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Protein

Transforming protein RhoA

Gene

Rhoa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Required for the apical junction formation of keratinocyte cell-cell adhesion. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436).By similarity3 Publications

Enzyme regulationi

GTP hydrolysis is stimulated by ARHGAP30.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi59 – 635GTPBy similarity
Nucleotide bindingi117 – 1204GTPBy similarity

GO - Molecular functioni

  • GDP binding Source: Ensembl
  • GTPase activity Source: MGI
  • GTP binding Source: UniProtKB
  • myosin binding Source: MGI

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • actin cytoskeleton reorganization Source: UniProtKB
  • alpha-beta T cell lineage commitment Source: CACAO
  • androgen receptor signaling pathway Source: MGI
  • apical junction assembly Source: UniProtKB
  • apolipoprotein A-I-mediated signaling pathway Source: MGI
  • beta selection Source: CACAO
  • cell adhesion Source: MGI
  • cell differentiation Source: MGI
  • cell-matrix adhesion Source: MGI
  • cell migration Source: UniProtKB
  • cell morphogenesis Source: MGI
  • cerebral cortex cell migration Source: MGI
  • cleavage furrow formation Source: UniProtKB
  • cytoskeleton organization Source: MGI
  • endothelial cell migration Source: MGI
  • endothelial tube lumen extension Source: MGI
  • forebrain radial glial cell differentiation Source: MGI
  • GTP metabolic process Source: Ensembl
  • integrin-mediated signaling pathway Source: MGI
  • mitotic cleavage furrow formation Source: UniProtKB
  • mitotic spindle assembly Source: MGI
  • negative chemotaxis Source: MGI
  • negative regulation of cell migration involved in sprouting angiogenesis Source: MGI
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • negative regulation of intracellular steroid hormone receptor signaling pathway Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of neuron differentiation Source: Ensembl
  • negative regulation of oxidative phosphorylation Source: CACAO
  • negative regulation of reactive oxygen species biosynthetic process Source: CACAO
  • neuron projection morphogenesis Source: Ensembl
  • odontogenesis Source: UniProtKB
  • ossification involved in bone maturation Source: BHF-UCL
  • positive regulation of actin filament polymerization Source: Ensembl
  • positive regulation of alpha-beta T cell differentiation Source: CACAO
  • positive regulation of cell growth Source: Ensembl
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of lipase activity Source: MGI
  • positive regulation of neuron apoptotic process Source: Ensembl
  • positive regulation of neuron differentiation Source: MGI
  • positive regulation of podosome assembly Source: MGI
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of smooth muscle contraction Source: Ensembl
  • positive regulation of stress fiber assembly Source: MGI
  • positive regulation of translation Source: Ensembl
  • positive regulation of vasoconstriction Source: Ensembl
  • regulation of actin cytoskeleton organization Source: CACAO
  • regulation of calcium ion transport Source: Ensembl
  • regulation of cell migration Source: UniProtKB
  • regulation of dendrite development Source: Ensembl
  • regulation of microtubule cytoskeleton organization Source: CACAO
  • regulation of neural precursor cell proliferation Source: MGI
  • regulation of neuron projection development Source: MGI
  • regulation of osteoblast proliferation Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to amino acid Source: Ensembl
  • response to drug Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to glucose Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to mechanical stimulus Source: Ensembl
  • Rho protein signal transduction Source: UniProtKB
  • Roundabout signaling pathway Source: UniProtKB
  • skeletal muscle satellite cell migration Source: AgBase
  • skeletal muscle tissue development Source: MGI
  • stress-activated protein kinase signaling cascade Source: Ensembl
  • stress fiber assembly Source: MGI
  • trabecula morphogenesis Source: BHF-UCL
  • wound healing, spreading of cells Source: AgBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-193634. Axonal growth inhibition (RHOA activation).
R-MMU-194840. Rho GTPase cycle.
R-MMU-198203. PI3K/AKT activation.
R-MMU-209563. Axonal growth stimulation.
R-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-392451. G beta:gamma signalling through PI3Kgamma.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-4086400. PCP/CE pathway.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-416550. Sema4D mediated inhibition of cell attachment and migration.
R-MMU-416572. Sema4D induced cell migration and growth-cone collapse.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5625740. RHO GTPases activate PKNs.
R-MMU-5625900. RHO GTPases activate CIT.
R-MMU-5625970. RHO GTPases activate KTN1.
R-MMU-5627117. RHO GTPases Activate ROCKs.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-5666185. RHO GTPases Activate Rhotekin and Rhophilins.

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming protein RhoA
Gene namesi
Name:Rhoa
Synonyms:Arha, Arha2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1096342. Rhoa.

