 123.81 – 123.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ras-related GTP binding C, also known as RRAGC, is a protein which in humans is encoded by the RRAGC gene.[5][6]

RRAGC is a monomeric guanine nucleotide-binding protein, or G protein. By binding GTP or GDP, small G proteins act as molecular switches in numerous cell processes and signaling pathways.[5]

Interactions

RRAGC has been shown to interact with RRAGA.[6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116954 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028646 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: RRAGC Ras-related GTP binding C".
  6. ^ a b Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T (Mar 2001). "Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B". The Journal of Biological Chemistry. 276 (10): 7246–57. doi:10.1074/jbc.M004389200. PMID 11073942.
  7. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

Further reading

  • Horwitz MS (Jan 2001). "Adenovirus immunoregulatory genes and their cellular targets". Virology. 279 (1): 1–8. doi:10.1006/viro.2000.0738. PMID 11145883.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Sekiguchi T, Todaka Y, Wang Y, Hirose E, Nakashima N, Nishimoto T (Feb 2004). "A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D". The Journal of Biological Chemistry. 279 (9): 8343–50. doi:10.1074/jbc.M305935200. PMID 14660641.
  • Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T (Mar 2001). "Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B". The Journal of Biological Chemistry. 276 (10): 7246–57. doi:10.1074/jbc.M004389200. PMID 11073942.
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