GAB2_HUMAN
ID GAB2_HUMAN Reviewed; 676 AA.
AC Q9UQC2; A2RRM2; A6NEW9; A7MD36; O60317;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=GRB2-associated-binding protein 2;
DE AltName: Full=GRB2-associated binder 2;
DE AltName: Full=Growth factor receptor bound protein 2-associated protein 2;
DE AltName: Full=pp100;
GN Name=GAB2; Synonyms=KIAA0571;
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 PTPN11.
RC TISSUE=Myeloma;
RX PubMed=10068651;
RA Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T.,
RA Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.;
RT "Gab-family adapter proteins act downstream of cytokine and growth factor
RT receptors and T- and B-cell antigen receptors.";
RL Blood 93:1809-1816(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP SEQUENCE REVISION.
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP PHOSPHORYLATION BY HCK, AND INTERACTION WITH HCK; CRKL PTPN11 AND GRB2.
RX PubMed=15010462; DOI=10.1074/jbc.m305783200;
RA Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P.,
RA Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C.;
RT "Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation
RT of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation
RT and survival of multiple myeloma cells.";
RL J. Biol. Chem. 279:21658-21665(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH TNFRSF11A.
RX PubMed=15750601; DOI=10.1038/nm1203;
RA Wada T., Nakashima T., Oliveira-dos-Santos A.J., Gasser J., Hara H.,
RA Schett G., Penninger J.M.;
RT "The molecular scaffold Gab2 is a crucial component of RANK signaling and
RT osteoclastogenesis.";
RL Nat. Med. 11:394-399(2005).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGFR; GRB2; PTPN11; PI-3
RP KINASE; SFN; SHC1; YWHAB; YWHAE; YWHAG; YWHAH; YWHAQ AND YWHAZ, MUTAGENESIS
RP OF SER-210 AND THR-391, AND PHOSPHORYLATION AT SER-133; SER-140; SER-141;
RP SER-148; SER-149; SER-159; SER-164; SER-210; SER-218; SER-223; SER-264;
RP THR-278; SER-281; THR-287; TYR-293; THR-331; THR-385; THR-391; SER-405;
RP SER-480; SER-543; SER-622 AND SER-623.
RX PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M.,
RA James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the
RT Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, AND IDENTIFICATION BY
RP 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 [11]
RP 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-148; SER-149; SER-223;
RP SER-264; SER-285; THR-287; SER-368; THR-391; SER-422; SER-425; SER-543 AND
RP TYR-643, AND IDENTIFICATION BY 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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 350-358 IN COMPLEX WITH GRB2, AND
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 508-522 IN COMPLEX WITH GRB2.
RX PubMed=19523899; DOI=10.1016/j.str.2009.03.017;
RA Harkiolaki M., Tsirka T., Lewitzky M., Simister P.C., Joshi D., Bird L.E.,
RA Jones E.Y., O'Reilly N., Feller S.M.;
RT "Distinct binding modes of two epitopes in Gab2 that interact with the SH3C
RT domain of Grb2.";
RL Structure 17:809-822(2009).
CC -!- FUNCTION: Adapter protein which acts downstream of several membrane
CC receptors including cytokine, antigen, hormone, cell matrix and growth
CC factor receptors to regulate multiple signaling pathways. Regulates
CC osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In
CC allergic response, it plays a role in mast cells activation and
CC degranulation through PI-3-kinase regulation. Also involved in the
CC regulation of cell proliferation and hematopoiesis.
CC {ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:19172738}.
CC -!- SUBUNIT: Interacts with SHC1; may mediate interaction with receptors
CC (By similarity). Interacts with SYK (By similarity). Interacts with PI-
CC 3 kinase. Interacts with GRB2 (via SH3 2 domain). Interacts
CC (phosphorylated) with PTPN11. Interacts with TNFRSF11A (via cytoplasmic
CC domain). Interacts (phosphorylated) with 14-3-3 family proteins SFN,
CC YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ; prevents interaction with
CC GRB2 and attenuates GAB2 signaling. Interacts with HCK. {ECO:0000250,
CC ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:15010462,
CC ECO:0000269|PubMed:15750601, ECO:0000269|PubMed:19172738,
CC ECO:0000269|PubMed:19523899}.
