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

 ABL1_MOUSE              Reviewed;        1123 AA.
P00520; P97896; Q61252; Q61253; Q61254; Q61255; Q61256; Q61257;
Q61258; Q61259; Q61260; Q61261; Q6PCM5; Q8C1X4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 3.
22-NOV-2017, entry version 225.
RecName: Full=Tyrosine-protein kinase ABL1;
EC=2.7.10.2 {ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:19878872, ECO:0000269|PubMed:20072125};
AltName: Full=Abelson murine leukemia viral oncogene homolog 1;
AltName: Full=Abelson tyrosine-protein kinase 1;
AltName: Full=Proto-oncogene c-Abl;
AltName: Full=p150;
Name=Abl1; Synonyms=Abl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
TISSUE=Testis;
PubMed=3317402; DOI=10.1073/pnas.84.23.8200;
Oppi C., Shore S.K., Reddy E.P.;
"Nucleotide sequence of testis-derived c-abl cDNAs: implications for
testis-specific transcription and abl oncogene activation.";
Proc. Natl. Acad. Sci. U.S.A. 84:8200-8204(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
STRAIN=ICR; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IV).
STRAIN=C57BL/6J; 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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187 (ISOFORMS I; II; III AND
IV).
PubMed=7665185; DOI=10.1006/geno.1995.1008;
Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D.,
Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y.,
McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G.,
Heisterkamp N., Groffen J., Roe B.A.;
"Sequence and analysis of the human ABL gene, the BCR gene, and
regions involved in the Philadelphia chromosomal translocation.";
Genomics 27:67-82(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-182.
PubMed=6319018; DOI=10.1016/0092-8674(84)90228-9;
Wang J.Y.J., Ledley F., Goff S., Lee R., Groner Y., Baltimore D.;
"The mouse c-abl locus: molecular cloning and characterization.";
Cell 36:349-356(1984).
[6]
ALTERNATIVE SPLICING.
PubMed=3283651;
Bernards A., Paskind M., Baltimore D.;
"Four murine c-abl mRNAs arise by usage of two transcriptional
promoters and alternative splicing.";
Oncogene 2:297-304(1988).
[7]
PHOSPHORYLATION AT THR-547 AND SER-569.
PubMed=2183353; DOI=10.1126/science.2183353;
Kipreos E.T., Wang J.Y.;
"Differential phosphorylation of c-Abl in cell cycle determined by
cdc2 kinase and phosphatase activity.";
Science 248:217-220(1990).
[8]
DISRUPTION PHENOTYPE.
PubMed=2065352; DOI=10.1016/0092-8674(91)90011-M;
Tybulewicz V.L., Crawford C.E., Jackson P.K., Bronson R.T.,
Mulligan R.C.;
"Neonatal lethality and lymphopenia in mice with a homozygous
disruption of the c-abl proto-oncogene.";
Cell 65:1153-1163(1991).
[9]
DISRUPTION PHENOTYPE.
PubMed=2065353; DOI=10.1016/0092-8674(91)90012-N;
Schwartzberg P.L., Stall A.M., Hardin J.D., Bowdish K.S., Humaran T.,
Boast S., Harbison M.L., Robertson E.J., Goff S.P.;
"Mice homozygous for the ablm1 mutation show poor viability and
depletion of selected B and T cell populations.";
Cell 65:1165-1175(1991).
[10]
DNA-BINDING, DOMAIN, AND PHOSPHORYLATION.
PubMed=1566087; DOI=10.1126/science.256.5055.382;
Kipreos E.T., Wang J.Y.;
"Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA.";
Science 256:382-385(1992).
[11]
FUNCTION.
PubMed=8194526;
Feller S.M., Knudsen B., Hanafusa H.;
"c-Abl kinase regulates the protein binding activity of c-Crk.";
EMBO J. 13:2341-2351(1994).
[12]
FUNCTION.
PubMed=7780740; DOI=10.1016/S0960-9822(95)00060-1;
Mayer B.J., Hirai H., Sakai R.;
"Evidence that SH2 domains promote processive phosphorylation by
protein-tyrosine kinases.";
Curr. Biol. 5:296-305(1995).
[13]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
SER-446, AND MUTAGENESIS OF SER-446.
PubMed=9109492; DOI=10.1038/386732a0;
Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M.,
Weichselbaum R., Weaver D., Kufe D.;
"Functional interaction between DNA-PK and c-Abl in response to DNA
damage.";
Nature 386:732-735(1997).
[14]
SUBCELLULAR LOCATION.
PubMed=9636171; DOI=10.1073/pnas.95.13.7457;
Taagepera S., McDonald D., Loeb J.E., Whitaker L.L., McElroy A.K.,
Wang J.Y., Hope T.J.;
"Nuclear-cytoplasmic shuttling of C-ABL tyrosine kinase.";
Proc. Natl. Acad. Sci. U.S.A. 95:7457-7462(1998).
[15]
IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, AND
INTERACTION WITH CABLES1.
TISSUE=Brain;
PubMed=10896159; DOI=10.1016/S0896-6273(00)81200-3;
Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L.,
Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.;
"Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine
phosphorylation, kinase upregulation, and neurite outgrowth.";
Neuron 26:633-646(2000).
