RHOG_HUMAN
ID RHOG_HUMAN Reviewed; 191 AA.
AC P84095; P35238; Q8NI04;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 171.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1620121; DOI=10.1128/mcb.12.7.3138-3148.1992;
RA Vincent S., Jeanteur P., Fort P.;
RT "Growth-regulated expression of rhoG, a new member of the ras homolog gene
RT 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 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 sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GLYCOSYLATION AT THR-35 (MICROBIAL INFECTION).
RX PubMed=8810274; DOI=10.1074/jbc.271.41.25173;
RA Selzer J., Hofmann F., Rex G., Wilm M., Mann M., Just I., Aktories K.;
RT "Clostridium novyi alpha-toxin-catalyzed incorporation of GlcNAc into Rho
RT subfamily proteins.";
RL J. Biol. Chem. 271:25173-25177(1996).
RN [5]
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 [6]
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 Salmonella-host
RT cell interactions.";
RL J. Cell Biol. 175:453-463(2006).
RN [7]
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 [8]
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 [9]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND THR-180, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP GLYCOSYLATION AT THR-35 (MICROBIAL INFECTION).
RX PubMed=24905543; DOI=10.1111/cmi.12321;
RA Genth H., Pauillac S., Schelle I., Bouvet P., Bouchier C.,
RA Varela-Chavez C., Just I., Popoff M.R.;
RT "Haemorrhagic toxin and lethal toxin from Clostridium sordellii strain
RT vpi9048: molecular characterization and comparative analysis of substrate
RT specificity of the large clostridial glucosylating toxins.";
RL Cell. Microbiol. 16:1706-1721(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Required for the formation of membrane ruffles during
CC macropinocytosis. Plays a role in cell migration and is required for
CC the formation of cup-like structures during trans-endothelial migration
CC of leukocytes. In case of Salmonella enterica infection, activated by
CC SopB and ARHGEF26/SGEF, which induces cytoskeleton rearrangements and
CC promotes bacterial entry. {ECO:0000269|PubMed:15133129,
CC ECO:0000269|PubMed:17074883, ECO:0000269|PubMed:17875742,
CC ECO:0000269|PubMed:20679435}.
CC -!- SUBUNIT: Interacts with ARHGEF26. Interacts with ARHGEF16.
CC {ECO:0000269|PubMed:15133129, ECO:0000269|PubMed:20679435}.
CC -!- INTERACTION:
CC P84095; Q92556: ELMO1; NbExp=3; IntAct=EBI-446579, EBI-346417;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- PTM: (Microbial infection) Glucosylated at Thr-35 by C.difficile toxin
CC TcdB. {ECO:0000269|PubMed:24905543}.
CC -!- PTM: (Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-35 by
CC C.novyi toxin TcdA (PubMed:8810274). O-GlcNAcylation completely
CC prevents the recognition of the downstream effector, blocking the
CC GTPases in their inactive form, leading to actin cytoskeleton
CC disruption (PubMed:8810274). {ECO:0000269|PubMed:8810274}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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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 CCDS; CCDS7748.1; -.
DR PIR; S25722; TVHURG.
DR RefSeq; NP_001656.2; NM_001665.3.
DR RefSeq; XP_005252973.1; XM_005252916.2.
DR RefSeq; XP_016873208.1; XM_017017719.1.
DR PDB; 6UKA; X-ray; 2.40 A; A=1-191.
DR PDBsum; 6UKA; -.
DR AlphaFoldDB; P84095; -.
DR SMR; P84095; -.
DR BioGRID; 106884; 889.
DR IntAct; P84095; 16.
DR MINT; P84095; -.
DR STRING; 9606.ENSP00000339467; -.
DR iPTMnet; P84095; -.
DR PhosphoSitePlus; P84095; -.
DR SwissPalm; P84095; -.
DR BioMuta; RHOG; -.
DR DMDM; 51338611; -.
DR EPD; P84095; -.
DR jPOST; P84095; -.
DR MassIVE; P84095; -.
DR PaxDb; P84095; -.
DR PeptideAtlas; P84095; -.
DR PRIDE; P84095; -.
DR ProteomicsDB; 57750; -.
DR Antibodypedia; 23440; 201 antibodies from 33 providers.
DR DNASU; 391; -.
DR Ensembl; ENST00000351018.5; ENSP00000339467.4; ENSG00000177105.10.
DR Ensembl; ENST00000396978.1; ENSP00000380175.1; ENSG00000177105.10.
DR Ensembl; ENST00000396979.1; ENSP00000380176.1; ENSG00000177105.10.
DR Ensembl; ENST00000533217.1; ENSP00000436932.1; ENSG00000177105.10.
DR GeneID; 391; -.
DR KEGG; hsa:391; -.
DR MANE-Select; ENST00000351018.5; ENSP00000339467.4; NM_001665.4; NP_001656.2.
DR CTD; 391; -.
DR DisGeNET; 391; -.
DR GeneCards; RHOG; -.
DR HGNC; HGNC:672; RHOG.
DR HPA; ENSG00000177105; Tissue enhanced (bone).
DR MIM; 179505; gene.
DR neXtProt; NX_P84095; -.
DR OpenTargets; ENSG00000177105; -.
DR PharmGKB; PA24955; -.
DR VEuPathDB; HostDB:ENSG00000177105; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000155158; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P84095; -.
DR OMA; DNVASKW; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P84095; -.
DR TreeFam; TF101109; -.
DR PathwayCommons; P84095; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-5625970; RHO GTPases activate KTN1.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; P84095; -.
DR BioGRID-ORCS; 391; 40 hits in 1079 CRISPR screens.
DR ChiTaRS; RHOG; human.
DR GeneWiki; RhoG; -.
DR GenomeRNAi; 391; -.
DR Pharos; P84095; Tbio.
DR PRO; PR:P84095; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P84095; protein.
DR Bgee; ENSG00000177105; Expressed in granulocyte and 201 other tissues.
DR ExpressionAtlas; P84095; baseline and differential.
DR Genevisible; P84095; HS.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:1902622; P:regulation of neutrophil migration; IBA:GO_Central.
DR GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR CDD; cd01875; RhoG; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR042734; RhoG.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
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 3D-structure; ADP-ribosylation; Cell membrane; Glycoprotein; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Rho-related GTP-binding protein RhoG"
FT /id="PRO_0000042028"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042029"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="ADP-ribosylasparagine; by botulinum toxin"
FT /evidence="ECO:0000250"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="(Microbial infection) O-alpha-linked (GlcNAc)
FT threonine; by C.novyi toxin TcdA; alternate"
FT /evidence="ECO:0000269|PubMed:8810274"
FT CARBOHYD 35
FT /note="(Microbial infection) O-linked (Glc) threonine; by
FT C.difficile toxin TcdB; alternate"
FT /evidence="ECO:0000269|PubMed:24905543"
FT CONFLICT 133
FT /note="G -> S (in Ref. 1; CAA43784)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="F -> L (in Ref. 3; AAM21121)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:6UKA"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:6UKA"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:6UKA"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:6UKA"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:6UKA"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6UKA"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:6UKA"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:6UKA"
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
