Relation Results

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-48818	Ser446	PYPGIDLsQVYELLE	Homo sapiens	Neuron
pmid	sentence
9168116	Ataxia telangiectasia mutant protein activates c-abl tyrosine kinase in response to ionizing radiation. Atm kinase domain corrects this defect, as it phosphorylates the c-abl tyrosine kinase in vitro at ser 465, leading to the activation of c-abl.

Identifier	Residue	Organism
SIGNOR-48822		Homo sapiens
pmid	sentence
9168117	Our results demonstrate that the sh3 domain of c-abl interacts with a dpapnpphfp motif (residues 1,373-1,382) of atm.These findings indicate that atm is involved in the activation of c-abl by dna damag

Publications:

2

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-160215	Ser618	APTPPKRsSSFREMD	Homo sapiens
pmid	sentence
18161990	The interaction of c-abl with the abl interactor protein abi2 is shown to be negatively regulated by phosphorylation of serines 637 and 638. These serines are adjacent to the pxxp motif (ptppkrs637s638sfr) that binds the sh3 domain of abi. phosphorylation of c-abl by pak2 inhibits the interaction between the sh3 domain of abi2 and the pxxp motif of c-abl.

Identifier	Residue	Sequence	Organism
SIGNOR-160219	Ser619	PTPPKRSsSFREMDG	Homo sapiens
pmid	sentence
18161990	The interaction of c-abl with the abl interactor protein abi2 is shown to be negatively regulated by phosphorylation of serines 637 and 638. These serines are adjacent to the pxxp motif (ptppkrs637s638sfr) that binds the sh3 domain of abi. phosphorylation of c-abl by pak2 inhibits the interaction between the sh3 domain of abi2 and the pxxp motif of c-abl.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276497	Thr178	VYHYRINtASDGKLY	in vitro
pmid	sentence
23852372	Inhibition of c-Abl by Lats2 was mediated through Lats2 interaction with and phosphorylation of c-Abl. Lats2 phosphorylates c-Abl at Thr197 in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-181052	Thr735	DTEWRSVtLPRDLQS	Homo sapiens
pmid	sentence
18794806	Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181060	Thr735	DTEWRSVtLPRDLQS	Homo sapiens
pmid	sentence
18794806	Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181056	Thr735	DTEWRSVtLPRDLQS	Homo sapiens
pmid	sentence
18794806	Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181064	Thr735	DTEWRSVtLPRDLQS	Homo sapiens
pmid	sentence
18794806	Ttk phosphorylation of thr735 was associated with partial inhibition of nuclear targeting of c-abl.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181031	Thr735	DTEWRSVtLPRDLQS	Homo sapiens
pmid	sentence
18794806	Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276002	Tyr1003	KGKKFLQyNRLQLSR	Homo sapiens	HEK-293T Cell
pmid	sentence
12652307	C-Abl induces Tyr phosphorylation of PLC-γ1 in vivo. These findings demonstrate that c-Abl phosphorylates PLC-γ1 in vivo predominantly at Tyr 771 and Tyr 1003.c-Abl phosphorylation of PLC-γ1 causes downregulation of PLC activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276001	Tyr771	IGTAEPDyGALYEGR	Homo sapiens	HEK-293T Cell
pmid	sentence
12652307	C-Abl induces Tyr phosphorylation of PLC-γ1 in vivo. These findings demonstrate that c-Abl phosphorylates PLC-γ1 in vivo predominantly at Tyr 771 and Tyr 1003.c-Abl phosphorylation of PLC-γ1 causes downregulation of PLC activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-245365	Tyr1007	VLPQDKEyYKVKEPG	in vitro
pmid	sentence
11593427	Jak2 peptide substrate studies indicated that the Bcr-Abl and Abl tyrosine kinases specifically phosphorylated Y1007 of Jak2 but only poorly phosphorylated Y1008. Phosphorylation of Y1007 of Jak2 is known to be critical for its tyrosine kinase activation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262297	Tyr102	YDLKLQEyQSAIKVE	Mus musculus	HEK-293 Cell, 3T3-L1 Cell
pmid	sentence
25368164	We show that the tyrosine kinase Abelson murine leukemia viral oncogene (cAbl) is an adipogenic key regulator. c-Abl promotes adipogenesis by phosphorylation and subsequent stabilization of PPARγ.

Identifier	Residue	Sequence	Organism
SIGNOR-255912	Tyr78	SSISTPHyEDIPFTR	Mus musculus
pmid	sentence
25368164	We show that the tyrosine kinase Abelson murine leukemia viral oncogene (cAbl) is an adipogenic key regulator. c-Abl promotes adipogenesis by phosphorylation and subsequent stabilization of PPARγ.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273536	Tyr104	KPEQQMMyAGSKNRL	Homo sapiens	Respiratory Smooth Muscle
pmid	sentence
24818551	Acetylcholine stimulation also increased GMF-γ phosphorylation at Tyr-104. GMF-γ phosphorylation at this residue was mediated by c-Abl tyrosine kinase. The GMF-γ mutant Y104F (phenylalanine substitution at Tyr-104) had higher association with Arp2 in HASM cells upon contractile activation.Furthermore, expression of mutant Y104F GMF-γ attenuated actin polymerization and contraction in smooth muscle.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251435	Tyr104	DLNNGKFyVGVCAFV	Homo sapiens	HEK-293 Cell
pmid	sentence
12379650	C-Abl tyrosine kinase associates with and phosphorylates Rad52 on tyrosine 104. he functional significance of c-Abl-dependent phosphorylation of Rad52 is underscored by our findings that cells that express the phosphorylation-resistant Rad52 mutant, in which tyrosine 104 is replaced by phenylalanine, exhibit compromised nuclear foci formation in response to IR.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247661	Tyr104	DLNNGKFyVGVCAFV	Homo sapiens	HEK-293 Cell
pmid	sentence
12379650	We show here that c-Abl tyrosine kinase associates with and phosphorylates Rad52 on tyrosine 104. Importantly, the very same site of Rad52 is phosphorylated on exposure of cells to ionizing radiation (IR).

Publications:

2

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-196043	Tyr105	VDPGERLyDLNMPAY	Homo sapiens
pmid	sentence
22327338	Activated c-abl reduces the amplitude of mitogen-activated protein kinases (erk1/2, jnks and p38) activation in a dose-dependent manner by a negative feedback mechanism. By analysis of the adaptor proteins nck1 and grb2 mutants we further show that the negative loop on p38 is mediated by c-abl phosphorylation at tyrosine 105 of the adaptor protein nck1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260937	Tyr106	EDPVTVEyITRYIAS	Homo sapiens
pmid	sentence
25620702	PSMA7 degradation is suppressed by c-Abl-mediated tyrosine phosphorylation at Y106

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-166493	Tyr107	AYPATGPyGAPAGPL	Homo sapiens
pmid	sentence
20600357	In this report we have identified novel tyrosine phosphorylation sites in galectin-3 as well as the kinase responsible for its phosphorylation. Our results demonstrate that tyrosines at positions 79, 107 and 118 can be phosphorylated in vitro and in vivo by c-abl kinase. our results demonstrate that cells expressing galectin-3 y107f variant showed reduced migration in wound healing assay ( fig. 5). This result confirms the role of galectin-3 tyrosine phosphorylation in cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-166497	Tyr118	AGPLIVPyNLPLPGG	Homo sapiens
pmid	sentence
20600357	In this report we have identified novel tyrosine phosphorylation sites in galectin-3 as well as the kinase responsible for its phosphorylation. Our results demonstrate that tyrosines at positions 79, 107 and 118 can be phosphorylated in vitro and in vivo by c-abl kinase. our results demonstrate that cells expressing galectin-3 y107f variant showed reduced migration in wound healing assay ( fig. 5). This result confirms the role of galectin-3 tyrosine phosphorylation in cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-166501	Tyr79	GAPAPGVyPGPPSGP	Homo sapiens
pmid	sentence
20600357	In this report we have identified novel tyrosine phosphorylation sites in galectin-3 as well as the kinase responsible for its phosphorylation. Our results demonstrate that tyrosines at positions 79, 107 and 118 can be phosphorylated in vitro and in vivo by c-abl kinase. our results demonstrate that cells expressing galectin-3 y107f variant showed reduced migration in wound healing assay ( fig. 5). This result confirms the role of galectin-3 tyrosine phosphorylation in cell motility.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-78993	Tyr1073	PSGQPTPyATTQLIQ	Homo sapiens
pmid	sentence
10892742	Abl functions to antagonize robo signaling both abl and ena can directly bind to robo's cytoplasmic domain.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-149273	Tyr1172	ISLDNPDyQQDFFPK	Homo sapiens
pmid	sentence
16943190	We show that activated abl phosphorylates the egfr primarily on tyrosine 1173.

