RHOB

This article is about the ras homolog gene family. For the Rayburn House Office Building, see Rayburn House Office Building.

RHOB
Identifiers
Aliases	RHOB, ARH6, ARHB, MST081, MSTP081, RHOH6, ras homolog family member B
External IDs	OMIM: 165370; MGI: 107949; HomoloGene: 68377; GeneCards: RHOB; OMA:RHOB - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2FV8
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.6.5.2 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 2 (human) Band 2p24.1 Start 20,447,074 bp End 20,449,440 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 A1.1 Start 8,547,661 bp End 8,550,009 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastric mucosa saphenous vein popliteal artery tibial arteries vena cava urethra internal globus pallidus nipple left uterine tube tail of epididymis Top expressed in molar decidua granulocyte dorsomedial hypothalamic nucleus left lung lobe olfactory tubercle globus pallidus lateral geniculate nucleus stroma of bone marrow subiculum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding GDP binding GTP binding protein binding GTPase activity protein kinase binding Cellular component cytosol endosome late endosome membrane late endosome membrane focal adhesion plasma membrane early endosome cleavage furrow endosome membrane extracellular exosome nucleus intracellular anatomical structure cytoplasm cell cortex cell division site intracellular membrane-bounded organelle Biological process cell differentiation regulation of cell migration endosome to lysosome transport endothelial tube morphogenesis negative regulation of cell cycle positive regulation of angiogenesis positive regulation of endothelial cell migration multicellular organism development platelet activation cell adhesion negative regulation of cell migration angiogenesis Rho protein signal transduction cellular response to ionizing radiation protein transport intracellular protein transport regulation of small GTPase mediated signal transduction cellular response to hydrogen peroxide apoptotic process small GTPase mediated signal transduction positive regulation of apoptotic process transport mitotic cytokinesis G protein-coupled receptor signaling pathway actin filament organization regulation of cell shape cell migration establishment or maintenance of actin cytoskeleton polarity regulation of actin cytoskeleton organization actin filament bundle assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 388 11852 Ensembl ENSG00000143878 ENSMUSG00000054364 UniProt P62745 P62746 RefSeq (mRNA) NM_004040 NM_007483 RefSeq (protein) NP_004031 NP_031509 Location (UCSC) Chr 2: 20.45 – 20.45 Mb Chr 12: 8.55 – 8.55 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Ras homolog gene family, member B, also known as RHOB, is a protein which in humans is encoded by the RHOB gene.

RHOB is a member of the Rho GTP-binding protein family.

Interactions

RHOB has been shown to interact with CIT, ARHGEF3, ARHGDIG and RHPN2.

