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P61586

- RHOA_HUMAN

UniProt

P61586 - RHOA_HUMAN

Protein

Transforming protein RhoA

Gene

RHOA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. 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.8 Publications

    Cofactori

    Magnesium.

    Enzyme regulationi

    GTP hydrolysis is stimulated by ARHGAP30.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei189 – 1902Cleavage; by yopT

    Regions

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

    GO - Molecular functioni

    1. GTPase activity Source: UniProtKB
    2. GTP binding Source: UniProtKB-KW
    3. myosin binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. apical junction assembly Source: UniProtKB
    3. axon guidance Source: Reactome
    4. blood coagulation Source: Reactome
    5. cleavage furrow formation Source: UniProtKB
    6. GTP catabolic process Source: GOC
    7. negative regulation of axonogenesis Source: Reactome
    8. neurotrophin TRK receptor signaling pathway Source: Reactome
    9. ossification involved in bone maturation Source: BHF-UCL
    10. phosphatidylinositol-mediated signaling Source: Reactome
    11. platelet activation Source: Reactome
    12. positive regulation of axonogenesis Source: Reactome
    13. positive regulation of cytokinesis Source: UniProtKB
    14. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    15. positive regulation of neuron differentiation Source: MGI
    16. positive regulation of NF-kappaB import into nucleus Source: UniProtKB
    17. positive regulation of stress fiber assembly Source: MGI
    18. regulation of axonogenesis Source: Reactome
    19. regulation of cell migration Source: UniProtKB
    20. regulation of osteoblast proliferation Source: BHF-UCL
    21. regulation of small GTPase mediated signal transduction Source: Reactome
    22. Rho protein signal transduction Source: UniProtKB
    23. small GTPase mediated signal transduction Source: Reactome
    24. spindle assembly involved in mitosis Source: BHF-UCL
    25. substantia nigra development Source: UniProt
    26. trabecula morphogenesis Source: BHF-UCL
    27. transforming growth factor beta receptor signaling pathway Source: Reactome
    28. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Host-virus interaction

    Keywords - Ligandi

    GTP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_12464. PI3K/AKT activation.
    REACT_13779. Axonal growth stimulation.
    REACT_13815. Axonal growth inhibition (RHOA activation).
    REACT_1695. GPVI-mediated activation cascade.
    REACT_172581. PCP/CE pathway.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    REACT_19290. G beta:gamma signalling through PI3Kgamma.
    SignaLinkiP61586.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transforming protein RhoA
    Alternative name(s):
    Rho cDNA clone 12
    Short name:
    h12
    Gene namesi
    Name:RHOA
    Synonyms:ARH12, ARHA, RHO12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:667. RHOA.

    Subcellular locationi

    Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmcytoskeleton. Cleavage furrow. Cytoplasmcell cortex. Midbody. Cell projectionlamellipodium By similarity
    Note: Localized to cell-cell contacts in calcium-treated keratinocytes By similarity. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Localizes to the equatorial cell cortex (at the site of the presumptive furrow) in early anaphase in a activated form and in a myosin- and actin-independent manner.By similarity

    GO - Cellular componenti

    1. apical junction complex Source: UniProtKB
    2. cell cortex Source: UniProtKB
    3. cell junction Source: Reactome
    4. cleavage furrow Source: UniProtKB-SubCell
    5. cytoskeleton Source: UniProtKB-SubCell
    6. cytosol Source: Reactome
    7. extracellular vesicular exosome Source: UniProt
    8. lamellipodium Source: UniProtKB
    9. midbody Source: UniProtKB-SubCell
    10. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141G → V: Causes constitutive activation. 1 Publication
    Mutagenesisi34 – 341Y → A: Abolishes interaction with DGKQ. 2 Publications
    Mutagenesisi34 – 341Y → F: Abolishes AMPylation by Haemophilus IbpA. 2 Publications
    Mutagenesisi63 – 631Q → L: Causes constitutive activation.
    Mutagenesisi193 – 1931L → M: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA134865095.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190Transforming protein RhoAPRO_0000030411Add
    BLAST
    Propeptidei191 – 1933Removed in mature formPRO_0000030412

