ID   GIT2_HUMAN              Reviewed;         759 AA.
AC   Q14161; Q86U59; Q96CI2; Q9BV91; Q9Y5V2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   27-MAR-2024, entry version 219.
DE   RecName: Full=ARF GTPase-activating protein GIT2;
DE            Short=ARF GAP GIT2;
DE   AltName: Full=Cool-interacting tyrosine-phosphorylated protein 2;
DE            Short=CAT-2;
DE            Short=CAT2;
DE   AltName: Full=G protein-coupled receptor kinase-interactor 2;
DE   AltName: Full=GRK-interacting protein 2;
GN   Name=GIT2; Synonyms=KIAA0148;
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] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9),
RP   FUNCTION, AND INTERACTION WITH ARHGEF7 AND PAK3.
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 10).
RC   TISSUE=Bone marrow;
RX   PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA   Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. IV. The
RT   coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:167-174(1995).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 29-759 (ISOFORM 11).
RC   TISSUE=B-cell, and Skin;
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   [6]
RP   INTERACTION WITH PAXILLIN.
RX   PubMed=11251077; DOI=10.1091/mbc.12.3.645;
RA   Mazaki Y., Hashimoto S., Okawa K., Tsubouchi A., Nakamura K., Yagi R.,
RA   Yano H., Kondo A., Iwamatsu A., Mizoguchi A., Sabe H.;
RT   "An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148
RT   is involved in subcellular localization of paxillin and actin cytoskeletal
RT   organization.";
RL   Mol. Biol. Cell 12:645-662(2001).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=15144186; DOI=10.1021/ac035352d;
RA   Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA   Peters E.C.;
RT   "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT   human T cells using immobilized metal affinity chromatography and tandem
RT   mass spectrometry.";
RL   Anal. Chem. 76:2763-2772(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-418 AND SER-421, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-397, AND
RP   IDENTIFICATION BY MASS 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-397; SER-559 AND
RP   SER-614, 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION BY
RP   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   [14]
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   [15]
RP   IDENTIFICATION IN A COMPLEX WITH BIN2 AND ARHGEF6.
RX   PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA   Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA   Veprintsev D.B., Evans P.R., McMahon H.T.;
RT   "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT   podosomes, motility and phagocytosis.";
RL   PLoS ONE 7:E52401-E52401(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION BY
RP   MASS 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP   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).
CC   -!- FUNCTION: GTPase-activating protein for ADP ribosylation factor family
CC       members, including ARF1. {ECO:0000269|PubMed:10896954}.
CC   -!- SUBUNIT: May form heterooligomers with GIT1 (By similarity). Directly
CC       interacts with protein Piccolo/PCLO (By similarity). Interacts with
CC       PPFIA1 and PPFIA2 (By similarity). Interacts with ARHGEF7
CC       (PubMed:10896954). Identified in a complex with ARHGEF6 and BIN2
CC       (PubMed:23285027). Interacts with PAK3 (PubMed:10896954). Interacts
CC       with PXN/paxillin (PubMed:11251077). Interacts with TGFB1I1 (By
CC       similarity). Forms a complex with EFNB1 and GRB4/NCK2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q66H91, ECO:0000250|UniProtKB:Q9JLQ2,
CC       ECO:0000269|PubMed:10896954, ECO:0000269|PubMed:11251077,
CC       ECO:0000269|PubMed:23285027}.
