RhoH

RHOH
Identifiers
Aliases	RHOH, ARHH, TTF, RhoH, ras homolog family member H
External IDs	OMIM: 602037 MGI: 1921984 HomoloGene: 3180 GeneCards: RHOH
Gene location (Human)
Chr.	Chromosome 4 (human)[1]
End	40,246,967 bp[1]
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)[2]
End	65,896,700 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• GTPase inhibitor activity; • nucleotide binding; • Rho GTPase binding; • GTP binding; • kinase inhibitor activity; • GO:0001948 protein binding; • GTPase activity; • protein kinase binding;
Cellular component	• cytosol; • cell membrane; • cytoplasm; • membrane; • immunological synapse; • intracellular; • cell cortex; • cell projection;
Biological process	• regulation of small GTPase mediated signal transduction; • regulation of transcription, DNA-templated; • negative regulation of I-kappaB kinase/NF-kappaB signaling; • mast cell activation; • T cell differentiation; • negative regulation of phosphorylation; • GO:0034259 negative regulation of GTPase activity; • small GTPase mediated signal transduction; • actin filament organization; • establishment or maintenance of cell polarity; • Rho protein signal transduction; • regulation of cell shape; • actin cytoskeleton organization; • negative regulation of kinase activity; • regulation of actin cytoskeleton organization;
	Sources:Amigo / QuickGO
Orthologs
	399
	74734
	ENSG00000168421
	ENSMUSG00000029204
	Q15669
	Q9D3G9
NM_001278359; NM_001278360; NM_001278361; NM_001278362; NM_001278363;
	NM_001278364; NM_001278365; NM_001278366; NM_001278367; NM_001278368; NM_001278369; NM_004310
	NM_001081105; NM_001363454
NP_001265288; NP_001265289; NP_001265290; NP_001265291; NP_001265292;
	NP_001265293; NP_001265294; NP_001265295; NP_001265296; NP_001265297; NP_001265298; NP_004301
	NP_001074574; NP_001350383
	Wikidata
View/Edit Human	View/Edit Mouse

RhoH (Ras homolog gene family, member H) is a small (~21 kDa) signaling G protein (more specifically a GTPase), and is a member of the Rac subfamily of the family Rho family of GTPases.[5] It is encoded by the gene RHOH.[6]

Gene

Expression of a chimeric transcript of LAZ3 and this gene has been reported as a result of the translocation t(3;4) in non-Hodgkin's lymphomas. Unlike most other small G proteins which are expressed ubiquitously, this gene is transcribed only in hemopoietic cells.[6]

Interactions

RhoH has been shown to interact with ARHGDIA.[7][8]

References

GRCh38: Ensembl release 89: ENSG00000168421 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000029204 - 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.
Ridley AJ (October 2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends in Cell Biology. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
"Entrez Gene: RHOH ras homolog gene family, member H".
Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (February 2002). "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function". Molecular and Cellular Biology. 22 (4): 1158–71. doi:10.1128/MCB.22.4.1158-1171.2002. PMC 134637. PMID 11809807.
Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. doi:10.1016/S0300-9084(01)01263-9. PMID 11368848.

Dallery E, Galiègue-Zouitina S, Collyn-d'Hooghe M, Quief S, Denis C, Hildebrand MP, Lantoine D, Deweindt C, Tilly H, Bastard C (June 1995). "TTF, a gene encoding a novel small G protein, fuses to the lymphoma-associated LAZ3 gene by t(3;4) chromosomal translocation". Oncogene. 10 (11): 2171–8. PMID 7784061.
Dallery-Prudhomme E, Roumier C, Denis C, Preudhomme C, Kerckaert JP, Galiegue-Zouitina S (July 1997). "Genomic structure and assignment of the RhoH/TTF small GTPase gene (ARHH) to 4p13 by in situ hybridization". Genomics. 43 (1): 89–94. doi:10.1006/geno.1997.4788. PMID 9226377.
Yousefi S, Cooper PR, Mueck B, Potter SL, Jarai G (October 2000). "cDNA representational difference analysis of human neutrophils stimulated by GM-CSF". Biochemical and Biophysical Research Communications. 277 (2): 401–9. doi:10.1006/bbrc.2000.3678. PMID 11032736.
Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. doi:10.1016/S0300-9084(01)01263-9. PMID 11368848.
Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (February 2002). "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function". Molecular and Cellular Biology. 22 (4): 1158–71. doi:10.1128/MCB.22.4.1158-1171.2002. PMC 134637. PMID 11809807.
Lahousse S, Smorowski AL, Denis C, Lantoine D, Kerckaert JP, Galiègue-Zouitina S (December 2004). "Structural features of hematopoiesis-specific RhoH/ARHH gene: high diversity of 5'-UTR in different hematopoietic lineages suggests a complex post-transcriptional regulation". Gene. 343 (1): 55–68. doi:10.1016/j.gene.2004.08.022. PMID 15563831.
Lopez-Ilasaca MA, Bernabe-Ortiz JC, Na SY, Dzau VJ, Xavier RJ (January 2005). "Bioluminescence resonance energy transfer identify scaffold protein CNK1 interactions in intact cells". FEBS Letters. 579 (3): 648–54. doi:10.1016/j.febslet.2004.12.039. PMID 15670823. S2CID 34302075.
Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (March 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Reiniger L, Bödör C, Bognár A, Balogh Z, Csomor J, Szepesi A, Kopper L, Matolcsy A (June 2006). "Richter's and prolymphocytic transformation of chronic lymphocytic leukemia are associated with high mRNA expression of activation-induced cytidine deaminase and aberrant somatic hypermutation". Leukemia. 20 (6): 1089–95. doi:10.1038/sj.leu.2404183. PMID 16541139.
Hiraga J, Katsumi A, Iwasaki T, Abe A, Kiyoi H, Matsushita T, Kinoshita T, Naoe T (August 2007). "Prognostic analysis of aberrant somatic hypermutation of RhoH gene in diffuse large B cell lymphoma". Leukemia. 21 (8): 1846–7. doi:10.1038/sj.leu.2404717. PMID 17443219.
Traverse-Glehen A, Verney A, Baseggio L, Felman P, Callet-Bauchu E, Thieblemont C, Ffrench M, Magaud JP, Coiffier B, Berger F, Salles G (August 2007). "Analysis of BCL-6, CD95, PIM1, RHO/TTF and PAX5 mutations in splenic and nodal marginal zone B-cell lymphomas suggests a particular B-cell origin". Leukemia. 21 (8): 1821–4. doi:10.1038/sj.leu.2404706. PMID 17476282.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000168421 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000029204 - 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.

[Ridley-5] Ridley AJ (October 2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends in Cell Biology. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.

[entrez-6] "Entrez Gene: RHOH ras homolog gene family, member H".

[pmid11809807-7] Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (February 2002). "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function". Molecular and Cellular Biology. 22 (4): 1158–71. doi:10.1128/MCB.22.4.1158-1171.2002. PMC 134637. PMID 11809807.

[pmid11368848-8] Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. doi:10.1016/S0300-9084(01)01263-9. PMID 11368848.

RhoH

Gene

Interactions

References

Further reading