IdA stringlengths 6 21 | IdB stringlengths 6 21 | labels float64 0 2 | mechanism stringclasses 40
values | effect stringclasses 10
values | score float64 0.1 0.99 ⌀ | sentence stringlengths 10 1.63k ⌀ | signor_id stringlengths 12 14 |
|---|---|---|---|---|---|---|---|
P00742 | P08709 | 2 | binding | up-regulates activity | 0.541 | TF has a high affinity for FVII and enables the trace levels (∼1% of the total FVII) of activated FVII (FVIIa) in the blood to cleave specific sites in the serine proteases FIX and FX, activating them into FIXa and FXa, respectively. | SIGNOR-263545 |
P08709 | P00742 | 2 | cleavage | up-regulates activity | 0.541 | The factor VII zymogen is cleaved at arginine 152 by a variety of proteases, including thrombin, factor IXa, factor Xa, and factor VIIa–tissue factor to produce the serine protease factor VIIa. | SIGNOR-263523 |
P15172 | Q6STE5 | 2 | binding | up-regulates activity | 0.538 | We show that the muscle determination factor MyoD and the SWI/SNF subunit BAF60c interact on the regulatory elements of MyoD-target genes in myoblasts, prior to activation of transcription. BAF60c facilitates MyoD binding to target genes and marks the chromatin for signal-dependent recruitment of the SWI/SNF core to mu... | SIGNOR-238289 |
Q6STE5 | P15172 | 2 | binding | up-regulates | 0.538 | This suggests a novel mechanism by which myod interacts with the promoter indirectly via pbx-1 and recruits chromatin-remodeling enzymes, which then facilitate the binding of myod and other regulators. Demonstration of physical interactions between brg1 and myod and brg1 and pbx support this conclusion | SIGNOR-136130 |
P23458 | P52333 | 2 | phosphorylation | up-regulates | 0.536 | Il-7r signalling is initiated when il-7 crosslinks the extracellular domains of il-7ralpha and gammac, bringing together jak1 and jak3, which mutually phosphorylate each other, increasing their kinase activity. | SIGNOR-152917 |
P60484 | P12931 | 2 | phosphorylation | down-regulates | 0.536 | Activated src reduces the ability of pten to dephosphorylate phosphatidylinositols in micelles and promotes akt translocation to cellular plasma membranes but does not alter pten activity toward water-soluble phosphatidylinositols. | SIGNOR-103721 |
P52333 | P23458 | 2 | phosphorylation | up-regulates | 0.536 | Il-7r signalling is initiated when il-7 crosslinks the extracellular domains of il-7ralpha and gammac, bringing together jak1 and jak3, which mutually phosphorylate each other, increasing their kinase activity. | SIGNOR-152914 |
P12931 | P60484 | 2 | dephosphorylation | down-regulates activity | 0.536 | Antisense- or shRNA mediated downregulation of PTEN induced SRC Tyr416 phosphorylation, SRC activation, and ultimately elevated TZMB resistance, whereas induction of PTEN phosphatase activity directly dephosphorylated SRC Tyr416 residue and so abolished SRC activity .|These observations indicate that the loss of PTEN p... | SIGNOR-277009 |
O60674 | P15509 | 2 | binding | up-regulates activity | 0.533 | JAK2 is a primary kinase regulating all the known activities of GM-CSF. JAK2 mediates GM-CSF induced c-fos activation through receptor phosphorylation and Shc/PTP 1D activation. | SIGNOR-249502 |
P15509 | O60674 | 2 | phosphorylation | up-regulates activity | 0.533 | JAK2 is a primary kinase regulating all the known activities of GM-CSF. JAK2 mediates GM-CSF induced c-fos activation through receptor phosphorylation and Shc/PTP 1D activation. | SIGNOR-249503 |
Q9UKV5 | P06744 | 2 | binding | up-regulates | 0.53 | Pgi is a housekeeping gene encoding phosphoglucose isomerase (pgi) a glycolytic enzyme that also functions as a cytokine (autocrine motility factor (amf)/neuroleukin/maturation factor) upon secretion from the cell and binding to its 78 kda seven-transmembrane domain receptor (gp78/amf-r) | SIGNOR-97270 |
