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Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)

 ABL1_HUMAN              Reviewed;        1130 AA.
P00519; A3KFJ3; Q13869; Q13870; Q16133; Q17R61; Q45F09;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 4.
25-OCT-2017, entry version 240.
RecName: Full=Tyrosine-protein kinase ABL1;
EC=2.7.10.2 {ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:28428613};
AltName: Full=Abelson murine leukemia viral oncogene homolog 1;
AltName: Full=Abelson tyrosine-protein kinase 1;
AltName: Full=Proto-oncogene c-Abl;
AltName: Full=p150;
Name=ABL1; Synonyms=ABL, JTK7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA), ALTERNATIVE SPLICING, AND
VARIANT PRO-140.
PubMed=3021337; DOI=10.1016/0092-8674(86)90450-2;
Shtivelman E., Lifshitz B., Gale R.P., Roe B.A., Canaani E.;
"Alternative splicing of RNAs transcribed from the human abl gene and
from the bcr-abl fused gene.";
Cell 47:277-284(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA).
TISSUE=Fibroblast;
PubMed=2687768;
Fainstein E., Einat M., Gokkel E., Marcelle C., Croce C.M., Gale R.P.,
Canaani E.;
"Nucleotide sequence analysis of human abl and bcr-abl cDNAs.";
Oncogene 4:1477-1481(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS IA AND IB).
TISSUE=Lung;
PubMed=7665185; DOI=10.1006/geno.1995.1008;
Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D.,
Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y.,
McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G.,
Heisterkamp N., Groffen J., Roe B.A.;
"Sequence and analysis of the human ABL gene, the BCR gene, and
regions involved in the Philadelphia chromosomal translocation.";
Genomics 27:67-82(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-706; PRO-852;
SER-900 AND LEU-972.
NIEHS SNPs program;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IB).
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-40, AND SUBCELLULAR COMPONENT.
PubMed=2825022; DOI=10.1038/330386a0;
Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P.,
Dreazen O., Smith S.D., Croce C.M.;
"A new fused transcript in Philadelphia chromosome positive acute
lymphocytic leukaemia.";
Nature 330:386-388(1987).
[9]
NUCLEOTIDE SEQUENCE OF 360-426.
PubMed=6191223; DOI=10.1038/304167a0;
Groffen J., Heisterkamp N., Reynolds F.H. Jr., Stephenson J.R.;
"Homology between phosphotyrosine acceptor site of human c-abl and
viral oncogene products.";
Nature 304:167-169(1983).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-845.
PubMed=7545908;
Inokuchi K., Futaki M., Dan K., Nomura T.;
"Sequence analysis of the mutation at codon 834 and the sequence
variation of codon 837 of c-abl gene.";
Leukemia 8:343-344(1994).
[11]
MYRISTOYLATION AT GLY-2 (ISOFORM IB).
PubMed=2542016;
Jackson P., Baltimore D.;
"N-terminal mutations activate the leukemogenic potential of the
myristoylated form of c-abl.";
EMBO J. 8:449-456(1989).
[12]
DOMAIN, AND DNA-BINDING.
PubMed=2183353; DOI=10.1126/science.2183353;
Kipreos E.T., Wang J.Y.;
"Differential phosphorylation of c-Abl in cell cycle determined by
cdc2 kinase and phosphatase activity.";
Science 248:217-220(1990).
[13]
FUNCTION.
PubMed=9037071; DOI=10.1073/pnas.94.4.1437;
Yuan Z.M., Huang Y., Ishiko T., Kharbanda S., Weichselbaum R.,
Kufe D.;
"Regulation of DNA damage-induced apoptosis by the c-Abl tyrosine
kinase.";
Proc. Natl. Acad. Sci. U.S.A. 94:1437-1440(1997).
[14]
INTERACTION WITH RIN1, AND FUNCTION.
PubMed=9144171; DOI=10.1073/pnas.94.10.4954;
Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W.,
Herschman H., Witte O., Colicelli J.;
"Protein binding and signaling properties of RIN1 suggest a unique
effector function.";
Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997).
[15]
FUNCTION, AND INTERACTION WITH RAD51.
PubMed=9461559; DOI=10.1074/jbc.273.7.3799;
Yuan Z.M., Huang Y., Ishiko T., Nakada S., Utsugisawa T.,
Kharbanda S., Wang R., Sung P., Shinohara A., Weichselbaum R.,
Kufe D.;
"Regulation of Rad51 function by c-Abl in response to DNA damage.";
J. Biol. Chem. 273:3799-3802(1998).
[16]
INTERACTION WITH INPPL1.
PubMed=10194451;
Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H.,
Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B.;
"A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-
phosphatase (SHIP2) is constitutively tyrosine phosphorylated and
associated with src homologous and collagen gene (SHC) in chronic
myelogenous leukemia progenitor cells.";
Blood 93:2707-2720(1999).
[17]
FUNCTION, ENZYME REGULATION, AND INTERACTION WITH TP73.
PubMed=10391250; DOI=10.1038/21697;
Agami R., Blandino G., Oren M., Shaul Y.;
"Interaction of c-Abl and p73alpha and their collaboration to induce
apoptosis.";
Nature 399:809-813(1999).
[18]
DNA-BINDING.
PubMed=10325413; DOI=10.1093/nar/27.11.2265;
David-Cordonnier M.H., Payet D., D'Halluin J.C., Waring M.J.,
Travers A.A., Bailly C.;
"The DNA-binding domain of human c-Abl tyrosine kinase promotes the
interaction of a HMG chromosomal protein with DNA.";
Nucleic Acids Res. 27:2265-2270(1999).
[19]
REVIEW ON FUNCTION.
PubMed=11114745; DOI=10.1038/sj.onc.1203878;
Wang J.Y.;
"Regulation of cell death by the Abl tyrosine kinase.";
Oncogene 19:5643-5650(2000).
[20]
INTERACTION WITH SORBS1.
PubMed=11374898; DOI=10.1006/geno.2001.6541;
Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y.,
Chuang L.-M.;
"Cloning, mapping, and characterization of the human sorbin and SH3
domain containing 1 (SORBS1) gene: a protein associated with c-Abl
during insulin signaling in the hepatoma cell line Hep3B.";
Genomics 74:12-20(2001).
[21]
FUNCTION, AND INTERACTION WITH RAD52.
PubMed=12379650; DOI=10.1074/jbc.M208151200;
Kitao H., Yuan Z.M.;
"Regulation of ionizing radiation-induced Rad52 nuclear foci formation
by c-Abl-mediated phosphorylation.";
J. Biol. Chem. 277:48944-48948(2002).
[22]
FUNCTION, AND INTERACTION WITH RAD9A.
PubMed=11971963; DOI=10.1128/MCB.22.10.3292-3300.2002;
Yoshida K., Komatsu K., Wang H.-G., Kufe D.;
"c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in
response to DNA damage.";
Mol. Cell. Biol. 22:3292-3300(2002).
[23]
UBIQUITINATION.
PubMed=12475393; DOI=10.1042/BJ20021539;
Soubeyran P., Barac A., Szymkiewicz I., Dikic I.;
"Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-
Abl.";
Biochem. J. 370:29-34(2003).
[24]
FUNCTION.
PubMed=12531427; DOI=10.1016/S0898-6568(02)00090-6;
Sanguinetti A.R., Mastick C.C.;
"c-Abl is required for oxidative stress-induced phosphorylation of
caveolin-1 on tyrosine 14.";
Cell. Signal. 15:289-298(2003).
[25]
FUNCTION.
PubMed=12672821; DOI=10.1074/jbc.M301447200;
Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H.,
Shishido T.;
"Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
enabled (Mena) by c-Abl kinase.";
J. Biol. Chem. 278:21685-21692(2003).
[26]
REVIEW ON FUNCTION.
