Full text data of RHOG
RHOG
(ARHG)
[Confidence: high (present in two of the MS resources)]
Rho-related GTP-binding protein RhoG; Flags: Precursor
Rho-related GTP-binding protein RhoG; Flags: Precursor
UniProt
P84095
ID RHOG_HUMAN Reviewed; 191 AA.
AC P84095; P35238; Q8NI04;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Rho-related GTP-binding protein RhoG;
DE Flags: Precursor;
GN Name=RHOG; Synonyms=ARHG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1620121;
RA Vincent S., Jeanteur P., Fort P.;
RT "Growth-regulated expression of rhoG, a new member of the ras homolog
RT gene family.";
RL Mol. Cell. Biol. 12:3138-3148(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8464478; DOI=10.1038/362462a0;
RA Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.;
RT "Oncogene ect2 is related to regulators of small GTP-binding
RT proteins.";
RL Nature 362:462-465(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH ARHGEF26, AND FUNCTION.
RX PubMed=15133129; DOI=10.1091/mbc.E04-02-0146;
RA Ellerbroek S.M., Wennerberg K., Arthur W.T., Dunty J.M., Bowman D.R.,
RA DeMali K.A., Der C., Burridge K.;
RT "SGEF, a RhoG guanine nucleotide exchange factor that stimulates
RT macropinocytosis.";
RL Mol. Biol. Cell 15:3309-3319(2004).
RN [5]
RP FUNCTION.
RX PubMed=17074883; DOI=10.1083/jcb.200605144;
RA Patel J.C., Galan J.E.;
RT "Differential activation and function of Rho GTPases during
RT Salmonella-host cell interactions.";
RL J. Cell Biol. 175:453-463(2006).
RN [6]
RP FUNCTION.
RX PubMed=17875742; DOI=10.1083/jcb.200612053;
RA van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E.,
RA Garcia-Mata R., Burridge K.;
RT "RhoG regulates endothelial apical cup assembly downstream from ICAM1
RT engagement and is involved in leukocyte trans-endothelial migration.";
RL J. Cell Biol. 178:1279-1293(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH ARHGEF16.
RX PubMed=20679435; DOI=10.1083/jcb.201005141;
RA Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S.,
RA Negishi M., Katoh H.;
RT "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent
RT mechanism.";
RL J. Cell Biol. 190:461-477(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Required for the formation of membrane ruffles during
CC macropinocytosis. Plays a role in cell migration and is required
CC for the formation of cup-like structures during trans-endothelial
CC migration of leukocytes. In case of Salmonella enterica infection,
CC activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton
CC rearrangements and promotes bacterial entry.
CC -!- SUBUNIT: Interacts with ARHGEF26. Interacts with ARHGEF16.
CC -!- INTERACTION:
CC Q92556:ELMO1; NbExp=3; IntAct=EBI-446579, EBI-346417;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L11317; AAA60268.1; -; mRNA.
DR EMBL; X61587; CAA43784.1; -; mRNA.
DR EMBL; AF498974; AAM21121.1; -; mRNA.
DR EMBL; AY563952; AAS75333.1; -; mRNA.
DR PIR; S25722; TVHURG.
DR RefSeq; NP_001656.2; NM_001665.3.
DR RefSeq; XP_005252973.1; XM_005252916.1.
DR UniGene; Hs.501728; -.
DR ProteinModelPortal; P84095; -.
DR SMR; P84095; 1-177.
DR IntAct; P84095; 2.
DR MINT; MINT-4132365; -.
DR STRING; 9606.ENSP00000339467; -.
DR PhosphoSite; P84095; -.
DR DMDM; 51338611; -.
DR PaxDb; P84095; -.
DR PeptideAtlas; P84095; -.
DR PRIDE; P84095; -.
DR DNASU; 391; -.
DR Ensembl; ENST00000351018; ENSP00000339467; ENSG00000177105.
DR Ensembl; ENST00000396978; ENSP00000380175; ENSG00000177105.
DR Ensembl; ENST00000396979; ENSP00000380176; ENSG00000177105.
DR Ensembl; ENST00000533217; ENSP00000436932; ENSG00000177105.
DR GeneID; 391; -.
DR KEGG; hsa:391; -.
DR UCSC; uc001lyu.2; human.
DR CTD; 391; -.
DR GeneCards; GC11M003848; -.
DR HGNC; HGNC:672; RHOG.
DR HPA; HPA039871; -.
DR MIM; 179505; gene.
DR neXtProt; NX_P84095; -.
DR PharmGKB; PA24955; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233974; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P84095; -.
DR KO; K07863; -.
DR OMA; DLREDRH; -.
DR OrthoDB; EOG764747; -.
DR PhylomeDB; P84095; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; RHOG; human.
DR GeneWiki; RhoG; -.
