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Q07960

- RHG01_HUMAN

UniProt

Q07960 - RHG01_HUMAN

Protein

Rho GTPase-activating protein 1

Gene

ARHGAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei282 – 2821Involved in G-protein binding to GAPsCurated

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. Rac GTPase activator activity Source: Ensembl
    3. Rho GTPase activator activity Source: MGI
    4. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. positive regulation of signal transduction Source: GOC
    2. regulation of small GTPase mediated signal transduction Source: Reactome
    3. Rho protein signal transduction Source: ProtInc
    4. small GTPase mediated signal transduction Source: MGI

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho GTPase-activating protein 1
    Alternative name(s):
    CDC42 GTPase-activating protein
    GTPase-activating protein rhoOGAP
    Rho-related small GTPase protein activator
    Rho-type GTPase-activating protein 1
    p50-RhoGAP
    Gene namesi
    Name:ARHGAP1
    Synonyms:CDC42GAP, RHOGAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:673. ARHGAP1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24956.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Rho GTPase-activating protein 1PRO_0000056700Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei51 – 511Phosphoserine3 Publications
    Modified residuei65 – 651PhosphotyrosineBy similarity
    Modified residuei80 – 801N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ07960.
    PaxDbiQ07960.
    PeptideAtlasiQ07960.
    PRIDEiQ07960.

    2D gel databases

    OGPiQ07960.

    PTM databases

    PhosphoSiteiQ07960.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ07960.
    BgeeiQ07960.
    CleanExiHS_ARHGAP1.
    GenevestigatoriQ07960.

    Organism-specific databases

    HPAiHPA004689.
    HPA008285.

    Interactioni

    Subunit structurei

    Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with BNIPL.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC42P609532EBI-602762,EBI-81752
    CDC42P60953-22EBI-602762,EBI-287394
    RHOAP615862EBI-602762,EBI-446668

    Protein-protein interaction databases

    BioGridi106885. 14 interactions.
    DIPiDIP-6081N.
    IntActiQ07960. 6 interactions.
    MINTiMINT-5006067.
    STRINGi9606.ENSP00000310491.

    Structurei

    Secondary structure

    1
    439
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi242 – 2443
    Helixi246 – 2527
    Helixi261 – 27313
    Turni278 – 2825
    Helixi287 – 29812
    Helixi305 – 3073
    Helixi312 – 32413
    Beta strandi325 – 3273
    Helixi332 – 3343
    Helixi335 – 3395
    Helixi341 – 3433
    Helixi346 – 3483
    Helixi349 – 3579
    Helixi362 – 38019
    Helixi382 – 3854
    Helixi389 – 40012
    Helixi406 – 4116
    Helixi413 – 42513
    Helixi427 – 4304

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AM4X-ray2.70A/B/C233-431[»]
    1GRNX-ray2.10B237-439[»]
    1OW3X-ray1.80A198-439[»]
    1RGPX-ray2.00A198-439[»]
    1TX4X-ray1.65A234-431[»]
    2NGRX-ray1.90B206-439[»]
    DisProtiDP00459.
    ProteinModelPortaliQ07960.
    SMRiQ07960. Positions 236-431.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07960.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 218156CRAL-TRIOPROSITE-ProRule annotationAdd
    BLAST
    Domaini244 – 431188Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi228 – 23811SH3-bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiNOG260235.
    HOGENOMiHOG000231442.
    HOVERGENiHBG054433.
    InParanoidiQ07960.
    OMAiFYDIARH.
    PhylomeDBiQ07960.
    TreeFamiTF324164.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    3.40.525.10. 1 hit.
    InterProiIPR001251. CRAL-TRIO_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF13716. CRAL_TRIO_2. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00324. RhoGAP. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF52087. SSF52087. 1 hit.
    PROSITEiPS50191. CRAL_TRIO. 1 hit.
    PS50238. RHOGAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07960-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPLSELQDD LTLDDTSEAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS    50
    SPELVTHLKW DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD 100
    HSKLLGYLKH TLDQYVESDY TLLYLHHGLT SDNKPSLSWL RDAYREFDRK 150
    YKKNIKALYI VHPTMFIKTL LILFKPLISF KFGQKIFYVN YLSELSEHVK 200
    LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ QFGVSLQHLQ 250
    EKNPEQEPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG 300
    LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV 350
    PATLQVLQTL PEENYQVLRF LTAFLVQISA HSDQNKMTNT NLAVVFGPNL 400
    LWAKDAAITL KAINPINTFT KFLLDHQGEL FPSPDPSGL 439
    Length:439
    Mass (Da):50,436
    Last modified:November 1, 1996 - v1
    Checksum:i4DD0CC4419849C35
    GO

    Sequence cautioni

    The sequence AAA16142.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti369 – 3691R → C.
    Corresponds to variant rs11822837 [ dbSNP | Ensembl ].
    VAR_049137

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02570 mRNA. Translation: AAA16142.1. Different initiation.
    Z23024 mRNA. Translation: CAA80560.1.
    CH471064 Genomic DNA. Translation: EAW67983.1.
    CH471064 Genomic DNA. Translation: EAW67984.1.
    BC018118 mRNA. Translation: AAH18118.1.
    CCDSiCCDS7922.1.
    PIRiA49678.
    RefSeqiNP_004299.1. NM_004308.3.
    UniGeneiHs.138860.

    Genome annotation databases

    EnsembliENST00000311956; ENSP00000310491; ENSG00000175220.
    GeneIDi392.
    KEGGihsa:392.
    UCSCiuc001ndd.4. human.

    Polymorphism databases

    DMDMi3024550.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02570 mRNA. Translation: AAA16142.1 . Different initiation.
    Z23024 mRNA. Translation: CAA80560.1 .
    CH471064 Genomic DNA. Translation: EAW67983.1 .
    CH471064 Genomic DNA. Translation: EAW67984.1 .
    BC018118 mRNA. Translation: AAH18118.1 .
    CCDSi CCDS7922.1.
    PIRi A49678.
    RefSeqi NP_004299.1. NM_004308.3.
    UniGenei Hs.138860.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AM4 X-ray 2.70 A/B/C 233-431 [» ]
    1GRN X-ray 2.10 B 237-439 [» ]
    1OW3 X-ray 1.80 A 198-439 [» ]
    1RGP X-ray 2.00 A 198-439 [» ]
    1TX4 X-ray 1.65 A 234-431 [» ]
    2NGR X-ray 1.90 B 206-439 [» ]
    DisProti DP00459.
    ProteinModelPortali Q07960.
    SMRi Q07960. Positions 236-431.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106885. 14 interactions.
    DIPi DIP-6081N.
    IntActi Q07960. 6 interactions.
    MINTi MINT-5006067.
    STRINGi 9606.ENSP00000310491.

    PTM databases

    PhosphoSitei Q07960.

    Polymorphism databases

    DMDMi 3024550.

    2D gel databases

    OGPi Q07960.

    Proteomic databases

    MaxQBi Q07960.
    PaxDbi Q07960.
    PeptideAtlasi Q07960.
    PRIDEi Q07960.

    Protocols and materials databases

    DNASUi 392.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311956 ; ENSP00000310491 ; ENSG00000175220 .
    GeneIDi 392.
    KEGGi hsa:392.
    UCSCi uc001ndd.4. human.

    Organism-specific databases

    CTDi 392.
    GeneCardsi GC11M046698.
    HGNCi HGNC:673. ARHGAP1.
    HPAi HPA004689.
    HPA008285.
    MIMi 602732. gene.
    neXtProti NX_Q07960.
    PharmGKBi PA24956.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260235.
    HOGENOMi HOG000231442.
    HOVERGENi HBG054433.
    InParanoidi Q07960.
    OMAi FYDIARH.
    PhylomeDBi Q07960.
    TreeFami TF324164.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi ARHGAP1. human.
    EvolutionaryTracei Q07960.
    GeneWikii ARHGAP1.
    GenomeRNAii 392.
    NextBioi 1635.
    PROi Q07960.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07960.
    Bgeei Q07960.
    CleanExi HS_ARHGAP1.
    Genevestigatori Q07960.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    3.40.525.10. 1 hit.
    InterProi IPR001251. CRAL-TRIO_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF13716. CRAL_TRIO_2. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00324. RhoGAP. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF52087. SSF52087. 1 hit.
    PROSITEi PS50191. CRAL_TRIO. 1 hit.
    PS50238. RHOGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a human CDC42 GTPase-activating protein reveals a functional SH3-binding domain."
      Barfod E.T., Zheng Y., Kuang W.-J., Hart M.J., Evans T., Cerione R.A., Ashkenazi A.
      J. Biol. Chem. 268:26059-26062(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Platelet.
    2. "Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases."
      Lancaster C.A., Taylor-Harris P.M., Self A.J., Brill S., van Erp H.E., Hall A.
      J. Biol. Chem. 269:1137-1142(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibrosarcoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Pancreas.
    5. "Purification and N-terminal sequence of the p21rho GTPase-activating protein, rho GAP."
      Garrett M.D., Major G.N., Totty N., Hall A.
      Biochem. J. 276:833-836(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 213-227.
      Tissue: Spleen.
    6. Cited for: PROTEIN SEQUENCE OF 386-416.
    7. "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis."
      Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H., Zhang P., Shen L., Wan D., Gu J.
      Biochem. Biophys. Res. Commun. 308:379-385(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BNIPL.
    8. "Exportin 7 defines a novel general nuclear export pathway."
      Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
      EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; EIF4A1; VPS26A; VPS29; VPS35 AND SFN.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 198-439.
    18. "Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP."
      Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D., Laue E., Gamblin S.J., Smerdon S.J.
      Nature 388:693-697(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 233-431 IN COMPLEX WITH CDC42.

    Entry informationi

    Entry nameiRHG01_HUMAN
    AccessioniPrimary (citable) accession number: Q07960
    Secondary accession number(s): D3DQQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 153 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 11
      Human chromosome 11: 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