[16]
INTERACTION WITH PSTPIP1.
PubMed=11163214; DOI=10.1016/S1097-2765(00)00138-6;
Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A.,
Goff S.P.;
"Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine
phosphatase to the c-Abl kinase to mediate Abl dephosphorylation.";
Mol. Cell 6:1413-1423(2000).
[17]
REVIEW ON FUNCTION.
PubMed=11114745; DOI=10.1038/sj.onc.1203878;
Wang J.Y.;
"Regulation of cell death by the Abl tyrosine kinase.";
Oncogene 19:5643-5650(2000).
[18]
INTERACTION WITH CRK, AND FUNCTION.
PubMed=11279004; DOI=10.1074/jbc.M100095200;
Kain K.H., Klemke R.L.;
"Inhibition of cell migration by Abl family tyrosine kinases through
uncoupling of Crk-CAS complexes.";
J. Biol. Chem. 276:16185-16192(2001).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11350980; DOI=10.1074/jbc.M101414200;
Kumar S., Bharti A., Mishra N.C., Raina D., Kharbanda S., Saxena S.,
Kufe D.;
"Targeting of the c-Abl tyrosine kinase to mitochondria in the
necrotic cell death response to oxidative stress.";
J. Biol. Chem. 276:17281-17285(2001).
[20]
FUNCTION.
PubMed=11279131; DOI=10.1074/jbc.M100792200;
Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C.,
Schettini G., Sudol M., Russo T.;
"The beta-amyloid precursor protein APP is tyrosine-phosphorylated in
cells expressing a constitutively active form of the Abl
protoncogene.";
J. Biol. Chem. 276:19787-19792(2001).
[21]
INTERACTION WITH ZDHHC16.
PubMed=12021275; DOI=10.1074/jbc.M202388200;
Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.;
"Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has
pro-apoptotic activity.";
J. Biol. Chem. 277:28870-28876(2002).
[22]
FUNCTION.
PubMed=12107171; DOI=10.1074/jbc.M204416200;
Cong F., Tang J., Hwang B.J., Vuong B.Q., Chu G., Goff S.P.;
"Interaction between UV-damaged DNA binding activity proteins and the
c-Abl tyrosine kinase.";
J. Biol. Chem. 277:34870-34878(2002).
[23]
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).
[24]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, INTERACTION
WITH CRK, PHOSPHORYLATION AT TYR-226 AND TYR-393, AND MUTAGENESIS OF
TYR-226; LYS-271 AND TYR-393.
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).
[25]
FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION.
PubMed=14993293; DOI=10.1128/MCB.24.6.2573-2583.2004;
Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.;
"Bidirectional signaling links the Abelson kinases to the platelet-
derived growth factor receptor.";
Mol. Cell. Biol. 24:2573-2583(2004).
[26]
REVIEW ON FUNCTION.
PubMed=15686624; DOI=10.1038/sj.cr.7290261;
Shaul Y., Ben-Yehoyada M.;
"Role of c-Abl in the DNA damage stress response.";
Cell Res. 15:33-35(2005).
[27]
FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION, AND
INTERACTION WITH ITGB1; HCK AND FGR.
PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
Berton G.;
"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
migration.";
FEBS Lett. 584:15-21(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]
FUNCTION, AND INTERACTION WITH TBX21.
PubMed=21690296; DOI=10.1128/MCB.05383-11;
Chen A., Lee S.M., Gao B., Shannon S., Zhu Z., Fang D.;
"c-Abl-mediated tyrosine phosphorylation of the T-bet DNA-binding
domain regulates CD4+ T-cell differentiation and allergic lung
inflammation.";
Mol. Cell. Biol. 31:3445-3456(2011).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
PubMed=7664083; DOI=10.1038/nsb0894-546;
Musacchio A., Saraste M., Wilmanns M.;
"High-resolution crystal structures of tyrosine kinase SH3 domains
complexed with proline-rich peptides.";
Nat. Struct. Biol. 1:546-551(1994).
[31]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515 IN COMPLEX WITH
INHIBITOR STI-571, CATALYTIC ACTIVITY, ENZYME REGULATION,
PHOSPHORYLATION AT TYR-393, AND ACTIVATION LOOP.
PubMed=10988075; DOI=10.1126/science.289.5486.1938;
Schindler T., Bornmann W., Pellicena P., Miller W.T., Clarkson B.,
Kuriyan J.;
"Structural mechanism for STI-571 inhibition of Abelson tyrosine
kinase.";
Science 289:1938-1942(2000).
[32]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 229-515, MYRISTOYLATION AT
GLY-2 (ISOFORM IV), AND ENZYME REGULATION.
PubMed=12654251; DOI=10.1016/S0092-8674(03)00194-6;
Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D.,
Bornmann W., Clarkson B., Superti-Furga G., Kuriyan J.;
"Structural basis for the autoinhibition of c-Abl tyrosine kinase.";
Cell 112:859-871(2003).
[33]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 229-515 OF WILD-TYPE AND
MUTANT ILE-315 IN COMPLEX WITH INHIBITOR PPY-A.
