RHOB

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

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Identifiers
Aliases|
External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
Entrez| |

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Location (UCSC)| n/a| n/a
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Wikidata
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Ras homolog gene family, member B, also known as RHOB, is a protein which in humans is encoded by the RHOB gene.[1][2]

RHOB is a member of the Rho GTP-binding protein family.[3]

## Contents

* 1 Interactions
* 2 References
* 3 Further reading
* 4 See also

## Interactions

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RHOB has been shown to interact with CIT,[4] ARHGEF3,[5] ARHGDIG[6] and RHPN2.[7]

## References

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1. ↑ "Entrez Gene: RHOB ras homolog gene family, member B".
2. ↑ 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.
3. ↑ 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.
4. ↑ 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. doi:10.1016/0014-5793(95)01351-2. ISSN 0014-5793. PMID 8543060.
5. ↑ 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. doi:10.1074/jbc.M207401200. ISSN 0021-9258. PMID 12221096.
6. ↑ 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. doi:10.1074/jbc.271.48.30366. ISSN 0021-9258. PMID 8939998.
7. ↑ 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. doi:10.1046/j.1432-1033.2002.03343.x. ISSN 0014-2956. PMID 12473120.

## Further reading

[edit | edit source]

* Bravo-Nuevo A, Sugimoto H, et al. (2011). "RhoB loss prevents streptozotocin-induced diabetes and ameliorates diabetic complications in mice". Am J Pathol. 178 (1): 245–252. doi:10.1016/j.ajpath.2010.11.040. PMC 3069827. PMID 21224061.
* Casey PJ, Seabra MC (1996). "Protein prenyltransferases". J. Biol. Chem. 271 (10): 5289–92. doi:10.1074/jbc.271.10.5289. PMID 8621375.
* 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, et al. (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 (1988). "Coding sequence of human rho cDNAs clone 6 and clone 9". Nucleic Acids Res. 16 (6): 2717. doi:10.1093/nar/16.6.2717. PMC 336400. PMID 3283705.
* Madaule P, Axel R (1985). "A novel ras-related gene family". Cell. 41 (1): 31–40. doi:10.1016/0092-8674(85)90058-3. PMID 3888408.
* Robertson D, Paterson HF, Adamson P, et al. (1995). "Ultrastructural localization of ras-related proteins using epitope-tagged plasmids". J. Histochem. Cytochem. 43 (5): 471–80. doi:10.1177/43.5.7537292. PMID 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. doi:10.1074/jbc.270.14.7864. PMID 7713879.
* Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
* Zalcman G, Closson V, Camonis J, et al. (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. doi:10.1074/jbc.271.48.30366. PMID 8939998.
* Mellor H, Flynn P, Nobes CD, et al. (1998). "PRK1 is targeted to endosomes by the small GTPase, RhoB". J. Biol. Chem. 273 (9): 4811–4. doi:10.1074/jbc.273.9.4811. PMID 9478917.
* Ishikawa K, Nagase T, Suyama M, et al. (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. doi:10.1093/dnares/5.3.169. PMID 9734811.
* 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. doi:10.1016/S0960-9822(99)80422-9. PMID 10508588.
* Matarrese P, Conti L, Varano B, et al. (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. doi:10.1038/sj.cdd.4400616. PMID 10713718.
* Liu A, Du W, Liu JP, et al. (2000). "RhoB alteration is necessary for apoptotic and antineoplastic responses to farnesyltransferase inhibitors". Mol. Cell. Biol. 20 (16): 6105–13. doi:10.1128/MCB.20.16.6105-6113.2000. PMC 86086. PMID 10913192.
* Michaelson D, Silletti J, Murphy G, et al. (2001). "Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding". J. Cell Biol. 152 (1): 111–26. doi:10.1083/jcb.152.1.111. PMC 2193662. PMID 11149925.
* 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. doi:10.1073/pnas.111137198. PMC 33444. PMID 11353846.
* 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. doi:10.1074/jbc.M106629200. PMID 11546812.
* Adnane J, Seijo E, Chen Z, et al. (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. doi:10.1074/jbc.M104367200. PMID 11741970.

