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Q92888

- ARHG1_HUMAN

UniProt

Q92888 - ARHG1_HUMAN

Protein

Rho guanine nucleotide exchange factor 1

Gene

ARHGEF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (29 Aug 2003)
      Previous versions | rss
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    Functioni

    Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12. Mediates angiotensin-2-induced RhoA activation.4 Publications

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. Rho guanyl-nucleotide exchange factor activity Source: ProtInc

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. negative regulation of axonogenesis Source: Reactome
    3. neurotrophin TRK receptor signaling pathway Source: Reactome
    4. positive regulation of Rho GTPase activity Source: GOC
    5. regulation of axonogenesis Source: Reactome
    6. Rho protein signal transduction Source: ProtInc
    7. termination of G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    GTPase activation, Guanine-nucleotide releasing factor

    Enzyme and pathway databases

    ReactomeiREACT_13815. Axonal growth inhibition (RHOA activation).
    REACT_18407. G alpha (12/13) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho guanine nucleotide exchange factor 1
    Alternative name(s):
    115 kDa guanine nucleotide exchange factor
    Short name:
    p115-RhoGEF
    Short name:
    p115RhoGEF
    Sub1.5
    Gene namesi
    Name:ARHGEF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:681. ARHGEF1.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane 1 Publication
    Note: Translocated to the membrane by activated GNA13 or LPA stimulation.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi487 – 4871Y → F: No effect. 1 Publication
    Mutagenesisi738 – 7381Y → F: Lowers the exchange activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24966.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 912912Rho guanine nucleotide exchange factor 1PRO_0000080906Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei738 – 7381Phosphotyrosine; by JAK22 Publications
    Modified residuei863 – 8631Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by PKCA. Angiotensin-2 induced Tyr-738 phosphorylation is mediated by JAK2.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ92888.
    PaxDbiQ92888.
    PRIDEiQ92888.

    PTM databases

    PhosphoSiteiQ92888.

    Miscellaneous databases

    PMAP-CutDBQ92888.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ92888.
    BgeeiQ92888.
    CleanExiHS_ARHGEF1.
    GenevestigatoriQ92888.

    Organism-specific databases

    HPAiCAB009502.
    HPA012924.

    Interactioni

    Subunit structurei

    Interacts with RHOA, GNA12 and GNA13. Homooligomerizes through the coiled coil region. May interact with CCPG1 By similarity. Interacts with CTNNAL1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GNA13Q143443EBI-465400,EBI-465387
    Z5115Q7DB747EBI-465400,EBI-7864788From a different organism.

    Protein-protein interaction databases

    BioGridi114585. 19 interactions.
    IntActiQ92888. 13 interactions.
    MINTiMINT-2813461.
    STRINGi9606.ENSP00000337261.

    Structurei

    Secondary structure

    1
    912
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 203
    Turni26 – 338
    Helixi49 – 524
    Helixi56 – 6914
    Helixi73 – 8412
    Helixi89 – 10315
    Helixi116 – 1227
    Turni127 – 1293
    Helixi132 – 14413
    Helixi147 – 16216
    Helixi169 – 1768
    Helixi183 – 20321
    Helixi205 – 2073
    Helixi212 – 22817
    Turni399 – 4013
    Helixi404 – 4074
    Helixi413 – 44129
    Helixi443 – 4497
    Helixi454 – 4607
    Helixi464 – 48421
    Helixi493 – 5008
    Helixi502 – 51716
    Helixi519 – 53214
    Helixi534 – 54411
    Helixi547 – 5493
    Helixi554 – 5574
    Helixi560 – 57718
    Helixi582 – 62140
    Helixi625 – 6295
    Helixi633 – 6353
    Beta strandi636 – 6383
    Beta strandi644 – 6463
    Beta strandi648 – 66114
    Beta strandi663 – 68119
    Beta strandi684 – 6863
    Beta strandi694 – 6974
    Beta strandi706 – 7094
    Helixi710 – 7123
    Beta strandi713 – 7175
    Beta strandi719 – 7213
    Beta strandi724 – 7296
    Beta strandi737 – 7415
    Helixi745 – 76016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IAPX-ray1.90A42-252[»]
    1SHZX-ray2.85C/F7-239[»]
    3AB3X-ray2.40B/D1-233[»]
    3ODOX-ray2.90A/B395-766[»]
    3ODWX-ray3.20A/B240-766[»]
    3ODXX-ray3.20A/B353-766[»]
    3P6AX-ray2.50A/B395-766[»]
    ProteinModelPortaliQ92888.
    SMRiQ92888. Positions 44-233, 395-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92888.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 232192RGSLAdd
    BLAST
    Domaini416 – 605190DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini647 – 760114PHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili865 – 89632Sequence AnalysisAdd
    BLAST

