BCR_MOUSE
ID BCR_MOUSE Reviewed; 1270 AA.
AC Q6PAJ1; E9PZL3; Q61339; Q6ZPE5; Q99LW5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Breakpoint cluster region protein {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P11274};
GN Name=Bcr {ECO:0000312|EMBL:AC160402}; Synonyms=Kiaa3017;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-1270.
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-428.
RX PubMed=2263470; DOI=10.1093/nar/18.23.7119;
RA Zhu Q.S., Heisterkamp N., Groffen J.;
RT "Unique organization of the human BCR gene promoter.";
RL Nucleic Acids Res. 18:7119-7125(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-1270.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP POSSIBLE INTERACTION WITH CCPG1.
RX PubMed=17000758; DOI=10.1128/mcb.00670-06;
RA Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT "Ccpg1, a novel scaffold protein that regulates the activity of the Rho
RT guanine nucleotide exchange factor Dbs.";
RL Mol. Cell. Biol. 26:8964-8975(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND TYR-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP FUNCTION.
RX PubMed=17116687; DOI=10.1128/mcb.00756-06;
RA Cho Y.J., Cunnick J.M., Yi S.J., Kaartinen V., Groffen J., Heisterkamp N.;
RT "Abr and Bcr, two homologous Rac GTPase-activating proteins, control
RT multiple cellular functions of murine macrophages.";
RL Mol. Cell. Biol. 27:899-911(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; THR-387; SER-461;
RP SER-465 AND SER-1263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20962234; DOI=10.1523/jneurosci.1711-10.2010;
RA Oh D., Han S., Seo J., Lee J.R., Choi J., Groffen J., Kim K., Cho Y.S.,
RA Choi H.S., Shin H., Woo J., Won H., Park S.K., Kim S.Y., Jo J.,
RA Whitcomb D.J., Cho K., Kim H., Bae Y.C., Heisterkamp N., Choi S.Y., Kim E.;
RT "Regulation of synaptic Rac1 activity, long-term potentiation maintenance,
RT and learning and memory by BCR and ABR Rac GTPase-activating proteins.";
RL J. Neurosci. 30:14134-14144(2010).
RN [12]
RP TISSUE SPECIFICITY, INTERACTION WITH SH2D5, AND SUBCELLULAR LOCATION.
RX PubMed=25331951; DOI=10.1074/jbc.m114.615112;
RA Gray E.J., Petsalaki E., James D.A., Bagshaw R.D., Stacey M.M., Rocks O.,
RA Gingras A.C., Pawson T.;
RT "src homology 2 domain containing protein 5 (sh2d5) binds the breakpoint
RT cluster region protein, BCR, and regulates levels of Rac1-GTP.";
RL J. Biol. Chem. 289:35397-35408(2014).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-473, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Protein with a unique structure having two opposing
CC regulatory activities toward small GTP-binding proteins. The C-terminus
CC is a GTPase-activating protein (GAP) domain which stimulates GTP
CC hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of
CC GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the
CC active GTP-bound form. The central Dbl homology (DH) domain functions
CC as guanine nucleotide exchange factor (GEF) that modulates the GTPases
CC CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1
CC from the GDP-bound to the GTP-bound form. The amino terminus contains
CC an intrinsic kinase activity (By similarity). Functions as an important
CC negative regulator of neuronal RAC1 activity (PubMed:20962234).
CC Regulates macrophage functions such as CSF1-directed motility and
CC phagocytosis through the modulation of RAC1 activity (PubMed:17116687).
CC Plays a major role as a RHOA GEF in keratinocytes being involved in
CC focal adhesion formation and keratinocyte differentiation (By
CC similarity). {ECO:0000250|UniProtKB:P11274,
CC ECO:0000269|PubMed:17116687, ECO:0000269|PubMed:20962234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P11274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P11274};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Homotetramer. Interacts with PDZK1. Interacts with HCK,
CC FES/FPS, ABL1, PIK3R1 and GRB2 (By similarity). May interact with CCPG1
CC (PubMed:17000758). Interacts with SH2D5 (PubMed:25331951). Interacts
CC with DLG4 (By similarity). {ECO:0000250|UniProtKB:P11274,
CC ECO:0000269|PubMed:17000758, ECO:0000269|PubMed:25331951}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000269|PubMed:25331951}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:20962234}. Cell projection, axon
CC {ECO:0000269|PubMed:20962234}. Synapse {ECO:0000250|UniProtKB:F1LXF1}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (PubMed:25331951). In
CC hippocampal subregions, most abundant in the CA1 region and expressed
CC at successively lower levels in the dentate gyrus and the CA3 region
CC (PubMed:20962234). {ECO:0000269|PubMed:20962234,
CC ECO:0000269|PubMed:25331951}.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC {ECO:0000269|PubMed:17000758}.
CC -!- DOMAIN: The region involved in binding to ABL1 SH2-domain is rich in
CC serine residues and needs to be Ser/Thr phosphorylated prior to SH2
CC binding. This region is essential for the activation of the ABL1
CC tyrosine kinase and transforming potential of the chimeric BCR-ABL
CC oncogene. {ECO:0000250|UniProtKB:P11274}.
CC -!- DOMAIN: The amino terminus contains an intrinsic kinase activity. The
CC central Dbl homology (DH) domain functions as guanine nucleotide
CC exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1.
CC Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to
CC the GTP-bound form. The C-terminus is a Rho-GAP domain which stimulates
CC GTP hydrolysis by RAC1, RAC2 and CDC42. The protein has a unique
CC structure having two opposing regulatory activities toward small GTP-
CC binding proteins. {ECO:0000250|UniProtKB:P11274}.
CC -!- PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine
CC residues, leading to down-regulation of the BCR kinase activity.
CC Phosphorylation at Tyr-178 by HCK is important for interaction with
CC GRB2. {ECO:0000250|UniProtKB:P11274}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show impaired spatial and object
CC recognition memory with reduced maintenance of long-term potentiation
CC (LTP) in Schaffer collateral-CA1 pyramidal neuron synapses.
CC {ECO:0000269|PubMed:20962234}.
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; AC160402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002193; AAH02193.1; -; mRNA.
DR EMBL; BC060270; AAH60270.1; -; mRNA.
DR EMBL; X52831; CAA37013.1; -; Genomic_DNA.
DR EMBL; AK129482; BAC98292.1; -; mRNA.
DR CCDS; CCDS35935.1; -.
DR PIR; S14194; S14193.
DR RefSeq; NP_001074881.1; NM_001081412.2.
DR AlphaFoldDB; Q6PAJ1; -.
DR SMR; Q6PAJ1; -.
DR BioGRID; 225455; 13.
DR IntAct; Q6PAJ1; 7.
DR MINT; Q6PAJ1; -.
DR STRING; 10090.ENSMUSP00000126377; -.
DR iPTMnet; Q6PAJ1; -.
DR PhosphoSitePlus; Q6PAJ1; -.
DR SwissPalm; Q6PAJ1; -.
DR EPD; Q6PAJ1; -.
DR jPOST; Q6PAJ1; -.
DR MaxQB; Q6PAJ1; -.
DR PaxDb; Q6PAJ1; -.
DR PeptideAtlas; Q6PAJ1; -.
DR PRIDE; Q6PAJ1; -.
DR ProteomicsDB; 273480; -.
DR Antibodypedia; 9277; 673 antibodies from 40 providers.
DR DNASU; 110279; -.
DR Ensembl; ENSMUST00000164107; ENSMUSP00000126377; ENSMUSG00000009681.
DR GeneID; 110279; -.
DR KEGG; mmu:110279; -.
DR UCSC; uc007fqb.2; mouse.
DR CTD; 613; -.
DR MGI; MGI:88141; Bcr.
DR VEuPathDB; HostDB:ENSMUSG00000009681; -.
DR eggNOG; KOG4269; Eukaryota.
DR GeneTree; ENSGT00940000153491; -.
DR HOGENOM; CLU_004164_0_0_1; -.
DR InParanoid; Q6PAJ1; -.
DR OMA; EKSYNRT; -.
DR OrthoDB; 762492at2759; -.
DR PhylomeDB; Q6PAJ1; -.
DR TreeFam; TF105082; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 110279; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Bcr; mouse.
DR PRO; PR:Q6PAJ1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6PAJ1; protein.
DR Bgee; ENSMUSG00000009681; Expressed in olfactory tubercle and 233 other tissues.
DR ExpressionAtlas; Q6PAJ1; baseline and differential.
DR Genevisible; Q6PAJ1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IGI:MGI.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IMP:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:1905517; P:macrophage migration; IGI:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0060313; P:negative regulation of blood vessel remodeling; IMP:CACAO.
DR GO; GO:0002692; P:negative regulation of cellular extravasation; IMP:CACAO.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:1905522; P:negative regulation of macrophage migration; IGI:MGI.
DR GO; GO:0043314; P:negative regulation of neutrophil degranulation; IGI:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:MGI.
DR GO; GO:0060268; P:negative regulation of respiratory burst; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR GO; GO:0043312; P:neutrophil degranulation; IGI:MGI.
DR GO; GO:0006909; P:phagocytosis; IGI:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IGI:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IMP:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0043114; P:regulation of vascular permeability; IMP:CACAO.
DR GO; GO:0003014; P:renal system process; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 4.10.280.30; -; 1.
DR InterPro; IPR037769; Abr/Bcr.
DR InterPro; IPR015123; Bcr-Abl_oncoprot_oligo.
DR InterPro; IPR036481; Bcr-Abl_oncoprot_oligo_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23182; PTHR23182; 1.
DR Pfam; PF09036; Bcr-Abl_Oligo; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF69036; SSF69036; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell projection; Coiled coil; GTPase activation;
KW Guanine-nucleotide releasing factor; Kinase; Methylation;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..1270
FT /note="Breakpoint cluster region protein"
FT /id="PRO_0000273731"
FT DOMAIN 497..690
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 707..865
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 892..1019
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1053..1247
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..428
FT /note="Kinase"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT REGION 67..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..387
FT /note="Binding to ABL SH2-domain"
FT /evidence="ECO:0000250"
FT REGION 201..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..55
FT /evidence="ECO:0000255"
FT COMPBIAS 90..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 178
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 247
FT /note="Phosphotyrosine; by FES"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 387
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 473
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 553
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 640
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 643
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11274"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 418
FT /note="S -> H (in Ref. 3; CAA37013)"
FT /evidence="ECO:0000305"
FT CONFLICT 1213
FT /note="P -> S (in Ref. 2; AAH60270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1270 AA; 143072 MW; 2F3E6D8485DE6717 CRC64;
MVDSVGFAEA WRAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN QERFRMIYLQ
TLLAKEKKSY DRQRWGFRRA AQPPDGAAEP RASAPRPPPA PADGADPAPV EESEARPDGE
GSPSKGRSAS ARRPAAAASA DRDDRGPPTS VAALRSNFEK IRKGPAQPGS ADAEKPFYVN
VEFHHERGLV KVNDKEVSDR ISSLGSQAMQ MERKKSQQSA GQGLGEAPRP HYRGRSSESS
CGLDGDYEDA ELNPRFLKDN LINANGGNRP PWPPLEYQPY QSIYVGGMMV EGEGKSPLLR
SQSTSEQEKR LTWPRRSYSP RSFEDSGGGY TPDCSSNENL TSSEEDFSSG QSSRVSPSPT
TYRMFRDKSR SPSQNSQQSF DSSSPPTPQC QKRHRQCQVV VSEATIVGVR KTGQIWPSDG
DSTFQGEADS SFGTPPGYGC AADQAEEQRR HQDGLPYIDD SPSSSPHLSS KGRGSLASGA
LDPTKVSELD LEKGLEMRKW VLSGILASEE TYLSHLEALL LPMKPLKAAA TTSQPVLTSQ
QIETIFFKVP ELYEIHKEFY DGLFPRVQQW SHQQRVGDLF QKLASQLGVY RAFVDNYGVA
METAEKCCQA NAQFAEISEN LRARSNKDVK DSTTKNSLET LLYKPVDRVT RSTLVLHDLL
KHTPSSHPDH SLLQDALRIS QNFLSSINEE ITPRRQSMTV KKGEHRQLLK DSFMVELVEG
ARKLRHIFLF TDLLLCTKLK KQSGGKTQQY DCKWYIPLTD LSFQMVDELE ALPNIPLVPD
EELDALKIKI SQIKSDIQRE KRANKGSKVM ERLRKKLSEQ ESLLLLMSPS MAFRVHSRNG
KSYTFLISSD YERAEWRESI REQQKKCFKS FSLTSVELQM LTNSCVKLQT VHHIPLTINK
EDDESPGLYG FLHVIVHSAT GFKQSSNLYC TLEVDSFGYF VNKAKTRVYR DTTEPNWNEE
FEIELEGSQT LRILCYEKCY NKMKMTKEDG ESADKLMGKG QVQLDPQTLQ DRDWQRTVID
MNGIEVKLSV KFTSREFSLK RMPSRKQTGV FGVKIAVVTK RERSKVPYIV RQCVEEIERR
GMEEVGIYRV SGVATDIQAL KAAFDVNNKD VSVMMSEMDV NAIAGTLKLY FRELPEPLFT
DEFYPNFAEG IALSDPVAKE SCMLNLLLSL PEANLLTFLF LLDHLKRVAE KETVNKMSLH
NLATVFGPTL LRPSEKESKL PANPSQPITM TDSWSLEVMS QVQVLLYFLQ LEAIPAPDSK
RQSILFSTEV
