ABL2_MOUSE
ID ABL2_MOUSE Reviewed; 1182 AA.
AC Q4JIM5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tyrosine-protein kinase ABL2;
DE EC=2.7.10.2;
DE AltName: Full=Abelson murine leukemia viral oncogene homolog 2;
DE AltName: Full=Abelson tyrosine-protein kinase 2;
DE AltName: Full=Abelson-related gene protein;
DE AltName: Full=Tyrosine-protein kinase ARG;
GN Name=Abl2 {ECO:0000312|EMBL:AAY86039.1, ECO:0000312|MGI:MGI:87860};
GN Synonyms=Arg;
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] {ECO:0000305, ECO:0000312|EMBL:AAY86039.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND
RP ACTIN-BINDING.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:AAY86039.1};
RX PubMed=11752434; DOI=10.1073/pnas.251249298;
RA Wang Y., Miller A.L., Mooseker M.S., Koleske A.J.;
RT "The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-
RT binding domains to bundle F-actin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14865-14870(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAY86039.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CAP DOMAIN, FUNCTION, ACTIVITY REGULATION,
RP INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND
RP TYR-684, AND MUTAGENESIS OF TYR-272; LYS-317; TYR-439; TYR-568 AND TYR-684.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:AAY86039.1};
RX PubMed=12748290; DOI=10.1128/mcb.23.11.3884-3896.2003;
RA Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.;
RT "Two distinct phosphorylation pathways have additive effects on Abl family
RT kinase activation.";
RL Mol. Cell. Biol. 23:3884-3896(2003).
RN [3]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=9883720; DOI=10.1016/s0896-6273(00)80646-7;
RA Koleske A.J., Gifford A.M., Scott M.L., Nee M., Bronson R.T., Miczek K.A.,
RA Baltimore D.;
RT "Essential roles for the Abl and Arg tyrosine kinases in neurulation.";
RL Neuron 21:1259-1272(1998).
RN [4]
RP FUNCTION.
RX PubMed=11279004; DOI=10.1074/jbc.m100095200;
RA Kain K.H., Klemke R.L.;
RT "Inhibition of cell migration by Abl family tyrosine kinases through
RT uncoupling of Crk-CAS complexes.";
RL J. Biol. Chem. 276:16185-16192(2001).
RN [5]
RP REVIEW ON FUNCTION.
RX PubMed=12775773; DOI=10.1242/jcs.00622;
RA Woodring P.J., Hunter T., Wang J.Y.;
RT "Regulation of F-actin-dependent processes by the Abl family of tyrosine
RT kinases.";
RL J. Cell Sci. 116:2613-2626(2003).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND PHOSPHORYLATION.
RX PubMed=14993293; DOI=10.1128/mcb.24.6.2573-2583.2004;
RA Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.;
RT "Bidirectional signaling links the Abelson kinases to the platelet-derived
RT growth factor receptor.";
RL Mol. Cell. Biol. 24:2573-2583(2004).
RN [7]
RP REVIEW ON FUNCTION.
RX PubMed=14729179; DOI=10.1016/j.tcb.2003.11.003;
RA Hernandez S.E., Krishnaswami M., Miller A.L., Koleske A.J.;
RT "How do Abl family kinases regulate cell shape and movement?";
RL Trends Cell Biol. 14:36-44(2004).
RN [8]
RP FUNCTION.
RX PubMed=16971514; DOI=10.1091/mbc.e06-02-0132;
RA Bradley W.D., Hernandez S.E., Settleman J., Koleske A.J.;
RT "Integrin signaling through Arg activates p190RhoGAP by promoting its
RT binding to p120RasGAP and recruitment to the membrane.";
RL Mol. Biol. Cell 17:4827-4836(2006).
RN [9]
RP FUNCTION.
RX PubMed=17892306; DOI=10.1021/bi701119s;
RA Boyle S.N., Koleske A.J.;
RT "Use of a chemical genetic technique to identify myosin IIb as a substrate
RT of the Abl-related gene (Arg) tyrosine kinase.";
RL Biochemistry 46:11614-11620(2007).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=18182299; DOI=10.1016/j.tibs.2007.10.006;
RA Backert S., Feller S.M., Wessler S.;
RT "Emerging roles of Abl family tyrosine kinases in microbial pathogenesis.";
RL Trends Biochem. Sci. 33:80-90(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-632 AND SER-936, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-632 AND SER-822, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, 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 [13]
RP REVIEW ON FUNCTION, AND DOMAIN.