Identifier	Residue	Sequence	Organism
SIGNOR-149277	Tyr1197	STAENAEyLRVAPQS	Homo sapiens
pmid	sentence
16943190	we show that activated Abl phosphorylates the EGFR primarily on tyrosine 1173Furthermore, we show that activated Abl allows the ligand-activated EGFR to escape Cbl-dependent down-regulation by inhibiting the accumulation of Cbl at the plasma membrane in response to epidermal growth factor stimulation and disrupting the formation of the EGFR.Cbl complex without affecting Cbl protein stability. These findings reveal a novel role for Abl in promoting increased cell-surface expression of the EGFR and suggest that Abl/EGFR signaling may cooperate in human

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262605	Tyr1226	GGSHISGyATLRRGP	in vitro
pmid	sentence
20417104	Here we show that phosphorylation of Lpd by c-Abl increases its interaction with Ena/VASP proteins. This analysis revealed that, in vitro, four Lpd peptides harboring tyrosines (Y426, Y456, Y513, Y1226) are highly phosphorylated, and eight additional peptides are phosphorylated to a lesser extent (Figure 1C).

Identifier	Residue	Sequence	Organism
SIGNOR-262606	Tyr426	LLRASGIyYVPKGKA	in vitro
pmid	sentence
20417104	Here we show that phosphorylation of Lpd by c-Abl increases its interaction with Ena/VASP proteins. This analysis revealed that, in vitro, four Lpd peptides harboring tyrosines (Y426, Y456, Y513, Y1226) are highly phosphorylated, and eight additional peptides are phosphorylated to a lesser extent (Figure 1C).

Identifier	Residue	Sequence	Organism
SIGNOR-262607	Tyr456	NVYYGQDyRNKYKAP	in vitro
pmid	sentence
20417104	Here we show that phosphorylation of Lpd by c-Abl increases its interaction with Ena/VASP proteins. This analysis revealed that, in vitro, four Lpd peptides harboring tyrosines (Y426, Y456, Y513, Y1226) are highly phosphorylated, and eight additional peptides are phosphorylated to a lesser extent (Figure 1C).

Identifier	Residue	Sequence	Organism
SIGNOR-262608	Tyr513	GKQLYMNyQEALKRT	in vitro
pmid	sentence
20417104	Here we show that phosphorylation of Lpd by c-Abl increases its interaction with Ena/VASP proteins. This analysis revealed that, in vitro, four Lpd peptides harboring tyrosines (Y426, Y456, Y513, Y1226) are highly phosphorylated, and eight additional peptides are phosphorylated to a lesser extent (Figure 1C).

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-260830	Tyr1243	NGGSSLSyTNPAVAA	Homo sapiens
pmid	sentence
16888623	The results demonstrate that ABL1 phosphorylates MUC1 on Tyr-60 and forms a complex with MUC1 by binding of the ABL1 SH2 domain to the pTyr-60 site.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-180571	Tyr1357	HPQAASIyQSSEMKG	Homo sapiens
pmid	sentence
18765637	Tyrosine phosphorylation of the nuclear receptor coactivator aib1/src-3 is enhanced by abl kinase and is required for its activity in cancer cellstyrosine kinase directly phosphorylates aib1/src-3 at y1357 and modulates the association of aib1 with c-abl, eralpha, the transcriptional cofactor p300,

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276187	Tyr136	GIAVPDVySACKRFE	in vitro
pmid	sentence
34838714	We show that Glo1 activity is promoted by phosphorylation on Tyrosine 136 via multiple kinases. Glo1 Y136 is phosphorylated by multiple different kinases including all members of the Src family. Depletion of multiple different kinases led to a partial reduction in Glo1(Y136) phosphorylation. These included members of the Src family (Src, Yes1, FGR, and the related Abl1), and of the FAK, EPHA, FGFR, and VEGFR families (Figure 2B), suggesting phosphorylation of Glo1 on Y136 by multiple different kinases. In vitro kinase assays revealed that all the members of the Src family, as well as Epha5 and VEGFR3, can efficiently phosphorylate recombinant Glo1 on Y136 (Figure 2C–D).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277626	Tyr137	ETLVSLDyAISKPEV	Homo sapiens	SH-SY5Y Cell
pmid	sentence
34581802	C-Abl-mediated phosphorylation of PARIS at Y137 (within the Krüppel-associated box domain) drives its association with KAP1 and the repression of genes with diverse functions in pathways such as chromatin remodelling and p53-dependent cell death.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167853	Tyr143	SPAGRSIyNSFYVYC	Homo sapiens
pmid	sentence
20823226	Here we show that the nonreceptor tyrosine kinase c-abl phosphorylates tyrosine 143 of parkin, inhibiting parkin's ubiquitin e3 ligase activity and protective function.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-260934	Tyr149	SVTAPSPyAQPSSTF	Homo sapiens
pmid	sentence
19783996	In cell lines, upon cisplatin treatment, c-Abl phosphorylates TAp63 on specific tyrosine residues. Such modifications affect p63 stability and induce a p63-dependent activation of proapoptotic promoters.

Identifier	Residue	Sequence	Organism
SIGNOR-260932	Tyr171	AIPSNTDyPGPHSFD	Homo sapiens
pmid	sentence
19783996	In cell lines, upon cisplatin treatment, c-Abl phosphorylates TAp63 on specific tyrosine residues. Such modifications affect p63 stability and induce a p63-dependent activation of proapoptotic promoters.

Identifier	Residue	Sequence	Organism
SIGNOR-260933	Tyr290	RQSVLVPyEPPQVGT	Homo sapiens
pmid	sentence
19783996	In cell lines, upon cisplatin treatment, c-Abl phosphorylates TAp63 on specific tyrosine residues. Such modifications affect p63 stability and induce a p63-dependent activation of proapoptotic promoters.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245288	Tyr15	EKIGEGTyGTVFKAK	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
10896159	Phosphorylation of Cdk5 by c-Abl occurs on tyrosine 15 (Y15), which is stimulatory for p35/Cdk5 kinase activity.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262299	Tyr151	KKDGLKFyTDPSYFF	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
17623672	WAVE3-Abl interaction promotes the tyrosine phosphorylation of WAVE3 by Abl, and STI-571, a specific inhibitor of Abl kinase activity, abrogates the Abl-mediated phosphorylation of WAVE3.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262300	Tyr248	HASDVTDySYPATPN	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
17623672	WAVE3-Abl interaction promotes the tyrosine phosphorylation of WAVE3 by Abl, and STI-571, a specific inhibitor of Abl kinase activity, abrogates the Abl-mediated phosphorylation of WAVE3.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262301	Tyr337	LPAQIIEyYNPSGPP	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
17623672	WAVE3-Abl interaction promotes the tyrosine phosphorylation of WAVE3 by Abl, and STI-571, a specific inhibitor of Abl kinase activity, abrogates the Abl-mediated phosphorylation of WAVE3.

