RHOQ

Rho-related GTP-binding protein RhoQ is a protein that in humans is encoded by the RHOQ gene.

RHOQ
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2ATX
Identifiers
Aliases	RHOQ, ARHQ, HEL-S-42, RASL7A, TC10, TC10A, ras homolog family member Q
External IDs	OMIM: 605857; MGI: 1931553; HomoloGene: 22704; GeneCards: RHOQ; OMA:RHOQ - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2p21 Start 46,541,806 bp End 46,584,688 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17 E4|17 56.9 cM Start 87,270,510 bp End 87,307,497 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in myocardium of left ventricle right ventricle Achilles tendon Skeletal muscle tissue of biceps brachii Skeletal muscle tissue of rectus abdominis vastus lateralis muscle thoracic diaphragm cardiac muscle tissue of right atrium Epithelium of choroid plexus muscle of thigh Top expressed in parotid gland lacrimal gland submandibular gland sternocleidomastoid muscle temporal muscle triceps brachii muscle vastus lateralis muscle ankle digastric muscle atrioventricular valve More reference expression data BioGPS More reference expression data
Gene ontology Molecular function GBD domain binding profilin binding nucleotide binding GTP binding GTPase activity protein kinase binding Cellular component cytoplasm cytosol membrane plasma membrane actin filament membrane raft Golgi-associated vesicle membrane extracellular exosome intracellular anatomical structure cell cortex cell projection Biological process positive regulation of glucose import insulin receptor signaling pathway regulation of actin cytoskeleton organization regulation of cell shape cellular response to insulin stimulus regulation of small GTPase mediated signal transduction cortical actin cytoskeleton organization positive regulation of filopodium assembly positive regulation of transcription by RNA polymerase II GTP metabolic process small GTPase mediated signal transduction negative regulation of protein localization to plasma membrane endocytosis actin filament organization establishment or maintenance of cell polarity Rho protein signal transduction cell projection assembly actin cytoskeleton organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23433 104215 Ensembl ENSG00000119729 ENSMUSG00000024143 UniProt P17081 Q8R527 RefSeq (mRNA) NM_012249 NM_145491 RefSeq (protein) NP_036381 NP_663466 Location (UCSC) Chr 2: 46.54 – 46.58 Mb Chr 17: 87.27 – 87.31 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

TC10 is a member of the RAS superfamily of small GTP-binding proteins (see HRAS, MIM 190020) involved in insulin-stimulated glucose uptake.[supplied by OMIM]

In melanocytic cells RHOQ gene expression may be regulated by MITF.

Interactions

RHOQ has been shown to interact with EXOC7, GOPC, PARD6B, WASL, CDC42EP2, TRIP10 and CDC42EP3.

Further reading

• Murphy GA, Solski PA, Jillian SA, et al. (1999). "Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth". Oncogene. 18 (26): 3831–45. doi:10.1038/sj.onc.1202758. PMID 10445846. S2CID 13589258.
• Joberty G, Perlungher RR, Macara IG (2000). "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins". Mol. Cell. Biol. 19 (10): 6585–97. doi:10.1128/MCB.19.10.6585. PMC 84628. PMID 10490598.
• Joberty G, Petersen C, Gao L, Macara IG (2000). "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42". Nat. Cell Biol. 2 (8): 531–9. doi:10.1038/35019573. PMID 10934474. S2CID 27139234.
• Vignal E, De Toledo M, Comunale F, et al. (2000). "Characterization of TCL, a new GTPase of the rho family related to TC10 andCcdc42". J. Biol. Chem. 275 (46): 36457–64. doi:10.1074/jbc.M003487200. PMID 10967094.
• 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.
• Neudauer CL, Joberty G, Macara IG (2001). "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10". Biochem. Biophys. Res. Commun. 280 (2): 541–7. doi:10.1006/bbrc.2000.4160. PMID 11162552.
• Chiang SH, Hou JC, Hwang J, et al. (2002). "Cloning and functional characterization of related TC10 isoforms, a subfamily of Rho proteins involved in insulin-stimulated glucose transport". J. Biol. Chem. 277 (15): 13067–73. doi:10.1074/jbc.M109471200. PMID 11821390.
• Kanzaki M, Watson RT, Hou JC, et al. (2003). "Small GTP-binding protein TC10 differentially regulates two distinct populations of filamentous actin in 3T3L1 adipocytes". Mol. Biol. Cell. 13 (7): 2334–46. doi:10.1091/mbc.01-10-0490. PMC 117317. PMID 12134073.
• Chang L, Adams RD, Saltiel AR (2002). "The TC10-interacting protein CIP4/2 is required for insulin-stimulated Glut4 translocation in 3T3L1 adipocytes". Proc. Natl. Acad. Sci. U.S.A. 99 (20): 12835–40. Bibcode:2002PNAS...9912835C. doi:10.1073/pnas.202495599. PMC 130546. PMID 12242347.
• Abe T, Kato M, Miki H, et al. (2003). "Small GTPase Tc10 and its homologue RhoT induce N-WASP-mediated long process formation and neurite outgrowth". J. Cell Sci. 116 (Pt 1): 155–68. doi:10.1242/jcs.00208. PMID 12456725. S2CID 26953137.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Heilig R, Eckenberg R, Petit JL, et al. (2003). "The DNA sequence and analysis of human chromosome 14". Nature. 421 (6923): 601–7. Bibcode:2003Natur.421..601H. doi:10.1038/nature01348. PMID 12508121.
• Watson RT, Furukawa M, Chiang SH, et al. (2003). "The exocytotic trafficking of TC10 occurs through both classical and nonclassical secretory transport pathways in 3T3L1 adipocytes". Mol. Cell. Biol. 23 (3): 961–74. doi:10.1128/MCB.23.3.961-974.2003. PMC 140699. PMID 12529401.
• Inoue M, Chang L, Hwang J, et al. (2003). "The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin" (PDF). Nature. 422 (6932): 629–33. Bibcode:2003Natur.422..629I. doi:10.1038/nature01533. hdl:2027.42/62982. PMID 12687004. S2CID 4395760.
• Chunqiu Hou J, Pessin JE (2004). "Lipid Raft targeting of the TC10 amino terminal domain is responsible for disruption of adipocyte cortical actin". Mol. Biol. Cell. 14 (9): 3578–91. doi:10.1091/mbc.E03-01-0012. PMC 196551. PMID 12972548.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Ng Y, Tan I, Lim L, Leung T (2004). "Expression of the human myotonic dystrophy kinase-related Cdc42-binding kinase gamma is regulated by promoter DNA methylation and Sp1 binding". J. Biol. Chem. 279 (33): 34156–64. doi:10.1074/jbc.M405252200. PMID 15194684.
• Ruusala A, Aspenström P (2004). "Isolation and characterisation of DOCK8, a member of the DOCK180-related regulators of cell morphology". FEBS Lett. 572 (1–3): 159–66. doi:10.1016/j.febslet.2004.06.095. PMID 15304341. S2CID 9107914.
• Nalbant P, Hodgson L, Kraynov V, et al. (2004). "Activation of endogenous Cdc42 visualized in living cells". Science. 305 (5690): 1615–9. Bibcode:2004Sci...305.1615N. doi:10.1126/science.1100367. PMID 15361624. S2CID 42166147.