DR GenomeRNAi; 391; -.
DR NextBio; 1631; -.
DR PRO; PR:P84095; -.
DR ArrayExpress; P84095; -.
DR Bgee; P84095; -.
DR CleanEx; HS_RHOG; -.
DR Genevestigator; P84095; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0032863; P:activation of Rac GTPase activity; IMP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Cell membrane; Complete proteome; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1 188 Rho-related GTP-binding protein RhoG.
FT /FTId=PRO_0000042028.
FT PROPEP 189 191 Removed in mature form (By similarity).
FT /FTId=PRO_0000042029.
FT NP_BIND 10 17 GTP (By similarity).
FT NP_BIND 57 61 GTP (By similarity).
FT NP_BIND 115 118 GTP (By similarity).
FT MOTIF 32 40 Effector region (Potential).
FT MOD_RES 39 39 ADP-ribosylasparagine; by botulinum toxin
FT (By similarity).
FT MOD_RES 188 188 Cysteine methyl ester (By similarity).
FT LIPID 188 188 S-geranylgeranyl cysteine (By
FT similarity).
FT CONFLICT 133 133 G -> S (in Ref. 1; CAA43784).
FT CONFLICT 169 169 F -> L (in Ref. 3; AAM21121).
SQ SEQUENCE 191 AA; 21309 MW; 0C4FE9C54140F499 CRC64;
MQSIKCVVVG DGAVGKTCLL ICYTTNAFPK EYIPTVFDNY SAQSAVDGRT VNLNLWDTAG
QEEYDRLRTL SYPQTNVFVI CFSIASPPSY ENVRHKWHPE VCHHCPDVPI LLVGTKKDLR
AQPDTLRRLK EQGQAPITPQ QGQALAKQIH AVRYLECSAL QQDGVKEVFA EAVRAVLNPT
PIKRGRSCIL L
//
ID RHOG_HUMAN Reviewed; 191 AA.
AC P84095; P35238; Q8NI04;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Rho-related GTP-binding protein RhoG;
DE Flags: Precursor;
GN Name=RHOG; Synonyms=ARHG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1620121;
RA Vincent S., Jeanteur P., Fort P.;
RT "Growth-regulated expression of rhoG, a new member of the ras homolog
RT gene family.";
RL Mol. Cell. Biol. 12:3138-3148(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8464478; DOI=10.1038/362462a0;
RA Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.;
RT "Oncogene ect2 is related to regulators of small GTP-binding
RT proteins.";
RL Nature 362:462-465(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH ARHGEF26, AND FUNCTION.
RX PubMed=15133129; DOI=10.1091/mbc.E04-02-0146;
RA Ellerbroek S.M., Wennerberg K., Arthur W.T., Dunty J.M., Bowman D.R.,
RA DeMali K.A., Der C., Burridge K.;
RT "SGEF, a RhoG guanine nucleotide exchange factor that stimulates
RT macropinocytosis.";
RL Mol. Biol. Cell 15:3309-3319(2004).
RN [5]
RP FUNCTION.
RX PubMed=17074883; DOI=10.1083/jcb.200605144;
RA Patel J.C., Galan J.E.;
RT "Differential activation and function of Rho GTPases during
RT Salmonella-host cell interactions.";
RL J. Cell Biol. 175:453-463(2006).
RN [6]
RP FUNCTION.
RX PubMed=17875742; DOI=10.1083/jcb.200612053;
RA van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E.,
RA Garcia-Mata R., Burridge K.;
RT "RhoG regulates endothelial apical cup assembly downstream from ICAM1
RT engagement and is involved in leukocyte trans-endothelial migration.";
RL J. Cell Biol. 178:1279-1293(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH ARHGEF16.
RX PubMed=20679435; DOI=10.1083/jcb.201005141;
RA Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S.,
RA Negishi M., Katoh H.;
RT "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent
RT mechanism.";
RL J. Cell Biol. 190:461-477(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Required for the formation of membrane ruffles during
CC macropinocytosis. Plays a role in cell migration and is required
CC for the formation of cup-like structures during trans-endothelial
CC migration of leukocytes. In case of Salmonella enterica infection,
CC activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton
CC rearrangements and promotes bacterial entry.
CC -!- SUBUNIT: Interacts with ARHGEF26. Interacts with ARHGEF16.
CC -!- INTERACTION:
CC Q92556:ELMO1; NbExp=3; IntAct=EBI-446579, EBI-346417;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L11317; AAA60268.1; -; mRNA.
DR EMBL; X61587; CAA43784.1; -; mRNA.
DR EMBL; AF498974; AAM21121.1; -; mRNA.
DR EMBL; AY563952; AAS75333.1; -; mRNA.
DR PIR; S25722; TVHURG.
DR RefSeq; NP_001656.2; NM_001665.3.
