GIT1_HUMAN
ID GIT1_HUMAN Reviewed; 761 AA.
AC Q9Y2X7; B4DGU9; B4DSV3; Q86SS0; Q9BRJ4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=ARF GTPase-activating protein GIT1;
DE Short=ARF GAP GIT1;
DE AltName: Full=Cool-associated and tyrosine-phosphorylated protein 1;
DE Short=CAT-1;
DE Short=CAT1;
DE AltName: Full=G protein-coupled receptor kinase-interactor 1;
DE AltName: Full=GRK-interacting protein 1;
DE AltName: Full=p95-APP1 {ECO:0000303|PubMed:15182672};
GN Name=GIT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH ARHGEF7; PAK3
RP AND PXN.
RX PubMed=10896954; DOI=10.1074/jbc.275.29.22373;
RA Premont R.T., Claing A., Vitale N., Perry S.J., Lefkowitz R.J.;
RT "The GIT family of ADP-ribosylation factor GTPase-activating proteins.
RT Functional diversity of GIT2 through alternative splicing.";
RL J. Biol. Chem. 275:22373-22380(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 585-761 (ISOFORM 1).
RC TISSUE=Lung, and Melanoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH PXN, AND SUBCELLULAR LOCATION.
RX PubMed=10938112; DOI=10.1128/mcb.20.17.6354-6363.2000;
RA Zhao Z.-S., Manser E., Loo T.-H., Lim L.;
RT "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal
RT complex disassembly.";
RL Mol. Cell. Biol. 20:6354-6363(2000).
RN [6]
RP INTERACTION WITH TGFB1I1.
RX PubMed=12153727; DOI=10.1093/oxfordjournals.jbchem.a003222;
RA Nishiya N., Shirai T., Suzuki W., Nose K.;
RT "Hic-5 interacts with GIT1 with a different binding mode from paxillin.";
RL J. Biochem. 132:279-289(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11896197; DOI=10.1242/jcs.115.7.1497;
RA Manabe R., Kovalenko M., Webb D.J., Horwitz A.R.;
RT "GIT1 functions in a motile, multi-molecular signaling complex that
RT regulates protrusive activity and cell migration.";
RL J. Cell Sci. 115:1497-1510(2002).
RN [8]
RP FUNCTION.
RX PubMed=12695502; DOI=10.1083/jcb.200211002;
RA Zhang H., Webb D.J., Asmussen H., Horwitz A.F.;
RT "Synapse formation is regulated by the signaling adaptor GIT1.";
RL J. Cell Biol. 161:131-142(2003).
RN [9]
RP INTERACTION WITH SCRIB.
RX PubMed=15182672; DOI=10.1016/j.cub.2004.05.051;
RA Audebert S., Navarro C., Nourry C., Chasserot-Golaz S., Lecine P.,
RA Bellaiche Y., Dupont J.-L., Premont R.T., Sempere C., Strub J.-M.,
RA Van Dorsselaer A., Vitale N., Borg J.-P.;
RT "Mammalian Scribble forms a tight complex with the betaPIX exchange
RT factor.";
RL Curr. Biol. 14:987-995(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15923189; DOI=10.1074/jbc.m502271200;
RA Yin G., Zheng Q., Yan C., Berk B.C.;
RT "GIT1 is a scaffold for ERK1/2 activation in focal adhesions.";
RL J. Biol. Chem. 280:27705-27712(2005).
RN [11]
RP FUNCTION.
RX PubMed=15800193; DOI=10.1523/jneurosci.3553-04.2005;
RA Zhang H., Webb D.J., Asmussen H., Niu S., Horwitz A.F.;
RT "A GIT1/PIX/Rac/PAK signaling module regulates spine morphogenesis and
RT synapse formation through MLC.";
RL J. Neurosci. 25:3379-3388(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-592, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP INTERACTION WITH SCRIB, AND INDUCTION BY MYC.