See also

• neural crest

Further reading

• Bravo-Nuevo A, Sugimoto H, Iyer S, Fallon Z, Lucas JM, Kazerounian S, Prendergast GC, Kalluri R, Shapiro NI, Benjamin LE (January 2011). "RhoB loss prevents streptozotocin-induced diabetes and ameliorates diabetic complications in mice". The American Journal of Pathology. 178 (1): 245–52. doi:10.1016/j.ajpath.2010.11.040. PMC 3069827. PMID 21224061.
• Casey PJ, Seabra MC (March 1996). "Protein prenyltransferases". The Journal of Biological Chemistry. 271 (10): 5289–92. doi:10.1074/jbc.271.10.5289. PMID 8621375.
• Adamson P, Marshall CJ, Hall A, Tilbrook PA (October 1992). "Post-translational modifications of p21rho proteins". The Journal of Biological Chemistry. 267 (28): 20033–8. doi:10.1016/S0021-9258(19)88661-1. PMID 1400319.
• Cannizzaro LA, Madaule P, Hecht F, Axel R, Croce CM, Huebner K (February 1990). "Chromosome localization of human ARH genes, a ras-related gene family". Genomics. 6 (2): 197–203. doi:10.1016/0888-7543(90)90557-B. PMID 2407642.
• Chardin P, Madaule P, Tavitian A (March 1988). "Coding sequence of human rho cDNAs clone 6 and clone 9". Nucleic Acids Research. 16 (6): 2717. doi:10.1093/nar/16.6.2717. PMC 336400. PMID 3283705.
• Madaule P, Axel R (May 1985). "A novel ras-related gene family". Cell. 41 (1): 31–40. doi:10.1016/0092-8674(85)90058-3. PMID 3888408. S2CID 32708060.
• Robertson D, Paterson HF, Adamson P, Hall A, Monaghan P (May 1995). "Ultrastructural localization of ras-related proteins using epitope-tagged plasmids". The Journal of Histochemistry and Cytochemistry. 43 (5): 471–80. doi:10.1177/43.5.7537292. PMID 7537292.
• Armstrong SA, Hannah VC, Goldstein JL, Brown MS (April 1995). "CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB". The Journal of Biological Chemistry. 270 (14): 7864–8. doi:10.1074/jbc.270.14.7864. PMID 7713879.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Zalcman G, Closson V, Camonis J, Honoré N, Rousseau-Merck MF, Tavitian A, Olofsson B (November 1996). "RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG". The Journal of Biological Chemistry. 271 (48): 30366–74. doi:10.1074/jbc.271.48.30366. PMID 8939998.
• Mellor H, Flynn P, Nobes CD, Hall A, Parker PJ (February 1998). "PRK1 is targeted to endosomes by the small GTPase, RhoB". The Journal of Biological Chemistry. 273 (9): 4811–4. doi:10.1074/jbc.273.9.4811. PMID 9478917.
• Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (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.
• Liu JP, Jessell TM (December 1998). "A role for rhoB in the delamination of neural crest cells from the dorsal neural tube". Development. 125 (24): 5055–67. doi:10.1242/dev.125.24.5055. PMID 9811589.
• Gampel A, Parker PJ, Mellor H (September 1999). "Regulation of epidermal growth factor receptor traffic by the small GTPase rhoB". Current Biology. 9 (17): 955–8. Bibcode:1999CBio....9..955G. doi:10.1016/S0960-9822(99)80422-9. PMID 10508588. S2CID 9616910.
• Matarrese P, Conti L, Varano B, Gauzzi MC, Belardelli F, Gessani S, Malorni W (January 2000). "The HIV-1 vpr protein induces anoikis-resistance by modulating cell adhesion process and microfilament system assembly". Cell Death and Differentiation. 7 (1): 25–36. doi:10.1038/sj.cdd.4400616. PMID 10713718.
• Liu Ax, Du W, Liu JP, Jessell TM, Prendergast GC (August 2000). "RhoB alteration is necessary for apoptotic and antineoplastic responses to farnesyltransferase inhibitors". Molecular and Cellular Biology. 20 (16): 6105–13. doi:10.1128/MCB.20.16.6105-6113.2000. PMC 86086. PMID 10913192.
• Michaelson D, Silletti J, Murphy G, D'Eustachio P, Rush M, Philips MR (January 2001). "Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding". The Journal of Cell Biology. 152 (1): 111–26. doi:10.1083/jcb.152.1.111. PMC 2193662. PMID 11149925.
• Cerniglia GJ, Bernhard EJ, Prendergast GC (May 2001). "RhoB is required to mediate apoptosis in neoplastically transformed cells after DNA damage". Proceedings of the National Academy of Sciences of the United States of America. 98 (11): 6192–7. Bibcode:2001PNAS...98.6192L. doi:10.1073/pnas.111137198. PMC 33444. PMID 11353846.
• Diviani D, Soderling J, Scott JD (November 2001). "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation". The Journal of Biological Chemistry. 276 (47): 44247–57. doi:10.1074/jbc.M106629200. PMID 11546812.
• Adnane J, Seijo E, Chen Z, Bizouarn F, Leal M, Sebti SM, Muñoz-Antonia T (March 2002). "RhoB, not RhoA, represses the transcription of the transforming growth factor beta type II receptor by a mechanism involving activator protein 1". The Journal of Biological Chemistry. 277 (10): 8500–7. doi:10.1074/jbc.M104367200. PMID 11741970.