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341O-AMP-tyrosine; by Haemophilus IbpA1 Publication
    Modified residuei37 – 371O-AMP-threonine; by Vibrio VopS1 Publication
    Modified residuei41 – 411ADP-ribosylasparagine; by botulinum toxin1 Publication
    Modified residuei188 – 1881Phosphoserine; by PKG/PRKG11 Publication
    Modified residuei190 – 1901Cysteine methyl esterBy similarity
    Lipidationi190 – 1901S-geranylgeranyl cysteineBy similarity

    Post-translational modificationi

    Substrate for botulinum ADP-ribosyltransferase.
    Cleaved by yopT protease when the cell is infected by some Yersinia pathogens. This removes the lipid attachment, and leads to its displacement from plasma membrane and to subsequent cytoskeleton cleavage.2 Publications
    AMPylation at Tyr-34 and Thr-37 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.2 Publications
    Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling.1 Publication
    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.1 Publication

    Keywords - PTMi

    ADP-ribosylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

    Proteomic databases

    MaxQBiP61586.
    PaxDbiP61586.
    PeptideAtlasiP61586.
    PRIDEiP61586.

    PTM databases

    PhosphoSiteiP61586.

    Miscellaneous databases

    PMAP-CutDBP61586.

    Expressioni

    Gene expression databases

    ArrayExpressiP61586.
    BgeeiP61586.
    CleanExiHS_RHOA.
    GenevestigatoriP61586.

    Organism-specific databases

    HPAiCAB005052.

    Interactioni

    Subunit structurei

    Interacts with ARHGEF28 By similarity. Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts with PLCE1 and AKAP13. Interacts (in the constitutively activated, GTP-bound form) with DGKQ. Interacts with human respiratory syncytial virus (HRSV) protein F; this interaction facilitates virus-induced syncytium formation. Interacts with GNB2L1/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. Interacts with ARHGDIA; this interaction inactivates and stabilizes RHOA. Interacts with ARHGDIB.By similarity20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGERQ151092EBI-446668,EBI-1646426
    ARHGAP1Q079602EBI-446668,EBI-602762
    ARHGDIAP525652EBI-446668,EBI-712693
    ARHGEF11O150856EBI-446668,EBI-311099
    ARHGEF12Q9NZN52EBI-446668,EBI-821440
    ARHGEF19Q8IW932EBI-446668,EBI-7799822
    DAAM1Q9Y4D15EBI-446668,EBI-2817289
    DIAPH1O606103EBI-446668,EBI-3959709
    Diaph1O088083EBI-446668,EBI-1026445From a different organism.
    Mcf2lQ6PDM63EBI-446668,EBI-602149From a different organism.
    NCLP193383EBI-446668,EBI-346967
    Rabac1Q9Z0S93EBI-446668,EBI-476965From a different organism.
    ROCK1Q134644EBI-446668,EBI-876651
    RTKNQ9BST95EBI-446668,EBI-446694
    RtknQ8C6B23EBI-446668,EBI-1162441From a different organism.
    SMAD2Q157962EBI-446668,EBI-1040141
    SMURF1Q9HCE72EBI-446668,EBI-976466

    Protein-protein interaction databases

    BioGridi106880. 110 interactions.
    DIPiDIP-29642N.
    IntActiP61586. 48 interactions.
    MINTiMINT-4999683.
    STRINGi9606.ENSP00000400175.

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Turni15 – 173
    Helixi18 – 2710
    Beta strandi38 – 4811
    Beta strandi51 – 6010
    Helixi64 – 663
    Turni67 – 693
    Helixi70 – 734
    Beta strandi78 – 858
    Helixi89 – 979
    Helixi99 – 1068
    Beta strandi112 – 1176
    Helixi119 – 1213
    Helixi125 – 1339
    Helixi141 – 15010
    Beta strandi154 – 1585
    Turni161 – 1633
    Helixi167 – 17913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A2BX-ray2.40A1-181[»]
    1CC0X-ray5.00A/C1-190[»]
    1CXZX-ray2.20A1-181[»]
    1DPFX-ray2.00A1-180[»]
    1FTNX-ray2.10A1-193[»]
    1KMQX-ray1.55A4-181[»]
    1LB1X-ray2.81B/D/F/H1-190[»]
    1OW3X-ray1.80B1-193[»]
    1S1CX-ray2.60A/B1-181[»]
    1TX4X-ray1.65B3-179[»]
    1X86X-ray3.22B/D/F/H1-193[»]
    1XCGX-ray2.50B/F3-180[»]
    2RGNX-ray3.50C/F1-193[»]
    3KZ1X-ray2.70E/F1-181[»]
    3LW8X-ray1.85A/B/C/D2-181[»]
    3LWNX-ray2.28A/B2-181[»]
    3LXRX-ray1.68A2-181[»]
    3MSXX-ray1.65A1-180[»]
    3T06X-ray2.84B/F3-180[»]
    4D0NX-ray2.10A1-184[»]
    ProteinModelPortaliP61586.
    SMRiP61586. Positions 2-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61586.

