Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-255812	Tyr1007	VLPQDKEyYKVKEPG	Mus musculus
pmid	sentence
11593427	In this report, we show that Bcr–Abl forms a complex with Jak2, and induces tyrosine phosphorylation of Jak2; full phosphorylation requires the SH2 domain of Bcr–Abl. We found that Y1007 of Jak2 was phosphorylated in Bcr–Abl positive cells; phosphorylation of Jak2 Y1007 is known to be required for Jak2 kinase activation.

Publications:

1

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML

Identifier	Residue	Sequence	Organism
SIGNOR-262531	Tyr104	DLNNGKFyVGVCAFV	Homo sapiens
pmid	sentence
23836560	Have found that BCR-ABL1 interacts with the C-terminal portion of RAD52, resulting in tyrosine phosphorylation of Y104 located in RAD52 DNA II and enhanced nuclear foci formation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247146	Tyr160	QVPQQPTyVQALFDF	Homo sapiens	HEK-293 Cell
pmid	sentence
20554525	Our data show that BCR-ABL also phosphorylates Grb2 in Tyr160Previous reports suggested an inhibitory role of Grb2 Tyr7, Tyr37, Tyr52, and Tyr209 phosphorylation in receptor tyrosine kinase signaling (16) (43). Instead, in our system Grb2 Tyr160 mutation was not show to have a role in ALCL proliferation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271703	Tyr171	IPTSAPVyQQPQQQP	Homo sapiens	K-562 Cell
pmid	sentence
24913448	LASP1 is a novel BCR-ABL substrate and a phosphorylation-dependent binding partner of CRKL in chronic myeloid leukemia\|We demonstrate that LASP1 is specifically phosphorylated by BCR-ABL at tyrosine-171 in CML patients

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-40611	Tyr177	ADAEKPFyVNVEFHH	Homo sapiens
pmid	sentence
8622703	We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrosine 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr.

Identifier	Residue	Sequence	Organism
SIGNOR-260829	Tyr328	YSPRSFEdCGGGYTP	Homo sapiens
pmid	sentence
9467953	Thus, we propose that the phosphorylation of tyrosine 328 and 360 within Bcr by Bcr ± Abl will drastically interfere with Bcr's kinase role in either signal transduction or some other cellular mechanism.

Identifier	Residue	Sequence	Organism
SIGNOR-262530	Tyr360	VSPSPTTyRMFRDKS	Chlorocebus aethiops
pmid	sentence
8622703	These results indicate that tyrosine phosphorylation of Bcr by Bcr-Abl inhibits Bcr‚Äôs serine/threonine kinase activity.

Identifier	Residue	Sequence	Organism
SIGNOR-260828	Tyr360	YSPRSFEdCGGGYTP	Homo sapiens
pmid	sentence
9467953	Thus, we propose that the phosphorylation of tyrosine 328 and 360 within Bcr by Bcr-Abl will drastically interfere with Bcr's kinase role in either signal transduction or some other cellular mechanism.

Publications:

4

Organism:

Homo Sapiens, Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-53964	Tyr177	ADAEKPFyVNVEFHH	Homo sapiens
pmid	sentence
9407116	The src family kinase hck interacts with bcr-abl by a kinase-independent mechanism and phosphorylates the grb2-binding site of bcr

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-46893	Tyr207	IPEPAHAyAQPQTTT	Homo sapiens	Leukemia Cell
pmid	sentence
9053848	Tyrosine 207 in crkl is the bcr/abl phosphorylation sitephosphorylation of y207 provides a binding site for the crkl sh2 domain and potentially for other sh2-containing proteins.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-112354	Tyr209	TGMFPRNyVTPVNRN	Homo sapiens	A-431 Cell
pmid	sentence
11726515	Phosphorylation of grb2 by bcr/abl or egf receptor reduced its sh3-dependent binding to sos in vivo, but not its sh2-dependent binding to bcr/abl. Tyr209 within the c-terminal sh3 domain of grb2 was identified as one of the tyrosine phosphorylation sites

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246281	Tyr209	TGMFPRNyVTPVNRN	Homo sapiens	HEK-293 Cell
pmid	sentence
20554525	More recently, however, tyrosine phosphorylation of Grb2 in BCR-ABL-transformed cells on residues Tyr7, Tyr37, Tyr52, and Tyr209 in the SH3 domains has been reported and shown to negatively regulate the Ras/MAPK pathway.