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PDB gallery

* 2fv8: The crystal structure of RhoB in the GDP-bound state

2fv8: The crystal structure of RhoB in the GDP-bound state

## See also

[edit | edit source]

* neural crest

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Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1|

* Pyrophosphatase
* Inorganic
* Thiamine
* Apyrase
* Thiamine-triphosphatase

3.6.2|

* Adenylylsulfatase
* Phosphoadenylylsulfatase

3.6.3-4: ATPase|

| 3.6.3|

| Cu++ (3.6.3.4)|

* Menkes/ATP7A
* Wilson/ATP7B

|

Ca+ (3.6.3.8)|

* SERCA
* ATP2A1
* ATP2A2
* ATP2A3
* Plasma membrane
* ATP2B1
* ATP2B2
* ATP2B3
* ATP2B4
* SPCA
* ATP2C1
* ATP2C2

Na+/K+ (3.6.3.9)|

* ATP1A1
* ATP1A2
* ATP1A3
* ATP1A4
* ATP1B1
* ATP1B2
* ATP1B3
* ATP1B4

H+/K+ (3.6.3.10)|

* ATP4A

Other P-type ATPase|

* ATP8B1
* ATP10A
* ATP11B
* ATP12A
* ATP13A2
* ATP13A3

3.6.4|

* Dynein
* Kinesin
* Myosin
* Katanin

3.6.5: GTPase|

| 3.6.5.1: Heterotrimeric G protein|

* Gαs
* Gαi
* GNAI1
* GNAI2
* GNAI3
* Gαq/11
* GNAQ
* GNA11
* Gα12/13
* GNA12
* GNA13
* Transducin
* GNAT1
* GNAT2
* Gustducin
* GNAT3

|

3.6.5.2: Small GTPase > Ras superfamily|

* Rho family of GTPases: Cdc42
* CDC42
* TC10
* TCL
* RhoUV
* RhoU
* RhoV
* Rac
* Rac1
* 2
* 3
* RhoG
* RhoBTB
* 1
* 2
* RhoH
* Rho
* A
* B
* C
* Rnd
* 1
* 2
* 3
* RhoDF
* RhoF
* RhoD

* other: Ras
* HRAS
* KRAS
* NRAS
* Rab
* RAB23
* RAB27
* Arf
* ARF6
* SAR1B
* ARL13B
* ARL6
* Ran
* Rheb
* Rap
* RGK

3.6.5.3: Protein-synthesizing GTPase|

* Prokaryotic
* IF-2
* EF-Tu
* EF-G
* Eukaryotic

3.6.5.5-6: Polymerization motors|

* Dynamin
* Tubulin

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Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1|

* Pyrophosphatase
* Inorganic
* Thiamine
* Apyrase
* Thiamine-triphosphatase

3.6.2|

* Adenylylsulfatase
* Phosphoadenylylsulfatase

3.6.3-4: ATPase|

| 3.6.3|

| Cu++ (3.6.3.4)|

* Menkes/ATP7A
* Wilson/ATP7B

|

Ca+ (3.6.3.8)|

* SERCA
* ATP2A1
* ATP2A2
* ATP2A3
* Plasma membrane
* ATP2B1
* ATP2B2
* ATP2B3
* ATP2B4
* SPCA
* ATP2C1
* ATP2C2

Na+/K+ (3.6.3.9)|

* ATP1A1
* ATP1A2
* ATP1A3
* ATP1A4
* ATP1B1
* ATP1B2
* ATP1B3
* ATP1B4

H+/K+ (3.6.3.10)|

* ATP4A

Other P-type ATPase|

* ATP8B1
* ATP10A
* ATP11B
* ATP12A
* ATP13A2
* ATP13A3

3.6.4|

* Dynein
* Kinesin
* Myosin
* Katanin

3.6.5: GTPase|

| 3.6.5.1: Heterotrimeric G protein|

* Gαs
* Gαi
* GNAI1
* GNAI2
* GNAI3
* Gαq/11
* GNAQ
* GNA11
* Gα12/13
* GNA12
* GNA13
* Transducin
* GNAT1
* GNAT2
* Gustducin
* GNAT3

|

3.6.5.2: Small GTPase > Ras superfamily|

* Rho family of GTPases: Cdc42
* CDC42
* TC10
* TCL
* RhoUV
* RhoU
* RhoV
* Rac
* Rac1
* 2
* 3
* RhoG
* RhoBTB
* 1
* 2
* RhoH
* Rho
* A
* B
* C
* Rnd
* 1
* 2
* 3
* RhoDF
* RhoF
* RhoD

* other: Ras
* HRAS
* KRAS
* NRAS
* Rab
* RAB23
* RAB27
* Arf
* ARF6
* SAR1B
* ARL13B
* ARL6
* Ran
* Rheb
* Rap
* RGK

3.6.5.3: Protein-synthesizing GTPase|

* Prokaryotic
* IF-2
* EF-Tu
* EF-G
* Eukaryotic

3.6.5.5-6: Polymerization motors|

* Dynamin
* Tubulin

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