LinkDB: ABL_DROME M9PFI5_DROME M9PCT8_DROME M9PFS1_DROME M9PCU1_DROME X2JGR4_DROME A8JNU2_DROME M9PFI8_DROME M9PFX0_DROME M9PI83_DROME
Original site: ABL_DROME M9PFI5_DROME M9PCT8_DROME M9PFS1_DROME M9PCU1_DROME X2JGR4_DROME A8JNU2_DROME M9PFI8_DROME M9PFX0_DROME M9PI83_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 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 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: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. 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 //
Ontology (39) GO (39) Chemical reaction (1) KEGG ENZYME (1) Gene (3) KEGG GENES (1) NCBI-Gene (1) FLYBASE (1) Protein sequence (2) RefSeq(pep) (2) DNA sequence (6) EMBL (6) Protein domain (25) InterPro (12) Pfam (4) PROSITE (5) SMART (4) Literature (10) PubMed (10) Enzyme (1) BRENDA (1) All databases (87)
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ID M9PFI5_DROME Unreviewed; 1607 AA.
AC M9PFI5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:AGB94653.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:AGB94653.1}, ABL
GN {ECO:0000313|EMBL:AGB94653.1}, abl {ECO:0000313|EMBL:AGB94653.1}, Abl1
GN {ECO:0000313|EMBL:AGB94653.1}, abl1 {ECO:0000313|EMBL:AGB94653.1},
GN Ableson {ECO:0000313|EMBL:AGB94653.1}, AblK
GN {ECO:0000313|EMBL:AGB94653.1}, Am ABL {ECO:0000313|EMBL:AGB94653.1},
GN C-abl {ECO:0000313|EMBL:AGB94653.1}, c-abl
GN {ECO:0000313|EMBL:AGB94653.1}, cAbl {ECO:0000313|EMBL:AGB94653.1},
GN D-Abl {ECO:0000313|EMBL:AGB94653.1}, D-abl
GN {ECO:0000313|EMBL:AGB94653.1}, D-ash {ECO:0000313|EMBL:AGB94653.1},
GN DAbl {ECO:0000313|EMBL:AGB94653.1}, Dabl
GN {ECO:0000313|EMBL:AGB94653.1}, dAbl {ECO:0000313|EMBL:AGB94653.1},
GN Dash {ECO:0000313|EMBL:AGB94653.1}, Ddash/abl
GN {ECO:0000313|EMBL:AGB94653.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:AGB94653.1}, DROTKABL3
GN {ECO:0000313|EMBL:AGB94653.1}, Dsrc7 {ECO:0000313|EMBL:AGB94653.1},
GN l(3)04674 {ECO:0000313|EMBL:AGB94653.1}, l(3)73Ba
GN {ECO:0000313|EMBL:AGB94653.1}, l(3)c-abl
GN {ECO:0000313|EMBL:AGB94653.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:AGB94653.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:AGB94653.1};
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 {ECO:0000313|EMBL:AGB94653.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB94653.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AGB94653.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AGB94653.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AGB94653.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AGB94653.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; AGB94653.1; -; Genomic_DNA.
DR RefSeq; NP_001261960.1; NM_001275031.1.
DR SMR; M9PFI5; -.
DR EnsemblMetazoa; FBtr0330131; FBpp0303164; FBgn0000017.
DR GeneID; 45821; -.
DR AGR; FB:FBgn0000017; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR GeneTree; ENSGT00940000173757; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; M9PFI5; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGB94653.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PFI5};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGB94653.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 205..266
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 272..364
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 389..645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1607 AA; 171684 MW; A4C753392116D315 CRC64;
MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS
RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NGTKHSSFRG
HPGKYHMNLE ALLQSRPLPH IPAGSTAASL LADAAELQQH QQDSGGLGLQ GSSLGGGHSS
TTSVFESAHR WTSKENLLAP GPEEDDPQLF VALYDFQAGG ENQLSLKKGE QVRILSYNKS
GEWCEAHSDS GNVGWVPSNY VTPLNSLEKH SWYHGPISRN AAEYLLSSGI NGSFLVRESE
SSPGQRSISL RYEGRVYHYR ISEDPDGKVF VTQEAKFNTL AELVHHHSVP HEGHGLITPL
LYPAPKQNKP TVFPLSPEPD EWEICRTDIM MKHKLGGGQY GEVYEAVWKR YGNTVAVKTL
KEDTMALKDF LEEAAIMKEM KHPNLVQLIG VCTREPPFYI ITEFMSHGNL LDFLRSAGRE
TLDAVALLYM ATQIASGMSY LESRNYIHRD LAARNCLVGD NKLVKVADFG LARLMRDDTY
TAHAGAKFPI KWTAPEGLAY NKFSTKSDVW AFGVLLWEIA TYGMSPYPAI DLTDVYHKLD
KGYRMERPPG CPPEVYDLMR QCWQWDATDR PTFKSIHHAL EHMFQESSIT EAVEKQLNAN
ATSASSSAPS TSGVATGGGA TTTTAASGCA SSSSATASLS LTPQMVKKGL PGGQALTPNA
HHNDPHQQQA STPMSETGST STKLSTFSSQ GKGNVQMRRT TNKQGKQAPA PPKRTSLLSS
SRDSTYREED PANARCNFID DLSTNGIHKL KTANYFSQTL SRNFKTQIPT HHTHQIRTQQ
QQQQQSVQQQ QQIVPLSVQQ QAHQQQQKQQ QYSIKKSSSC SSFLYDILFR GLARDINSLT
QRYDSETDPA ADPDTDATGD SLEQSLSQVI AAPVTNKMQH SLHSGGGGGG IGPRSSQQHS
SFKRPTGTPV MGNRGLETRQ SKRSQLHSQA PGPGPPSTQP HHGNNGVVTS AHPITVGALD
VMNVKQVVNR YGTLPKGARI GAYLDSLEDS SEAAPALPAT APSLPPANGH ATPPAARLNP
KASPIPPQQM IRSNSSGGVT MQNNAAASLN KLQRHRTTTE GTMMTFSSFR AGGSSSSPKR
SASGVASGVQ PALANLEFPP PPLDLPPPPE EFEGGPPPPP PAPESAVQAI QQHLHAQLPN
NGNISNGNGT NNNDSSHNDV SNIAPSVEEA SSRFGVSLRK REPSTDSCSS LGSPPEDLKE
KLITEIKAAG KDTAPASHLA NGSGIAVVDP VSLLVTELAE SMNLPKPPPQ QQQKLTNGNS
TGSGFKAQLK KVEPKKMSAP MPKAEPANTI IDFKAHLRRV DKEKEPATPA PAPATVAVAN
NANCNTTGTL NRKEDGSKKF SQAMQKTEIK IDVTNSNVEA DAGAAGEGDL GKRRSTDDEE
QSHTEGLGSG GQGSADMTQS LYEQKPQIQQ KPAVPHKPTK LTIYATPIAK LTEPASSASS
TQISRESILE LVGLLEGSLK HPVNAIAGSQ WLQLSDKLNI LHNSCVIFAE NGAMPPHSKF
QFRELVTRVE AQSQHLRSAG SKNVQDNERL VAEVGQSLRQ ISNALNR
//
ID M9PCT8_DROME Unreviewed; 1705 AA.