CC -!- INTERACTION:
CC Q9UQC2; P11117: ACP2; NbExp=3; IntAct=EBI-975200, EBI-2907070;
CC Q9UQC2; P00533: EGFR; NbExp=3; IntAct=EBI-975200, EBI-297353;
CC Q9UQC2; O75791: GRAP2; NbExp=3; IntAct=EBI-975200, EBI-740418;
CC Q9UQC2; P62993: GRB2; NbExp=14; IntAct=EBI-975200, EBI-401755;
CC Q9UQC2; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-975200, EBI-14103818;
CC Q9UQC2; P42858: HTT; NbExp=3; IntAct=EBI-975200, EBI-466029;
CC Q9UQC2; Q06124: PTPN11; NbExp=4; IntAct=EBI-975200, EBI-297779;
CC Q9UQC2; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-975200, EBI-25839575;
CC Q9UQC2; P08865: RPSA; NbExp=3; IntAct=EBI-975200, EBI-354112;
CC Q9UQC2; P31946: YWHAB; NbExp=4; IntAct=EBI-975200, EBI-359815;
CC Q9UQC2-1; P62993-1: GRB2; NbExp=3; IntAct=EBI-15787947, EBI-15787932;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19172738}. Cell
CC membrane {ECO:0000269|PubMed:19172738}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UQC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UQC2-2; Sequence=VSP_038520;
CC -!- DOMAIN: The SH3-binding motifs mediate interaction with SHC1 and GRB2.
CC {ECO:0000250}.
CC -!- DOMAIN: The PH domain mediates phosphatidylinositol 3,4,5-trisphosphate
CC and phosphatidylinositol 3,4-bisphosphate binding. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residue(s) by the thrombopoietin
CC receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and B-
CC cell antigen receptors, gp130, IL-2R and IL-3R (By similarity).
CC Phosphorylated upon stimulation of TNFRSF11A/RANK by TNFSF11/RANKL (By
CC similarity). Phosphorylated upon EGF stimulation. Phosphorylated on
CC tyrosine residues by HCK upon IL6 signaling. {ECO:0000250,
CC ECO:0000269|PubMed:15010462, ECO:0000269|PubMed:19172738}.
CC -!- PTM: Dephosphorylated by PTPN11.
CC -!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25497.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GAB2ID40664ch11q14.html";
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DR EMBL; AB018413; BAA76737.1; -; mRNA.
DR EMBL; AB011143; BAA25497.2; ALT_INIT; mRNA.
DR EMBL; AP002985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW75057.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW75058.1; -; Genomic_DNA.
DR EMBL; BC131711; AAI31712.1; -; mRNA.
DR EMBL; BC152459; AAI52460.1; -; mRNA.
DR CCDS; CCDS8259.1; -. [Q9UQC2-1]
DR CCDS; CCDS8260.1; -. [Q9UQC2-2]
DR RefSeq; NP_036428.1; NM_012296.3. [Q9UQC2-2]
DR RefSeq; NP_536739.1; NM_080491.2. [Q9UQC2-1]
DR RefSeq; XP_006718816.1; XM_006718753.2. [Q9UQC2-2]
DR PDB; 2VWF; X-ray; 1.58 A; B=508-522.
DR PDB; 2W0Z; X-ray; 1.70 A; B=350-358.
DR PDB; 5EWZ; X-ray; 2.34 A; C=387-395, D=207-212.
DR PDB; 5EXA; X-ray; 1.95 A; C/D=387-396.
DR PDB; 6Y3R; X-ray; 1.50 A; P=387-398.
