ID ABL1_HUMAN Reviewed; 1130 AA. AC P00519; A3KFJ3; Q13869; Q13870; Q16133; Q17R61; Q45F09; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 4. DT 27-MAR-2024, entry version 284. DE RecName: Full=Tyrosine-protein kinase ABL1; DE EC=2.7.10.2 {ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:28428613}; DE AltName: Full=Abelson murine leukemia viral oncogene homolog 1; DE AltName: Full=Abelson tyrosine-protein kinase 1; DE AltName: Full=Proto-oncogene c-Abl; DE AltName: Full=p150; GN Name=ABL1; Synonyms=ABL, JTK7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA), ALTERNATIVE SPLICING, CHROMOSOMAL RP TRANSLOCATION WITH BRC, AND VARIANT PRO-140. RX PubMed=3021337; DOI=10.1016/0092-8674(86)90450-2; RA Shtivelman E., Lifshitz B., Gale R.P., Roe B.A., Canaani E.; RT "Alternative splicing of RNAs transcribed from the human abl gene and from RT the bcr-abl fused gene."; RL Cell 47:277-284(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA). RC TISSUE=Fibroblast; RX PubMed=2687768; RA Fainstein E., Einat M., Gokkel E., Marcelle C., Croce C.M., Gale R.P., RA Canaani E.; RT "Nucleotide sequence analysis of human abl and bcr-abl cDNAs."; RL Oncogene 4:1477-1481(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS IA AND IB). RC TISSUE=Lung; RX PubMed=7665185; DOI=10.1006/geno.1995.1008; RA Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D., RA Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y., RA McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G., RA Heisterkamp N., Groffen J., Roe B.A.; RT "Sequence and analysis of the human ABL gene, the BCR gene, and regions RT involved in the Philadelphia chromosomal translocation."; RL Genomics 27:67-82(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-706; PRO-852; SER-900 RP AND LEU-972. RG NIEHS SNPs program; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IB). RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-40, AND SUBCELLULAR COMPONENT. RX PubMed=2825022; DOI=10.1038/330386a0; RA Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P., Dreazen O., RA Smith S.D., Croce C.M.; RT "A new fused transcript in Philadelphia chromosome positive acute RT lymphocytic leukaemia."; RL Nature 330:386-388(1987). RN [9] RP NUCLEOTIDE SEQUENCE OF 360-426. 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). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-845. RX PubMed=7545908; RA Inokuchi K., Futaki M., Dan K., Nomura T.; RT "Sequence analysis of the mutation at codon 834 and the sequence variation RT of codon 837 of c-abl gene."; RL Leukemia 8:343-344(1994). RN [11] RP MYRISTOYLATION AT GLY-2 (ISOFORM IB). RX PubMed=2542016; DOI=10.1002/j.1460-2075.1989.tb03397.x; RA Jackson P., Baltimore D.; RT "N-terminal mutations activate the leukemogenic potential of the RT myristoylated form of c-abl."; RL EMBO J. 8:449-456(1989). RN [12] RP DOMAIN, AND DNA-BINDING. RX PubMed=2183353; DOI=10.1126/science.2183353; RA Kipreos E.T., Wang J.Y.; RT "Differential phosphorylation of c-Abl in cell cycle determined by cdc2 RT kinase and phosphatase activity."; RL Science 248:217-220(1990). RN [13] RP FUNCTION. RX PubMed=9037071; DOI=10.1073/pnas.94.4.1437; RA Yuan Z.M., Huang Y., Ishiko T., Kharbanda S., Weichselbaum R., Kufe D.; RT "Regulation of DNA damage-induced apoptosis by the c-Abl tyrosine kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 94:1437-1440(1997). RN [14] RP INTERACTION WITH RIN1, AND FUNCTION. RX PubMed=9144171; DOI=10.1073/pnas.94.10.4954; RA Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W., Herschman H., RA Witte O., Colicelli J.; RT "Protein binding and signaling properties of RIN1 suggest a unique effector RT function."; RL Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997). RN [15] RP FUNCTION, AND INTERACTION WITH RAD51. RX PubMed=9461559; DOI=10.1074/jbc.273.7.3799; RA Yuan Z.M., Huang Y., Ishiko T., Nakada S., Utsugisawa T., Kharbanda S., RA Wang R., Sung P., Shinohara A., Weichselbaum R., Kufe D.; RT "Regulation of Rad51 function by c-Abl in response to DNA damage."; RL J. Biol. Chem. 273:3799-3802(1998). RN [16] RP INTERACTION WITH INPPL1. RX PubMed=10194451; RA Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., Geromanos S., RA Kavanaugh W.M., Tempst P., Clarkson B.; RT "A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5- RT phosphatase (SHIP2) is constitutively tyrosine phosphorylated and RT associated with src homologous and collagen gene (SHC) in chronic RT myelogenous leukemia progenitor cells."; RL Blood 93:2707-2720(1999). RN [17] RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH TP73. RX PubMed=10391250; DOI=10.1038/21697; RA Agami R., Blandino G., Oren M., Shaul Y.; RT "Interaction of c-Abl and p73alpha and their collaboration to induce RT apoptosis."; RL Nature 399:809-813(1999). RN [18] RP DNA-BINDING. RX PubMed=10325413; DOI=10.1093/nar/27.11.2265; RA David-Cordonnier M.H., Payet D., D'Halluin J.C., Waring M.J., Travers A.A., RA Bailly C.; RT "The DNA-binding domain of human c-Abl tyrosine kinase promotes the RT interaction of a HMG chromosomal protein with DNA."; RL Nucleic Acids Res. 27:2265-2270(1999). RN [19] RP REVIEW ON FUNCTION. RX PubMed=11114745; DOI=10.1038/sj.onc.1203878; RA Wang J.Y.; RT "Regulation of cell death by the Abl tyrosine kinase."; RL Oncogene 19:5643-5650(2000). RN [20] RP INTERACTION WITH SORBS1. RX PubMed=11374898; DOI=10.1006/geno.2001.6541; RA Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y., RA Chuang L.-M.; RT "Cloning, mapping, and characterization of the human sorbin and SH3 domain RT containing 1 (SORBS1) gene: a protein associated with c-Abl during insulin RT signaling in the hepatoma cell line Hep3B."; RL Genomics 74:12-20(2001). RN [21] RP FUNCTION, AND INTERACTION WITH RAD52. RX PubMed=12379650; DOI=10.1074/jbc.m208151200; RA Kitao H., Yuan Z.M.; RT "Regulation of ionizing radiation-induced Rad52 nuclear foci formation by RT c-Abl-mediated phosphorylation."; RL J. Biol. Chem. 277:48944-48948(2002). RN [22] RP FUNCTION, AND INTERACTION WITH RAD9A. RX PubMed=11971963; DOI=10.1128/mcb.22.10.3292-3300.2002; RA Yoshida K., Komatsu K., Wang H.-G., Kufe D.; RT "c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in RT response to DNA damage."; RL Mol. Cell. Biol. 22:3292-3300(2002). RN [23] RP UBIQUITINATION. RX PubMed=12475393; DOI=10.1042/bj20021539; RA Soubeyran P., Barac A., Szymkiewicz I., Dikic I.; RT "Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl."; RL Biochem. J. 370:29-34(2003). RN [24] RP FUNCTION. RX PubMed=12531427; DOI=10.1016/s0898-6568(02)00090-6; RA Sanguinetti A.R., Mastick C.C.; RT "c-Abl is required for oxidative stress-induced phosphorylation of RT caveolin-1 on tyrosine 14."; RL Cell. Signal. 15:289-298(2003). RN [25] RP FUNCTION. RX PubMed=12672821; DOI=10.1074/jbc.m301447200; RA Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H., RA Shishido T.; RT "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian RT enabled (Mena) by c-Abl kinase."; RL J. Biol. Chem. 278:21685-21692(2003). RN [26] RP REVIEW ON FUNCTION. RX PubMed=12775773; DOI=10.1242/jcs.00622; RA Woodring P.J., Hunter T., Wang J.Y.; RT "Regulation of F-actin-dependent processes by the Abl family of tyrosine RT kinases."; RL J. Cell Sci. 116:2613-2626(2003). RN [27] RP INTERACTION WITH BCR. RX PubMed=15302586; DOI=10.1016/j.yexcr.2004.05.010; RA Laurent C.E., Smithgall T.E.; RT "The c-Fes tyrosine kinase cooperates with the breakpoint cluster region RT protein (Bcr) to induce neurite extension in a Rac- and Cdc42-dependent RT manner."; RL Exp. Cell Res. 299:188-198(2004). RN [28] RP FUNCTION. RX PubMed=15556646; DOI=10.1016/j.febslet.2004.10.054; RA Grossmann A.H., Kolibaba K.S., Willis S.G., Corbin A.S., Langdon W.S., RA Deininger M.W., Druker B.J.; RT "Catalytic domains of tyrosine kinases determine the phosphorylation sites RT within c-Cbl."; RL FEBS Lett. 577:555-562(2004). RN [29] RP FUNCTION. RX PubMed=15031292; DOI=10.1074/jbc.m311479200; RA Perkinton M.S., Standen C.L., Lau K.F., Kesavapany S., Byers H.L., Ward M., RA McLoughlin D.M., Miller C.C.; RT "The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to RT stimulate Fe65/amyloid precursor protein nuclear signaling."; RL J. Biol. Chem. 279:22084-22091(2004). RN [30] RP REVIEW ON FUNCTION. RX PubMed=15686624; DOI=10.1038/sj.cr.7290261; RA Shaul Y., Ben-Yehoyada M.; RT "Role of c-Abl in the DNA damage stress response."; RL Cell Res. 15:33-35(2005). RN [31] RP FUNCTION. RX PubMed=15886098; DOI=10.1016/j.cub.2005.03.049; RA Hu H., Bliss J.M., Wang Y., Colicelli J.; RT "RIN1 is an ABL tyrosine kinase activator and a regulator of epithelial- RT cell adhesion and migration."; RL Curr. Biol. 15:815-823(2005). RN [32] RP FUNCTION, AND INTERACTION WITH CASP9. RX PubMed=15657060; DOI=10.1074/jbc.m413787200; RA Raina D., Pandey P., Ahmad R., Bharti A., Ren J., Kharbanda S., RA Weichselbaum R., Kufe D.; RT "c-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic RT response to DNA damage."; RL J. Biol. Chem. 280:11147-11151(2005). RN [33] RP INTERACTION WITH YWHAB; YWHAE; YWHAG; YWHAH; SFN AND YWHAZ, PHOSPHORYLATION RP AT THR-735, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF THR-735. RX PubMed=15696159; DOI=10.1038/ncb1228; RA Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.; RT "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c- RT Abl in the apoptotic response to DNA damage."; RL Nat. Cell Biol. 7:278-285(2005). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [35] RP ACETYLATION AT LYS-711, AND SUBCELLULAR LOCATION. RX PubMed=16648821; DOI=10.1038/sj.embor.7400700; RA di Bari M.G., Ciuffini L., Mingardi M., Testi R., Soddu S., Barila D.; RT "c-Abl acetylation by histone acetyltransferases regulates its nuclear- RT cytoplasmic localization."; RL EMBO Rep. 7:727-733(2006). RN [36] RP PHOSPHORYLATION AT TYR-70; TYR-115; TYR-128; TYR-139; TYR-172; TYR-185 RP TYR-215; TYR-226 AND TYR-393, INTERACTION WITH HCK; LYN AND FYN, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16912036; DOI=10.1074/jbc.m605902200; RA Meyn M.A. III, Wilson M.B., Abdi F.A., Fahey N., Schiavone A.P., Wu J., RA Hochrein J.M., Engen J.R., Smithgall T.E.; RT "Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate RT Bcr-Abl transforming activity."; RL J. Biol. Chem. 281:30907-30916(2006). RN [37] RP FUNCTION. RX PubMed=16943190; DOI=10.1074/jbc.m603126200; RA Tanos B., Pendergast A.M.; RT "Abl tyrosine kinase regulates endocytosis of the epidermal growth factor RT receptor."; RL J. Biol. Chem. 281:32714-32723(2006). RN [38] RP FUNCTION, AND INTERACTION WITH PSMA7. RX PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007; RA Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., Cao C.; RT "Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit RT PSMA7 regulates proteasome degradation."; RL Mol. Cell 22:317-327(2006). RN [39] RP FUNCTION. RX PubMed=17306540; DOI=10.1016/j.cub.2007.01.057; RA Boyle S.N., Michaud G.A., Schweitzer B., Predki P.F., Koleske A.J.; RT "A critical role for cortactin phosphorylation by Abl-family kinases in RT PDGF-induced dorsal-wave formation."; RL Curr. Biol. 17:445-451(2007). RN [40] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASF3. RX PubMed=17623672; DOI=10.1074/jbc.m701484200; RA Sossey-Alaoui K., Li X., Cowell J.K.; RT "c-Abl-mediated phosphorylation of WAVE3 is required for lamellipodia RT formation and cell migration."; RL J. Biol. Chem. 282:26257-26265(2007). RN [41] RP PHOSPHORYLATION AT SER-618 AND SER-619, AND INTERACTION WITH ABI2 AND CRK. RX PubMed=18161990; DOI=10.1021/bi701533j; RA Jung J.H., Pendergast A.M., Zipfel P.A., Traugh J.A.; RT "Phosphorylation of c-Abl by protein kinase Pak2 regulates differential RT binding of ABI2 and CRK."; RL Biochemistry 47:1094-1104(2008). RN [42] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=18328268; DOI=10.1016/j.bbamcr.2008.01.028; RA Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X., RA Debnath A.K., Cowburn D., Kotula L.; RT "Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by RT phosphopeptides derived from Abi1/Hssh3bp1."; RL Biochim. Biophys. Acta 1783:737-747(2008). RN [43] RP FUNCTION. RX PubMed=18945674; DOI=10.1074/jbc.m804543200; RA Yogalingam G., Pendergast A.M.; RT "Abl kinases regulate autophagy by promoting the trafficking and function RT of lysosomal components."; RL J. Biol. Chem. 283:35941-35953(2008). RN [44] RP PHOSPHORYLATION AT TYR-70, AND INTERACTION WITH ABI1. RX PubMed=18775435; DOI=10.1016/j.jmb.2008.08.040; RA Chen S., O'Reilly L.P., Smithgall T.E., Engen J.R.; RT "Tyrosine phosphorylation in the SH3 domain disrupts negative regulatory RT interactions within the c-Abl kinase core."; RL J. Mol. Biol. 383:414-423(2008). RN [45] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-569; SER-659; RP THR-814; THR-844 AND SER-977, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [46] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; THR-852 AND SER-917, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [47] RP REVIEW ON FUNCTION. RX PubMed=18182299; DOI=10.1016/j.tibs.2007.10.006; RA Backert S., Feller S.M., Wessler S.; RT "Emerging roles of Abl family tyrosine kinases in microbial pathogenesis."; RL Trends Biochem. Sci. 33:80-90(2008). RN [48] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [49] RP FUNCTION. RX PubMed=19891780; DOI=10.1186/1471-2121-10-80; RA Fernow I., Tomasovic A., Siehoff-Icking A., Tikkanen R.; RT "Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src RT kinases."; RL BMC Cell Biol. 10:80-80(2009). RN [50] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [51] RP IDENTIFICATION IN A COMPLEX WITH UNC119; ABL2 AND CRK. RX PubMed=19381274; DOI=10.1371/journal.pone.0005211; RA Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.; RT "Unc119 protects from Shigella infection by inhibiting the Abl family RT kinases."; RL PLoS ONE 4:E5211-E5211(2009). RN [52] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-569, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [53] RP FUNCTION. RX PubMed=20417104; DOI=10.1016/j.cub.2010.03.048; RA Michael M., Vehlow A., Navarro C., Krause M.; RT "c-Abl, Lamellipodin, and Ena/VASP proteins cooperate in dorsal ruffling of RT fibroblasts and axonal morphogenesis."; RL Curr. Biol. 20:783-791(2010). RN [54] RP INTERACTION WITH MYLK AND CTTN. RX PubMed=20861316; DOI=10.1091/mbc.e09-10-0876; RA Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., RA Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., RA Imam S.Z., Garcia J.G.N.; RT "Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to RT regulate endothelial barrier function."; RL Mol. Biol. Cell 21:4042-4056(2010). RN [55] RP REVIEW ON FUNCTION, AND DOMAIN. RX PubMed=20841568; DOI=10.1126/scisignal.3139re6; RA Colicelli J.; RT "ABL tyrosine kinases: evolution of function, regulation, and RT specificity."; RL Sci. Signal. 3:RE6-RE6(2010). RN [56] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [57] RP INTERACTION WITH STX17. RX PubMed=23006999; DOI=10.1016/j.bbamcr.2012.09.003; RA Muppirala M., Gupta V., Swarup G.; RT "Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: Implications for RT membrane trafficking in the early secretory pathway."; RL Biochim. Biophys. Acta 1823:2109-2119(2012). RN [58] RP FUNCTION, AND INTERACTION WITH NEDD9. RX PubMed=22810897; DOI=10.1126/scisignal.2002632; RA Gu J.J., Lavau C.P., Pugacheva E., Soderblom E.J., Moseley M.A., RA Pendergast A.M.; RT "Abl family kinases modulate T cell-mediated inflammation and chemokine- RT induced migration through the adaptor HEF1 and the GTPase Rap1."; RL Sci. Signal. 5:ra51-ra51(2012). RN [59] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253; TYR-257; TYR-413; RP SER-559; SER-569; SER-620; SER-683; SER-718; THR-751; THR-781; THR-823; RP THR-844; THR-852; SER-855 AND SER-917, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [60] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [61] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=28428613; DOI=10.1038/s41598-017-00800-w; RA Cobbaut M., Derua R., Doeppler H., Lou H.J., Vandoninck S., Storz P., RA Turk B.E., Seufferlein T., Waelkens E., Janssens V., Van Lint J.; RT "Differential regulation of PKD isoforms in oxidative stress conditions RT through phosphorylation of a conserved Tyr in the P+1 loop."; RL Sci. Rep. 7:887-887(2017). RN [62] RP STRUCTURE BY NMR OF SH2 DOMAIN. RX PubMed=1505033; DOI=10.1016/0092-8674(92)90437-h; RA Overduin M., Rios C.B., Mayer B.J., Baltimore D., Cowburn D.; RT "Three-dimensional solution structure of the src homology 2 domain of c- RT abl."; RL Cell 70:697-704(1992). RN [63] RP STRUCTURE BY NMR OF SH2 DOMAIN. RX PubMed=1281542; DOI=10.1073/pnas.89.24.11673; RA Overduin M., Mayer B.J., Rios C.B., Baltimore D., Cowburn D.; RT "Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR RT spectroscopy in solution."