Relation Results

Summary

Name ABL2
Full Name Tyrosine-protein kinase ABL2
Synonyms Abelson murine leukemia viral oncogene homolog 2, Abelson-related gene protein, Tyrosine-protein kinase ARG | ABLL, ARG
Primary ID P42684
Links - -
Type protein
Relations 31
Function Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remo ...
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Type: Score: Layout: SPV 
0.3080.20.5910.6870.3460.20.4970.20.3410.3080.2780.3280.6030.70.20.2PDGFRBABL2LGALS3PSMA7CRKCATABL1IRF3SIVA1CEBPBGPX1RIN1Actin_cytoskeleton_reorganizationDIP2ABTF3

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ PDGFRBup-regulates activity img/direct-activation.png phosphorylation ABL2 0.308
Identifier Residue Sequence Organism Cell Line
SIGNOR-277304 Tyr116 PNLFVALyDFVASGD in vitro
pmid sentence
 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
 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
 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
 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
 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
 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
 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
+ ABL2up-regulates img/direct-activation.png phosphorylation LGALS3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-163743 Tyr118 AGPLIVPyNLPLPGG Homo sapiens
pmid sentence
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
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
+ ABL2down-regulates img/direct_inhibition.png phosphorylation PSMA7 0.591
Identifier Residue Sequence Organism Cell Line
SIGNOR-146589 Tyr153 QTDPSGTyHAWKANA Homo sapiens
pmid sentence
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
+ ABL2down-regulates img/direct_inhibition.png phosphorylation CRK 0.687
Identifier Residue Sequence Organism Cell Line
SIGNOR-136955 Tyr221 GGPEPGPyAQPSVNT Mus musculus
pmid sentence
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
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
+ ABL2up-regulates img/direct-activation.png phosphorylation CAT 0.346
Identifier Residue Sequence Organism Cell Line
SIGNOR-86680 Tyr231 NANGEAVyCKFHYKT Homo sapiens
pmid sentence
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
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
+ ABL2up-regulates activity img/direct-activation.png phosphorylation CAT 0.346
Identifier Residue Sequence Organism Cell Line
SIGNOR-260771 Tyr231 NANGEAVyCKFHYKT Homo sapiens
pmid sentence
These findings indicate that (i) ABL1 and Arg activate catalase by phosphorylation at both Tyr231 and Tyr386
Identifier Residue Sequence Organism Cell Line
SIGNOR-101306 Tyr231 NANGEAVyCKFHYKT Homo sapiens MCF-7 Cell
pmid sentence
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
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
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
+ ABL2up-regulates quantity by stabilization img/direct-activation.png phosphorylation ABL2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276033 Tyr261 GLVTTLHyPAPKCNK in vitro
pmid sentence
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
+ ABL1up-regulates img/direct-activation.png phosphorylation ABL2 0.497
Identifier Residue Sequence Organism Cell Line
SIGNOR-134396 Tyr261 GLVTTLHyPAPKCNK Homo sapiens
pmid sentence
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
+ ABL2up-regulates img/direct-activation.png phosphorylation ABL2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-134400 Tyr261 GLVTTLHyPAPKCNK Homo sapiens
pmid sentence
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
+ ABL2up-regulates activity img/direct-activation.png phosphorylation IRF3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277441 Tyr292 RLGHCHTyWAVSEEL Homo sapiens HEK-293 Cell
pmid sentence
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
+ ABL2up-regulates img/direct-activation.png phosphorylation SIVA1 0.341
Identifier Residue Sequence Organism Cell Line
SIGNOR-104992 Tyr34 RGVCAERySQEVFEK Homo sapiens
pmid sentence
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
+ ABL2down-regulates quantity by destabilization img/direct_inhibition.png phosphorylation ABL2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276032 Tyr439 RLMTGDTyTAHAGAK in vitro
pmid sentence
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
+ ABL2up-regulates activity img/direct-activation.png phosphorylation PDGFRB 0.308
Identifier Residue Sequence Organism Cell Line
SIGNOR-276140 Tyr686 IITEYCRyGDLVDYL in vitro
pmid sentence
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
+ ABL2up-regulates img/direct-activation.png phosphorylation CEBPB 0.278
Identifier Residue Sequence Organism Cell Line
SIGNOR-186427 Tyr78 RAIDFSPyLEPLGAP Homo sapiens HEK-293 Cell
pmid sentence
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
+ ABL2up-regulates activity img/direct-activation.png phosphorylation GPX1 0.328
Identifier Residue Sequence Organism Cell Line
SIGNOR-104328 Tyr98 EILNSLKyVRPGGGF Homo sapiens
pmid sentence
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
+ RIN1up-regulates img/direct-activation.png phosphorylation ABL2 0.603
Identifier Residue Sequence Organism Cell Line
SIGNOR-136961 Homo sapiens
pmid sentence
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
+ ABL2up-regulates img/indirect-activation.png Actin_cytoskeleton_reorganization 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-266594 Mus musculus
pmid sentence
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
+ DIP2Aup-regulates activity img/direct-activation.png binding ABL2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-266593 Mus musculus Pyramidal Neuron
pmid sentence
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
+ BTF3up-regulates quantity by expression img/indirect-activation.png transcriptional regulation ABL2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-253947 Homo sapiens Pancreatic Cancer Cell
pmid sentence
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
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