Identifier	Residue	Sequence	Organism
SIGNOR-246289	Tyr37	EECDQNWyKAELNGK	Homo sapiens
pmid	sentence
20554525	More recently, however, tyrosine phosphorylation of Grb2 in BCR-ABL-transformed cells on residues Tyr7, Tyr37, Tyr52, and Tyr209 in the SH3 domains has been reported and shown to negatively regulate the Ras/MAPK pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246293	Tyr52	DGFIPKNyIEMKPHP	Homo sapiens	HEK-293 Cell
pmid	sentence
20554525	More recently, however, tyrosine phosphorylation of Grb2 in BCR-ABL-transformed cells on residues Tyr7, Tyr37, Tyr52, and Tyr209 in the SH3 domains has been reported and shown to negatively regulate the Ras/MAPK pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246285	Tyr7	yDFKATAD	Homo sapiens	HEK-293 Cell
pmid	sentence
20554525	More recently, however, tyrosine phosphorylation of Grb2 in BCR-ABL-transformed cells on residues Tyr7, Tyr37, Tyr52, and Tyr209 in the SH3 domains has been reported and shown to negatively regulate the Ras/MAPK pathway.

Publications:

4

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-40615	Tyr283	YQPYQSIyVGGMMEG	Homo sapiens	Leukemia Cell
pmid	sentence
8622703	We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrose 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-40619	Tyr360	VSPSPTTyRMFRDKS	Homo sapiens	Leukemia Cell
pmid	sentence
8622703	We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrose 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271707	Tyr315	ETRICKIyDSPCLPE	Homo sapiens	32D Cell
pmid	sentence
11684015	RAD51 is one of six mitotic human homologs of the E. coli RecA protein (RAD51-Paralogs) that play a central role in homologous recombination and repair of DNA double-strand breaks (DSBs).\|Phosphorylation of the RAD51 Tyr-315 residue by BCR/ABL appears essential for enhanced DSB repair and drug resistance.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271700	Tyr34	KDQFPEVyVPTVFEN	Homo sapiens	HeLa Cell
pmid	sentence
23027962	When these RhoA mutants were coexpressed with Bcr-Abl, phosphorylation levels of Y34F and Y66F RhoA mutants dramatically decreased to 32% and 17%, respectively. As expected, when Y34 and Y66 were both mutated to phenylalanine, phosphorylation was completely abolished. Together, these observations indicate that Y34 and Y66 are the two predominant phosphorylation sites, and that the Src kinase and Bcr-Abl are the two candidate kinases that may phosphorylate these sites.\|In contrast to active RhoA, RhoAQ63L(Y34,66E) had a dramatic decrease in RBD binding. This binding fraction was even lower than that of WT RhoA, suggesting phosphorylation at these sites could have a negative effect on RhoA activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271699	Tyr66	DTAGQEDyDRLRPLS	Homo sapiens	HeLa Cell
pmid	sentence
23027962	When these RhoA mutants were coexpressed with Bcr-Abl, phosphorylation levels of Y34F and Y66F RhoA mutants dramatically decreased to 32% and 17%, respectively. As expected, when Y34 and Y66 were both mutated to phenylalanine, phosphorylation was completely abolished. Together, these observations indicate that Y34 and Y66 are the two predominant phosphorylation sites, and that the Src kinase and Bcr-Abl are the two candidate kinases that may phosphorylate these sites.\|In contrast to active RhoA, RhoAQ63L(Y34,66E) had a dramatic decrease in RBD binding. This binding fraction was even lower than that of WT RhoA, suggesting phosphorylation at these sites could have a negative effect on RhoA activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-153431	Tyr654	RNEGVATyAAAVLFR	Homo sapiens	Leukemia Cell
pmid	sentence
17318191	Bcr-abl stabilizes beta-catenin in chronic myeloid leukemia through its tyrosine phosphorylationthe notion that y86 and y654 are located respectively within the n_ and c_terminal transcriptional domains of __catenin suggests that one or both residues might regulate the transactivating function of __catenin. In this regard, phosphorylation of y654 was reported to strengthen __catenin association with the basal transcription factor tata_binding protein (tbp)

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, Onco-fusion proteins in AML

Identifier	Residue	Sequence	Organism
SIGNOR-260810	Tyr730	PNLFVALyDFVASGD	Homo sapiens
pmid	sentence
16912036	Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. \| Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.