Identifier	Residue	Sequence	Organism
SIGNOR-259077	Tyr486	SRRIAVEySDSDDDS	Homo sapiens
pmid	sentence
17623672	WAVE3-Abl interaction promotes the tyrosine phosphorylation of WAVE3 by Abl, and STI-571, a specific inhibitor of Abl kinase activity, abrogates the Abl-mediated phosphorylation of WAVE3.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277406	Tyr153	ASKIRSGyFDERYVL	Homo sapiens	BT-474 Cell
pmid	sentence
30174304	Here, we show that oncogenic HER2 tyrosine kinase signaling induces phosphorylation of mitochondrial creatine kinase 1 (MtCK1) on tyrosine 153 (Y153) in an ABL-dependent manner in breast cancer cells. Y153 phosphorylation, which is commonly upregulated in HER2+ breast cancers, stabilizes MtCK1 to increase the phosphocreatine energy shuttle and promote proliferation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-146585	Tyr153	QTDPSGTyHAWKANA	Homo sapiens
pmid	sentence
16678104	Proteasome-mediated proteolysis is a primary protein degradation pathway in cells. The present study demonstrates that c-abl and arg (abl-related gene) tyrosine kinases associate with and phosphorylate the proteasome psma7 (alpha4) subunit at tyr-153. Consequently, proteasome-dependent proteolysis is compromised

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-133260	Tyr153	RGNADLAyILSMEPC	Homo sapiens
pmid	sentence
15657060	C-abl phosphorylates casp9 on tyr-153 in vitro and in vivo in response to dna damage.The Present results demonstrate that c-abl binds directly to casp9.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260792	Tyr153	LAYILSMePCGHCLI	Homo sapiens
pmid	sentence
15657060	We show that ABL1 phosphorylates caspase-9 on Tyr-153 in vitro and in cells treated with DNA damaging agents. ! Moreover, inhibition of ABL1 with STI571 blocked DNA damage-induced autoprocessing of caspase-9 to the p35 subunit and activation of caspase-3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273538	Tyr157	SQSLTQIyALPEIPQ	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
23006999	C-Abl was identified as one of the kinases, which phosphorylates syntaxin 17.Western blot shows phosphorylation of syntaxin 17 on Tyr-156 by overexpression and activation of c-Abl. A phospho-mimicking mutant (Y156E) of syntaxin 17 showed reduced interaction with COPI vesicles. These results suggest that tyrosine phosphorylation of syntaxin 17 is likely to have a role in regulating syntaxin 17 dependent membrane trafficking in the early secretory pathway.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-202003	Tyr164	KTEEAIIySYGFATI	Homo sapiens
pmid	sentence
23629659	We demonstrated that the er-resident human protein serine palmitoyltransferase long chain-1 (sptlc1), which is the first enzyme of sphingolipid biosynthesis, is phosphorylated at tyr(164) by the tyrosine kinase abl. this occurred through the specific abl-mediated phosphorylation of sptlc1 on tyr164, leading to the attenuation of its activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251428	Tyr170	LHSEPPVyANLSNFN	in vitro
pmid	sentence
10637231	Active nuclear Abl efficiently phosphorylate c-Jun. After phosphorylation of c-Jun by Abl on Tyr170, both proteins interacted via the SH2 domain of Abl.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-245370	Tyr170	LHSEPPVyANLSNFN	Homo sapiens
pmid	sentence
10637231	After phosphorylation of c-Jun by Abl on Tyr170, both proteins interacted via the SH2 domain of Abl

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124719	Tyr171	IPTSAPVyQQPQQQP	Homo sapiens	Breast Cancer Cell
pmid	sentence
15138294	C-abl activation by apoptotic agents specifically promotes phosphorylation of lasp-1 at tyrosine 171, which is associated with the loss of lasp-1 localization to focal adhesions and induction of cell death. Thus, lasp-1 is a dynamic focal adhesion protein necessary for cell migration and survival in response to growth factors and ecm proteins.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247666	Tyr175	EITTNRFyGPQVNNI	Mus musculus
pmid	sentence
16199863	Mutation of both tyrosines 175 and 256 to phenylalanine was required to abolish Abl-mediated phosphorylation of N-WASP in the presence of Grb2 [] suggesting that phosphorylation at tyrosine 175 is not critical for comet tail formation by Shigella

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-251436	Tyr175	EITTNRFyGPQVNNI	in vitro
pmid	sentence
16199863	Abl phosphorylates N-WASP on tyrosines 175 and 256. Phosphorylation at this site stabilizes the active conformation of N-WASP, resulting in comet tail elongation.

Identifier	Residue	Sequence	Organism
SIGNOR-251437	Tyr256	RETSKVIyDFIEKTG	in vitro
pmid	sentence
16199863	Abl phosphorylates N-WASP on tyrosines 175 and 256. Phosphorylation at this site stabilizes the active conformation of N-WASP, resulting in comet tail elongation.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276280	Tyr193	NVDDSKEyFSKHN	in vitro
pmid	sentence
20178744	Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. To determine whether Prxs are phosphorylated, we subjected recombinant human PrxI and II to an in vitro kinase assay with two nonreceptor PTKs, Lck and Abl, in the presence of [γ-32P]ATP. Both PTKs phosphorylated PrxI and PrxII. Phosphorylation of the wild-type protein was detected, whereas that of the Y194F mutant was not (Figure 1B), indicating that Tyr194 is the only site of tyrosine phosphorylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276278	Tyr194	DVQKSKEyFSKQK	in vitro
pmid	sentence
20178744	Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. To determine whether Prxs are phosphorylated, we subjected recombinant human PrxI and II to an in vitro kinase assay with two nonreceptor PTKs, Lck and Abl, in the presence of [γ-32P]ATP. Both PTKs phosphorylated PrxI and PrxII. Phosphorylation of the wild-type protein was detected, whereas that of the Y194F mutant was not (Figure 1B), indicating that Tyr194 is the only site of tyrosine phosphorylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-172017	Tyr213	PPTVPNDyMTSPARL	Homo sapiens
pmid	sentence
21320496	Abi-1 is an adaptor protein for abelson kinase (c-abl). Here, we identified a new phosphorylation site (y398) in the sh3 domain of abi1, and disruption of y398, combined with the previously identified phosphorylation site y213, significantly weakens the binding of abi-1 to c-abl. Phosphorylation of abi-1 is dependent on c-abl kinase

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-163562	Tyr219	SIQGHNDyMCPATNQ	Homo sapiens	Breast Cancer Cell
pmid	sentence
20101225	Eralpha can be phosphorylated on two sites, tyrosine 52 (y-52) and tyrosine 219 (y-219). Eralpha phosphorylation by c-abl stabilizes eralpha, resulting in enhanced eralpha transcriptional activity and increased expression of endogenous eralpha target genes.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-163566	Tyr52	DSSKPAVyNYPEGAA	Homo sapiens	Breast Cancer Cell
pmid	sentence
20101225	Eralpha can be phosphorylated on two sites, tyrosine 52 (y-52) and tyrosine 219 (y-219). Eralpha phosphorylation by c-abl stabilizes eralpha, resulting in enhanced eralpha transcriptional activity and increased expression of endogenous eralpha target genes.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-175135	Tyr221	GGPEPGPyAQPSVNT	Homo sapiens
pmid	sentence
21779437	Negative regulation of crk by abl is essential for the antitumorigenic effects of ephrinb2,similar pathways may operate for crkl

Identifier	Residue	Sequence	Organism
SIGNOR-173845	Tyr221	GGPEPGPyAQPSVNT	Homo sapiens
pmid	sentence
21602891	Abl induces phosphorylation at y251 in vivo, and that the kinetics of phosphorylation at y251 and the negative regulatory y221 site in vitro are similar.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260928	Tyr222	IGAGKGKyYAVNFPM	Rattus norvegicus
pmid	sentence
25219501	C-Abl stabilizes HDAC2 levels by tyrosine phosphorylation repressing neuronal gene expression in Alzheimer's disease.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-260801	Tyr223	LKKVVALyDYMPMNA	Homo sapiens
pmid	sentence
12445832	In this report we describe for the first time that ABL1 and Btk physically interact and that ABL1 can phosphorylate tyrosine 223 in the SH3 domain of Btk. \| This is presumably due to the negative regulatory effectof Btk SH3 domain phosphorylation caused by ABL1,which would result in a decreased catalytic activity ofBtk resulting in impaired autophosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245278	Tyr223	LKKVVALyDYMPMNA	Homo sapiens	HeLa Cell
pmid	sentence
12445832	In this report we describe for the first time that c-Abl and Btk physically interact and that c-Abl can phosphorylate tyrosine 223 in the SH3 domain of Btk

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260938	Tyr223	LTSPEELyRVFTTQE	Homo sapiens
pmid	sentence
26235616	Here, we show that c-Abl kinase phosphorylates Y223 in human Aha1 (hAha1), promoting its interaction with Hsp90. This, consequently, results in an increased Hsp90 ATPase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-246307	Tyr226	KRNKPTVyGVSPNYD	Homo sapiens
pmid	sentence
11847100	c-Src-induced c-Abl activation involves phosphorylation of Y245 and Y412, two residues required for c-Abl mitogenic function.

