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 27-MAR-2024, entry version 230. 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). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=37041188; DOI=10.1038/s41598-023-32943-4; RA Vaikakkara Chithran A., Allan D.W., O'Connor T.P.; RT "Adult expression of Semaphorins and Plexins is essential for motor neuron RT survival."; RL Sci. Rep. 13:5894-5894(2023). 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 (PubMed:11756472, PubMed:12973825, PubMed:9635189). Plays a CC critical role in transducing embryonic midline repulsive cues; may CC regulate cytoskeletal dynamics underlying a growth cone's response to CC midline cues (PubMed:12973825). 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 (PubMed:12973825). Function in neurons is essential CC for adult survival, and is important for climbing behavior and activity CC (PubMed:37041188). {ECO:0000269|PubMed:11756472, CC ECO:0000269|PubMed:12973825, ECO:0000269|PubMed:37041188, CC 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; P51140: dsh; NbExp=6; IntAct=EBI-534090, EBI-499383; 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 (PubMed:11756472, PubMed:9635189). RNAi-mediated CC knockdown in the neurons of adult males, significantly reduces survival CC to 53 percent (PubMed:37041188). Adult survival begins to decrease from CC approximately day 14 post eclosion (PubMed:37041188). Pan-neuronal or CC glutamatergic neuron-specific RNAi-mediated knockdown decreases adult CC climbing behavior (PubMed:37041188). Glutamatergic neuron-specific CC RNAi-mediated knockdown also increases activity, at least during the CC light cycle (PubMed:37041188). {ECO:0000269|PubMed:11756472, CC ECO:0000269|PubMed:37041188, 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}; 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; 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; 9. DR STRING; 7227.FBpp0303166; -. DR iPTMnet; P00522; -. DR PaxDb; 7227-FBpp0303166; -. DR EnsemblMetazoa; FBtr0075357; FBpp0075116; FBgn0000017. DR EnsemblMetazoa; FBtr0345369; FBpp0311523; FBgn0000017. DR GeneID; 45821; -. DR KEGG; dme:Dmel_CG4032; -. DR AGR; FB:FBgn0000017; -. DR CTD; 45821; -. DR FlyBase; FBgn0000017; Abl. DR VEuPathDB; VectorBase:FBgn0000017; -. DR eggNOG; KOG4278; Eukaryota. DR InParanoid; P00522; -. 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 Reactome; R-DME-9013423; RAC3 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 cell types or tissues. DR ExpressionAtlas; P00522; baseline and differential. 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:0005829; C:cytosol; IDA:FlyBase. DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; 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: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:0016318; P:ommatidial rotation; IMP:FlyBase. DR GO; GO:0007300; P:ovarian nurse cell to oocyte transport; 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:1903391; P:regulation of adherens junction organization; IMP: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; cd05052; PTKc_Abl; 1. DR CDD; cd09935; SH2_ABL; 1. DR CDD; cd11850; SH3_Abl; 1. DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24418:SF162; TYROSINE-PROTEIN KINASE ABL; 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; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 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. DR Genevisible; P00522; DM. 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 //