ID ABL_MLVAB Reviewed; 746 AA. AC P00521; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=Tyrosine-protein kinase transforming protein Abl; DE EC=2.7.10.2; DE AltName: Full=V-abl; GN Name=ABL; OS Abelson murine leukemia virus. OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus. OX NCBI_TaxID=11788; OH NCBI_TaxID=10090; Mus musculus (Mouse). RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=6304726; DOI=10.1073/pnas.80.12.3623; RA Reddy E.P., Smith M.J., Srinivasan A.; RT "Nucleotide sequence of Abelson murine leukemia virus genome: structural RT similarity of its transforming gene product to other onc gene products with RT tyrosine-specific kinase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 80:3623-3627(1983). RN [2] RP ERRATUM OF PUBMED:6304726, AND SEQUENCE REVISION TO 588-746. RA Reddy E.P., Smith M.J., Srinivasan A.; RL Proc. Natl. Acad. Sci. U.S.A. 80:7372-7372(1983). RN [3] RP NUCLEOTIDE SEQUENCE OF 233-327. RX PubMed=6191223; DOI=10.1038/304167a0; RA Groffen J., Heisterkamp N., Reynolds F.H. Jr., Stephenson J.R.; RT "Homology between phosphotyrosine acceptor site of human c-abl and viral RT oncogene products."; RL Nature 304:167-169(1983). 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 -!- MISCELLANEOUS: This protein is synthesized as a Gag-Abl polyprotein. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. ABL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; V01541; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; K00010; AAA46470.1; -; Genomic_RNA. DR BMRB; P00521; -. DR SMR; P00521; -. DR IntAct; P00521; 1. DR BindingDB; P00521; -. DR ChEMBL; CHEMBL5166; -. DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid. DR DrugBank; DB05489; ACA 125. DR DrugBank; DB03878; N-[4-Methyl-3-[[4-(3-Pyridinyl)-2-Pyrimidinyl]Amino]Phenyl]-3-Pyridinecarboxamide. DR DrugBank; DB02567; PD173955. DR BRENDA; 2.7.10.2; 1. DR SABIO-RK; P00521; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0023052; P:signaling; IEA:UniProt. DR CDD; cd05052; PTKc_Abl; 1. DR CDD; cd09935; SH2_ABL; 1. DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1. DR Gene3D; 3.30.505.10; SH2 domain; 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; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24418:SF438; TYROSINE-PROTEIN KINASE ABL1; 1. DR Pfam; PF08919; F_actin_bind; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF00017; SH2; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00808; FABD; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 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. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Oncogene; SH2 domain; Transferase; KW Tyrosine-protein kinase. FT CHAIN 1..746 FT /note="Tyrosine-protein kinase transforming protein Abl" FT /id="PRO_0000088057" FT DOMAIN 13..103 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 128..379 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 389..613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 267..291 FT /note="Kinase activation loop" FT /evidence="ECO:0000250" FT COMPBIAS 437..456 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 486..511 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 569..601 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 249 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 134..142 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 157 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 202..208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 746 AA; 81872 MW; B9072FFF55FE9257 CRC64; YITPVNSLEK HSWYHGPVSR NAAEYLLSSG INGSFLVRES ESSPGQRSIS LRYEGRVYHY RINTASDGKL YVSSESRFNT LAELVHHHST VADGLITTLH YPAPKRNKPT IYGVSPNYDK WEMERTDITM KHKLGGGQYG EVYEGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTREPPFYII TEFMTYGNLL DYLRECNRQE VSAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN HLVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN KFSIKSDVWA FGVLLWEIAT YGMSPYPGID LSQVYELLEK DYRMERPEGC PEKVYELMRA CWQWNPSDRP SFAEIHQAFE TMFQESSISD EVEKELGKRG TRGGAGSMLQ APELPTKTRT CRRAAEQKAS PPSLTPKLLR RQVTASPSSG LSHKKEATKG SASGMGTPAT AEPAPPSNKV GLSKASSEEM RVRRHKHSSE SPGRDKGRLA KLKPAPPPPP ACTGKAGKPA QSPSQEAGEA GGPTKTKCTS LAMDAVNTDP TKAGPPGEGL RKPVPPSVPK PQSTAKPPGT PTSPVSTPST APAPSPLAGD QQPSSAAFIP LISTRVSLRK TRQPPERIAS GTITKGVVLD STEALCLAIS RNSEQMASHS AVLEAGKNLY TFCVSYVDSI QQMRNKFAFR EAINKLESNL RELQICPATA SSGPAATQDF SKLLSSVKEI SDIVRR //