Identifier	Residue	Sequence	Organism
SIGNOR-246311	Tyr393	RLMTGDTyTAHAGAK	Homo sapiens
pmid	sentence
11847100	c-Src-induced c-Abl activation involves phosphorylation of Y245 and Y412, two residues required for c-Abl mitogenic function.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277012	Tyr226	KRNKPTVyGVSPNYD	Homo sapiens
pmid	sentence
28924170	We also found that PTPN13 dephosphorylates and inhibits c-Abl.\|While the above results indicated that calpain-2 could cleave PTPN13 and that PTPN13 could dephosphorylate c-Abl at tyrosine 245, they did not determine whether calpain-2-mediated cleavage of PTPN13 resulted in its inactivation and increased tyrosine phosphorylation of c-Abl at tyrosine 245.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-86581	Tyr231	NANGEAVyCKFHYKT	Homo sapiens
pmid	sentence
12950161	C-abl and arg phosphorylated catalase at tyr231 and tyr386 in vitro.catalase is a major effector in the defense of aerobic cells against oxidative stress. Recent studies have shown that catalase activity is stimulated by the c-abl and arg tyrosine kinases

Identifier	Residue	Sequence	Organism
SIGNOR-86585	Tyr386	YRARVANyQRDGPMC	Homo sapiens
pmid	sentence
12950161	C-abl and arg phosphorylated catalase at tyr231 and tyr386 in vitrocatalase is a major effector in the defense of aerobic cells against oxidative stress. Recent studies have shown that catalase activity is stimulated by the c-abl and arg tyrosine kinases

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260769	Tyr231	NANGEAVyCKFHYKT	Homo sapiens
pmid	sentence
12777400	These findings indicate that (i) ABL1 and Arg activate catalase by phosphorylation at both Tyr231 and Tyr386

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101298	Tyr231	NANGEAVyCKFHYKT	Homo sapiens	MCF-7 Cell
pmid	sentence
12777400	The SH3 domains of c-Abl and Arg bound directly to catalase at a P293FNP site. c-Abl and Arg phosphorylated catalase at Tyr231 and Tyr386 in vitro and in the response of cells to H2O2

Identifier	Residue	Sequence	Organism
SIGNOR-260770	Tyr386	YRARVANyQRDGPMC	Homo sapiens
pmid	sentence
12777400	These findings indicate that (i) ABL1 and Arg activate catalase by phosphorylation at both Tyr231 and Tyr386

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101302	Tyr386	YRARVANyQRDGPMC	Homo sapiens	MCF-7 Cell
pmid	sentence
12777400	C-abl and arg phosphorylated catalase at tyr231 and tyr386 in vitrocatalase is a major effector in the defense of aerobic cells against oxidative stress. Recent studies have shown that catalase activity is stimulated by the c-abl and arg tyrosine kinases

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167989	Tyr231	NQDDVGVyTCLVVNG	Homo sapiens
pmid	sentence
20861316	Nonmuscle myosin light chain kinase (nmmlck), a multi-functional cytoskeletal protein critical to vascular homeostasis, is highly regulated by tyrosine phosphorylation. We identified multiple novel c-abl-mediated nmmlck phosphorylation sites by mass spectroscopy analysis (including y231, y464, y556, y846) and examined their influence on nmmlck function and human lung endothelial cell (ec) barrier regulation. Tyrosine phosphorylation of nmmlck increased kinase activity

Identifier	Residue	Sequence	Organism
SIGNOR-167993	Tyr464	QEGSIEVyEDAGSHY	Homo sapiens
pmid	sentence
20861316	We identified multiple novel c-abl-mediated nmmlck phosphorylation sites by mass spectroscopy analysis (including y231, y464, y556, y846) and examined their influence on nmmlck function and human lung endothelial cell (ec) barrier regulation. Tyrosine phosphorylation of nmmlck increased kinase activity

Identifier	Residue	Sequence	Organism
SIGNOR-167997	Tyr556	LNGQPIQyARSTCEA	Homo sapiens
pmid	sentence
20861316	Nonmuscle myosin light chain kinase (nmmlck), a multi-functional cytoskeletal protein critical to vascular homeostasis, is highly regulated by tyrosine phosphorylation. We identified multiple novel c-abl-mediated nmmlck phosphorylation sites by mass spectroscopy analysis (including y231, y464, y556, y846) and examined their influence on nmmlck function and human lung endothelial cell (ec) barrier regulation. Tyrosine phosphorylation of nmmlck increased kinase activity

Identifier	Residue	Sequence	Organism
SIGNOR-168001	Tyr846	DGGGSDRyGSLRPGW	Homo sapiens
pmid	sentence
20861316	Nonmuscle myosin light chain kinase (nmmlck), a multi-functional cytoskeletal protein critical to vascular homeostasis, is highly regulated by tyrosine phosphorylation. We identified multiple novel c-abl-mediated nmmlck phosphorylation sites by mass spectroscopy analysis (including y231, y464, y556, y846) and examined their influence on nmmlck function and human lung endothelial cell (ec) barrier regulation. Tyrosine phosphorylation of nmmlck increased kinase activity

Publications:

4

Organism:

Homo Sapiens

Tissue:

Lung

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251429	Tyr232	FLMTKSGyQPPRLKE	Homo sapiens	HEK-293 Cell
pmid	sentence
11278340	C-Abl phosphorylates HPK1 in cytoplasm and stimulates HPK1 activity. the c-Abl phosphorylation site (YXXP) in HPK1 (Y232QPP; aa 232–235) is localized in HPK1-KD

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-134396	Tyr261	GLVTTLHyPAPKCNK	Homo sapiens
pmid	sentence
15735735	The results show that arg is stabilized in response to 0.1 mm h2o2 by autophosphorylation of y-261, consistent with involvement of the arg kinase function in regulating arg levels. The results further demonstrate that c-abl-mediated phosphorylation of arg on y-261 similarly confers arg stabilization

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-200854	Tyr264	IYRKEPLyAAFPGSH	Homo sapiens
pmid	sentence
23383002	Furthermore, we identify abl as the major tyrosine kinase that can trigger p140cap phosphorylation on these sequences.

Identifier	Residue	Sequence	Organism
SIGNOR-200858	Tyr396	LVKGEGLyADPYGLL	Homo sapiens
pmid	sentence
23383002	Mapping of p140cap phosphorylation sites: the eplya and eglya motifs have a key role in tyrosine phosphorylation and csk binding, and are substrates of the abl kinase

Publications:

2

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277328	Tyr266	TDSIRDEyAFLQKKY	Homo sapiens	SH-SY5Y Cell
pmid	sentence
29022905	In this study, we found that c-Abl phosphorylated Drp1 at tyrosine 266, 368 and 449 in vitro and in vivo, which augmented the GTPase activity of Drp1 and promoted Drp1-mediated mitochondrial fragmentation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277329	Tyr368	CGGARICyIFHETFG	Homo sapiens	SH-SY5Y Cell
pmid	sentence
29022905	In this study, we found that c-Abl phosphorylated Drp1 at tyrosine 266, 368 and 449 in vitro and in vivo, which augmented the GTPase activity of Drp1 and promoted Drp1-mediated mitochondrial fragmentation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277327	Tyr449	IIQHCSNySTQELLR	Homo sapiens	SH-SY5Y Cell
pmid	sentence
29022905	In this study, we found that c-Abl phosphorylated Drp1 at tyrosine 266, 368 and 449 in vitro and in vivo, which augmented the GTPase activity of Drp1 and promoted Drp1-mediated mitochondrial fragmentation.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262604	Tyr267	KRRTEEKyGGDSDHP	Homo sapiens	HEK-293 Cell
pmid	sentence
26126715	The kinase ABL phosphorylates the microprocessor subunit DGCR8 to stimulate primary microRNA processing in response to DNA damage. When coexpressed in HEK293T cells, ABL phosphorylated DGCR8 at Tyr(267).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260775	Tyr268	AKMLDHEyTTKEIFR	Homo sapiens
pmid	sentence
15448168	This study demonstrates that ABL1-dependent phosphorylation up-regulates topo I activity. The ABL1 SH3 domain bound directly to the N-terminal region of topo I. The results demonstrate that ABL1 phosphorylated topo I at Tyr268 in core subdomain II.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-169699	Tyr276	SDEDDEVyQVTVYQA	Homo sapiens
pmid	sentence
21081495	Mdm2 has three known c-abl phosphorylation sites (tyr276, tyr394, and tyr405)these data show that c-abl is important for reducing mdm2 and mdmx protein levels after genotoxic stress and suggest another cellular mechanism for the stabilization and activation of p53.