Q14457 | Q92995 | 2 | deubiquitination | up-regulates quantity by stabilization | 0.53 | Similarly, the overexpression of USP13 reduced the levels of ubiquitinated Beclin1 which was inhibited by spautin-1 (Figure 4E) | SIGNOR-260295 |
P06744 | Q9UKV5 | 2 | polyubiquitination | down-regulates quantity by destabilization | 0.53 | Gp78 is a ubiquitin ligase that plays a vital role in endoplasmic reticulum (ER)-associated degradation (ERAD). Here we report that autocrine motility factor (AMF), also known as phosphoglucose isomerase (PGI), is a novel substrate of gp78. We show that polyubiquitylation of AMF requires cooperative interaction between... | SIGNOR-272177 |
Q92995 | Q14457 | 2 | deubiquitination | up-regulates quantity by stabilization | 0.53 | We found that endogenous Beclin1 can interact with USP13 and the interaction was reduced in the presence of spautin-1 (Figure 5C). Interestingly, the DUB activities were significantly increased when USP13 and USP10 coincubated together or with Beclin1 or all 3 proteins together, suggesting the DUB activity can be signi... | SIGNOR-260296 |
P22681 | P06213 | 2 | phosphorylation | up-regulates activity | 0.528 | Insulin receptor phosphorylates Cbl on tyrosines 371, 700, and 774 in the presence of APS. This phosphorylation event is required for the recruitment of Crk to the CAP/Cbl complex and for the subsequent activation of GLUT4 translocation. | SIGNOR-251304 |
P06213 | P22681 | 2 | ubiquitination | down-regulates | 0.528 | Aps couples c-cbl to theinsulinreceptor, resulting in ubiquitination of theinsulinreceptor | SIGNOR-109688 |
P29350 | P12931 | 2 | phosphorylation | up-regulates | 0.527 | Recombinant shp-1 had elevated activity subsequent to phosphorylation by src in vitro, and shp-1 variants with mutated phosphorylation sites in the c terminus, shp-1 y538f, and shp-1 y538f,y566f were less active toward src-generated phosphoproteins in intact cells. | SIGNOR-120492 |
P09619 | P00519 | 2 | phosphorylation | down-regulates activity | 0.527 | 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. | SIGNOR-260931 |
P00519 | P09619 | 2 | phosphorylation | up-regulates activity | 0.527 | Here, we show that PDGFR-beta-phosphorylation of Abl kinases has functional consequences as PDGFR-beta phosphorylates Abl kinases on Y245 and Y412, sites known to be required for activation of Abl kinases. | SIGNOR-278319 |
P12931 | P29350 | 2 | dephosphorylation | up-regulates activity | 0.527 | Several protein tyrosine phosphatases are capable of activating Src by dephosphorylating Y530 (reviewed in ref. 9). These include PTP-α, PTP-λ, SHP-1, SHP-2, and PTP1B | SIGNOR-248472 |
O43526 | O43525 | 2 | binding | up-regulates activity | 0.515 | The M-current regulates the subthreshold electrical excitability of many neurons, determining their firing properties and responsiveness to synaptic input. To date, however, the genes that encode subunits of this important channel have not been identified. The biophysical properties, sensitivity to pharmacological bloc... | SIGNOR-268832 |
O43525 | O43526 | 2 | binding | up-regulates activity | 0.515 | The M-current regulates the subthreshold electrical excitability of many neurons, determining their firing properties and responsiveness to synaptic input. To date, however, the genes that encode subunits of this important channel have not been identified. The biophysical properties, sensitivity to pharmacological bloc... | SIGNOR-268833 |
Q13362 | P28482 | 2 | phosphorylation | down-regulates | 0.513 | Iex-1 binds to b56 subunits and perk independently, enhances b56 phosphorylation by erk at a conserved ser/pro site in this complex and triggers dissociation from the catalytic subunit. | SIGNOR-144313 |
P28482 | Q13362 | 2 | binding | down-regulates | 0.513 | B56-containing pp2a dephosphorylate erk and their activity is controlled by the early gene iex-1 and erk | SIGNOR-144325 |