AC M9PCT8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:AGB94652.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:AGB94652.1}, ABL
GN {ECO:0000313|EMBL:AGB94652.1}, abl {ECO:0000313|EMBL:AGB94652.1}, Abl1
GN {ECO:0000313|EMBL:AGB94652.1}, abl1 {ECO:0000313|EMBL:AGB94652.1},
GN Ableson {ECO:0000313|EMBL:AGB94652.1}, AblK
GN {ECO:0000313|EMBL:AGB94652.1}, Am ABL {ECO:0000313|EMBL:AGB94652.1},
GN C-abl {ECO:0000313|EMBL:AGB94652.1}, c-abl
GN {ECO:0000313|EMBL:AGB94652.1}, cAbl {ECO:0000313|EMBL:AGB94652.1},
GN D-Abl {ECO:0000313|EMBL:AGB94652.1}, D-abl
GN {ECO:0000313|EMBL:AGB94652.1}, D-ash {ECO:0000313|EMBL:AGB94652.1},
GN DAbl {ECO:0000313|EMBL:AGB94652.1}, Dabl
GN {ECO:0000313|EMBL:AGB94652.1}, dAbl {ECO:0000313|EMBL:AGB94652.1},
GN Dash {ECO:0000313|EMBL:AGB94652.1}, Ddash/abl
GN {ECO:0000313|EMBL:AGB94652.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:AGB94652.1}, DROTKABL3
GN {ECO:0000313|EMBL:AGB94652.1}, Dsrc7 {ECO:0000313|EMBL:AGB94652.1},
GN l(3)04674 {ECO:0000313|EMBL:AGB94652.1}, l(3)73Ba
GN {ECO:0000313|EMBL:AGB94652.1}, l(3)c-abl
GN {ECO:0000313|EMBL:AGB94652.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:AGB94652.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:AGB94652.1};
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 {ECO:0000313|EMBL:AGB94652.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB94652.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AGB94652.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AGB94652.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AGB94652.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AGB94652.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; AGB94652.1; -; Genomic_DNA.
DR RefSeq; NP_001261959.1; NM_001275030.1.
DR SMR; M9PCT8; -.
DR EnsemblMetazoa; FBtr0330130; FBpp0303163; FBgn0000017.
DR GeneID; 45821; -.
DR AGR; FB:FBgn0000017; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR GeneTree; ENSGT00940000173757; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; M9PCT8; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGB94652.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PCT8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGB94652.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 187..248
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 254..346
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 371..627
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
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..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 933..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1705 AA; 181652 MW; 3374A78DFA3CF321 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
IDDLSTNGIH KLKTANYFSQ TLSRNFKTQI PTHHTHQIRT QQQQQQQSVQ QQQQIVPLSV
QQQAHQQQQK QQQYSIKKSS SCSSFLYDIL FRGLARDINS LTQRYDSETD PAADPDTDAT
GDSLEQSLSQ VIAAPVTNKM QHSLHSGGGG GGIGPRSSQQ HSSFKRPTGT PVMGNRGLET
RQSKRSQLHS QAPGPGPPST QPHHGNNGVV TSAHPITVGA LDVMNVKQVV NRYGTLPKGA
RIGAYLDSLE DSSEAAPALP ATAPSLPPAN GHATPPAARL NPKASPIPPQ QMIRSNSSGG
VTMQNNAAAS LNKLQRHRTT TEGTMMTFSS FRAGGSSSSP KRSASGVASG VQPALANLEF
PPPPLDLPPP PEEFEGGPPP PPPAPESAVQ AIQQHLHAQL PNNGNISNGN GTNNNDSSHN
DVSNIAPSVE EASSRFGVSL RKREPSTDSC SSLGSPPEDL KEKLITEIKA AGKDTAPASH
LANGSGIAVV DPVSLLVTEL AESMNLPKPP PQQQQKLTNG NSTGSGFKAQ LKKVEPKKMS
APMPKAEPAN TIIDFKAHLR RVDKEKEPAT PAPAPATVAV ANNANCNTTG TLNRKEDGSK
KFSQAMQKTE IKIDVTNSNV EADAGAAGEG DLGKRRSTGS INSLKKLWEQ QPPAPDYATS
TILQQQPSVV NGGGTPNAQL SPKYGMKSGA INTVGTLPAK LGNKQPPAAP PPPPPNCTTS
NSSTTSISTS SRDCTSRQQA SSTIKTSHST QLFTDDEEQS HTEGLGSGGQ GSADMTQSLY
EQKPQIQQKP AVPHKPTKLT IYATPIAKLT EPASSASSTQ ISRESILELV GLLEGSLKHP
VNAIAGSQWL QLSDKLNILH NSCVIFAENG AMPPHSKFQF RELVTRVEAQ SQHLRSAGSK
NVQDNERLVA EVGQSLRQIS NALNR
//
ID M9PFS1_DROME Unreviewed; 1723 AA.