Identifier	Residue	Sequence	Organism
SIGNOR-169703	Tyr405	STSSSIIySSQEDVK	Homo sapiens
pmid	sentence
21081495	Mdm2 has three known c-abl phosphorylation sites (tyr276, tyr394, and tyr405)these data show that c-abl is important for reducing mdm2 and mdmx protein levels after genotoxic stress and suggest another cellular mechanism for the stabilization and activation of p53.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-86186	Tyr28	SRIGDELyLEPLEDG	Homo sapiens
pmid	sentence
11971963	C-abl phosphorylates the rad9 bcl-2 homology 3 domain (tyr-28) in vitro and in cells exposed to dna-damaging agents. The results also demonstrate that c-abl-mediated phosphorylation of rad9 induces binding of rad9 to the antiapototic bcl-x(l) protein

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260843	Tyr28	AVHSLSRiGDELYLE	Homo sapiens
pmid	sentence
11971963	The SH3 domain of c-Abl interacts directly with the C-terminal region of Rad9. c-Abl phosphorylates the Rad9 Bcl-2 homology 3 domain (Tyr-28) in vitro and in cells exposed to DNA-damaging agents. \| c-Abl-mediated phosphorylation of Rad9 induces binding of Rad9 to Bcl-xL \|these findings indicate that Rad9 is regulated by a c-Abl-dependent mechanism in the apoptotic response to genotoxic stress.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167632	Tyr291	DTDQLKLyEEPLSKL	Homo sapiens
pmid	sentence
20798688	C-abl can phosphorylate atr on y291 and y310 and this phosphorylation appears to have a positive role in atr activation under genotoxic stress.

Identifier	Residue	Sequence	Organism
SIGNOR-167636	Tyr310	FPFEAEAyRNIEPVY	Homo sapiens
pmid	sentence
20798688	C-abl can phosphorylate atr on y291 and y310 and this phosphorylation appears to have a positive role in atr activation under genotoxic stress.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277440	Tyr292	RLGHCHTyWAVSEEL	Homo sapiens	HEK-293 Cell
pmid	sentence
30842273	The data in this study show that IRF3 is physically associated with c-Abl in vivo and directly binds to c-Abl in vitro. IRF3 is phosphorylated by c-Abl and c-Abl-related kinase, Arg, mainly at Y292.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276598	Tyr294	HPPGNEIyRKGTISF	Homo sapiens	HEK-293 Cell
pmid	sentence
24044023	We present evidence that Tip60 is modified on tyrosine 327 by Abl kinase. We show that this causes functional changes in HAT activity and the subcellular localization of TIP60, which forms a complex with Abl kinase. The Tip60 mutation Y327F abolished tyrosine phosphorylation, reduced the inhibition of Tip60 HAT activity, and caused G0-G1 arrest and association with FE65.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-253055	Tyr30	FATTDDFyDDPCFDSP	Homo sapiens	HEK-293 Cell
pmid	sentence
12415271	We have found that c-Abl can phosphorylate MyoD at a conserved N-terminal tyrosine (Tyr30) that is located within the transactivation domain. Mutation of Tyr30 to Phe does not interfere with the function of MyoD, but theTyr30Phe mutant becomes resistant to the inhibitory effect of DNA damage.

Publications:

1

Organism:

Homo Sapiens

Pathways:

P38 Signaling and Myogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-260777	Tyr315	ETRICKIyDSPCLPE	Homo sapiens
pmid	sentence
10212258	Tyrosine Phosphorylation of Rad51 by ABL1 Enhances the Interaction between Rad51 and Rad52 \| our studies of Rad51·Rad52 complex formation in vitro and in vivo suggest that the ATM and ABL1-mediated signaling is likely to promote repair given the biochemical evidence that Rad51 acts in concert with Rad52 in homologous recombination

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247599	Tyr315	ETRICKIyDSPCLPE	Mus musculus	32D Clone3 Cell
pmid	sentence
11684015	Phosphorylation of the RAD51 Tyr-315 residue by BCR/ABL appears essential for enhanced DSB repair and drug resistance

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251434	Tyr315	ETRICKIyDSPCLPE	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
10212258	C-Abl phosphorylates Rad51 in vitro and in vivo. phosphorylation of Rad51 by c-Abl enhances complex formation between Rad51 and Rad52, which cooperates with Rad51 in recombination and repair. c-Abl phosphorylates Rad51 Tyr315

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247594	Tyr315	ETRICKIyDSPCLPE	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
10212258	Mutation of Rad51 Tyr315, but not Tyr205, Tyr191, or Tyr54 to phenylalanine abolished Rad51 tyrosine phosphorylation by c-Abl (Fig. 3 b). These results strongly suggest that c-Abl phosphorylates Rad51 Tyr315 in vivo

Publications:

4

Organism:

Homo Sapiens, Mus Musculus, Chlorocebus Aethiops

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251431	Tyr345	PERNEGVyTAIAVQE	Chlorocebus aethiops	COS Cell
pmid	sentence
11163214	PSTPIP1 was phosphorylated by c-Abl. Tyr-344 is a major c-Abl phosphorylation site.PSTPIP1 was able to bridge c-Abl to the PEST-type PTPs.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-260809	Tyr345	PERNEGVyTAIAVQE	Homo sapiens
pmid	sentence
11163214	PSTPIP1 was phosphorylated by ABL1, and growth factor–induced PSTPIP1 phosphorylation was diminished in Abl null fibroblasts.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246219	Tyr345	PERNEGVyTAIAVQE	Mus musculus	COS Cell
pmid	sentence
11163214	These data suggest that Tyr-344 is a major c-Abl phosphorylation site, or that phosphorylation of Tyr-344 is required for subsequent phosphorylation at other tyrosine residues.

Publications:

2

Organism:

Homo Sapiens, Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-260936	Tyr367	TYLQSRYyRAPEIIL	Homo sapiens
pmid	sentence
25944899	The Tyrosine Kinase c-Abl Promotes Homeodomain-interacting Protein Kinase 2 (HIPK2) Accumulation and Activation in Response to DNA Damage

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-113659	Tyr393	RLMTGDTyTAHAGAK	Homo sapiens
pmid	sentence
11781820	Phosphorylation of tyr412 can occur autocatalytically by a trans-mechanism and cause activation of otherwise inactive c-abl, suggesting a positive feedback loop on c-abl activity.

Identifier	Residue	Sequence	Organism
SIGNOR-260781	Tyr393	FGLSRLMtGDTYTAH	Homo sapiens
pmid	sentence
10964922	We demonstrate here that autophosphorylation of ABL1 is intermolecular and stimulates Abl catalytic activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-39142	Tyr393	RLMTGDTyTAHAGAK	Homo sapiens	Leukemia Cell
pmid	sentence
8441409	Sh1 domain autophosphorylation of p210 bcr/abl is required for transformation but not growth factor independence.

Publications:

3

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition, P38 Signaling and Myogenesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235568	Tyr393	RLMTGDTyTAHAGAK	Chlorocebus aethiops	COS Cell
pmid	sentence
11163214	Several experiments suggest that the pest-type ptps negatively regulate c-abl activity: c-abl was hyperphosphorylated in ptp-pest-deficient cells dephosphorylation of c-abl by pest-type ptp represents a novel mechanism by which c-abl activity is regulated.

