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 27-MAR-2024, entry version 168. 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 a 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; 19. DR IntAct; Q6PAJ1; 7. DR MINT; Q6PAJ1; -. DR STRING; 10090.ENSMUSP00000126377; -. DR BindingDB; Q6PAJ1; -. DR GlyGen; Q6PAJ1; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q6PAJ1; -. DR PhosphoSitePlus; Q6PAJ1; -. DR SwissPalm; Q6PAJ1; -. DR EPD; Q6PAJ1; -. DR jPOST; Q6PAJ1; -. DR MaxQB; Q6PAJ1; -. DR PaxDb; 10090-ENSMUSP00000126377; -. DR PeptideAtlas; Q6PAJ1; -. DR ProteomicsDB; 273480; -. DR Pumba; Q6PAJ1; -. DR Antibodypedia; 9277; 754 antibodies from 40 providers. DR DNASU; 110279; -. DR Ensembl; ENSMUST00000164107.3; ENSMUSP00000126377.2; ENSMUSG00000009681.11. DR GeneID; 110279; -. DR KEGG; mmu:110279; -. DR UCSC; uc007fqb.2; mouse. DR AGR; MGI:88141; -. 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; IKVKISH; -. DR OrthoDB; 2916231at2759; -. 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; 2 hits in 80 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 236 other cell types or tissues. DR ExpressionAtlas; Q6PAJ1; baseline and differential. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. 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; IDA: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; IDA: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; IDA: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:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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: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; cd08686; C2_ABR; 1. DR CDD; cd04387; RhoGAP_Bcr; 1. DR CDD; cd00160; RhoGEF; 1. DR Gene3D; 4.10.280.30; Bcr-Abl oncoprotein oligomerisation domain; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 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:SF3; BREAKPOINT CLUSTER REGION PROTEIN; 1. DR PANTHER; PTHR23182; BREAKPOINT CLUSTER REGION PROTEIN BCR; 1. DR Pfam; PF09036; Bcr-Abl_Oligo; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF19057; PH_19; 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; SSF69036; Bcr-Abl oncoprotein oligomerization domain; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF50729; PH domain-like; 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. DR Genevisible; Q6PAJ1; MM. 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 //