AC M9PFS1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:AGB94655.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:AGB94655.1}, ABL
GN {ECO:0000313|EMBL:AGB94655.1}, abl {ECO:0000313|EMBL:AGB94655.1}, Abl1
GN {ECO:0000313|EMBL:AGB94655.1}, abl1 {ECO:0000313|EMBL:AGB94655.1},
GN Ableson {ECO:0000313|EMBL:AGB94655.1}, AblK
GN {ECO:0000313|EMBL:AGB94655.1}, Am ABL {ECO:0000313|EMBL:AGB94655.1},
GN C-abl {ECO:0000313|EMBL:AGB94655.1}, c-abl
GN {ECO:0000313|EMBL:AGB94655.1}, cAbl {ECO:0000313|EMBL:AGB94655.1},
GN D-Abl {ECO:0000313|EMBL:AGB94655.1}, D-abl
GN {ECO:0000313|EMBL:AGB94655.1}, D-ash {ECO:0000313|EMBL:AGB94655.1},
GN DAbl {ECO:0000313|EMBL:AGB94655.1}, Dabl
GN {ECO:0000313|EMBL:AGB94655.1}, dAbl {ECO:0000313|EMBL:AGB94655.1},
GN Dash {ECO:0000313|EMBL:AGB94655.1}, Ddash/abl
GN {ECO:0000313|EMBL:AGB94655.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:AGB94655.1}, DROTKABL3
GN {ECO:0000313|EMBL:AGB94655.1}, Dsrc7 {ECO:0000313|EMBL:AGB94655.1},
GN l(3)04674 {ECO:0000313|EMBL:AGB94655.1}, l(3)73Ba
GN {ECO:0000313|EMBL:AGB94655.1}, l(3)c-abl
GN {ECO:0000313|EMBL:AGB94655.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:AGB94655.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:AGB94655.1};
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 {ECO:0000313|EMBL:AGB94655.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB94655.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AGB94655.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AGB94655.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AGB94655.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AGB94655.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; AGB94655.1; -; Genomic_DNA.
DR RefSeq; NP_001261962.1; NM_001275033.1.
DR SMR; M9PFS1; -.
DR EnsemblMetazoa; FBtr0330133; FBpp0303166; FBgn0000017.
DR GeneID; 45821; -.
DR AGR; FB:FBgn0000017; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR GeneTree; ENSGT00940000173757; -.
DR OMA; SGVVNTY; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; M9PFS1; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGB94655.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PFS1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGB94655.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 205..266
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 272..364
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 389..645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1723 AA; 183689 MW; 845A0421FB08BE4B CRC64;
MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS
RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NGTKHSSFRG
HPGKYHMNLE ALLQSRPLPH IPAGSTAASL LADAAELQQH QQDSGGLGLQ GSSLGGGHSS
TTSVFESAHR WTSKENLLAP GPEEDDPQLF VALYDFQAGG ENQLSLKKGE QVRILSYNKS
GEWCEAHSDS GNVGWVPSNY VTPLNSLEKH SWYHGPISRN AAEYLLSSGI NGSFLVRESE
SSPGQRSISL RYEGRVYHYR ISEDPDGKVF VTQEAKFNTL AELVHHHSVP HEGHGLITPL
LYPAPKQNKP TVFPLSPEPD EWEICRTDIM MKHKLGGGQY GEVYEAVWKR YGNTVAVKTL
KEDTMALKDF LEEAAIMKEM KHPNLVQLIG VCTREPPFYI ITEFMSHGNL LDFLRSAGRE
TLDAVALLYM ATQIASGMSY LESRNYIHRD LAARNCLVGD NKLVKVADFG LARLMRDDTY
TAHAGAKFPI KWTAPEGLAY NKFSTKSDVW AFGVLLWEIA TYGMSPYPAI DLTDVYHKLD
KGYRMERPPG CPPEVYDLMR QCWQWDATDR PTFKSIHHAL EHMFQESSIT EAVEKQLNAN
ATSASSSAPS TSGVATGGGA TTTTAASGCA SSSSATASLS LTPQMVKKGL PGGQALTPNA
HHNDPHQQQA STPMSETGST STKLSTFSSQ GKGNVQMRRT TNKQGKQAPA PPKRTSLLSS
SRDSTYREED PANARCNFID DLSTNGIHKL KTANYFSQTL SRNFKTQIPT HHTHQIRTQQ
QQQQQSVQQQ QQIVPLSVQQ QAHQQQQKQQ QYSIKKSSSC SSFLYDILFR GLARDINSLT
QRYDSETDPA ADPDTDATGD SLEQSLSQVI AAPVTNKMQH SLHSGGGGGG IGPRSSQQHS
SFKRPTGTPV MGNRGLETRQ SKRSQLHSQA PGPGPPSTQP HHGNNGVVTS AHPITVGALD
VMNVKQVVNR YGTLPKGARI GAYLDSLEDS SEAAPALPAT APSLPPANGH ATPPAARLNP
KASPIPPQQM IRSNSSGGVT MQNNAAASLN KLQRHRTTTE GTMMTFSSFR AGGSSSSPKR
SASGVASGVQ PALANLEFPP PPLDLPPPPE EFEGGPPPPP PAPESAVQAI QQHLHAQLPN
NGNISNGNGT NNNDSSHNDV SNIAPSVEEA SSRFGVSLRK REPSTDSCSS LGSPPEDLKE
KLITEIKAAG KDTAPASHLA NGSGIAVVDP VSLLVTELAE SMNLPKPPPQ QQQKLTNGNS
TGSGFKAQLK KVEPKKMSAP MPKAEPANTI IDFKAHLRRV DKEKEPATPA PAPATVAVAN
NANCNTTGTL NRKEDGSKKF SQAMQKTEIK IDVTNSNVEA DAGAAGEGDL GKRRSTGSIN
SLKKLWEQQP PAPDYATSTI LQQQPSVVNG GGTPNAQLSP KYGMKSGAIN TVGTLPAKLG
NKQPPAAPPP PPPNCTTSNS STTSISTSSR DCTSRQQASS TIKTSHSTQL FTDDEEQSHT
EGLGSGGQGS ADMTQSLYEQ KPQIQQKPAV PHKPTKLTIY ATPIAKLTEP ASSASSTQIS
RESILELVGL LEGSLKHPVN AIAGSQWLQL SDKLNILHNS CVIFAENGAM PPHSKFQFRE
LVTRVEAQSQ HLRSAGSKNV QDNERLVAEV GQSLRQISNA LNR
//
ID M9PCU1_DROME Unreviewed; 1504 AA.