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11673-11677(1992). RN [64] RP 3D-STRUCTURE MODELING OF SH3 DOMAIN. RX PubMed=7892170; DOI=10.1002/prot.340200302; RA Pisabarro M.T., Ortiz A.R., Serrano L., Wade R.C.; RT "Homology modeling of the Abl-SH3 domain."; RL Proteins 20:203-215(1994). RN [65] RP STRUCTURE BY NMR OF SH3 DOMAIN. RX PubMed=8590002; DOI=10.1016/s0969-2126(01)00243-x; RA Gosser Y.Q., Zheng J., Overduin M., Mayer B.J., Cowburn D.; RT "The solution structure of Abl SH3, and its relationship to SH2 in the RT SH(32) construct."; RL Structure 3:1075-1086(1995). RN [66] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 64-121. RX PubMed=9698566; DOI=10.1006/jmbi.1998.1932; RA Pisabarro M.T., Serrano L., Wilmanns M.; RT "Crystal structure of the abl-SH3 domain complexed with a designed high- RT affinity peptide ligand: implications for SH3-ligand interactions."; RL J. Mol. Biol. 281:513-521(1998). RN [67] RP STRUCTURE BY NMR OF 62-122 IN COMPLEX WITH CRK. RX PubMed=12384576; DOI=10.1073/pnas.212518799; RA Donaldson L.W., Gish G., Pawson T., Kay L.E., Forman-Kay J.D.; RT "Structure of a regulatory complex involving the Abl SH3 domain, the Crk RT SH2 domain, and a Crk-derived phosphopeptide."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14053-14058(2002). RN [68] RP X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS) OF 27-512, MYRISTOYLATION AT GLY-2 RP (ISOFORM IB), ACTIVITY REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12654251; DOI=10.1016/s0092-8674(03)00194-6; RA Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D., Bornmann W., RA Clarkson B., Superti-Furga G., Kuriyan J.; RT "Structural basis for the autoinhibition of c-Abl tyrosine kinase."; RL Cell 112:859-871(2003). RN [69] RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 229-513 OF MUTANT PRO-396 IN RP COMPLEX WITH INHIBITOR VX-680, FUNCTION, AND ACTIVITY REGULATION. RX PubMed=16424036; DOI=10.1158/0008-5472.can-05-2788; RA Young M.A., Shah N.P., Chao L.H., Seeliger M., Milanov Z.V., RA Biggs W.H. III, Treiber D.K., Patel H.K., Zarrinkar P.P., Lockhart D.J., RA Sawyers C.L., Kuriyan J.; RT "Structure of the kinase domain of an imatinib-resistant Abl mutant in RT complex with the Aurora kinase inhibitor VX-680."; RL Cancer Res. 66:1007-1014(2006). RN [70] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 38-512, IDENTIFICATION BY MASS RP SPECTROMETRY, MYRISTOYLATION AT GLY-2 (ISOFORM IB), PHOSPHORYLATION AT RP SER-50, AUTOINHIBITORY MECHANISM, AND ACTIVITY REGULATION. RX PubMed=16543148; DOI=10.1016/j.molcel.2006.01.035; RA Nagar B., Hantschel O., Seeliger M., Davies J.M., Weis W.I., RA Superti-Furga G., Kuriyan J.; RT "Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl RT tyrosine kinase."; RL Mol. Cell 21:787-798(2006). RN [71] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 229-512 IN COMPLEXES WITH RP ATP-PEPTIDE CONJUGATE, AND CONFORMATION CHANGES DURING ACTIVATION. RX PubMed=16640460; DOI=10.1371/journal.pbio.0040144; RA Levinson N.M., Kuchment O., Shen K., Young M.A., Koldobskiy M., Karplus M., RA Cole P.A., Kuriyan J.; RT "A Src-like inactive conformation in the abl tyrosine kinase domain."; RL PLoS Biol. 4:E144-E144(2006). RN [72] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 229-500 IN COMPLEXES WITH IMATINIB RP AND WITH THE INHIBITORS NVP-AEG082; NVP-AFN941; NVP-AFG210 AND PD180970. RX PubMed=17164530; DOI=10.1107/s0907444906047287; RA Cowan-Jacob S.W., Fendrich G., Floersheimer A., Furet P., Liebetanz J., RA Rummel G., Rheinberger P., Centeleghe M., Fabbro D., Manley P.W.; RT "Structural biology contributions to the discovery of drugs to treat RT chronic myelogenous leukaemia."; RL Acta Crystallogr. D 63:80-93(2007). RN [73] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 64-121 OF MUTANT ALA-114 IN RP COMPLEX WITH PROLINE-RICH PEPTIDE. RX PubMed=17452790; DOI=10.1107/s0907444907011109; RA Camara-Artigas A., Palencia A., Martinez J.C., Luque I., Gavira J.A., RA Garcia-Ruiz J.M.; RT "Crystallization by capillary counter-diffusion and structure determination RT of the N114A mutant of the SH3 domain of Abl tyrosine kinase complexed with RT a high-affinity peptide ligand."; RL Acta Crystallogr. D 63:646-652(2007). RN [74] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 60-121 IN COMPLEX WITH RP PROLINE-RICH PEPTIDE P41. RX PubMed=19906645; DOI=10.1074/jbc.m109.048033; RA Palencia A., Camara-Artigas A., Pisabarro M.T., Martinez J.C., Luque I.; RT "Role of interfacial water molecules in proline-rich ligand recognition by RT the Src homology 3 domain of Abl."; RL J. Biol. Chem. 285:2823-2833(2010). RN [75] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 121-232 IN COMPLEX WITH ANTIBODY RP MIMIC HA4, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20357770; DOI=10.1038/nsmb.1793; RA Wojcik J., Hantschel O., Grebien F., Kaupe I., Bennett K.L., Barkinge J., RA Jones R.B., Koide A., Superti-Furga G., Koide S.; RT "A potent and highly specific FN3 monobody inhibitor of the Abl SH2 RT domain."; RL Nat. Struct. Mol. Biol. 17:519-527(2010). RN [76] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH NUP214. RX PubMed=15361874; DOI=10.1038/ng1425; RA Graux C., Cools J., Melotte C., Quentmeier H., Ferrando A., Levine R., RA Vermeesch J.R., Stul M., Dutta B., Boeckx N., Bosly A., Heimann P., RA Uyttebroeck A., Mentens N., Somers R., MacLeod R.A., Drexler H.G., RA Look A.T., Gilliland D.G., Michaux L., Vandenberghe P., Wlodarska I., RA Marynen P., Hagemeijer A.; RT "Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute RT lymphoblastic leukemia."; RL Nat. Genet. 36:1084-1089(2004). RN [77] RP VARIANTS GLY-47; LYS-166; VAL-706; LEU-810 AND LEU-972. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [78] RP INVOLVEMENT IN CHDSKM, VARIANTS CHDSKM CYS-226 AND THR-337, AND RP CHARACTERIZATION OF VARIANTS CHDSKM CYS-226 AND THR-337. RX PubMed=28288113; DOI=10.1038/ng.3815; RA Wang X., Charng W.L., Chen C.A., Rosenfeld J.A., Al Shamsi A., RA Al-Gazali L., McGuire M., Mew N.A., Arnold G.L., Qu C., Ding Y., RA Muzny D.M., Gibbs R.A., Eng C.M., Walkiewicz M., Xia F., Plon S.E., RA Lupski J.R., Schaaf C.P., Yang Y.; RT "Germline mutations in ABL1 cause an autosomal dominant syndrome RT characterized by congenital heart defects and skeletal malformations."; RL Nat. Genet. 49:613-617(2017). CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in CC many key processes linked to cell growth and survival such as CC cytoskeleton remodeling in response to extracellular stimuli, cell CC motility and adhesion, receptor endocytosis, autophagy, DNA damage CC response and apoptosis. Coordinates actin remodeling through tyrosine CC phosphorylation of proteins controlling cytoskeleton dynamics like CC WASF3 (involved in branch formation); ANXA1 (involved in membrane CC anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); CC or MAPT and PXN (microtubule-binding proteins). Phosphorylation of CC WASF3 is critical for the stimulation of lamellipodia formation and CC cell migration. Involved in the regulation of cell adhesion and CC motility through phosphorylation of key regulators of these processes CC such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9 (PubMed:22810897). CC Phosphorylates multiple receptor tyrosine kinases and more particularly CC promotes endocytosis of EGFR, facilitates the formation of CC neuromuscular synapses through MUSK, inhibits PDGFRB-mediated CC chemotaxis and modulates the endocytosis of activated B-cell receptor CC complexes. Other substrates which are involved in endocytosis CC regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates CC the CBL family of ubiquitin ligases that drive receptor down-regulation CC and actin remodeling. Phosphorylation of CBL leads to increased EGFR CC stability. Involved in late-stage autophagy by regulating positively CC the trafficking and function of lysosomal components. ABL1 targets to CC mitochondria in response to oxidative stress and thereby mediates CC mitochondrial dysfunction and cell death. In response to oxidative CC stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' CC (PubMed:28428613). ABL1 is also translocated in the nucleus where it CC has DNA-binding activity and is involved in DNA-damage response and CC apoptosis. Many substrates are known mediators of DNA repair: DDB1, CC DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the CC proapoptotic pathway when the DNA damage is too severe to be repaired. CC Phosphorylates TP73, a primary regulator for this type of damage- CC induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and CC regulates its processing in the apoptotic response to DNA damage. CC Phosphorylates PSMA7 that leads to an inhibition of proteasomal CC activity and cell cycle transition blocks. ABL1 acts also as a CC regulator of multiple pathological signaling cascades during infection. CC Several known tyrosine-phosphorylated microbial proteins have been CC identified as ABL1 substrates. This is the case of A36R of Vaccinia CC virus, Tir (translocated intimin receptor) of pathogenic E.coli and CC possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, CC or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. CC Pathogens can highjack ABL1 kinase signaling to reorganize the host CC actin cytoskeleton for multiple purposes, like facilitating CC intracellular movement and host cell exit. Finally, functions as its CC own regulator through autocatalytic activity as well as through CC phosphorylation of its inhibitor, ABI1. Regulates T-cell CC differentiation in a TBX21-dependent manner (By similarity). Positively CC regulates chemokine-mediated T-cell migration, polarization, and homing CC to lymph nodes and immune-challenged tissues, potentially via CC activation of NEDD9/HEF1 and RAP1 (By similarity). Phosphorylates TBX21 CC on tyrosine residues leading to an enhancement of its transcriptional CC activator activity (By similarity). {ECO:0000250|UniProtKB:P00520, CC ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:11971963, CC ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:12531427, CC ECO:0000269|PubMed:12672821, ECO:0000269|PubMed:15031292, CC ECO:0000269|PubMed:15556646, ECO:0000269|PubMed:15657060, CC ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16424036, CC ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:16943190, CC ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:17623672, CC ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:18945674, CC ECO:0000269|PubMed:19891780, ECO:0000269|PubMed:20357770, CC ECO:0000269|PubMed:20417104, ECO:0000269|PubMed:22810897, CC ECO:0000269|PubMed:28428613, ECO:0000269|PubMed:9037071, CC ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9461559}. 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:20357770, ECO:0000269|PubMed:28428613}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P00520}; CC -!- ACTIVITY REGULATION: Stabilized in the inactive form by an association CC between the SH3 domain and the SH2-TK linker region, interactions of CC the N-terminal cap, and contributions from an N-terminal myristoyl CC group and phospholipids. Activated by autophosphorylation as well as by CC SRC-family kinase-mediated phosphorylation. Activated by RIN1 binding CC to the SH2 and SH3 domains. Also stimulated by cell death inducers and CC DNA-damage. Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly CC abundant phosphoinositide known to regulate cytoskeletal and membrane CC proteins, inhibits also the tyrosine kinase activity (By similarity). CC Activated by 5-(1,3-diaryl-1H-pyrazol-4-yl)hydantoin, 5-[3-(4- CC fluorophenyl)-1-phenyl-1H-pyrazol-4-yl]-2,4-imidazolidinedione (DPH) CC (PubMed:28428613). Inhibited by ABI1, whose activity is controlled by CC ABL1 itself through tyrosine phosphorylation. Also inhibited by CC imatinib mesylate (Gleevec) which is used for the treatment of chronic CC myeloid leukemia (CML), and by VX-680, an inhibitor that acts also on CC imatinib-resistant mutants (PubMed:28428613). {ECO:0000250, CC ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:12654251, CC ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16543148, CC ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:28428613}. CC -!- SUBUNIT: Interacts with SORBS1 following insulin stimulation. Found in CC a trimolecular complex containing CDK5 and CABLES1. Interacts with CC CABLES1 and PSTPIP1. Interacts with ZDHHC16, ITGB1 and HCK (By CC similarity). Interacts with STX17; probably phosphorylates STX17. CC Interacts with INPPL1/SHIP2. Interacts with the 14-3-3 proteins, YWHAB, CC YWHAE, YWHAG, YWHAH, SFN and YWHAZ; the interaction with 14-3-3 CC proteins requires phosphorylation on Thr-735 and, sequesters ABL1 into CC the cytoplasm. Interacts with ABI1, ABI2, BCR, CRK, FGR, FYN, HCK, LYN, CC PSMA7 RAD9A, RAD51, RAD52, TP73 and WASF3. A complex made of ABL1, CTTN CC and MYLK regulates cortical actin-based cytoskeletal rearrangement CC critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell CC (EC) barrier enhancement. Interacts (via SH3 domain) with CASP9; the CC interaction is direct and increases in the response of cells to CC genotoxic stress and ABL1/c-Abl activation. Found in a complex with CC ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK CC phosphorylation by ABL kinases. Interacts with TBX21 (By similarity). CC Interacts with NEDD9/HEF1; interaction is induced by CXCL12 promotion CC of ABL-mediated phosphorylation of NEDD9/HEF1 (PubMed:22810897). CC {ECO:0000250|UniProtKB:P00520, ECO:0000269|PubMed:10194451, CC ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:11374898, CC ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12379650, CC ECO:0000269|PubMed:12384576, ECO:0000269|PubMed:15302586, CC ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:15696159, CC ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16678104, CC ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:17452790, CC ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:18161990, CC ECO:0000269|PubMed:18775435, ECO:0000269|PubMed:19381274, CC ECO:0000269|PubMed:19906645, ECO:0000269|PubMed:20357770, CC ECO:0000269|PubMed:20861316, ECO:0000269|PubMed:22810897, CC ECO:0000269|PubMed:23006999, ECO:0000269|PubMed:9144171, CC ECO:0000269|PubMed:9461559}. CC -!- INTERACTION: CC P00519; Q8IZP0: ABI1; NbExp=11; IntAct=EBI-375543, EBI-375446; CC P00519; Q9NYB9: ABI2; NbExp=2; IntAct=EBI-375543, EBI-743598; CC P00519; O14672: ADAM10; NbExp=2; IntAct=EBI-375543, EBI-1536151; CC P00519; P10275: AR; NbExp=2; IntAct=EBI-375543, EBI-608057; CC P00519; Q13315: ATM; NbExp=4; IntAct=EBI-375543, EBI-495465; CC P00519; Q4KMG0: CDON; NbExp=2; IntAct=EBI-375543, EBI-7016840; CC P00519; P46108: CRK; NbExp=4; IntAct=EBI-375543, EBI-886; CC P00519; P46109: CRKL; NbExp=3; IntAct=EBI-375543, EBI-910; CC P00519; P35222: CTNNB1; NbExp=2; IntAct=EBI-375543, EBI-491549; CC P00519; P00533: EGFR; NbExp=3; IntAct=EBI-375543, EBI-297353; CC P00519; P04626: ERBB2; NbExp=2; IntAct=EBI-375543, EBI-641062; CC P00519; Q03468: ERCC6; NbExp=8; IntAct=EBI-375543, EBI-295284; CC P00519; Q14315: FLNC; NbExp=2; IntAct=EBI-375543, EBI-489954; CC P00519; P36888: FLT3; NbExp=2; IntAct=EBI-375543, EBI-3946257; CC P00519; P05107: ITGB2; NbExp=4; IntAct=EBI-375543, EBI-300173; CC P00519; P10721: KIT; NbExp=2; IntAct=EBI-375543, EBI-1379503; CC P00519; Q38SD2: LRRK1; NbExp=3; IntAct=EBI-375543, EBI-1050422; CC P00519; Q92918: MAP4K1; NbExp=3; IntAct=EBI-375543, EBI-881; CC P00519; Q7Z434: MAVS; NbExp=6; IntAct=EBI-375543, EBI-995373; CC P00519; O43196: MSH5; NbExp=10; IntAct=EBI-375543, EBI-6092730; CC P00519; P15941: MUC1; NbExp=4; IntAct=EBI-375543, EBI-2804728; CC P00519; P15941-12: MUC1; NbExp=4; IntAct=EBI-375543, EBI-34603716; CC P00519; P16333: NCK1; NbExp=2; IntAct=EBI-375543, EBI-389883; CC P00519; O43900: PRICKLE3; NbExp=2; IntAct=EBI-375543, EBI-1751761; CC P00519; Q13905: RAPGEF1; NbExp=4; IntAct=EBI-375543, EBI-976876; CC P00519; Q86UR5: RIMS1; NbExp=2; IntAct=EBI-375543, EBI-1043236; CC P00519; Q13671: RIN1; NbExp=5; IntAct=EBI-375543, EBI-366017; CC P00519; P31947: SFN; NbExp=5; IntAct=EBI-375543, EBI-476295; CC P00519; Q15464: SHB; NbExp=5; IntAct=EBI-375543, EBI-4402156; CC P00519; O75751: SLC22A3; NbExp=2; IntAct=EBI-375543, EBI-1752674; CC P00519; P37840: SNCA; NbExp=3; IntAct=EBI-375543, EBI-985879; CC P00519; Q9BX66: SORBS1; NbExp=2; IntAct=EBI-375543, EBI-433642; CC P00519; O60504-2: SORBS3; NbExp=5; IntAct=EBI-375543, EBI-1222956; CC P00519; Q07890: SOS2; NbExp=2; IntAct=EBI-375543, EBI-298181; CC P00519; P12931: SRC; NbExp=2; IntAct=EBI-375543, EBI-621482; CC P00519; P51692: STAT5B; NbExp=2; IntAct=EBI-375543, EBI-1186119; CC P00519; Q9Y4G6: TLN2; NbExp=3; IntAct=EBI-375543, EBI-1220811; CC P00519; P11387: TOP1; NbExp=7; IntAct=EBI-375543, EBI-876302; CC P00519; P15498: VAV1; NbExp=5; IntAct=EBI-375543, EBI-625518; CC P00519; P62258: YWHAE; NbExp=5; IntAct=EBI-375543, EBI-356498; CC P00519; P61981: YWHAG; NbExp=5; IntAct=EBI-375543, EBI-359832; CC P00519; P63104: YWHAZ; NbExp=3; IntAct=EBI-375543, EBI-347088; CC P00519; O35158: Cdon; Xeno; NbExp=4; IntAct=EBI-375543, EBI-7016767; CC P00519-1; P37840: SNCA; NbExp=6; IntAct=EBI-5278159, EBI-985879; CC P00519-2; P48165: GJA8; NbExp=3; IntAct=EBI-9254597, EBI-17458373; CC P00519-2; Q15323: KRT31; NbExp=3; IntAct=EBI-9254597, EBI-948001; CC P00519-2; P37840: SNCA; NbExp=5; IntAct=EBI-9254597, EBI-985879; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion CC {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm CC depending on environmental signals. Sequestered into the cytoplasm CC through interaction with 14-3-3 proteins. Localizes to mitochondria in CC response to oxidative stress (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform IB]: Nucleus membrane; Lipid-anchor. CC Note=The myristoylated c-ABL protein is reported to be nuclear. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=IA; CC IsoId=P00519-1; Sequence=Displayed; CC Name=IB; CC IsoId=P00519-2; Sequence=VSP_004957; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- PTM: Acetylated at Lys-711 by EP300 which promotes the cytoplasmic CC translocation. {ECO:0000269|PubMed:16648821}. CC -!- PTM: Phosphorylation at Tyr-70 by members of the SRC family of kinases CC disrupts SH3 domain-based autoinhibitory interactions and CC intermolecular associations, such as that with ABI1, and also enhances CC kinase activity. Phosphorylation at Tyr-226 and Tyr-393 correlate with CC increased activity. DNA damage-induced activation of ABL1 requires the CC function of ATM and Ser-446 phosphorylation (By similarity). CC Phosphorylation at Ser-569 has been attributed to a CDC2-associated CC kinase and is coupled to cell division (By similarity). Phosphorylation CC at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces CC binding to ABI1. Phosphorylation on Thr-735 is required for binding 14- CC 3-3 proteins for cytoplasmic translocation. Phosphorylated by PRKDC (By CC similarity). {ECO:0000250}. CC -!- PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to CC degradation. {ECO:0000269|PubMed:12475393}. CC -!- DISEASE: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal CC myeloproliferative disorder of a pluripotent stem cell with a specific CC cytogenetic abnormality, the Philadelphia chromosome (Ph), involving CC myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T- CC lymphoid cells, but not marrow fibroblasts. Note=The gene represented CC in this entry is involved in disease pathogenesis. CC -!- DISEASE: Note=A chromosomal aberration involving ABL1 has been found in CC patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) CC with BCR. The translocation produces a BCR-ABL found also in acute CC myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). CC {ECO:0000269|PubMed:3021337}. CC -!- DISEASE: Note=A chromosomal aberration involving ABL1 is found in a CC form of acute lymphoblastic leukemia (PubMed:15361874). Translocation CC t(9;9)(q34;q34) with NUP214 (PubMed:15361874). CC {ECO:0000269|PubMed:15361874}. CC -!- DISEASE: Congenital heart defects and skeletal malformations syndrome CC (CHDSKM) [MIM:617602]: An autosomal dominant disorder characterized by CC congenital heart disease with atrial and ventricular septal defects, CC variable skeletal abnormalities, and failure to thrive. Skeletal CC defects include pectus excavatum, scoliosis, and finger contractures. CC Some patient exhibit joint laxity. {ECO:0000269|PubMed:28288113}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. ABL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/1/ABL"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/abl1/"; 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; M14752; AAA51561.1; -; mRNA. DR EMBL; X16416; CAA34438.1; -; mRNA. DR EMBL; U07563; AAB60394.1; -; Genomic_DNA. DR EMBL; U07563; AAB60393.1; -; Genomic_DNA. DR EMBL; U07561; AAB60393.1; JOINED; Genomic_DNA. DR EMBL; DQ145721; AAZ38718.1; -; Genomic_DNA. DR EMBL; AL359092; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL161733; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87948.1; -; Genomic_DNA. DR EMBL; BC117451; AAI17452.1; -; mRNA. DR EMBL; S69223; AAD14034.1; -; Genomic_DNA. DR CCDS; CCDS35165.1; -. [P00519-2] DR CCDS; CCDS35166.1; -. [P00519-1] DR PIR; S08519; TVHUA. DR RefSeq; NP_005148.2; NM_005157.5. [P00519-1] DR RefSeq; NP_009297.2; NM_007313.2. [P00519-2] DR PDB; 1AB2; NMR; -; A=120-220. DR PDB; 1AWO; NMR; -; A=65-119. DR PDB; 1BBZ; X-ray; 1.65 A; A/C/E/G=64-121. DR PDB; 1JU5; NMR; -; C=62-122. DR PDB; 1OPL; X-ray; 3.42 A; A/B=27-512. DR PDB; 1ZZP; NMR; -; A=1007-1130. DR PDB; 2ABL; X-ray; 2.50 A; A=57-218. DR PDB; 2E2B; X-ray; 2.20 A; A/B=229-515. DR PDB; 2F4J; X-ray; 1.91 A; A=229-513. DR PDB; 2FO0; X-ray; 2.27 A; A=38-512. DR PDB; 2G1T; X-ray; 1.80 A; A/B/C/D=229-512. DR PDB; 2G2F; X-ray; 2.70 A; A/B=229-512. DR PDB; 2G2H; X-ray; 2.00 A; A/B=229-512. DR PDB; 2G2I; X-ray; 3.12 A; A/B=229-512. DR PDB; 2GQG; X-ray; 2.40 A; A/B=229-500. DR PDB; 2HIW; X-ray; 2.20 A; A/B=230-512. DR PDB; 2HYY; X-ray; 2.40 A; A/B/C/D=228-500. DR PDB; 2HZ0; X-ray; 2.10 A; A/B=228-497. DR PDB; 2HZ4; X-ray; 2.80 A; A/B/C=228-500. DR PDB; 2HZI; X-ray; 1.70 A; A/B=229-500. DR PDB; 2O88; X-ray; 1.75 A; A/B=64-121. DR PDB; 2V7A; X-ray; 2.50 A; A/B=229-512. DR PDB; 3CS9; X-ray; 2.21 A; A/B/C/D=229-500. DR PDB; 3EG0; X-ray; 2.30 A; A=60-121. DR PDB; 3EG1; X-ray; 1.85 A; A/B=60-121. DR PDB; 3EG2; X-ray; 1.80 A; A=60-121. DR PDB; 3EG3; X-ray; 1.40 A; A=60-121. DR PDB; 3EGU; X-ray; 2.25 A; A=60-121. DR PDB; 3K2M; X-ray; 1.75 A; A/B=121-232. DR PDB; 3PYY; X-ray; 1.85 A; A/B=229-512. DR PDB; 3QRI; X-ray; 2.10 A; A/B=229-499. DR PDB; 3QRJ; X-ray; 1.82 A; A/B=229-499. DR PDB; 3QRK; X-ray; 2.30 A; A=229-499. DR PDB; 3T04; X-ray; 2.10 A; A=112-232. DR PDB; 3UE4; X-ray; 2.42 A; A/B=229-512. DR PDB; 3UYO; X-ray; 1.83 A; A=112-232. DR PDB; 4J9B; X-ray; 1.70 A; A=60-121. DR PDB; 4J9C; X-ray; 1.05 A; A=60-121. DR PDB; 4J9D; X-ray; 1.50 A; A/C/E=60-121. DR PDB; 4J9E; X-ray; 1.40 A; A/C/E=60-121. DR PDB; 4J9F; X-ray; 1.09 A; A/C/E=60-121. DR PDB; 4J9G; X-ray; 1.80 A; A/C/E=60-121. DR PDB; 4J9H; X-ray; 1.70 A; A/B/C/D/E/F=60-121. DR PDB; 4J9I; X-ray; 2.20 A; A/C/E=60-121. DR PDB; 4JJB; X-ray; 1.65 A; A=60-121. DR PDB; 4JJC; X-ray; 1.60 A; A=60-121. DR PDB; 4JJD; X-ray; 1.60 A; A=60-121. DR PDB; 4TWP; X-ray; 2.40 A; A/B=233-503. DR PDB; 4WA9; X-ray; 2.20 A; A/B=246-512. DR PDB; 4XEY; X-ray; 2.89 A; A/B=119-515. DR PDB; 4YC8; X-ray; 2.90 A; A/B=229-512. DR PDB; 4ZOG; X-ray; 2.30 A; A/B=229-511. DR PDB; 5DC0; X-ray; 2.23 A; B=112-232. DR PDB; 5DC4; X-ray; 1.48 A; A=112-232. DR PDB; 5DC9; X-ray; 1.56 A; A=112-232. DR PDB; 5HU9; X-ray; 1.53 A; A=229-500. DR PDB; 5MO4; X-ray; 2.17 A; A=27-515. DR PDB; 5NP2; X-ray; 1.60 A; A/B=64-120. DR PDB; 5OAZ; X-ray; 1.03 A; A/B=60-121. DR PDB; 6AMV; NMR; -; A=26-236. DR PDB; 6AMW; NMR; -; A=26-236. DR PDB; 6BL8; X-ray; 2.50 A; A/B=233-504. DR PDB; 6NPE; X-ray; 2.15 A; A/B=229-512. DR PDB; 6NPU; X-ray; 2.33 A; A/B=229-512. DR PDB; 6NPV; X-ray; 1.86 A; A/B=229-512. DR PDB; 6XR6; NMR; -; A=229-515. DR PDB; 6XR7; NMR; -; A=229-515. DR PDB; 6XRG; NMR; -; A=229-515. DR PDB; 7CC2; X-ray; 2.72 A; A/B=229-510. DR PDB; 7DT2; X-ray; 2.30 A; A/B=229-510. DR PDB; 7N9G; X-ray; 2.20 A; A/B/C=229-499. DR PDB; 7PVQ; X-ray; 1.55 A; A/B=63-120. DR PDB; 7PVR; X-ray; 1.65 A; A=63-120. DR PDB; 7PVS; X-ray; 1.05 A; A/B=63-120. DR PDB; 7PVV; X-ray; 1.82 A; A=63-120. DR PDB; 7PW2; X-ray; 1.10 A; A=63-120. DR PDB; 7W7X; X-ray; 2.00 A; A/B=229-500. DR PDB; 7W7Y; X-ray; 2.20 A; A/B=229-504. DR PDB; 8H7F; X-ray; 2.45 A; A/B=229-500. DR PDB; 8H7H; X-ray; 2.28 A; A/B=229-500. DR PDB; 8SSN; X-ray; 2.86 A; A/B=64-510. DR PDBsum; 1AB2; -. DR PDBsum; 1AWO; -. DR PDBsum; 1BBZ; -. DR PDBsum; 1JU5; -. DR PDBsum; 1OPL; -. DR PDBsum; 1ZZP; -. DR PDBsum; 2ABL; -. DR PDBsum; 2E2B; -. DR PDBsum; 2F4J; -. DR PDBsum; 2FO0; -. DR PDBsum; 2G1T; -. DR PDBsum; 2G2F; -. DR PDBsum; 2G2H; -. DR PDBsum; 2G2I; -. DR PDBsum; 