ABL_DROME
ID ABL_DROME Reviewed; 1620 AA.
AC P00522; Q95TV1; Q9VV86;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Tyrosine-protein kinase Abl;
DE EC=2.7.10.2;
DE AltName: Full=D-ash;
DE AltName: Full=Protein abelson;
GN Name=Abl; Synonyms=ABL-1, Dash; ORFNames=CG4032;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=2832740; DOI=10.1128/mcb.8.2.843-853.1988;
RA Henkemeyer M.J., Bennett R.L., Gertler F.B., Hoffmann F.M.;
RT "DNA sequence, structure, and tyrosine kinase activity of the Drosophila
RT melanogaster Abelson proto-oncogene homolog.";
RL Mol. Cell. Biol. 8:843-853(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-1620.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-631.
RX PubMed=6317185; DOI=10.1016/0092-8674(83)90172-1;
RA Hoffmann F.M., Fresco L.D., Hoffman-Falk H., Shilo B.-Z.;
RT "Nucleotide sequences of the Drosophila src and abl homologs: conservation
RT and variability in the src family oncogenes.";
RL Cell 35:393-401(1983).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9635189; DOI=10.1016/s0960-9822(98)70249-0;
RA Loureiro J., Peifer M.;
RT "Roles of Armadillo, a Drosophila catenin, during central nervous system
RT development.";
RL Curr. Biol. 8:622-632(1998).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11756472; DOI=10.1083/jcb.200105102;
RA Grevengoed E.E., Loureiro J.J., Jesse T.L., Peifer M.;
RT "Abelson kinase regulates epithelial morphogenesis in Drosophila.";
RL J. Cell Biol. 155:1185-1198(2001).
RN [8]
RP FUNCTION.
RX PubMed=12973825; DOI=10.1002/neu.10232;
RA Hsouna A., Kim Y.-S., VanBerkum M.F.A.;
RT "Abelson tyrosine kinase is required to transduce midline repulsive cues.";
RL J. Neurobiol. 57:15-30(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1497, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Arm and Abl proteins function cooperatively at adherens
CC junctions in both the CNS and epidermis; critical for embryonic
CC epithelial morphogenesis regulating cell shape changes and cell
CC migration. Plays a critical role in transducing embryonic midline
CC repulsive cues; may regulate cytoskeletal dynamics underlying a growth
CC cone's response to midline cues. The ability of pCC/MP2 axons to
CC correctly interpret midline repulsive cues and stay on the ipsilateral
CC side is dependent on the strength of both Slit/robo and Abl-dependent
CC signaling pathways. {ECO:0000269|PubMed:11756472,
CC ECO:0000269|PubMed:12973825, ECO:0000269|PubMed:9635189}.
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:2832740};
CC -!- INTERACTION:
CC P00522; Q8T4F7: ena; NbExp=2; IntAct=EBI-534090, EBI-466810;
CC P00522; P16621: Lar; NbExp=4; IntAct=EBI-534090, EBI-668630;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Arm and ena colocalize with Abl at adherens
CC junctions throughout development. {ECO:0000269|PubMed:11756472,
CC ECO:0000269|PubMed:9635189}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:2832740}.
CC -!- DISRUPTION PHENOTYPE: Both loss- and gain-of-function mutants exhibit
CC neurons within the pCC/MP2 pathway that incorrectly project across the
CC midline. Loss of Abl disrupts cell migration and cell shape changes
CC during dorsal closure. {ECO:0000269|PubMed:11756472,
CC ECO:0000269|PubMed:9635189}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ABL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28934.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL13726.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M19692; AAA28934.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M19690; AAA28934.1; JOINED; Genomic_DNA.
DR EMBL; M19691; AAA28934.1; JOINED; Genomic_DNA.
DR EMBL; AE014296; AAF49431.2; -; Genomic_DNA.
DR EMBL; AY058497; AAL13726.1; ALT_FRAME; mRNA.
DR EMBL; K01042; AAA28443.1; -; Genomic_DNA.
DR PIR; A28128; TVFFA.
DR RefSeq; NP_001287085.1; NM_001300156.1.
DR RefSeq; NP_524843.2; NM_080104.3.
DR AlphaFoldDB; P00522; -.
DR SMR; P00522; -.
DR BioGRID; 69904; 43.
DR IntAct; P00522; 8.
DR STRING; 7227.FBpp0303166; -.
DR iPTMnet; P00522; -.
DR PaxDb; P00522; -.
DR PRIDE; P00522; -.
DR EnsemblMetazoa; FBtr0075357; FBpp0075116; FBgn0000017.
DR EnsemblMetazoa; FBtr0345369; FBpp0311523; FBgn0000017.
DR GeneID; 45821; -.
DR KEGG; dme:Dmel_CG4032; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR eggNOG; KOG4278; Eukaryota.
DR InParanoid; P00522; -.
DR OMA; NMFQESS; -.
DR BRENDA; 2.7.10.2; 1994.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-DME-525793; Myogenesis.
DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR SignaLink; P00522; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR PRO; PR:P00522; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other tissues.
DR ExpressionAtlas; P00522; baseline and differential.
DR Genevisible; P00522; DM.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005927; C:muscle tendon junction; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0003401; P:axis elongation; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IGI:FlyBase.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:CACAO.
