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Q9Y2X7

- GIT1_HUMAN

UniProt

Q9Y2X7 - GIT1_HUMAN

Protein

ARF GTPase-activating protein GIT1

Gene

GIT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (15 Mar 2004)
      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.1 Publication

    Regions

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

    GO - Molecular functioni

    1. ARF GTPase activator activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. regulation of ARF GTPase activity Source: InterPro
    2. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ9Y2X7.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4272. GIT1.

    Subcellular locationi

    Cytoplasm 1 Publication
    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.

    GO - Cellular componenti

    1. aggresome Source: HPA
    2. cytoplasm Source: HPA
    3. focal adhesion Source: HPA
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28683.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 761761ARF GTPase-activating protein GIT1PRO_0000074200Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei224 – 2241PhosphotyrosineBy similarity
    Modified residuei362 – 3621Phosphoserine3 Publications
    Modified residuei364 – 3641Phosphothreonine2 Publications
    Modified residuei375 – 3751Phosphoserine1 Publication
    Modified residuei383 – 3831Phosphotyrosine2 Publications
    Modified residuei385 – 3851Phosphoserine3 Publications
    Modified residuei388 – 3881Phosphoserine7 Publications
    Modified residuei392 – 3921Phosphothreonine2 Publications
    Modified residuei410 – 4101Phosphoserine3 Publications
    Modified residuei545 – 5451Phosphotyrosine1 Publication
    Modified residuei554 – 5541Phosphotyrosine1 Publication
    Modified residuei592 – 5921Phosphoserine4 Publications
    Modified residuei596 – 5961Phosphoserine2 Publications
    Modified residuei601 – 6011Phosphothreonine1 Publication

    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

    MaxQBiQ9Y2X7.
    PaxDbiQ9Y2X7.
    PRIDEiQ9Y2X7.

    PTM databases

    PhosphoSiteiQ9Y2X7.

    Miscellaneous databases

    PMAP-CutDBQ9Y2X7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y2X7.
    BgeeiQ9Y2X7.
    CleanExiHS_GIT1.
    GenevestigatoriQ9Y2X7.

    Organism-specific databases

    HPAiHPA004059.
    HPA004186.

    Interactioni

    Subunit structurei

    Interacts with G protein-coupled receptor kinases: ADRBK1/GRK2, PPFIA1 and PPFIA4. Interacts with ARHGEF6/alpha-PIX, with ARHGEF7/beta-PIX, with PXN/paxillin and with PTK2/FAK1 By similarity. Component of cytoplasmic complexes, which also contain PXN, ARHGEF6 and PAK1. Interacts with TGFB1I1. Interacts with SCRIB.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADRBK1P250985EBI-466061,EBI-3904795
    ARHGEF7Q141554EBI-466061,EBI-717515
    BARD1Q997282EBI-466061,EBI-473181
    CHD3Q128732EBI-466061,EBI-523590
    HTTP4285810EBI-466061,EBI-466029
    KIAA1377Q9P2H02EBI-466061,EBI-473176
    LRIF1Q5T3J32EBI-466061,EBI-473196
    PAK1Q131532EBI-466061,EBI-1307
    PXNP490243EBI-466061,EBI-2896280From a different organism.

    Protein-protein interaction databases

    BioGridi118789. 55 interactions.
    IntActiQ9Y2X7. 39 interactions.
    MINTiMINT-243639.
    STRINGi9606.ENSP00000378338.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2X7.
    SMRiQ9Y2X7. Positions 3-285, 418-473, 631-761.
    ModBaseiSearch...
    MobiDBiSearch...

    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
    Regioni251 – 415165PTK2/FAK1-bindingBy similarityAdd
    BLAST
    Regioni254 – 367114ARHGEF6-bindingBy similarityAdd
    BLAST
    Regioni637 – 761125Interaction with PXN and TGFB1I1By similarityAdd
    BLAST

    Domaini

    The paxillin-binding domain is masked in the full-length protein and is regulated by ARHGEF6.By similarity

    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

    eggNOGiCOG5347.
    HOGENOMiHOG000232135.
    HOVERGENiHBG012506.
    KOiK05737.
    OMAiSARSQSD.
    OrthoDBiEOG7KQ212.
    PhylomeDBiQ9Y2X7.
    TreeFamiTF317762.