2GQG; -. DR PDBsum; 2HIW; -. DR PDBsum; 2HYY; -. DR PDBsum; 2HZ0; -. DR PDBsum; 2HZ4; -. DR PDBsum; 2HZI; -. DR PDBsum; 2O88; -. DR PDBsum; 2V7A; -. DR PDBsum; 3CS9; -. DR PDBsum; 3EG0; -. DR PDBsum; 3EG1; -. DR PDBsum; 3EG2; -. DR PDBsum; 3EG3; -. DR PDBsum; 3EGU; -. DR PDBsum; 3K2M; -. DR PDBsum; 3PYY; -. DR PDBsum; 3QRI; -. DR PDBsum; 3QRJ; -. DR PDBsum; 3QRK; -. DR PDBsum; 3T04; -. DR PDBsum; 3UE4; -. DR PDBsum; 3UYO; -. DR PDBsum; 4J9B; -. DR PDBsum; 4J9C; -. DR PDBsum; 4J9D; -. DR PDBsum; 4J9E; -. DR PDBsum; 4J9F; -. DR PDBsum; 4J9G; -. DR PDBsum; 4J9H; -. DR PDBsum; 4J9I; -. DR PDBsum; 4JJB; -. DR PDBsum; 4JJC; -. DR PDBsum; 4JJD; -. DR PDBsum; 4TWP; -. DR PDBsum; 4WA9; -. DR PDBsum; 4XEY; -. DR PDBsum; 4YC8; -. DR PDBsum; 4ZOG; -. DR PDBsum; 5DC0; -. DR PDBsum; 5DC4; -. DR PDBsum; 5DC9; -. DR PDBsum; 5HU9; -. DR PDBsum; 5MO4; -. DR PDBsum; 5NP2; -. DR PDBsum; 5OAZ; -. DR PDBsum; 6AMV; -. DR PDBsum; 6AMW; -. DR PDBsum; 6BL8; -. DR PDBsum; 6NPE; -. DR PDBsum; 6NPU; -. DR PDBsum; 6NPV; -. DR PDBsum; 6XR6; -. DR PDBsum; 6XR7; -. DR PDBsum; 6XRG; -. DR PDBsum; 7CC2; -. DR PDBsum; 7DT2; -. DR PDBsum; 7N9G; -. DR PDBsum; 7PVQ; -. DR PDBsum; 7PVR; -. DR PDBsum; 7PVS; -. DR PDBsum; 7PVV; -. DR PDBsum; 7PW2; -. DR PDBsum; 7W7X; -. DR PDBsum; 7W7Y; -. DR PDBsum; 8H7F; -. DR PDBsum; 8H7H; -. DR PDBsum; 8SSN; -. DR AlphaFoldDB; P00519; -. DR BMRB; P00519; -. DR SMR; P00519; -. DR BioGRID; 106543; 226. DR CORUM; P00519; -. DR DIP; DIP-1042N; -. DR IntAct; P00519; 252. DR MINT; P00519; -. DR STRING; 9606.ENSP00000361423; -. DR BindingDB; P00519; -. DR ChEMBL; CHEMBL1862; -. DR DrugBank; DB08043; 1-[4-(PYRIDIN-4-YLOXY)PHENYL]-3-[3-(TRIFLUOROMETHYL)PHENYL]UREA. DR DrugBank; DB08583; 2-amino-5-[3-(1-ethyl-1H-pyrazol-5-yl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-N,N-dimethylbenzamide. DR DrugBank; DB07831; 2-{[(6-OXO-1,6-DIHYDROPYRIDIN-3-YL)METHYL]AMINO}-N-[4-PROPYL-3-(TRIFLUOROMETHYL)PHENYL]BENZAMIDE. DR DrugBank; DB08350; 5-[3-(2-METHOXYPHENYL)-1H-PYRROLO[2,3-B]PYRIDIN-5-YL]-N,N-DIMETHYLPYRIDINE-3-CARBOXAMIDE. DR DrugBank; DB12597; Asciminib. DR DrugBank; DB00171; ATP. DR DrugBank; DB06616; Bosutinib. DR DrugBank; DB12267; Brigatinib. DR DrugBank; DB01254; Dasatinib. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB13749; Magnesium gluconate. DR DrugBank; DB08231; Myristic acid. DR DrugBank; DB03878; N-[4-Methyl-3-[[4-(3-Pyridinyl)-2-Pyrimidinyl]Amino]Phenyl]-3-Pyridinecarboxamide. DR DrugBank; DB04868; Nilotinib. DR DrugBank; DB08339; PD-166326. DR DrugBank; DB08901; Ponatinib. DR DrugBank; DB12323; Radotinib. DR DrugBank; DB08896; Regorafenib. DR DrugBank; DB14989; Umbralisib. DR DrugBank; DB05184; XL228. DR DrugCentral; P00519; -. DR GuidetoPHARMACOLOGY; 1923; -. DR MoonDB; P00519; Predicted. DR GlyCosmos; P00519; 1 site, 1 glycan. DR GlyGen; P00519; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P00519; -. DR PhosphoSitePlus; P00519; -. DR BioMuta; ABL1; -. DR DMDM; 85681908; -. DR CPTAC; CPTAC-1776; -. DR CPTAC; CPTAC-1788; -. DR CPTAC; CPTAC-3041; -. DR CPTAC; CPTAC-3042; -. DR EPD; P00519; -. DR jPOST; P00519; -. DR MassIVE; P00519; -. DR MaxQB; P00519; -. DR PaxDb; 9606-ENSP00000361423; -. DR PeptideAtlas; P00519; -. DR ProteomicsDB; 51259; -. [P00519-1] DR ProteomicsDB; 51260; -. [P00519-2] DR Pumba; P00519; -. DR Antibodypedia; 3637; 2507 antibodies from 44 providers. DR DNASU; 25; -. DR Ensembl; ENST00000318560.6; ENSP00000323315.5; ENSG00000097007.20. [P00519-1] DR Ensembl; ENST00000372348.9; ENSP00000361423.2; ENSG00000097007.20. [P00519-2] DR GeneID; 25; -. DR KEGG; hsa:25; -. DR MANE-Select; ENST00000318560.6; ENSP00000323315.5; NM_005157.6; NP_005148.2. DR UCSC; uc004bzv.4; human. [P00519-1] DR AGR; HGNC:76; -. DR CTD; 25; -. DR DisGeNET; 25; -. DR GeneCards; ABL1; -. DR HGNC; HGNC:76; ABL1. DR HPA; ENSG00000097007; Low tissue specificity. DR MalaCards; ABL1; -. DR MIM; 189980; gene. DR MIM; 608232; phenotype. DR MIM; 617602; phenotype. DR neXtProt; NX_P00519; -. DR OpenTargets; ENSG00000097007; -. DR Orphanet; 585909; B-lymphoblastic leukemia/lymphoma with t(9;22)(q34.1;q11.2). DR Orphanet; 521; Chronic myeloid leukemia. DR Orphanet; 643503; Marfanoid habitus-facial dysmorphism-skeletal abnormality-heart defect syndrome. DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia. DR PharmGKB; PA24413; -. DR VEuPathDB; HostDB:ENSG00000097007; -. DR eggNOG; KOG4278; Eukaryota. DR GeneTree; ENSGT00940000153838; -. DR HOGENOM; CLU_002795_0_0_1; -. DR InParanoid; P00519; -. DR OMA; KCKSSNI; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P00519; -. DR TreeFam; TF105081; -. DR BRENDA; 2.7.10.2; 2681. DR PathwayCommons; P00519; -. DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling. DR Reactome; R-HSA-525793; Myogenesis. DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-HSA-69231; Cyclin D associated events in G1. DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation. DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P00519; -. DR SIGNOR; P00519; -. DR BioGRID-ORCS; 25; 30 hits in 1205 CRISPR screens. DR ChiTaRS; ABL1; human. DR EvolutionaryTrace; P00519; -. DR GeneWiki; ABL_(gene); -. DR GenomeRNAi; 25; -. DR Pharos; P00519; Tclin. DR PRO; PR:P00519; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P00519; Protein. DR Bgee; ENSG00000097007; Expressed in frontal pole and 196 other cell types or tissues. DR ExpressionAtlas; P00519; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL. DR GO; GO:0030426; C:growth cone; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; NAS:ParkinsonsUK-UCL. DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL. DR GO; GO:0032991; C:protein-containing complex; IPI:CAFA. DR GO; GO:0001726; C:ruffle; IEA:Ensembl. DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl. DR GO; GO:0003785; F:actin monomer binding; TAS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0000405; F:bubble DNA binding; IDA:ARUK-UCL. DR GO; GO:0070097; F:delta-catenin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0046875; F:ephrin receptor binding; ISS:ARUK-UCL. DR GO; GO:0000400; F:four-way junction DNA binding; IDA:ARUK-UCL. DR GO; GO:0016301; F:kinase activity; IMP:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:BHF-UCL. DR GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL. DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; TAS:UniProtKB. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA. DR GO; GO:0070064; F:proline-rich region binding; IDA:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:MGI. DR GO; GO:0005080; F:protein kinase C binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0043621; F:protein self-association; IPI:BHF-UCL. DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0042169; F:SH2 domain binding; IPI:CAFA. DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB. DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; TAS:ARUK-UCL. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl. DR GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl. DR GO; GO:1990051; P:activation of protein kinase C activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl. DR GO; GO:0008306; P:associative learning; IEA:Ensembl. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0002322; P:B cell proliferation involved in immune response; IEA:Ensembl. DR GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl. DR GO; GO:0001922; P:B-1 B cell homeostasis; IEA:Ensembl. DR GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl. DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl. DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl. DR GO; GO:1903351; P:cellular response to dopamine; TAS:ParkinsonsUK-UCL. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:ParkinsonsUK-UCL. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0034599; P:cellular response to oxidative stress; TAS:ParkinsonsUK-UCL. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl. DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl. DR GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl. DR GO; GO:1904157; P:DN4 thymocyte differentiation; IEA:Ensembl. DR GO; GO:0071103; P:DNA conformation change; IDA:ARUK-UCL. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0043542; P:endothelial cell migration; IMP:BHF-UCL. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:BHF-UCL. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; TAS:UniProtKB. DR GO; GO:0030035; P:microspike assembly; IEA:Ensembl. DR GO; GO:0006298; P:mismatch repair; TAS:ProtInc. DR GO; GO:0051882; P:mitochondrial depolarization; TAS:ParkinsonsUK-UCL. DR GO; GO:0000278; P:mitotic cell cycle; TAS:ParkinsonsUK-UCL. DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl. DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl. DR GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl. DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISS:ARUK-UCL. DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl. DR GO; GO:1900275; P:negative regulation of phospholipase C activity; IMP:MGI. DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IDA:BHF-UCL. DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:MGI. DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl. DR GO; GO:0060563; P:neuroepithelial cell differentiation; IEA:Ensembl. DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl. DR GO; GO:0038189; P:neuropilin signaling pathway; IMP:BHF-UCL. DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IMP:UniProtKB. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IMP:UniProtKB. DR GO; GO:1903210; P:podocyte apoptotic process; IEA:Ensembl. DR GO; GO:1904531; P:positive regulation of actin filament binding; IMP:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:1905555; P:positive regulation of blood vessel branching; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:MGI. DR GO; GO:1900006; P:positive regulation of dendrite development; IEA:Ensembl. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:1903905; P:positive regulation of establishment of T cell polarity; ISS:UniProtKB. DR GO; GO:1903055; P:positive regulation of extracellular matrix organization; IEA:Ensembl. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl. DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:BHF-UCL. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl. DR GO; GO:1904528; P:positive regulation of microtubule binding; IMP:UniProtKB. DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl. DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:BHF-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB. DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:BHF-UCL. DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:BHF-UCL. DR GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; TAS:ARUK-UCL. DR GO; GO:0032729; P:positive regulation of type II interferon production; IEA:Ensembl. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl. DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0046777; P:protein autophosphorylation; IDA:ParkinsonsUK-UCL. DR GO; GO:1904518; P:protein localization to cytoplasmic microtubule plus-end; IMP:UniProtKB. DR GO; GO:0036211; P:protein modification process; NAS:UniProtKB. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0010506; P:regulation of autophagy; TAS:UniProtKB. DR GO; GO:0030516; P:regulation of axon extension; IMP:UniProtKB. DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL. DR GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; TAS:ParkinsonsUK-UCL. DR GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc. DR GO; GO:0030100; P:regulation of endocytosis; TAS:UniProtKB. DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome. DR GO; GO:0031113; P:regulation of microtubule polymerization; IMP:UniProtKB. DR GO; GO:1905244; P:regulation of modification of synaptic structure; ISS:ARUK-UCL. DR GO; GO:0045580; P:regulation of T cell differentiation; ISS:UniProtKB. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl. DR GO; GO:0071871; P:response to epinephrine; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IGI:MGI. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:UniProtKB. DR GO; GO:0048536; P:spleen development; IEA:Ensembl. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl. DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl. DR GO; GO:0048538; P:thymus development; IEA:Ensembl. DR GO; GO:0002333; P:transitional one stage B cell differentiation; IEA:Ensembl. 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 IDEAL; IID00645; -. 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: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 Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00808; FABD; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; P00519; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding; KW Autophagy; Cell adhesion; Chromosomal rearrangement; Cytoplasm; KW Cytoskeleton; Disease variant; DNA damage; DNA repair; DNA-binding; KW Endocytosis; Kinase; Lipoprotein; Magnesium; Manganese; Membrane; KW Metal-binding; Mitochondrion; Myristate; Nucleotide-binding; Nucleus; KW Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain; KW Transferase; Tyrosine-protein kinase; Ubl conjugation. FT CHAIN 1..1130 FT /note="Tyrosine-protein kinase ABL1" FT /id="PRO_0000088050" FT DOMAIN 61..121 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 127..217 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 242..493 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..60 FT /note="CAP" FT REGION 518..996 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 869..968 FT /note="DNA-binding" FT /evidence="ECO:0000250" FT REGION 953..1130 FT /note="F-actin-binding" FT MOTIF 381..405 FT /note="Kinase activation loop" FT MOTIF 605..609 FT /note="Nuclear localization signal 1" FT /evidence="ECO:0000255" FT MOTIF 709..715 FT /note="Nuclear localization signal 2" FT /evidence="ECO:0000255" FT MOTIF 762..769 FT /note="Nuclear localization signal 3" FT /evidence="ECO:0000255" FT MOTIF 1090..1100 FT /note="Nuclear export signal" FT /evidence="ECO:0000250" FT COMPBIAS 533..549 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 579..601 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 622..638 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 685..703 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 735..753 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 758..772 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 870..894 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 363 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 248..256 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 316..322 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT SITE 26..27 FT /note="Breakpoint for translocation to form BCR-ABL and FT NUP214-ABL1 fusion proteins" FT /evidence="ECO:0000269|PubMed:15361874, FT ECO:0000269|PubMed:3021337" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16543148, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332" FT MOD_RES 70 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:16912036, FT ECO:0000269|PubMed:18775435" FT MOD_RES 115 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:16912036" FT MOD_RES 128 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:16912036" FT MOD_RES 139 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:16912036" FT MOD_RES 172 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:16912036" FT MOD_RES 185 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:16912036" FT MOD_RES 215 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:16912036" FT MOD_RES 226 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:16912036" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P42684" FT MOD_RES 253 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 257 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 393 FT /note="Phosphotyrosine; by autocatalysis and SRC-type Tyr- FT kinases" FT /evidence="ECO:0000269|PubMed:16912036" FT MOD_RES 413 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 446 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00520" FT MOD_RES 559 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 618 FT /note="Phosphoserine; by PAK2" FT /evidence="ECO:0000269|PubMed:18161990" FT MOD_RES 619 FT /note="Phosphoserine; by PAK2" FT /evidence="ECO:0000269|PubMed:18161990" FT MOD_RES 620 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 659 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 683 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 711 FT /note="N6-acetyllysine; by EP300" FT /evidence="ECO:0000269|PubMed:16648821" FT MOD_RES 718 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 735 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:15696159" FT MOD_RES 751 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 781 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 814 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 823 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 844 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:23186163" FT MOD_RES 852 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 855 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 917 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 977 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT VAR_SEQ 1..26 FT /note="MLEICLKLVGCKSKKGLSSSSSCYLE -> MGQQPGKVLGDQRRPSLPALHF FT IKGAGKKESSRHGGPHCNVFVEH (in isoform IB)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_004957" FT VARIANT 47 FT /note="R -> G (in a lung large cell carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_032676" FT VARIANT 140 FT /note="L -> P (in dbSNP:rs1064152)" FT /evidence="ECO:0000269|PubMed:3021337" FT /id="VAR_051692" FT VARIANT 166 FT /note="R -> K (in a melanoma sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_032677" FT VARIANT 226 FT /note="Y -> C (in CHDSKM; increases kinase activity; no FT effect on protein levels; dbSNP:rs1060499547)" FT /evidence="ECO:0000269|PubMed:28288113" FT /id="VAR_079482" FT VARIANT 247 FT /note="K -> R (in dbSNP:rs34549764)" FT /id="VAR_051693" FT VARIANT 337 FT /note="A -> T (in CHDSKM; increases kinase activity; no FT effect on protein levels; dbSNP:rs1060499548)" FT /evidence="ECO:0000269|PubMed:28288113" FT /id="VAR_079483" FT VARIANT 706 FT /note="G -> V (in dbSNP:rs34634745)" FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4" FT /id="VAR_025043" FT VARIANT 810 FT /note="P -> L (in dbSNP:rs2229071)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_032678" FT VARIANT 852 FT /note="T -> P (in dbSNP:rs1588283506)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_025044" FT VARIANT 900 FT /note="P -> S (in dbSNP:rs35266696)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_025045" FT VARIANT 968 FT /note="S -> P (in dbSNP:rs1064165)" FT /id="VAR_051694" FT VARIANT 972 FT /note="S -> L (in dbSNP:rs2229067)" FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4" FT /id="VAR_025046" FT MUTAGEN 735 FT /note="T->A: Abolishes phosphorylation. Loss of binding FT YWHAS and YWHAZ. Localizes to the nucleus. No effect on FT kinase activity." FT /evidence="ECO:0000269|PubMed:15696159" FT CONFLICT 159 FT /note="G -> S (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 424..425 FT /note="AF -> GK (in Ref. 9)" FT /evidence="ECO:0000305" FT CONFLICT 445 FT /note="L -> R (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="E -> K (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 520 FT /note="S -> T (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 719 FT /note="A -> V (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 837 FT /note="G -> E (in Ref. 2; CAA34438)" FT /evidence="ECO:0000305" FT CONFLICT 837 FT /note="G -> W (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 863 FT /note="G -> R (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 894 FT /note="R -> K (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 917..919 FT /note="SPS -> RPG (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 952 FT /note="G -> A (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 967..968 FT /note="QS -> HP (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 982 FT /note="P -> PL (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 1022 FT /note="Missing (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 1045 FT /note="R -> G (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT CONFLICT 1103 FT /note="T -> S (in Ref. 1; AAA51561)" FT /evidence="ECO:0000305" FT STRAND 26..32 FT /evidence="ECO:0007829|PDB:6AMV" FT STRAND 39..44 FT /evidence="ECO:0007829|PDB:6AMV" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:6AMV" FT HELIX 49..53 FT /evidence="ECO:0007829|PDB:2FO0" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:2FO0" FT STRAND 65..70 FT /evidence="ECO:0007829|PDB:5OAZ" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:3EG3" FT STRAND 87..93 FT /evidence="ECO:0007829|PDB:5OAZ" FT STRAND 97..104 FT /evidence="ECO:0007829|PDB:5OAZ" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:5OAZ" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:5OAZ" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:5OAZ" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:5DC4" FT HELIX 134..140 FT /evidence="ECO:0007829|PDB:5DC4" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 148..153 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 161..167 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 170..175 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:4XEY" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:4XEY" FT STRAND 184..187 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:5DC4" FT HELIX 195..202 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:5DC4" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:5MO4" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:2GQG" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:2G1T" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 242..247 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 254..261 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 266..271 FT /evidence="ECO:0007829|PDB:5HU9" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 280..290 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 301..305 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 307..310 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 319..322 FT /evidence="ECO:0007829|PDB:2HZI" FT HELIX 323..329 FT /evidence="ECO:0007829|PDB:5HU9" FT TURN 332..334 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 337..356 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:2G2H" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 373..375 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:2G2F" FT HELIX 384..387 FT /evidence="ECO:0007829|PDB:2G1T" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:2G1T" FT STRAND 393..396 FT /evidence="ECO:0007829|PDB:3QRJ" FT STRAND 399..401 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 403..405 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 408..413 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 418..433 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 445..447 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 448..453 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 466..475 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 480..482 FT /evidence="ECO:0007829|PDB:5HU9" FT HELIX 486..496 FT /evidence="ECO:0007829|PDB:5HU9" FT STRAND 498..500 FT /evidence="ECO:0007829|PDB:1OPL" FT HELIX 503..506 FT /evidence="ECO:0007829|PDB:2G1T" FT TURN 510..512 FT /evidence="ECO:0007829|PDB:2F4J" FT HELIX 1029..1045 FT /evidence="ECO:0007829|PDB:1ZZP" FT TURN 1046..1048 FT /evidence="ECO:0007829|PDB:1ZZP" FT HELIX 1053..1070 FT /evidence="ECO:0007829|PDB:1ZZP" FT HELIX 1071..1073 FT /evidence="ECO:0007829|PDB:1ZZP" FT HELIX 1080..1097 FT /evidence="ECO:0007829|PDB:1ZZP" FT STRAND 1101..1104 FT /evidence="ECO:0007829|PDB:1ZZP" FT STRAND 1106..1108 FT /evidence="ECO:0007829|PDB:1ZZP" FT HELIX 1115..1128 FT /evidence="ECO:0007829|PDB:1ZZP" FT LIPID P00519-2:2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000305" SQ SEQUENCE 1130 AA; 122873 MW; 85FE6C1C0E483EA2 CRC64; MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTVYGVSP NYDKWEMERT DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVNAVVL LYMATQISSA MEYLEKKNFI HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP SDRPSFAEIH QAFETMFQES SISDEVEKEL GKQGVRGAVS TLLQAPELPT KTRTSRRAAE HRDTTDVPEM PHSKGQGESD PLDHEPAVSP LLPRKERGPP EGGLNEDERL LPKDKKTNLF SALIKKKKKT APTPPKRSSS FREMDGQPER RGAGEEEGRD ISNGALAFTP LDTADPAKSP KPSNGAGVPN GALRESGGSG FRSPHLWKKS STLTSSRLAT GEEEGGGSSS KRFLRSCSAS CVPHGAKDTE WRSVTLPRDL QSTGRQFDSS TFGGHKSEKP ALPRKRAGEN RSDQVTRGTV TPPPRLVKKN EEAADEVFKD IMESSPGSSP PNLTPKPLRR QVTVAPASGL PHKEEAGKGS ALGTPAAAEP VTPTSKAGSG APGGTSKGPA EESRVRRHKH SSESPGRDKG KLSRLKPAPP PPPAASAGKA GGKPSQSPSQ EAAGEAVLGA KTKATSLVDA VNSDAAKPSQ PGEGLKKPVL PATPKPQSAK PSGTPISPAP VPSTLPSASS ALAGDQPSST AFIPLISTRV SLRKTRQPPE RIASGAITKG VVLDSTEALC LAISRNSEQM ASHSAVLEAG KNLYTFCVSY VDSIQQMRNK FAFREAINKL ENNLRELQIC PATAGSGPAA TQDFSKLLSS VKEISDIVQR //