DR GO; GO:0007417; P:central nervous system development; IGI:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:CACAO.
DR GO; GO:0048749; P:compound eye development; IGI:FlyBase.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:FlyBase.
DR GO; GO:0007611; P:learning or memory; IMP:CACAO.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:CACAO.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0001764; P:neuron migration; IMP:FlyBase.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:CACAO.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:FlyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:FlyBase.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; TAS:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR GO; GO:0032880; P:regulation of protein localization; IDA:FlyBase.
DR GO; GO:0031647; P:regulation of protein stability; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR CDD; cd09935; SH2_ABL; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR033221; ABL1.
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 PANTHER; PTHR24418:SF162; PTHR24418:SF162; 1.
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; PR00452; SH3DOMAIN.
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 ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..1620
FT /note="Tyrosine-protein kinase Abl"
FT /id="PRO_0000088054"
FT DOMAIN 187..248
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 254..346
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 371..627
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 510..534
FT /note="Kinase activation loop"
FT /evidence="ECO:0000250"
FT COMPBIAS 23..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1082
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 492
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 377..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 445..451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 522
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1497
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 129..136
FT /note="AASLLADA -> RPLFWRI (in Ref. 1; AAA28934)"
FT /evidence="ECO:0000305"
FT CONFLICT 357..360
FT /note="LSPE -> ASAQ (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 628..631
FT /note="ESSI -> VGDV (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 1241..1243
FT /note="AEP -> RT (in Ref. 1; AAA28934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1620 AA; 171588 MW; 14287B02CC8FE86B CRC64;
MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS
RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NEALLQSRPL
PHIPAGSTAA SLLADAAELQ QHQQDSGGLG LQGSSLGGGH SSTTSVFESA HRWTSKENLL
APGPEEDDPQ LFVALYDFQA GGENQLSLKK GEQVRILSYN KSGEWCEAHS DSGNVGWVPS
NYVTPLNSLE KHSWYHGPIS RNAAEYLLSS GINGSFLVRE SESSPGQRSI SLRYEGRVYH
YRISEDPDGK VFVTQEAKFN TLAELVHHHS VPHEGHGLIT PLLYPAPKQN KPTVFPLSPE
PDEWEICRTD IMMKHKLGGG QYGEVYEAVW KRYGNTVAVK TLKEDTMALK DFLEEAAIMK
EMKHPNLVQL IGVCTREPPF YIITEFMSHG NLLDFLRSAG RETLDAVALL YMATQIASGM
SYLESRNYIH RDLAARNCLV GDNKLVKVAD FGLARLMRDD TYTAHAGAKF PIKWTAPEGL
AYNKFSTKSD VWAFGVLLWE IATYGMSPYP AIDLTDVYHK LDKGYRMERP PGCPPEVYDL
MRQCWQWDAT DRPTFKSIHH ALEHMFQESS ITEAVEKQLN ANATSASSSA PSTSGVATGG
GATTTTAASG CASSSSATAS LSLTPQMVKK GLPGGQALTP NAHHNDPHQQ QASTPMSETG
STSTKLSTFS SQGKGNVQMR RTTNKQGKQA PAPPKRTSLL SSSRDSTYRE EDPANARCNF
IDDLSTNGLA RDINSLTQRY DSETDPAADP DTDATGDSLE QSLSQVIAAP VTNKMQHSLH
SGGGGGGIGP RSSQQHSSFK RPTGTPVMGN RGLETRQSKR SQLHSQAPGP GPPSTQPHHG
NNGVVTSAHP ITVGALDVMN VKQVVNRYGT LPKGARIGAY LDSLEDSSEA APALPATAPS
LPPANGHATP PAARLNPKAS PIPPQQMIRS NSSGGVTMQN NAAASLNKLQ RHRTTTEGTM
MTFSSFRAGG SSSSPKRSAS GVASGVQPAL ANLEFPPPPL DLPPPPEEFE GGPPPPPPAP
ESAVQAIQQH LHAQLPNNGN ISNGNGTNNN DSSHNDVSNI APSVEEASSR FGVSLRKREP
STDSCSSLGS PPEDLKEKLI TEIKAAGKDT APASHLANGS GIAVVDPVSL LVTELAESMN
LPKPPPQQQQ KLTNGNSTGS GFKAQLKKVE PKKMSAPMPK AEPANTIIDF KAHLRRVDKE
KEPATPAPAP ATVAVANNAN CNTTGTLNRK EDGSKKFSQA MQKTEIKIDV TNSNVEADAG
AAGEGDLGKR RSTGSINSLK KLWEQQPPAP DYATSTILQQ QPSVVNGGGT PNAQLSPKYG
MKSGAINTVG TLPAKLGNKQ PPAAPPPPPP NCTTSNSSTT SISTSSRDCT SRQQASSTIK
TSHSTQLFTD DEEQSHTEGL GSGGQGSADM TQSLYEQKPQ IQQKPAVPHK PTKLTIYATP
IAKLTEPASS ASSTQISRES ILELVGLLEG SLKHPVNAIA GSQWLQLSDK LNILHNSCVI
FAENGAMPPH SKFQFRELVT RVEAQSQHLR SAGSKNVQDN ERLVAEVGQS LRQISNALNR