AC M9PCU1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:AGB94657.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:AGB94657.1}, ABL
GN {ECO:0000313|EMBL:AGB94657.1}, abl {ECO:0000313|EMBL:AGB94657.1}, Abl1
GN {ECO:0000313|EMBL:AGB94657.1}, abl1 {ECO:0000313|EMBL:AGB94657.1},
GN Ableson {ECO:0000313|EMBL:AGB94657.1}, AblK
GN {ECO:0000313|EMBL:AGB94657.1}, Am ABL {ECO:0000313|EMBL:AGB94657.1},
GN C-abl {ECO:0000313|EMBL:AGB94657.1}, c-abl
GN {ECO:0000313|EMBL:AGB94657.1}, cAbl {ECO:0000313|EMBL:AGB94657.1},
GN D-Abl {ECO:0000313|EMBL:AGB94657.1}, D-abl
GN {ECO:0000313|EMBL:AGB94657.1}, D-ash {ECO:0000313|EMBL:AGB94657.1},
GN DAbl {ECO:0000313|EMBL:AGB94657.1}, Dabl
GN {ECO:0000313|EMBL:AGB94657.1}, dAbl {ECO:0000313|EMBL:AGB94657.1},
GN Dash {ECO:0000313|EMBL:AGB94657.1}, Ddash/abl
GN {ECO:0000313|EMBL:AGB94657.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:AGB94657.1}, DROTKABL3
GN {ECO:0000313|EMBL:AGB94657.1}, Dsrc7 {ECO:0000313|EMBL:AGB94657.1},
GN l(3)04674 {ECO:0000313|EMBL:AGB94657.1}, l(3)73Ba
GN {ECO:0000313|EMBL:AGB94657.1}, l(3)c-abl
GN {ECO:0000313|EMBL:AGB94657.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:AGB94657.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:AGB94657.1};
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 {ECO:0000313|EMBL:AGB94657.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB94657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AGB94657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AGB94657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AGB94657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AGB94657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; AGB94657.1; -; Genomic_DNA.
DR RefSeq; NP_001261964.1; NM_001275035.1.
DR SMR; M9PCU1; -.
DR EnsemblMetazoa; FBtr0330135; FBpp0303168; FBgn0000017.
DR GeneID; 45821; -.
DR AGR; FB:FBgn0000017; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR GeneTree; ENSGT00940000173757; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; M9PCU1; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGB94657.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PCU1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGB94657.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 187..248
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 254..346
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 371..627
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
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 1309..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1323..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1504 AA; 159584 MW; 0B1D05FB224C1342 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 RSTDDEEQSH TEGLGSGGQG SADMTQSLYE QKPQIQQKPA VPHKPTKLTI
YATPIAKLTE PASSASSTQI SRESILELVG LLEGSLKHPV NAIAGSQWLQ LSDKLNILHN
SCVIFAENGA MPPHSKFQFR ELVTRVEAQS QHLRSAGSKN VQDNERLVAE VGQSLRQISN
ALNR
//
ID X2JGR4_DROME Unreviewed; 1620 AA.
AC X2JGR4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:AHN58110.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:AHN58110.1}, ABL
GN {ECO:0000313|EMBL:AHN58110.1}, abl {ECO:0000313|EMBL:AHN58110.1}, Abl1
GN {ECO:0000313|EMBL:AHN58110.1}, abl1 {ECO:0000313|EMBL:AHN58110.1},
GN Ableson {ECO:0000313|EMBL:AHN58110.1}, AblK
GN {ECO:0000313|EMBL:AHN58110.1}, Am ABL {ECO:0000313|EMBL:AHN58110.1},
GN C-abl {ECO:0000313|EMBL:AHN58110.1}, c-abl
GN {ECO:0000313|EMBL:AHN58110.1}, cAbl {ECO:0000313|EMBL:AHN58110.1},
GN D-Abl {ECO:0000313|EMBL:AHN58110.1}, D-abl
GN {ECO:0000313|EMBL:AHN58110.1}, D-ash {ECO:0000313|EMBL:AHN58110.1},
GN DAbl {ECO:0000313|EMBL:AHN58110.1}, Dabl
GN {ECO:0000313|EMBL:AHN58110.1}, dAbl {ECO:0000313|EMBL:AHN58110.1},
GN Dash {ECO:0000313|EMBL:AHN58110.1}, Ddash/abl
GN {ECO:0000313|EMBL:AHN58110.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:AHN58110.1}, DROTKABL3
GN {ECO:0000313|EMBL:AHN58110.1}, Dsrc7 {ECO:0000313|EMBL:AHN58110.1},
GN l(3)04674 {ECO:0000313|EMBL:AHN58110.1}, l(3)73Ba
GN {ECO:0000313|EMBL:AHN58110.1}, l(3)c-abl
GN {ECO:0000313|EMBL:AHN58110.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:AHN58110.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:AHN58110.1};
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 {ECO:0000313|EMBL:AHN58110.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AHN58110.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AHN58110.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AHN58110.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AHN58110.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AHN58110.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; AHN58110.1; -; Genomic_DNA.
DR RefSeq; NP_001287085.1; NM_001300156.1.
DR RefSeq; NP_524843.2; NM_080104.3.
DR SMR; X2JGR4; -.
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 GeneTree; ENSGT00940000173757; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; X2JGR4; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AHN58110.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:X2JGR4};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHN58110.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 187..248
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 254..346
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 371..627
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
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 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 BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
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
//
Ontology (11) GO (11) Chemical reaction (1) KEGG ENZYME (1) Gene (3) KEGG GENES (1) NCBI-Gene (1) FLYBASE (1) Protein sequence (2) RefSeq(pep) (2) DNA sequence (1) EMBL (1) Protein domain (25) InterPro (12) Pfam (4) PROSITE (5) SMART (4) Literature (8) PubMed (8) All databases (51)
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ID A8JNU2_DROME Unreviewed; 1638 AA.
