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RHOD
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2J1L
Identifiers
Aliases	RHOD, ARHD, RHOHP1, RHOM, Rho, RhoD, ras homolog family member D
External IDs	OMIM: 605781; MGI: 108446; HomoloGene: 22409; GeneCards: RHOD; OMA:RHOD - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	67,072,017 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	4,489,460 bp
RNA expression pattern
	Top expressed in
	pancreatic ductal cell; ; right lobe of liver; ; apex of heart; ; skin of leg; ; skin of abdomen; ; gums; ; gingival epithelium; ; left ventricle; ; skin of thigh; ; amniotic fluid;
	Top expressed in
	saccule; ; otic placode; ; otic vesicle; ; lip; ; esophagus; ; corneal stroma; ; choroid plexus of fourth ventricle; ; right kidney; ; jejunum; ; duodenum;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; protein kinase binding; GTP binding; GTPase activity;
Cellular component	early endosome; endosome membrane; endosome; membrane; cytosol; plasma membrane; intracellular anatomical structure; cytoplasm; cell cortex; cell division site; intracellular membrane-bounded organelle;
Biological process	positive regulation of cell adhesion; focal adhesion assembly; actin filament bundle assembly; regulation of actin cytoskeleton reorganization; positive regulation of cell migration; lamellipodium assembly; Rho protein signal transduction; regulation of focal adhesion assembly; protein targeting; regulation of small GTPase mediated signal transduction; small GTPase mediated signal transduction; actin filament organization; regulation of cell shape; cell migration; regulation of cell migration; establishment or maintenance of actin cytoskeleton polarity; regulation of actin cytoskeleton organization;
	Sources:Amigo / QuickGO
Orthologs
	29984
	11854
	ENSG00000173156
	ENSMUSG00000041845
	O00212
	P97348
	NM_014578; NM_001300886
	NM_007485; NM_001329989
	NP_001287815; NP_055393
	NP_001316918; NP_031511
	Wikidata
View/Edit Human	View/Edit Mouse

RhoD (Ras homolog gene family, member D) 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 RHOD.^[6]

It binds GTP and is involved in endosome dynamics and reorganization of the actin cytoskeleton, and it may coordinate membrane transport with the function of the cytoskeleton.^[6]^[7]

Interactions

RhoD has been shown to interact with CNKSR1^[8] and DIAPH2.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000173156 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000041845 – 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): 522–529. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
^ ^a ^b "Entrez Gene: RHOD ras homolog gene family, member D".
^ Nehru V, Voytyuk O, Lennartsson J, Aspenström P (December 2013). "RhoD binds the Rab5 effector Rabankyrin-5 and has a role in trafficking of the platelet-derived growth factor receptor". Traffic. 14 (12): 1242–1254. doi:10.1111/tra.12121. PMID 24102721. S2CID 3416403.
^ Jaffe AB, Aspenström P, Hall A (February 2004). "Human CNK1 acts as a scaffold protein, linking Rho and Ras signal transduction pathways". Molecular and Cellular Biology. 24 (4): 1736–1746. doi:10.1128/MCB.24.4.1736-1746.2004. PMC 344169. PMID 14749388.
^ Gasman S, Kalaidzidis Y, Zerial M (March 2003). "RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase". Nature Cell Biology. 5 (3): 195–204. doi:10.1038/ncb935. PMID 12577064. S2CID 17891748.

Ridley AJ (May 2001). "Rho proteins: linking signaling with membrane trafficking". Traffic. 2 (5): 303–310. doi:10.1034/j.1600-0854.2001.002005303.x. PMID 11350626. S2CID 37763952.
Shimizu F, Watanabe TK, Okuno S, Omori Y, Fujiwara T, Takahashi E, Nakamura Y (March 1997). "Isolation of a novel human cDNA (rhoHP1) homologous to rho genes". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1351 (1–2): 13–16. doi:10.1016/s0167-4781(97)00008-0. PMID 9116026.
Kim HS, Choi JY, Jung AR, Jang KL, Lee WH, Choi WC, et al. (2000). "Assignment of the human RhoHP1 gene (ARHD) to chromosome 11q14.3 by radiation hybrid mapping". Cytogenetics and Cell Genetics. 89 (1–2): 53. doi:10.1159/000015562. PMID 10894936. S2CID 84584317.
Murphy C, Saffrich R, Olivo-Marin JC, Giner A, Ansorge W, Fotsis T, Zerial M (June 2001). "Dual function of rhoD in vesicular movement and cell motility". European Journal of Cell Biology. 80 (6): 391–398. doi:10.1078/0171-9335-00173. PMID 11484930.
Zanata SM, Hovatta I, Rohm B, Püschel AW (January 2002). "Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse". The Journal of Neuroscience. 22 (2): 471–477. doi:10.1523/JNEUROSCI.22-02-00471.2002. PMC 6758682. PMID 11784792.
Gasman S, Kalaidzidis Y, Zerial M (March 2003). "RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase". Nature Cell Biology. 5 (3): 195–204. doi:10.1038/ncb935. PMID 12577064. S2CID 17891748.
Jaffe AB, Aspenström P, Hall A (February 2004). "Human CNK1 acts as a scaffold protein, linking Rho and Ras signal transduction pathways". Molecular and Cellular Biology. 24 (4): 1736–1746. doi:10.1128/MCB.24.4.1736-1746.2004. PMC 344169. PMID 14749388.
Flaxenburg JA, Melter M, Lapchak PH, Briscoe DM, Pal S (June 2004). "The CD40-induced signaling pathway in endothelial cells resulting in the overexpression of vascular endothelial growth factor involves Ras and phosphatidylinositol 3-kinase". Journal of Immunology. 172 (12): 7503–7509. doi:10.4049/jimmunol.172.12.7503. PMID 15187129.
Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, et al. (March 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–1625. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
Birukova AA, Chatchavalvanich S, Rios A, Kawkitinarong K, Garcia JG, Birukov KG (May 2006). "Differential regulation of pulmonary endothelial monolayer integrity by varying degrees of cyclic stretch". The American Journal of Pathology. 168 (5): 1749–1761. doi:10.2353/ajpath.2006.050431. PMC 1606576. PMID 16651639.
Ito Y, Kanamaru A, Tada A (March 2007). "A novel agent, methylophiopogonanone B, promotes Rho activation and tubulin depolymerization". Molecular and Cellular Biochemistry. 297 (1–2): 121–129. doi:10.1007/s11010-006-9336-y. PMID 17029007. S2CID 33688226.
Tan W, Martin D, Gutkind JS (December 2006). "The Galpha13-Rho signaling axis is required for SDF-1-induced migration through CXCR4". The Journal of Biological Chemistry. 281 (51): 39542–39549. doi:10.1074/jbc.M609062200. PMID 17056591.
Lakshman N, Kim A, Bayless KJ, Davis GE, Petroll WM (June 2007). "Rho plays a central role in regulating local cell-matrix mechanical interactions in 3D culture". Cell Motility and the Cytoskeleton. 64 (6): 434–445. doi:10.1002/cm.20194. PMID 17342762.