Subcellular locationi

GO - Cellular componenti

  • apical junction complex Source: MGI
  • axon Source: Ensembl
  • cell cortex Source: UniProtKB
  • cell periphery Source: MGI
  • cleavage furrow Source: UniProtKB-SubCell
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: MGI
  • endosome Source: MGI
  • extracellular exosome Source: MGI
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • focal adhesion Source: MGI
  • lamellipodium Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • ruffle membrane Source: MGI
  • vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Transforming protein RhoAPRO_0000030413Add
BLAST
Propeptidei191 – 1933Removed in mature formBy similarityPRO_0000030414

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Phosphoserine; by PKG/PRKG1By similarity
Modified residuei190 – 1901Cysteine methyl esterBy similarity
Lipidationi190 – 1901S-geranylgeranyl cysteineBy similarity

Post-translational modificationi

Substrate for botulinum ADP-ribosyltransferase.By similarity
Ubiquitinated by the BCR(BACURD1) and BCR(BACURD2) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration.By similarity
Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (By similarity). Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

EPDiQ9QUI0.
MaxQBiQ9QUI0.
PaxDbiQ9QUI0.
PRIDEiQ9QUI0.

PTM databases

iPTMnetiQ9QUI0.
PhosphoSiteiQ9QUI0.
SwissPalmiQ9QUI0.

Expressioni

Inductioni

Up-regulated during keratinocyte differentiation.1 Publication

Gene expression databases

BgeeiQ9QUI0.
CleanExiMM_RHOA.
ExpressionAtlasiQ9QUI0. baseline and differential.
GenevisibleiQ9QUI0. MM.

Interactioni

Subunit structurei

Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2 and ARHGEF3. Interacts with PLCE1 and AKAP13. Interacts with DIAPH1. Interacts (in the constitutively activated, GTP-bound form) with DGKQ. Interacts with RACK1; enhances RHOA activation. Interacts with PKP4; the interaction is detected at the midbody. Interacts (GTP-bound form preferentially) with PKN2; the interaction stimulates autophosphorylation and phosphorylation of PKN2 (By similarity). Interacts with NET1, ARHGEF28 and RTKN. Interacts with ARHGDIA; this interaction inactivates and stabilizes RHOA. Interacts with ARHGDIB (By similarity). Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (PubMed:9635436).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RTKNQ9BST92EBI-643583,EBI-446694From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198192. 37 interactions.
DIPiDIP-29984N.
IntActiQ9QUI0. 34 interactions.
MINTiMINT-118662.
STRINGi10090.ENSMUSP00000007959.

Structurei

Secondary structure

1
193
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Helixi18 – 269Combined sources
Beta strandi42 – 476Combined sources
Beta strandi52 – 587Combined sources
Helixi64 – 663Combined sources
Turni67 – 693Combined sources
Helixi70 – 734Combined sources
Beta strandi78 – 858Combined sources
Helixi89 – 935Combined sources
Turni94 – 985Combined sources
Helixi99 – 1068Combined sources
Beta strandi112 – 1176Combined sources
Helixi119 – 1213Combined sources
Helixi125 – 1339Combined sources
Helixi141 – 15010Combined sources
Beta strandi154 – 1585Combined sources
Turni161 – 1633Combined sources
Helixi167 – 17812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F38X-ray2.80A1-191[»]
ProteinModelPortaliQ9QUI0.
SMRiQ9QUI0. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector regionSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi182 – 1876Arg/Lys-rich (basic)

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ9QUI0.
KOiK04513.
OMAiAYKSLEC.
OrthoDBiEOG73FQPD.
PhylomeDBiQ9QUI0.
TreeFamiTF300837.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QUI0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT
110 120 130 140 150
PEVKHFCPNV PIILVGNKKD LRNDEHTRRE LAKMKQEPVK PEEGRDMANR
160 170 180 190
IGAFGYMECS AKTKDGVREV FEMATRAALQ ARRGKKKSGC LIL
Length:193
Mass (Da):21,782
Last modified:May 1, 2000 - v1
Checksum:iC4C8BDC31FF858BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681R → C in AAC23710 (PubMed:9598304).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014371 mRNA. Translation: AAC23710.1.
AF178958 mRNA. Translation: AAD52675.1.
AF178959 mRNA. Translation: AAD52676.1.
AF178960 mRNA. Translation: AAD52677.1.
AF178961 mRNA. Translation: AAD52678.1.
AK077606 mRNA. Translation: BAC36896.1.
AK083624 mRNA. Translation: BAC38971.1.
BC068115 mRNA. Translation: AAH68115.1.
CCDSiCCDS23521.1.
RefSeqiNP_001300890.1. NM_001313961.1.
NP_001300891.1. NM_001313962.1.
NP_058082.2. NM_016802.5.
UniGeneiMm.318359.
Mm.757.