AC A8JNU2;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:ABW08554.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:ABW08554.1}, ABL
GN {ECO:0000313|EMBL:ABW08554.1}, abl {ECO:0000313|EMBL:ABW08554.1}, Abl1
GN {ECO:0000313|EMBL:ABW08554.1}, abl1 {ECO:0000313|EMBL:ABW08554.1},
GN Ableson {ECO:0000313|EMBL:ABW08554.1}, AblK
GN {ECO:0000313|EMBL:ABW08554.1}, Am ABL {ECO:0000313|EMBL:ABW08554.1},
GN C-abl {ECO:0000313|EMBL:ABW08554.1}, c-abl
GN {ECO:0000313|EMBL:ABW08554.1}, cAbl {ECO:0000313|EMBL:ABW08554.1},
GN D-Abl {ECO:0000313|EMBL:ABW08554.1}, D-abl
GN {ECO:0000313|EMBL:ABW08554.1}, D-ash {ECO:0000313|EMBL:ABW08554.1},
GN DAbl {ECO:0000313|EMBL:ABW08554.1}, Dabl
GN {ECO:0000313|EMBL:ABW08554.1}, dAbl {ECO:0000313|EMBL:ABW08554.1},
GN Dash {ECO:0000313|EMBL:ABW08554.1}, Ddash/abl
GN {ECO:0000313|EMBL:ABW08554.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:ABW08554.1}, DROTKABL3
GN {ECO:0000313|EMBL:ABW08554.1}, Dsrc7 {ECO:0000313|EMBL:ABW08554.1},
GN l(3)04674 {ECO:0000313|EMBL:ABW08554.1}, l(3)73Ba
GN {ECO:0000313|EMBL:ABW08554.1}, l(3)c-abl
GN {ECO:0000313|EMBL:ABW08554.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:ABW08554.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:ABW08554.1};
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 {ECO:0000313|EMBL:ABW08554.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:ABW08554.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:ABW08554.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:ABW08554.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:ABW08554.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:ABW08554.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; ABW08554.1; -; Genomic_DNA.
DR RefSeq; NP_001097623.1; NM_001104153.3.
DR SMR; A8JNU2; -.
DR EnsemblMetazoa; FBtr0112790; FBpp0111702; FBgn0000017.
DR GeneID; 45821; -.
DR UCSC; CG4032-RB; d. melanogaster.
DR AGR; FB:FBgn0000017; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR GeneTree; ENSGT00940000173757; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; A8JNU2; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; A8JNU2; baseline and differential.
DR Genevisible; A8JNU2; DM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABW08554.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A8JNU2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABW08554.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 205..266
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 272..364
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 389..645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1638 AA; 173624 MW; 1B3058D2CE25FC98 CRC64;
MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS
RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NGTKHSSFRG
HPGKYHMNLE ALLQSRPLPH IPAGSTAASL LADAAELQQH QQDSGGLGLQ GSSLGGGHSS
TTSVFESAHR WTSKENLLAP GPEEDDPQLF VALYDFQAGG ENQLSLKKGE QVRILSYNKS
GEWCEAHSDS GNVGWVPSNY VTPLNSLEKH SWYHGPISRN AAEYLLSSGI NGSFLVRESE
SSPGQRSISL RYEGRVYHYR ISEDPDGKVF VTQEAKFNTL AELVHHHSVP HEGHGLITPL
LYPAPKQNKP TVFPLSPEPD EWEICRTDIM MKHKLGGGQY GEVYEAVWKR YGNTVAVKTL
KEDTMALKDF LEEAAIMKEM KHPNLVQLIG VCTREPPFYI ITEFMSHGNL LDFLRSAGRE
TLDAVALLYM ATQIASGMSY LESRNYIHRD LAARNCLVGD NKLVKVADFG LARLMRDDTY
TAHAGAKFPI KWTAPEGLAY NKFSTKSDVW AFGVLLWEIA TYGMSPYPAI DLTDVYHKLD
KGYRMERPPG CPPEVYDLMR QCWQWDATDR PTFKSIHHAL EHMFQESSIT EAVEKQLNAN
ATSASSSAPS TSGVATGGGA TTTTAASGCA SSSSATASLS LTPQMVKKGL PGGQALTPNA
HHNDPHQQQA STPMSETGST STKLSTFSSQ GKGNVQMRRT TNKQGKQAPA PPKRTSLLSS
SRDSTYREED PANARCNFID DLSTNGLARD INSLTQRYDS ETDPAADPDT DATGDSLEQS
LSQVIAAPVT NKMQHSLHSG GGGGGIGPRS SQQHSSFKRP TGTPVMGNRG LETRQSKRSQ
LHSQAPGPGP PSTQPHHGNN GVVTSAHPIT VGALDVMNVK QVVNRYGTLP KGARIGAYLD
SLEDSSEAAP ALPATAPSLP PANGHATPPA ARLNPKASPI PPQQMIRSNS SGGVTMQNNA
AASLNKLQRH RTTTEGTMMT FSSFRAGGSS SSPKRSASGV ASGVQPALAN LEFPPPPLDL
PPPPEEFEGG PPPPPPAPES AVQAIQQHLH AQLPNNGNIS NGNGTNNNDS SHNDVSNIAP
SVEEASSRFG VSLRKREPST DSCSSLGSPP EDLKEKLITE IKAAGKDTAP ASHLANGSGI
AVVDPVSLLV TELAESMNLP KPPPQQQQKL TNGNSTGSGF KAQLKKVEPK KMSAPMPKAE
PANTIIDFKA HLRRVDKEKE PATPAPAPAT VAVANNANCN TTGTLNRKED GSKKFSQAMQ
KTEIKIDVTN SNVEADAGAA GEGDLGKRRS TGSINSLKKL WEQQPPAPDY ATSTILQQQP
SVVNGGGTPN AQLSPKYGMK SGAINTVGTL PAKLGNKQPP AAPPPPPPNC TTSNSSTTSI
STSSRDCTSR QQASSTIKTS HSTQLFTDDE EQSHTEGLGS GGQGSADMTQ SLYEQKPQIQ
QKPAVPHKPT KLTIYATPIA KLTEPASSAS STQISRESIL ELVGLLEGSL KHPVNAIAGS
QWLQLSDKLN ILHNSCVIFA ENGAMPPHSK FQFRELVTRV EAQSQHLRSA GSKNVQDNER
LVAEVGQSLR QISNALNR
//
ID M9PFI8_DROME Unreviewed; 1666 AA.