    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)

    Domaini

    The basic-rich region is essential for yopT recognition and cleavage.

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rho family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    InParanoidiP61586.
    KOiK04513.
    OMAiRNDPHTI.
    OrthoDBiEOG73FQPD.
    PhylomeDBiP61586.
    TreeFamiTF300837.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00174. RHO. 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.

    P61586-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG    50
    KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT 100
    PEVKHFCPNV PIILVGNKKD LRNDEHTRRE LAKMKQEPVK PEEGRDMANR 150
    IGAFGYMECS AKTKDGVREV FEMATRAALQ ARRGKKKSGC LVL 193
    Length:193
    Mass (Da):21,768
    Last modified:January 1, 1988 - v1
    Checksum:iC4DA2DC31FF858BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231I → T in BAD96276. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05026 mRNA. Translation: CAA28690.1.
    L25080 mRNA. Translation: AAC33178.1.
    AF498970 mRNA. Translation: AAM21117.1.
    BT019870 mRNA. Translation: AAV38673.1.
    AK222556 mRNA. Translation: BAD96276.1.
    BX647063 mRNA. Translation: CAE46190.1.
    AC104452 Genomic DNA. No translation available.
    AC121247 Genomic DNA. No translation available.
    AC137114 Genomic DNA. No translation available.
    BC001360 mRNA. Translation: AAH01360.1.
    BC005976 mRNA. Translation: AAH05976.1.
    L09159 mRNA. Translation: AAA50612.1.
    M83094 Genomic DNA. Translation: AAA67539.1.
    CCDSiCCDS2795.1.
    PIRiA26675. TVHU12.
    RefSeqiNP_001655.1. NM_001664.2.
    UniGeneiHs.247077.

    Genome annotation databases

    EnsembliENST00000418115; ENSP00000400175; ENSG00000067560.
    GeneIDi387.
    KEGGihsa:387.
    UCSCiuc003cwu.3. human.

    Polymorphism databases

    DMDMi47606458.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05026 mRNA. Translation: CAA28690.1 .
    L25080 mRNA. Translation: AAC33178.1 .
    AF498970 mRNA. Translation: AAM21117.1 .
    BT019870 mRNA. Translation: AAV38673.1 .
    AK222556 mRNA. Translation: BAD96276.1 .
    BX647063 mRNA. Translation: CAE46190.1 .
    AC104452 Genomic DNA. No translation available.
    AC121247 Genomic DNA. No translation available.
    AC137114 Genomic DNA. No translation available.
    BC001360 mRNA. Translation: AAH01360.1 .
    BC005976 mRNA. Translation: AAH05976.1 .
    L09159 mRNA. Translation: AAA50612.1 .
    M83094 Genomic DNA. Translation: AAA67539.1 .
    CCDSi CCDS2795.1.
    PIRi A26675. TVHU12.
    RefSeqi NP_001655.1. NM_001664.2.
    UniGenei Hs.247077.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A2B X-ray 2.40 A 1-181 [» ]
    1CC0 X-ray 5.00 A/C 1-190 [» ]
    1CXZ X-ray 2.20 A 1-181 [» ]
    1DPF X-ray 2.00 A 1-180 [» ]
    1FTN X-ray 2.10 A 1-193 [» ]
    1KMQ X-ray 1.55 A 4-181 [» ]
    1LB1 X-ray 2.81 B/D/F/H 1-190 [» ]
    1OW3 X-ray 1.80 B 1-193 [» ]
    1S1C X-ray 2.60 A/B 1-181 [» ]
    1TX4 X-ray 1.65 B 3-179 [» ]
    1X86 X-ray 3.22 B/D/F/H 1-193 [» ]
    1XCG X-ray 2.50 B/F 3-180 [» ]
    2RGN X-ray 3.50 C/F 1-193 [» ]
    3KZ1 X-ray 2.70 E/F 1-181 [» ]
    3LW8 X-ray 1.85 A/B/C/D 2-181 [» ]
    3LWN X-ray 2.28 A/B 2-181 [» ]
    3LXR X-ray 1.68 A 2-181 [» ]
    3MSX X-ray 1.65 A 1-180 [» ]
    3T06 X-ray 2.84 B/F 3-180 [» ]
    4D0N X-ray 2.10 A 1-184 [» ]
    ProteinModelPortali P61586.
    SMRi P61586. Positions 2-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106880. 110 interactions.
    DIPi DIP-29642N.
    IntActi P61586. 48 interactions.
    MINTi MINT-4999683.
    STRINGi 9606.ENSP00000400175.