PubMed=17718712; DOI=10.1111/j.1747-0285.2007.00556.x;
Zhou T., Parillon L., Li F., Wang Y., Keats J., Lamore S., Xu Q.,
Shakespeare W., Dalgarno D., Zhu X.;
"Crystal structure of the T315I mutant of AbI kinase.";
Chem. Biol. Drug Des. 70:171-181(2007).
[34]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 229-515 OF MUTANT ILE-315 IN
COMPLEX WITH INHIBITOR AP24534, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=19878872; DOI=10.1016/j.ccr.2009.09.028;
O'Hare T., Shakespeare W.C., Zhu X., Eide C.A., Rivera V.M., Wang F.,
Adrian L.T., Zhou T., Huang W.S., Xu Q., Metcalf C.A. III, Tyner J.W.,
Loriaux M.M., Corbin A.S., Wardwell S., Ning Y., Keats J.A., Wang Y.,
Sundaramoorthi R., Thomas M., Zhou D., Snodgrass J., Commodore L.,
Sawyer T.K., Dalgarno D.C., Deininger M.W., Druker B.J., Clackson T.;
"AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia,
potently inhibits the T315I mutant and overcomes mutation-based
resistance.";
Cancer Cell 16:401-412(2009).
[35]
X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 115-401 IN COMPLEXES WITH
INHIBITORS AP24283 AND AP24163.
PubMed=19895503; DOI=10.1111/j.1747-0285.2009.00905.x;
Zhou T., Commodore L., Huang W.S., Wang Y., Sawyer T.K.,
Shakespeare W.C., Clackson T., Zhu X., Dalgarno D.C.;
"Structural analysis of DFG-in and DFG-out dual Src-Abl inhibitors
sharing a common vinyl purine template.";
Chem. Biol. Drug Des. 75:18-28(2010).
[36]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 115-401 IN COMPLEX WITH
INHIBITORS IMATINIB AND GNF-2, CATALYTIC ACTIVITY, ENZYME REGULATION,
AUTOPHOSPHORYLATION, AND MUTAGENESIS OF PRO-112; TYR-128; TYR-139;
SER-229; THR-315; CYS-464; PRO-465; PHE-497; GLU-505 AND VAL-506.
PubMed=20072125; DOI=10.1038/nature08675;
Zhang J., Adrian F.J., Jahnke W., Cowan-Jacob S.W., Li A.G.,
Iacob R.E., Sim T., Powers J., Dierks C., Sun F., Guo G.R., Ding Q.,
Okram B., Choi Y., Wojciechowski A., Deng X., Liu G., Fendrich G.,
Strauss A., Vajpai N., Grzesiek S., Tuntland T., Liu Y., Bursulaya B.,
Azam M., Manley P.W., Engen J.R., Daley G.Q., Warmuth M., Gray N.S.;
"Targeting Bcr-Abl by combining allosteric with ATP-binding-site
inhibitors.";
Nature 463:501-506(2010).
-!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role
in many key processes linked to cell growth and survival such as
cytoskeleton remodeling in response to extracellular stimuli, cell
motility and adhesion, receptor endocytosis, autophagy, DNA damage
response and apoptosis. Coordinates actin remodeling through
tyrosine phosphorylation of proteins controlling cytoskeleton
dynamics like WASF3 (involved in branch formation); ANXA1
(involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH
(involved in signaling); or MAPT and PXN (microtubule-binding
proteins). Phosphorylation of WASF3 is critical for the
stimulation of lamellipodia formation and cell migration. Involved
in the regulation of cell adhesion and motility through
phosphorylation of key regulators of these processes such as
BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple
receptor tyrosine kinases and more particularly promotes
endocytosis of EGFR, facilitates the formation of neuromuscular
synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and
modulates the endocytosis of activated B-cell receptor complexes.
Other substrates which are involved in endocytosis regulation are
the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL
family of ubiquitin ligases that drive receptor down-regulation
and actin remodeling. Phosphorylation of CBL leads to increased
EGFR stability. Involved in late-stage autophagy by regulating
positively the trafficking and function of lysosomal components.
ABL1 targets to mitochondria in response to oxidative stress and
thereby mediates mitochondrial dysfunction and cell death. In
response to oxidative stress, phosphorylates serine/threonine
kinase PRKD2 at 'Tyr-717' (By similarity). ABL1 is also
translocated in the nucleus where it has DNA-binding activity and
is involved in DNA-damage response and apoptosis. Many substrates
are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6,
RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway
when the DNA damage is too severe to be repaired. Phosphorylates
TP73, a primary regulator for this type of damage-induced
apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191' and
regulates its processing in the apoptotic response to DNA damage.
Phosphorylates PSMA7 that leads to an inhibition of proteasomal
activity and cell cycle transition blocks. Regulates T-cell
differentiation in a TBX21-dependent manner (PubMed:21690296).
