Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P84095

- RHOG_HUMAN

UniProt

P84095 - RHOG_HUMAN

Protein

Rho-related GTP-binding protein RhoG

Gene

RHOG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Required for the formation of membrane ruffles during macropinocytosis. Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton rearrangements and promotes bacterial entry.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 178GTPBy similarity
    Nucleotide bindingi57 – 615GTPBy similarity
    Nucleotide bindingi115 – 1184GTPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. actin cytoskeleton organization Source: MGI
    2. activation of Rac GTPase activity Source: UniProtKB
    3. axon guidance Source: Reactome
    4. blood coagulation Source: Reactome
    5. cell chemotaxis Source: UniProtKB
    6. GTP catabolic process Source: GOC
    7. platelet activation Source: Reactome
    8. positive regulation of cell proliferation Source: ProtInc
    9. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
    10. positive regulation of transcription, DNA-templated Source: MGI
    11. Rac protein signal transduction Source: MGI
    12. regulation of small GTPase mediated signal transduction Source: Reactome
    13. Rho protein signal transduction Source: MGI
    14. small GTPase mediated signal transduction Source: Reactome

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-related GTP-binding protein RhoG
    Gene namesi
    Name:RHOG
    Synonyms:ARHG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:672. RHOG.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24955.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 188188Rho-related GTP-binding protein RhoGPRO_0000042028Add
    BLAST
    Propeptidei189 – 1913Removed in mature formBy similarityPRO_0000042029

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391ADP-ribosylasparagine; by botulinum toxinBy similarity
    Modified residuei188 – 1881Cysteine methyl esterBy similarity
    Lipidationi188 – 1881S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    ADP-ribosylation, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP84095.
    PaxDbiP84095.
    PeptideAtlasiP84095.
    PRIDEiP84095.

    PTM databases

    PhosphoSiteiP84095.

    Expressioni

    Gene expression databases

    ArrayExpressiP84095.
    BgeeiP84095.
    CleanExiHS_RHOG.
    GenevestigatoriP84095.

    Organism-specific databases

    HPAiHPA039871.

    Interactioni

    Subunit structurei

    Interacts with ARHGEF26. Interacts with ARHGEF16.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ELMO1Q925563EBI-446579,EBI-346417

    Protein-protein interaction databases

    BioGridi106884. 10 interactions.
    IntActiP84095. 2 interactions.
    MINTiMINT-4132365.
    STRINGi9606.ENSP00000339467.

    Structurei

    3D structure databases

    ProteinModelPortaliP84095.
    SMRiP84095. Positions 1-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi32 – 409Effector regionSequence Analysis

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rho family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    InParanoidiP84095.
    KOiK07863.
    OMAiKRGRSCF.
    OrthoDBiEOG764747.
    PhylomeDBiP84095.
    TreeFamiTF101109.

    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.

    P84095-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSIKCVVVG DGAVGKTCLL ICYTTNAFPK EYIPTVFDNY SAQSAVDGRT    50
    VNLNLWDTAG QEEYDRLRTL SYPQTNVFVI CFSIASPPSY ENVRHKWHPE 100
    VCHHCPDVPI LLVGTKKDLR AQPDTLRRLK EQGQAPITPQ QGQALAKQIH 150
    AVRYLECSAL QQDGVKEVFA EAVRAVLNPT PIKRGRSCIL L 191
    Length:191
    Mass (Da):21,309
    Last modified:August 16, 2004 - v1
    Checksum:i0C4FE9C54140F499
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331G → S in CAA43784. (PubMed:1620121)Curated
    Sequence conflicti169 – 1691F → L in AAM21121. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11317 mRNA. Translation: AAA60268.1.
    X61587 mRNA. Translation: CAA43784.1.
    AF498974 mRNA. Translation: AAM21121.1.
    AY563952 mRNA. Translation: AAS75333.1.
    CCDSiCCDS7748.1.
    PIRiS25722. TVHURG.
    RefSeqiNP_001656.2. NM_001665.3.
    XP_005252973.1. XM_005252916.1.
    UniGeneiHs.501728.