Identifier	Residue	Sequence	Organism
SIGNOR-260811	Tyr775	QGWVPSNyITPVNSL	Homo sapiens
pmid	sentence
16912036	Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. \| Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.

Identifier	Residue	Sequence	Organism
SIGNOR-260813	Tyr788	SLEKHSWyHGPVSRN	Homo sapiens
pmid	sentence
16912036	Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. \| Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.

Identifier	Residue	Sequence	Organism
SIGNOR-260812	Tyr798	VSRNAAEyLLSSGIN	Homo sapiens
pmid	sentence
16912036	Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. \| Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.

Identifier	Residue	Sequence	Organism
SIGNOR-260814	Tyr832	LRYEGRVyHYRINTA	Homo sapiens
pmid	sentence
16912036	Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. \| Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.

Identifier	Residue	Sequence	Organism
SIGNOR-260815	Tyr845	TASDGKLyVSSESRF	Homo sapiens
pmid	sentence
16912036	Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. \| Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.

Identifier	Residue	Sequence	Organism
SIGNOR-260816	Tyr875	GLITTLHyPAPKRNK	Homo sapiens
pmid	sentence
16912036	Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. \| Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.

Publications:

7

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-153435	Tyr86	VADIDGQyAMTRAQR	Homo sapiens	Leukemia Cell
pmid	sentence
17318191	Bcr_abl_mediated phosphorylation of y86 could induce a conformational change of __catenin impairing its binding to axin

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, Onco-fusion proteins in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-259270		Homo sapiens	Myeloid Leukemia Cell
pmid	sentence
23409026	Pre-existing BCR-ABL mutations can be detected in a substantial number of chronic-phase CML patients by sensitive allele-specific PCR technique using CD34+ cells. These mutations are associated with imatinib resistance if affecting drug binding directly or indirectly. After the recent approval of nilotinib, dasatinib, bosutinib and ponatinib for treatment of chronic myeloid leukemia along with imatinib, all of which vary in their effectiveness against mutated BCR-ABL forms, detection of pre-existing BCR-ABL mutations can help in selection of appropriate first-line drug therapy.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-255820		Homo sapiens	HEK-293T Cell
pmid	sentence
11726515	However, direct binding of Grb2 to Bcr/Abl also facilitates its tyrosine phosphorylation, which we propose reflects activation of a physiological negative regulatory mechanism by this oncogenic tyrosine kinase.Direct binding of Grb2 to Bcr/Abl facilitates Grb2 phosphorylation.

Identifier	Residue	Organism	Cell Line
SIGNOR-248199		Chlorocebus aethiops	COS-7 Cell
pmid	sentence
8402896	BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein. Mutation of Y177 to phenylalanine (Y177F) abolishes GRB-2 binding and abrogates BCR-ABL-induced Ras activation

Publications:

2

Organism:

Homo Sapiens, Chlorocebus Aethiops

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-272145		Homo sapiens	Chronic Myeloid Leukemia Cell Line
pmid	sentence
34902205	RUNX1 transactivates BCR-ABL1 expression in Philadelphia chromosome positive acute lymphoblastic leukemia.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, Onco-fusion proteins in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-259268		Homo sapiens	Myeloid Leukemia Cell
pmid	sentence
23409026	Pre-existing BCR-ABL mutations can be detected in a substantial number of chronic-phase CML patients by sensitive allele-specific PCR technique using CD34+ cells. These mutations are associated with imatinib resistance if affecting drug binding directly or indirectly. After the recent approval of nilotinib, dasatinib, bosutinib and ponatinib for treatment of chronic myeloid leukemia along with imatinib, all of which vary in their effectiveness against mutated BCR-ABL forms, detection of pre-existing BCR-ABL mutations can help in selection of appropriate first-line drug therapy.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-255818		Homo sapiens
pmid	sentence
19108785	Nilotinib is an oral second-generation bcr-abl TKI indicated for the treatment of imatinib resistant or -intolerant Ph+ CML-CP and -AP in adults. Nilotinib binds to inactive configuration of the abl kinase, thus preventing the tyrosine phosphorylation of proteins involved in bcr-abl signal transduction. Nilotinib binds to the inactive (unphosphorylated) configuration of the abl TK, with the P-Ioop folding over, disrupting the ATP binding site and catalytic activity of the enzyme.