Phosphorylates TBX21 on tyrosine residues leading to an
enhancement of its transcriptional activator activity
(PubMed:21690296). {ECO:0000250|UniProtKB:P00519,
ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:11279131,
ECO:0000269|PubMed:11350980, ECO:0000269|PubMed:12107171,
ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293,
ECO:0000269|PubMed:19878872, ECO:0000269|PubMed:19903482,
ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:7780740,
ECO:0000269|PubMed:8194526, ECO:0000269|PubMed:9109492}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:10988075,
ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:19878872,
ECO:0000269|PubMed:20072125}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12748290};
Note=Mg(2+) and Mn(2+) were both present in the kinase buffer but
Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305};
-!- ENZYME REGULATION: Stabilized in the inactive form by an
association between the SH3 domain and the SH2-TK linker region,
interactions of the N-terminal cap, and contributions from an N-
terminal myristoyl group and phospholipids. Activated by
autophosphorylation as well as by SRC-family kinase-mediated
phosphorylation (By similarity). Activated by RIN1 binding to the
SH2 and SH3 domains. Also stimulated by cell death inducers and
DNA-damage (By similarity). Phosphatidylinositol 4,5-bisphosphate
(PIP2), a highly abundant phosphoinositide known to regulate
cytoskeletal and membrane proteins, inhibits also the tyrosine
kinase activity. Inhibited by imatinib mesylate (Gleevec).
{ECO:0000250, ECO:0000269|PubMed:10988075,
ECO:0000269|PubMed:12654251, ECO:0000269|PubMed:12748290,
ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:20072125,
ECO:0000269|PubMed:9109492}.
-!- SUBUNIT: Interacts with INPPL1/SHIP2. Interacts with SORBS1
following insulin stimulation. Found in a trimolecular complex
containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1.
Interacts with ZDHHC16. Interacts with the 14-3-3 proteins, YWHAB,
YWHAE, YWHAG, YWHAH, SFN AND YWHAZ; the interaction with 14-3-3
proteins requires phosphorylation on Thr-734 and sequesters ABL1
into the cytoplasm. Interacts (via SH3 domain) with CASP9; the
interaction is direct and increases in the response of cells to
genotoxic stress and ABL1/c-Abl activation (By similarity).
Interacts with ABI1, ABI2, BCR, CRK, FYN, LYN, PSMA7 RAD9A, RAD51,
RAD52, TP73 and WASF3. A complex made of ABL1, CTTN and MYLK
regulates cortical actin-based cytoskeletal rearrangement critical
to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC)
barrier enhancement. Interacts with STX17; probably phosphorylates
STX17 (By similarity). Interacts with ITGB1, HCK and FGR. Found in
a complex with ABL1, ABL2, CRK and UNC119; leading to the
inhibition of CRK phosphorylation by ABL kinases (By similarity).
Interacts with TBX21 (PubMed:21690296).
{ECO:0000250|UniProtKB:P00519, ECO:0000269|PubMed:10896159,
ECO:0000269|PubMed:11163214, ECO:0000269|PubMed:11279004,
ECO:0000269|PubMed:12021275, ECO:0000269|PubMed:12748290,
ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21690296}.
-!- INTERACTION:
Q8IZP0-4:ABI1 (xeno); NbExp=5; IntAct=EBI-8593082, EBI-8593095;
P46527:CDKN1B (xeno); NbExp=2; IntAct=EBI-914519, EBI-519280;
Q32MD9:Cdon; NbExp=2; IntAct=EBI-914519, EBI-7017034;
P97465:Dok1; NbExp=4; IntAct=EBI-914519, EBI-914917;
P28693-2:EPHB2 (xeno); NbExp=5; IntAct=EBI-914519, EBI-6725926;
Q99M51:Nck1; NbExp=2; IntAct=EBI-914519, EBI-642202;
P97814:Pstpip1; NbExp=5; IntAct=EBI-914519, EBI-7484574;
P70602:Ptpn18 (xeno); NbExp=2; IntAct=EBI-914519, EBI-7484661;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus.
Mitochondrion. Note=The myristoylated c-ABL protein is reported to
be nuclear. Sequestered into the cytoplasm through interaction
with 14-3-3 proteins (By similarity). Localizes to mitochondria in
response to oxidative stress. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=I;
IsoId=P00520-1; Sequence=Displayed;
Name=II;
IsoId=P00520-2; Sequence=VSP_004959;
Name=III;
IsoId=P00520-3; Sequence=VSP_004958;
Name=IV;
IsoId=P00520-4; Sequence=VSP_004960;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2. {ECO:0000269|PubMed:12654251};
-!- TISSUE SPECIFICITY: Widely expressed.
-!- PTM: Acetylated at Lys-710 by EP300 which promotes the cytoplasmic
translocation. {ECO:0000250}.
-!- PTM: Phosphorylation at Tyr-70 by members of the SRC family of
kinases disrupts SH3 domain-based autoinhibitory interactions and
intermolecular associations, such as that with ABI1, and also
enhances kinase activity (By similarity). Phosphorylation at Tyr-
226 and Tyr-393 correlate with increased activity (By similarity).
DNA damage-induced activation of ABL1 requires the function of ATM
and Ser-446 phosphorylation. Phosphorylation at Thr-547 and Ser-
569 has been attributed to a CDC2-associated kinase and is coupled
to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2
increases binding to CRK and reduces binding to ABI1 (By
similarity). Phosphorylation on Thr-734 is required for binding
14-3-3 proteins for cytoplasmic translocation (By similarity).
Phosphorylated by PDGFRB and PRKDC. {ECO:0000250,
ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290,
ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:1566087,
ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:2183353,
ECO:0000269|PubMed:9109492}.