DR RefSeq; XP_005252973.1; XM_005252916.1.
DR UniGene; Hs.501728; -.
DR ProteinModelPortal; P84095; -.
DR SMR; P84095; 1-177.
DR IntAct; P84095; 2.
DR MINT; MINT-4132365; -.
DR STRING; 9606.ENSP00000339467; -.
DR PhosphoSite; P84095; -.
DR DMDM; 51338611; -.
DR PaxDb; P84095; -.
DR PeptideAtlas; P84095; -.
DR PRIDE; P84095; -.
DR DNASU; 391; -.
DR Ensembl; ENST00000351018; ENSP00000339467; ENSG00000177105.
DR Ensembl; ENST00000396978; ENSP00000380175; ENSG00000177105.
DR Ensembl; ENST00000396979; ENSP00000380176; ENSG00000177105.
DR Ensembl; ENST00000533217; ENSP00000436932; ENSG00000177105.
DR GeneID; 391; -.
DR KEGG; hsa:391; -.
DR UCSC; uc001lyu.2; human.
DR CTD; 391; -.
DR GeneCards; GC11M003848; -.
DR HGNC; HGNC:672; RHOG.
DR HPA; HPA039871; -.
DR MIM; 179505; gene.
DR neXtProt; NX_P84095; -.
DR PharmGKB; PA24955; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233974; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P84095; -.
DR KO; K07863; -.
DR OMA; DLREDRH; -.
DR OrthoDB; EOG764747; -.
DR PhylomeDB; P84095; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; RHOG; human.
DR GeneWiki; RhoG; -.
DR GenomeRNAi; 391; -.
DR NextBio; 1631; -.
DR PRO; PR:P84095; -.
DR ArrayExpress; P84095; -.
DR Bgee; P84095; -.
DR CleanEx; HS_RHOG; -.
DR Genevestigator; P84095; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0032863; P:activation of Rac GTPase activity; IMP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Cell membrane; Complete proteome; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1 188 Rho-related GTP-binding protein RhoG.
FT /FTId=PRO_0000042028.
FT PROPEP 189 191 Removed in mature form (By similarity).
FT /FTId=PRO_0000042029.
FT NP_BIND 10 17 GTP (By similarity).
FT NP_BIND 57 61 GTP (By similarity).
FT NP_BIND 115 118 GTP (By similarity).
FT MOTIF 32 40 Effector region (Potential).
FT MOD_RES 39 39 ADP-ribosylasparagine; by botulinum toxin
FT (By similarity).
FT MOD_RES 188 188 Cysteine methyl ester (By similarity).
FT LIPID 188 188 S-geranylgeranyl cysteine (By
FT similarity).
FT CONFLICT 133 133 G -> S (in Ref. 1; CAA43784).
FT CONFLICT 169 169 F -> L (in Ref. 3; AAM21121).
SQ SEQUENCE 191 AA; 21309 MW; 0C4FE9C54140F499 CRC64;
MQSIKCVVVG DGAVGKTCLL ICYTTNAFPK EYIPTVFDNY SAQSAVDGRT VNLNLWDTAG
QEEYDRLRTL SYPQTNVFVI CFSIASPPSY ENVRHKWHPE VCHHCPDVPI LLVGTKKDLR
AQPDTLRRLK EQGQAPITPQ QGQALAKQIH AVRYLECSAL QQDGVKEVFA EAVRAVLNPT
PIKRGRSCIL L
//
MIM
179505
*RECORD*
*FIELD* NO
179505
*FIELD* TI
*179505 RAS HOMOLOG GENE FAMILY, MEMBER G; RHOG
;;RAS HOMOLOG GENE G;;
ARHG
*FIELD* TX
read more
DESCRIPTION
ARHG is a member of the RAS superfamily of genes, which encode
GTP-binding proteins that act in the pathway of signal transduction and
play a key role in the regulation of cellular functions.
CLONING
Vincent et al. (1992) isolated a new member of the RAS homolog gene
family, ARHG, from hamster and human. The ARHG gene is a late induced
gene, and RNA accumulation is proportional to the strength of the
mitogen used. Phylogenetic studies suggested that it may have diverged
early during evolution.
GENE FUNCTION
Katoh and Negishi (2003) demonstrated that RHO G interacts directly with
ELMO2 (606421) in a GTP-dependent manner and forms a ternary complex
with DOCK180 (601403) to induce activation of RAC1 (602048). The RHO
G-ELMO2-DOCK180 pathway is required for activation of RAC1 and cell
spreading mediated by integrin, as well as for neurite outgrowth induced
by nerve growth factor. Katoh and Negishi (2003) concluded that RHO G
activates RAC1 through ELMO and DOCK180 to control cell morphology.
