GIT2_HUMAN
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 03-AUG-2022, entry version 210.
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; 131.
DR CORUM; Q14161; -.
DR IntAct; Q14161; 65.
DR MINT; Q14161; -.
DR STRING; 9606.ENSP00000347464; -.
DR GlyGen; Q14161; 7 sites, 2 O-linked glycans (7 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; Q14161; -.
DR PeptideAtlas; Q14161; -.
DR PRIDE; 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 ABCD; Q14161; 1 sequenced antibody.
DR Antibodypedia; 30932; 320 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 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; ELWMAMQ; -.
DR OrthoDB; 349344at2759; -.
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; 16 hits in 1085 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 179 other tissues.
DR ExpressionAtlas; Q14161; baseline and differential.
DR Genevisible; Q14161; HS.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
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 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; 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