    Domaini

    The RGSL domain, also known as rgRGS domain, is necessary but not sufficient for GAP activity.
    The DH domain is involved in interaction with CCPG1.By similarity

    Sequence similaritiesi

    Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 RGSL (RGS-like) domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5422.
    HOGENOMiHOG000034043.
    HOVERGENiHBG050565.
    KOiK12330.
    OrthoDBiEOG7GJ6CF.
    PhylomeDBiQ92888.
    TreeFamiTF106495.

    Family and domain databases

    Gene3Di1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR000219. DH-domain.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR015212. RGS-like_dom.
    IPR015721. RhoGEF-like.
    [Graphical view]
    PANTHERiPTHR22825. PTHR22825. 1 hit.
    PfamiPF09128. RGS-like. 1 hit.
    PF00621. RhoGEF. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    [Graphical view]
    SUPFAMiSSF48065. SSF48065. 1 hit.
    SSF48097. SSF48097. 1 hit.
    PROSITEiPS50010. DH_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92888-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEDFARGAAS PGPSRPGLVP VSIIGAEDED FENELETNSE EQNSQFQSLE    50
    QVKRRPAHLM ALLQHVALQF EPGPLLCCLH ADMLGSLGPK EAKKAFLDFY 100
    HSFLEKTAVL RVPVPPNVAF ELDRTRADLI SEDVQRRFVQ EVVQSQQVAV 150
    GRQLEDFRSK RLMGMTPWEQ ELAQLEAWVG RDRASYEARE RHVAERLLMH 200
    LEEMQHTIST DEEKSAAVVN AIGLYMRHLG VRTKSGDKKS GRNFFRKKVM 250
    GNRRSDEPAK TKKGLSSILD AARWNRGEPQ VPDFRHLKAE VDAEKPGATD 300
    RKGGVGMPSR DRNIGAPGQD TPGVSLHPLS LDSPDREPGA DAPLELGDSS 350
    PQGPMSLESL APPESTDEGA ETESPEPGDE GEPGRSGLEL EPEEPPGWRE 400
    LVPPDTLHSL PKSQVKRQEV ISELLVTEAA HVRMLRVLHD LFFQPMAECL 450
    FFPLEELQNI FPSLDELIEV HSLFLDRLMK RRQESGYLIE EIGDVLLARF 500
    DGAEGSWFQK ISSRFCSRQS FALEQLKAKQ RKDPRFCAFV QEAESRPRCR 550
    RLQLKDMIPT EMQRLTKYPL LLQSIGQNTE EPTEREKVEL AAECCREILH 600
    HVNQAVRDME DLLRLKDYQR RLDLSHLRQS SDPMLSEFKN LDITKKKLVH 650
    EGPLTWRVTK DKAVEVHVLL LDDLLLLLQR QDERLLLKSH SRTLTPTPDG 700
    KTMLRPVLRL TSAMTREVAT DHKAFYVLFT WDQEAQIYEL VAQTVSERKN 750
    WCALITETAG SLKVPAPASR PKPRPSPSST REPLLSSSEN GNGGRETSPA 800
    DARTERILSD LLPFCRPGPE GQLAATALRK VLSLKQLLFP AEEDNGAGPP 850
    RDGDGVPGGG PLSPARTQEI QENLLSLEET MKQLEELEEE FCRLRPLLSQ 900
    LGGNSVPQPG CT 912
    Length:912
    Mass (Da):102,435
    Last modified:August 29, 2003 - v2
    Checksum:i1E773D041652190D
    GO
    Isoform 2 (identifier: Q92888-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-108: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:879
    Mass (Da):98,768
    Checksum:i1D0863A5D1A57C9B
    GO
    Isoform 3 (identifier: Q92888-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MASLSTWSSPAEPREM

    Note: No experimental confirmation available.