DR PDB; 6Y3S; X-ray; 1.95 A; P=205-214.
DR PDB; 6ZVB; X-ray; 2.51 A; P=386-398.
DR PDB; 6ZVC; X-ray; 2.51 A; P=386-398.
DR PDB; 6ZVD; X-ray; 2.50 A; P=386-398.
DR PDB; 6ZVE; X-ray; 2.51 A; P=386-398.
DR PDBsum; 2VWF; -.
DR PDBsum; 2W0Z; -.
DR PDBsum; 5EWZ; -.
DR PDBsum; 5EXA; -.
DR PDBsum; 6Y3R; -.
DR PDBsum; 6Y3S; -.
DR PDBsum; 6ZVB; -.
DR PDBsum; 6ZVC; -.
DR PDBsum; 6ZVD; -.
DR PDBsum; 6ZVE; -.
DR AlphaFoldDB; Q9UQC2; -.
DR SMR; Q9UQC2; -.
DR BioGRID; 115181; 119.
DR DIP; DIP-36653N; -.
DR IntAct; Q9UQC2; 63.
DR MINT; Q9UQC2; -.
DR STRING; 9606.ENSP00000354952; -.
DR iPTMnet; Q9UQC2; -.
DR PhosphoSitePlus; Q9UQC2; -.
DR BioMuta; GAB2; -.
DR DMDM; 46396035; -.
DR EPD; Q9UQC2; -.
DR jPOST; Q9UQC2; -.
DR MassIVE; Q9UQC2; -.
DR MaxQB; Q9UQC2; -.
DR PaxDb; Q9UQC2; -.
DR PeptideAtlas; Q9UQC2; -.
DR PRIDE; Q9UQC2; -.
DR ProteomicsDB; 85541; -. [Q9UQC2-1]
DR ProteomicsDB; 85542; -. [Q9UQC2-2]
DR Antibodypedia; 600; 766 antibodies from 39 providers.
DR DNASU; 9846; -.
DR Ensembl; ENST00000340149.6; ENSP00000343959.2; ENSG00000033327.13. [Q9UQC2-2]
DR Ensembl; ENST00000361507.5; ENSP00000354952.4; ENSG00000033327.13. [Q9UQC2-1]
DR GeneID; 9846; -.
DR KEGG; hsa:9846; -.
DR MANE-Select; ENST00000361507.5; ENSP00000354952.4; NM_080491.3; NP_536739.1.
DR UCSC; uc001ozg.4; human. [Q9UQC2-1]
DR CTD; 9846; -.
DR DisGeNET; 9846; -.
DR GeneCards; GAB2; -.
DR HGNC; HGNC:14458; GAB2.
DR HPA; ENSG00000033327; Tissue enhanced (brain).
DR MIM; 606203; gene.
DR neXtProt; NX_Q9UQC2; -.
DR OpenTargets; ENSG00000033327; -.
DR PharmGKB; PA28478; -.
DR VEuPathDB; HostDB:ENSG00000033327; -.
DR eggNOG; ENOG502QTS1; Eukaryota.
DR GeneTree; ENSGT00940000157792; -.
DR HOGENOM; CLU_028652_0_0_1; -.
DR InParanoid; Q9UQC2; -.
DR OMA; FEPPMSN; -.
DR OrthoDB; 1153633at2759; -.
DR PhylomeDB; Q9UQC2; -.
DR TreeFam; TF329487; -.
DR PathwayCommons; Q9UQC2; -.
DR Reactome; R-HSA-109704; PI3K Cascade.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8853659; RET signaling.
DR Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR Reactome; R-HSA-9607240; FLT3 Signaling.
DR Reactome; R-HSA-9645135; STAT5 Activation.
DR Reactome; R-HSA-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-HSA-9702518; STAT5 activation downstream of FLT3 ITD mutants.
DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR Reactome; R-HSA-9703648; Signaling by FLT3 ITD and TKD mutants.