AC M9PFI8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:AGB94658.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:AGB94658.1}, ABL
GN {ECO:0000313|EMBL:AGB94658.1}, abl {ECO:0000313|EMBL:AGB94658.1}, Abl1
GN {ECO:0000313|EMBL:AGB94658.1}, abl1 {ECO:0000313|EMBL:AGB94658.1},
GN Ableson {ECO:0000313|EMBL:AGB94658.1}, AblK
GN {ECO:0000313|EMBL:AGB94658.1}, Am ABL {ECO:0000313|EMBL:AGB94658.1},
GN C-abl {ECO:0000313|EMBL:AGB94658.1}, c-abl
GN {ECO:0000313|EMBL:AGB94658.1}, cAbl {ECO:0000313|EMBL:AGB94658.1},
GN D-Abl {ECO:0000313|EMBL:AGB94658.1}, D-abl
GN {ECO:0000313|EMBL:AGB94658.1}, D-ash {ECO:0000313|EMBL:AGB94658.1},
GN DAbl {ECO:0000313|EMBL:AGB94658.1}, Dabl
GN {ECO:0000313|EMBL:AGB94658.1}, dAbl {ECO:0000313|EMBL:AGB94658.1},
GN Dash {ECO:0000313|EMBL:AGB94658.1}, Ddash/abl
GN {ECO:0000313|EMBL:AGB94658.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:AGB94658.1}, DROTKABL3
GN {ECO:0000313|EMBL:AGB94658.1}, Dsrc7 {ECO:0000313|EMBL:AGB94658.1},
GN l(3)04674 {ECO:0000313|EMBL:AGB94658.1}, l(3)73Ba
GN {ECO:0000313|EMBL:AGB94658.1}, l(3)c-abl
GN {ECO:0000313|EMBL:AGB94658.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:AGB94658.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:AGB94658.1};
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 {ECO:0000313|EMBL:AGB94658.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB94658.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AGB94658.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AGB94658.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AGB94658.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AGB94658.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; AGB94658.1; -; Genomic_DNA.
DR RefSeq; NP_001261965.1; NM_001275036.1.
DR EnsemblMetazoa; FBtr0330136; FBpp0303169; FBgn0000017.
DR GeneID; 45821; -.
DR AGR; FB:FBgn0000017; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR GeneTree; ENSGT00940000173757; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; M9PFI8; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGB94658.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PFI8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGB94658.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 205..266
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 272..364
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 389..645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1666 AA; 176901 MW; 8D1783A802E639C4 CRC64;
MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS
RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NGTKHSSFRG
HPGKYHMNLE ALLQSRPLPH IPAGSTAASL LADAAELQQH QQDSGGLGLQ GSSLGGGHSS
TTSVFESAHR WTSKENLLAP GPEEDDPQLF VALYDFQAGG ENQLSLKKGE QVRILSYNKS
GEWCEAHSDS GNVGWVPSNY VTPLNSLEKH SWYHGPISRN AAEYLLSSGI NGSFLVRESE
SSPGQRSISL RYEGRVYHYR ISEDPDGKVF VTQEAKFNTL AELVHHHSVP HEGHGLITPL
LYPAPKQNKP TVFPLSPEPD EWEICRTDIM MKHKLGGGQY GEVYEAVWKR YGNTVAVKTL
KEDTMALKDF LEEAAIMKEM KHPNLVQLIG VCTREPPFYI ITEFMSHGNL LDFLRSAGRE
TLDAVALLYM ATQIASGMSY LESRNYIHRD LAARNCLVGD NKLVKVADFG LARLMRDDTY
TAHAGAKFPI KWTAPEGLAY NKFSTKSDVW AFGVLLWEIA TYGMSPYPAI DLTDVYHKLD
KGYRMERPPG CPPEVYDLMR QCWQWDATDR PTFKSIHHAL EHMFQESSIT EAVEKQLNAN
ATSASSSAPS TSGVATGGGA TTTTAASGCA SSSSATASLS LTPQMVKKGL PGGQALTPNA
HHNDPHQQQA STPMSETGST STKLSTFSSQ GKGNVQMRRT TNKQGKQAPA PPKRTSLLSS
SRDSTYREED PANARCNFID DLSTNGLARD INSLTQRYDS ETDPAADPDT DATGDSLEQS
LSQVIAAPVT NKMQHSLHSG GGGGGIGPRS SQQHSSFKRP TGTPVMGNRG LETRQSKRSQ
LHSQAPGPGP PSTQPHHGNN GVVTSAHPIT VGALDVMNVK QVVNRYGTLP KGARIGAYLD
SLEDSSEAAP ALPATAPSLP PANGHATPPA ARLNPKASPI PPQQMIRSNS SGGVTMQNNA
AASLNKLQRH RTTTEGTMMT FSSFRAGGSS SSPKRSASGV ASGVQPALAN LEFPPPPLDL
PPPPEEFEGG PPPPPPAPES AVQAIQQHLH AQLPNNGNIS NGNGTNNNDS SHNDVSNIAP
SVEEASSRFG VSLRKREPST DSCSSLGSPP EDLKEKLITE IKAAGKDTAP ASHLANGSGI
AVVDPVSLLV TELAESMNLP KPPPQQQQKL TNGNSTGSGF KAQLKKVEPK KMSAPMPKAE
PANTIIDFKA HLRRVDKEKE PATPAPAPAT VAVANNANCN TTGTLNRKED GSKKFSQAMQ
KTEIKIDVTN SNVEADAGAA GEGDLGKRRS TGSINSLKKL WEQQPPAPDY ATSTILQQQP
SVVNGGGTPN AQLSPKYGMK SGAINTVGTL PAKLGNKQPP AAPPPPPPNC TTSNSSTTSI
STSSRDCTSR QQASSTIKTS HSTQLFTDDE EQSHTEGLGS GGQGSADMTQ SLYEQKPQIQ
QKPAVPHKPT KLTIYATPIA KLTEPASSAS STQISRESIL ELVGLLEGSL KHPVNAIAGS
QWLQLSDKLN ILHNSCVIFA ENGAMPPHSK FQFRELVTRV EAQSQHLRSA GSKNVQDNER
LVAEVGQSLR QISNALNRXM IRRGMDAPDQ HQGIWLDAEG NFIKRK
//
ID M9PFX0_DROME Unreviewed; 1589 AA.
