ID ABL2_HUMAN Reviewed; 1182 AA.
AC P42684; A0M8X0; B7UEF2; B7UEF3; B7UEF4; B7UEF5; Q5T0X6; Q5W0C5; Q6NZY6;
AC Q7Z301;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 242.
DE RecName: Full=Tyrosine-protein kinase ABL2;
DE EC=2.7.10.2;
DE AltName: Full=Abelson murine leukemia viral oncogene homolog 2;
DE AltName: Full=Abelson tyrosine-protein kinase 2;
DE AltName: Full=Abelson-related gene protein;
DE AltName: Full=Tyrosine-protein kinase ARG;
GN Name=ABL2; Synonyms=ABLL, ARG;
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 1), AND ALTERNATIVE SPLICING (ISOFORM
RP 2).
RX PubMed=2198571; DOI=10.1073/pnas.87.15.5802;
RA Kruh G.D., Perego R., Miki T., Aaronson S.A.;
RT "The complete coding sequence of arg defines the Abelson subfamily of
RT cytoplasmic tyrosine kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5802-5806(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7), ALTERNATIVE SPLICING
RP (ISOFORM 10), AND VARIANT THR-12 (ISOFORM 4).
RX PubMed=18810762; DOI=10.1002/jcb.21922;
RA Bianchi C., Torsello B., Angeloni V., Bombelli S., Soldi M., Invernizzi L.,
RA Brambilla P., Perego R.A.;
RT "Eight full-length abelson related gene (Arg) isoforms are constitutively
RT expressed in caki-1 cell line and cell distribution of two isoforms has
RT been analyzed after transfection.";
RL J. Cell. Biochem. 105:1219-1227(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-930; MET-946; ARG-996;
RP ASN-1085 AND ALA-1101.
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 343-469.
RX PubMed=3787260; DOI=10.1126/science.3787260;
RA Kruh G.D., King C.R., Kraus M.H., Popescu N.C., Amsbaugh S.C.,
RA McBride W.O., Aaronson S.A.;
RT "A novel human gene closely related to the abl proto-oncogene.";
RL Science 234:1545-1548(1986).
RN [10]
RP PHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND TYR-683, AND ACTIVITY
RP REGULATION.
RX PubMed=12748290; DOI=10.1128/mcb.23.11.3884-3896.2003;
RA Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.;
RT "Two distinct phosphorylation pathways have additive effects on Abl family
RT kinase activation.";
RL Mol. Cell. Biol. 23:3884-3896(2003).
RN [11]
RP INTERACTION WITH RIN1, FUNCTION, AND ACTIVITY REGULATION.
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 [12]
RP FUNCTION, PHOSPHORYLATION AT TYR-261, AND UBIQUITINATION.
RX PubMed=15735735; DOI=10.1038/sj.onc.1208454;
RA Cao C., Li Y., Leng Y., Li P., Ma Q., Kufe D.;
RT "Ubiquitination and degradation of the Arg tyrosine kinase is regulated by
RT oxidative stress.";
RL Oncogene 24:2433-2440(2005).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [17]
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 [18]
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 [19]
RP REVIEW ON FUNCTION.
RX PubMed=14729179; DOI=10.1016/j.tcb.2003.11.003;
RA Hernandez S.E., Krishnaswami M., Miller A.L., Koleske A.J.;
RT "How do Abl family kinases regulate cell shape and movement?";
RL Trends Cell Biol. 14:36-44(2004).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-915, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-633;
RP SER-655; SER-817; SER-820 AND SER-936, AND IDENTIFICATION BY MASS
RP 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 [22]
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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-718, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT TYR-668 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT TYR-647 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP TYR-683 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-662
RP (ISOFORM 7), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [25]
RP IDENTIFICATION IN A COMPLEX WITH UNC119: ABL1 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-936, 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-936, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-655;
RP SER-671; SER-783; SER-817; SER-820 AND SER-936, 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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620 AND SER-631, AND
RP IDENTIFICATION BY 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 [32]
RP STRUCTURE BY NMR OF 163-268.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the human ABL2 SH2 domain.";
RL Submitted (FEB-2008) to the PDB data bank.
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 279-546 IN COMPLEXES WITH
RP INHIBITORS.