    Show »
    Length:927
    Mass (Da):104,066
    Checksum:iB2E593D5B2DCE417
    GO

    Sequence cautioni

    The sequence CAA70356.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence CAA70356.1 differs from that shown. Reason: Frameshift at position 904.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti257 – 2593EPA → DPP in AAB17896. (PubMed:8810315)Curated
    Sequence conflicti305 – 3084VGMP → GGDA in CAA70356. (PubMed:9135076)Curated
    Sequence conflicti339 – 3391Missing in CAA70356. (PubMed:9135076)Curated
    Sequence conflicti346 – 3527LGDSSPQ → PGGLIPA in CAA70356. (PubMed:9135076)Curated
    Sequence conflicti549 – 5491C → S in CAA70356. (PubMed:9135076)Curated
    Sequence conflicti752 – 7521C → S in CAA70356. (PubMed:9135076)Curated
    Sequence conflicti776 – 7761S → R in AAB17896. (PubMed:8810315)Curated
    Sequence conflicti862 – 8621L → R in CAA70356. (PubMed:9135076)Curated
    Sequence conflicti876 – 8761S → R in CAA70356. (PubMed:9135076)Curated
    Sequence conflicti883 – 8831Q → T in CAA70356. (PubMed:9135076)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti165 – 1651M → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035969
    Natural varianti375 – 3751P → L.
    Corresponds to variant rs2303797 [ dbSNP | Ensembl ].
    VAR_033521

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MASLSTWSSPAEPREM in isoform 3. 1 PublicationVSP_037766
    Alternative sequencei76 – 10833Missing in isoform 2. 1 PublicationVSP_008125Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U64105 mRNA. Translation: AAB17896.1.
    BC005155 mRNA. Translation: AAH05155.2.
    BC011726 mRNA. Translation: AAH11726.1.
    BC015652 mRNA. No translation available.
    BC034013 mRNA. Translation: AAH34013.2.
    Y09160 mRNA. Translation: CAA70356.1. Sequence problems.
    BT007421 mRNA. Translation: AAP36089.1.
    CCDSiCCDS12590.1. [Q92888-3]
    CCDS12591.1. [Q92888-1]
    CCDS12592.1. [Q92888-2]
    RefSeqiNP_004697.2. NM_004706.3. [Q92888-1]
    NP_945328.1. NM_198977.1. [Q92888-2]
    NP_945353.1. NM_199002.1. [Q92888-3]
    UniGeneiHs.631550.

    Genome annotation databases

    EnsembliENST00000337665; ENSP00000337261; ENSG00000076928. [Q92888-3]
    ENST00000347545; ENSP00000344429; ENSG00000076928. [Q92888-2]
    ENST00000354532; ENSP00000346532; ENSG00000076928. [Q92888-1]
    GeneIDi9138.
    KEGGihsa:9138.
    UCSCiuc002orx.3. human. [Q92888-1]
    uc002ory.3. human. [Q92888-2]
    uc002osa.3. human. [Q92888-3]

    Polymorphism databases

    DMDMi34395524.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U64105 mRNA. Translation: AAB17896.1 .
    BC005155 mRNA. Translation: AAH05155.2 .
    BC011726 mRNA. Translation: AAH11726.1 .
    BC015652 mRNA. No translation available.
    BC034013 mRNA. Translation: AAH34013.2 .
    Y09160 mRNA. Translation: CAA70356.1 . Sequence problems.
    BT007421 mRNA. Translation: AAP36089.1 .
    CCDSi CCDS12590.1. [Q92888-3 ]
    CCDS12591.1. [Q92888-1 ]
    CCDS12592.1. [Q92888-2 ]
    RefSeqi NP_004697.2. NM_004706.3. [Q92888-1 ]
    NP_945328.1. NM_198977.1. [Q92888-2 ]
    NP_945353.1. NM_199002.1. [Q92888-3 ]
    UniGenei Hs.631550.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IAP X-ray 1.90 A 42-252 [» ]
    1SHZ X-ray 2.85 C/F 7-239 [» ]
    3AB3 X-ray 2.40 B/D 1-233 [» ]
    3ODO X-ray 2.90 A/B 395-766 [» ]
    3ODW X-ray 3.20 A/B 240-766 [» ]
    3ODX X-ray 3.20 A/B 353-766 [» ]
    3P6A X-ray 2.50 A/B 395-766 [» ]
    ProteinModelPortali Q92888.
    SMRi Q92888. Positions 44-233, 395-761.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114585. 19 interactions.
    IntActi Q92888. 13 interactions.
    MINTi MINT-2813461.
    STRINGi 9606.ENSP00000337261.

    PTM databases

    PhosphoSitei Q92888.

    Polymorphism databases

    DMDMi 34395524.

    Proteomic databases

    MaxQBi Q92888.
    PaxDbi Q92888.
    PRIDEi Q92888.