CC   -!- INTERACTION:
CC       Q14161; Q9Y6K9: IKBKG; NbExp=6; IntAct=EBI-1046878, EBI-81279;
CC       Q14161; Q13153: PAK1; NbExp=3; IntAct=EBI-1046878, EBI-1307;
CC       Q14161; P49023: PXN; NbExp=4; IntAct=EBI-1046878, EBI-702209;
CC       Q14161; Q15025: TNIP1; NbExp=3; IntAct=EBI-1046878, EBI-357849;
CC       Q14161; Q13077: TRAF1; NbExp=2; IntAct=EBI-1046878, EBI-359224;
CC       Q14161; Q15631: TSN; NbExp=2; IntAct=EBI-1046878, EBI-1044160;
CC       Q14161; Q9ES28: Arhgef7; Xeno; NbExp=2; IntAct=EBI-1046878, EBI-642580;
CC       Q14161-11; Q15052: ARHGEF6; NbExp=9; IntAct=EBI-12028686, EBI-1642523;
CC       Q14161-11; Q7L5D6: GET4; NbExp=3; IntAct=EBI-12028686, EBI-711823;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=11;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q14161-1; Sequence=Displayed;
CC       Name=2; Synonyms=GIT2-short;
CC         IsoId=Q14161-2; Sequence=VSP_000303, VSP_000304;
CC       Name=3; Synonyms=C-;
CC         IsoId=Q14161-3; Sequence=VSP_000307;
CC       Name=4; Synonyms=BC-;
CC         IsoId=Q14161-4; Sequence=VSP_000306, VSP_000307;
CC       Name=5; Synonyms=E-;
CC         IsoId=Q14161-5; Sequence=VSP_000309;
CC       Name=6; Synonyms=CD-;
CC         IsoId=Q14161-6; Sequence=VSP_000307, VSP_000308;
CC       Name=7; Synonyms=DE-;
CC         IsoId=Q14161-7; Sequence=VSP_000308, VSP_000309;
CC       Name=8; Synonyms=BE-;
CC         IsoId=Q14161-8; Sequence=VSP_000306, VSP_000309;
CC       Name=9; Synonyms=AE-;
CC         IsoId=Q14161-9; Sequence=VSP_000305, VSP_000309;
CC       Name=10;
CC         IsoId=Q14161-10; Sequence=VSP_026456, VSP_008654, VSP_000309;
CC       Name=11;
CC         IsoId=Q14161-11; Sequence=VSP_000307, VSP_000308, VSP_000309;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA09769.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF124491; AAD28047.1; -; mRNA.
DR   EMBL; D63482; BAA09769.2; ALT_INIT; mRNA.
DR   EMBL; BT007312; AAP35976.1; -; mRNA.
DR   EMBL; BC001379; AAH01379.1; -; mRNA.
DR   EMBL; BC014223; AAH14223.2; -; mRNA.
DR   CCDS; CCDS44968.1; -. [Q14161-5]
DR   CCDS; CCDS44969.1; -. [Q14161-11]
DR   CCDS; CCDS55884.1; -. [Q14161-10]
DR   CCDS; CCDS9138.1; -. [Q14161-1]
DR   CCDS; CCDS9139.1; -. [Q14161-2]
DR   RefSeq; NP_001128685.1; NM_001135213.2. [Q14161-10]
DR   RefSeq; NP_001128686.1; NM_001135214.2. [Q14161-5]
DR   RefSeq; NP_001317082.1; NM_001330153.1.
DR   RefSeq; NP_055591.2; NM_014776.4.
DR   RefSeq; NP_476510.1; NM_057169.4. [Q14161-1]
DR   RefSeq; NP_476511.1; NM_057170.4. [Q14161-11]
DR   RefSeq; XP_006719770.1; XM_006719707.3. [Q14161-3]
DR   RefSeq; XP_006719772.1; XM_006719709.3. [Q14161-4]
DR   AlphaFoldDB; Q14161; -.
DR   SMR; Q14161; -.
DR   BioGRID; 115154; 138.
DR   CORUM; Q14161; -.
DR   IntAct; Q14161; 66.
DR   MINT; Q14161; -.
DR   STRING; 9606.ENSP00000347464; -.
DR   GlyCosmos; Q14161; 7 sites, 2 glycans.
DR   GlyGen; Q14161; 8 sites, 2 O-linked glycans (8 sites).
DR   iPTMnet; Q14161; -.
DR   PhosphoSitePlus; Q14161; -.
DR   BioMuta; GIT2; -.
DR   DMDM; 17376322; -.
DR   EPD; Q14161; -.
DR   jPOST; Q14161; -.
DR   MassIVE; Q14161; -.
DR   MaxQB; Q14161; -.
DR   PaxDb; 9606-ENSP00000347464; -.
DR   PeptideAtlas; Q14161; -.
