RHOD

Available structures

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

Gene location (Human)

Chr.	Chromosome 11 (human)^[1]

Band	11q13.2	Start	67,056,847 bp^[1]
Band	11q13.2	End	67,072,017 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 19 (mouse)^[2]

Band	19\|19 A	Start	4,475,487 bp^[2]
Band	19\|19 A	End	4,489,460 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

pancreatic ductal cell

right lobe of liver

skin of abdomen

gums

left ventricle

amniotic fluid

oral cavity

periodontal fiber

right coronary artery

epithelium of esophagus

Top expressed in

saccule

otic placode

lip

esophagus

corneal stroma

jejunum

duodenum

yolk sac

intestinal villus

pyloric antrum

More reference expression data

BioGPS


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

Species

Human

Mouse

Entrez


29984


11854

Ensembl


ENSG00000173156


ENSMUSG00000041845

UniProt


O00212


P97348

RefSeq (mRNA)


NM_014578 NM_001300886


NM_007485 NM_001329989

RefSeq (protein)


NP_001287815 NP_055393


NP_001316918 NP_031511

Location (UCSC)

Chr 11: 67.06 – 67.07 Mb

Chr 19: 4.48 – 4.49 Mb

PubMed search

^[3]

^[4]

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

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.

v t e PDB gallery
2j1l: CRYSTAL STRUCTURE OF HUMAN RHO-RELATED GTP-BINDING PROTEIN RHOD

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

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

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_olf G_αi GNAI1 GNAI2 GNAI3 Transducin GNAT1 GNAT2 Gustducin GNAT3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13
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 superfamily Dynamin Guanylate-binding protein Mitofusin-1 MX1 and MX2 OPA1 Tubulin

Interactions

References

Further reading