Identifier	Residue	Organism
SIGNOR-246222		Mus musculus
pmid	sentence
11163214	Several experiments suggest that the PEST-type PTPs negatively regulate c-Abl activity: c-Abl was hyperphosphorylated in PTP-PEST-deficient cells; disruption of the c-Abl-PSTPIP1-PEST-type PTP ternary complex by overexpression of PSTPIP1 mutants increased c-Abl phosphotyrosine content

Publications:

2

Organism:

Chlorocebus Aethiops, Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-90512	Tyr394	QSQESEDySQPSTSS	Homo sapiens
pmid	sentence
12110584	C-abl binds and phosphorylates mdm2 in vivo and in vitro;phosphorylation of mdm2 by c-abl impairs the inhibition of p53 by mdm2.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-160860	Tyr407	SGLSMSSySVPRTPD	Homo sapiens
pmid	sentence
18280240	In this study, we show that c-abl directly phosphorylates yap1 at position y357 in response to dna damage. Tyrosine-phosphorylated yap1 is a more stable protein that displays higher affinity to p73 and selectively coactivates p73 proapoptotic target genes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-254691	Tyr413	TAPESLAyNKFSIKS	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-260935	Tyr425	SDKYGLGyQLCDNSV	Homo sapiens
pmid	sentence
27899378	C-ABL can directly phosphorylate PLK1 and activate PLK1. \| The above results indicate that c-ABL–mediated PLK1 Y425 phosphorylation regulates PLK1 ubiquitination and stability.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246211	Tyr432	KEGWMVHyTSKDTLR	Homo sapiens	HeLa Cell
pmid	sentence
12637538	Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. [..] Mutation of the other two sites, Tyr432 and Tyr502, had no significant influence on PKD activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246215	Tyr502	TTANVVYyVGENVVN	Homo sapiens	HeLa Cell
pmid	sentence
12637538	Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. [..] Mutation of the other two sites, Tyr432 and Tyr502, had no significant influence on PKD activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260927	Tyr433	KIPQDGDyEFLKSWT	Rattus norvegicus
pmid	sentence
21715626	In the present study, we demonstrate that the protein kinase c-Abl phosphorylates MST1 at Y433, which triggers the stabilization and activation of MST1.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-260791	Tyr463	NDTGSRYyKEIPLSE	Homo sapiens
pmid	sentence
12637538	We show that Abl directly phosphorylates PKD at Tyr(463) in vitro, and in cells phosphorylation of this site is sufficient to mediate full activation of PKD

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251430	Tyr463	NDTGSRYyKEIPLSE	Homo sapiens	HeLa Cell
pmid	sentence
12637538	Abl Phosphorylates and Activates PKD through Tyr463 Phosphorylation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-99255	Tyr463	NDTGSRYyKEIPLSE	Homo sapiens
pmid	sentence
12637538	By using a phospho-specific antibody, we show that abl directly phosphorylates pkd at tyr(463) in vitro, and in cells phosphorylation of this site is sufficient to mediate full activation of pkd

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-166422	Tyr504	APIPSVPyAPFAAIL	Homo sapiens
pmid	sentence
20581864	Activation of endogenous c-abl by oxidative stress was associated with phosphorylation of cellular c3g on y504. Inhibition of c3g expression and function using rnai or dominant-negative approaches inhibited c-abl-mediated cell death.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-245283	Tyr508	EDMRGILyAAPQLRS	Mus musculus
pmid	sentence
11120811	The results revealed that only tyrosine (Y)490 of CD19 was phosphorylated by c-Abl.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-185649	Tyr52	LTRDETNyGIPQRAL	Homo sapiens
pmid	sentence
19423701	Phosphorylation of rack1 on tyrosine 52 by c-abl is required for insulin-like growth factor i-mediated regulation of focal adhesion kinase.Tyrosine 52 is further shown to be phosphorylated by c-abl kinase, and the c-abl inhibitor sti571 disrupts fak interaction with rack1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260820	Tyr536	QKGQESEyGNITYPP	Homo sapiens
pmid	sentence
8692915	The results demonstrate that the SH3 domain of ABL1 interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that ABL1 phosphorylates C terminal Y536 and Y564 sites.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246227	Tyr536	QKGQESEyGNITYPP	Homo sapiens	U-937 Cell
pmid	sentence
8692915	Treatment with ionizing radiation is associated with c-Abl-dependent tyrosine phosphorylation of SHPTP1. The results demonstrate that the SH3 domain of c-Abl interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that c-Abl phosphorylates C terminal Y536 and Y564 sites.

Identifier	Residue	Sequence	Organism
SIGNOR-246236	Tyr536	QKGQESEyGNITYPP	in vitro
pmid	sentence
12468540	Incorporation of Pmp at the 536 site led to 4-fold stimulation of the SHP-1 tyrosine phosphatase activity whereas incorporation at the 564 site led to no effect

Identifier	Residue	Sequence	Organism
SIGNOR-260821	Tyr564	SKHKEDVyENLHTKN	Homo sapiens
pmid	sentence
8692915	The results demonstrate that the SH3 domain of ABL1 interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that ABL1 phosphorylates C terminal Y536 and Y564 sites.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251433	Tyr564	SKHKEDVyENLHTKN	Homo sapiens	U-937 Cell
pmid	sentence
8692915	The SH3 domain of c-Abl interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that c-Abl phosphorylates C terminal Y536 and Y564 sites. The functional significance of the c-Abl-SHPTP1 interaction is supported by the demonstration that, like c-Abl, SHPTP1 regulates the induction of Jun kinase activity following DNA damage.

Publications:

5

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-55482	Tyr54	HTVEAVAyAPKKELI	Homo sapiens
pmid	sentence
9461559	Here we demonstrate that c-abl interacts constitutively with rad51. We show that c-abl phosphorylates rad51 on tyr-54 in vitro. The results also show that treatment of cells with ionizing radiation induces c-abl-dependent phosphorylation of rad51. Phosphorylation of rad51 by c-abl inhibits the binding of rad51 to dna and the function of rad51 in atp-dependent dna strand exchange reactions.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-123476	Tyr547	VQKFQVYyLGNVPVA	Homo sapiens
pmid	sentence
15031292	The c-abl tyrosine kinase phosphorylates the fe65 adaptor protein to stimulate fe65/amyloid precursor protein nuclear signaling. Here, we show that active c-abl stimulates app/fe65-mediated gene transcription and that this effect is mediated by phosphorylation of fe65 on tyrosine 547 within its second ptb domain.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246231	Tyr564	SKHKEDVyENLHTKN	Homo sapiens	U-937 Cell
pmid	sentence
8692915	Treatment with ionizing radiation is associated with c-Abl-dependent tyrosine phosphorylation of SHPTP1. The results demonstrate that the SH3 domain of c-Abl interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that c-Abl phosphorylates C terminal Y536 and Y564 sites.

Identifier	Residue	Sequence	Organism
SIGNOR-246240	Tyr564	SKHKEDVyENLHTKN	in vitro
pmid	sentence
12468540	Incorporation of Pmp at the 536 site led to 4-fold stimulation of the SHP-1 tyrosine phosphatase activity whereas incorporation at the 564 site led to no effect

Publications:

2

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-149988	Tyr593	NGMNQQAyAYPATAA	Homo sapiens
pmid	sentence
17018282	These results suggested that p68 was phosphorylated by c-abl in ht-29 cells under stimulation of pdgf. we demonstrated that tyrosine phosphorylation of p68 at y593 mediated pdgf-stimulated epithelial-mesenchymal transition (emt). We showed that pdgf treatment led to phosphorylation of p68 at y593 in the cell nucleus. The y593-phosphorylated p68 (referred to as phosphor-p68) promotes beta-catenin nuclear translocation via a wnt-independent pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260930	Tyr659	GDSHPVLyQSLKDLL	Homo sapiens
pmid	sentence
23581475	Our results suggest that c-Abl protects p53 from HPV-E6-E6AP complex-mediated degradation by phosphorylating E6AP and impairing its E3 ligase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276142	Tyr686	IITEYCRyGDLVDYL	in vitro
pmid	sentence
19275932	C-Abl phosphorylates three tyrosine residues on PDGFR-beta (Y686, Y934, Y970), while Arg only phosphorylatesY686. Y686 and Y934 reside in PDGFR-beta catalytic domains, while Y970 is in the C-terminal tail. Using site-directed mutagenesis, we show that Abl-dependent phosphorylation of PDGFR-beta activates PDGFR-beta activity, in vitro, but serves to downregulate PDGFR-mediated chemotaxis.

Identifier	Residue	Sequence	Organism
SIGNOR-276141	Tyr934	AHASDEIyEIMQKCW	in vitro
pmid	sentence
19275932	C-Abl phosphorylates three tyrosine residues on PDGFR-beta (Y686, Y934, Y970), while Arg only phosphorylatesY686. Y686 and Y934 reside in PDGFR-beta catalytic domains, while Y970 is in the C-terminal tail. Using site-directed mutagenesis, we show that Abl-dependent phosphorylation of PDGFR-beta activates PDGFR-beta activity, in vitro, but serves to downregulate PDGFR-mediated chemotaxis.