RX PubMed=20841568; DOI=10.1126/scisignal.3139re6;
RA Colicelli J.;
RT "ABL tyrosine kinases: evolution of function, regulation, and
RT specificity.";
RL Sci. Signal. 3:RE6-RE6(2010).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1-
CC overlapping role in key processes linked to cell growth and survival
CC such as cytoskeleton remodeling in response to extracellular stimuli,
CC cell motility and adhesion, receptor endocytosis, autophagy, DNA damage
CC response and apoptosis. Coordinates actin remodeling through tyrosine
CC phosphorylation of proteins controlling cytoskeleton dynamics like
CC MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1
CC and TUBB (microtubule subunits). Binds directly F-actin and regulates
CC actin cytoskeletal structure through its F-actin-bundling activity.
CC Involved in the regulation of cell adhesion and motility through
CC phosphorylation of key regulators of these processes such as CRK, CRKL
CC or DOK1. Required for adhesion-dependent phosphorylation of ARHGAP35
CC which promotes its association with RASA1, resulting in recruitment of
CC ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates
CC multiple receptor tyrosine kinases like PDGFRB and other substrates
CC which are involved in endocytosis regulation such as RIN1. In brain,
CC may regulate neurotransmission by phosphorylating proteins at the
CC synapse. Finally, functions as its own regulator through autocatalytic
CC activity as well as through phosphorylation of its inhibitor, ABI1.
CC {ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:11752434,
CC ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293,
CC ECO:0000269|PubMed:16971514, ECO:0000269|PubMed:17892306,
CC ECO:0000269|PubMed:9883720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:12748290};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12748290};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12748290};
CC -!- ACTIVITY REGULATION: Stabilized in the inactive form by an association
CC between the SH3 domain and the SH2-TK linker region, interactions of
CC the N-terminal cap, and contributions from an N-terminal myristoyl
CC group and phospholipids. Activated by autophosphorylation as well as by
CC SRC-family kinase-mediated phosphorylation. Activated by RIN1 binding
CC to the SH2 and SH3 domains (By similarity). Inhibited by imatinib
CC mesylate (Gleevec). Phosphatidylinositol 4,5-bisphosphate (PIP2), a
CC highly abundant phosphoinositide known to regulate cytoskeletal and
CC membrane proteins, inhibits the tyrosine kinase activity. {ECO:0000250,
CC ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293}.
CC -!- SUBUNIT: Interacts with PSMA7. Interacts with CTTN (By similarity).
CC Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the
CC inhibition of CRK phosphorylation by ABL kinases (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11752434}.
CC -!- TISSUE SPECIFICITY: Most abundant in adult mouse brain, especially in
CC synapse-rich regions. {ECO:0000269|PubMed:9883720}.
CC -!- DOMAIN: Contains two distinct classes of F-actin-binding domains.
CC Although both can each bind F-actin, the 2 are required to bundle actin
CC filaments. {ECO:0000269|PubMed:11752434, ECO:0000269|PubMed:20841568}.
CC -!- PTM: Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress
CC (By similarity). Phosphorylated by PDGFRB. {ECO:0000250,
CC ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293}.
CC -!- PTM: Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation
CC (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Leads to defects in neuronal function.
CC {ECO:0000269|PubMed:9883720}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ABL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; DQ084361; AAY86039.1; -; mRNA.
DR CCDS; CCDS15393.1; -.
DR PDB; 4XLI; X-ray; 2.50 A; A/B=279-546.
DR PDBsum; 4XLI; -.
DR AlphaFoldDB; Q4JIM5; -.
DR SMR; Q4JIM5; -.
DR CORUM; Q4JIM5; -.
DR DIP; DIP-60989N; -.
DR IntAct; Q4JIM5; 4.
DR STRING; 10090.ENSMUSP00000027888; -.
DR ChEMBL; CHEMBL5222; -.
DR iPTMnet; Q4JIM5; -.
DR PhosphoSitePlus; Q4JIM5; -.
DR EPD; Q4JIM5; -.
DR jPOST; Q4JIM5; -.
DR MaxQB; Q4JIM5; -.
DR PaxDb; Q4JIM5; -.
DR PeptideAtlas; Q4JIM5; -.
DR PRIDE; Q4JIM5; -.
DR ProteomicsDB; 285830; -.
DR MGI; MGI:87860; Abl2.
DR eggNOG; KOG4278; Eukaryota.
DR InParanoid; Q4JIM5; -.
DR PhylomeDB; Q4JIM5; -.
DR Reactome; R-MMU-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9706369; Negative regulation of FLT3.
DR ChiTaRS; Abl2; mouse.
DR PRO; PR:Q4JIM5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q4JIM5; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; TAS:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0001891; C:phagocytic cup; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0002118; P:aggressive behavior; IMP:MGI.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IGI:MGI.
DR GO; GO:0031223; P:auditory behavior; IMP:MGI.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IGI:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
DR GO; GO:0021587; P:cerebellum morphogenesis; IGI:MGI.
DR GO; GO:0072359; P:circulatory system development; IGI:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0097062; P:dendritic spine maintenance; IMP:MGI.