Q14457 | Q14694 | 2 | deubiquitination | up-regulates quantity by stabilization | 0.509 | Similarly, the overexpression of USP13 reduced the levels of ubiquitinated Beclin1 which was inhibited by spautin-1 (Figure 4E) | SIGNOR-260299 |
Q14694 | Q14457 | 2 | deubiquitination | up-regulates quantity by stabilization | 0.509 | Interestingly, Beclin1 also controls the protein stabilities of USP10 and USP13 by regulating their deubiquitinating activities. | SIGNOR-260298 |
P10721 | Q9ULZ2 | 2 | binding | up-regulates activity | 0.507 | STAP-1 was tyrosine-phosphorylated by activated c-kit. An in vitro binding assay suggested that the STAP-1 SH2 domain interacted with several tyrosine-phosphorylated proteins including c-kit and STAT5. These suggest that STAP-1 functions as an adaptor molecule downstream of c-kit in hematopoietic stem cells. | SIGNOR-261822 |
Q9ULZ2 | P10721 | 2 | phosphorylation | up-regulates activity | 0.507 | STAP-1 was tyrosine-phosphorylated by activated c-kit. An in vitro binding assay suggested that the STAP-1 SH2 domain interacted with several tyrosine-phosphorylated proteins including c-kit and STAT5. These suggest that STAP-1 functions as an adaptor molecule downstream of c-kit in hematopoietic stem cells. | SIGNOR-261820 |
P38398 | P31749 | 2 | phosphorylation | up-regulates | 0.506 | Phosphatidylinositol 3-kinase/akt signaling enhances nuclear localization and transcriptional activity of brca1. mutation of threonine 509 in brca1, the site of akt phosphorylation, to an alanine, attenuates the ability of heregulin to induce brca1 nuclear accumulation | SIGNOR-154312 |
P31749 | P38398 | 2 | ubiquitination | down-regulates quantity by destabilization | 0.506 | The BRCA1-BRCT domains bind to phosphorylated AKT (pAKT) and lead to its ubiquitination toward protein degradation | SIGNOR-252435 |
O75385 | P54646 | 2 | phosphorylation | up-regulates | 0.505 | In a screen for conserved substrates of ampk, we identified ulk1 and ulk2, mammalian orthologs of the yeast protein kinase atg1, which is required for autophagy. | SIGNOR-186637 |
P54646 | O75385 | 2 | phosphorylation | down-regulates | 0.505 | Here we report that ulk1/2 in turn phosphorylates all three subunits of ampk and thereby negatively regulates its activity. Thus, we propose that ulk1 is not only involved in the induction of autophagy, but also in terminating signaling events that trigger autophagy. In our model, phosphorylation of ampk by ulk1 repres... | SIGNOR-173050 |
O75626 | Q02548 | 2 | transcriptional regulation | down-regulates quantity | 0.502 | Overexpression of BSAP reduced Blimp-1 expression in CH12.LX.A2 clones but not in MPC11 clones. In addition, overexpression of BSAP in CH12.LX.A2 cells suppressed spontaneous appearance of cells with high Syndecan-1 expression and high amounts of intracytosolic as well as secreted Ig synthesi | SIGNOR-269085 |
Q02548 | O75626 | 2 | transcriptional regulation | down-regulates quantity | 0.502 | Blimp-1 binds a site on the Pax-5 promoter in vitro and in vivo and represses the Pax-5 promoter in a binding-site-dependent manner. | SIGNOR-269089 |
Q99801 | P10275 | 2 | transcriptional regulation | up-regulates quantity by expression | 0.502 | Whereas androgen receptor (AR) positively regulates NKX3.1 expression, NKX3.1 negatively modulates AR transcription and consequently the AR-associated signaling events. | SIGNOR-251546 |
P10275 | Q99801 | 2 | transcriptional regulation | down-regulates quantity by repression | 0.502 | Whereas androgen receptor (AR) positively regulates NKX3.1 expression, NKX3.1 negatively modulates AR transcription and consequently the AR-associated signaling events. | SIGNOR-251547 |
Q06187 | Q08881 | 2 | phosphorylation | down-regulates activity | 0.497 | Btk-SH3 mutant Y223A was not phosphorylated by Itk. Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop.|In Btk, the SH3 domain mutation Y223F results in enhanced fibr... | SIGNOR-251333 |