Identifier	Residue	Sequence	Organism
SIGNOR-276143	Tyr970	GEGYKKKyQQVDEEF	in vitro
pmid	sentence
19275932	C-Abl phosphorylates three tyrosine residues on PDGFR-beta (Y686, Y934, Y970), while Arg only phosphorylatesY686. Y686 and Y934 reside in PDGFR-beta catalytic domains, while Y970 is in the C-terminal tail. Using site-directed mutagenesis, we show that Abl-dependent phosphorylation of PDGFR-beta activates PDGFR-beta activity, in vitro, but serves to downregulate PDGFR-mediated chemotaxis.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-184552	Tyr686	IITEYCRyGDLVDYL	Homo sapiens	Breast Cancer Cell, Glioblastoma Cell
pmid	sentence
19275932	These data are exciting as they indicate that abl kinases not only are activated by pdgfr and promote pdgfr-mediated proliferation and migration,but also act in an intricate negative feedback loop to turn-off pdgfr-mediated chemotaxis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-184556	Tyr970	GEGYKKKyQQVDEEF	Homo sapiens	Breast Cancer Cell, Glioblastoma Cell
pmid	sentence
19275932	These data are exciting as they indicate that abl kinases not only are activated by pdgfr and promote pdgfr-mediated proliferation and migration,but also act in an intricate negative feedback loop to turn-off pdgfr-mediated chemotaxis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260807	Tyr69	PVPNQPVyNQPVYNQ	Homo sapiens
pmid	sentence
11390389	Our data establish that the Abl SH3 domain binds to the N-terminal proline-rich segment of PLSCR1 and that ABL1 phosphorylates Tyr residues of the PLSCR1 polypeptide, most likely Tyr69 and Tyr74 within the tandem repeat sequence

Identifier	Residue	Sequence	Organism
SIGNOR-86013	Tyr69	PVPNQPVyNQPVYNQ	Homo sapiens
pmid	sentence
11390389	C-abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1. Phosphorylation was abolished by mutation of tyr residues tyr(69)/tyr(74) within the tandem repeat sequence (68)vynqpvynqp(77) of plscr1

Identifier	Residue	Sequence	Organism
SIGNOR-260808	Tyr74	PVYNQPVyNQPVGAA	Homo sapiens
pmid	sentence
11390389	Our data establish that the Abl SH3 domain binds to the N-terminal proline-rich segment of PLSCR1 and that ABL1 phosphorylates Tyr residues of the PLSCR1 polypeptide, most likely Tyr69 and Tyr74 within the tandem repeat sequence

Identifier	Residue	Sequence	Organism
SIGNOR-86017	Tyr74	PVYNQPVyNQPVGAA	Homo sapiens
pmid	sentence
11390389	C-abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1. Phosphorylation was abolished by mutation of tyr residues tyr(69)/tyr(74) within the tandem repeat sequence (68)vynqpvynqp(77) of plscr1

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-186423	Tyr78	RAIDFSPyLEPLGAP	Homo sapiens	HEK-293 Cell
pmid	sentence
19563810	The y79 amino acid residue of c/ebpbeta was phosphorylated by c-abl or arg. The phosphorylation of c/ebpbeta resulted in an increased c/ebpbeta stability and a potentiation of c/ebpbeta transcription activation activity in cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-140396	Tyr805	RIPGGNIyISPLKSP	Homo sapiens	Leukemia Cell
pmid	sentence
16158058	Rb-induced apoptosis is compromised by abl-catalysed phosphorylation of rb at y805.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-277519	Tyr81	WEVGSITyDTLSAQA	Homo sapiens
pmid	sentence
32653904	Two kinases, i.e. abelson-tyrosine protein kinase (ABL)1 and Src were identified as eNOS Tyr81 kinases as their inhibition and down-regulation significantly reduced the basal and Yoda1-induced tyrosine phosphorylation and activity of eNOS.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-197538	Tyr81	MQQCDSPyVVKYYGS	Homo sapiens	Neuron
pmid	sentence
22590567	We demonstrate that c-abl kinase phosphorylates mst2 at an evolutionarily conserved site, y81, within the kinase domain. We further show that the phosphorylation of mst2 by c-abl leads to the disruption of the interaction with raf-1 proteins and the enhancement of homodimerization of mst2 proteins. It thereby enhances the mst2 activation and induces neuronal cell death.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245293	Tyr88	KGSLPEFyYRPPRPP	Homo sapiens	HEK-293 Cell, HeLa Cell
pmid	sentence
17254966	A conserved tyrosine residue (Y88) in the Cdk-binding domain of p27 can be phosphorylated by the Src-family kinase Lyn and the oncogene product BCR-ABL

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-251426	Tyr88	KGSLPEFyYRPPRPP	in vitro
pmid	sentence
17254966	Lyn and Abl phosphorylate Y88 of p27 in vitro. phosphorylation of Y88 in p27 impaired its ability to inhibit the bound kinase complex

Publications:

1

Organism:

In Vitro

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Sequence	Organism
SIGNOR-251933	Tyr932	GANRVVIyDPDWNPS	Homo sapiens
pmid	sentence
17626041	N-terminal region of CSB interacts with the SH3 domain of c-Abl in vitro and in vivo. In addition, c-Abl kinase phosphorylates CSB at Tyr932. our results suggest that c-Abl interacts with and tyrosine phosphorylates CSB. This interaction may play an important role in the response to oxidative stress, resulting in activation of c-Abl, tyrosine phosphorylation of CSB and more efficient BER of oxidative DNA damage. Tyrosine-phosphorylated CSB may serve as a signal for repair proteins to localize to DNA damage and may help maintain active transcription in the nucleolus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260931	Tyr934	PAHASDEiYEIMQKC	Homo sapiens
pmid	sentence
19275932	C-Abl phosphorylates three tyrosine residues on PDGFR-β (Y686, Y934, Y970) \| These data are exciting as they indicate that abl kinases not only are activated by pdgfr and promote pdgfr-mediated proliferation and migration,but also act in an intricate negative feedback loop to turn-off pdgfr-mediated chemotaxis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276641	Tyr94	SILKANEySFKVPEF	Mus musculus	NIH-3T3 Cell
pmid	sentence
24962578	Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262609	Tyr95	DRRFRGRyRSPYSGP	Homo sapiens	HEK-293 Cell
pmid	sentence
27018250	In this paper, we report that RBM39 interacts with the nonreceptor tyrosine kinase c-Abl. Both the Src homology (SH) 2 and SH3 domains of c-Abl interact with RBM39. The major tyrosine phosphorylation sites on RBM39 that are phosphorylated by c-Abl are Y95 and Y99, as demonstrated by liquid chromatography coupled with tandem mass spectrometry (LC/MS/MS) and mutational analysis. c-Abl was shown boost the transcriptional coactivation activity of RBM39 for ERα and PRβ in a tyrosine kinase-dependent manner.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262610	Tyr99	RGRYRSPySGPKFNS	Homo sapiens	HEK-293 Cell
pmid	sentence
27018250	In this paper, we report that RBM39 interacts with the nonreceptor tyrosine kinase c-Abl. Both the Src homology (SH) 2 and SH3 domains of c-Abl interact with RBM39. The major tyrosine phosphorylation sites on RBM39 that are phosphorylated by c-Abl are Y95 and Y99, as demonstrated by liquid chromatography coupled with tandem mass spectrometry (LC/MS/MS) and mutational analysis. c-Abl was shown boost the transcriptional coactivation activity of RBM39 for ERα and PRβ in a tyrosine kinase-dependent manner.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-104324	Tyr98	EILNSLKyVRPGGGF	Homo sapiens
pmid	sentence
12893824	GPx1 also functions as a substrate for c-Abl- and Arg-mediated phosphorylation on Tyr-96. The results further show that c-Abl and Arg stimulate GPx activity and that these kinases contribute to GPx-mediated protection of cells against oxidative stress.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-68931	Tyr99	SVPTHSPyAQPSSTF	Homo sapiens
pmid	sentence
10391251	C-abl phosphorylates p73 on a tyrosine residue at position 99 both in vitro and in cells that have been exposed to ionizing radiation. Our results show that c-abl stimulates p73-mediated transactivation and apoptosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-37139		Homo sapiens
pmid	sentence
8242749	A domain in the c-terminus of rb, outside of the a/b pocket, binds to the atp-binding lobe of the c-abl tyrosine kinase, resulting in kinase inhibition.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Organism
SIGNOR-217019		Homo sapiens
pmid	sentence
19470755	We report that abl associates with both cdo and jlp during myoblast differentiation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-175138		Homo sapiens
pmid	sentence
21779437	Negative regulation of crk by abl is essential for the antitumorigenic effects of ephrinb2,similar pathways may operate for crkl

