Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01332
Entry Name
UniProt Accession
Theoretical PI
8.41
Molecular Weight
21308.5
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Rho-related GTP-binding protein RhoG
Protein Synonyms/Alias
Gene Name
RHOG
Gene Synonyms/Alias
ARHG;
Created Date
16-AUG-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
188
Canonical
PIKRGRSCILL****
[1][2]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Wennerberg K, Der CJ. Rho-family GTPases: it's not only Rac and Rho (and Ilike it). J Cell Sci. 2004 Mar 15;117(Pt 8):1301-12. Review.[PMID:15020670]
[2] Morimoto K, Janssen WJ, Fessler MB, McPhillips KA, Borges VM, Bowler RP, Xiao YQ, Kench JA, Henson PM, Vandivier RW. Lovastatin enhances clearance of apoptoticcells (efferocytosis) with implications for chronic obstructive pulmonarydisease. J Immunol. 2006 Jun 15;176(12):7657-65.[PMID:16751413]
Functional Description
Required for the formation of membrane ruffles during macropinocytosis. Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton rearrangements and promotes bacterial entry.
Sequence Annotation
Nucleotide-binding: 10 17 GTP.
Nucleotide-binding: 57 61 GTP.
Nucleotide-binding: 115 118 GTP.
Motif: 32 40 Effector region.
Modified residue: 39 39 ADP-ribosylasparagine; by botulinumtoxin.
Modified residue: 188 188 Cysteine methyl ester.
Protein Length
191 AA.
Protein Sequence
(Canonical)
MQSIKCVVVG DGAVGKTCLL ICYTTNAFPK EYIPTVFDNY SAQSAVDGRT VNLNLWDTAG  60
QEEYDRLRTL SYPQTNVFVI CFSIASPPSY ENVRHKWHPE VCHHCPDVPI LLVGTKKDLR  120
AQPDTLRRLK EQGQAPITPQ QGQALAKQIH AVRYLECSAL QQDGVKEVFA EAVRAVLNPT  180
PIKRGRSCIL L                                                       191
FASTA
(Canonical)
>LipidDB-9606-01332|P84095
MQSIKCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQSAVDGRTVNLNLWDTAG
QEEYDRLRTLSYPQTNVFVICFSIASPPSYENVRHKWHPEVCHHCPDVPILLVGTKKDLR
AQPDTLRRLKEQGQAPITPQQGQALAKQIHAVRYLECSALQQDGVKEVFAEAVRAVLNPT
PIKRGRSCILL
Gene Ontology
GO:0005829; C:cytosol; TAS:Reactome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IDA:MGI
GO:0030036; P:actin cytoskeleton organization; IDA:MGI
GO:0032863; P:activation of Rac GTPase activity; IMP:UniProtKB
GO:0007411; P:axon guidance; TAS:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0060326; P:cell chemotaxis; IMP:UniProtKB
GO:0006184; P:GTP catabolic process; IDA:GOC
GO:0030168; P:platelet activation; TAS:Reactome
GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc
GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IMP:UniProtKB
GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI
GO:0016601; P:Rac protein signal transduction; IDA:MGI
GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl
GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome
GO:0007266; P:Rho protein signal transduction; IDA:MGI
GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR003578; Small_GTPase_Rho
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00174; RHO;
PROSITE
PROSITE; PS51420; RHO;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;