GEM (gene)

From Wikipedia, the free encyclopedia

GTP binding protein overexpressed in skeletal muscle

PDB rendering based on 2cjw.

Available structures: 2cjw, 2g3y, 2ht6

Identifiers

Symbol(s)

GEM; KIR; MGC26294

External IDs

OMIM: 600164 MGI: 99844 HomoloGene: 38024

Gene ontology
Molecular Function:	• nucleotide binding • calmodulin binding • GTP binding
Cellular Component:	• membrane
Biological Process:	• immune response • cell surface receptor linked signal transduction • small GTPase mediated signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005261 (mRNA)
NP_005252 (protein)

NM_010276 (mRNA)
NP_034406 (protein)

Location

Chr 8: 95.33 - 95.34 Mb

Chr 4: 11.63 - 11.64 Mb

Pubmed search

[1]

[2]

GTP binding protein overexpressed in skeletal muscle, also known as GEM, is a human gene.^[1]

The protein encoded by this gene belongs to the RAD/GEM family of GTP-binding proteins. It is associated with the inner face of the plasma membrane and could play a role as a regulatory protein in receptor-mediated signal transduction. Alternative splicing occurs at this locus and two transcript variants encoding the same protein have been identified.^[1]

[edit] References

^ ^a ^b Entrez Gene: GEM GTP binding protein overexpressed in skeletal muscle.

[edit] Further reading

Cohen L, Mohr R, Chen YY, et al. (1995). "Transcriptional activation of a ras-like gene (kir) by oncogenic tyrosine kinases.". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12448-52. PMID 7809057.
Maguire J, Santoro T, Jensen P, et al. (1994). "Gem: an induced, immediate early protein belonging to the Ras family.". Science 265 (5169): 241-4. PMID 7912851.
Santoro T, Maguire J, McBride OW, et al. (1997). "Chromosomal organization and transcriptional regulation of human GEM and localization of the human and mouse GEM loci encoding an inducible Ras-like protein.". Genomics 30 (3): 558-64. doi:10.1006/geno.1995.1277. PMID 8825643.
Moyers JS, Bilan PJ, Zhu J, Kahn CR (1997). "Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II.". J. Biol. Chem. 272 (18): 11832-9. PMID 9115241.
Béguin P, Nagashima K, Gonoi T, et al. (2001). "Regulation of Ca2+ channel expression at the cell surface by the small G-protein kir/Gem.". Nature 411 (6838): 701-6. doi:10.1038/35079621. PMID 11395774.
Ward Y, Yap SF, Ravichandran V, et al. (2002). "The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway.". J. Cell Biol. 157 (2): 291-302. doi:10.1083/jcb.200111026. PMID 11956230.
Aresta S, de Tand-Heim MF, Béranger F, de Gunzburg J (2003). "A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases.". Biochem. J. 367 (Pt 1): 57-65. doi:10.1042/BJ20020829. PMID 12093360.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514.
Kelly K (2006). "The RGK family: a regulatory tail of small GTP-binding proteins.". Trends Cell Biol. 15 (12): 640-3. doi:10.1016/j.tcb.2005.10.002. PMID 16242932.
Opatowsky Y, Sasson Y, Shaked I, et al. (2006). "Structure-function studies of the G-domain from human gem, a novel small G-protein.". FEBS Lett. 580 (25): 5959-64. doi:10.1016/j.febslet.2006.09.067. PMID 17052716.
Splingard A, Ménétrey J, Perderiset M, et al. (2007). "Biochemical and structural characterization of the gem GTPase.". J. Biol. Chem. 282 (3): 1905-15. doi:10.1074/jbc.M604363200. PMID 17107948.