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Database: UniProt
Entry: P42684
LinkDB: P42684
Original site: P42684 
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   17-JUN-2020, entry version 223.
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.
CC       {ECO:0000269|PubMed:15735735, ECO:0000269|PubMed:15886098,
CC       ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:17306540,
CC       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   -!- 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="http://atlasgeneticsoncology.org/Genes/ABL2ID226.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/abl2/";
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; CCDS44283.1; -. [P42684-8]
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   SMR; P42684; -.
DR   BioGRID; 106545; 48.
DR   CORUM; P42684; -.
DR   DIP; DIP-91N; -.
DR   IntAct; P42684; 55.
DR   MINT; P42684; -.
DR   STRING; 9606.ENSP00000427562; -.
DR   BindingDB; P42684; -.
DR   ChEMBL; CHEMBL4014; -.
DR   DrugBank; DB07664; 5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE.
DR   DrugBank; DB00171; ATP.
DR   DrugBank; DB01254; Dasatinib.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugBank; DB05184; XL228.
DR   DrugCentral; P42684; -.
DR   GuidetoPHARMACOLOGY; 1924; -.
DR   MoonDB; P42684; Predicted.
DR   iPTMnet; P42684; -.
DR   PhosphoSitePlus; P42684; -.
DR   BioMuta; ABL2; -.
DR   DMDM; 1168268; -.
DR   EPD; P42684; -.
DR   jPOST; P42684; -.
DR   MassIVE; P42684; -.
DR   MaxQB; P42684; -.
DR   PaxDb; P42684; -.
DR   PeptideAtlas; P42684; -.
DR   PRIDE; 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   Antibodypedia; 736; 468 antibodies.
DR   DNASU; 27; -.
DR   Ensembl; ENST00000344730; ENSP00000339209; ENSG00000143322. [P42684-10]
DR   Ensembl; ENST00000367623; ENSP00000356595; ENSG00000143322. [P42684-6]
DR   Ensembl; ENST00000392043; ENSP00000375897; ENSG00000143322. [P42684-8]
DR   Ensembl; ENST00000502732; ENSP00000427562; ENSG00000143322. [P42684-1]
DR   Ensembl; ENST00000504405; ENSP00000426831; ENSG00000143322. [P42684-4]
DR   Ensembl; ENST00000507173; ENSP00000423413; ENSG00000143322. [P42684-7]
DR   Ensembl; ENST00000511413; ENSP00000424697; ENSG00000143322. [P42684-5]
DR   Ensembl; ENST00000512653; ENSP00000423578; ENSG00000143322. [P42684-3]
DR   GeneID; 27; -.
DR   KEGG; hsa:27; -.
DR   UCSC; uc001gmg.5; human. [P42684-1]
DR   CTD; 27; -.
DR   DisGeNET; 27; -.
DR   EuPathDB; HostDB:ENSG00000143322.19; -.
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   eggNOG; KOG0197; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   GeneTree; ENSGT00940000153838; -.
DR   HOGENOM; CLU_002795_0_0_1; -.
DR   InParanoid; P42684; -.
DR   KO; K08887; -.
DR   OMA; PPKCCGG; -.
DR   OrthoDB; 182823at2759; -.
DR   PhylomeDB; P42684; -.
DR   TreeFam; TF105081; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
DR   SignaLink; P42684; -.
DR   SIGNOR; P42684; -.
DR   BioGRID-ORCS; 27; 2 hits in 816 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 198 other tissues.
DR   Genevisible; P42684; HS.
DR   GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB.
DR   GO; GO:0005623; C:cell; IEA:GOC.
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:0006464; P:cellular protein modification process; TAS:ProtInc.
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: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:2000249; P:regulation of actin cytoskeleton reorganization; 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; cd09935; SH2_ABL; 1.
DR   Gene3D; 3.30.505.10; -; 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   Pfam; PF08919; F_actin_bind; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 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; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
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   Polymorphism; 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   NP_BIND         294..302
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         362..368
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          2..106
FT                   /note="CAP"
FT   REGION          694..930
FT                   /note="F-actin-binding"
FT                   /evidence="ECO:0000250"
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        561..564
FT                   /note="Poly-Ser"
FT   COMPBIAS        732..739
FT                   /note="Poly-Gly"
FT   COMPBIAS        843..1055
FT                   /note="Pro-rich"
FT   COMPBIAS        984..988
FT                   /note="Poly-Pro"
FT   ACT_SITE        409
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         317
FT                   /note="ATP"
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:0000244|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:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   MOD_RES         631
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   MOD_RES         633
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         655
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|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:0000244|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:0000244|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:0000244|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:0000244|PubMed:17525332,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163"
FT   MOD_RES         820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163"
FT   MOD_RES         915
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976"
FT   MOD_RES         936
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|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:0000244|PDB:5NP5"
FT   STRAND          133..139
FT                   /evidence="ECO:0000244|PDB:5NP5"
FT   STRAND          141..150
FT                   /evidence="ECO:0000244|PDB:5NP5"
FT   STRAND          153..158
FT                   /evidence="ECO:0000244|PDB:5NP5"
FT   HELIX           159..161
FT                   /evidence="ECO:0000244|PDB:5NP5"
FT   STRAND          162..164
FT                   /evidence="ECO:0000244|PDB:5NP5"
FT   HELIX           168..170
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   STRAND          174..177
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   HELIX           180..187
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   STRAND          194..199
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   STRAND          207..213
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   STRAND          216..221
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   STRAND          226..228
FT                   /evidence="ECO:0000244|PDB:2ECD"
FT   STRAND          230..233
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   STRAND          236..240
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   HELIX           241..248
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   STRAND          255..257
FT                   /evidence="ECO:0000244|PDB:4EIH"
FT   STRAND          280..282
FT                   /evidence="ECO:0000244|PDB:3GVU"
FT   HELIX           285..287
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          288..293
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           294..297
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          300..307
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           308..310
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          312..318
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           326..337
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          347..351
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          353..356
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          358..362
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           369..375
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   TURN            378..380
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           383..402
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           412..414
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          415..417
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           419..421
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          423..425
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   STRAND          435..437
FT                   /evidence="ECO:0000244|PDB:2XYN"
FT   STRAND          438..440
FT                   /evidence="ECO:0000244|PDB:3GVU"
FT   HELIX           449..451
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           454..459
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           464..479
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           491..493
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           494..499
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           512..521
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           526..528
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           532..545
FT                   /evidence="ECO:0000244|PDB:3HMI"
FT   HELIX           1069..1071
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   TURN            1076..1078
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   HELIX           1080..1083
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   HELIX           1086..1099
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   HELIX           1106..1123
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   HELIX           1124..1126
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   HELIX           1130..1152
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   STRAND          1155..1158
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   HELIX           1165..1181
FT                   /evidence="ECO:0000244|PDB:2KK1"
FT   MOD_RES         P42684-4:647
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:19369195"
FT   VARIANT         P42684-4:12
FT                   /note="S -> T (in dbSNP:rs1318056)"
FT                   /evidence="ECO:0000244|PubMed:17344846,
FT                   ECO:0000269|PubMed:18810762"
FT                   /id="VAR_082895"
FT   MOD_RES         P42684-5:683
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:19369195"
FT   MOD_RES         P42684-7:662
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|PubMed:19369195"
FT   MOD_RES         P42684-10:668
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000244|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
//
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