RHOB

RHOB
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2FV8
Identifiers
Aliases	RHOB, ARH6, ARHB, MST081, MSTP081, RHOH6, ras homolog family member B
External IDs	OMIM: 165370 MGI: 107949 HomoloGene: 68377 GeneCards: RHOB
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	20,449,440 bp[1]
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)[2]
End	8,500,009 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• nucleotide binding; • GDP binding; • GTP binding; • GO:0001948 protein binding; • GTPase activity; • protein kinase binding;
Cellular component	• cytosol; • endosome; • late endosome; • membrane; • late endosome membrane; • focal adhesion; • cell membrane; • early endosome; • cleavage furrow; • endosome membrane; • extracellular exosome; • cell nucleus; • intracellular; • 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
	388
	11852
	ENSG00000143878
	ENSMUSG00000054364
	P62745
	P62746
	NM_004040
	NM_007483
	NP_004031
	NP_031509
	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.[5][6]

RHOB is a member of the Rho GTP-binding protein family.[7]

Interactions

RHOB has been shown to interact with CIT,[8] ARHGEF3,[9] ARHGDIG[10] and RHPN2.[11]

References

GRCh38: Ensembl release 89: ENSG00000143878 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000054364 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: RHOB ras homolog gene family, member B".
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.
Wennerberg K, Der CJ (March 2004). "Rho-family GTPases: it's not only Rac and Rho (and I like it)". Journal of Cell Science. 117 (Pt 8): 1301–12. doi:10.1242/jcs.01118. PMID 15020670.
Madaule P, Furuyashiki T, Reid T, Ishizaki T, Watanabe G, Morii N, Narumiya S (December 1995). "A novel partner for the GTP-bound forms of rho and rac". FEBS Letters. 377 (2): 243–8. doi:10.1016/0014-5793(95)01351-2. PMID 8543060.
Arthur WT, Ellerbroek SM, Der CJ, Burridge K, Wennerberg K (November 2002). "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC". The Journal of Biological Chemistry. 277 (45): 42964–72. doi:10.1074/jbc.M207401200. PMID 12221096.
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.
Mircescu H, Steuve S, Savonet V, Degraef C, Mellor H, Dumont JE, Maenhaut C, Pirson I (December 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" (PDF). European Journal of Biochemistry. 269 (24): 6241–9. doi:10.1046/j.1432-1033.2002.03343.x. PMID 12473120.

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. 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. 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. 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000143878 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000054364 - 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.

[entrez-5] "Entrez Gene: RHOB ras homolog gene family, member B".

[pmid3283705-6] 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.

[pmid15020670-7] Wennerberg K, Der CJ (March 2004). "Rho-family GTPases: it's not only Rac and Rho (and I like it)". Journal of Cell Science. 117 (Pt 8): 1301–12. doi:10.1242/jcs.01118. PMID 15020670.

[pmid8543060-8] Madaule P, Furuyashiki T, Reid T, Ishizaki T, Watanabe G, Morii N, Narumiya S (December 1995). "A novel partner for the GTP-bound forms of rho and rac". FEBS Letters. 377 (2): 243–8. doi:10.1016/0014-5793(95)01351-2. PMID 8543060.

[pmid12221096-9] Arthur WT, Ellerbroek SM, Der CJ, Burridge K, Wennerberg K (November 2002). "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC". The Journal of Biological Chemistry. 277 (45): 42964–72. doi:10.1074/jbc.M207401200. PMID 12221096.

[pmid8939998-10] 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.

[pmid12473120-11] Mircescu H, Steuve S, Savonet V, Degraef C, Mellor H, Dumont JE, Maenhaut C, Pirson I (December 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" (PDF). European Journal of Biochemistry. 269 (24): 6241–9. doi:10.1046/j.1432-1033.2002.03343.x. PMID 12473120.

RHOB

Interactions

See also

References

Further reading