Genome annotation databases

EnsembliENSMUST00000007959; ENSMUSP00000007959; ENSMUSG00000007815.
GeneIDi11848.
KEGGimmu:11848.
UCSCiuc009rpe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014371 mRNA. Translation: AAC23710.1.
AF178958 mRNA. Translation: AAD52675.1.
AF178959 mRNA. Translation: AAD52676.1.
AF178960 mRNA. Translation: AAD52677.1.
AF178961 mRNA. Translation: AAD52678.1.
AK077606 mRNA. Translation: BAC36896.1.
AK083624 mRNA. Translation: BAC38971.1.
BC068115 mRNA. Translation: AAH68115.1.
CCDSiCCDS23521.1.
RefSeqiNP_001300890.1. NM_001313961.1.
NP_001300891.1. NM_001313962.1.
NP_058082.2. NM_016802.5.
UniGeneiMm.318359.
Mm.757.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F38X-ray2.80A1-191[»]
ProteinModelPortaliQ9QUI0.
SMRiQ9QUI0. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198192. 37 interactions.
DIPiDIP-29984N.
IntActiQ9QUI0. 34 interactions.
MINTiMINT-118662.
STRINGi10090.ENSMUSP00000007959.

PTM databases

iPTMnetiQ9QUI0.
PhosphoSiteiQ9QUI0.
SwissPalmiQ9QUI0.

Proteomic databases

EPDiQ9QUI0.
MaxQBiQ9QUI0.
PaxDbiQ9QUI0.
PRIDEiQ9QUI0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007959; ENSMUSP00000007959; ENSMUSG00000007815.
GeneIDi11848.
KEGGimmu:11848.
UCSCiuc009rpe.2. mouse.

Organism-specific databases

CTDi387.
MGIiMGI:1096342. Rhoa.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ9QUI0.
KOiK04513.
OMAiAYKSLEC.
OrthoDBiEOG73FQPD.
PhylomeDBiQ9QUI0.
TreeFamiTF300837.

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-193634. Axonal growth inhibition (RHOA activation).
R-MMU-194840. Rho GTPase cycle.
R-MMU-198203. PI3K/AKT activation.
R-MMU-209563. Axonal growth stimulation.
R-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-392451. G beta:gamma signalling through PI3Kgamma.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-4086400. PCP/CE pathway.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-416550. Sema4D mediated inhibition of cell attachment and migration.
R-MMU-416572. Sema4D induced cell migration and growth-cone collapse.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5625740. RHO GTPases activate PKNs.
R-MMU-5625900. RHO GTPases activate CIT.
R-MMU-5625970. RHO GTPases activate KTN1.
R-MMU-5627117. RHO GTPases Activate ROCKs.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-5666185. RHO GTPases Activate Rhotekin and Rhophilins.

Miscellaneous databases

ChiTaRSiRhoa. mouse.
NextBioi279815.
PROiQ9QUI0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUI0.
CleanExiMM_RHOA.
ExpressionAtlasiQ9QUI0. baseline and differential.
GenevisibleiQ9QUI0. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transposition of RhoA to the murine Y chromosome."
    Boettger-Tong H.L., Agulnik A.I., Ty T.I., Bishop C.E.
    Genomics 49:180-187(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. Budge P.J., Graham B.S.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ, C57BL/6J, CD-1 and FVB/N.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain."
    Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N., Fujisawa K., Morii N., Madaule P., Narumiya S.
    J. Biol. Chem. 271:13556-13560(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RTKN.
  6. "p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin."
    Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A., Saito Y., Nakao K., Jockusch B.M., Narumiya S.
    EMBO J. 16:3044-3056(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DIAPH1.
  7. "The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel."
    Cachero T.G., Morielli A.D., Peralta E.G.
    Cell 93:1077-1085(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNA2.
  8. "Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7."
    Alberts A.S., Bouquin N., Johnston L.H., Treisman R.
    J. Biol. Chem. 273:8616-8622(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NET1.
  9. "Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules."
    van Horck F.P.G., Ahmadian M.R., Haeusler L.C., Moolenaar W.H., Kranenburg O.
    J. Biol. Chem. 276:4948-4956(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGEF28.
  10. "Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion."
    Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J., Dotto G.P.
    J. Cell Biol. 156:137-148(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  12. "Rab13-dependent trafficking of RhoA is required for directional migration and angiogenesis."
    Wu C., Agrawal S., Vasanji A., Drazba J., Sarkaria S., Xie J., Welch C.M., Liu M., Anand-Apte B., Horowitz A.
    J. Biol. Chem. 286:23511-23520(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
    Wallace S.W., Magalhaes A., Hall A.
    Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKN2.

Entry informationi

Entry nameiRHOA_MOUSE
AccessioniPrimary (citable) accession number: Q9QUI0
Secondary accession number(s): O88336
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.