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-193387		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-259209		Homo sapiens
pmid	sentence
24756792	In biochemical in vitro or cell-based assays, Regorafenib or its major human active metabolites M-2 and M-5 inhibited the activity of RET,VEGFR 1-3, KIT, PDGFR-alpha, PDGFR-beta, FGFR1, FGFR2, TIE2, DDR2, TrkA, Eph2A, RAF-1, BRAF, BRAFV600E, SAPK2, PTK5, and Abl at concentrations that can be achieved clinically.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-200871		Homo sapiens	Leukemia Cell
pmid	sentence
23399893	We show that the grb2-related adapter protein, gads, also associates with bcr-abl, specifically through y177 and demonstrate that bcr-abl-driven lymphoid disease requires gads

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-67069		Homo sapiens
pmid	sentence
10212258	C-abl phosphorylates rad51 in vitro and in vivo. In assays using purified components, phosphorylation of rad51 by c-abl enhances complex formation between rad51 and rad52, which cooperates with rad51 in recombination and repair

Publications:

1

Organism:

Homo Sapiens

Pathways:

Cell cycle: G2/M phase transition

Identifier	Residue	Organism
SIGNOR-206277		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-191301		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-90446		Homo sapiens
pmid	sentence
12107171	C-abl might act as a negative regulator of uv-ddb by phosphorylating ddb2

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190696		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-57516		Homo sapiens
pmid	sentence
9583676	We show that rfxi and c-abl are in direct interaction, in vitro and in cell extracts, through the rfxi proline rich (pxxp) motif and the c-abl sh3 domain. Remarkably, this interaction significantly potentiates c-abl but not v-abl auto-kinase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-105035		Homo sapiens
pmid	sentence
11163214	Cytoskeletal protein pstpip1 directs the pest-type protein tyrosine phosphatase to the c-abl kinase to mediate abl dephosphorylationSeveral experiments suggest that the PEST-type PTPs negatively regulate c-Abl activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258256		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-185765		Homo sapiens	Myoblast
pmid	sentence
19470755	We report that abl associates with both cdo and jlp during myoblast differentiation

Publications:

1

Organism:

Homo Sapiens

Pathways:

P38 Signaling and Myogenesis

Identifier	Residue	Organism
SIGNOR-258063		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-258088		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-258263		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272999
pmid	sentence
35569509	This suggests that by interacting with Sdc4, either directly or indirectly, RON is activated via transphosphorylation when clustered, engages the ABL1 SH2 domain, and activates ABL1 by phosphorylation.

Publications:

1

Identifier	Residue	Organism	Cell Line
SIGNOR-109668		Homo sapiens	Neuron
pmid	sentence
11494128	Two-hybrid screens identified regions of abl and arg that bind to the ephb2 and epha4 receptors, suggesting a novel signaling connection involving the two kinase families.The connection between EphB2 and Abl/Arg appears to be reciprocal. Activated EphB2 causes tyrosine phosphorylation of Abl and Arg, and vice versa. Interestingly, treatment of COS cells and B35 neuronal-like cells with ephrin-B1 to activate endogenous EphB2 decreased the kinase activity of endogenous Abl.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-76562		Homo sapiens
pmid	sentence
10753870	Abl binds directly to raft1 and phosphorylates raft1 in vitro and in vivo. c-abl inhibits autophosphorylation of raft1 and raft1-mediated phosphorylation p70(s6k).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258120		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-56815		Homo sapiens
pmid	sentence
9566916	These results illustrate selectivity in the effects of ptps in a cellular context and suggest that ptp1b may function as a specific, negative regulator of p210 bcr-abl signalling in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-45325		Homo sapiens
pmid	sentence
8943360	We identified a novel protein, aap1 (abl-associated protein 1), that associates with these c-abl domains and fails to bind to the sh3 domain in the activated oncoprotein bcrabl. we conclude that aap1 inhibits c-abl tyrosine kinase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270219		Homo sapiens
pmid	sentence
18794806	Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-191313		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-86497		Homo sapiens	HeLa Cell, Leukemia Cell
pmid	sentence
12944467	We thus hypothesized that wrn may interact with the abl tyrosine kinase in the dna damage response. Here, we provide evidence for a functional and physical interaction between wrn and c-abl, including wrn relocalization in response to dna damage, suggesting that this protein-protein interaction participates in a shared pathway of genome surveillance.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-75402		Homo sapiens
pmid	sentence
10708759	Autophosphorylated trka binds directly to plc?, Abl, and shc.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-109672		Homo sapiens
pmid	sentence
11494134	We also show that overexpression of nck could repress the phosphorylation of cbl by abl in vivo. Studies with nck mutants suggested that the nck sh2 domain is responsible for inhibiting the activity of abl toward both cbl and nck itself, most likely by competing with the abl sh2 for tyrosine-phosphorylated binding sites

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-125167		Homo sapiens
pmid	sentence
15175272	We show that yt521-b is tyrosine phosphorylated by c-abl in the nucleus.We propose that tyrosine phosphorylation causes sequestration of YT521-B in an insoluble nuclear form, which abolishes the ability of YT521-B to change alternative splice sites.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258127		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-269946		Homo sapiens	Neuron
pmid	sentence
22590567	We demonstrate that c-abl kinase phosphorylates mst2 at an evolutionarily conserved site, y81, within the kinase domain. We further show that the phosphorylation of mst2 by c-abl leads to the disruption of the interaction with raf-1 proteins and the enhancement of homodimerization of mst2 proteins. It thereby enhances the mst2 activation and induces neuronal cell death.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-45994		Homo sapiens
pmid	sentence
9010225	Our results are in agreement with previous report showing that abi-1, the putative mouse homologue of e3b1, is a abl binding protein

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190008		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-193612		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-48142		Homo sapiens
pmid	sentence
9144171	We also report that the amino-terminal domain of rin1 contains sequences that can mediate interactions with the abl tyrosine kinase and that rin1 is itself tyrosine phosphorylated by c-abl.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-193372		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-39049		Homo sapiens	Leukemia Cell
pmid	sentence
8402896	We demonstrate that bcr-abl exists in a complex with grb-2 in vivo. Binding of grb-2 to bcr-abl is mediated by the direct interaction of the grb-2 sh2 domain with a phosphorylated tyrosine, y177, within the bcr first exon.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-167194		Homo sapiens	Leukemia Cell
pmid	sentence
20675402	We found that while c-cbl e3 ligase induced ubiquitin-dependent degradation of mature and phosphorylated bcr-abl proteins

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-194913		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-114091		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-194838		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-185762		Homo sapiens	Myoblast
pmid	sentence
19470755	Abl binds a proline-rich motif in cdo via its sh3 domain, and these regions of abl and cdo are required for their promyogenic effects. Cdo is important for full abl kinase activity

Publications:

1

Organism:

Homo Sapiens

Pathways:

P38 Signaling and Myogenesis

Name	ABL1 View Modifications
Full Name	Tyrosine-protein kinase ABL1
Synonyms	Abelson murine leukemia viral oncogene homolog 1, Abelson tyrosine-protein kinase 1, Proto-oncogene c-Abl, p150 \| ABL, JTK7
Primary ID	P00519
Links	- -
Type	protein
Relations	199
Pathways	Cell cycle: G2/M phase transition, Myogenesis modulation: DNA damage, P38 Signaling and Myogenesis, Satellite: DDR inhibition, YAP/TAZ regulation
Inhibitors	imatinib methanesulfonate; regorafenib; ponatinib; dasatinib (anhydrous); bosutinib; nilotinib; PD173955; imatinib; DCC-2036; [4-[2-(1H-indazol-3-yl)ethenyl]phenyl]-(1-piperazinyl)methanone; AT9283; 4-methyl-3-[[1-methyl-6-(3-pyridinyl)-4-pyrazolo[3,4-d]pyrimidinyl]amino]-N-[3-(trifluoromethyl)phenyl]benzamide; nocodazole
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' (PubMed:28428613). 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

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