RHPN2
Rhophilin-2 is a protein that in humans is encoded by the RHPN2 gene.[1][2]
Interactions
RHPN2 has been shown to interact with RHOB.[3]
References
- ^ Peck JW, Oberst M, Bouker KB, Bowden E, Burbelo PD (Nov 2002). "The RhoA-binding protein, rhophilin-2, regulates actin cytoskeleton organization". J Biol Chem 277 (46): 43924–32. doi:10.1074/jbc.M203569200. PMID 12221077.
- ^ "Entrez Gene: RHPN2 rhophilin, Rho GTPase binding protein 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85415.
- ^ Mircescu, Hortensia; Steuve Séverine, Savonet Valérie, Degraef Chantal, Mellor Harry, Dumont Jacques E, Maenhaut Carine, Pirson Isabelle (Dec. 2002). "Identification and characterization of a novel activated RhoB binding protein containing a PDZ domain whose expression is specifically modulated in thyroid cells by cAMP". Eur. J. Biochem. (Germany) 269 (24): 6241–9. doi:10.1046/j.1432-1033.2002.03343.x. ISSN 0014-2956. PMID 12473120.
Further reading
- Mircescu H, Steuve S, Savonet V, et al. (2003). "Identification and characterization of a novel activated RhoB binding protein containing a PDZ domain whose expression is specifically modulated in thyroid cells by cAMP.". Eur. J. Biochem. 269 (24): 6241–9. doi:10.1046/j.1432-1033.2002.03343.x. PMID 12473120.
- 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Jaffe AB, Aspenström P, Hall A (2004). "Human CNK1 acts as a scaffold protein, linking Rho and Ras signal transduction pathways.". Mol. Cell. Biol. 24 (4): 1736–46. doi:10.1128/MCB.24.4.1736-1746.2004. PMC 344169. PMID 14749388. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=344169.
- 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells.". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
- Benzinger A, Muster N, Koch HB, et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer.". Mol. Cell Proteomics 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
- 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.
- Zhan X, Desiderio DM (2006). "Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry.". Anal. Biochem. 354 (2): 279–89. doi:10.1016/j.ab.2006.05.024. PMID 16777052.
- Steuve S, Devosse T, Lauwers E, et al. (2007). "Rhophilin-2 is targeted to late-endosomal structures of the vesicular machinery in the presence of activated RhoB.". Exp. Cell Res. 312 (20): 3981–9. doi:10.1016/j.yexcr.2006.08.028. PMID 17054945.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.