RHOB

RHOB
Estructuras disponibles
PDB	Búsqueda ortóloga: PDBe RCSB
Lista de codigos id de PDB
	2FV8
Identificadores
Alias	RHOB, ARH6, ARHB, MST081, MSTP081, RHOH6, ras homolog family member B
IDs externos	OMIM: 165370 MGI: 107949 HomoloGene: 68377 GeneCards: RHOB
EC number	3.6.5.2
Ontología génica
Función molecular	• nucleotide binding; • GDP binding; • GTP binding; • GO:0001948, GO:0016582 unión a proteína plasmática; • GO:0006184 GTPase activity; • protein kinase binding;
Componente celular	• citosol; • endosoma; • late endosome; • membrana; • late endosome membrane; • focal adhesion; • membrana plasmática; • early endosome; • cleavage furrow; • endosome membrane; • Exosoma (vesícula); • núcleo celular; • intracelular; • citoplasma; • corteza celular; • cell division site; • intracellular membrane-bounded organelle;
Proceso biológico	• diferenciación celular; • regulation of cell migration; • endosome to lysosome transport; • endothelial tube morphogenesis; • regulación negativa del ciclo celular; • positive regulation of angiogenesis; • positive regulation of endothelial cell migration; • desarrollo de organismo multicelular; • platelet activation; • adherencia celular; • negative regulation of cell migration; • angiogénesis; • 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; • GO:0097285 apoptosis; • small GTPase mediated signal transduction; • positive regulation of apoptotic process; • GO:0015915 transporte; • mitotic cytokinesis; • fsh follicle stimulation hormone; • actin filament organization; • regulation of cell shape; • migración celular; • establishment or maintenance of actin cytoskeleton polarity; • regulation of actin cytoskeleton organization; • actin filament bundle assembly;
	Fuentes: Amigo / QuickGO
Patrón de la expressión del ARN
	Más referencias a datos de expressión
Ortólogos
	388
	11852
	ENSG00000143878
	ENSMUSG00000054364
	P62745
	P62746
	NM_004040
	NM_007483
	NP_004031
	NP_031509
	Wikidata
Ver/Editar Humano	Ver/Editar Ratón

El miembro B de la familia de genes homólogos de Ras, también conocido como RHOB, es una proteína que en humanos está codificada por el gen RHOB.

RHOB es un miembro de la familia de proteínas Rho de unión a GTP.

Interacciones

Se ha demostrado que RHOB interactúa con CIT, ARHGEF3, ARHGDIG y RHPN2.

Significación clínica

Existe 322 enfermedades descritas que coinciden con ‘’RHOB’’.

Véase también

Cresta neural

Referencias

↑ «Human PubMed Reference:».
↑ «Mouse PubMed Reference:».
↑ «Entrez Gene: RHOB ras homolog gene family, member B».
↑ «Coding sequence of human rho cDNAs clone 6 and clone 9». Nucleic Acids Research 16 (6): 2717. March 1988. PMC 336400. PMID 3283705. doi:10.1093/nar/16.6.2717.
↑ «Rho-family GTPases: it's not only Rac and Rho (and I like it)». Journal of Cell Science 117 (Pt 8): 1301-12. March 2004. PMID 15020670. doi:10.1242/jcs.01118.
↑ Madaule, P; Furuyashiki T; Reid T; Ishizaki T; Watanabe G; Morii N; Narumiya S (Dec 1995). «A novel partner for the GTP-bound forms of rho and rac». FEBS Lett. 377 (2): 243-8. ISSN 0014-5793. PMID 8543060. doi:10.1016/0014-5793(95)01351-2.
↑ Arthur, William T; Ellerbroek Shawn M; Der Channing J; Burridge Keith; Wennerberg Krister (Nov 2002). «XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC». J. Biol. Chem. 277 (45): 42964-72. ISSN 0021-9258. PMID 12221096. doi:10.1074/jbc.M207401200.
↑ Zalcman, G; Closson V; Camonis J; Honoré N; Rousseau-Merck M F; Tavitian A; Olofsson B (Nov 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». J. Biol. Chem. 271 (48): 30366-74. ISSN 0021-9258. PMID 8939998. doi:10.1074/jbc.271.48.30366.
↑ 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. 269 (24): 6241-9. ISSN 0014-2956. PMID 12473120. doi:10.1046/j.1432-1033.2002.03343.x.
↑ RHOB «MalaCards». Consultado el 13 de diciembre de 2025.