AC M9PFX0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:AGB94654.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:AGB94654.1}, ABL
GN {ECO:0000313|EMBL:AGB94654.1}, abl {ECO:0000313|EMBL:AGB94654.1}, Abl1
GN {ECO:0000313|EMBL:AGB94654.1}, abl1 {ECO:0000313|EMBL:AGB94654.1},
GN Ableson {ECO:0000313|EMBL:AGB94654.1}, AblK
GN {ECO:0000313|EMBL:AGB94654.1}, Am ABL {ECO:0000313|EMBL:AGB94654.1},
GN C-abl {ECO:0000313|EMBL:AGB94654.1}, c-abl
GN {ECO:0000313|EMBL:AGB94654.1}, cAbl {ECO:0000313|EMBL:AGB94654.1},
GN D-Abl {ECO:0000313|EMBL:AGB94654.1}, D-abl
GN {ECO:0000313|EMBL:AGB94654.1}, D-ash {ECO:0000313|EMBL:AGB94654.1},
GN DAbl {ECO:0000313|EMBL:AGB94654.1}, Dabl
GN {ECO:0000313|EMBL:AGB94654.1}, dAbl {ECO:0000313|EMBL:AGB94654.1},
GN Dash {ECO:0000313|EMBL:AGB94654.1}, Ddash/abl
GN {ECO:0000313|EMBL:AGB94654.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:AGB94654.1}, DROTKABL3
GN {ECO:0000313|EMBL:AGB94654.1}, Dsrc7 {ECO:0000313|EMBL:AGB94654.1},
GN l(3)04674 {ECO:0000313|EMBL:AGB94654.1}, l(3)73Ba
GN {ECO:0000313|EMBL:AGB94654.1}, l(3)c-abl
GN {ECO:0000313|EMBL:AGB94654.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:AGB94654.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:AGB94654.1};
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 {ECO:0000313|EMBL:AGB94654.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB94654.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AGB94654.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AGB94654.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AGB94654.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AGB94654.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; AGB94654.1; -; Genomic_DNA.
DR RefSeq; NP_001261961.1; NM_001275032.1.
DR SMR; M9PFX0; -.
DR EnsemblMetazoa; FBtr0330132; FBpp0303165; FBgn0000017.
DR GeneID; 45821; -.
DR AGR; FB:FBgn0000017; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR GeneTree; ENSGT00940000173757; -.
DR HOGENOM; CLU_002795_1_0_1; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; M9PFX0; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGB94654.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PFX0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGB94654.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 187..248
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 254..346
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 371..627
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
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..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 933..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1589 AA; 169648 MW; 842911300186582A 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
IDDLSTNGIH KLKTANYFSQ TLSRNFKTQI PTHHTHQIRT QQQQQQQSVQ QQQQIVPLSV
QQQAHQQQQK QQQYSIKKSS SCSSFLYDIL FRGLARDINS LTQRYDSETD PAADPDTDAT
GDSLEQSLSQ VIAAPVTNKM QHSLHSGGGG GGIGPRSSQQ HSSFKRPTGT PVMGNRGLET
RQSKRSQLHS QAPGPGPPST QPHHGNNGVV TSAHPITVGA LDVMNVKQVV NRYGTLPKGA
RIGAYLDSLE DSSEAAPALP ATAPSLPPAN GHATPPAARL NPKASPIPPQ QMIRSNSSGG
VTMQNNAAAS LNKLQRHRTT TEGTMMTFSS FRAGGSSSSP KRSASGVASG VQPALANLEF
PPPPLDLPPP PEEFEGGPPP PPPAPESAVQ AIQQHLHAQL PNNGNISNGN GTNNNDSSHN
DVSNIAPSVE EASSRFGVSL RKREPSTDSC SSLGSPPEDL KEKLITEIKA AGKDTAPASH
LANGSGIAVV DPVSLLVTEL AESMNLPKPP PQQQQKLTNG NSTGSGFKAQ LKKVEPKKMS
APMPKAEPAN TIIDFKAHLR RVDKEKEPAT PAPAPATVAV ANNANCNTTG TLNRKEDGSK
KFSQAMQKTE IKIDVTNSNV EADAGAAGEG DLGKRRSTDD EEQSHTEGLG SGGQGSADMT
QSLYEQKPQI QQKPAVPHKP TKLTIYATPI AKLTEPASSA SSTQISRESI LELVGLLEGS
LKHPVNAIAG SQWLQLSDKL NILHNSCVIF AENGAMPPHS KFQFRELVTR VEAQSQHLRS
AGSKNVQDNE RLVAEVGQSL RQISNALNR
//
ID M9PI83_DROME Unreviewed; 1522 AA.
AC M9PI83;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=Abl {ECO:0000313|EMBL:AGB94656.1,
GN ECO:0000313|FlyBase:FBgn0000017};
GN Synonyms=4674 {ECO:0000313|EMBL:AGB94656.1}, ABL
GN {ECO:0000313|EMBL:AGB94656.1}, abl {ECO:0000313|EMBL:AGB94656.1}, Abl1
GN {ECO:0000313|EMBL:AGB94656.1}, abl1 {ECO:0000313|EMBL:AGB94656.1},
GN Ableson {ECO:0000313|EMBL:AGB94656.1}, AblK
GN {ECO:0000313|EMBL:AGB94656.1}, Am ABL {ECO:0000313|EMBL:AGB94656.1},
GN C-abl {ECO:0000313|EMBL:AGB94656.1}, c-abl
GN {ECO:0000313|EMBL:AGB94656.1}, cAbl {ECO:0000313|EMBL:AGB94656.1},
GN D-Abl {ECO:0000313|EMBL:AGB94656.1}, D-abl
GN {ECO:0000313|EMBL:AGB94656.1}, D-ash {ECO:0000313|EMBL:AGB94656.1},
GN DAbl {ECO:0000313|EMBL:AGB94656.1}, Dabl
GN {ECO:0000313|EMBL:AGB94656.1}, dAbl {ECO:0000313|EMBL:AGB94656.1},
GN Dash {ECO:0000313|EMBL:AGB94656.1}, Ddash/abl
GN {ECO:0000313|EMBL:AGB94656.1}, Dmel\CG4032
GN {ECO:0000313|EMBL:AGB94656.1}, DROTKABL3
GN {ECO:0000313|EMBL:AGB94656.1}, Dsrc7 {ECO:0000313|EMBL:AGB94656.1},
GN l(3)04674 {ECO:0000313|EMBL:AGB94656.1}, l(3)73Ba
GN {ECO:0000313|EMBL:AGB94656.1}, l(3)c-abl
GN {ECO:0000313|EMBL:AGB94656.1};
GN ORFNames=CG4032 {ECO:0000313|EMBL:AGB94656.1,
GN ECO:0000313|FlyBase:FBgn0000017}, Dmel_CG4032
GN {ECO:0000313|EMBL:AGB94656.1};
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 {ECO:0000313|EMBL:AGB94656.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB94656.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AGB94656.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AGB94656.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AGB94656.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AGB94656.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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:0000256|ARBA:ARBA00001149};
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DR EMBL; AE014296; AGB94656.1; -; Genomic_DNA.
DR RefSeq; NP_001261963.1; NM_001275034.1.
DR SMR; M9PI83; -.
DR EnsemblMetazoa; FBtr0330134; FBpp0303167; FBgn0000017.
DR GeneID; 45821; -.
DR AGR; FB:FBgn0000017; -.
DR CTD; 45821; -.
DR FlyBase; FBgn0000017; Abl.
DR VEuPathDB; VectorBase:FBgn0000017; -.
DR GeneTree; ENSGT00940000173757; -.
DR OrthoDB; 1614410at2759; -.
DR BioGRID-ORCS; 45821; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45821; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000017; Expressed in central nervous system and 27 other cell types or tissues.
DR ExpressionAtlas; M9PI83; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
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.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGB94656.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PI83};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGB94656.1};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 205..266
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 272..364
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 389..645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1522 AA; 161620 MW; C56F52A82D28D156 CRC64;
MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS
RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NGTKHSSFRG
HPGKYHMNLE ALLQSRPLPH IPAGSTAASL LADAAELQQH QQDSGGLGLQ GSSLGGGHSS
TTSVFESAHR WTSKENLLAP GPEEDDPQLF VALYDFQAGG ENQLSLKKGE QVRILSYNKS
GEWCEAHSDS GNVGWVPSNY VTPLNSLEKH SWYHGPISRN AAEYLLSSGI NGSFLVRESE
SSPGQRSISL RYEGRVYHYR ISEDPDGKVF VTQEAKFNTL AELVHHHSVP HEGHGLITPL
LYPAPKQNKP TVFPLSPEPD EWEICRTDIM MKHKLGGGQY GEVYEAVWKR YGNTVAVKTL
KEDTMALKDF LEEAAIMKEM KHPNLVQLIG VCTREPPFYI ITEFMSHGNL LDFLRSAGRE
TLDAVALLYM ATQIASGMSY LESRNYIHRD LAARNCLVGD NKLVKVADFG LARLMRDDTY
TAHAGAKFPI KWTAPEGLAY NKFSTKSDVW AFGVLLWEIA TYGMSPYPAI DLTDVYHKLD
KGYRMERPPG CPPEVYDLMR QCWQWDATDR PTFKSIHHAL EHMFQESSIT EAVEKQLNAN
ATSASSSAPS TSGVATGGGA TTTTAASGCA SSSSATASLS LTPQMVKKGL PGGQALTPNA
HHNDPHQQQA STPMSETGST STKLSTFSSQ GKGNVQMRRT TNKQGKQAPA PPKRTSLLSS
SRDSTYREED PANARCNFID DLSTNGLARD INSLTQRYDS ETDPAADPDT DATGDSLEQS
LSQVIAAPVT NKMQHSLHSG GGGGGIGPRS SQQHSSFKRP TGTPVMGNRG LETRQSKRSQ
LHSQAPGPGP PSTQPHHGNN GVVTSAHPIT VGALDVMNVK QVVNRYGTLP KGARIGAYLD
SLEDSSEAAP ALPATAPSLP PANGHATPPA ARLNPKASPI PPQQMIRSNS SGGVTMQNNA
AASLNKLQRH RTTTEGTMMT FSSFRAGGSS SSPKRSASGV ASGVQPALAN LEFPPPPLDL
PPPPEEFEGG PPPPPPAPES AVQAIQQHLH AQLPNNGNIS NGNGTNNNDS SHNDVSNIAP
SVEEASSRFG VSLRKREPST DSCSSLGSPP EDLKEKLITE IKAAGKDTAP ASHLANGSGI
AVVDPVSLLV TELAESMNLP KPPPQQQQKL TNGNSTGSGF KAQLKKVEPK KMSAPMPKAE
PANTIIDFKA HLRRVDKEKE PATPAPAPAT VAVANNANCN TTGTLNRKED GSKKFSQAMQ
KTEIKIDVTN SNVEADAGAA GEGDLGKRRS TDDEEQSHTE GLGSGGQGSA DMTQSLYEQK
PQIQQKPAVP HKPTKLTIYA TPIAKLTEPA SSASSTQISR ESILELVGLL EGSLKHPVNA
IAGSQWLQLS DKLNILHNSC VIFAENGAMP PHSKFQFREL VTRVEAQSQH LRSAGSKNVQ
DNERLVAEVG QSLRQISNAL NR
//