-!- PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to
degradation (By similarity). {ECO:0000250}.
-!- PTM: Isoform IV is myristoylated on Gly-2.
{ECO:0000269|PubMed:12654251}.
-!- DISRUPTION PHENOTYPE: Mutants are born with the expected Mendelian
frequency, but fail to thrive and most die within three weeks
after birth. Most mutants are runted, and have atrophied thymuses
with severe thymocyte deficiency. Mutants that survive to weaning
age are most often runted, and about half of them show
lymphopenia. They display a major reduction in the number of pre-B
and immature B-cell classes in bone marrow with a wide variation
between individuals, but essentially normal mature B-cell levels.
Mutants are highly susceptible to infections.
{ECO:0000269|PubMed:2065352, ECO:0000269|PubMed:2065353}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. ABL subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; J02995; AAA88241.1; -; mRNA.
EMBL; AK090095; BAC41088.1; -; mRNA.
EMBL; BC059260; AAH59260.1; -; mRNA.
EMBL; U14721; AAB60451.1; -; Genomic_DNA.
EMBL; U14720; AAB60451.1; JOINED; Genomic_DNA.
EMBL; U14721; AAB60450.1; -; Genomic_DNA.
EMBL; U14720; AAB60450.1; JOINED; Genomic_DNA.
EMBL; U14721; AAB60448.1; -; Genomic_DNA.
EMBL; U13835; AAB60448.1; JOINED; Genomic_DNA.
EMBL; U14721; AAB60449.1; -; Genomic_DNA.
EMBL; U13835; AAB60449.1; JOINED; Genomic_DNA.
EMBL; X07539; CAA30411.1; -; Genomic_DNA.
EMBL; X07539; CAA30412.1; -; Genomic_DNA.
EMBL; X07540; CAA30413.1; -; Genomic_DNA.
EMBL; X07541; CAA30414.1; -; Genomic_DNA.
EMBL; M12263; AAA37136.1; -; mRNA.
EMBL; M12264; AAA37137.1; -; mRNA.
EMBL; M12265; AAA37138.1; -; mRNA.
EMBL; M12266; AAA37134.1; -; Genomic_DNA.
EMBL; K03228; AAA37135.1; -; mRNA.
CCDS; CCDS15901.1; -. [P00520-1]
CCDS; CCDS50563.1; -. [P00520-4]
PIR; A39962; A39962.
PIR; S00774; S00774.
RefSeq; NP_001106174.1; NM_001112703.2. [P00520-4]
RefSeq; NP_001269974.1; NM_001283045.1. [P00520-3]
RefSeq; NP_001269975.1; NM_001283046.1. [P00520-2]
RefSeq; NP_033724.2; NM_009594.4. [P00520-1]
UniGene; Mm.1318; -.
PDB; 1ABO; X-ray; 2.00 A; A/B=61-121.
PDB; 1ABQ; X-ray; 2.80 A; A=61-121.
PDB; 1FPU; X-ray; 2.40 A; A/B=229-515.
PDB; 1IEP; X-ray; 2.10 A; A/B=229-515.
PDB; 1M52; X-ray; 2.60 A; A/B=229-515.
PDB; 1OPJ; X-ray; 1.75 A; A/B=229-515.
PDB; 1OPK; X-ray; 1.80 A; A=27-515.
PDB; 2HZN; X-ray; 2.70 A; A=229-515.
PDB; 2QOH; X-ray; 1.95 A; A/B=229-515.
PDB; 2Z60; X-ray; 1.95 A; A=229-515.
PDB; 3DK3; X-ray; 2.02 A; A/B=233-514.
PDB; 3DK6; X-ray; 2.02 A; A/B=233-514.
PDB; 3DK7; X-ray; 2.01 A; A/B=233-505.
PDB; 3IK3; X-ray; 1.90 A; A/B=229-513.
PDB; 3K5V; X-ray; 1.74 A; A/B=229-515.
PDB; 3KF4; X-ray; 1.90 A; A/B=229-515.
PDB; 3KFA; X-ray; 1.22 A; A/B=229-515.
PDB; 3MS9; X-ray; 1.80 A; A/B=229-515.
PDB; 3MSS; X-ray; 1.95 A; A/B/C/D=229-515.
PDB; 3OXZ; X-ray; 2.20 A; A=229-511.
PDB; 3OY3; X-ray; 1.95 A; A/B=229-511.
PDB; 5IH2; X-ray; 1.80 A; M/N=757-765.
PDBsum; 1ABO; -.
PDBsum; 1ABQ; -.
PDBsum; 1FPU; -.
PDBsum; 1IEP; -.
PDBsum; 1M52; -.
PDBsum; 1OPJ; -.
PDBsum; 1OPK; -.
PDBsum; 2HZN; -.
PDBsum; 2QOH; -.
PDBsum; 2Z60; -.
PDBsum; 3DK3; -.
PDBsum; 3DK6; -.
PDBsum; 3DK7; -.
PDBsum; 3IK3; -.
PDBsum; 3K5V; -.
PDBsum; 3KF4; -.
PDBsum; 3KFA; -.
PDBsum; 3MS9; -.
PDBsum; 3MSS; -.
