| + |
PDGFRB | up-regulates activity 
phosphorylation
|
ABL2 |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277304 |
Tyr116 |
PNLFVALyDFVASGD |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277302 |
Tyr139 |
EKLRVLGyNQNGEWS |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277306 |
Tyr161 |
QGWVPSNyITPVNSL |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277305 |
Tyr272 |
KCNKPTVyGVSPIHD |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277301 |
Tyr299 |
HKLGGGQyGEVYVGV |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277303 |
Tyr303 |
GGQYGEVyVGVWKKY |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277300 |
Tyr310 |
YVGVWKKySLTVAVK |
in vitro |
|
| pmid |
sentence |
| 34144039 |
PDGFRβ directly phosphorylates multiple novel sites on the N-terminal half of Abl2, including Y116, Y139, and Y161 within the Src homology 3 domain, and Y299, Y303, and Y310 on the kinase domain.We also found that PDGFRβ-mediated phosphorylation of Abl2 in vitro activates Abl2 kinase activity, but mutation of these four tyrosines (Y116, Y161, Y272, and Y310) to phenylalanine abrogated PDGFRβ-mediated activation of Abl2. |
|
| Publications: |
7 |
Organism: |
In Vitro |
| + |
ABL2 | up-regulates
phosphorylation
|
LGALS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163743 |
Tyr118 |
AGPLIVPyNLPLPGG |
Homo sapiens |
|
| pmid |
sentence |
| 20150913 |
The sh (src homology)3 domains of c-abl/arg bind to a p(80)gppsgp motif of gal3, and tyr79 and tyr118 are the major tyrosine phosphorylation sites. A consequence of this interaction and phosphorylation is the significant impairment of chaperone-mediated autophagy of gal3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163747 |
Tyr79 |
GAPAPGVyPGPPSGP |
Homo sapiens |
|
| pmid |
sentence |
| 20150913 |
The sh (src homology)3 domains of c-abl/arg bind to a p(80)gppsgp motif of gal3, and tyr79 and tyr118 are the major tyrosine phosphorylation sites. A consequence of this interaction and phosphorylation is the significant impairment of chaperone-mediated autophagy of gal3. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ABL2 | down-regulates 
phosphorylation
|
PSMA7 |
0.591 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146589 |
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 |
| + |
ABL2 | down-regulates
phosphorylation
|
CRK |
0.684 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-136955 |
Tyr221 |
GGPEPGPyAQPSVNT |
Mus musculus |
|
| pmid |
sentence |
| 15886098 |
Rin1 binds to the abl sh3 and sh2 domains, and these interactions stimulate abl2 catalytic activity. This leads to increased phosphorylation of crk and crkl, inhibiting these cytoskeletal regulators by promoting intramolecular over intermolecular associations. the ability of crk to function as an adaptor protein is negatively regulated and terminated by phosphorylation on y221, which results in an intramolecular sh2-ptyr clamp, thereby resulting in the disassembly of crk-mediated signaling complexes |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-136958 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15886098 |
Abl2 kinase activity toward crk leads to increased phosphorylation of crk, inhibiting this cytoskeletal regulator by promoting intramolecular over intermolecular associations. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| Tissue: |
Breast |
| + |
ABL2 | up-regulates activity
phosphorylation
|
CAT |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101306 |
Tyr231 |
NANGEAVyCKFHYKT |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260771 |
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-101310 |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260772 |
Tyr386 |
YRARVANyQRDGPMC |
Homo sapiens |
|
| pmid |
sentence |
| 12777400 |
These findings indicate that (i) ABL1 and Arg activate catalase by phosphorylation at both Tyr231 and Tyr386 |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
ABL2 | up-regulates
phosphorylation
|
CAT |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86680 |
Tyr231 |
NANGEAVyCKFHYKT |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86684 |
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 |
| + |
ABL1 | up-regulates
phosphorylation
|
ABL2 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
| + |
ABL2 | up-regulates quantity by stabilization
phosphorylation
|
ABL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276033 |
Tyr261 |
GLVTTLHyPAPKCNK |
in vitro |
|
| 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.. These findings indicate that abrogation of the Arg kinase function by the Y261F mutation is dependent on phosphorylation of the Y-439 site. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ABL2 | up-regulates
phosphorylation
|
ABL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134400 |
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 |
| + |
ABL2 | up-regulates activity
phosphorylation
|
IRF3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277441 |
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 |
| + |
ABL2 | up-regulates
phosphorylation
|
SIVA1 |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104992 |
Tyr34 |
RGVCAERySQEVFEK |
Homo sapiens |
|
| pmid |
sentence |
| 11278261 |
Our results also demonstrate that mutation of the siva-1 tyr48 site abrogates the apoptotic function of siva-1 and that apoptosis induced by siva-1 is dependent on expression of kinase-active arg. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL2 | down-regulates quantity by destabilization
phosphorylation
|
ABL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276032 |
Tyr439 |
RLMTGDTyTAHAGAK |
in vitro |
|
| 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.. These findings indicate that abrogation of the Arg kinase function by the Y261F mutation is dependent on phosphorylation of the Y-439 site.). Our results thus indicate that phosphorylation of Arg on Y-261 plays a dual role in retaining the Arg kinase function and preventing Arg degradation by blocking ubiquitination (Figure 6). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ABL2 | up-regulates activity
phosphorylation
|
PDGFRB |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276140 |
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. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ABL2 | up-regulates
phosphorylation
|
CEBPB |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186427 |
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 |
| + |
ABL2 | up-regulates activity
phosphorylation
|
GPX1 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104328 |
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 |
| + |
ABL2 | up-regulates 
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266594 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 33622779 |
Here, using cultured hippocampal neurons pooled from both sexes of mice, we provide evidence that binding to cortactin tethers Abl2 in spines, where Abl2 and cortactin maintain the small pool of stable actin required for dendritic spine stability. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RIN1 | up-regulates
phosphorylation
|
ABL2 |
0.603 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-136961 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15886098 |
Rin1 binds to the abl sh3 and sh2 domains, and these inetractions stimulate abl2 catalytic activity. This leads to increased phosphorylation of crk and crkl |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| + |
DIP2A | up-regulates activity
binding
|
ABL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266593 |
|
|
Mus musculus |
Pyramidal Neuron |
| pmid |
sentence |
| 33622779 |
Here, using cultured hippocampal neurons pooled from both sexes of mice, we provide evidence that binding to cortactin tethers Abl2 in spines, where Abl2 and cortactin maintain the small pool of stable actin required for dendritic spine stability. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BTF3 | up-regulates quantity by expression
transcriptional regulation
|
ABL2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253947 |
|
|
Homo sapiens |
Pancreatic Cancer Cell |
| pmid |
sentence |
| 17312387 |
In contrast, BTF3 silencing resulted in down-regulation of several cancer-associated genes, including EPHB2, ABL2, HPSE2 and ATM, and up-regulation of KRAG, RRAS2, NFkappa-B, MRVI1, MADCAM1 and others. In conclusion, BTF3 is overexpressed in PDAC, where it acts as a transcriptional regulator rather than a direct modulator of apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ABL2
- 
- 