    Protocols and materials databases

    DNASUi 9138.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337665 ; ENSP00000337261 ; ENSG00000076928 . [Q92888-3 ]
    ENST00000347545 ; ENSP00000344429 ; ENSG00000076928 . [Q92888-2 ]
    ENST00000354532 ; ENSP00000346532 ; ENSG00000076928 . [Q92888-1 ]
    GeneIDi 9138.
    KEGGi hsa:9138.
    UCSCi uc002orx.3. human. [Q92888-1 ]
    uc002ory.3. human. [Q92888-2 ]
    uc002osa.3. human. [Q92888-3 ]

    Organism-specific databases

    CTDi 9138.
    GeneCardsi GC19P042387.
    HGNCi HGNC:681. ARHGEF1.
    HPAi CAB009502.
    HPA012924.
    MIMi 601855. gene.
    neXtProti NX_Q92888.
    PharmGKBi PA24966.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5422.
    HOGENOMi HOG000034043.
    HOVERGENi HBG050565.
    KOi K12330.
    OrthoDBi EOG7GJ6CF.
    PhylomeDBi Q92888.
    TreeFami TF106495.

    Enzyme and pathway databases

    Reactomei REACT_13815. Axonal growth inhibition (RHOA activation).
    REACT_18407. G alpha (12/13) signalling events.

    Miscellaneous databases

    ChiTaRSi ARHGEF1. human.
    EvolutionaryTracei Q92888.
    GeneWikii ARHGEF1.
    GenomeRNAii 9138.
    NextBioi 34263.
    PMAP-CutDB Q92888.
    PROi Q92888.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92888.
    Bgeei Q92888.
    CleanExi HS_ARHGEF1.
    Genevestigatori Q92888.

    Family and domain databases

    Gene3Di 1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR000219. DH-domain.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR015212. RGS-like_dom.
    IPR015721. RhoGEF-like.
    [Graphical view ]
    PANTHERi PTHR22825. PTHR22825. 1 hit.
    Pfami PF09128. RGS-like. 1 hit.
    PF00621. RhoGEF. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48065. SSF48065. 1 hit.
    SSF48097. SSF48097. 1 hit.
    PROSITEi PS50010. DH_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel guanine nucleotide exchange factor for the rho GTPase."
      Hart M.J., Sharma S., el Masry N., Qiu R.-G., McCabe P., Polakis P., Bollag G.
      J. Biol. Chem. 271:25452-25458(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RHOA, TISSUE SPECIFICITY.
    2. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: B-cell, Muscle and Placenta.
    3. "Characterization, expression and chromosomal localization of a human gene homologous to the mouse Lsc oncogene, with strongest expression in hematopoetic tissues."
      Aasheim H.-C., Pedeutour F., Smeland E.B.
      Oncogene 14:1747-1752(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-912 (ISOFORM 1), TISSUE SPECIFICITY.
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-912 (ISOFORM 1).
    5. "p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13."
      Kozasa T., Jiang X., Hart M.J., Sternweis P.M., Singer W.D., Gilman A.G., Bollag G., Sternweis P.C.
      Science 280:2109-2111(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13."
      Hart M.J., Jiang X., Kozasa T., Roscoe W., Singer W.D., Gilman A.G., Sternweis P.C., Bollag G.
      Science 280:2112-2114(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GNA13.
    7. "Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding."
      Bhattacharyya R., Wedegaertner P.B.
      J. Biol. Chem. 275:14992-14999(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports serum response factor activation."
      Park B., Nguyen N.T., Dutt P., Merdek K.D., Bashar M., Sterpetti P., Tosolini A., Testa J.R., Toksoz D.
      J. Biol. Chem. 277:45361-45370(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTNNAL1.
    9. "PKCa-induced p115RhoGEF phosphorylation signals endothelial cytoskeletal rearrangement."
      Holinstat M., Mehta D., Kozasa T., Minshall R.D., Malik A.B.
      J. Biol. Chem. 278:28793-28798(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PKCA.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on vascular tone and blood pressure."
      Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M., Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A., Torres R.M., Offermanns S., Pacaud P., Loirand G.
      Nat. Med. 16:183-190(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT TYR-738, MUTAGENESIS OF TYR-487 AND TYR-738.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-252.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-165.

    Entry informationi

    Entry nameiARHG1_HUMAN
    AccessioniPrimary (citable) accession number: Q92888
    Secondary accession number(s): O00513
    , Q8N4J4, Q96BF4, Q96F17, Q9BSB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2003
    Last sequence update: August 29, 2003
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3