Identifier	Residue	Organism	Cell Line
SIGNOR-259269		Homo sapiens	Myeloid Leukemia Cell
pmid	sentence
23409026	Pre-existing BCR-ABL mutations can be detected in a substantial number of chronic-phase CML patients by sensitive allele-specific PCR technique using CD34+ cells. These mutations are associated with imatinib resistance if affecting drug binding directly or indirectly. After the recent approval of nilotinib, dasatinib, bosutinib and ponatinib for treatment of chronic myeloid leukemia along with imatinib, all of which vary in their effectiveness against mutated BCR-ABL forms, detection of pre-existing BCR-ABL mutations can help in selection of appropriate first-line drug therapy.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-194640		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-271704		Homo sapiens	32D Cell
pmid	sentence
11684015	BCR/ABL Tyrosine Kinase Enhances Expression of RAD51 by Stimulation of STAT5-Mediated Transactivation and Inhibition of Caspase-3-Dependent Degradation\|

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-261506		Chlorocebus aethiops
pmid	sentence
8402896	BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein. Mutation of Y177 to phenylalanine (Y177F) abolishes GRB-2 binding and abrogates BCR-ABL-induced Ras activation.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

Acute Myeloid Leukemia, Onco-fusion proteins in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-114094		Homo sapiens	Leukemia Cell
pmid	sentence
11790798	Thus, the c-terminal tail of vav serves as a direct substrate of bcr-abl in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190224		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-256123		Mus musculus	Bone Marrow Stem Cell
pmid	sentence
14500898	This up-regulation required BCR-ABL tyrosine kinase activity and led to IL-3Rbetac/beta chain tyrosine phosphorylation in the absence of detectable IL-3 production. These results suggested that cytokine-independent IL-3 receptor activation could be a dominant signaling component in BCR-ABL-induced leukemogenesis. However, the IL-3Rβc/β chain could act as a cofactor in BCR-ABL-induced leukemogenesis by activation of its many known oncogenic signaling pathways.

Identifier	Residue	Organism	Cell Line
SIGNOR-255999		Homo sapiens	M-07E Cell
pmid	sentence
8758906	We demonstrated that Bcr-Abl co-immunoprecipitates with, and constitutively phosphorylates, the common βc,subunit of the interleukin 3 and granulocyte/macrophage-colony stimulating factor receptors.We demonstrate that Bcr-Abl interacts with the common βc subunit of the IL-3 family of receptors and phosphorylates it on tyrosine.

Publications:

2

Organism:

Mus Musculus, Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-260080		Homo sapiens	Chronic Myeloid Leukemia Cell
pmid	sentence
31374292	PTEN targets the protein phosphatase activity of BCR-ABL. PTEN has the same function as PTP1B, which can regulate BCR-ABL dephosphorylation [13]. However, whether PTEN can mediate BCR-ABL dephosphorylation remains unknown. We found that under-expression of PTEN significantly upregulated phosphorylation level of BCR-ABL. In order to verify the mechanisms, co-IP assays were applied, demonstrating the ways in which PTEN and BCR-ABL interact with each other.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-255813		Mus musculus	32D Cell
pmid	sentence
8642285	Phosphorylation of STAT1 and STAT5 was directly due to the tyrosine kinase activity of Bcr/Abl since it could be activated or deactivated by temperature shifting of cells expressing the Bcr/Abl ts mutant.These data suggest that STATs can be activated directly by Bcr/Abl, possibly bypassing JAK family kinase activation.