RX PubMed=21417343; DOI=10.1021/jm101506n;
RA Salah E., Ugochukwu E., Barr A.J., von Delft F., Knapp S., Elkins J.M.;
RT "Crystal structures of ABL-related gene (ABL2) in complex with imatinib,
RT tozasertib (VX-680), and a type I inhibitor of the triazole carbothioamide
RT class.";
RL J. Med. Chem. 54:2359-2367(2011).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 563-579 IN COMPLEX WITH CTTN, AND
RP INTERACTION WITH CTTN.
RX PubMed=22297987; DOI=10.1107/s1744309111056132;
RA Liu W., MacGrath S.M., Koleske A.J., Boggon T.J.;
RT "Lysozyme contamination facilitates crystallization of a heterotrimeric
RT cortactin-Arg-lysozyme complex.";
RL Acta Crystallogr. F 68:154-158(2012).
RN [35]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-78; GLN-99; ILE-519; SER-769; ARG-930
RP AND ARG-996, AND VARIANT [LARGE SCALE ANALYSIS] THR-12 (ISOFORM 4).
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).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1-
CC overlapping role in key processes linked to cell growth and survival
CC such as cytoskeleton remodeling in response to extracellular stimuli,
CC cell motility and adhesion and receptor endocytosis. Coordinates actin
CC remodeling through tyrosine phosphorylation of proteins controlling
CC cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved
CC in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly
CC F-actin and regulates actin cytoskeletal structure through its F-actin-
CC bundling activity. Involved in the regulation of cell adhesion and
CC motility through phosphorylation of key regulators of these processes
CC such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation
CC of ARHGAP35 promotes its association with RASA1, resulting in
CC recruitment of ARHGAP35 to the cell periphery where it inhibits RHO.
CC Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other
CC substrates which are involved in endocytosis regulation such as RIN1.
CC In brain, may regulate neurotransmission by phosphorylating proteins at
CC the synapse. ABL2 acts also as a regulator of multiple pathological
CC signaling cascades during infection. Pathogens can highjack ABL2 kinase
CC signaling to reorganize the host actin cytoskeleton for multiple
CC purposes, like facilitating intracellular movement and host cell exit.
CC Finally, functions as its own regulator through autocatalytic activity
CC as well as through phosphorylation of its inhibitor, ABI1. 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).
CC {ECO:0000250|UniProtKB:Q4JIM5, ECO:0000269|PubMed:15735735,
CC ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16678104,
CC ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:18945674}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
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. Inhibited by imatinib mesylate (Gleevec)
CC which is used for the treatment of chronic myeloid leukemia (CML).
CC Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant
CC phosphoinositide known to regulate cytoskeletal and membrane proteins,
CC inhibits the tyrosine kinase activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PSMA7. Interacts with CTTN. Found in a complex
CC with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK
CC phosphorylation by ABL kinases. {ECO:0000269|PubMed:15886098,
CC ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:19381274,
CC ECO:0000269|PubMed:22297987}.
CC -!- INTERACTION:
CC P42684; Q8IZP0: ABI1; NbExp=2; IntAct=EBI-1102694, EBI-375446;
CC P42684; P46108: CRK; NbExp=5; IntAct=EBI-1102694, EBI-886;
CC P42684; P00533: EGFR; NbExp=9; IntAct=EBI-1102694, EBI-297353;
CC P42684; P04626: ERBB2; NbExp=6; IntAct=EBI-1102694, EBI-641062;
CC P42684; P21860: ERBB3; NbExp=10; IntAct=EBI-1102694, EBI-720706;
CC P42684; Q15303: ERBB4; NbExp=4; IntAct=EBI-1102694, EBI-80371;
CC P42684; P36888: FLT3; NbExp=3; IntAct=EBI-1102694, EBI-3946257;
CC P42684; P06241: FYN; NbExp=2; IntAct=EBI-1102694, EBI-515315;
CC P42684; P62993: GRB2; NbExp=2; IntAct=EBI-1102694, EBI-401755;
CC P42684; P10721: KIT; NbExp=2; IntAct=EBI-1102694, EBI-1379503;
CC P42684; P16333: NCK1; NbExp=4; IntAct=EBI-1102694, EBI-389883;
CC P42684; P27986: PIK3R1; NbExp=2; IntAct=EBI-1102694, EBI-79464;
CC P42684; P19174: PLCG1; NbExp=4; IntAct=EBI-1102694, EBI-79387;
CC P42684; Q13671: RIN1; NbExp=5; IntAct=EBI-1102694, EBI-366017;
CC P42684; Q15637: SF1; NbExp=3; IntAct=EBI-1102694, EBI-744603;
CC P42684; P12931: SRC; NbExp=2; IntAct=EBI-1102694, EBI-621482;
CC P42684-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-10693977, EBI-11096309;
CC P42684-3; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-10693977, EBI-6550597;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q4JIM5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=IB, 1BLCTL;
CC IsoId=P42684-1; Sequence=Displayed;
CC Name=2; Synonyms=IA, 1ASCTL;
CC IsoId=P42684-2; Sequence=VSP_004961;
CC Name=3; Synonyms=IC, 1ALCTL;
CC IsoId=P42684-3; Sequence=VSP_017112;
CC Name=4; Synonyms=1ASCTS;
CC IsoId=P42684-4; Sequence=VSP_004961, VSP_021308;
CC Name=5; Synonyms=1BLCTS;
CC IsoId=P42684-5; Sequence=VSP_021308;
CC Name=6; Synonyms=1BSCTL;
CC IsoId=P42684-6; Sequence=VSP_041772;
CC Name=7; Synonyms=1BSCTS;
CC IsoId=P42684-7; Sequence=VSP_041772, VSP_021308;
CC Name=10; Synonyms=1ALCTS;
CC IsoId=P42684-10; Sequence=VSP_017112, VSP_021308;
CC Name=8;
CC IsoId=P42684-8; Sequence=VSP_041772, VSP_041773, VSP_041774;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: Contains two distinct classes of F-actin-binding domains.
CC Although both can bind F-actin, the 2 are required to bundle actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress.
CC Phosphorylated by PDGFRB (By similarity). {ECO:0000250}.
CC -!- PTM: Polyubiquitinated. Polyubiquitination of ABL2 leads to
CC degradation. {ECO:0000269|PubMed:15735735}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ABL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD98092.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/226/ABL2";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/abl2/";
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DR EMBL; M35296; AAA35553.1; -; mRNA.
DR EMBL; FJ542283; ACK76601.1; -; mRNA.
DR EMBL; FJ542284; ACK76602.1; -; mRNA.
DR EMBL; FJ542285; ACK76603.1; -; mRNA.
DR EMBL; FJ542286; ACK76604.1; -; mRNA.
DR EMBL; AK311045; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX538317; CAD98092.1; ALT_INIT; mRNA.
DR EMBL; DQ009672; AAY16984.1; -; Genomic_DNA.
DR EMBL; AL139132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91040.1; -; Genomic_DNA.
DR EMBL; BC065912; AAH65912.1; -; mRNA.
DR CCDS; CCDS30947.1; -. [P42684-1]
DR CCDS; CCDS41441.2; -. [P42684-3]
DR CCDS; CCDS44282.1; -. [P42684-10]
DR CCDS; CCDS53435.1; -. [P42684-4]
DR CCDS; CCDS53436.1; -. [P42684-6]
DR CCDS; CCDS53437.1; -. [P42684-7]
DR CCDS; CCDS53438.1; -. [P42684-5]
DR PIR; A35962; A35962.
DR PIR; B35962; B35962.
DR RefSeq; NP_001129472.1; NM_001136000.2. [P42684-10]
DR RefSeq; NP_001129473.1; NM_001136001.1. [P42684-8]
DR RefSeq; NP_001161708.1; NM_001168236.1. [P42684-6]
DR RefSeq; NP_001161709.1; NM_001168237.1. [P42684-5]
DR RefSeq; NP_001161710.1; NM_001168238.1. [P42684-7]
DR RefSeq; NP_001161711.1; NM_001168239.1. [P42684-4]
DR RefSeq; NP_005149.4; NM_005158.4. [P42684-3]
DR RefSeq; NP_009298.1; NM_007314.3. [P42684-1]
DR RefSeq; XP_005245145.1; XM_005245088.2. [P42684-2]
DR PDB; 2ECD; NMR; -; A=163-268.
DR PDB; 2KK1; NMR; -; A=1058-1182.
DR PDB; 2XYN; X-ray; 2.81 A; A/B/C=279-546.
DR PDB; 3GVU; X-ray; 2.05 A; A=279-546.
DR PDB; 3HMI; X-ray; 1.65 A; A=279-546.
DR PDB; 3ULR; X-ray; 1.65 A; C=563-579.
DR PDB; 4EIH; X-ray; 1.20 A; A=165-273.
DR PDB; 5NP3; X-ray; 2.00 A; A/B/C/D=110-166.
DR PDB; 5NP5; X-ray; 1.40 A; A/B=110-166.
DR PDBsum; 2ECD; -.
DR PDBsum; 2KK1; -.
DR PDBsum; 2XYN; -.
DR PDBsum; 3GVU; -.
DR PDBsum; 3HMI; -.
DR PDBsum; 3ULR; -.
DR PDBsum; 4EIH; -.
DR PDBsum; 5NP3; -.
DR PDBsum; 5NP5; -.
DR AlphaFoldDB; P42684; -.
DR BMRB; P42684; -.
DR EMDB; EMD-41169; -.
DR SMR; P42684; -.
DR BioGRID; 106545; 104.
DR CORUM; P42684; -.
DR DIP; DIP-91N; -.
DR IntAct; P42684; 75.
DR MINT; P42684; -.
DR STRING; 9606.ENSP00000427562; -.
DR BindingDB; P42684; -.
DR ChEMBL; CHEMBL4014; -.
DR DrugBank; DB00171; ATP.
DR DrugBank; DB01254; Dasatinib.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB07664; K-00546.
DR DrugBank; DB05184; XL228.
DR DrugCentral; P42684; -.
DR GuidetoPHARMACOLOGY; 1924; -.
DR MoonDB; P42684; Predicted.
DR GlyGen; P42684; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P42684; -.
DR PhosphoSitePlus; P42684; -.
DR BioMuta; ABL2; -.
DR DMDM; 1168268; -.
DR CPTAC; CPTAC-3138; -.
DR CPTAC; CPTAC-3139; -.
DR EPD; P42684; -.
DR jPOST; P42684; -.
DR MassIVE; P42684; -.
DR MaxQB; P42684; -.
DR PaxDb; 9606-ENSP00000427562; -.
DR PeptideAtlas; P42684; -.
DR ProteomicsDB; 55528; -. [P42684-1]
DR ProteomicsDB; 55529; -. [P42684-10]
DR ProteomicsDB; 55530; -. [P42684-2]
DR ProteomicsDB; 55531; -. [P42684-3]
DR ProteomicsDB; 55532; -. [P42684-4]
DR ProteomicsDB; 55533; -. [P42684-5]
DR ProteomicsDB; 55534; -. [P42684-6]
DR ProteomicsDB; 55535; -. [P42684-7]
DR ProteomicsDB; 55536; -. [P42684-8]
DR Pumba; P42684; -.
DR Antibodypedia; 736; 563 antibodies from 38 providers.
DR DNASU; 27; -.
DR Ensembl; ENST00000344730.8; ENSP00000339209.3; ENSG00000143322.22. [P42684-10]
DR Ensembl; ENST00000367623.8; ENSP00000356595.4; ENSG00000143322.22. [P42684-6]
DR Ensembl; ENST00000502732.6; ENSP00000427562.1; ENSG00000143322.22. [P42684-1]
DR Ensembl; ENST00000504405.5; ENSP00000426831.1; ENSG00000143322.22. [P42684-4]
DR Ensembl; ENST00000507173.5; ENSP00000423413.1; ENSG00000143322.22. [P42684-7]
DR Ensembl; ENST00000511413.5; ENSP00000424697.1; ENSG00000143322.22. [P42684-5]
DR Ensembl; ENST00000512653.5; ENSP00000423578.1; ENSG00000143322.22. [P42684-3]
DR GeneID; 27; -.
DR KEGG; hsa:27; -.
DR MANE-Select; ENST00000502732.6; ENSP00000427562.1; NM_007314.4; NP_009298.1.
DR UCSC; uc001gmg.5; human. [P42684-1]
DR AGR; HGNC:77; -.
DR CTD; 27; -.
DR DisGeNET; 27; -.
DR GeneCards; ABL2; -.
DR HGNC; HGNC:77; ABL2.
DR HPA; ENSG00000143322; Low tissue specificity.
DR MIM; 164690; gene.
DR neXtProt; NX_P42684; -.
DR OpenTargets; ENSG00000143322; -.
DR PharmGKB; PA24414; -.
DR VEuPathDB; HostDB:ENSG00000143322; -.
DR eggNOG; KOG4278; Eukaryota.
DR GeneTree; ENSGT00940000153838; -.
DR HOGENOM; CLU_002795_0_0_1; -.
DR InParanoid; P42684; -.
DR OMA; NIFTQHX; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; P42684; -.
DR TreeFam; TF105081; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; P42684; -.
DR Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9706369; Negative regulation of FLT3.
DR SignaLink; P42684; -.
DR SIGNOR; P42684; -.
DR BioGRID-ORCS; 27; 8 hits in 1191 CRISPR screens.
DR ChiTaRS; ABL2; human.
DR EvolutionaryTrace; P42684; -.
DR GeneWiki; ABL2; -.
DR GenomeRNAi; 27; -.
DR Pharos; P42684; Tchem.
DR PRO; PR:P42684; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P42684; Protein.
DR Bgee; ENSG00000143322; Expressed in tendon of biceps brachii and 175 other cell types or tissues.
DR Genevisible; P42684; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0051015; F:actin filament binding; TAS:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; TAS:UniProtKB.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
DR GO; GO:0035640; P:exploration behavior; ISS:ARUK-UCL.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:ARUK-UCL.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:MGI.
DR GO; GO:1903905; P:positive regulation of establishment of T cell polarity; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:BHF-UCL.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IMP:MGI.
DR GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS: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:0030155; P:regulation of cell adhesion; TAS:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; TAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd05052; PTKc_Abl; 1.
DR CDD; cd09935; SH2_ABL; 1.
DR CDD; cd11850; SH3_Abl; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035837; ABL_SH2.
DR InterPro; IPR015015; F-actin-binding.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF87; TYROSINE-PROTEIN KINASE ABL2; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell adhesion; Cytoplasm; Cytoskeleton; Kinase; Lipoprotein; Magnesium;
KW Manganese; Metal-binding; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..1182
FT /note="Tyrosine-protein kinase ABL2"
FT /id="PRO_0000088052"
FT DOMAIN 107..167
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 173..263
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 288..539
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..106
FT /note="CAP"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..930
FT /note="F-actin-binding"
FT /evidence="ECO:0000250"
FT REGION 763..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1182
FT /note="F-actin-binding"
FT /evidence="ECO:0000250"
FT MOTIF 427..451
FT /note="Kinase activation loop"
FT /evidence="ECO:0000250"
FT MOTIF 658..660
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 774..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 294..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 362..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 174
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 218
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 231
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 261
FT /note="Phosphotyrosine; by ABL1 and autocatalysis"
FT /evidence="ECO:0000269|PubMed:15735735"
FT MOD_RES 272
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12748290"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 299
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 303
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 439
FT /note="Phosphotyrosine; by autocatalysis and SRC-type Tyr-
FT kinases"
FT /evidence="ECO:0000269|PubMed:12748290"
FT MOD_RES 459
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 568
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12748290"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 683
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12748290"
FT MOD_RES 718
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 776
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 800
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00519"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..73
FT /note="MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTTETGFNIFTQH
FT DHFASCVEDGFEGDKTGGSSP -> MVLGTVLLPPNSYGRDQDTSLCCLCTEASESALP
FT DLT (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:18810762"
FT /id="VSP_004961"
FT VAR_SEQ 1..52
FT /note="MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTTETGFNIFTQH
FT -> MVLGTVLLPPNSYGRDQDTSLCCLCTEASESALPDLT (in isoform 3 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017112"
FT VAR_SEQ 53..73
FT /note="Missing (in isoform 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18810762"
FT /id="VSP_041772"
FT VAR_SEQ 550..564
FT /note="EEVAEELGRAASSSS -> EVLLHCANQTCITL (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041773"
FT VAR_SEQ 565..1182
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041774"
FT VAR_SEQ 688..790
FT /note="Missing (in isoform 4, isoform 5, isoform 7 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:18810762"
FT /id="VSP_021308"
FT VARIANT 78
FT /note="R -> H (in dbSNP:rs55655202)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_055411"
FT VARIANT 99
FT /note="E -> Q (somatic mutation in a breast cancer sample)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_055412"
FT VARIANT 519
FT /note="R -> I (somatic mutation in a lung squamous cell
FT carcinoma)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_055413"
FT VARIANT 769
FT /note="T -> S (in dbSNP:rs55892721)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_055414"
FT VARIANT 930
FT /note="K -> R (in dbSNP:rs17277288)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.5"
FT /id="VAR_029232"
FT VARIANT 946
FT /note="V -> M (in dbSNP:rs28913889)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_029233"
FT VARIANT 996
FT /note="P -> R (in dbSNP:rs28913890)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.5"
FT /id="VAR_029234"
FT VARIANT 1085
FT /note="S -> N (in dbSNP:rs28913891)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_029235"
FT VARIANT 1101
FT /note="T -> A (in dbSNP:rs28913892)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_029236"
FT CONFLICT 343..344
FT /note="NL -> TI (in Ref. 9; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="T -> I (in Ref. 3; AK311045)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="K -> R (in Ref. 4; CAD98092)"
FT /evidence="ECO:0000305"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5NP5"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5NP5"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:5NP5"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:5NP5"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5NP5"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5NP5"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4EIH"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:4EIH"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:4EIH"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:4EIH"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:4EIH"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:4EIH"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2ECD"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:4EIH"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4EIH"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:4EIH"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4EIH"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:3GVU"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 326..337
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:3HMI"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 383..402
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:3HMI"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:2XYN"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:3GVU"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 464..479
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 494..499
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 512..521
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 532..545
FT /evidence="ECO:0007829|PDB:3HMI"
FT HELIX 1069..1071
FT /evidence="ECO:0007829|PDB:2KK1"
FT TURN 1076..1078
FT /evidence="ECO:0007829|PDB:2KK1"
FT HELIX 1080..1083
FT /evidence="ECO:0007829|PDB:2KK1"
FT HELIX 1086..1099
FT /evidence="ECO:0007829|PDB:2KK1"
FT HELIX 1106..1123
FT /evidence="ECO:0007829|PDB:2KK1"
FT HELIX 1124..1126
FT /evidence="ECO:0007829|PDB:2KK1"
FT HELIX 1130..1152
FT /evidence="ECO:0007829|PDB:2KK1"
FT STRAND 1155..1158
FT /evidence="ECO:0007829|PDB:2KK1"
FT HELIX 1165..1181
FT /evidence="ECO:0007829|PDB:2KK1"
FT MOD_RES P42684-4:647
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VARIANT P42684-4:12
FT /note="S -> T (in dbSNP:rs1318056)"
FT /evidence="ECO:0000269|PubMed:18810762,
FT ECO:0007744|PubMed:17344846"
FT /id="VAR_082895"
FT MOD_RES P42684-5:683
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES P42684-7:662
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES P42684-10:668
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
SQ SEQUENCE 1182 AA; 128343 MW; ED93869BC2B14FAA CRC64;
MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT QHDHFASCVE
DGFEGDKTGG SSPEALHRPY GCDVEPQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA
SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR
SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTADGKV YVTAESRFST
LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG
EVYVGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV
TEYMPYGNLL DYLRECNREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN
HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT
YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE
TMFHDSSISE EVAEELGRAA SSSSVVPYLP RLPILPSKTR TLKKQVENKE NIEGAQDATE
NSASSLAPGF IRGAQASSGS PALPRKQRDK SPSSLLEDAK ETCFTRDRKG GFFSSFMKKR
NAPTPPKRSS SFREMENQPH KKYELTGNFS SVASLQHADG FSFTPAQQEA NLVPPKCYGG
SFAQRNLCND DGGGGGGSGT AGGGWSGITG FFTPRLIKKT LGLRAGKPTA SDDTSKPFPR
SNSTSSMSSG LPEQDRMAMT LPRNCQRSKL QLERTVSTSS QPEENVDRAN DMLPKKSEES
AAPSRERPKA KLLPRGATAL PLRTPSGDLA ITEKDPPGVG VAGVAAAPKG KEKNGGARLG
MAGVPEDGEQ PGWPSPAKAA PVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL
LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSICS DPTEEPTALT AGQSTSETQE
GGKKAALGAV PISGKAGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS
ADKISKEALL ECADLLSSAL TEPVPNSQLV DTGHQLLDYC SGYVDCIPQT RNKFAFREAV
SKLELSLQEL QVSSAAAGVP GTNPVLNNLL SCVQEISDVV QR
//
