G3BP2

Ras GTPase-activating protein-binding protein 2 is an enzyme that in humans is encoded by the G3BP2 gene.[5][6][7]

G3BP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5DRV
Identifiers
Aliases	G3BP2, G3BP stress granule assembly factor 2
External IDs	MGI: 2442040 HomoloGene: 137244 GeneCards: G3BP2
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q21.1 Start 75,642,782 bp[1] End 75,724,525 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 E2 Start 92,052,146 bp[2] End 92,083,719 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • receptor signaling complex scaffold activity • GO:0001948 protein binding • nucleic acid binding • mRNA binding • RNA binding Cellular component • intracellular • cytoplasm • cytosol • ribonucleoprotein • cytoplasmic stress granule Biological process • mRNA transport • Ras protein signal transduction • cytoplasmic sequestering of NF-kappaB • stress granule assembly • transport • positive regulation of signal transduction • GO:0022415 viral process • protein homooligomerization • positive regulation of stress granule assembly • immune system process • innate immune system Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9908	23881
Ensembl	ENSG00000138757	ENSMUSG00000029405
UniProt	Q9UN86	P97379
RefSeq (mRNA)	NM_012297 NM_203504 NM_203505	NM_001080794 NM_001080795 NM_001080796 NM_001080797 NM_011816 NM_001359195 NM_001359196 NM_001359197
RefSeq (protein)	NP_036429 NP_987100 NP_987101 NP_987100.1	NP_001074263 NP_001074264 NP_001074265 NP_001074266 NP_035946 NP_001346124 NP_001346125 NP_001346126
Location (UCSC)	Chr 4: 75.64 – 75.72 Mb	Chr 5: 92.05 – 92.08 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

G3BP2 has been shown to interact with IκBα.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000138757 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029405 - 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. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, et al. (June 1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 5 (3): 169–76. doi:10.1093/dnares/5.3.169. PMID 9734811.
6. Kennedy D, Wood SA, Ramsdale T, Tam PP, Steiner KA, Mattick JS (June 1998). "Identification of a mouse orthologue of the human ras-GAP-SH3-domain binding protein and structural confirmation that these proteins contain an RNA recognition motif". Biomedical Peptides, Proteins & Nucleic Acids. 2 (3): 93–9. PMID 9575347.
7. "Entrez Gene: G3BP2 GTPase activating protein (SH3 domain) binding protein 2".
8. Prigent M, Barlat I, Langen H, Dargemont C (November 2000). "IkappaBalpha and IkappaBalpha /NF-kappa B complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2". The Journal of Biological Chemistry. 275 (46): 36441–9. doi:10.1074/jbc.M004751200. PMID 10969074.

Further reading

• Kim MM, Wiederschain D, Kennedy D, Hansen E, Yuan ZM (June 2007). "Modulation of p53 and MDM2 activity by novel interaction with Ras-GAP binding proteins (G3BP)". Oncogene. 26 (29): 4209–15. doi:10.1038/sj.onc.1210212. PMID 17297477.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Ong SE, Mittler G, Mann M (November 2004). "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nature Methods. 1 (2): 119–26. doi:10.1038/nmeth715. PMID 15782174.
• Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (November 2004). "Phosphoproteomic analysis of the developing mouse brain". Molecular & Cellular Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
• Prigent M, Barlat I, Langen H, Dargemont C (November 2000). "IkappaBalpha and IkappaBalpha /NF-kappa B complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2". The Journal of Biological Chemistry. 275 (46): 36441–9. doi:10.1074/jbc.M004751200. PMID 10969074.
• Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, et al. (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.