    Genome annotation databases

    EnsembliENST00000351018; ENSP00000339467; ENSG00000177105.
    ENST00000396978; ENSP00000380175; ENSG00000177105.
    ENST00000396979; ENSP00000380176; ENSG00000177105.
    ENST00000533217; ENSP00000436932; ENSG00000177105.
    GeneIDi391.
    KEGGihsa:391.
    UCSCiuc001lyu.2. human.

    Polymorphism databases

    DMDMi51338611.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11317 mRNA. Translation: AAA60268.1 .
    X61587 mRNA. Translation: CAA43784.1 .
    AF498974 mRNA. Translation: AAM21121.1 .
    AY563952 mRNA. Translation: AAS75333.1 .
    CCDSi CCDS7748.1.
    PIRi S25722. TVHURG.
    RefSeqi NP_001656.2. NM_001665.3.
    XP_005252973.1. XM_005252916.1.
    UniGenei Hs.501728.

    3D structure databases

    ProteinModelPortali P84095.
    SMRi P84095. Positions 1-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106884. 10 interactions.
    IntActi P84095. 2 interactions.
    MINTi MINT-4132365.
    STRINGi 9606.ENSP00000339467.

    PTM databases

    PhosphoSitei P84095.

    Polymorphism databases

    DMDMi 51338611.

    Proteomic databases

    MaxQBi P84095.
    PaxDbi P84095.
    PeptideAtlasi P84095.
    PRIDEi P84095.

    Protocols and materials databases

    DNASUi 391.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351018 ; ENSP00000339467 ; ENSG00000177105 .
    ENST00000396978 ; ENSP00000380175 ; ENSG00000177105 .
    ENST00000396979 ; ENSP00000380176 ; ENSG00000177105 .
    ENST00000533217 ; ENSP00000436932 ; ENSG00000177105 .
    GeneIDi 391.
    KEGGi hsa:391.
    UCSCi uc001lyu.2. human.

    Organism-specific databases

    CTDi 391.
    GeneCardsi GC11M003848.
    HGNCi HGNC:672. RHOG.
    HPAi HPA039871.
    MIMi 179505. gene.
    neXtProti NX_P84095.
    PharmGKBi PA24955.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi P84095.
    KOi K07863.
    OMAi KRGRSCF.
    OrthoDBi EOG764747.
    PhylomeDBi P84095.
    TreeFami TF101109.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.

    Miscellaneous databases

    ChiTaRSi RHOG. human.
    GeneWikii RhoG.
    GenomeRNAii 391.
    NextBioi 1631.
    PROi P84095.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P84095.
    Bgeei P84095.
    CleanExi HS_RHOG.
    Genevestigatori P84095.

    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. "Growth-regulated expression of rhoG, a new member of the ras homolog gene family."
      Vincent S., Jeanteur P., Fort P.
      Mol. Cell. Biol. 12:3138-3148(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Oncogene ect2 is related to regulators of small GTP-binding proteins."
      Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.
      Nature 362:462-465(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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 (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "SGEF, a RhoG guanine nucleotide exchange factor that stimulates macropinocytosis."
      Ellerbroek S.M., Wennerberg K., Arthur W.T., Dunty J.M., Bowman D.R., DeMali K.A., Der C., Burridge K.
      Mol. Biol. Cell 15:3309-3319(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF26, FUNCTION.
    5. "Differential activation and function of Rho GTPases during Salmonella-host cell interactions."
      Patel J.C., Galan J.E.
      J. Cell Biol. 175:453-463(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration."
      van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E., Garcia-Mata R., Burridge K.
      J. Cell Biol. 178:1279-1293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism."
      Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S., Negishi M., Katoh H.
      J. Cell Biol. 190:461-477(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARHGEF16.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRHOG_HUMAN
    AccessioniPrimary (citable) accession number: P84095
    Secondary accession number(s): P35238, Q8NI04
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 113 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3