Bibliografía

Bravo-Nuevo A, Sugimoto H, etal (2011). «RhoB loss prevents streptozotocin-induced diabetes and ameliorates diabetic complications in mice.». Am J Pathol 178 (1): 245-252. PMC 3069827. PMID 21224061. doi:10.1016/j.ajpath.2010.11.040.
Casey PJ, Seabra MC (1996). «Protein prenyltransferases.». J. Biol. Chem. 271 (10): 5289-92. PMID 8621375. doi:10.1074/jbc.271.10.5289.
Adamson P, Marshall CJ, Hall A, Tilbrook PA (1992). «Post-translational modifications of p21rho proteins.». J. Biol. Chem. 267 (28): 20033-8. PMID 1400319.
Cannizzaro LA, Madaule P, Hecht F, etal (1990). «Chromosome localization of human ARH genes, a ras-related gene family.». Genomics 6 (2): 197-203. PMID 2407642. doi:10.1016/0888-7543(90)90557-B.
Chardin P, Madaule P, Tavitian A (1988). «Coding sequence of human rho cDNAs clone 6 and clone 9.». Nucleic Acids Res. 16 (6): 2717. PMC 336400. PMID 3283705. doi:10.1093/nar/16.6.2717.
Madaule P, Axel R (1985). «A novel ras-related gene family.». Cell 41 (1): 31-40. PMID 3888408. doi:10.1016/0092-8674(85)90058-3.
Robertson D, Paterson HF, Adamson P, etal (1995). «Ultrastructural localization of ras-related proteins using epitope-tagged plasmids.». J. Histochem. Cytochem. 43 (5): 471-80. PMID 7537292. doi:10.1177/43.5.7537292.
Armstrong SA, Hannah VC, Goldstein JL, Brown MS (1995). «CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB.». J. Biol. Chem. 270 (14): 7864-8. PMID 7713879. doi:10.1074/jbc.270.14.7864.
Bonaldo MF, Lennon G, Soares MB (1997). «Normalization and subtraction: two approaches to facilitate gene discovery.». Genome Res. 6 (9): 791-806. PMID 8889548. doi:10.1101/gr.6.9.791.
Zalcman G, Closson V, Camonis J, etal (1997). «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.». J. Biol. Chem. 271 (48): 30366-74. PMID 8939998. doi:10.1074/jbc.271.48.30366.
Mellor H, Flynn P, Nobes CD, etal (1998). «PRK1 is targeted to endosomes by the small GTPase, RhoB.». J. Biol. Chem. 273 (9): 4811-4. PMID 9478917. doi:10.1074/jbc.273.9.4811.
Ishikawa K, Nagase T, Suyama M, etal (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 Res. 5 (3): 169-76. PMID 9734811. doi:10.1093/dnares/5.3.169.
Liu JP, Jessell TM (1999). «A role for rhoB in the delamination of neural crest cells from the dorsal neural tube.». Development 125 (24): 5055-67. PMID 9811589.
Gampel A, Parker PJ, Mellor H (2000). «Regulation of epidermal growth factor receptor traffic by the small GTPase rhoB.». Curr. Biol. 9 (17): 955-8. PMID 10508588. doi:10.1016/S0960-9822(99)80422-9.
Matarrese P, Conti L, Varano B, etal (2000). «The HIV-1 vpr protein induces anoikis-resistance by modulating cell adhesion process and microfilament system assembly.». Cell Death Differ. 7 (1): 25-36. PMID 10713718. doi:10.1038/sj.cdd.4400616.
Liu A, Du W, Liu JP, etal (2000). «RhoB alteration is necessary for apoptotic and antineoplastic responses to farnesyltransferase inhibitors.». Mol. Cell. Biol. 20 (16): 6105-13. PMC 86086. PMID 10913192. doi:10.1128/MCB.20.16.6105-6113.2000.
Michaelson D, Silletti J, Murphy G, etal (2001). «Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding.». J. Cell Biol. 152 (1): 111-26. PMC 2193662. PMID 11149925. doi:10.1083/jcb.152.1.111.
Liu Ax; Cerniglia GJ; Bernhard EJ; Prendergast GC (2001). «RhoB is required to mediate apoptosis in neoplastically transformed cells after DNA damage.». Proc. Natl. Acad. Sci. U.S.A. 98 (11): 6192-7. Bibcode:2001PNAS...98.6192L. PMC 33444. PMID 11353846. doi:10.1073/pnas.111137198.
Diviani D, Soderling J, Scott JD (2001). «AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation.». J. Biol. Chem. 276 (47): 44247-57. PMID 11546812. doi:10.1074/jbc.M106629200.
Adnane J, Seijo E, Chen Z, etal (2002). «RhoB, not RhoA, represses the transcription of the transforming growth factor beta type II receptor by a mechanism involving activator protein 1.». J. Biol. Chem. 277 (10): 8500-7. PMID 11741970. doi:10.1074/jbc.M104367200.