RX PubMed=19041750; DOI=10.1016/j.cell.2008.09.045;
RA Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C.,
RA Muthuswamy S.K.;
RT "Deregulation of scribble promotes mammary tumorigenesis and reveals a role
RT for cell polarity in carcinoma.";
RL Cell 135:865-878(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-592, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; TYR-383; SER-385;
RP SER-388; THR-392; SER-410; SER-592 AND SER-596, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP FUNCTION.
RX PubMed=19273721; DOI=10.1161/circulationaha.108.823997;
RA Pang J., Hoefen R., Pryhuber G.S., Wang J., Yin G., White R.J., Xu X.,
RA O'Dell M.R., Mohan A., Michaloski H., Massett M.P., Yan C., Berk B.C.;
RT "G-protein-coupled receptor kinase interacting protein-1 is required for
RT pulmonary vascular development.";
RL Circulation 119:1524-1532(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; THR-364; SER-375;
RP TYR-383; SER-385; SER-388; THR-392; SER-410; TYR-545; SER-592; SER-596 AND
RP THR-601, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-364; SER-385; SER-388 AND
RP SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362 AND SER-388, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; THR-364; SER-370;
RP SER-388; SER-498; SER-592 AND SER-596, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP FUNCTION, INTERACTION WITH ENTR1 AND PTPN13, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-39.
RX PubMed=23108400; DOI=10.1038/onc.2012.485;
RA Hagemann N., Ackermann N., Christmann J., Brier S., Yu F., Erdmann K.S.;
RT "The serologically defined colon cancer antigen-3 interacts with the
RT protein tyrosine phosphatase PTPN13 and is involved in the regulation of
RT cytokinesis.";
RL Oncogene 32:4602-4613(2013).
RN [26]
RP FUNCTION.
RX PubMed=25284783; DOI=10.1016/j.celrep.2014.08.061;
RA Smith K.R., Davenport E.C., Wei J., Li X., Pathania M., Vaccaro V., Yan Z.,
RA Kittler J.T.;
RT "GIT1 and betaPIX are essential for GABA(A) receptor synaptic stability and
RT inhibitory neurotransmission.";
RL Cell Rep. 9:298-310(2014).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; THR-480 AND SER-592, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP FUNCTION, INTERACTION WITH ARHGEF7; GAMMA-TUBULIN; PAK1 AND PXN,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=27012601; DOI=10.1016/j.bbamcr.2016.03.016;
RA Cernohorska M., Sulimenko V., Hajkova Z., Sulimenko T., Sladkova V.,
RA Vinopal S., Draberova E., Draber P.;
RT "GIT1/betaPIX signaling proteins and PAK1 kinase regulate microtubule
RT nucleation.";
RL Biochim. Biophys. Acta 1863:1282-1297(2016).
RN [29]
RP FUNCTION, AND INTERACTION WITH IKBKG.
RX PubMed=31502302; DOI=10.1111/cpr.12689;
RA Li L., Tang P., Zhou Z., Wang Q., Xu T., Zhao S., Huang Y., Kong F.,
RA Liu W., Cheng L., Zhou Z., Zhao X., Gu C., Luo Y., Tao G., Qian D.,
RA Chen J., Fan J., Yin G.;
RT "GIT1 regulates angiogenic factor secretion in bone marrow mesenchymal stem
RT cells via NF-kappaB/Notch signalling to promote angiogenesis.";
RL Cell Prolif. 52:e12689-e12689(2019).
CC -!- FUNCTION: GTPase-activating protein for ADP ribosylation factor family
CC members, including ARF1. Multidomain scaffold protein that interacts
CC with numerous proteins and therefore participates in many cellular
CC functions, including receptor internalization, focal adhesion
CC remodeling, and signaling by both G protein-coupled receptors and
CC tyrosine kinase receptors (By similarity). Through PAK1 activation,
CC positively regulates microtubule nucleation during interphase
CC (PubMed:27012601). Plays a role in the regulation of cytokinesis; for
CC this function, may act in a pathway also involving ENTR1 and PTPN13
CC (PubMed:23108400). May promote cell motility both by regulating focal
CC complex dynamics and by local activation of RAC1 (PubMed:10938112,
CC PubMed:11896197). May act as scaffold for MAPK1/3 signal transduction
CC in focal adhesions. Recruits MAPK1/3/ERK1/2 to focal adhesions after
CC EGF stimulation via a Src-dependent pathway, hence stimulating cell
CC migration (PubMed:15923189). Plays a role in brain development and
CC function. Involved in the regulation of spine density and synaptic
CC plasticity that is required for processes involved in learning (By
CC similarity). Plays an important role in dendritic spine morphogenesis
CC and synapse formation (PubMed:12695502, PubMed:15800193). In
CC hippocampal neurons, recruits guanine nucleotide exchange factors
CC (GEFs), such as ARHGEF7/beta-PIX, to the synaptic membrane. These in
CC turn locally activate RAC1, which is an essential step for spine
CC morphogenesis and synapse formation (PubMed:12695502). May contribute
CC to the organization of presynaptic active zones through oligomerization
CC and formation of a Piccolo/PCLO-based protein network, which includes
CC ARHGEF7/beta-PIX and FAK1 (By similarity). In neurons, through its
CC interaction with liprin-alpha family members, may be required for AMPA
CC receptor (GRIA2/3) proper targeting to the cell membrane (By
CC similarity). In complex with GABA(A) receptors and ARHGEF7, plays a
CC crucial role in regulating GABA(A) receptor synaptic stability,
CC maintaining GPHN/gephyrin scaffolds and hence GABAergic inhibitory
CC synaptic transmission, by locally coordinating RAC1 and PAK1 downstream
CC effector activity, leading to F-actin stabilization (PubMed:25284783).
CC May also be important for RAC1 downstream signaling pathway through
CC PAK3 and regulation of neuronal inhibitory transmission at presynaptic
CC input (By similarity). Required for successful bone regeneration during
CC fracture healing (By similarity). The function in intramembranous
CC ossification may, at least partly, exerted by macrophages in which GIT1
CC is a key negative regulator of redox homeostasis, IL1B production, and
CC glycolysis, acting through the ERK1/2/NRF2/NFE2L2 axis (By similarity).
CC May play a role in angiogenesis during fracture healing (By
CC similarity). In this process, may regulate activation of the canonical
CC NF-kappa-B signal in bone mesenchymal stem cells by enhancing the
CC interaction between NEMO and 'Lys-63'-ubiquitinated RIPK1/RIP1,
CC eventually leading to enhanced production of VEGFA and others
CC angiogenic factors (PubMed:31502302). Essential for VEGF signaling
CC through the activation of phospholipase C-gamma and ERK1/2, hence may
CC control endothelial cell proliferation and angiogenesis
CC (PubMed:19273721). {ECO:0000250|UniProtKB:Q68FF6,
CC ECO:0000250|UniProtKB:Q9Z272, ECO:0000269|PubMed:10938112,
CC ECO:0000269|PubMed:11896197, ECO:0000269|PubMed:12695502,
CC ECO:0000269|PubMed:15800193, ECO:0000269|PubMed:15923189,
CC ECO:0000269|PubMed:19273721, ECO:0000269|PubMed:23108400,
CC ECO:0000269|PubMed:25284783, ECO:0000269|PubMed:27012601,
CC ECO:0000269|PubMed:31502302}.
CC -!- SUBUNIT: Forms homodimers and possibly oligomers (By similarity). May
CC forms heterooligomers with GIT2 (By similarity). Interacts with G
CC protein-coupled receptor kinases, including GRK2, GRK3, GRK5 and GRK6
CC (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA4 (By
CC similarity). Interacts with GRIP1 and forms a ternary complex with
CC PPFIA1 and GRIP1 (By similarity). Directly interacts with ARHGEF7/beta-
CC PIX, forming in vitro a heptameric complex made of a GIT1 dimer and an
CC ARHGEF7 trimer (PubMed:10896954, PubMed:27012601). Directly interacts
CC with PXN/paxillin; this interaction is enhanced in the presence of
CC ARHGEF7 (PubMed:10896954, PubMed:10938112, PubMed:27012601). Directly
CC interacts (via C-terminus) with TGFB1I1/Hic-5 (via LD motif 3)
CC (PubMed:12153727). Directly interacts with PTK2/FAK1 (By similarity).
CC May interact with PTK2B/PYK2; this interaction may be indirect (By
CC similarity). Interacts with AMPA receptors GRIA2/3 (By similarity).
CC Directly interacts with protein Piccolo/PCLO (By similarity). Forms a
CC complex with Ephrin-B1/EFNB1 and NCK2/GRB4 (via SH2); this interaction
CC is important for spine morphogenesis and synapse formation. Interaction
CC with NCK2 is transient and depends upon GIT1 phosphorylation at Tyr-383
CC (By similarity). Interacts with GRIN3A/GluN3A (via C-terminus); this
CC interaction competes with GIT1 interaction with ARHGEF7 and limits
CC synaptic localization of GIT1 (By similarity). Interacts with
CC IKBKG/NEMO in resting bone mesenchymal stem cells, as well as in TNF-
CC stimulated cells; this interaction may increase IKBKG affinity for
CC 'Lys-63'-linked polyubiquitin chains (PubMed:31502302). Interacts with
CC GABA(A) receptors, including GABRB3 and GABRG2 (By similarity).
CC Interacts with SCRIB (PubMed:15182672, PubMed:19041750). Interacts (via
CC N- and C-terminus) with ENTR1/SDCCAG3 (via N-terminus); this
CC interaction is direct (PubMed:23108400). May form a tripartite complex
CC with ENTR1 and PTPN13 (PubMed:23108400). Interacts with YWHAZ (By
CC similarity). Interacts with PAK1 (PubMed:27012601). Interacts with PAK3
CC (PubMed:10896954). Directly interacts (via N-terminus) with gamma-
CC tubulin (PubMed:27012601). Interacts with MAPK1 and MAPK3; this
CC interaction is required for MAPK1/3 recruitment to focal adhesions (By
CC similarity). {ECO:0000250|UniProtKB:Q68FF6,
CC ECO:0000250|UniProtKB:Q9Z272, ECO:0000269|PubMed:10896954,
CC ECO:0000269|PubMed:10938112, ECO:0000269|PubMed:12153727,
CC ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:19041750,
CC ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:27012601,
CC ECO:0000269|PubMed:31502302}.
CC -!- INTERACTION:
CC Q9Y2X7; Q14155: ARHGEF7; NbExp=4; IntAct=EBI-466061, EBI-717515;
CC Q9Y2X7; Q99728: BARD1; NbExp=2; IntAct=EBI-466061, EBI-473181;
CC Q9Y2X7; Q9P2H0: CEP126; NbExp=2; IntAct=EBI-466061, EBI-473176;
CC Q9Y2X7; Q12873: CHD3; NbExp=2; IntAct=EBI-466061, EBI-523590;
CC Q9Y2X7; P62993: GRB2; NbExp=4; IntAct=EBI-466061, EBI-401755;
CC Q9Y2X7; P25098: GRK2; NbExp=5; IntAct=EBI-466061, EBI-3904795;
CC Q9Y2X7; P42858: HTT; NbExp=10; IntAct=EBI-466061, EBI-466029;
CC Q9Y2X7; Q5T3J3: LRIF1; NbExp=2; IntAct=EBI-466061, EBI-473196;
CC Q9Y2X7; Q13153: PAK1; NbExp=5; IntAct=EBI-466061, EBI-1307;
CC Q9Y2X7; P49023: PXN; NbExp=3; IntAct=EBI-466061, EBI-702209;
CC Q9Y2X7; P49024: PXN; Xeno; NbExp=3; IntAct=EBI-466061, EBI-2896280;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11896197}. Synapse
CC {ECO:0000269|PubMed:12695502}. Presynapse
CC {ECO:0000250|UniProtKB:Q9Z272}. Postsynapse
CC {ECO:0000250|UniProtKB:Q9Z272}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9Z272}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:10938112, ECO:0000269|PubMed:11896197,
CC ECO:0000269|PubMed:15923189}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:11896197}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:23108400,
CC ECO:0000269|PubMed:27012601}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:27012601}. Note=Cycles between at least 3 distinct
CC intracellular compartments, including focal adhesions, cytosolic
CC complexes, containing at least PXN/paxillin, ARHGEF7 and PAK1, and
CC membrane protrusions. During cell migration, moves from the
CC disassembling adhesions into the cytosol and towards the leading edge.