GENE STRUCTURE
Le Gallic and Fort (1997) determined that the ARHG gene spans 25 kb and
contains only 2 exons with an intervening 20-kb intron. The first exon
is noncoding and 85% GC-rich. The ARHG gene lacks TATA and CAAT boxes,
typical of housekeeping genes.
MAPPING
By fluorescence in situ hybridization on human metaphase chromosomes,
Taviaux et al. (1993) assigned the RHOG gene to 11p15.5-p.15.4. Precise
observations indicated it was located distal to WEE1 (193525).
*FIELD* RF
1. Katoh, H.; Negishi, M.: RhoG activates Rac1 by direct interaction
with the Dock180-binding protein Elmo. Nature 424: 461-464, 2003.
2. le Gallic, L.; Fort, P.: Structure of the human ARHG locus encoding
the Rho/Rac-like RhoG GTPase. Genomics 42: 157-160, 1997.
3. Taviaux, S. A.; Vincent, S.; Fort, P.; Demaille, J. G.: Localization
of ARHG, a member of the RAS homolog gene family, to 11p15.5-11p15.4
by fluorescence in situ hybridization. Genomics 16: 788-790, 1993.
4. Vincent, S.; Jeanteur, P.; Fort, P.: Growth-regulated expression
of rhoG, a new member of the ras homolog gene family. Molec. Cell.
Biol. 12: 3138-3148, 1992.
*FIELD* CN
Ada Hamosh - updated: 7/24/2003
Paul J. Converse - updated: 4/12/2001
*FIELD* CD
Victor A. McKusick: 6/24/1993
*FIELD* ED
alopez: 04/04/2007
tkritzer: 7/25/2003
terry: 7/24/2003
mgross: 4/12/2001
alopez: 8/3/1998
carol: 6/24/1993
*RECORD*
*FIELD* NO
179505
*FIELD* TI
*179505 RAS HOMOLOG GENE FAMILY, MEMBER G; RHOG
;;RAS HOMOLOG GENE G;;
ARHG
*FIELD* TX
read more
DESCRIPTION
ARHG is a member of the RAS superfamily of genes, which encode
GTP-binding proteins that act in the pathway of signal transduction and
play a key role in the regulation of cellular functions.
CLONING
Vincent et al. (1992) isolated a new member of the RAS homolog gene
family, ARHG, from hamster and human. The ARHG gene is a late induced
gene, and RNA accumulation is proportional to the strength of the
mitogen used. Phylogenetic studies suggested that it may have diverged
early during evolution.
GENE FUNCTION
Katoh and Negishi (2003) demonstrated that RHO G interacts directly with
ELMO2 (606421) in a GTP-dependent manner and forms a ternary complex
with DOCK180 (601403) to induce activation of RAC1 (602048). The RHO
G-ELMO2-DOCK180 pathway is required for activation of RAC1 and cell
spreading mediated by integrin, as well as for neurite outgrowth induced
by nerve growth factor. Katoh and Negishi (2003) concluded that RHO G
activates RAC1 through ELMO and DOCK180 to control cell morphology.
GENE STRUCTURE
Le Gallic and Fort (1997) determined that the ARHG gene spans 25 kb and
contains only 2 exons with an intervening 20-kb intron. The first exon
is noncoding and 85% GC-rich. The ARHG gene lacks TATA and CAAT boxes,
typical of housekeeping genes.
MAPPING
By fluorescence in situ hybridization on human metaphase chromosomes,
Taviaux et al. (1993) assigned the RHOG gene to 11p15.5-p.15.4. Precise
observations indicated it was located distal to WEE1 (193525).
*FIELD* RF
1. Katoh, H.; Negishi, M.: RhoG activates Rac1 by direct interaction
with the Dock180-binding protein Elmo. Nature 424: 461-464, 2003.
2. le Gallic, L.; Fort, P.: Structure of the human ARHG locus encoding
the Rho/Rac-like RhoG GTPase. Genomics 42: 157-160, 1997.
3. Taviaux, S. A.; Vincent, S.; Fort, P.; Demaille, J. G.: Localization
of ARHG, a member of the RAS homolog gene family, to 11p15.5-11p15.4
by fluorescence in situ hybridization. Genomics 16: 788-790, 1993.
4. Vincent, S.; Jeanteur, P.; Fort, P.: Growth-regulated expression
of rhoG, a new member of the ras homolog gene family. Molec. Cell.
Biol. 12: 3138-3148, 1992.
*FIELD* CN
Ada Hamosh - updated: 7/24/2003
Paul J. Converse - updated: 4/12/2001
*FIELD* CD
Victor A. McKusick: 6/24/1993
*FIELD* ED
alopez: 04/04/2007
tkritzer: 7/25/2003
terry: 7/24/2003
mgross: 4/12/2001
alopez: 8/3/1998
carol: 6/24/1993