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 24-JAN-2024, entry version 223. 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; 140. DR CORUM; Q9Y2X7; -. DR IntAct; Q9Y2X7; 67. DR MINT; Q9Y2X7; -. DR STRING; 9606.ENSP00000378338; -. DR GlyCosmos; Q9Y2X7; 1 site, 1 glycan. DR GlyGen; Q9Y2X7; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000378338; -. DR PeptideAtlas; Q9Y2X7; -. DR ProteomicsDB; 85928; -. [Q9Y2X7-1] DR ProteomicsDB; 85929; -. [Q9Y2X7-2] DR ProteomicsDB; 85930; -. [Q9Y2X7-3] DR Pumba; Q9Y2X7; -. DR ABCD; Q9Y2X7; 1 sequenced antibody. DR Antibodypedia; 1365; 581 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 AGR; HGNC:4272; -. 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; IDHKNGH; -. DR OrthoDB; 2877020at2759; -. 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 1155 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 205 other cell types or tissues. DR ExpressionAtlas; Q9Y2X7; baseline and differential. 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 CDD; cd08846; ArfGap_GIT1; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1. DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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; IPR047161; GIT-like. DR InterPro; IPR032352; GIT1/2_CC. DR InterPro; IPR022018; GIT1_C. DR InterPro; IPR013724; GIT_SHD. DR PANTHER; PTHR46097:SF1; ARF GTPASE-ACTIVATING PROTEIN GIT1; 1. DR PANTHER; PTHR46097; G PROTEIN-COUPLED RECEPTOR KINASE INTERACTING ARFGAP; 1. 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; Ankyrin repeat; 1. DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS50115; ARFGAP; 1. DR Genevisible; Q9Y2X7; HS. 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 //