    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]
    PfamiPF12796. Ank_2. 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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2X7-1) [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

    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
    MADSLDLSEL AKAAKKKLQA LSNRLFEELA MDVYDEVDRR ENDAVWLATQ 300
    NHSTLVTERS AVPFLPVNPE YSATRNQGRQ KLARFNAREF ATLIIDILSE 350
    AKRRQQGKSL SSPTDNLELS LRSQSDLDDQ HDYDSVASDE DTDQEPLRST 400
    GATRSNRARS MDSSDLSDGA VTLQEYLELK KALATSEAKV QQLMKVNSSL 450
    SDELRRLQRE IHKLQAENLQ LRQPPGPVPT PPLPSERAEH TPMAPGGSTH 500
    RRDRQAFSMY EPGSALKPFG GPPGDELTTR LQPFHSTELE DDAIYSVHVP 550
    AGLYRIRKGV SASAVPFTPS SPLLSCSQEG SRHTSKLSRH GSGADSDYEN 600
    TQSGDPLLGL EGKRFLELGK EEDFHPELES LDGDLDPGLP STEDVILKTE 650
    QVTKNIQELL RAAQEFKHDS FVPCSEKIHL AVTEMASLFP KRPALEPVRS 700
    SLRLLNASAY RLQSECRKTV PPEPGAPVDF QLLTQQVIQC AYDIAKAAKQ 750
    LVTITTREKK Q 761
    Length:761
    Mass (Da):84,341
    Last modified:March 15, 2004 - v2
    Checksum:i702744942A796399
    GO
    Isoform 2 (identifier: Q9Y2X7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-176: SKQLHSSVRT...GTTPLHVAAK → TGHRSWATPD...VPWCPPLSSP
         177-761: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:176
    Mass (Da):19,160
    Checksum:i2B5BB45555AB5201
    GO
    Isoform 3 (identifier: Q9Y2X7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         253-253: D → DRSRQKCMSQ

    Show »
    Length:770
    Mass (Da):85,446
    Checksum:i278AD8D706C32EE0
    GO

    Sequence cautioni

    The sequence AAH48196.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211P → S in AAD28046. (PubMed:10896954)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei134 – 17643SKQLH…HVAAK → TGHRSWATPDINPHPNRATG TSALSAATLPGSQVPWCPPL SSP in isoform 2. 1 PublicationVSP_009666Add
    BLAST
    Alternative sequencei177 – 761585Missing in isoform 2. 1 PublicationVSP_009667Add
    BLAST
    Alternative sequencei253 – 2531D → DRSRQKCMSQ in isoform 3. 1 PublicationVSP_040984

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124490 mRNA. Translation: AAD28046.1.
    AK294785 mRNA. Translation: BAG57910.1.
    AK299932 mRNA. Translation: BAG61765.1.
    AC104564 Genomic DNA. No translation available.
    BC006227 mRNA. Translation: AAH06227.2.
    BC048196 mRNA. Translation: AAH48196.1. Different initiation.
    CCDSiCCDS11250.1. [Q9Y2X7-1]
    CCDS42290.1. [Q9Y2X7-3]
    RefSeqiNP_001078923.1. NM_001085454.1. [Q9Y2X7-3]
    NP_054749.2. NM_014030.3. [Q9Y2X7-1]
    UniGeneiHs.514051.

    Genome annotation databases

    EnsembliENST00000225394; ENSP00000225394; ENSG00000108262. [Q9Y2X7-1]
    ENST00000394869; ENSP00000378338; ENSG00000108262. [Q9Y2X7-3]
    ENST00000581348; ENSP00000462775; ENSG00000108262.
    GeneIDi28964.
    KEGGihsa:28964.
    UCSCiuc002hef.2. human. [Q9Y2X7-1]
    uc002heg.2. human. [Q9Y2X7-3]

    Polymorphism databases

    DMDMi45645212.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124490 mRNA. Translation: AAD28046.1 .
    AK294785 mRNA. Translation: BAG57910.1 .
    AK299932 mRNA. Translation: BAG61765.1 .
    AC104564 Genomic DNA. No translation available.
    BC006227 mRNA. Translation: AAH06227.2 .
    BC048196 mRNA. Translation: AAH48196.1 . Different initiation.
    CCDSi CCDS11250.1. [Q9Y2X7-1 ]
    CCDS42290.1. [Q9Y2X7-3 ]
    RefSeqi NP_001078923.1. NM_001085454.1. [Q9Y2X7-3 ]
    NP_054749.2. NM_014030.3. [Q9Y2X7-1 ]
    UniGenei Hs.514051.

    3D structure databases

    ProteinModelPortali Q9Y2X7.
    SMRi Q9Y2X7. Positions 3-285, 418-473, 631-761.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118789. 55 interactions.
    IntActi Q9Y2X7. 39 interactions.
    MINTi MINT-243639.
    STRINGi 9606.ENSP00000378338.

    PTM databases

    PhosphoSitei Q9Y2X7.

    Polymorphism databases

    DMDMi 45645212.

    Proteomic databases

    MaxQBi Q9Y2X7.
    PaxDbi Q9Y2X7.
    PRIDEi Q9Y2X7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225394 ; ENSP00000225394 ; ENSG00000108262 . [Q9Y2X7-1 ]
    ENST00000394869 ; ENSP00000378338 ; ENSG00000108262 . [Q9Y2X7-3 ]
    ENST00000581348 ; ENSP00000462775 ; ENSG00000108262 .
    GeneIDi 28964.
    KEGGi hsa:28964.
    UCSCi uc002hef.2. human. [Q9Y2X7-1 ]
    uc002heg.2. human. [Q9Y2X7-3 ]

    Organism-specific databases

    CTDi 28964.
    GeneCardsi GC17M027900.
    H-InvDB HIX0013673.
    HGNCi HGNC:4272. GIT1.
    HPAi HPA004059.
    HPA004186.
    MIMi 608434. gene.
    neXtProti NX_Q9Y2X7.
    PharmGKBi PA28683.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5347.
    HOGENOMi HOG000232135.
    HOVERGENi HBG012506.
    KOi K05737.
    OMAi SARSQSD.
    OrthoDBi EOG7KQ212.
    PhylomeDBi Q9Y2X7.
    TreeFami TF317762.

    Enzyme and pathway databases

    SignaLinki Q9Y2X7.

    Miscellaneous databases

    ChiTaRSi GIT1. human.
    GeneWikii GIT1.
    GenomeRNAii 28964.
    NextBioi 51807.
    PMAP-CutDB Q9Y2X7.
    PROi Q9Y2X7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2X7.
    Bgeei Q9Y2X7.
    CleanExi HS_GIT1.
    Genevestigatori Q9Y2X7.

    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 PF12796. Ank_2. 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. "The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing."
      Premont R.T., Claing A., Vitale N., Perry S.J., Lefkowitz R.J.
      J. Biol. Chem. 275:22373-22380(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 585-761 (ISOFORM 1).
      Tissue: Lung and Melanoma.
    5. "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: CHARACTERIZATION.
    6. "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.
    7. "GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration."
      Manabe R., Kovalenko M., Webb D.J., Horwitz A.R.
      J. Cell Sci. 115:1497-1510(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION IN CELL MIGRATION.
    8. Cited for: INTERACTION WITH SCRIB.
    9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Deregulation of scribble promotes mammary tumorigenesis and reveals a role for cell polarity in carcinoma."
      Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C., Muthuswamy S.K.
      Cell 135:865-878(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCRIB.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; TYR-383; SER-385; SER-388; THR-392; SER-410; SER-592 AND SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; THR-364; SER-375; TYR-383; SER-385; SER-388; THR-392; SER-410; TYR-545; SER-592; SER-596 AND THR-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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 THR-364; SER-385; SER-388 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-362 AND SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGIT1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2X7
    Secondary accession number(s): B4DGU9
    , B4DSV3, Q86SS0, Q9BRJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: March 15, 2004
    Last modified: October 1, 2014
    This is version 150 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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