CC In adherent cells, localizes to adhesions. Recruitment to adhesions may
CC be mediated by RAC and active tyrosine-phosphorylated PXN
CC (PubMed:11896197). May be present in both excitatory and inhibitory
CC synapses. In hippocampal neurons, recruitment of GIT1 to synapses is
CC regulated by ephrinB activation and ephrinB downstream effector
CC GRB4/NCK2. In hippocampal neurons, partially colocalizes with PCLO (By
CC similarity). Interaction with GRIN3A limits GIT1 synaptic localization
CC (By similarity). Localization to the centrosome does not depend upon
CC the presence of gamma-tubulin (PubMed:27012601).
CC {ECO:0000250|UniProtKB:Q9Z272, ECO:0000269|PubMed:11896197,
CC ECO:0000269|PubMed:27012601}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y2X7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2X7-2; Sequence=VSP_009666, VSP_009667;
CC Name=3;
CC IsoId=Q9Y2X7-3; Sequence=VSP_040984;
CC -!- INDUCTION: Up-regulated at the transcriptional level by MYC.
CC {ECO:0000269|PubMed:19041750}.
CC -!- DOMAIN: The coiled coil region mediates dimerization.
CC {ECO:0000250|UniProtKB:Q9Z272}.
CC -!- PTM: Phosphorylated by PAK1 (PubMed:27012601). Phosphorylation on
CC tyrosine residues may be catalyzed by PTK2/FAK1 and SRC in growing
CC fibroblasts. Phosphorylation at Tyr-383 is induced by activation of
CC Ephrin-B1/EFNB1 and catalyzed by SRC family kinases. It is required for
CC the interaction with NCK2 and for GIT1 recruitment to synapses in
CC hippocampal neurons (By similarity). {ECO:0000250|UniProtKB:Q9Z272,
CC ECO:0000269|PubMed:27012601}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48196.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF124490; AAD28046.1; -; mRNA.
DR EMBL; AK294785; BAG57910.1; -; mRNA.
DR EMBL; AK299932; BAG61765.1; -; mRNA.
DR EMBL; AC104564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006227; AAH06227.2; -; mRNA.
DR EMBL; BC048196; AAH48196.1; ALT_INIT; mRNA.
DR CCDS; CCDS11250.1; -. [Q9Y2X7-1]
DR CCDS; CCDS42290.1; -. [Q9Y2X7-3]
DR RefSeq; NP_001078923.1; NM_001085454.1. [Q9Y2X7-3]
DR RefSeq; NP_054749.2; NM_014030.3. [Q9Y2X7-1]
DR AlphaFoldDB; Q9Y2X7; -.
DR SMR; Q9Y2X7; -.
DR BioGRID; 118789; 128.
DR CORUM; Q9Y2X7; -.
DR IntAct; Q9Y2X7; 62.
DR MINT; Q9Y2X7; -.
DR STRING; 9606.ENSP00000378338; -.
DR GlyGen; Q9Y2X7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2X7; -.
DR PhosphoSitePlus; Q9Y2X7; -.
DR SwissPalm; Q9Y2X7; -.
DR BioMuta; GIT1; -.
DR DMDM; 45645212; -.
DR EPD; Q9Y2X7; -.
DR jPOST; Q9Y2X7; -.
DR MassIVE; Q9Y2X7; -.
DR MaxQB; Q9Y2X7; -.
DR PaxDb; Q9Y2X7; -.
DR PeptideAtlas; Q9Y2X7; -.
DR PRIDE; Q9Y2X7; -.
DR ProteomicsDB; 85928; -. [Q9Y2X7-1]
DR ProteomicsDB; 85929; -. [Q9Y2X7-2]
DR ProteomicsDB; 85930; -. [Q9Y2X7-3]
DR ABCD; Q9Y2X7; 1 sequenced antibody.
DR Antibodypedia; 1365; 497 antibodies from 36 providers.
DR DNASU; 28964; -.
DR Ensembl; ENST00000225394.8; ENSP00000225394.3; ENSG00000108262.16. [Q9Y2X7-1]
DR Ensembl; ENST00000394869.7; ENSP00000378338.3; ENSG00000108262.16. [Q9Y2X7-3]
DR GeneID; 28964; -.
DR KEGG; hsa:28964; -.
DR MANE-Select; ENST00000225394.8; ENSP00000225394.3; NM_014030.4; NP_054749.2.
DR UCSC; uc002hef.3; human. [Q9Y2X7-1]
DR CTD; 28964; -.
DR DisGeNET; 28964; -.
DR GeneCards; GIT1; -.
DR HGNC; HGNC:4272; GIT1.
DR HPA; ENSG00000108262; Tissue enhanced (brain).
DR MIM; 608434; gene.
DR neXtProt; NX_Q9Y2X7; -.
DR OpenTargets; ENSG00000108262; -.
DR PharmGKB; PA28683; -.
DR VEuPathDB; HostDB:ENSG00000108262; -.
DR eggNOG; KOG0818; Eukaryota.
DR GeneTree; ENSGT00940000159604; -.
DR InParanoid; Q9Y2X7; -.
DR OMA; FRNANDC; -.
DR OrthoDB; 349344at2759; -.
DR PhylomeDB; Q9Y2X7; -.
DR TreeFam; TF317762; -.
DR PathwayCommons; Q9Y2X7; -.
DR Reactome; R-HSA-3928664; Ephrin signaling.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9619229; Activation of RAC1 downstream of NMDARs.
DR SignaLink; Q9Y2X7; -.
DR SIGNOR; Q9Y2X7; -.
DR BioGRID-ORCS; 28964; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; GIT1; human.
DR GeneWiki; GIT1; -.
DR GenomeRNAi; 28964; -.
DR Pharos; Q9Y2X7; Tbio.
DR PRO; PR:Q9Y2X7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y2X7; protein.
DR Bgee; ENSG00000108262; Expressed in right frontal lobe and 203 other tissues.
DR ExpressionAtlas; Q9Y2X7; baseline and differential.
DR Genevisible; Q9Y2X7; HS.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001957; P:intramembranous ossification; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0061743; P:motor learning; IEA:Ensembl.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0106015; P:negative regulation of inflammatory response to wounding; ISS:UniProtKB.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IMP:UniProtKB.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IBA:GO_Central.
DR GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0036465; P:synaptic vesicle recycling; IBA:GO_Central.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR032352; GIT1/2_CC.
DR InterPro; IPR022018; GIT1_C.
DR InterPro; IPR013724; GIT_SHD.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF12205; GIT1_C; 1.
DR Pfam; PF16559; GIT_CC; 1.