PDBsum; 3OXZ; -.
PDBsum; 3OY3; -.
PDBsum; 5IH2; -.
ProteinModelPortal; P00520; -.
SMR; P00520; -.
BioGrid; 197906; 20.
CORUM; P00520; -.
ELM; P00520; -.
IntAct; P00520; 22.
MINT; MINT-85127; -.
STRING; 10090.ENSMUSP00000075167; -.
BindingDB; P00520; -.
ChEMBL; CHEMBL3099; -.
iPTMnet; P00520; -.
PhosphoSitePlus; P00520; -.
MaxQB; P00520; -.
PaxDb; P00520; -.
PeptideAtlas; P00520; -.
PRIDE; P00520; -.
Ensembl; ENSMUST00000028190; ENSMUSP00000028190; ENSMUSG00000026842. [P00520-1]
Ensembl; ENSMUST00000075759; ENSMUSP00000075167; ENSMUSG00000026842. [P00520-4]
GeneID; 11350; -.
KEGG; mmu:11350; -.
UCSC; uc008jdz.3; mouse. [P00520-1]
UCSC; uc033hmk.1; mouse. [P00520-2]
UCSC; uc033hml.1; mouse. [P00520-3]
CTD; 25; -.
MGI; MGI:87859; Abl1.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOVERGEN; HBG004162; -.
InParanoid; P00520; -.
KO; K06619; -.
OMA; GAFRESG; -.
TreeFam; TF105081; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-375170; CDO in myogenesis.
Reactome; R-MMU-428890; Role of ABL in ROBO-SLIT signaling.
Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
EvolutionaryTrace; P00520; -.
PRO; PR:P00520; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026842; -.
CleanEx; MM_ABL1; -.
ExpressionAtlas; P00520; baseline and differential.
Genevisible; P00520; MM.
GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
GO; GO:0031252; C:cell leading edge; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISA:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0051015; F:actin filament binding; IDA:MGI.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046875; F:ephrin receptor binding; IPI:ARUK-UCL.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0019905; F:syntaxin binding; ISO:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0090135; P:actin filament branching; IMP:MGI.
GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
GO; GO:1990051; P:activation of protein kinase C activity; ISO:MGI.
GO; GO:0046632; P:alpha-beta T cell differentiation; IGI:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0042100; P:B cell proliferation; IMP:MGI.
GO; GO:0002322; P:B cell proliferation involved in immune response; IMP:MGI.
GO; GO:0050853; P:B cell receptor signaling pathway; IMP:MGI.
GO; GO:0001922; P:B-1 B cell homeostasis; IMP:MGI.
GO; GO:0060020; P:Bergmann glial cell differentiation; IGI:MGI.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0072358; P:cardiovascular system development; IGI:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
GO; GO:0021587; P:cerebellum morphogenesis; IGI:MGI.
GO; GO:0048668; P:collateral sprouting; IMP:MGI.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; ISO:MGI.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0043542; P:endothelial cell migration; ISO:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
GO; GO:0030035; P:microspike assembly; IDA:MGI.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:MGI.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IGI:MGI.
GO; GO:2000773; P:negative regulation of cellular senescence; IGI:MGI.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IGI:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:MGI.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:MGI.
GO; GO:1900275; P:negative regulation of phospholipase C activity; ISO:MGI.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0001843; P:neural tube closure; IGI:MGI.
GO; GO:0060563; P:neuroepithelial cell differentiation; IGI:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
GO; GO:0030182; P:neuron differentiation; IGI:MGI.
GO; GO:0038189; P:neuropilin signaling pathway; ISO:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISO:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; IMP:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:MGI.
GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
GO; GO:1905555; P:positive regulation blood vessel branching; IMP:BHF-UCL.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
GO; GO:1904531; P:positive regulation of actin filament binding; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:MGI.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; IGI:MGI.
GO; GO:1900042; P:positive regulation of interleukin-2 secretion; IGI:MGI.
GO; GO:1904528; P:positive regulation of microtubule binding; ISO:MGI.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IGI:MGI.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:1901216; P:positive regulation of neuron death; IMP:MGI.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:MGI.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IGI:MGI.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IGI:MGI.
GO; GO:0009791; P:post-embryonic development; IGI:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:MGI.
GO; GO:0030516; P:regulation of axon extension; ISO:MGI.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:MGI.
GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:2000772; P:regulation of cellular senescence; IGI:MGI.
GO; GO:1903053; P:regulation of extracellular matrix organization; IGI:MGI.
GO; GO:0031113; P:regulation of microtubule polymerization; ISO:MGI.
GO; GO:1905244; P:regulation of modification of synaptic structure; IGI:ARUK-UCL.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISO:MGI.
GO; GO:0045580; P:regulation of T cell differentiation; IMP:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0042770; P:signal transduction in response to DNA damage; ISS:UniProtKB.
GO; GO:0048536; P:spleen development; IMP:MGI.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
GO; GO:0002333; P:transitional one stage B cell differentiation; IMP:MGI.
CDD; cd09935; SH2_ABL; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR033221; ABL1.
InterPro; IPR035837; ABL_SH2.
InterPro; IPR015015; F-actin_binding.
InterPro; IPR011009; Kinase-like_dom_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.