PubMed=12775773; DOI=10.1242/jcs.00622;
Woodring P.J., Hunter T., Wang J.Y.;
"Regulation of F-actin-dependent processes by the Abl family of
tyrosine kinases.";
J. Cell Sci. 116:2613-2626(2003).
[27]
INTERACTION WITH BCR.
PubMed=15302586; DOI=10.1016/j.yexcr.2004.05.010;
Laurent C.E., Smithgall T.E.;
"The c-Fes tyrosine kinase cooperates with the breakpoint cluster
region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-
dependent manner.";
Exp. Cell Res. 299:188-198(2004).
[28]
FUNCTION.
PubMed=15556646; DOI=10.1016/j.febslet.2004.10.054;
Grossmann A.H., Kolibaba K.S., Willis S.G., Corbin A.S., Langdon W.S.,
Deininger M.W., Druker B.J.;
"Catalytic domains of tyrosine kinases determine the phosphorylation
sites within c-Cbl.";
FEBS Lett. 577:555-562(2004).
[29]
FUNCTION.
PubMed=15031292; DOI=10.1074/jbc.M311479200;
Perkinton M.S., Standen C.L., Lau K.F., Kesavapany S., Byers H.L.,
Ward M., McLoughlin D.M., Miller C.C.;
"The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to
stimulate Fe65/amyloid precursor protein nuclear signaling.";
J. Biol. Chem. 279:22084-22091(2004).
[30]
REVIEW ON FUNCTION.
PubMed=15686624; DOI=10.1038/sj.cr.7290261;
Shaul Y., Ben-Yehoyada M.;
"Role of c-Abl in the DNA damage stress response.";
Cell Res. 15:33-35(2005).
[31]
FUNCTION.
PubMed=15886098; DOI=10.1016/j.cub.2005.03.049;
Hu H., Bliss J.M., Wang Y., Colicelli J.;
"RIN1 is an ABL tyrosine kinase activator and a regulator of
epithelial-cell adhesion and migration.";
Curr. Biol. 15:815-823(2005).
[32]
FUNCTION, AND INTERACTION WITH CASP9.
PubMed=15657060; DOI=10.1074/jbc.M413787200;
Raina D., Pandey P., Ahmad R., Bharti A., Ren J., Kharbanda S.,
Weichselbaum R., Kufe D.;
"c-Abl tyrosine kinase regulates caspase-9 autocleavage in the
apoptotic response to DNA damage.";
J. Biol. Chem. 280:11147-11151(2005).
[33]
INTERACTION WITH YWHAB; YWHAE; YWHAG; YWHAH; SFN AND YWHAZ,
PHOSPHORYLATION AT THR-735, IDENTIFICATION BY MASS SPECTROMETRY,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-735.
PubMed=15696159; DOI=10.1038/ncb1228;
Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
c-Abl in the apoptotic response to DNA damage.";
Nat. Cell Biol. 7:278-285(2005).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[35]
ACETYLATION AT LYS-711, AND SUBCELLULAR LOCATION.
PubMed=16648821; DOI=10.1038/sj.embor.7400700;
di Bari M.G., Ciuffini L., Mingardi M., Testi R., Soddu S., Barila D.;
"c-Abl acetylation by histone acetyltransferases regulates its
nuclear-cytoplasmic localization.";
EMBO Rep. 7:727-733(2006).
[36]
PHOSPHORYLATION AT TYR-70; TYR-115; TYR-128; TYR-139; TYR-172; TYR-185
TYR-215; TYR-226 AND TYR-393, INTERACTION WITH HCK; LYN AND FYN, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16912036; DOI=10.1074/jbc.M605902200;
Meyn M.A. III, Wilson M.B., Abdi F.A., Fahey N., Schiavone A.P.,
Wu J., Hochrein J.M., Engen J.R., Smithgall T.E.;
"Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and
modulate Bcr-Abl transforming activity.";
J. Biol. Chem. 281:30907-30916(2006).
[37]
FUNCTION.
PubMed=16943190; DOI=10.1074/jbc.M603126200;
Tanos B., Pendergast A.M.;
"Abl tyrosine kinase regulates endocytosis of the epidermal growth
factor receptor.";
J. Biol. Chem. 281:32714-32723(2006).
[38]
FUNCTION, AND INTERACTION WITH PSMA7.
PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007;
Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q.,
Cao C.;
"Interaction between c-Abl and Arg tyrosine kinases and proteasome
subunit PSMA7 regulates proteasome degradation.";
Mol. Cell 22:317-327(2006).
[39]
FUNCTION.
PubMed=17306540; DOI=10.1016/j.cub.2007.01.057;
Boyle S.N., Michaud G.A., Schweitzer B., Predki P.F., Koleske A.J.;
"A critical role for cortactin phosphorylation by Abl-family kinases
in PDGF-induced dorsal-wave formation.";
Curr. Biol. 17:445-451(2007).
[40]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASF3.
PubMed=17623672; DOI=10.1074/jbc.M701484200;
Sossey-Alaoui K., Li X., Cowell J.K.;
"c-Abl-mediated phosphorylation of WAVE3 is required for lamellipodia
formation and cell migration.";
J. Biol. Chem. 282:26257-26265(2007).
[41]
PHOSPHORYLATION AT SER-618 AND SER-619, AND INTERACTION WITH ABI2 AND
CRK.
PubMed=18161990; DOI=10.1021/bi701533j;
Jung J.H., Pendergast A.M., Zipfel P.A., Traugh J.A.;
"Phosphorylation of c-Abl by protein kinase Pak2 regulates
differential binding of ABI2 and CRK.";
Biochemistry 47:1094-1104(2008).
[42]
FUNCTION, AND ENZYME REGULATION.
PubMed=18328268; DOI=10.1016/j.bbamcr.2008.01.028;
Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X.,
Debnath A.K., Cowburn D., Kotula L.;
"Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase
by phosphopeptides derived from Abi1/Hssh3bp1.";
Biochim. Biophys. Acta 1783:737-747(2008).
[43]
FUNCTION.
PubMed=18945674; DOI=10.1074/jbc.M804543200;
Yogalingam G., Pendergast A.M.;
"Abl kinases regulate autophagy by promoting the trafficking and
function of lysosomal components.";
J. Biol. Chem. 283:35941-35953(2008).
[44]
PHOSPHORYLATION AT TYR-70, AND INTERACTION WITH ABI1.
PubMed=18775435; DOI=10.1016/j.jmb.2008.08.040;
Chen S., O'Reilly L.P., Smithgall T.E., Engen J.R.;
"Tyrosine phosphorylation in the SH3 domain disrupts negative
regulatory interactions within the c-Abl kinase core.";
J. Mol. Biol. 383:414-423(2008).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-569; SER-659;
THR-814; THR-844 AND SER-977, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; THR-852 AND
SER-917, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[47]
REVIEW ON FUNCTION.
PubMed=18182299; DOI=10.1016/j.tibs.2007.10.006;
Backert S., Feller S.M., Wessler S.;
"Emerging roles of Abl family tyrosine kinases in microbial
pathogenesis.";
Trends Biochem. Sci. 33:80-90(2008).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[49]
FUNCTION.
PubMed=19891780; DOI=10.1186/1471-2121-10-80;
Fernow I., Tomasovic A., Siehoff-Icking A., Tikkanen R.;
"Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src
kinases.";
BMC Cell Biol. 10:80-80(2009).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[51]
IDENTIFICATION IN A COMPLEX WITH UNC119; ABL2 AND CRK.
PubMed=19381274; DOI=10.1371/journal.pone.0005211;
Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.;
"Unc119 protects from Shigella infection by inhibiting the Abl family
kinases.";
PLoS ONE 4:E5211-E5211(2009).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-569, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[53]
FUNCTION.
PubMed=20417104; DOI=10.1016/j.cub.2010.03.048;
Michael M., Vehlow A., Navarro C., Krause M.;
"c-Abl, Lamellipodin, and Ena/VASP proteins cooperate in dorsal
ruffling of fibroblasts and axonal morphogenesis.";
Curr. Biol. 20:783-791(2010).
[54]
INTERACTION WITH MYLK AND CTTN.
PubMed=20861316; DOI=10.1091/mbc.E09-10-0876;
Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E.,
Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E.,
Imam S.Z., Garcia J.G.N.;
"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain
kinase to regulate endothelial barrier function.";
Mol. Biol. Cell 21:4042-4056(2010).
[55]
REVIEW ON FUNCTION, AND DOMAIN.
PubMed=20841568; DOI=10.1126/scisignal.3139re6;
Colicelli J.;
"ABL tyrosine kinases: evolution of function, regulation, and
specificity.";
Sci. Signal. 3:RE6-RE6(2010).
[56]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[57]
INTERACTION WITH STX17.
PubMed=23006999; DOI=10.1016/j.bbamcr.2012.09.003;
Muppirala M., Gupta V., Swarup G.;
"Tyrosine phosphorylation of a SNARE protein, Syntaxin 17:
Implications for membrane trafficking in the early secretory
pathway.";
Biochim. Biophys. Acta 1823:2109-2119(2012).
[58]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253; TYR-257; TYR-413;
SER-559; SER-569; SER-620; SER-683; SER-718; THR-751; THR-781;
THR-823; THR-844; THR-852; SER-855 AND SER-917, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[59]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[60]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=28428613; DOI=10.1038/s41598-017-00800-w;
Cobbaut M., Derua R., Doeppler H., Lou H.J., Vandoninck S., Storz P.,
Turk B.E., Seufferlein T., Waelkens E., Janssens V., Van Lint J.;
"Differential regulation of PKD isoforms in oxidative stress
conditions through phosphorylation of a conserved Tyr in the P+1
loop.";
Sci. Rep. 7:887-887(2017).
[61]
STRUCTURE BY NMR OF SH2 DOMAIN.
PubMed=1505033; DOI=10.1016/0092-8674(92)90437-H;
Overduin M., Rios C.B., Mayer B.J., Baltimore D., Cowburn D.;
"Three-dimensional solution structure of the src homology 2 domain of
c-abl.";
Cell 70:697-704(1992).
[62]
STRUCTURE BY NMR OF SH2 DOMAIN.
PubMed=1281542; DOI=10.1073/pnas.89.24.11673;
Overduin M., Mayer B.J., Rios C.B., Baltimore D., Cowburn D.;
"Secondary structure of Src homology 2 domain of c-Abl by
heteronuclear NMR spectroscopy in solution.";
Proc. Natl. Acad. Sci. U.S.A. 89:11673-11677(1992).
[63]
3D-STRUCTURE MODELING OF SH3 DOMAIN.
PubMed=7892170; DOI=10.1002/prot.340200302;
Pisabarro M.T., Ortiz A.R., Serrano L., Wade R.C.;
"Homology modeling of the Abl-SH3 domain.";
Proteins 20:203-215(1994).
[64]
STRUCTURE BY NMR OF SH3 DOMAIN.
PubMed=8590002; DOI=10.1016/S0969-2126(01)00243-X;
Gosser Y.Q., Zheng J., Overduin M., Mayer B.J., Cowburn D.;
"The solution structure of Abl SH3, and its relationship to SH2 in the
SH(32) construct.";
Structure 3:1075-1086(1995).
[65]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 64-121.
PubMed=9698566; DOI=10.1006/jmbi.1998.1932;
Pisabarro M.T., Serrano L., Wilmanns M.;
"Crystal structure of the abl-SH3 domain complexed with a designed
high-affinity peptide ligand: implications for SH3-ligand
interactions.";
J. Mol. Biol. 281:513-521(1998).
[66]
STRUCTURE BY NMR OF 62-122 IN COMPLEX WITH CRK.
PubMed=12384576; DOI=10.1073/pnas.212518799;
Donaldson L.W., Gish G., Pawson T., Kay L.E., Forman-Kay J.D.;
"Structure of a regulatory complex involving the Abl SH3 domain, the
Crk SH2 domain, and a Crk-derived phosphopeptide.";
Proc. Natl. Acad. Sci. U.S.A. 99:14053-14058(2002).
[67]
X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS) OF 27-512, MYRISTOYLATION AT
GLY-2 (ISOFORM IB), ENZYME REGULATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12654251; DOI=10.1016/S0092-8674(03)00194-6;
Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D.,
Bornmann W., Clarkson B., Superti-Furga G., Kuriyan J.;
"Structural basis for the autoinhibition of c-Abl tyrosine kinase.";
Cell 112:859-871(2003).
[68]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 229-513 OF MUTANT PRO-396 IN
COMPLEX WITH INHIBITOR VX-680, FUNCTION, AND ENZYME REGULATION.
PubMed=16424036; DOI=10.1158/0008-5472.CAN-05-2788;
Young M.A., Shah N.P., Chao L.H., Seeliger M., Milanov Z.V.,
Biggs W.H. III, Treiber D.K., Patel H.K., Zarrinkar P.P.,
Lockhart D.J., Sawyers C.L., Kuriyan J.;
"Structure of the kinase domain of an imatinib-resistant Abl mutant in
complex with the Aurora kinase inhibitor VX-680.";
Cancer Res. 66:1007-1014(2006).
[69]
X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 38-512, IDENTIFICATION BY
MASS SPECTROMETRY, MYRISTOYLATION AT GLY-2 (ISOFORM IB),
PHOSPHORYLATION AT SER-50, AUTOINHIBITORY MECHANISM, AND ENZYME
REGULATION.
PubMed=16543148; DOI=10.1016/j.molcel.2006.01.035;
Nagar B., Hantschel O., Seeliger M., Davies J.M., Weis W.I.,
Superti-Furga G., Kuriyan J.;
"Organization of the SH3-SH2 unit in active and inactive forms of the
c-Abl tyrosine kinase.";
Mol. Cell 21:787-798(2006).
[70]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 229-512 IN COMPLEXES WITH
ATP-PEPTIDE CONJUGATE, AND CONFORMATION CHANGES DURING ACTIVATION.
PubMed=16640460; DOI=10.1371/journal.pbio.0040144;
Levinson N.M., Kuchment O., Shen K., Young M.A., Koldobskiy M.,
Karplus M., Cole P.A., Kuriyan J.;
"A Src-like inactive conformation in the abl tyrosine kinase domain.";
PLoS Biol. 4:E144-E144(2006).
[71]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 229-500 IN COMPLEXES WITH
IMATINIB AND WITH THE INHIBITORS NVP-AEG082; NVP-AFN941; NVP-AFG210
AND PD180970.
PubMed=17164530; DOI=10.1107/S0907444906047287;
Cowan-Jacob S.W., Fendrich G., Floersheimer A., Furet P.,
Liebetanz J., Rummel G., Rheinberger P., Centeleghe M., Fabbro D.,
Manley P.W.;
"Structural biology contributions to the discovery of drugs to treat
chronic myelogenous leukaemia.";
Acta Crystallogr. D 63:80-93(2007).
[72]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 64-121 OF MUTANT ALA-114 IN
COMPLEX WITH PROLINE-RICH PEPTIDE.
PubMed=17452790; DOI=10.1107/S0907444907011109;
Camara-Artigas A., Palencia A., Martinez J.C., Luque I., Gavira J.A.,
Garcia-Ruiz J.M.;
"Crystallization by capillary counter-diffusion and structure
determination of the N114A mutant of the SH3 domain of Abl tyrosine
kinase complexed with a high-affinity peptide ligand.";
Acta Crystallogr. D 63:646-652(2007).
[73]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 60-121 IN COMPLEX WITH
PROLINE-RICH PEPTIDE P41.
PubMed=19906645; DOI=10.1074/jbc.M109.048033;
Palencia A., Camara-Artigas A., Pisabarro M.T., Martinez J.C.,
Luque I.;
"Role of interfacial water molecules in proline-rich ligand
recognition by the Src homology 3 domain of Abl.";
J. Biol. Chem. 285:2823-2833(2010).
[74]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 121-232 IN COMPLEX WITH
ANTIBODY MIMIC HA4, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20357770; DOI=10.1038/nsmb.1793;
Wojcik J., Hantschel O., Grebien F., Kaupe I., Bennett K.L.,
Barkinge J., Jones R.B., Koide A., Superti-Furga G., Koide S.;
"A potent and highly specific FN3 monobody inhibitor of the Abl SH2
domain.";
Nat. Struct. Mol. Biol. 17:519-527(2010).
[75]
VARIANTS GLY-47; LYS-166; VAL-706; LEU-810 AND LEU-972.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role
in many key processes linked to cell growth and survival such as
cytoskeleton remodeling in response to extracellular stimuli, cell
motility and adhesion, receptor endocytosis, autophagy, DNA damage
response and apoptosis. Coordinates actin remodeling through
tyrosine phosphorylation of proteins controlling cytoskeleton
dynamics like WASF3 (involved in branch formation); ANXA1
(involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH
(involved in signaling); or MAPT and PXN (microtubule-binding
proteins). Phosphorylation of WASF3 is critical for the
stimulation of lamellipodia formation and cell migration. Involved
in the regulation of cell adhesion and motility through
phosphorylation of key regulators of these processes such as
BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple
receptor tyrosine kinases and more particularly promotes
endocytosis of EGFR, facilitates the formation of neuromuscular
synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and
modulates the endocytosis of activated B-cell receptor complexes.
Other substrates which are involved in endocytosis regulation are
the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL
family of ubiquitin ligases that drive receptor down-regulation
and actin remodeling. Phosphorylation of CBL leads to increased
EGFR stability. Involved in late-stage autophagy by regulating
positively the trafficking and function of lysosomal components.
ABL1 targets to mitochondria in response to oxidative stress and
thereby mediates mitochondrial dysfunction and cell death. In
response to oxidative stress, phosphorylates serine/threonine
kinase PRKD2 at 'Tyr-717' (PubMed:28428613). ABL1 is also
translocated in the nucleus where it has DNA-binding activity and
is involved in DNA-damage response and apoptosis. Many substrates
are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6,
RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway
when the DNA damage is too severe to be repaired. Phosphorylates
TP73, a primary regulator for this type of damage-induced
apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and
regulates its processing in the apoptotic response to DNA damage.
Phosphorylates PSMA7 that leads to an inhibition of proteasomal
activity and cell cycle transition blocks. ABL1 acts also as a
regulator of multiple pathological signaling cascades during
infection. Several known tyrosine-phosphorylated microbial
proteins have been identified as ABL1 substrates. This is the case
of A36R of Vaccinia virus, Tir (translocated intimin receptor) of
pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-
associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing
protein A) of A.phagocytophilum. Pathogens can highjack ABL1
kinase signaling to reorganize the host actin cytoskeleton for
multiple purposes, like facilitating intracellular movement and
host cell exit. Finally, functions as its own regulator through
autocatalytic activity as well as through phosphorylation of its
inhibitor, ABI1. {ECO:0000269|PubMed:10391250,
ECO:0000269|PubMed:11971963, ECO:0000269|PubMed:12379650,
ECO:0000269|PubMed:12531427, ECO:0000269|PubMed:12672821,
ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:15556646,
ECO:0000269|PubMed:15657060, ECO:0000269|PubMed:15886098,
ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16678104,
ECO:0000269|PubMed:16943190, ECO:0000269|PubMed:17306540,
ECO:0000269|PubMed:17623672, ECO:0000269|PubMed:18328268,
ECO:0000269|PubMed:18945674, ECO:0000269|PubMed:19891780,
ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:20417104,
ECO:0000269|PubMed:28428613, ECO:0000269|PubMed:9037071,
ECO:0000269|PubMed:9144171, ECO:0000269|PubMed:9461559}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:20357770,
ECO:0000269|PubMed:28428613}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P00520};
-!- ENZYME REGULATION: Stabilized in the inactive form by an
association between the SH3 domain and the SH2-TK linker region,
interactions of the N-terminal cap, and contributions from an N-
terminal myristoyl group and phospholipids. Activated by
autophosphorylation as well as by SRC-family kinase-mediated
phosphorylation. Activated by RIN1 binding to the SH2 and SH3
domains. Also stimulated by cell death inducers and DNA-damage.
Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant
phosphoinositide known to regulate cytoskeletal and membrane
proteins, inhibits also the tyrosine kinase activity (By
similarity). Activated by 5-(1,3-diaryl-1H-pyrazol-4-yl)hydantoin,
5-[3-(4-fluorophenyl)-1-phenyl-1H-pyrazol-4-yl]-2,4-
imidazolidinedione (DPH) (PubMed:28428613). Inhibited by ABI1,
whose activity is controlled by ABL1 itself through tyrosine
phosphorylation. Also inhibited by imatinib mesylate (Gleevec)
which is used for the treatment of chronic myeloid leukemia (CML),
and by VX-680, an inhibitor that acts also on imatinib-resistant
mutants (PubMed:28428613). {ECO:0000250,
ECO:0000269|PubMed:10391250, ECO:0000269|PubMed:12654251,
ECO:0000269|PubMed:16424036, ECO:0000269|PubMed:16543148,
ECO:0000269|PubMed:18328268, ECO:0000269|PubMed:28428613}.
-!- SUBUNIT: Interacts with SORBS1 following insulin stimulation.
Found in a trimolecular complex containing CDK5 and CABLES1.
Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16, ITGB1
and HCK (By similarity). Interacts with STX17; probably
phosphorylates STX17. Interacts with INPPL1/SHIP2. Interacts with
the 14-3-3 proteins, YWHAB, YWHAE, YWHAG, YWHAH, SFN AND YWHAZ;
the interaction with 14-3-3 proteins requires phosphorylation on
Thr-735 and, sequesters ABL1 into the cytoplasm. Interacts with
ABI1, ABI2, BCR, CRK, FGR, FYN, HCK, LYN, PSMA7 RAD9A, RAD51,
RAD52, TP73 and WASF3. A complex made of ABL1, CTTN and MYLK
regulates cortical actin-based cytoskeletal rearrangement critical
to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC)
barrier enhancement. Interacts (via SH3 domain) with CASP9; the
interaction is direct and increases in the response of cells to
genotoxic stress and ABL1/c-Abl activation. Found in a complex
with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK
phosphorylation by ABL kinases. {ECO:0000250,
ECO:0000269|PubMed:10194451, ECO:0000269|PubMed:10391250,
ECO:0000269|PubMed:11374898, ECO:0000269|PubMed:11971963,
ECO:0000269|PubMed:12379650, ECO:0000269|PubMed:12384576,
ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:15657060,
ECO:0000269|PubMed:15696159, ECO:0000269|PubMed:16424036,
ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:16912036,
ECO:0000269|PubMed:17452790, ECO:0000269|PubMed:17623672,
ECO:0000269|PubMed:18161990, ECO:0000269|PubMed:18775435,
ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:19906645,
ECO:0000269|PubMed:20357770, ECO:0000269|PubMed:20861316,
ECO:0000269|PubMed:23006999, ECO:0000269|PubMed:9144171,
ECO:0000269|PubMed:9461559}.
-!- INTERACTION:
Q8IZP0:ABI1; NbExp=11; IntAct=EBI-375543, EBI-375446;
Q9NYB9:ABI2; NbExp=2; IntAct=EBI-375543, EBI-743598;
P10275:AR; NbExp=2; IntAct=EBI-375543, EBI-608057;
Q13315:ATM; NbExp=4; IntAct=EBI-375543, EBI-495465;
Q4KMG0:CDON; NbExp=2; IntAct=EBI-375543, EBI-7016840;
O35158:Cdon (xeno); NbExp=4; IntAct=EBI-375543, EBI-7016767;
P46108:CRK; NbExp=2; IntAct=EBI-375543, EBI-886;
P46109:CRKL; NbExp=3; IntAct=EBI-375543, EBI-910;
P35222:CTNNB1; NbExp=2; IntAct=EBI-375543, EBI-491549;
P00533:EGFR; NbExp=2; IntAct=EBI-375543, EBI-297353;
P04626:ERBB2; NbExp=2; IntAct=EBI-375543, EBI-641062;
Q14315:FLNC; NbExp=2; IntAct=EBI-375543, EBI-489954;
P05107:ITGB2; NbExp=4; IntAct=EBI-375543, EBI-300173;
P10721:KIT; NbExp=2; IntAct=EBI-375543, EBI-1379503;
Q38SD2:LRRK1; NbExp=3; IntAct=EBI-375543, EBI-1050422;
Q92918:MAP4K1; NbExp=3; IntAct=EBI-375543, EBI-881;
Q7Z434:MAVS; NbExp=6; IntAct=EBI-375543, EBI-995373;
O43196:MSH5; NbExp=10; IntAct=EBI-375543, EBI-6092730;
P15941:MUC1; NbExp=8; IntAct=EBI-375543, EBI-2804728;
P16333:NCK1; NbExp=2; IntAct=EBI-375543, EBI-389883;
O43900:PRICKLE3; NbExp=2; IntAct=EBI-375543, EBI-1751761;
Q13905:RAPGEF1; NbExp=4; IntAct=EBI-375543, EBI-976876;
Q86UR5:RIMS1; NbExp=2; IntAct=EBI-375543, EBI-1043236;
Q13671:RIN1; NbExp=4; IntAct=EBI-375543, EBI-366017;
P31947:SFN; NbExp=2; IntAct=EBI-375543, EBI-476295;
Q15464:SHB; NbExp=5; IntAct=EBI-375543, EBI-4402156;
O75751:SLC22A3; NbExp=2; IntAct=EBI-375543, EBI-1752674;
P37840:SNCA; NbExp=6; IntAct=EBI-5278159, EBI-985879;
Q9BX66:SORBS1; NbExp=2; IntAct=EBI-375543, EBI-433642;
O60504-2:SORBS3; NbExp=5; IntAct=EBI-375543, EBI-1222956;
Q07890:SOS2; NbExp=2; IntAct=EBI-375543, EBI-298181;
P12931:SRC; NbExp=2; IntAct=EBI-375543, EBI-621482;
Q9Y4G6:TLN2; NbExp=3; IntAct=EBI-375543, EBI-1220811;
P11387:TOP1; NbExp=7; IntAct=EBI-375543, EBI-876302;
P15498:VAV1; NbExp=5; IntAct=EBI-375543, EBI-625518;
P63104:YWHAZ; NbExp=3; IntAct=EBI-375543, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus.
Mitochondrion {ECO:0000250}. Note=Shuttles between the nucleus and
cytoplasm depending on environmental signals. Sequestered into the
cytoplasm through interaction with 14-3-3 proteins. Localizes to
mitochondria in response to oxidative stress (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform IB: Nucleus membrane; Lipid-anchor.
Note=The myristoylated c-ABL protein is reported to be nuclear.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=IA;
IsoId=P00519-1; Sequence=Displayed;
Name=IB;
IsoId=P00519-2; Sequence=VSP_004957;
Note=Contains a N-myristoyl glycine at position 2.;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- PTM: Acetylated at Lys-711 by EP300 which promotes the cytoplasmic
translocation. {ECO:0000269|PubMed:16648821}.
-!- PTM: Phosphorylation at Tyr-70 by members of the SRC family of
kinases disrupts SH3 domain-based autoinhibitory interactions and
intermolecular associations, such as that with ABI1, and also
enhances kinase activity. Phosphorylation at Tyr-226 and Tyr-393
correlate with increased activity. DNA damage-induced activation
of ABL1 requires the function of ATM and Ser-446 phosphorylation
(By similarity). Phosphorylation at Ser-569 has been attributed to
a CDC2-associated kinase and is coupled to cell division (By
similarity). Phosphorylation at Ser-618 and Ser-619 by PAK2
increases binding to CRK and reduces binding to ABI1.
Phosphorylation on Thr-735 is required for binding 14-3-3 proteins
for cytoplasmic translocation. Phosphorylated by PRKDC (By
similarity). {ECO:0000250}.
-!- PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to
degradation. {ECO:0000269|PubMed:12475393}.
-!- DISEASE: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal
myeloproliferative disorder of a pluripotent stem cell with a
specific cytogenetic abnormality, the Philadelphia chromosome
(Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid,
and sometimes T-lymphoid cells, but not marrow fibroblasts.
Note=The gene represented in this entry is involved in disease
pathogenesis.
-!- DISEASE: Note=A chromosomal aberration involving ABL1 has been
found in patients with chronic myeloid leukemia. Translocation
t(9;22)(q34;q11) with BCR. The translocation produces a BCR-ABL
found also in acute myeloid leukemia (AML) and acute lymphoblastic
leukemia (ALL).
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. ABL subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ABLID1.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/abl1/";
-----------------------------------------------------------------------
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EMBL; M14752; AAA51561.1; -; mRNA.
EMBL; X16416; CAA34438.1; -; mRNA.
EMBL; U07563; AAB60394.1; -; Genomic_DNA.
EMBL; U07563; AAB60393.1; -; Genomic_DNA.
EMBL; U07561; AAB60393.1; JOINED; Genomic_DNA.
EMBL; DQ145721; AAZ38718.1; -; Genomic_DNA.
EMBL; AL359092; CAM45752.1; -; Genomic_DNA.
EMBL; AL161733; CAM45752.1; JOINED; Genomic_DNA.
EMBL; AL161733; CAM45754.1; -; Genomic_DNA.
EMBL; AL161733; CAM45756.1; -; Genomic_DNA.
EMBL; AL359092; CAM45756.1; JOINED; Genomic_DNA.
EMBL; CH471090; EAW87948.1; -; Genomic_DNA.
EMBL; BC117451; AAI17452.1; -; mRNA.
EMBL; S69223; AAD14034.1; -; Genomic_DNA.
CCDS; CCDS35165.1; -. [P00519-2]
CCDS; CCDS35166.1; -. [P00519-1]
PIR; S08519; TVHUA.
RefSeq; NP_005148.2; NM_005157.5. [P00519-1]
RefSeq; NP_009297.2; NM_007313.2. [P00519-2]
UniGene; Hs.431048; -.
PDB; 1AB2; NMR; -; A=120-220.
PDB; 1ABL; Model; -; A=65-121.
PDB; 1AWO; NMR; -; A=65-119.
PDB; 1BBZ; X-ray; 1.65 A; A/C/E/G=64-121.
PDB; 1JU5; NMR; -; C=62-122.
PDB; 1OPL; X-ray; 3.42 A; A/B=27-512.
PDB; 1ZZP; NMR; -; A=1007-1130.
PDB; 2ABL; X-ray; 2.50 A; A=57-218.
PDB; 2E2B; X-ray; 2.20 A; A/B=229-515.
PDB; 2F4J; X-ray; 1.91 A; A=229-513.
PDB; 2FO0; X-ray; 2.27 A; A=38-512.
PDB; 2G1T; X-ray; 1.80 A; A/B/C/D=229-512.
PDB; 2G2F; X-ray; 2.70 A; A/B=229-512.
PDB; 2G2H; X-ray; 2.00 A; A/B=229-512.
PDB; 2G2I; X-ray; 3.12 A; A/B=229-512.
PDB; 2GQG; X-ray; 2.40 A; A/B=229-500.
PDB; 2HIW; X-ray; 2.20 A; A/B=230-512.
PDB; 2HYY; X-ray; 2.40 A; A/B/C/D=228-500.
PDB; 2HZ0; X-ray; 2.10 A; A/B=228-497.
PDB; 2HZ4; X-ray; 2.80 A; A/B/C=228-500.
PDB; 2HZI; X-ray; 1.70 A; A/B=229-500.
PDB; 2O88; X-ray; 1.75 A; A/B=64-121.
PDB; 2V7A; X-ray; 2.50 A; A/B=229-512.
PDB; 3CS9; X-ray; 2.21 A; A/B/C/D=229-500.
PDB; 3EG0; X-ray; 2.30 A; A=60-121.
PDB; 3EG1; X-ray; 1.85 A; A/B=60-121.
PDB; 3EG2; X-ray; 1.80 A; A=60-121.
PDB; 3EG3; X-ray; 1.40 A; A=60-121.
PDB; 3EGU; X-ray; 2.25 A; A=60-121.
PDB; 3K2M; X-ray; 1.75 A; A/B=121-232.
PDB; 3PYY; X-ray; 1.85 A; A/B=229-512.
PDB; 3QRI; X-ray; 2.10 A; A/B=229-499.
PDB; 3QRJ; X-ray; 1.82 A; A/B=229-499.
PDB; 3QRK; X-ray; 2.30 A; A=229-499.
PDB; 3T04; X-ray; 2.10 A; A=112-232.
PDB; 3UE4; X-ray; 2.42 A; A/B=229-512.
PDB; 3UYO; X-ray; 1.83 A; A=112-232.
PDB; 4J9B; X-ray; 1.70 A; A=60-121.
PDB; 4J9C; X-ray; 1.05 A; A=60-121.
PDB; 4J9D; X-ray; 1.50 A; A/C/E=60-121.
PDB; 4J9E; X-ray; 1.40 A; A/C/E=60-121.
PDB; 4J9F; X-ray; 1.09 A; A/C/E=60-121.
PDB; 4J9G; X-ray; 1.80 A; A/C/E=60-121.
PDB; 4J9H; X-ray; 1.70 A; A/B/C/D/E/F=60-121.
PDB; 4J9I; X-ray; 2.20 A; A/C/E=60-121.
PDB; 4JJB; X-ray; 1.65 A; A=60-121.
PDB; 4JJC; X-ray; 1.60 A; A=60-121.
PDB; 4JJD; X-ray; 1.60 A; A=60-121.
PDB; 4TWP; X-ray; 2.40 A; A/B=233-503.
PDB; 4WA9; X-ray; 2.20 A; A/B=246-512.
PDB; 4XEY; X-ray; 2.89 A; A/B=119-515.
PDB; 4YC8; X-ray; 2.90 A; A/B=229-512.
PDB; 4ZOG; X-ray; 2.30 A; A/B=229-511.
PDB; 5DC0; X-ray; 2.23 A; B=112-232.
PDB; 5DC4; X-ray; 1.48 A; A=112-232.
PDB; 5DC9; X-ray; 1.56 A; A=112-232.
PDB; 5HU9; X-ray; 1.53 A; A=229-500.
PDB; 5MO4; X-ray; 2.17 A; A=27-515.
PDB; 5OAZ; X-ray; 1.03 A; A/B=60-121.
PDBsum; 1AB2; -.
PDBsum; 1ABL; -.
PDBsum; 1AWO; -.
PDBsum; 1BBZ; -.
PDBsum; 1JU5; -.
PDBsum; 1OPL; -.
PDBsum; 1ZZP; -.
PDBsum; 2ABL; -.
PDBsum; 2E2B; -.
PDBsum; 2F4J; -.
PDBsum; 2FO0; -.
PDBsum; 2G1T; -.
PDBsum; 2G2F; -.
PDBsum; 2G2H; -.
PDBsum; 2G2I; -.
PDBsum; 2GQG; -.
PDBsum; 2HIW; -.
PDBsum; 2HYY; -.
PDBsum; 2HZ0; -.
PDBsum; 2HZ4; -.
PDBsum; 2HZI; -.
PDBsum; 2O88; -.
PDBsum; 2V7A; -.
PDBsum; 3CS9; -.
PDBsum; 3EG0; -.
PDBsum; 3EG1; -.
PDBsum; 3EG2; -.
PDBsum; 3EG3; -.
PDBsum; 3EGU; -.
PDBsum; 3K2M; -.
PDBsum; 3PYY; -.
PDBsum; 3QRI; -.
PDBsum; 3QRJ; -.
PDBsum; 3QRK; -.
PDBsum; 3T04; -.
PDBsum; 3UE4; -.
PDBsum; 3UYO; -.
PDBsum; 4J9B; -.
PDBsum; 4J9C; -.
PDBsum; 4J9D; -.
PDBsum; 4J9E; -.
PDBsum; 4J9F; -.
PDBsum; 4J9G; -.
PDBsum; 4J9H; -.
PDBsum; 4J9I; -.
PDBsum; 4JJB; -.
PDBsum; 4JJC; -.
PDBsum; 4JJD; -.
PDBsum; 4TWP; -.
PDBsum; 4WA9; -.
PDBsum; 4XEY; -.
PDBsum; 4YC8; -.
PDBsum; 4ZOG; -.
PDBsum; 5DC0; -.
PDBsum; 5DC4; -.
PDBsum; 5DC9; -.
PDBsum; 5HU9; -.
PDBsum; 5MO4; -.
PDBsum; 5OAZ; -.
ProteinModelPortal; P00519; -.
SMR; P00519; -.
BioGrid; 106543; 187.
CORUM; P00519; -.
DIP; DIP-1042N; -.
IntAct; P00519; 226.
MINT; MINT-7236141; -.
STRING; 9606.ENSP00000361423; -.
BindingDB; P00519; -.
ChEMBL; CHEMBL1862; -.
DrugBank; DB08043; 1-[4-(PYRIDIN-4-YLOXY)PHENYL]-3-[3-(TRIFLUOROMETHYL)PHENYL]UREA.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB06616; Bosutinib.
DrugBank; DB01254; Dasatinib.
DrugBank; DB00619; Imatinib.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB03878; N-[4-Methyl-3-[[4-(3-Pyridinyl)-2-Pyrimidinyl]Amino]Phenyl]-3-Pyridinecarboxamide.
DrugBank; DB04868; Nilotinib.
DrugBank; DB08901; Ponatinib.
DrugBank; DB12323; Radotinib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB05184; XL228.
GuidetoPHARMACOLOGY; 1923; -.
iPTMnet; P00519; -.
PhosphoSitePlus; P00519; -.
BioMuta; ABL1; -.
DMDM; 85681908; -.
EPD; P00519; -.
MaxQB; P00519; -.
PaxDb; P00519; -.
PeptideAtlas; P00519; -.
PRIDE; P00519; -.
DNASU; 25; -.
Ensembl; ENST00000318560; ENSP00000323315; ENSG00000097007. [P00519-1]
Ensembl; ENST00000372348; ENSP00000361423; ENSG00000097007. [P00519-2]
GeneID; 25; -.
KEGG; hsa:25; -.
UCSC; uc004bzv.4; human. [P00519-1]
CTD; 25; -.
DisGeNET; 25; -.
EuPathDB; HostDB:ENSG00000097007.17; -.
GeneCards; ABL1; -.
HGNC; HGNC:76; ABL1.
HPA; CAB002686; -.
HPA; HPA027251; -.
HPA; HPA027280; -.
HPA; HPA028409; -.
MalaCards; ABL1; -.
MIM; 189980; gene.
MIM; 608232; phenotype.
neXtProt; NX_P00519; -.
OpenTargets; ENSG00000097007; -.
Orphanet; 521; Chronic myeloid leukemia.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
PharmGKB; PA24413; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOVERGEN; HBG004162; -.
InParanoid; P00519; -.
KO; K06619; -.
OMA; GAFRESG; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P00519; -.
TreeFam; TF105081; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-375170; CDO in myogenesis.
Reactome; R-HSA-428890; Role of Abl in Robo-Slit signaling.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P00519; -.
SIGNOR; P00519; -.
ChiTaRS; ABL1; human.
EvolutionaryTrace; P00519; -.
GeneWiki; ABL_(gene); -.
GenomeRNAi; 25; -.
PMAP-CutDB; P00519; -.
PRO; PR:P00519; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000097007; -.
CleanEx; HS_ABL1; -.
ExpressionAtlas; P00519; baseline and differential.
Genevisible; P00519; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030425; C:dendrite; ISS:ARUK-UCL.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; NAS:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
GO; GO:0043234; C:protein complex; IPI:CAFA.
GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
GO; GO:0003785; F:actin monomer binding; TAS:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0046875; F:ephrin receptor binding; ISS:ARUK-UCL.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:BHF-UCL.
GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL.
GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; TAS:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0070064; F:proline-rich region binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0005080; F:protein kinase C binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0042169; F:SH2 domain binding; IPI:CAFA.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0090135; P:actin filament branching; IEA:Ensembl.
GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
GO; GO:1990051; P:activation of protein kinase C activity; IDA:ParkinsonsUK-UCL.
GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0002322; P:B cell proliferation involved in immune response; IEA:Ensembl.
GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0001922; P:B-1 B cell homeostasis; IEA:Ensembl.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0072358; P:cardiovascular system development; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; TAS:ParkinsonsUK-UCL.
GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:1903351; P:cellular response to dopamine; TAS:ParkinsonsUK-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:ParkinsonsUK-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:ParkinsonsUK-UCL.
GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl.
GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; IDA:UniProtKB.
GO; GO:0043542; P:endothelial cell migration; IMP:BHF-UCL.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; TAS:UniProtKB.
GO; GO:0030035; P:microspike assembly; IEA:Ensembl.
GO; GO:0006298; P:mismatch repair; TAS:ProtInc.
GO; GO:0051882; P:mitochondrial depolarization; TAS:ParkinsonsUK-UCL.
GO; GO:0000278; P:mitotic cell cycle; TAS:ParkinsonsUK-UCL.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:1900275; P:negative regulation of phospholipase C activity; IMP:MGI.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:MGI.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0060563; P:neuroepithelial cell differentiation; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0038189; P:neuropilin signaling pathway; IMP:BHF-UCL.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:BHF-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IMP:UniProtKB.
GO; GO:1905555; P:positive regulation blood vessel branching; IEA:Ensembl.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
GO; GO:1904531; P:positive regulation of actin filament binding; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:MGI.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; IEA:Ensembl.
GO; GO:1900042; P:positive regulation of interleukin-2 secretion; IEA:Ensembl.
GO; GO:1904528; P:positive regulation of microtubule binding; IMP:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IEA:Ensembl.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:BHF-UCL.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:BHF-UCL.
GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IMP:BHF-UCL.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; TAS:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; TAS:UniProtKB.
GO; GO:0030516; P:regulation of axon extension; IMP:UniProtKB.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL.
GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0030100; P:regulation of endocytosis; TAS:UniProtKB.
GO; GO:1903053; P:regulation of extracellular matrix organization; IEA:Ensembl.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0031113; P:regulation of microtubule polymerization; IMP:UniProtKB.
GO; GO:1905244; P:regulation of modification of synaptic structure; ISS:ARUK-UCL.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0006979; P:response to oxidative stress; IGI:MGI.
GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:UniProtKB.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0002333; P:transitional one stage B cell differentiation; IEA:Ensembl.
CDD; cd09935; SH2_ABL; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR033221; ABL1.
InterPro; IPR035837; ABL_SH2.
InterPro; IPR015015; F-actin_binding.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
PANTHER; PTHR24418:SF88; PTHR24418:SF88; 1.
Pfam; PF08919; F_actin_bind; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00808; FABD; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Autophagy; Cell adhesion; Chromosomal rearrangement;
Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
DNA-binding; Endocytosis; Kinase; Lipoprotein; Magnesium; Manganese;
Membrane; Metal-binding; Mitochondrion; Myristate; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase; Ubl conjugation.
CHAIN 1 1130 Tyrosine-protein kinase ABL1.
/FTId=PRO_0000088050.
DOMAIN 61 121 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 127 217 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 242 493 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 248 256 ATP.
NP_BIND 316 322 ATP.
REGION 1 60 CAP.
REGION 869 968 DNA-binding. {ECO:0000250}.
REGION 953 1130 F-actin-binding.
MOTIF 381 405 Kinase activation loop.
MOTIF 605 609 Nuclear localization signal 1.
{ECO:0000255}.
MOTIF 709 715 Nuclear localization signal 2.
{ECO:0000255}.
MOTIF 762 769 Nuclear localization signal 3.
{ECO:0000255}.
MOTIF 1090 1100 Nuclear export signal. {ECO:0000250}.
COMPBIAS 18 22 Poly-Ser.
COMPBIAS 605 609 Poly-Lys.
COMPBIAS 782 1019 Pro-rich.
COMPBIAS 897 903 Poly-Pro.
ACT_SITE 363 363 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 271 271 ATP.
SITE 26 27 Breakpoint for translocation to form BCR-
ABL oncogene.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:16543148}.
MOD_RES 70 70 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16912036,
ECO:0000269|PubMed:18775435}.
MOD_RES 115 115 Phosphotyrosine.
{ECO:0000269|PubMed:16912036}.
MOD_RES 128 128 Phosphotyrosine.
{ECO:0000269|PubMed:16912036}.
MOD_RES 139 139 Phosphotyrosine.
{ECO:0000269|PubMed:16912036}.
MOD_RES 172 172 Phosphotyrosine.
{ECO:0000269|PubMed:16912036}.
MOD_RES 185 185 Phosphotyrosine.
{ECO:0000269|PubMed:16912036}.
MOD_RES 215 215 Phosphotyrosine.
{ECO:0000269|PubMed:16912036}.
MOD_RES 226 226 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16912036}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 253 253 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 257 257 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 393 393 Phosphotyrosine; by autocatalysis and
SRC-type Tyr-kinases.
{ECO:0000269|PubMed:16912036}.
MOD_RES 413 413 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000250|UniProtKB:P00520}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 618 618 Phosphoserine; by PAK2.
{ECO:0000269|PubMed:18161990}.
MOD_RES 619 619 Phosphoserine; by PAK2.
{ECO:0000269|PubMed:18161990}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 711 711 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:16648821}.
MOD_RES 718 718 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 735 735 Phosphothreonine.
{ECO:0000269|PubMed:15696159}.
MOD_RES 751 751 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 781 781 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 814 814 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 823 823 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 844 844 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 852 852 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 855 855 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 917 917 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 977 977 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VAR_SEQ 1 26 MLEICLKLVGCKSKKGLSSSSSCYLE -> MGQQPGKVLGD
QRRPSLPALHFIKGAGKKESSRHGGPHCNVFVEH (in
isoform IB).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004957.
VARIANT 47 47 R -> G (in a lung large cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_032676.
VARIANT 140 140 L -> P (in dbSNP:rs1064152).
{ECO:0000269|PubMed:3021337}.
/FTId=VAR_051692.
VARIANT 166 166 R -> K (in a melanoma sample; somatic
mutation). {ECO:0000269|PubMed:17344846}.
/FTId=VAR_032677.
VARIANT 247 247 K -> R (in dbSNP:rs34549764).
/FTId=VAR_051693.
VARIANT 706 706 G -> V (in dbSNP:rs34634745).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.4}.
/FTId=VAR_025043.
VARIANT 810 810 P -> L (in dbSNP:rs2229071).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_032678.
VARIANT 852 852 T -> P. {ECO:0000269|Ref.4}.
/FTId=VAR_025044.
VARIANT 900 900 P -> S (in dbSNP:rs35266696).
{ECO:0000269|Ref.4}.
/FTId=VAR_025045.
VARIANT 968 968 S -> P (in dbSNP:rs1064165).
/FTId=VAR_051694.
VARIANT 972 972 S -> L (in dbSNP:rs2229067).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.4}.
/FTId=VAR_025046.
MUTAGEN 735 735 T->A: Abolishes phosphorylation. Loss of
binding YWHAS and YWHAZ. Localizes to the
nucleus. No effect on kinase activity.
{ECO:0000269|PubMed:15696159}.
CONFLICT 159 159 G -> S (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 424 425 AF -> GK (in Ref. 9). {ECO:0000305}.
CONFLICT 445 445 L -> R (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 459 459 E -> K (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 520 520 S -> T (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 719 719 A -> V (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 837 837 G -> E (in Ref. 2; CAA34438).
{ECO:0000305}.
CONFLICT 837 837 G -> W (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 863 863 G -> R (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 894 894 R -> K (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 917 919 SPS -> RPG (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 952 952 G -> A (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 967 968 QS -> HP (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 982 982 P -> PL (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 1022 1022 Missing (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 1045 1045 R -> G (in Ref. 1; AAA51561).
{ECO:0000305}.
CONFLICT 1103 1103 T -> S (in Ref. 1; AAA51561).
{ECO:0000305}.
HELIX 49 53 {ECO:0000244|PDB:2FO0}.
HELIX 58 60 {ECO:0000244|PDB:2FO0}.
STRAND 65 70 {ECO:0000244|PDB:4J9C}.
STRAND 76 79 {ECO:0000244|PDB:3EG3}.
STRAND 87 93 {ECO:0000244|PDB:4J9C}.
STRAND 97 104 {ECO:0000244|PDB:4J9C}.
STRAND 107 112 {ECO:0000244|PDB:4J9C}.
HELIX 113 115 {ECO:0000244|PDB:4J9C}.
STRAND 116 118 {ECO:0000244|PDB:4J9C}.
HELIX 122 124 {ECO:0000244|PDB:5DC4}.
STRAND 128 131 {ECO:0000244|PDB:5DC4}.
HELIX 134 140 {ECO:0000244|PDB:5DC4}.
TURN 141 143 {ECO:0000244|PDB:5DC4}.
STRAND 148 153 {ECO:0000244|PDB:5DC4}.
STRAND 155 157 {ECO:0000244|PDB:5DC4}.
STRAND 161 167 {ECO:0000244|PDB:5DC4}.
STRAND 170 175 {ECO:0000244|PDB:5DC4}.
STRAND 177 179 {ECO:0000244|PDB:4XEY}.
TURN 180 182 {ECO:0000244|PDB:4XEY}.
STRAND 184 187 {ECO:0000244|PDB:5DC4}.
STRAND 190 194 {ECO:0000244|PDB:5DC4}.
HELIX 195 202 {ECO:0000244|PDB:5DC4}.
STRAND 209 211 {ECO:0000244|PDB:5DC4}.
STRAND 226 228 {ECO:0000244|PDB:5MO4}.
STRAND 229 231 {ECO:0000244|PDB:2GQG}.
TURN 233 235 {ECO:0000244|PDB:2G1T}.
HELIX 239 241 {ECO:0000244|PDB:5HU9}.
STRAND 242 247 {ECO:0000244|PDB:5HU9}.
HELIX 248 251 {ECO:0000244|PDB:5HU9}.
STRAND 254 261 {ECO:0000244|PDB:5HU9}.
HELIX 262 264 {ECO:0000244|PDB:5HU9}.
STRAND 266 271 {ECO:0000244|PDB:5HU9}.
TURN 275 277 {ECO:0000244|PDB:5HU9}.
HELIX 280 290 {ECO:0000244|PDB:5HU9}.
STRAND 301 305 {ECO:0000244|PDB:5HU9}.
STRAND 307 310 {ECO:0000244|PDB:5HU9}.
STRAND 312 316 {ECO:0000244|PDB:5HU9}.
STRAND 319 322 {ECO:0000244|PDB:2HZI}.
HELIX 323 329 {ECO:0000244|PDB:5HU9}.
TURN 332 334 {ECO:0000244|PDB:5HU9}.
HELIX 337 356 {ECO:0000244|PDB:5HU9}.
STRAND 359 361 {ECO:0000244|PDB:2G2H}.
HELIX 366 368 {ECO:0000244|PDB:5HU9}.
STRAND 369 371 {ECO:0000244|PDB:5HU9}.
HELIX 373 375 {ECO:0000244|PDB:5HU9}.
STRAND 377 379 {ECO:0000244|PDB:5HU9}.
HELIX 381 383 {ECO:0000244|PDB:2G2F}.
HELIX 384 387 {ECO:0000244|PDB:2G1T}.
HELIX 390 392 {ECO:0000244|PDB:2G1T}.
STRAND 393 396 {ECO:0000244|PDB:3QRJ}.
STRAND 399 401 {ECO:0000244|PDB:5HU9}.
HELIX 403 405 {ECO:0000244|PDB:5HU9}.
HELIX 408 413 {ECO:0000244|PDB:5HU9}.
HELIX 418 433 {ECO:0000244|PDB:5HU9}.
HELIX 445 447 {ECO:0000244|PDB:5HU9}.
HELIX 448 453 {ECO:0000244|PDB:5HU9}.
HELIX 466 475 {ECO:0000244|PDB:5HU9}.
HELIX 480 482 {ECO:0000244|PDB:5HU9}.
HELIX 486 496 {ECO:0000244|PDB:5HU9}.
STRAND 498 500 {ECO:0000244|PDB:1OPL}.
HELIX 503 506 {ECO:0000244|PDB:2G1T}.
TURN 510 512 {ECO:0000244|PDB:2F4J}.
HELIX 1029 1045 {ECO:0000244|PDB:1ZZP}.
TURN 1046 1048 {ECO:0000244|PDB:1ZZP}.
HELIX 1053 1070 {ECO:0000244|PDB:1ZZP}.
HELIX 1071 1073 {ECO:0000244|PDB:1ZZP}.
HELIX 1080 1097 {ECO:0000244|PDB:1ZZP}.
STRAND 1101 1104 {ECO:0000244|PDB:1ZZP}.
STRAND 1106 1108 {ECO:0000244|PDB:1ZZP}.
HELIX 1115 1128 {ECO:0000244|PDB:1ZZP}.
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


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