Publications:

1

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML

Identifier	Residue	Organism	Cell Line
SIGNOR-271705		Homo sapiens	32D Cell
pmid	sentence
11684015	BCR/ABL Tyrosine Kinase Enhances Expression of RAD51 by Stimulation of STAT5-Mediated Transactivation and Inhibition of Caspase-3-Dependent Degradation\|

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-272143		Homo sapiens	K-562 Cell, LAMA-84 Cell
pmid	sentence
26179066	In the present study we demonstrate that MYC and its partner MAX bind to the BCR promoter, leading to up-regulation of BCR and BCR/ABL1 at both transcriptional and protein levels.\|Here we describe a regulatory pathway modulating BCR and BCR/ABL1 expression, showing that the BCR promoter is under the transcriptional control of the MYC/MAX heterodimer.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, BCR-ABL in AML

Identifier	Residue	Organism
SIGNOR-56822		Homo sapiens
pmid	sentence
9566916	We have observed association and dephosphorylation of p210 bcr-abl, but not v-abl, by ptp1b in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-259357		Homo sapiens	Myeloid Leukemia Cell Line
pmid	sentence
15206509	Imatinib mesylate (Gleevec/Glivec, Novartis, Basel, Switzerland), formerly called STI571, is a specific and potent inhibitor of the BCR-ABL tyrosine kinase, the molecular hallmark of chronic myeloid leukaemia.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-259271		Homo sapiens	Myeloid Leukemia Cell
pmid	sentence
23409026	Pre-existing BCR-ABL mutations can be detected in a substantial number of chronic-phase CML patients by sensitive allele-specific PCR technique using CD34+ cells. These mutations are associated with imatinib resistance if affecting drug binding directly or indirectly. After the recent approval of nilotinib, dasatinib, bosutinib and ponatinib for treatment of chronic myeloid leukemia along with imatinib, all of which vary in their effectiveness against mutated BCR-ABL forms, detection of pre-existing BCR-ABL mutations can help in selection of appropriate first-line drug therapy.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-255819		Homo sapiens
pmid	sentence
21154127	Bafetinib (NS-187, INNO-406) is a second-generation tyrosine kinase inhibitor in development by CytRx under license from Nippon Shinyaku for treating Bcr-Abl+ leukemia's, including chronic myelogenous leukemia (CML) and Philadelphia+ acute lymphoblastic leukemia. It is a rationally developed tyrosine kinase inhibitor based on the chemical structure of imatinib, with modifications added to improve binding and potency against Bcr-Abl kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-255814		Homo sapiens	M-07E Cell
pmid	sentence
8758906	We demonstrated that Bcr-Abl co-immunoprecipitates with, and constitutively phosphorylates, the common βc,subunit of the interleukin 3 and granulocyte/macrophage-colony stimulating factor receptors.We demonstrate that Bcr-Abl interacts with the common βc subunit of the IL-3 family of receptors and phosphorylates it on tyrosine.

Publications:

1

Organism:

Homo Sapiens

Name	BCR-ABL View Modifications
Primary ID	SIGNOR-FP6
Type	Fusion Protein
Formed by	P00519, P11274
Description	The hallmark genetic abnormality of CML is a t(9;22)(q34;q11) translocation, which was first discovered as an abnormal, small chromosome, named the Philadelphia chromosome. . The ABL gene from chromosome 9 joins to the BCR gene on chromosome 22, to form the BCR-ABL fusion gene. The Abl gene expresses a membrane-associated protein, a tyrosine kinase, and the BCR-Abl transcript is also translated into a tyrosine kinase. Since ABL activates a number of cell cycle-controlling proteins and enzymes, the result of the BCR-Abl fusion is to speed up cell division. Moreover, it inhibits DNA repair, causing genomic instability and potentially causing the feared blast crisis in CML. Finally, the BCR-ABL fusion gene is found in most patients with chronic myelogenous leukemia (CML), and in some patients with acute lymphoblastic leukemia (ALL) or acute myelogenous leukemia (AML).
Sequence	MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKSDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSKALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR
Relations	52
Pathways	Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML

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