DR GO; GO:1904157; P:DN4 thymocyte differentiation; IGI:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0035640; P:exploration behavior; IGI:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IGI:MGI.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IGI:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IGI:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IGI:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR GO; GO:0016322; P:neuron remodeling; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:MGI.
DR GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IGI:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IGI:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IGI:MGI.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:MGI.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:MGI.
DR GO; GO:2000406; P:positive regulation of T cell migration; IMP:UniProtKB.
DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IGI:MGI.
DR GO; GO:0009791; P:post-embryonic development; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; IGI:MGI.
DR GO; GO:0022414; P:reproductive process; IMP:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IGI:MGI.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IGI:MGI.
DR GO; GO:0060074; P:synapse maturation; IDA:SynGO.
DR GO; GO:0008542; P:visual learning; IGI:MGI.
DR CDD; cd09935; SH2_ABL; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035837; ABL_SH2.
DR InterPro; IPR015015; F-actin-binding.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF08919; F_actin_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00808; FABD; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell adhesion; Cytoplasm;
KW Cytoskeleton; Kinase; Lipoprotein; Magnesium; Manganese; Metal-binding;
KW Myristate; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..1182
FT /note="Tyrosine-protein kinase ABL2"
FT /id="PRO_0000258019"
FT DOMAIN 107..167
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 173..263
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 288..539
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..106
FT /note="CAP"
FT REGION 612..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..930
FT /note="F-actin-binding"
FT REGION 765..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1182
FT /note="F-actin-binding"
FT MOTIF 427..451
FT /note="Kinase activation loop"
FT /evidence="ECO:0000250"
FT MOTIF 659..661
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 776..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10028"
FT BINDING 294..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:12748290"
FT BINDING 362..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 174
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 218
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 231
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 261
FT /note="Phosphotyrosine; by ABL1 and autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 272
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12748290"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 299
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 303
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 439
FT /note="Phosphotyrosine; by autocatalysis and SRC-type Tyr-
FT kinases"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 459
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 568
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12748290"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 684
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12748290"
FT MOD_RES 719
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 778
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 802
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42684"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MUTAGEN 272
FT /note="Y->F: Minimal reduction in ability to
FT autophosphorylate."
FT /evidence="ECO:0000269|PubMed:12748290"
FT MUTAGEN 317
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12748290"
FT MUTAGEN 439
FT /note="Y->F: Partial reduction in ability to
FT autophosphorylate."
FT /evidence="ECO:0000269|PubMed:12748290"
FT MUTAGEN 568
FT /note="Y->F: No reduction in ability to autophosphorylate."
FT /evidence="ECO:0000269|PubMed:12748290"
FT MUTAGEN 684
FT /note="Y->F: Minimal reduction in ability to
FT autophosphorylate."
FT /evidence="ECO:0000269|PubMed:12748290"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:4XLI"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:4XLI"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:4XLI"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:4XLI"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:4XLI"
FT STRAND 353..362
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:4XLI"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 383..402
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:4XLI"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:4XLI"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:4XLI"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 464..479
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 494..499
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 512..521
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:4XLI"
FT HELIX 532..545
FT /evidence="ECO:0007829|PDB:4XLI"
SQ SEQUENCE 1182 AA; 128196 MW; 08507298A9081228 CRC64;
MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TADAGFNVFT QHDHFASCVE
DGFEGDKTGG SSPEVLHRPF GCDAESQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA
SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR
SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTTDSKV YVTAESRFST
LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG
EVYVGVWKKY SLTVAVKTFK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV
TEYMPYGNLL DYLRECSREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN
HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT
YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE
TMFHDSSISE EVAEELGRTA SSSSVVPYLP RLPLLPSKTR TLRKQGENKE NLDGGLDAAE
SLASSSAPAG FIRSTQASSG SPALPRKQRD KSPSSLLEDA KETCFTRDRK GGFFSSFMKK
RNAPTPPKRS SSFREMENQP HKKYELTGNF SPVASLQNAD GFSVAPSQQE PNLVPAKCYG
GSFAQRNLCA DDDSGGGGGS GTAGGGWSGI TGFFTPRLIK KTLGLRAGKP TASDDTSKPF
PRSNSTSSMS SGLPEQDRMA MTLPRNCQRS KLQLERTVST SSQPEENVDR ANDMLPKKSE
EGAAPARERP KAKLLPRGAT ALPLRAPDPA ITESDSPGVG VAGVAAAPKG KERNGGTRLG
VAGVPEDGEQ LGWSSPAKAV AVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL
LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSTCS DPEEEPTAPP AGQHTPETQE
GGKKAAPGPV PSSGKPGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS
ADKISKEALL ECADLLSSAI TEPVPNSQLV DTGHQLLDYC SGYVDSIPQT RNKFAFREAV
SKLELSLQEL QVSSTAAGVP GTNPVLNNLL SCVQEISDVV QR