PANTHER; PTHR24418:SF88; PTHR24418:SF88; 1.
Pfam; PF08919; F_actin_bind; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00808; FABD; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Autophagy; Cell adhesion; Chromosomal rearrangement;
Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
DNA-binding; Endocytosis; Kinase; Lipoprotein; Magnesium; Manganese;
Metal-binding; Mitochondrion; Myristate; Nucleotide-binding; Nucleus;
Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain;
SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
CHAIN 1 1123 Tyrosine-protein kinase ABL1.
/FTId=PRO_0000088051.
DOMAIN 61 121 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 127 217 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 242 493 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 248 256 ATP. {ECO:0000305}.
NP_BIND 316 322 ATP. {ECO:0000305}.
REGION 1 60 CAP.
REGION 863 961 DNA-binding.
REGION 945 1123 F-actin-binding. {ECO:0000250}.
MOTIF 381 405 Kinase activation loop.
MOTIF 605 609 Nuclear localization signal 1.
{ECO:0000255}.
MOTIF 708 714 Nuclear localization signal 2.
{ECO:0000255}.
MOTIF 761 768 Nuclear localization signal 3.
{ECO:0000255}.
MOTIF 1083 1093 Nuclear export signal.
COMPBIAS 18 22 Poly-Ser.
COMPBIAS 605 609 Poly-Lys.
COMPBIAS 804 1012 Pro-rich.
COMPBIAS 891 897 Poly-Pro.
ACT_SITE 363 363 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 271 271 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 70 70 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 115 115 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 128 128 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 139 139 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 172 172 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 185 185 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 215 215 Phosphotyrosine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 226 226 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12748290}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:P42684}.
MOD_RES 253 253 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 257 257 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 393 393 Phosphotyrosine; by autocatalysis and
SRC-type Tyr-kinases.
{ECO:0000269|PubMed:10988075,
ECO:0000269|PubMed:12748290}.
MOD_RES 413 413 Phosphotyrosine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000269|PubMed:9109492}.
MOD_RES 547 547 Phosphothreonine.
{ECO:0000269|PubMed:2183353}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000269|PubMed:2183353}.
MOD_RES 618 618 Phosphoserine; by PAK2.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 619 619 Phosphoserine; by PAK2.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 658 658 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 710 710 N6-acetyllysine; by EP300.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 717 717 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 734 734 Phosphothreonine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 750 750 Phosphothreonine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 812 812 Phosphothreonine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 821 821 Phosphothreonine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 844 844 Phosphothreonine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 909 909 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
MOD_RES 970 970 Phosphoserine.
{ECO:0000250|UniProtKB:P00519}.
VAR_SEQ 1 26 MLEICLKLVGCKSKKGLSSSSSCYLE -> MISFDLLSDEL
HLKLLVLDV (in isoform II). {ECO:0000305}.
/FTId=VSP_004959.
VAR_SEQ 1 26 MLEICLKLVGCKSKKGLSSSSSCYLE -> MSQRWTYTKCR
VQRDPALPFM (in isoform III).
{ECO:0000305}.
/FTId=VSP_004958.
VAR_SEQ 1 26 MLEICLKLVGCKSKKGLSSSSSCYLE -> MGQQPGKVLGD
QRRPSLPALHFIKGAGKRDSSRHGGPHCNVFVEH (in
isoform IV).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004960.
MUTAGEN 112 112 P->S: Strongly reduced inhibition by GNF-
2. {ECO:0000269|PubMed:20072125}.
MUTAGEN 128 128 Y->D: Strongly reduced inhibition by GNF-
2. {ECO:0000269|PubMed:20072125}.
MUTAGEN 139 139 Y->C: Strongly reduced inhibition by GNF-
2. {ECO:0000269|PubMed:20072125}.
MUTAGEN 226 226 Y->F: Minimal reduction in ability to
autophosphorylate.
{ECO:0000269|PubMed:12748290}.
MUTAGEN 229 229 S->P: Strongly reduced inhibition by GNF-
2. {ECO:0000269|PubMed:20072125}.
MUTAGEN 271 271 K->M: Loss of kinase activity.
{ECO:0000269|PubMed:12748290}.
MUTAGEN 315 315 T->I: Loss of inhibition by imatinib.
Loss of inhibition by GNF-2.
{ECO:0000269|PubMed:20072125}.
MUTAGEN 393 393 Y->F: Minimal reduction in ability to
autophosphorylate.
{ECO:0000269|PubMed:12748290}.
MUTAGEN 446 446 S->A: No effect on basal activity, but
abolishes ionizing radiation-induced
activation. {ECO:0000269|PubMed:9109492}.
MUTAGEN 464 464 C->Y: Loss of inhibition by GNF-2.
{ECO:0000269|PubMed:20072125}.
MUTAGEN 465 465 P->S: Loss of inhibition by GNF-2.
{ECO:0000269|PubMed:20072125}.
MUTAGEN 497 497 F->L: Strongly reduced inhibition by GNF-
2. {ECO:0000269|PubMed:20072125}.
MUTAGEN 505 505 E->K: Loss of inhibition by GNF-2.
{ECO:0000269|PubMed:20072125}.