DR   ProteomicsDB; 59876; -. [Q14161-1]
DR   ProteomicsDB; 59877; -. [Q14161-10]
DR   ProteomicsDB; 59878; -. [Q14161-11]
DR   ProteomicsDB; 59879; -. [Q14161-2]
DR   ProteomicsDB; 59880; -. [Q14161-3]
DR   ProteomicsDB; 59881; -. [Q14161-4]
DR   ProteomicsDB; 59882; -. [Q14161-5]
DR   ProteomicsDB; 59883; -. [Q14161-6]
DR   ProteomicsDB; 59884; -. [Q14161-7]
DR   ProteomicsDB; 59885; -. [Q14161-8]
DR   ProteomicsDB; 59886; -. [Q14161-9]
DR   Pumba; Q14161; -.
DR   ABCD; Q14161; 1 sequenced antibody.
DR   Antibodypedia; 30932; 365 antibodies from 35 providers.
DR   CPTC; Q14161; 1 antibody.
DR   DNASU; 9815; -.
DR   Ensembl; ENST00000355312.8; ENSP00000347464.3; ENSG00000139436.22. [Q14161-1]
DR   Ensembl; ENST00000361006.9; ENSP00000354282.5; ENSG00000139436.22. [Q14161-5]
DR   Ensembl; ENST00000457474.6; ENSP00000391813.2; ENSG00000139436.22. [Q14161-10]
DR   Ensembl; ENST00000547815.5; ENSP00000450348.1; ENSG00000139436.22. [Q14161-2]
DR   Ensembl; ENST00000553118.5; ENSP00000447465.1; ENSG00000139436.22. [Q14161-11]
DR   GeneID; 9815; -.
DR   KEGG; hsa:9815; -.
DR   MANE-Select; ENST00000355312.8; ENSP00000347464.3; NM_057169.5; NP_476510.1.
DR   UCSC; uc001tpq.3; human. [Q14161-1]
DR   AGR; HGNC:4273; -.
DR   CTD; 9815; -.
DR   DisGeNET; 9815; -.
DR   GeneCards; GIT2; -.
DR   HGNC; HGNC:4273; GIT2.
DR   HPA; ENSG00000139436; Low tissue specificity.
DR   MIM; 608564; gene.
DR   neXtProt; NX_Q14161; -.
DR   OpenTargets; ENSG00000139436; -.
DR   PharmGKB; PA28684; -.
DR   VEuPathDB; HostDB:ENSG00000139436; -.
DR   eggNOG; KOG0818; Eukaryota.
DR   GeneTree; ENSGT00940000156383; -.
DR   HOGENOM; CLU_009739_0_0_1; -.
DR   InParanoid; Q14161; -.
DR   OMA; DPNYYHE; -.
DR   OrthoDB; 2877020at2759; -.
DR   PhylomeDB; Q14161; -.
DR   TreeFam; TF317762; -.
DR   PathwayCommons; Q14161; -.
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   SignaLink; Q14161; -.
DR   SIGNOR; Q14161; -.
DR   BioGRID-ORCS; 9815; 17 hits in 1163 CRISPR screens.
DR   ChiTaRS; GIT2; human.
DR   GeneWiki; GIT2; -.
DR   GenomeRNAi; 9815; -.
DR   Pharos; Q14161; Tbio.
DR   PRO; PR:Q14161; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q14161; Protein.
DR   Bgee; ENSG00000139436; Expressed in monocyte and 181 other cell types or tissues.
DR   ExpressionAtlas; Q14161; baseline and differential.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
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:0031267; F:small GTPase binding; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; IBA:GO_Central.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IBA:GO_Central.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0036465; P:synaptic vesicle recycling; IBA:GO_Central.
DR   CDD; cd08847; ArfGap_GIT2; 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:SF4; ARF GTPASE-ACTIVATING PROTEIN GIT2; 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; Q14161; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Coiled coil; GTPase activation;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..759
FT                   /note="ARF GTPase-activating protein GIT2"
FT                   /id="PRO_0000074203"
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          379..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..478
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        408..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         397
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         401
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLQ2"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         484
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   MOD_RES         559
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLQ2"
FT   MOD_RES         570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLQ2"
FT   MOD_RES         587
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLQ2"
FT   MOD_RES         614
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:19690332"
FT   VAR_SEQ         255
FT                   /note="S -> RRL (in isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:8590280"
FT                   /id="VSP_026456"
FT   VAR_SEQ         334..414
FT                   /note="Missing (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:10896954"
FT                   /id="VSP_000305"
FT   VAR_SEQ         414..463
FT                   /note="Missing (in isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:8590280"
FT                   /id="VSP_008654"
FT   VAR_SEQ         415..449
FT                   /note="Missing (in isoform 4 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:10896954"
FT                   /id="VSP_000306"
FT   VAR_SEQ         450..464
FT                   /note="Missing (in isoform 3, isoform 4, isoform 6 and
FT                   isoform 11)"
FT                   /evidence="ECO:0000303|PubMed:10896954,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_000307"
FT   VAR_SEQ         465..547
FT                   /note="Missing (in isoform 6, isoform 7 and isoform 11)"
FT                   /evidence="ECO:0000303|PubMed:10896954,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_000308"
FT   VAR_SEQ         466..471
FT                   /note="QTLQSE -> LGKDAN (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10896954,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT                   /id="VSP_000303"
FT   VAR_SEQ         472..759
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10896954,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT                   /id="VSP_000304"
FT   VAR_SEQ         548..577
FT                   /note="Missing (in isoform 5, isoform 7, isoform 8, isoform
FT                   9, isoform 10 and isoform 11)"
FT                   /evidence="ECO:0000303|PubMed:10896954,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8590280"
FT                   /id="VSP_000309"
FT   VARIANT         338
FT                   /note="N -> S (in dbSNP:rs9804905)"
FT                   /id="VAR_048324"
FT   VARIANT         387
FT                   /note="N -> S (in dbSNP:rs925368)"
FT                   /id="VAR_024368"
FT   VARIANT         552
FT                   /note="A -> V (in dbSNP:rs11068997)"
FT                   /id="VAR_048325"
FT   CONFLICT        285
FT                   /note="V -> M (in Ref. 4; AAP35976 and 5; AAH01379)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   759 AA;  84543 MW;  07EFE266DB2F3258 CRC64;
     MSKRLRSSEV CADCSGPDPS WASVNRGTFL CDECCSVHRS LGRHISQVRH LKHTPWPPTL
     LQMVETLYNN GANSIWEHSL LDPASIMSGR RKANPQDKVH PNKAEFIRAK YQMLAFVHRL
     PCRDDDSVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGNTP LHVASKAGQI
     LQAELLAVYG ADPGTQDSSG KTPVDYARQG GHHELAERLV EIQYELTDRL AFYLCGRKPD
     HKNGQHFIIP QMADSSLDLS ELAKAAKKKL QSLSNHLFEE LAMDVYDEVD RRETDAVWLA
     TQNHSALVTE TTVVPFLPVN PEYSSTRNQG RQKLARFNAH EFATLVIDIL SDAKRRQQGS
     SLSGSKDNVE LILKTINNQH SVESQDNDQP DYDSVASDED TDLETTASKT NRQKSLDSDL
     SDGPVTVQEF MEVKNALVAS EAKIQQLMKV NNNLSDELRI MQKKLQTLQS ENSNLRKQAT
     TNVYQVQTGS EYTDTSNHSS LKRRPSARGS RPMSMYETGS GQKPYLPMGE ASRPEESRMR
     LQPFPAHIGR SALVTSSSSL PSFPSTLSWS RDESARRASR LEKQNSTPES DYDNTPNDME
     PDGMGSSRKG RQRSMVWPGD GLVPDTAEPH VAPSPTLPST EDVIRKTEQI TKNIQELLRA
     AQENKHDSYI PCSERIHVAV TEMAALFPKK PKSDMVRTSL RLLTSSAYRL QSECKKTLPG
     DPGSPTDVQL VTQQVIQCAY DIAKAAKQLV TITTKENNN
//