ABL_MLVAB
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 03-AUG-2022, entry version 131.
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;
OC unclassified 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}.
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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 CDD; cd09935; SH2_ABL; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR033221; ABL1.
DR InterPro; IPR035837; ABL_SH2.
DR InterPro; IPR015015; F-actin-binding.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418:SF162; PTHR24418:SF162; 1.
DR Pfam; PF08919; F_actin_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00808; FABD; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
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