DR Pfam; PF08518; GIT_SHD; 2.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00555; GIT; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell junction; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; GTPase activation; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..761
FT /note="ARF GTPase-activating protein GIT1"
FT /id="PRO_0000074200"
FT DOMAIN 1..124
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 132..161
FT /note="ANK 1"
FT REPEAT 166..195
FT /note="ANK 2"
FT REPEAT 199..228
FT /note="ANK 3"
FT ZN_FING 11..34
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 1..124
FT /note="Interaction with gamma-tubulin and localization to
FT the centrosome"
FT /evidence="ECO:0000269|PubMed:27012601"
FT REGION 245..365
FT /note="Interaction with PCLO"
FT /evidence="ECO:0000250|UniProtKB:Q9Z272"
FT REGION 253..415
FT /note="Interaction with PTK2/FAK1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z272"
FT REGION 254..367
FT /note="Interaction with ARHGEF7"
FT /evidence="ECO:0000250|UniProtKB:Q9Z272"
FT REGION 354..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..587
FT /note="Interaction with NCK2 and GRIN3A"
FT /evidence="ECO:0000250|UniProtKB:Q9Z272"
FT REGION 366..587
FT /note="Required for localization at synapses"
FT /evidence="ECO:0000269|PubMed:15800193"
FT REGION 411..466
FT /note="Interaction with MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q68FF6"
FT REGION 420..620
FT /note="Interaction with IKBKG"
FT /evidence="ECO:0000269|PubMed:31502302"
FT REGION 471..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..761
FT /note="Interaction with PXN and TGFB1I1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z272"
FT COILED 440..474
FT /evidence="ECO:0000255"
FT COMPBIAS 354..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 224
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68FF6"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FF6"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 383
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FF6"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FF6"
FT MOD_RES 480
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FF6"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68FF6"
FT MOD_RES 545
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 554
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FF6"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z272"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 601
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z272"
FT VAR_SEQ 134..176
FT /note="SKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGTTPLHVAAK -> TGHRS
FT WATPDINPHPNRATGTSALSAATLPGSQVPWCPPLSSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009666"
FT VAR_SEQ 177..761
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009667"
FT VAR_SEQ 253
FT /note="D -> DRSRQKCMSQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040984"
FT MUTAGEN 39
FT /note="R->A: When transfected to cells, increased number of
FT multinucleated cells."
FT /evidence="ECO:0000269|PubMed:23108400"
FT CONFLICT 121
FT /note="P -> S (in Ref. 1; AAD28046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 84341 MW; 702744942A796399 CRC64;
MSRKGPRAEV CADCSAPDPG WASISRGVLV CDECCSVHRS LGRHISIVKH LRHSAWPPTL
LQMVHTLASN GANSIWEHSL LDPAQVQSGR RKANPQDKVH PIKSEFIRAK YQMLAFVHKL
PCRDDDGVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGTTP LHVAAKAGQT
LQAELLVVYG ADPGSPDVNG RTPIDYARQA GHHELAERLV ECQYELTDRL AFYLCGRKPD
HKNGHYIIPQ MADSLDLSEL AKAAKKKLQA LSNRLFEELA MDVYDEVDRR ENDAVWLATQ
NHSTLVTERS AVPFLPVNPE YSATRNQGRQ KLARFNAREF ATLIIDILSE AKRRQQGKSL
SSPTDNLELS LRSQSDLDDQ HDYDSVASDE DTDQEPLRST GATRSNRARS MDSSDLSDGA
VTLQEYLELK KALATSEAKV QQLMKVNSSL SDELRRLQRE IHKLQAENLQ LRQPPGPVPT
PPLPSERAEH TPMAPGGSTH RRDRQAFSMY EPGSALKPFG GPPGDELTTR LQPFHSTELE
DDAIYSVHVP AGLYRIRKGV SASAVPFTPS SPLLSCSQEG SRHTSKLSRH GSGADSDYEN
TQSGDPLLGL EGKRFLELGK EEDFHPELES LDGDLDPGLP STEDVILKTE QVTKNIQELL
RAAQEFKHDS FVPCSEKIHL AVTEMASLFP KRPALEPVRS SLRLLNASAY RLQSECRKTV
PPEPGAPVDF QLLTQQVIQC AYDIAKAAKQ LVTITTREKK Q
