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UniProtKB/Swiss-Prot entry Q9QUI0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RHOA_MOUSE
Primary accession number Q9QUI0
Secondary accession number O88336
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 87)
Name and origin of the protein
Protein name Transforming protein RhoA [Precursor]
Synonyms None
Gene name
Name: Rhoa
Synonyms: Arha, Arha2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
DOI=10.1006/geno.1998.5219; PubMed=9598304 [NCBI, ExPASy, EBI, Israel, Japan]
Boettger-Tong H.L., Agulnik A.I., Ty T.I., Bishop C.E.;
"Transposition of RhoA to the murine Y chromosome.";
Genomics 49:180-187(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c, C57BL/6, CD-1, and FVB/N;
Budge P.J., Graham B.S.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6;
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH RTKN.
DOI=10.1074/jbc.271.23.13556; PubMed=8662891 [NCBI, ExPASy, EBI, Israel, Japan]
Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N., Fujisawa K., Morii N., Madaule P., Narumiya S.;
"Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain.";
J. Biol. Chem. 271:13556-13560(1996).
[6]
INTERACTION WITH NET1.
DOI=10.1074/jbc.273.15.8616; PubMed=9535835 [NCBI, ExPASy, EBI, Israel, Japan]
Alberts A.S., Bouquin N., Johnston L.H., Treisman R.;
"Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7.";
J. Biol. Chem. 273:8616-8622(1998).
[7]
INTERACTION WITH RGNEF.
DOI=10.1074/jbc.M003839200; PubMed=11058585 [NCBI, ExPASy, EBI, Israel, Japan]
van Horck F.P.G., Ahmadian M.R., Haeusler L.C., Moolenaar W.H., Kranenburg O.;
"Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules.";
J. Biol. Chem. 276:4948-4956(2001).
Comments
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
AF014371; AAC23710.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF178958; AAD52675.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF178959; AAD52676.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF178960; AAD52677.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF178961; AAD52678.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK077606; BAC36896.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK083624; BAC38971.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068115; AAH68115.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00315100; -.
RefSeq NP_058082.2; -.
UniGene Mm.471622
3D structure databases
HSSP P06749; 1LB1. [HSSP ENTRY / PDB]
SMR Q9QUI0; 1-181.
ModBase Q9QUI0.
Protein-protein interaction databases
IntAct Q9QUI0; 3.
PTM databases
PhosphoSite Q9QUI0; -.
Organism-specific databases
MGI MGI:1096342; Rhoa.
Gene expression databases
ArrayExpress Q9QUI0; -.
Bgee Q9QUI0; -.
CleanEx MM_RHOA; -.
GermOnline ENSMUSG00000007815; Mus musculus.
Ontologies
GO
GO:0005856; Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005829; Cellular component: cytosol (inferred from direct assay from MGI).
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from MGI).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003924; Molecular function: GTPase activity (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0030154; Biological process: cell differentiation (inferred from direct assay from MGI).
GO:0000902; Biological process: cell morphogenesis (inferred from genetic interaction from MGI).
GO:0007160; Biological process: cell-matrix adhesion (inferred from direct assay from MGI).
GO:0007229; Biological process: integrin-mediated signaling pathway (traceable author statement from MGI).
GO:0043524; Biological process: negative regulation of neuron apoptosis (inferred from mutant phenotype from MGI).
GO:0043123; Biological process: positive regulation of I-kappaB kinase/NF-kappaB cascade (inferred from sequence or structural similarity from UniProtKB).
GO:0006357; Biological process: regulation of transcription from RNA polymerase II promoter (inferred from direct assay from MGI).
GO:0007266; Biological process: Rho protein signal transduction (traceable author statement from MGI).
GO:0007519; Biological process: skeletal muscle tissue development (inferred from direct assay from MGI).
GO:0043149; Biological process: stress fiber formation (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR003578; GTPase_Rho.
IPR013753; Ras.
IPR001806; Ras_GTPase.
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.
PROSITE PS51420; RHO; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9QUI0; -.
Genome annotation databases
Ensembl ENSMUSG00000007815; Mus musculus. [Contig view]
GeneID 11848; -.
KEGG mmu:11848; -.
Phylogenomic databases
HOGENOM Q9QUI0; -.
HOVERGEN Q9QUI0; -.
OMA Q9QUI0; RNDEHAR.
Other
NextBio 279815; -.
SOURCE Rhoa; Mus musculus.
ProtoNet Q9QUI0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Cytoplasm; Cytoskeleton; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation; Proto-oncogene.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   190  190     Transforming protein RhoA. PRO_0000030413
PROPEP   191   193  3     Removed in mature form (By similarity). PRO_0000030414
NP_BIND   12    19  8     GTP (By similarity). 
NP_BIND   59    63  5     GTP (By similarity). 
NP_BIND   117   120  4     GTP (By similarity). 
MOTIF   34    42  9     Effector region (Potential). 
COMPBIAS   182   187  6     Arg/Lys-rich (basic). 
MOD_RES   190   190        Cysteine methyl ester (By similarity). 
LIPID   190   190        S-geranylgeranyl cysteine (By similarity). 
CONFLICT   68    68        R -> C (in Ref. 1; AAC23710). 
Sequence information
Length: 193 AA [This is the length of the unprocessed precursor] Molecular weight: 21782 Da [This is the MW of the unprocessed precursor] CRC64: C4C8BDC31FF858BC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT 

        70         80         90        100        110        120 
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD 

       130        140        150        160        170        180 
LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ 

       190 
ARRGKKKSGC LIL 

Q9QUI0 in FASTA format

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