DR SignaLink; Q9UQC2; -.
DR SIGNOR; Q9UQC2; -.
DR BioGRID-ORCS; 9846; 64 hits in 1086 CRISPR screens.
DR ChiTaRS; GAB2; human.
DR EvolutionaryTrace; Q9UQC2; -.
DR GeneWiki; GAB2; -.
DR GenomeRNAi; 9846; -.
DR Pharos; Q9UQC2; Tbio.
DR PRO; PR:Q9UQC2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UQC2; protein.
DR Bgee; ENSG00000033327; Expressed in inferior vagus X ganglion and 187 other tissues.
DR ExpressionAtlas; Q9UQC2; baseline and differential.
DR Genevisible; Q9UQC2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IDA:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR DisProt; DP01507; -.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID00522; -.
DR InterPro; IPR046355; Gab1-4-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR45960; PTHR45960; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..676
FT /note="GRB2-associated-binding protein 2"
FT /id="PRO_0000050285"
FT DOMAIN 6..117
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 127..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 351..358
FT /note="SH3-binding"
FT MOTIF 510..519
FT /note="SH3-binding"
FT COMPBIAS 348..362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1S8"
FT MOD_RES 266
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1S8"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19172738,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 293
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19172738,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1S8"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1S8"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19172738"
FT MOD_RES 643
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9628581"
FT /id="VSP_038520"
FT VARIANT 320
FT /note="P -> L (in dbSNP:rs752597583)"
FT /id="VAR_053097"
FT VARIANT 344
FT /note="P -> L (in dbSNP:rs2279374)"
FT /id="VAR_020407"
FT MUTAGEN 210
FT /note="S->A,E: Impaired interaction with 14-3-3 proteins
FT and increased EGF-independent cell proliferation; when
FT associated with A-391."
FT /evidence="ECO:0000269|PubMed:19172738"
FT MUTAGEN 391
FT /note="T->A,E: Impaired interaction with 14-3-3 proteins
FT and increased EGF-independent cell proliferation; when
FT associated with A-210."
FT /evidence="ECO:0000269|PubMed:19172738"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:2VWF"
SQ SEQUENCE 676 AA; 74458 MW; 107623FD07D884C9 CRC64;
MSGGGDVVCT GWLRKSPPEK KLRRYAWKKR WFILRSGRMS GDPDVLEYYK NDHSKKPLRI
INLNFCEQVD AGLTFNKKEL QDSFVFDIKT SERTFYLVAE TEEDMNKWVQ SICQICGFNQ
AEESTDSLRN VSSAGHGPRS SPAELSSSSQ HLLRERKSSA PSHSSQPTLF TFEPPVSNHM
QPTLSTSAPQ EYLYLHQCIS RRAENARSAS FSQGTRASFL MRSDTAVQKL AQGNGHCVNG
ISGQVHGFYS LPKPSRHNTE FRDSTYDLPR SLASHGHTKG SLTGSETDNE DVYTFKTPSN
TLCREFGDLL VDNMDVPATP LSAYQIPRTF TLDKNHNAMT VATPGDSAIA PPPRPPKPSQ
AETPRWGSPQ QRPPISENSR SVAATIPRRN TLPAMDNSRL HRASSCETYE YPQRGGESAG
RSAESMSDGV GSFLPGKMIV GRSDSTNSED NYVPMNPGSS TLLAMERAGD NSQSVYIPMS
PGAHHFDSLG YPSTTLPVHR GPSRGSEIQP PPVNRNLKPD RKAKPTPLDL RNNTVIDELP
FKSPITKSWS RANHTFNSSS SQYCRPISTQ SITSTDSGDS EENYVPMQNP VSASPVPSGT
NSPAPKKSTG SVDYLALDFQ PSSPSPHRKP STSSVTSDEK VDYVQVDKEK TQALQNTMQE
WTDVRQSSEP SKGAKL
