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P17081 (RHOQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-related GTP-binding protein RhoQ
Alternative name(s):
Ras-like protein TC10
Ras-like protein family member 7A
Gene names
Name:RHOQ
Synonyms:ARHQ, RASL7A, TC10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Enzyme regulation

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase.

Subunit structure

Interacts with CDC42EP4 in a GTP-dependent manner. Interacts with ARHGAP33/TCGAP By similarity. Interacts with CDC42EP1, CDC42EP2, CDC42EP3, PARD6A, PARD6G (and probably PARD6B) in a GTP-dependent manner. Part of a quaternary complex containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein (PRKCI or PRKCZ). Interacts with EXO70 in a GTP-dependent manner. Interacts with GOPC. Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm. Cell membrane; Lipid-anchor Ref.9.

Post-translational modification

May be post-translationally modified by both palmitoylation and polyisoprenylation.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Sequence caution

The sequence AAA36547.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAM21123.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay PubMed 10445846. Source: BHF-UCL

cellular response to insulin stimulus

Inferred from mutant phenotype PubMed 11309621. Source: BHF-UCL

cortical actin cytoskeleton organization

Inferred from mutant phenotype PubMed 11821390. Source: BHF-UCL

insulin receptor signaling pathway

Inferred from mutant phenotype PubMed 11309621. Source: BHF-UCL

negative regulation of establishment of protein localization to plasma membrane

Inferred from mutant phenotype PubMed 11309621. Source: BHF-UCL

positive regulation of filopodium assembly

Inferred from direct assay PubMed 10445846. Source: BHF-UCL

positive regulation of glucose import

Inferred from mutant phenotype PubMed 11309621. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10445846. Source: BHF-UCL

regulation of actin cytoskeleton organization

Inferred by curator PubMed 10445846. Source: BHF-UCL

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentactin filament

Inferred from direct assay PubMed 10445846. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

membrane raft

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 10445846. Source: BHF-UCL

   Molecular_functionGBD domain binding

Inferred from physical interaction PubMed 10445846. Source: BHF-UCL

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay PubMed 10445846. Source: BHF-UCL

profilin binding

Inferred from physical interaction PubMed 10445846. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202Rho-related GTP-binding protein RhoQ
PRO_0000198871
Propeptide203 – 2053Removed in mature form By similarity
PRO_0000281222

Regions

Nucleotide binding16 – 238GTP By similarity
Nucleotide binding63 – 675GTP By similarity
Nucleotide binding121 – 1244GTP By similarity
Motif38 – 469Effector region By similarity

Amino acid modifications

Modified residue2021Cysteine methyl ester By similarity
Lipidation2021S-farnesyl cysteine By similarity

Experimental info

Mutagenesis231T → N: Loss of interaction with GOPC. Ref.8
Mutagenesis441D → A: Loss of interaction with GOPC. Ref.8
Mutagenesis671Q → L: Constitutively active. Interacts with PARD6 proteins and GOPC. Ref.7

Secondary structure

................................ 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17081 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 82695B4F8FBF0B75

FASTA20522,659
        10         20         30         40         50         60 
MAHGPGALML KCVVVGDGAV GKTCLLMSYA NDAFPEEYVP TVFDHYAVSV TVGGKQYLLG 

        70         80         90        100        110        120 
LYDTAGQEDY DRLRPLSYPM TDVFLICFSV VNPASFQNVK EEWVPELKEY APNVPFLLIG 

       130        140        150        160        170        180 
TQIDLRDDPK TLARLNDMKE KPICVEQGQK LAKEIGACCY VECSALTQKG LKTVFDEAII 

       190        200 
AILTPKKHTV KKRIGSRCIN CCLIT 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line."
Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.
Mol. Cell. Biol. 10:1793-1798(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Skin.
[6]"The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins."
Joberty G., Perlungher R.R., Macara I.G.
Mol. Cell. Biol. 19:6585-6597(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC42EP1; CDC42EP2 AND CDC42EP3.
Tissue: Embryo.
[7]"The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
Joberty G., Petersen C., Gao L., Macara I.G.
Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD6A AND PARD6G, MUTAGENESIS OF GLN-67.
[8]"PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10."
Neudauer C.L., Joberty G., Macara I.G.
Biochem. Biophys. Res. Commun. 280:541-547(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GOPC, MUTAGENESIS OF THR-23 AND ASP-44.
[9]"Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10."
Cheng J., Wang H., Guggino W.B.
J. Biol. Chem. 280:3731-3739(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GOPC, SUBCELLULAR LOCATION, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31470 mRNA. Translation: AAA36547.1. Different initiation.
AF498976 mRNA. Translation: AAM21123.1. Different initiation.
AC018682 Genomic DNA. Translation: AAY14834.1.
CH471053 Genomic DNA. Translation: EAX00251.1.
BC056154 mRNA. Translation: AAH56154.3.
BC065291 mRNA. Translation: AAH65291.2.
BC070485 mRNA. Translation: AAH70485.2.
BC093805 mRNA. Translation: AAH93805.2.
BC101806 mRNA. Translation: AAI01807.1.
PIRTVHUC4. D34788.
RefSeqNP_036381.2. NM_012249.3.
UniGeneHs.709193.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ATXX-ray2.65A/B1-185[»]
ProteinModelPortalP17081.
SMRP17081. Positions 1-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117001. 13 interactions.
IntActP17081. 4 interactions.
STRING9606.ENSP00000238738.

PTM databases

PhosphoSiteP17081.

Polymorphism databases

DMDM62906861.

Proteomic databases

PaxDbP17081.
PRIDEP17081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238738; ENSP00000238738; ENSG00000119729.
GeneID23433.
KEGGhsa:23433.
UCSCuc002rva.3. human.

Organism-specific databases

CTD23433.
GeneCardsGC02P046768.
HGNCHGNC:17736. RHOQ.
MIM605857. gene.
neXtProtNX_P17081.
PharmGKBPA134904280.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG009351.
InParanoidP17081.
KOK07194.
OMALAPRCIN.
OrthoDBEOG764747.
PhylomeDBP17081.
TreeFamTF101109.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP17081.

Gene expression databases

ArrayExpressP17081.
BgeeP17081.
CleanExHS_RHOQ.
GenevestigatorP17081.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRHOQ. human.
EvolutionaryTraceP17081.
GeneWikiRHOQ.
GenomeRNAi23433.
NextBio45687.
PROP17081.
SOURCESearch...

Entry information

Entry nameRHOQ_HUMAN
AccessionPrimary (citable) accession number: P17081
Secondary accession number(s): D6W5A6 expand/collapse secondary AC list , Q0VGN1, Q52LS8, Q53SJ1, Q6NS39, Q6P146, Q7Z480
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM