Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01421
Entry Name
UniProt Accession
Theoretical PI
5.94
Molecular Weight
22659.46
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Rho-related GTP-binding protein RhoQ
Protein Synonyms/Alias
Ras-like protein TC10; Ras-like protein family member 7A;
Gene Name
RHOQ
Gene Synonyms/Alias
ARHQ; RASL7A; TC10;
Created Date
01-AUG-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
202
Canonical
GSRCINCCLIT****
[1]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Tamanoi F, Gau CL, Jiang C, Edamatsu H, Kato-Stankiewicz J. Proteinfarnesylation in mammalian cells: effects of farnesyltransferase inhibitors oncancer cells. Cell Mol Life Sci. 2001 Oct;58(11):1636-49. Review.[PMID:11706990]
Functional Description
Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia.
Sequence Annotation
Nucleotide-binding: 16 23 GTP.
Nucleotide-binding: 63 67 GTP.
Nucleotide-binding: 121 124 GTP.
Motif: 38 46 Effector region.
Modified residue: 202 202 Cysteine methyl ester.
Protein Length
205 AA.
Protein Sequence
(Canonical)
MAHGPGALML KCVVVGDGAV GKTCLLMSYA NDAFPEEYVP TVFDHYAVSV TVGGKQYLLG  60
LYDTAGQEDY DRLRPLSYPM TDVFLICFSV VNPASFQNVK EEWVPELKEY APNVPFLLIG  120
TQIDLRDDPK TLARLNDMKE KPICVEQGQK LAKEIGACCY VECSALTQKG LKTVFDEAII  180
AILTPKKHTV KKRIGSRCIN CCLIT                                        205
FASTA
(Canonical)
>LipidDB-9606-01421|P17081
MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLG
LYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIG
TQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAII
AILTPKKHTVKKRIGSRCINCCLIT
Gene Ontology
GO:0005884; C:actin filament; IDA:BHF-UCL
GO:0005829; C:cytosol; TAS:Reactome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0045121; C:membrane raft; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:BHF-UCL
GO:0032427; F:GBD domain binding; IPI:BHF-UCL
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IDA:BHF-UCL
GO:0005522; F:profilin binding; IPI:BHF-UCL
GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL
GO:0030866; P:cortical actin cytoskeleton organization; IMP:BHF-UCL
GO:0006184; P:GTP catabolic process; IDA:BHF-UCL
GO:0008286; P:insulin receptor signaling pathway; IMP:BHF-UCL
GO:0090005; P:negative regulation of establishment of protein localization to plasma membrane; IMP:BHF-UCL
GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL
GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL
GO:0032956; P:regulation of actin cytoskeleton organization; IC:BHF-UCL
GO:0008360; P:regulation of cell shape; IEA:Ensembl
GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome
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;