[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1620121 [NCBI, ExPASy, EBI, Israel, Japan] Vincent S., Jeanteur P., Fort P.; "Growth-regulated expression of rhoG, a new member of the ras homolog gene family."; Mol. Cell. Biol. 12:3138-3148(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1038/362462a0; PubMed=8464478 [NCBI, ExPASy, EBI, Israel, Japan] Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.; "Oncogene ect2 is related to regulators of small GTP-binding proteins."; Nature 362:462-465(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; Puhl H.L. III, Ikeda S.R., Aronstam R.S.; "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."; Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[4]	INTERACTION WITH SGEF, AND FUNCTION. DOI=10.1091/mbc.E04-02-0146; PubMed=15133129 [NCBI, ExPASy, EBI, Israel, Japan] Ellerbroek S.M., Wennerberg K., Arthur W.T., Dunty J.M., Bowman D.R., DeMali K.A., Der C., Burridge K.; "SGEF, a RhoG guanine nucleotide exchange factor that stimulates macropinocytosis."; Mol. Biol. Cell 15:3309-3319(2004).
[5]	FUNCTION. DOI=10.1083/jcb.200605144; PubMed=17074883 [NCBI, ExPASy, EBI, Israel, Japan] Patel J.C., Galan J.E.; "Differential activation and function of Rho GTPases during Salmonella-host cell interactions."; J. Cell Biol. 175:453-463(2006).
[6]	FUNCTION. DOI=10.1083/jcb.200612053; PubMed=17875742 [NCBI, ExPASy, EBI, Israel, Japan] van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E., Garcia-Mata R., Burridge K.; "RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration."; J. Cell Biol. 178:1279-1293(2007).

Comments

FUNCTION: Required for the formation of membrane ruffles during macropinocytosis. Required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB and SGEF, which induces cytoskeleton rearrangements and promotes bacterial entry.
SUBUNIT: Interacts with SGEF.
INTERACTION:
Q92556:ELMO1; NbExp=2; IntAct=EBI-446579, EBI-346417;
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side (Potential).
SIMILARITY: Belongs to the small GTPase superfamily. Rho family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L11317; AAA60268.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X61587; CAA43784.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF498974; AAM21121.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY563952; AAS75333.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S25722; TVHURG.

NP_001656.2; -.

3D structure databases

HSSP

P21181; 1AM4. [HSSP ENTRY / PDB]

SMR

P84095; 1-177.

ModBase

P84095.

Protein-protein interaction databases

IntAct

P84095; -.

Enzyme and pathway databases

Reactome

REACT_11044; Signaling by Rho GTPases.

Organism-specific databases

HIX0035905; -.

HGNC:672; RHOG.

179505; gene. [NCBI / EBI]

PharmGKB

PA24955; -.

GeneCards

P84095.

Gene expression databases

CleanEx

HS_RHOG; -.

GermOnline

ENSG00000177105; Homo sapiens.

Ontologies

GO:0003924;	Molecular function: GTPase activity (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008284;	Biological process: positive regulation of cell proliferation (traceable author statement from ProtInc).
GO:0007266;	Biological process: Rho protein signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR003578; GTPase_Rho.
IPR013753; Ras.
IPR001806; Ras_trnsfrmng.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.

Pfam

PF00071; Ras; 1.
Pfam graphical view of domain structure.

PRINTS

PR00449; RASTRNSFRMNG.

SMART

SM00174; RHO; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00231; small_GTP; 1.

BLOCKS

P84095.

Proteomic databases

PeptideAtlas

P84095; -.

Genome annotation databases

Ensembl

ENSG00000177105; Homo sapiens. [Contig view]

GeneID

391; -.

KEGG

hsa:391; -.

Phylogenomic databases

HOGENOM

P84095; -.

HOVERGEN

P84095; -.

Other

P84095; -.

RHOG; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ADP-ribosylation; Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 188`	`188`	`Rho-related GTP-binding protein RhoG.`	`PRO_0000042028`
`PROPEP`	`189 191`	`3`	`Removed in mature form (By similarity).`	`PRO_0000042029`
`NP_BIND`	`10 17`	`8`	`GTP (By similarity).`
`NP_BIND`	`57 61`	`5`	`GTP (By similarity).`
`NP_BIND`	`115 118`	`4`	`GTP (By similarity).`
`MOTIF`	`32 40`	`9`	`Effector region (Potential).`
`MOD_RES`	`39 39`		`ADP-ribosylasparagine; by botulinum toxin (By similarity).`
`MOD_RES`	`188 188`		`Cysteine methyl ester (By similarity).`
`LIPID`	`188 188`		`S-geranylgeranyl cysteine (By similarity).`
`CONFLICT`	`133 133`		`G -> S (in Ref. 1; CAA43784).`
`CONFLICT`	`169 169`		`F -> L (in Ref. 3; AAM21121).`

Sequence information

Length: 191 AA [This is the length of the unprocessed precursor]

Molecular weight: 21309 Da [This is the MW of the unprocessed precursor]

CRC64: 0C4FE9C54140F499 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQSIKCVVVG DGAVGKTCLL ICYTTNAFPK EYIPTVFDNY SAQSAVDGRT VNLNLWDTAG 

        70         80         90        100        110        120 
QEEYDRLRTL SYPQTNVFVI CFSIASPPSY ENVRHKWHPE VCHHCPDVPI LLVGTKKDLR 

       130        140        150        160        170        180 
AQPDTLRRLK EQGQAPITPQ QGQALAKQIH AVRYLECSAL QQDGVKEVFA EAVRAVLNPT 

       190 
PIKRGRSCIL L

P84095 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools