Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Abelson tyrosine-protein kinase 2 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 2) (Abelson-related gene protein) (Tyrosine-protein kinase ARG)

 ABL2_HUMAN              Reviewed;        1182 AA.
P42684; A0M8X0; B7UEF2; B7UEF3; B7UEF4; B7UEF5; Q5T0X6; Q5W0C5;
Q6NZY6; Q7Z301;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
12-SEP-2018, entry version 209.
RecName: Full=Tyrosine-protein kinase ABL2;
EC=2.7.10.2;
AltName: Full=Abelson murine leukemia viral oncogene homolog 2;
AltName: Full=Abelson tyrosine-protein kinase 2;
AltName: Full=Abelson-related gene protein;
AltName: Full=Tyrosine-protein kinase ARG;
Name=ABL2; Synonyms=ABLL, ARG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING
(ISOFORM 2).
PubMed=2198571; DOI=10.1073/pnas.87.15.5802;
Kruh G.D., Perego R., Miki T., Aaronson S.A.;
"The complete coding sequence of arg defines the Abelson subfamily of
cytoplasmic tyrosine kinases.";
Proc. Natl. Acad. Sci. U.S.A. 87:5802-5806(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7), ALTERNATIVE
SPLICING (ISOFORM 10), AND VARIANT THR-12 (ISOFORM 4).
PubMed=18810762; DOI=10.1002/jcb.21922;
Bianchi C., Torsello B., Angeloni V., Bombelli S., Soldi M.,
Invernizzi L., Brambilla P., Perego R.A.;
"Eight full-length abelson related gene (Arg) isoforms are
constitutively expressed in caki-1 cell line and cell distribution of
two isoforms has been analyzed after transfection.";
J. Cell. Biochem. 105:1219-1227(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Uterine endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-930; MET-946;
ARG-996; ASN-1085 AND ALA-1101.
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 343-469.
PubMed=3787260; DOI=10.1126/science.3787260;
Kruh G.D., King C.R., Kraus M.H., Popescu N.C., Amsbaugh S.C.,
McBride W.O., Aaronson S.A.;
"A novel human gene closely related to the abl proto-oncogene.";
Science 234:1545-1548(1986).
[10]
PHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND TYR-683, AND ACTIVITY
REGULATION.
PubMed=12748290; DOI=10.1128/MCB.23.11.3884-3896.2003;
Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.;
"Two distinct phosphorylation pathways have additive effects on Abl
family kinase activation.";
Mol. Cell. Biol. 23:3884-3896(2003).
[11]
INTERACTION WITH RIN1, FUNCTION, AND ACTIVITY REGULATION.
PubMed=15886098; DOI=10.1016/j.cub.2005.03.049;
Hu H., Bliss J.M., Wang Y., Colicelli J.;
"RIN1 is an ABL tyrosine kinase activator and a regulator of
epithelial-cell adhesion and migration.";
Curr. Biol. 15:815-823(2005).
[12]
FUNCTION, PHOSPHORYLATION AT TYR-261, AND UBIQUITINATION.
PubMed=15735735; DOI=10.1038/sj.onc.1208454;
Cao C., Li Y., Leng Y., Li P., Ma Q., Kufe D.;
"Ubiquitination and degradation of the Arg tyrosine kinase is
regulated by oxidative stress.";
Oncogene 24:2433-2440(2005).
[13]
FUNCTION, AND INTERACTION WITH PSMA7.
PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007;
Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q.,
Cao C.;
"Interaction between c-Abl and Arg tyrosine kinases and proteasome
subunit PSMA7 regulates proteasome degradation.";
Mol. Cell 22:317-327(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
FUNCTION.
PubMed=17306540; DOI=10.1016/j.cub.2007.01.057;
Boyle S.N., Michaud G.A., Schweitzer B., Predki P.F., Koleske A.J.;
"A critical role for cortactin phosphorylation by Abl-family kinases
in PDGF-induced dorsal-wave formation.";
Curr. Biol. 17:445-451(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
FUNCTION.
PubMed=18945674; DOI=10.1074/jbc.M804543200;
Yogalingam G., Pendergast A.M.;
"Abl kinases regulate autophagy by promoting the trafficking and
function of lysosomal components.";
J. Biol. Chem. 283:35941-35953(2008).
[18]
REVIEW ON FUNCTION.
PubMed=12775773; DOI=10.1242/jcs.00622;
Woodring P.J., Hunter T., Wang J.Y.;
"Regulation of F-actin-dependent processes by the Abl family of
tyrosine kinases.";
J. Cell Sci. 116:2613-2626(2003).
[19]
REVIEW ON FUNCTION.
PubMed=14729179; DOI=10.1016/j.tcb.2003.11.003;
Hernandez S.E., Krishnaswami M., Miller A.L., Koleske A.J.;
"How do Abl family kinases regulate cell shape and movement?";
Trends Cell Biol. 14:36-44(2004).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-915, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-633;
SER-655; SER-817; SER-820 AND SER-936, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
REVIEW ON FUNCTION.
PubMed=18182299; DOI=10.1016/j.tibs.2007.10.006;
Backert S., Feller S.M., Wessler S.;
"Emerging roles of Abl family tyrosine kinases in microbial
pathogenesis.";
Trends Biochem. Sci. 33:80-90(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-718, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT TYR-668 (ISOFORM 10), PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT TYR-647 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT TYR-683 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT TYR-662 (ISOFORM 7), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[25]
IDENTIFICATION IN A COMPLEX WITH UNC119: ABL1 AND CRK.
PubMed=19381274; DOI=10.1371/journal.pone.0005211;
Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.;
"Unc119 protects from Shigella infection by inhibiting the Abl family
kinases.";
PLoS ONE 4:E5211-E5211(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-936, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-936, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[28]
REVIEW ON FUNCTION, AND DOMAIN.
PubMed=20841568; DOI=10.1126/scisignal.3139re6;
Colicelli J.;
"ABL tyrosine kinases: evolution of function, regulation, and
specificity.";
Sci. Signal. 3:RE6-RE6(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-655;
SER-671; SER-783; SER-817; SER-820 AND SER-936, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620 AND SER-631, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
STRUCTURE BY NMR OF 163-268.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the human ABL2 SH2 domain.";
Submitted (FEB-2008) to the PDB data bank.
[33]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 279-546 IN COMPLEXES WITH
INHIBITORS.
PubMed=21417343; DOI=10.1021/jm101506n;
Salah E., Ugochukwu E., Barr A.J., von Delft F., Knapp S.,
Elkins J.M.;
"Crystal structures of ABL-related gene (ABL2) in complex with
imatinib, tozasertib (VX-680), and a type I inhibitor of the triazole
carbothioamide class.";
J. Med. Chem. 54:2359-2367(2011).
[34]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 563-579 IN COMPLEX WITH
CTTN, AND INTERACTION WITH CTTN.
PubMed=22297987; DOI=10.1107/S1744309111056132;
Liu W., MacGrath S.M., Koleske A.J., Boggon T.J.;
"Lysozyme contamination facilitates crystallization of a
heterotrimeric cortactin-Arg-lysozyme complex.";
Acta Crystallogr. F 68:154-158(2012).
[35]
VARIANTS [LARGE SCALE ANALYSIS] HIS-78; GLN-99; ILE-519; SER-769;
ARG-930 AND ARG-996, AND VARIANT [LARGE SCALE ANALYSIS] THR-12
(ISOFORM 4).
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1-
overlapping role in key processes linked to cell growth and
survival such as cytoskeleton remodeling in response to
extracellular stimuli, cell motility and adhesion and receptor
endocytosis. Coordinates actin remodeling through tyrosine
phosphorylation of proteins controlling cytoskeleton dynamics like
MYH10 (involved in movement); CTTN (involved in signaling); or
TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and
regulates actin cytoskeletal structure through its F-actin-
bundling activity. Involved in the regulation of cell adhesion and
motility through phosphorylation of key regulators of these
processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent
phosphorylation of ARHGAP35 promotes its association with RASA1,
resulting in recruitment of ARHGAP35 to the cell periphery where
it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases
like PDGFRB and other substrates which are involved in endocytosis
regulation such as RIN1. In brain, may regulate neurotransmission
by phosphorylating proteins at the synapse. ABL2 acts also as a
regulator of multiple pathological signaling cascades during
infection. Pathogens can highjack ABL2 kinase signaling to
reorganize the host actin cytoskeleton for multiple purposes, like
facilitating intracellular movement and host cell exit. Finally,
functions as its own regulator through autocatalytic activity as
well as through phosphorylation of its inhibitor, ABI1.
{ECO:0000269|PubMed:15735735, ECO:0000269|PubMed:15886098,
ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:17306540,
ECO:0000269|PubMed:18945674}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
-!- ACTIVITY REGULATION: Stabilized in the inactive form by an
association between the SH3 domain and the SH2-TK linker region,
interactions of the N-terminal cap, and contributions from an N-
terminal myristoyl group and phospholipids. Activated by
autophosphorylation as well as by SRC-family kinase-mediated
phosphorylation. Activated by RIN1 binding to the SH2 and SH3
domains. Inhibited by imatinib mesylate (Gleevec) which is used
for the treatment of chronic myeloid leukemia (CML).
Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant
phosphoinositide known to regulate cytoskeletal and membrane
proteins, inhibits the tyrosine kinase activity (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with PSMA7. Interacts with CTTN. Found in a
complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition
of CRK phosphorylation by ABL kinases.
{ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16678104,
ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:22297987}.
-!- INTERACTION:
Q8IZP0:ABI1; NbExp=2; IntAct=EBI-1102694, EBI-375446;
P46108:CRK; NbExp=5; IntAct=EBI-1102694, EBI-886;
P00533:EGFR; NbExp=8; IntAct=EBI-1102694, EBI-297353;
P04626:ERBB2; NbExp=6; IntAct=EBI-1102694, EBI-641062;
P21860:ERBB3; NbExp=10; IntAct=EBI-1102694, EBI-720706;
Q15303:ERBB4; NbExp=4; IntAct=EBI-1102694, EBI-80371;
P06241:FYN; NbExp=2; IntAct=EBI-1102694, EBI-515315;
P62993:GRB2; NbExp=2; IntAct=EBI-1102694, EBI-401755;
P10721:KIT; NbExp=2; IntAct=EBI-1102694, EBI-1379503;
P16333:NCK1; NbExp=4; IntAct=EBI-1102694, EBI-389883;
P27986:PIK3R1; NbExp=2; IntAct=EBI-1102694, EBI-79464;
P19174:PLCG1; NbExp=4; IntAct=EBI-1102694, EBI-79387;
Q13671:RIN1; NbExp=4; IntAct=EBI-1102694, EBI-366017;
Q15637:SF1; NbExp=3; IntAct=EBI-1102694, EBI-744603;
P12931:SRC; NbExp=2; IntAct=EBI-1102694, EBI-621482;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1; Synonyms=IB, 1BLCTL;
IsoId=P42684-1; Sequence=Displayed;
Name=2; Synonyms=IA, 1ASCTL;
IsoId=P42684-2; Sequence=VSP_004961;
Name=3; Synonyms=IC, 1ALCTL;
IsoId=P42684-3; Sequence=VSP_017112;
Name=4; Synonyms=1ASCTS;
IsoId=P42684-4; Sequence=VSP_004961, VSP_021308;
Note=Variant in position: 12:S->T (in dbSNP:rs1318056). Contains
a phosphotyrosine at position 647.
{ECO:0000244|PubMed:19369195};
Name=5; Synonyms=1BLCTS;
IsoId=P42684-5; Sequence=VSP_021308;
Note=Contains a phosphotyrosine at position 683.
{ECO:0000244|PubMed:19369195};
Name=6; Synonyms=1BSCTL;
IsoId=P42684-6; Sequence=VSP_041772;
Name=7; Synonyms=1BSCTS;
IsoId=P42684-7; Sequence=VSP_041772, VSP_021308;
Note=Contains a phosphotyrosine at position 662.
{ECO:0000244|PubMed:19369195};
Name=10; Synonyms=1ALCTS;
IsoId=P42684-10; Sequence=VSP_017112, VSP_021308;
Note=Contains a phosphotyrosine at position 668.
{ECO:0000244|PubMed:19369195};
Name=8;
IsoId=P42684-8; Sequence=VSP_041772, VSP_041773, VSP_041774;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DOMAIN: Contains two distinct classes of F-actin-binding domains.
Although both can bind F-actin, the 2 are required to bundle actin
filaments (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated at Tyr-261 by ABL1 in response to oxidative
stress. Phosphorylated by PDGFRB (By similarity). {ECO:0000250}.
-!- PTM: Polyubiquitinated. Polyubiquitination of ABL2 leads to
degradation. {ECO:0000269|PubMed:15735735}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. ABL subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=CAD98092.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ABL2ID226.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/abl2/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M35296; AAA35553.1; -; mRNA.
EMBL; FJ542283; ACK76601.1; -; mRNA.
EMBL; FJ542284; ACK76602.1; -; mRNA.
EMBL; FJ542285; ACK76603.1; -; mRNA.
EMBL; FJ542286; ACK76604.1; -; mRNA.
EMBL; AK311045; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BX538317; CAD98092.1; ALT_INIT; mRNA.
EMBL; DQ009672; AAY16984.1; -; Genomic_DNA.
EMBL; AL139132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91040.1; -; Genomic_DNA.
EMBL; BC065912; AAH65912.1; -; mRNA.
CCDS; CCDS30947.1; -. [P42684-1]
CCDS; CCDS41441.2; -. [P42684-3]
CCDS; CCDS44282.1; -. [P42684-10]
CCDS; CCDS44283.1; -. [P42684-8]
CCDS; CCDS53435.1; -. [P42684-4]
CCDS; CCDS53436.1; -. [P42684-6]
CCDS; CCDS53437.1; -. [P42684-7]
CCDS; CCDS53438.1; -. [P42684-5]
PIR; A35962; A35962.
PIR; B35962; B35962.
RefSeq; NP_001129472.1; NM_001136000.2. [P42684-10]
RefSeq; NP_001129473.1; NM_001136001.1. [P42684-8]
RefSeq; NP_001161708.1; NM_001168236.1. [P42684-6]
RefSeq; NP_001161709.1; NM_001168237.1. [P42684-5]
RefSeq; NP_001161710.1; NM_001168238.1. [P42684-7]
RefSeq; NP_001161711.1; NM_001168239.1. [P42684-4]
RefSeq; NP_005149.4; NM_005158.4. [P42684-3]
RefSeq; NP_009298.1; NM_007314.3. [P42684-1]
RefSeq; XP_005245145.1; XM_005245088.2. [P42684-2]
UniGene; Hs.159472; -.
PDB; 2ECD; NMR; -; A=163-268.
PDB; 2KK1; NMR; -; A=1058-1182.
PDB; 2XYN; X-ray; 2.81 A; A/B/C=279-546.
PDB; 3GVU; X-ray; 2.05 A; A=279-546.
PDB; 3HMI; X-ray; 1.65 A; A=279-546.
PDB; 3ULR; X-ray; 1.65 A; C=563-579.
PDB; 4EIH; X-ray; 1.20 A; A=165-273.
PDB; 5NP3; X-ray; 2.00 A; A/B/C/D=110-166.
PDB; 5NP5; X-ray; 1.40 A; A/B=110-166.
PDBsum; 2ECD; -.
PDBsum; 2KK1; -.
PDBsum; 2XYN; -.
PDBsum; 3GVU; -.
PDBsum; 3HMI; -.
PDBsum; 3ULR; -.
PDBsum; 4EIH; -.
PDBsum; 5NP3; -.
PDBsum; 5NP5; -.
ProteinModelPortal; P42684; -.
SMR; P42684; -.
BioGrid; 106545; 43.
CORUM; P42684; -.
DIP; DIP-91N; -.
IntAct; P42684; 44.
MINT; P42684; -.
STRING; 9606.ENSP00000427562; -.
BindingDB; P42684; -.
ChEMBL; CHEMBL4014; -.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB01254; Dasatinib.
DrugBank; DB05184; XL228.
GuidetoPHARMACOLOGY; 1924; -.
MoonDB; P42684; Predicted.
iPTMnet; P42684; -.
PhosphoSitePlus; P42684; -.
BioMuta; ABL2; -.
DMDM; 1168268; -.
EPD; P42684; -.
MaxQB; P42684; -.
PaxDb; P42684; -.
PeptideAtlas; P42684; -.
PRIDE; P42684; -.
ProteomicsDB; 55528; -.
ProteomicsDB; 55529; -. [P42684-10]
ProteomicsDB; 55530; -. [P42684-2]
ProteomicsDB; 55531; -. [P42684-3]
ProteomicsDB; 55532; -. [P42684-4]
ProteomicsDB; 55533; -. [P42684-5]
ProteomicsDB; 55534; -. [P42684-6]
ProteomicsDB; 55535; -. [P42684-7]
ProteomicsDB; 55536; -. [P42684-8]
DNASU; 27; -.
Ensembl; ENST00000344730; ENSP00000339209; ENSG00000143322. [P42684-10]
Ensembl; ENST00000367623; ENSP00000356595; ENSG00000143322. [P42684-6]
Ensembl; ENST00000392043; ENSP00000375897; ENSG00000143322. [P42684-8]
Ensembl; ENST00000502732; ENSP00000427562; ENSG00000143322. [P42684-1]
Ensembl; ENST00000504405; ENSP00000426831; ENSG00000143322. [P42684-4]
Ensembl; ENST00000507173; ENSP00000423413; ENSG00000143322. [P42684-7]
Ensembl; ENST00000511413; ENSP00000424697; ENSG00000143322. [P42684-5]
Ensembl; ENST00000512653; ENSP00000423578; ENSG00000143322. [P42684-3]
GeneID; 27; -.
KEGG; hsa:27; -.
UCSC; uc001gmg.5; human. [P42684-1]
CTD; 27; -.
DisGeNET; 27; -.
EuPathDB; HostDB:ENSG00000143322.19; -.
GeneCards; ABL2; -.
HGNC; HGNC:77; ABL2.
HPA; CAB017106; -.
HPA; HPA001866; -.
HPA; HPA072754; -.
MIM; 164690; gene.
neXtProt; NX_P42684; -.
OpenTargets; ENSG00000143322; -.
PharmGKB; PA24414; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOVERGEN; HBG004162; -.
InParanoid; P42684; -.
KO; K08887; -.
OMA; EMENQPH; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P42684; -.
TreeFam; TF105081; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
SignaLink; P42684; -.
SIGNOR; P42684; -.
ChiTaRS; ABL2; human.
EvolutionaryTrace; P42684; -.
GeneWiki; ABL2; -.
GenomeRNAi; 27; -.
PRO; PR:P42684; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143322; Expressed in 199 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_ABL2; -.
Genevisible; P42684; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0051015; F:actin filament binding; TAS:UniProtKB.
GO; GO:0003785; F:actin monomer binding; TAS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; TAS:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:BHF-UCL.
GO; GO:0010863; P:positive regulation of phospholipase C activity; IMP:MGI.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; TAS:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; TAS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0030100; P:regulation of endocytosis; TAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd09935; SH2_ABL; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035837; ABL_SH2.
InterPro; IPR015015; F-actin_binding.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF08919; F_actin_bind; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00808; FABD; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell adhesion; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
Lipoprotein; Magnesium; Manganese; Metal-binding; Myristate;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase;
Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 1182 Tyrosine-protein kinase ABL2.
/FTId=PRO_0000088052.
DOMAIN 107 167 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 173 263 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 288 539 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 294 302 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 362 368 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 106 CAP.
REGION 694 930 F-actin-binding. {ECO:0000250}.
REGION 1020 1182 F-actin-binding. {ECO:0000250}.
MOTIF 427 451 Kinase activation loop. {ECO:0000250}.
MOTIF 658 660 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 561 564 Poly-Ser.
COMPBIAS 732 739 Poly-Gly.
COMPBIAS 843 1055 Pro-rich.
COMPBIAS 984 988 Poly-Pro.
ACT_SITE 409 409 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 317 317 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 116 116 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 161 161 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 174 174 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 185 185 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 218 218 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 231 231 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 261 261 Phosphotyrosine; by ABL1 and
autocatalysis.
{ECO:0000269|PubMed:15735735}.
MOD_RES 272 272 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12748290}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 299 299 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 303 303 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 439 439 Phosphotyrosine; by autocatalysis and
SRC-type Tyr-kinases.
{ECO:0000269|PubMed:12748290}.
MOD_RES 459 459 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 568 568 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12748290}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 655 655 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 683 683 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12748290}.
MOD_RES 718 718 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 776 776 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 800 800 Phosphothreonine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 817 817 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 820 820 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 915 915 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 936 936 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
VAR_SEQ 1 73 MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRT
TETGFNIFTQHDHFASCVEDGFEGDKTGGSSP -> MVLGT
VLLPPNSYGRDQDTSLCCLCTEASESALPDLT (in
isoform 2 and isoform 4).
{ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:18810762}.
/FTId=VSP_004961.
VAR_SEQ 1 52 MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRT
TETGFNIFTQH -> MVLGTVLLPPNSYGRDQDTSLCCLCT
EASESALPDLT (in isoform 3 and isoform
10). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_017112.
VAR_SEQ 53 73 Missing (in isoform 6, isoform 7 and
isoform 8). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18810762}.
/FTId=VSP_041772.
VAR_SEQ 550 564 EEVAEELGRAASSSS -> EVLLHCANQTCITL (in
isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041773.
VAR_SEQ 565 1182 Missing (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041774.
VAR_SEQ 688 790 Missing (in isoform 4, isoform 5, isoform
7 and isoform 10).
{ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:18810762}.
/FTId=VSP_021308.
VARIANT 78 78 R -> H (in dbSNP:rs55655202).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_055411.
VARIANT 99 99 E -> Q (somatic mutation in a breast
cancer sample).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_055412.
VARIANT 519 519 R -> I (somatic mutation in a lung
squamous cell carcinoma).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_055413.
VARIANT 769 769 T -> S (in dbSNP:rs55892721).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_055414.
VARIANT 930 930 K -> R (in dbSNP:rs17277288).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.5}.
/FTId=VAR_029232.
VARIANT 946 946 V -> M (in dbSNP:rs28913889).
{ECO:0000269|Ref.5}.
/FTId=VAR_029233.
VARIANT 996 996 P -> R (in dbSNP:rs28913890).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.5}.
/FTId=VAR_029234.
VARIANT 1085 1085 S -> N (in dbSNP:rs28913891).
{ECO:0000269|Ref.5}.
/FTId=VAR_029235.
VARIANT 1101 1101 T -> A (in dbSNP:rs28913892).
{ECO:0000269|Ref.5}.
/FTId=VAR_029236.
CONFLICT 343 344 NL -> TI (in Ref. 9; no nucleotide
entry). {ECO:0000305}.
CONFLICT 435 435 T -> I (in Ref. 3; AK311045).
{ECO:0000305}.
CONFLICT 981 981 K -> R (in Ref. 4; CAD98092).
{ECO:0000305}.
STRAND 111 116 {ECO:0000244|PDB:5NP5}.
STRAND 133 139 {ECO:0000244|PDB:5NP5}.
STRAND 141 150 {ECO:0000244|PDB:5NP5}.
STRAND 153 158 {ECO:0000244|PDB:5NP5}.
HELIX 159 161 {ECO:0000244|PDB:5NP5}.
STRAND 162 164 {ECO:0000244|PDB:5NP5}.
HELIX 168 170 {ECO:0000244|PDB:4EIH}.
STRAND 174 177 {ECO:0000244|PDB:4EIH}.
HELIX 180 187 {ECO:0000244|PDB:4EIH}.
STRAND 194 199 {ECO:0000244|PDB:4EIH}.
STRAND 207 213 {ECO:0000244|PDB:4EIH}.
STRAND 216 221 {ECO:0000244|PDB:4EIH}.
STRAND 226 228 {ECO:0000244|PDB:2ECD}.
STRAND 230 233 {ECO:0000244|PDB:4EIH}.
STRAND 236 240 {ECO:0000244|PDB:4EIH}.
HELIX 241 248 {ECO:0000244|PDB:4EIH}.
STRAND 255 257 {ECO:0000244|PDB:4EIH}.
STRAND 280 282 {ECO:0000244|PDB:3GVU}.
HELIX 285 287 {ECO:0000244|PDB:3HMI}.
STRAND 288 293 {ECO:0000244|PDB:3HMI}.
HELIX 294 297 {ECO:0000244|PDB:3HMI}.
STRAND 300 307 {ECO:0000244|PDB:3HMI}.
HELIX 308 310 {ECO:0000244|PDB:3HMI}.
STRAND 312 318 {ECO:0000244|PDB:3HMI}.
HELIX 326 337 {ECO:0000244|PDB:3HMI}.
STRAND 347 351 {ECO:0000244|PDB:3HMI}.
STRAND 353 356 {ECO:0000244|PDB:3HMI}.
STRAND 358 362 {ECO:0000244|PDB:3HMI}.
HELIX 369 375 {ECO:0000244|PDB:3HMI}.
TURN 378 380 {ECO:0000244|PDB:3HMI}.
HELIX 383 402 {ECO:0000244|PDB:3HMI}.
HELIX 412 414 {ECO:0000244|PDB:3HMI}.
STRAND 415 417 {ECO:0000244|PDB:3HMI}.
HELIX 419 421 {ECO:0000244|PDB:3HMI}.
STRAND 423 425 {ECO:0000244|PDB:3HMI}.
STRAND 435 437 {ECO:0000244|PDB:2XYN}.
STRAND 438 440 {ECO:0000244|PDB:3GVU}.
HELIX 449 451 {ECO:0000244|PDB:3HMI}.
HELIX 454 459 {ECO:0000244|PDB:3HMI}.
HELIX 464 479 {ECO:0000244|PDB:3HMI}.
HELIX 491 493 {ECO:0000244|PDB:3HMI}.
HELIX 494 499 {ECO:0000244|PDB:3HMI}.
HELIX 512 521 {ECO:0000244|PDB:3HMI}.
HELIX 526 528 {ECO:0000244|PDB:3HMI}.
HELIX 532 545 {ECO:0000244|PDB:3HMI}.
HELIX 1069 1071 {ECO:0000244|PDB:2KK1}.
TURN 1076 1078 {ECO:0000244|PDB:2KK1}.
HELIX 1080 1083 {ECO:0000244|PDB:2KK1}.
HELIX 1086 1099 {ECO:0000244|PDB:2KK1}.
HELIX 1106 1123 {ECO:0000244|PDB:2KK1}.
HELIX 1124 1126 {ECO:0000244|PDB:2KK1}.
HELIX 1130 1152 {ECO:0000244|PDB:2KK1}.
STRAND 1155 1158 {ECO:0000244|PDB:2KK1}.
HELIX 1165 1181 {ECO:0000244|PDB:2KK1}.
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


Related products :

Catalog number Product name Quantity
201-20-6763 ABL2{v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene)}mouse.mAb 0.1ml
201-20-6537 ABL2{v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene)}mouse.mAb 0.1ml
CSB-EL001106HU Human v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene) (ABL2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL001106MO Mouse v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene) (ABL2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-PA001106GA01HU Rabbit anti-human v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA001106GA01HU Rabbit anti-human v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
bs-0583P Peptides: ABL1(v-abl Abelson murine leukemia viral oncogene homolog 1) Protein Length:12-25 amino acids. 200ug lyophilized
ABLIM2 ABL2 Gene v-abl Abelson murine leukemia viral oncogene homolog 2
32-104 ABL2(ARG, Abelson-related gene) is a cytoplasmic tyrosine kinase which is closely related to but distinct from ABL1. The similarity of the proteins includes the tyrosine kinase domains and extends ami 0.1 mL
201-20-7128 ABL1{v-abl Abelson murine leukemia viral oncogene homolog 1}rabbit.pAb 0.1ml
18-785-210008 c-Abl (Ab-412) - EC 2.7.10.2; p150; c-ABL; Abelson murine leukemia viral oncogene homolog 1 Polyclonal 0.05 mg
18-785-210008 c-Abl (Ab-412) - EC 2.7.10.2; p150; c-ABL; Abelson murine leukemia viral oncogene homolog 1 Polyclonal 0.1 mg
18-785-210007 c-Abl (Phospho-Tyr412) - EC 2.7.10.2; p150; c-ABL; Abelson murine leukemia viral oncogene homolog 1 Polyclonal 0.1 mg
18-785-210007 c-Abl (Phospho-Tyr412) - EC 2.7.10.2; p150; c-ABL; Abelson murine leukemia viral oncogene homolog 1 Polyclonal 0.05 mg
GWB-42A0EF Abelson Murine Leukemia Viral Oncogene Homolog 1 (ABL1) Rabbit anti-Human Polyclonal (Tyr412) Antibody
E14204h Human V_Abl Abelson Murine Leukemia Viral Oncogene 96T
18-272-196259 c - Abl - Rabbit polyclonal to c - Abl; EC 2.7.10.2; p150; c-ABL; Abelson murine leukemia viral oncogene homolog 1 Polyclonal 0.5 ml
20-272-190242 c - Abl - Mouse monoclonal [ABL - 148] to c - Abl; EC 2.7.10.2; p150; c-ABL; Abelson murine leukemia viral oncogene homolog 1 Monoclonal 0.1 ml
20-272-191354 c-Abl - Mouse monoclonal [19-110] to c-Abl; EC 2.7.10.2; p150; c-ABL; Abelson murine leukemia viral oncogene homolog 1 Monoclonal 0.05 mg
18-272-196261 c - Abl prediluted - Rabbit polyclonal to c - Abl prediluted; EC 2.7.10.2; p150; c-ABL; Abelson murine leukemia viral oncogene homolog 1 Polyclonal 7 ml
PR-337 AblGST SH3 domain Abelson Tyrosine Kinase, SH3 domainhuman, recombinant, E. coli 50
P3588Rb Rabbit anti_ v_abl Abelson murine leukemia viral o 40ug/0.2ml
PR-337 Proteins: AblGST SH3 domain Abelson Tyrosine Kinase, SH3 domainhuman, recombinant, E. coli 50
PR-337 AblGST SH3 domain Abelson Tyrosine Kinase, SH3 domain human, recombinant, E. coli 50
PR-337 AblGST SH3 domain Abelson Tyrosine Kinase, SH3 domain human, recombinant, E. coli 50 µg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur