Rnd2

Protein-coding gene in the species Homo sapiens

RND2

Identifiers

Aliases

RND2, ARHN, RHO7, RhoN, Rnd2, Rho family GTPase 2

External IDs

OMIM: 601555 MGI: 1338755 HomoloGene: 21123 GeneCards: RND2

Gene location (Human)

Chr.	Chromosome 17 (human)^[1]

Band	17q21.31	Start	43,025,231 bp^[1]
Band	17q21.31	End	43,032,041 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11\|11 D	Start	101,355,825 bp^[2]
Band	11\|11 D	End	101,362,679 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

internal globus pallidus

hypothalamus

substantia nigra

superior vestibular nucleus

nucleus accumbens

external globus pallidus

ventral tegmental area

pons

putamen

caudate nucleus

Top expressed in

ganglionic eminence

cerebellar cortex

pons

inferior colliculus

medulla oblongata

superior frontal gyrus

superior colliculus

olfactory bulb

placenta

piriform cortex

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	nucleotide binding GTP binding protein binding GTPase activity protein N-terminus binding protein kinase binding
Cellular component	early endosome acrosomal membrane membrane cytoplasmic vesicle intracellular anatomical structure cytoplasm plasma membrane cell cortex cell division site intracellular membrane-bounded organelle
Biological process	small GTPase mediated signal transduction positive regulation of collateral sprouting signal transduction actin filament organization Rho protein signal transduction regulation of cell shape regulation of cell migration establishment or maintenance of actin cytoskeleton polarity regulation of actin cytoskeleton organization actin filament bundle assembly
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


8153


11858

Ensembl


ENSG00000108830


ENSMUSG00000001313

UniProt


P52198


Q9QYM5

RefSeq (mRNA)


NM_005440


NM_009708

RefSeq (protein)


NP_005431


NP_033838

Location (UCSC)

Chr 17: 43.03 – 43.03 Mb

Chr 11: 101.36 – 101.36 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Rnd2 is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rnd subgroup of the Rho family of GTPases.^[5] It is encoded by the gene RND2.^[6]

Function

It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors (Nobes et al., 1998).[supplied by OMIM]^[7]

This particular family member has been implicated in the regulation of neuronal morphology and endosomal trafficking.

Clinical significance

The gene localizes to chromosome 17 and is the centromeric neighbor of the breast-ovarian cancer susceptibility gene BRCA1.^[6]

Interactions

Rnd2 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000108830 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000001313 – 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 (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. ISSN 0962-8924. PMID 16949823.
^ ^a ^b "Entrez Gene: RND2 Rho family GTPase 2".
^ "Entrez Gene: RND1 Rho family GTPase 1".
^ Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH (Jul 2003). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. 13 (13): 1106–15. Bibcode:2003CBio...13.1106W. doi:10.1016/s0960-9822(03)00418-4. PMC 6918695. PMID 12842009.
^ Naud N, Touré A, Liu J, Pineau C, Morin L, Dorseuil O, Escalier D, Chardin P, Gacon G (May 2003). "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells". Biochem. J. 372 (Pt 1): 105–12. doi:10.1042/BJ20021652. PMC 1223378. PMID 12590651.
^ Katoh H, Harada A, Mori K, Negishi M (May 2002). "Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers". Mol. Cell. Biol. 22 (9): 2952–64. doi:10.1128/mcb.22.9.2952-2964.2002. PMC 133765. PMID 11940653.

Chardin P (1991). "Small GTP-binding proteins of the ras family: a conserved functional mechanism?". Cancer Cells. 3 (4): 117–26. PMID 1909153.
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.
Smith TM, Lee MK, Szabo CI, Jerome N, McEuen M, Taylor M, Hood L, King MC (1997). "Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1". Genome Res. 6 (11): 1029–49. doi:10.1101/gr.6.11.1029. PMID 8938427.
Nobes CD, Lauritzen I, Mattei MG, Paris S, Hall A, Chardin P (1998). "A New Member of the Rho Family, Rnd1, Promotes Disassembly of Actin Filament Structures and Loss of Cell Adhesion". J. Cell Biol. 141 (1): 187–97. doi:10.1083/jcb.141.1.187. PMC 2132722. PMID 9531558.
Tanaka H, Fujita H, Katoh H, Mori K, Negishi M (2002). "Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2". Biochem. J. 365 (Pt 2): 349–53. doi:10.1042/BJ20020062. PMC 1222680. PMID 11931639.
Katoh H, Harada A, Mori K, Negishi M (2002). "Socius Is a Novel Rnd GTPase-Interacting Protein Involved in Disassembly of Actin Stress Fibers". Mol. Cell. Biol. 22 (9): 2952–64. doi:10.1128/MCB.22.9.2952-2964.2002. PMC 133765. PMID 11940653.
Fujita H, Katoh H, Ishikawa Y, Mori K, Negishi M (2003). "Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching". J. Biol. Chem. 277 (47): 45428–34. doi:10.1074/jbc.M208090200. PMID 12244061.
Naud N, Touré A, Liu J, Pineau C, Morin L, Dorseuil O, Escalier D, Chardin P, Gacon G (2003). "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells". Biochem. J. 372 (Pt 1): 105–12. doi:10.1042/BJ20021652. PMC 1223378. PMID 12590651.
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 (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Kim YS, Hori M, Yasuda K, Ozaki H (2006). "Differences in the gestational pattern of mRNA expression of the Rnd family in rat and human myometria". Comp. Biochem. Physiol. A. 142 (4): 410–5. doi:10.1016/j.cbpa.2005.08.028. PMID 16311049.
Tanaka H, Katoh H, Negishi M (2006). "Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity". J. Biol. Chem. 281 (15): 10355–64. doi:10.1074/jbc.M511314200. PMID 16481321.

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