    Chemistry

    BindingDBi P61586.
    ChEMBLi CHEMBL6052.
    DrugBanki DB01076. Atorvastatin.
    DB00641. Simvastatin.

    PTM databases

    PhosphoSitei P61586.

    Polymorphism databases

    DMDMi 47606458.

    Proteomic databases

    MaxQBi P61586.
    PaxDbi P61586.
    PeptideAtlasi P61586.
    PRIDEi P61586.

    Protocols and materials databases

    DNASUi 387.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000418115 ; ENSP00000400175 ; ENSG00000067560 .
    GeneIDi 387.
    KEGGi hsa:387.
    UCSCi uc003cwu.3. human.

    Organism-specific databases

    CTDi 387.
    GeneCardsi GC03M049371.
    HGNCi HGNC:667. RHOA.
    HPAi CAB005052.
    MIMi 165390. gene.
    neXtProti NX_P61586.
    PharmGKBi PA134865095.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi P61586.
    KOi K04513.
    OMAi RNDPHTI.
    OrthoDBi EOG73FQPD.
    PhylomeDBi P61586.
    TreeFami TF300837.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_12464. PI3K/AKT activation.
    REACT_13779. Axonal growth stimulation.
    REACT_13815. Axonal growth inhibition (RHOA activation).
    REACT_1695. GPVI-mediated activation cascade.
    REACT_172581. PCP/CE pathway.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    REACT_19290. G beta:gamma signalling through PI3Kgamma.
    SignaLinki P61586.

    Miscellaneous databases

    ChiTaRSi RHOA. human.
    EvolutionaryTracei P61586.
    GeneWikii RHOA.
    GenomeRNAii 387.
    NextBioi 1611.
    PMAP-CutDB P61586.
    PROi P61586.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61586.
    Bgeei P61586.
    CleanExi HS_RHOA.
    Genevestigatori P61586.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00174. RHO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51420. RHO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts."
      Fagan K.P., Oliveira L., Pittler S.J.
      Exp. Eye Res. 59:235-237(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Retina.
    3. "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.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adipose tissue.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Esophageal carcinoma.
    7. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Brain and Colon.
    9. "Utilization of multiple polyadenylation signals in the human RHOA protooncogene."
      Moscow J.A., He R., Gudas J.M., Cowan K.H.
      Gene 144:229-236(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-193.
      Tissue: Mammary cancer.
    10. "A rho gene product in human blood platelets. I. Identification of the platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA protein."
      Nemoto Y., Namba T., Teru-uchi T., Ushikubi F., Morii N., Narumiya S.
      J. Biol. Chem. 267:20916-20920(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-39; 45-57; 78-86; 130-144; 146-162 AND 165-184, ADP-RIBOSYLATION AT ASN-41.
      Tissue: Platelet.
    11. "Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1)."
      Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.
      J. Biol. Chem. 267:5949-5958(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-193.
    12. "The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase."
      Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A., Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.
      EMBO J. 15:1885-1893(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROCK1.
    13. "Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho."
      Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.
      EMBO J. 15:2208-2216(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROCK2.
    14. "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling."
      Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K., Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G., Der C.J.
      J. Biol. Chem. 271:28772-28776(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization."
      Vincent S., Settleman J.
      Mol. Cell. Biol. 17:2247-2256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PKN2.
    16. "Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases."
      Ren Y., Li R., Zheng Y., Busch H.
      J. Biol. Chem. 273:34954-34960(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF2.
    17. "Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA."
      Houssa B., de Widt J., Kranenburg O., Moolenaar W.H., van Blitterswijk W.J.
      J. Biol. Chem. 274:6820-6822(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DGKQ, MUTAGENESIS OF TYR-34.
    18. "RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation."
      Pastey M.K., Crowe J.E. Jr., Graham B.S.
      J. Virol. 73:7262-7270(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRSV PROTEIN F.
    19. "The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element."
      Reynaud C., Fabre S., Jalinot P.
      J. Biol. Chem. 275:33962-33968(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RTKN.
    20. Cited for: PHOSPHORYLATION AT SER-188 BY PRKG1.
    21. "Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling."
      Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V., Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.
      FEBS Lett. 507:264-268(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKAP13.
    22. "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC."
      Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K.
      J. Biol. Chem. 277:42964-42972(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF3.
    23. "A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis."
      Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E.
      Cell 109:575-588(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YERSINIA PESTIS YOPT, CLEAVAGE.
    24. "Direct activation of phospholipase C-epsilon by Rho."
      Wing M.R., Snyder J.T., Sondek J., Harden T.K.
      J. Biol. Chem. 278:41253-41258(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLCE1.
    25. "Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases."
      Shao F., Vacratsis P.O., Bao Z., Bowers K.E., Fierke C.A., Dixon J.E.
      Proc. Natl. Acad. Sci. U.S.A. 100:904-909(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPT, CLEAVAGE, MUTAGENESIS OF LEU-193.
    26. "An ECT2-centralspindlin complex regulates the localization and function of RhoA."
      Yuce O., Piekny A., Glotzer M.
      J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    27. "Dissecting the role of Rho-mediated signaling in contractile ring formation."
      Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.
      Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    28. "The armadillo protein p0071 regulates Rho signalling during cytokinesis."
      Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., Huttelmaier S., Hatzfeld M.
      Nat. Cell Biol. 8:1432-1440(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKP4, SUBCELLULAR LOCATION.
    29. "The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin dynamics and thereby regulate cell migration."
      Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L., Webb D.J.
      J. Cell Sci. 122:4535-4546(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. Cited for: AMPYLATION AT TYR-34, MUTAGENESIS OF TYR-34.
    31. "Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement."
      Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M., Peng H.B., Shao F.
      Mol. Cell 35:841-855(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    32. "AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling."
      Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.
      Science 323:269-272(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: AMPYLATION AT THR-37.
    33. "Activated Rac1 GTPase translocates protein phosphatase 5 to the cell membrane and stimulates phosphatase activity in vitro."
      Chatterjee A., Wang L., Armstrong D.L., Rossie S.
      J. Biol. Chem. 285:3872-3882(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-14.
    34. "Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1."
      Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G., Brennwald P.J., Burridge K.
      Nat. Cell Biol. 12:477-483(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGDIA.
    35. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
      Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
      Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion."
      Naji L., Pacholsky D., Aspenstrom P.
      Biochem. Biophys. Res. Commun. 409:96-102(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    38. "RACK1 promotes breast carcinoma migration/metastasis via activation of the RhoA/Rho kinase pathway."
      Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D., Liu X.P.
      Breast Cancer Res. Treat. 126:555-563(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GNB2L1.
    39. "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.
    40. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    41. "Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue."
      Ihara K., Muraguchi S., Kato M., Shimizu T., Shirakawa M., Kuroda S., Kaibuchi K., Hakoshima T.
      J. Biol. Chem. 273:9656-9666(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-181 OF MUTANT VAL-14.
    42. "Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA."
      Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K., Hakoshima T.
      J. Struct. Biol. 126:166-170(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-181 IN COMPLEX WITH PRKCL1.
    43. "An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism."
      Shimizu T., Ihara K., Maesaki R., Kuroda S., Kaibuchi K., Hakoshima T.
      J. Biol. Chem. 275:18311-18317(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-180 IN COMPLEX WITH GDP.
    44. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    45. "Structural basis for the selective activation of Rho GTPases by Dbl exchange factors."
      Snyder J.T., Worthylake D.K., Rossman K.L., Betts L., Pruitt W.M., Siderovski D.P., Der C.J., Sondek J.
      Nat. Struct. Biol. 9:468-475(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH MCF2.
    46. "Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution."
      Longenecker K., Read P., Lin S.-K., Somlyo A.P., Nakamoto R.K., Derewenda Z.S.
      Acta Crystallogr. D 59:876-880(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANT LEU-63 IN COMPLEX WITH A GTP ANALOG AND MG(2+).

    Entry informationi

    Entry nameiRHOA_HUMAN
    AccessioniPrimary (citable) accession number: P61586
    Secondary accession number(s): P06749
    , Q53HM4, Q5U024, Q9UDJ0, Q9UEJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3