MUTAGEN 506 506 V->L: Strongly reduced inhibition by GNF-
2. {ECO:0000269|PubMed:20072125}.
MUTAGEN 1083 1083 L->A: Loss of nuclear export.
CONFLICT 184 187 LYVS -> VGDW (in Ref. 4; AAB60451/
AAB60450). {ECO:0000305}.
CONFLICT 782 786 PPRLV -> LPGWL (in Ref. 1; AAA88241).
{ECO:0000305}.
CONFLICT 987 987 D -> G (in Ref. 2; BAC41088).
{ECO:0000305}.
STRAND 65 70 {ECO:0000244|PDB:1OPK}.
STRAND 76 79 {ECO:0000244|PDB:1ABQ}.
STRAND 87 93 {ECO:0000244|PDB:1OPK}.
STRAND 97 103 {ECO:0000244|PDB:1OPK}.
STRAND 108 112 {ECO:0000244|PDB:1OPK}.
HELIX 113 115 {ECO:0000244|PDB:1OPK}.
STRAND 116 121 {ECO:0000244|PDB:1OPK}.
HELIX 122 124 {ECO:0000244|PDB:1OPK}.
STRAND 128 131 {ECO:0000244|PDB:1OPK}.
HELIX 134 140 {ECO:0000244|PDB:1OPK}.
HELIX 141 143 {ECO:0000244|PDB:1OPK}.
STRAND 148 153 {ECO:0000244|PDB:1OPK}.
STRAND 155 157 {ECO:0000244|PDB:1OPK}.
STRAND 161 167 {ECO:0000244|PDB:1OPK}.
STRAND 170 175 {ECO:0000244|PDB:1OPK}.
STRAND 184 187 {ECO:0000244|PDB:1OPK}.
STRAND 192 194 {ECO:0000244|PDB:1OPK}.
HELIX 195 202 {ECO:0000244|PDB:1OPK}.
STRAND 209 211 {ECO:0000244|PDB:1OPK}.
STRAND 226 228 {ECO:0000244|PDB:1OPK}.
STRAND 230 233 {ECO:0000244|PDB:1OPK}.
HELIX 239 241 {ECO:0000244|PDB:3KFA}.
STRAND 242 248 {ECO:0000244|PDB:3KFA}.
HELIX 249 251 {ECO:0000244|PDB:3KFA}.
STRAND 255 261 {ECO:0000244|PDB:3KFA}.
HELIX 262 264 {ECO:0000244|PDB:3KFA}.
STRAND 266 273 {ECO:0000244|PDB:3KFA}.
STRAND 275 278 {ECO:0000244|PDB:1OPK}.
HELIX 280 292 {ECO:0000244|PDB:3KFA}.
STRAND 301 305 {ECO:0000244|PDB:3KFA}.
STRAND 307 316 {ECO:0000244|PDB:3KFA}.
HELIX 323 329 {ECO:0000244|PDB:3KFA}.
TURN 332 334 {ECO:0000244|PDB:3KFA}.
HELIX 337 357 {ECO:0000244|PDB:3KFA}.
STRAND 359 362 {ECO:0000244|PDB:1M52}.
HELIX 366 368 {ECO:0000244|PDB:3KFA}.
STRAND 369 371 {ECO:0000244|PDB:3KFA}.
HELIX 373 375 {ECO:0000244|PDB:3KFA}.
STRAND 377 379 {ECO:0000244|PDB:3KFA}.
HELIX 384 386 {ECO:0000244|PDB:3KFA}.
STRAND 390 396 {ECO:0000244|PDB:3KFA}.
STRAND 399 401 {ECO:0000244|PDB:3KFA}.
HELIX 403 405 {ECO:0000244|PDB:3KFA}.
HELIX 408 413 {ECO:0000244|PDB:3KFA}.
HELIX 418 433 {ECO:0000244|PDB:3KFA}.
STRAND 439 442 {ECO:0000244|PDB:2HZN}.
HELIX 445 447 {ECO:0000244|PDB:3KFA}.
HELIX 448 453 {ECO:0000244|PDB:3KFA}.
HELIX 466 475 {ECO:0000244|PDB:3KFA}.
HELIX 480 482 {ECO:0000244|PDB:3KFA}.
HELIX 486 509 {ECO:0000244|PDB:3KFA}.
SEQUENCE 1123 AA; 122673 MW; BD48ADE8557AE95C CRC64;
MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE
NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN
SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS
DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT
DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA MEYLEKKNFI
HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS
DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP
SDRPSFAEIH QAFETMFQES SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE
QKDAPDTPEL LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF
SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS DAAEPTKSPK
ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA EEESGMSSSK RFLRSCSASC
MPHGARDTEW RSVTLPRDLP SAGKQFDSST FGGHKSEKPA LPRKRTSESR SEQVAKSTAM
PPPRLVKKNE EAAEEGFKDT ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS
GMGTPATAEP APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT
GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP VPPSVPKPQS
TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS TRVSLRKTRQ PPERIASGTI
TKGVVLDSTE ALCLAISRNS EQMASHSAVL EAGKNLYTFC VSYVDSIQQM RNKFAFREAI
NKLESNLREL QICPATASSG PAATQDFSKL LSSVKEISDI VRR


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