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Q9Z272

- GIT1_RAT

UniProt

Q9Z272 - GIT1_RAT

Protein

ARF GTPase-activating protein GIT1

Gene

Git1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri11 – 3424C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ARF GTPase activator activity Source: RGD
    2. protein binding Source: IntAct
    3. protein homodimerization activity Source: RGD
    4. small GTPase binding Source: RGD
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. positive regulation of GTPase activity Source: GOC
    2. regulation of ARF GTPase activity Source: InterPro
    3. regulation of G-protein coupled receptor protein signaling pathway Source: RGD

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ARF GTPase-activating protein GIT1
    Short name:
    ARF GAP GIT1
    Alternative name(s):
    Cool-associated and tyrosine-phosphorylated protein 1
    Short name:
    CAT-1
    Short name:
    CAT1
    G protein-coupled receptor kinase-interactor 1
    GRK-interacting protein 1
    Gene namesi
    Name:Git1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69331. Git1.

    Subcellular locationi

    Cytoplasm By similarity
    Note: Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytoplasmic complexes and membrane protrusions. During cell migration, when cells detach, moves from the adhesions into the cytoplasmic complexes towards the leading edge, while, when cells adhere, it is found in vinculin-containing adhesions. Recruitment to adhesions may be mediated by active tyrosine-phosphorylated paxillin By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. focal adhesion Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 770770ARF GTPase-activating protein GIT1PRO_0000074202Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei224 – 2241PhosphotyrosineBy similarity
    Modified residuei371 – 3711PhosphoserineBy similarity
    Modified residuei373 – 3731PhosphothreonineBy similarity
    Modified residuei384 – 3841PhosphoserineBy similarity
    Modified residuei392 – 3921PhosphotyrosineBy similarity
    Modified residuei394 – 3941PhosphoserineBy similarity
    Modified residuei397 – 3971PhosphoserineBy similarity
    Modified residuei401 – 4011PhosphothreonineBy similarity
    Modified residuei419 – 4191PhosphoserineBy similarity
    Modified residuei554 – 5541PhosphotyrosineBy similarity
    Modified residuei563 – 5631PhosphotyrosineBy similarity
    Modified residuei601 – 6011PhosphoserineBy similarity
    Modified residuei605 – 6051PhosphoserineBy similarity
    Modified residuei610 – 6101PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues by PTK2/FAK1 and SRC in growing fibroblasts. Tyrosine-phosphorylation is increased following cell spreading on fibronectin, decreased in cells arrested in mitosis and increased in the ensuing G1 phase By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9Z272.
    PRIDEiQ9Z272.

    PTM databases

    PhosphoSiteiQ9Z272.

    Expressioni

    Tissue specificityi

    Expressed in numerous tissues, with highest levels in testis.1 Publication

    Gene expression databases

    GenevestigatoriQ9Z272.

    Interactioni

    Subunit structurei

    Interacts with SCRIB By similarity. Interacts with G protein-coupled receptor kinases: ADRBK1/GRK2, PPFIA1 and PPFIA4, with ARHGEF6/alpha-PIX, with ARHGEF7/beta-PIX, with PXN/paxillin and with PTK2/FAK1. Component of cytoplasmic complexes, which also contain PXN, ARHGEF6 and PAK1. Interacts with TGFB1I1.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Arhgef7Q9ES282EBI-3842379,EBI-642580From a different organism.

    Protein-protein interaction databases

    BioGridi249809. 4 interactions.
    IntActiQ9Z272. 3 interactions.
    MINTiMINT-261281.
    STRINGi10116.ENSRNOP00000020105.

    Structurei

    Secondary structure

    1
    770
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi432 – 48150
    Beta strandi645 – 6473
    Helixi651 – 67323
    Helixi677 – 69620
    Beta strandi700 – 7023
    Helixi705 – 72622
    Helixi739 – 76628

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JX0NMR-A640-770[»]
    2W6AX-ray1.40A/B426-483[»]
    ProteinModelPortaliQ9Z272.
    SMRiQ9Z272. Positions 640-770.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z272.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 124124Arf-GAPPROSITE-ProRule annotationAdd
    BLAST
    Repeati132 – 16130ANK 1Add
    BLAST
    Repeati166 – 19530ANK 2Add
    BLAST
    Repeati199 – 22830ANK 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni253 – 424172PTK2/FAK1-bindingAdd
    BLAST
    Regioni254 – 376123ARHGEF6-bindingAdd
    BLAST
    Regioni646 – 770125Interaction with PXN and TGFB1I1Add
    BLAST

    Sequence similaritiesi

    Contains 3 ANK repeats.PROSITE-ProRule annotation
    Contains 1 Arf-GAP domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri11 – 3424C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    ANK repeat, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG260681.
    HOGENOMiHOG000232135.
    HOVERGENiHBG012506.
    InParanoidiQ9Z272.
    KOiK05737.
    PhylomeDBiQ9Z272.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001164. ArfGAP.
    IPR022018. GIT1_C.
    IPR013724. GIT_SHD.
    [Graphical view]
    PfamiPF00023. Ank. 1 hit.
    PF01412. ArfGap. 1 hit.
    PF12205. GIT1_C. 1 hit.
    PF08518. GIT_SHD. 2 hits.
    [Graphical view]
    PRINTSiPR00405. REVINTRACTNG.
    SMARTiSM00248. ANK. 3 hits.
    SM00105. ArfGap. 1 hit.
    SM00555. GIT. 2 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 2 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    PS50115. ARFGAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Z272-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRKGPRAEV CADCSAPDPG WASISRGVLV CDECCSVHRS LGRHISIVKH    50
    LRHSAWPPTL LQMVHTLASN GANSIWEHSL LDPAQVQSGR RKANPQDKVH 100
    PIKSEFIRAK YQMLAFVHKL PCRDDDGVTA KDLSKQLHSS VRTGNLETCL 150
    RLLSLGAQAN FFHPEKGTTP LHVAAKAGQT LQAELLVVYG ADPGSPDVNG 200
    RTPIDYARQA GHHELAERLV ECQYELTDRL AFYLCGRKPD HKNGHYIIPQ 250
    MADRSRQKCM SQSLDLSELA KAAKKKLQAL SNRLFEELAM DVYDEVDRRE 300
    NDAVWLATQN HSTLVTERSA VPFLPVNPEY SATRNQGRQK LARFNAREFA 350
    TLIIDILSEA KRRQQGKSLS SPTDNLELSA RNQSDLDDQH DYDSVASDED 400
    TDQEPLPSAG ATRNNRARSM DSSDLSDGAV TLQEYLELKK ALATSEAKVQ 450
    QLMKVNSSLS DELRKLQREI HKLQAENLQL RQPPGPVPVP SLPSERAEHT 500
    LMGPGGSTHR RDRQAFSMYE PGSALKPFGG APGDELATRL QPFHSTELED 550
    DAIYSVHVPA GLYRIRKGVS ASSVTFTPSS PLLSSSQEGS RHASKLSRHG 600
    SGAESDYENT QSGEPLLGLE GKRFLELSKE DELHAELESL DGDPDPGLPS 650
    TEDVILKTEQ VTKNIQELLR AAQEFKHDSF VPCSEKIHLA VTEMASLFPK 700
    RPALEPVRSS LRLLNASAYR LQSECRKTVP PEPGAPVDFQ LLTQQVIQCA 750
    YDIAKAAKQL VTITTREKKQ 770
    Length:770
    Mass (Da):85,231
    Last modified:May 1, 1999 - v1
    Checksum:i797C8EB7FCB3F481
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF085693 mRNA. Translation: AAC83348.1.
    RefSeqiNP_114002.1. NM_031814.1.
    UniGeneiRn.34521.

    Genome annotation databases

    GeneIDi83709.
    KEGGirno:83709.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF085693 mRNA. Translation: AAC83348.1 .
    RefSeqi NP_114002.1. NM_031814.1.
    UniGenei Rn.34521.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JX0 NMR - A 640-770 [» ]
    2W6A X-ray 1.40 A/B 426-483 [» ]
    ProteinModelPortali Q9Z272.
    SMRi Q9Z272. Positions 640-770.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249809. 4 interactions.
    IntActi Q9Z272. 3 interactions.
    MINTi MINT-261281.
    STRINGi 10116.ENSRNOP00000020105.

    PTM databases

    PhosphoSitei Q9Z272.

    Proteomic databases

    PaxDbi Q9Z272.
    PRIDEi Q9Z272.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 83709.
    KEGGi rno:83709.

    Organism-specific databases

    CTDi 28964.
    RGDi 69331. Git1.

    Phylogenomic databases

    eggNOGi NOG260681.
    HOGENOMi HOG000232135.
    HOVERGENi HBG012506.
    InParanoidi Q9Z272.
    KOi K05737.
    PhylomeDBi Q9Z272.

    Miscellaneous databases

    EvolutionaryTracei Q9Z272.
    NextBioi 616273.
    PROi Q9Z272.

    Gene expression databases

    Genevestigatori Q9Z272.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001164. ArfGAP.
    IPR022018. GIT1_C.
    IPR013724. GIT_SHD.
    [Graphical view ]
    Pfami PF00023. Ank. 1 hit.
    PF01412. ArfGap. 1 hit.
    PF12205. GIT1_C. 1 hit.
    PF08518. GIT_SHD. 2 hits.
    [Graphical view ]
    PRINTSi PR00405. REVINTRACTNG.
    SMARTi SM00248. ANK. 3 hits.
    SM00105. ArfGap. 1 hit.
    SM00555. GIT. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 2 hits.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    PS50115. ARFGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Beta2-adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein."
      Premont R.T., Claing A., Vitale N., Freeman J.L.R., Pitcher J.A., Patton W.A., Moss J., Vaughan M., Lefkowitz R.J.
      Proc. Natl. Acad. Sci. U.S.A. 95:14082-14087(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADRBK1, TISSUE SPECIFICITY, CHARACTERIZATION.
    2. "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly."
      Zhao Z.-S., Manser E., Loo T.-H., Lim L.
      Mol. Cell. Biol. 20:6354-6363(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF6; PXN AND PTK2/FAK1.
    3. "Hic-5 interacts with GIT1 with a different binding mode from paxillin."
      Nishiya N., Shirai T., Suzuki W., Nose K.
      J. Biochem. 132:279-289(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1I1.
    4. "Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting."
      Ko J., Kim S., Valtschanoff J.G., Shin H., Lee J.R., Sheng M., Premont R.T., Weinberg R.J., Kim E.
      J. Neurosci. 23:1667-1677(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPFIA1 AND PPFIA4.

    Entry informationi

    Entry nameiGIT1_RAT
    AccessioniPrimary (citable) accession number: Q9Z272
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3