Q08881 | Q06187 | 2 | phosphorylation | up-regulates | 0.497 | Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanismthe major phosphorylation site... | SIGNOR-98036 |
P42680 | Q06187 | 2 | phosphorylation | up-regulates | 0.496 | Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. Here, we could confirm that ... | SIGNOR-98086 |
Q06187 | P42680 | 2 | phosphorylation | down-regulates activity | 0.496 | Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the SH3 domain via a transphosphorylation mechanism, which for Bruton's tyrosine ... | SIGNOR-246652 |
P01023 | P14780 | 2 | cleavage | down-regulates quantity by destabilization | 0.492 | The complex formation was confirmed by the use of 125I-labeled matrix metalloproteinase-2. The cleavage sites in the "bait" regions following formation of high-molecular-weight complexes of matrix metalloproteinases with the alpha-macroglobulins were determined by protein sequence analysis. Pregnancy zone protein was c... | SIGNOR-261740 |
P14780 | P01023 | 2 | binding | down-regulates activity | 0.492 | Both PZP and a2M collagenase complexes incubated with gelatin demonstrated a significant inhibition of the catalytic activity| MMP-2 and MMP-9 cause a significant degradation of these bands and the background, a degradation which is prevented by both a2M and PZP. | SIGNOR-261801 |
P28360 | P50458 | 2 | binding | down-regulates activity | 0.477 | Protein complex formation between Msx1 and Lhx2 homeoproteins is incompatible with DNA binding activity | SIGNOR-241327 |
P50458 | P28360 | 2 | binding | down-regulates activity | 0.477 | Protein complex formation between Msx1 and Lhx2 homeoproteins is incompatible with DNA binding activity | SIGNOR-241330 |
Q16539 | P43403 | 2 | phosphorylation | up-regulates activity | 0.476 | Lck, Fyn, and Zap70 activate p38 even in the absence of Tyr182 phosphorylation.p38 is a substrate for Fyn, Lck and Zap70.Thus, T cell Src family kinases and Zap70 activate p38 by phosphorylating Tyr323. | SIGNOR-276030 |
P43403 | Q16539 | 2 | phosphorylation | down-regulates activity | 0.476 | We have found that T cell p38 MAP kinase (MAPK), which is directly phosphorylated and activated by ZAP-70 downstream of the TCR, in turn phosphorylates Thr-293 in the interdomain B region of ZAP-70. These results identify a tight negative feedback loop in which ZAP-70-activated p38 reciprocally phosphorylates ZAP-70 an... | SIGNOR-277384 |
Q96LT7 | P62820 | 2 | binding | up-regulates activity | 0.474 | Thus, our data identify C9orf72 as a novel Rab1a effector in the regulation of autophagy and indicate that C9orf72 haploinsufficiency and associated reductions in autophagy might be the underlying cause of C9ALS/FTD-associated p62 pathology. | SIGNOR-261282 |
Q13363 | O60315 | 2 | binding | up-regulates activity | 0.474 | The two members of the ZEB family of zinc finger factors (ZEB-1/deltaEF1 and ZEB-2/SIP1) regulate TGFbeta/BMP signaling in opposite ways: ZEB-1/deltaEF1 synergizes with Smad-mediated transcriptional activation, while ZEB-2/SIP1 represses it. Here we report that these antagonistic effects by the ZEB proteins arise from ... | SIGNOR-268953 |
O60315 | Q13363 | 2 | binding | up-regulates activity | 0.474 | Polycomb protein Pc2 acts as an SUMO E3 ligase for SIP1. SIP1 is an active transcription repressor for many transcription factors and target genes. SIP1 Sumoylation Disrupts the Recruitment of the Corepressor CtBP | SIGNOR-225484 |
P62820 | Q96LT7 | 2 | binding | up-regulates activity | 0.474 | C9orf72 acts as an effector of Rab1a that recruits active Rab1a to theULK1 complex to promote translocation of the ULK1 complex to thephagophore during autophagy initiation | SIGNOR-261297 |
P24385 | Q92769 | 2 | binding | up-regulates | 0.469 | Cyclin d1 bound hdac in vivo and preferentially physically associated with hdac1, hdac2, hdac3, and hdac5. | SIGNOR-134062 |
Q92769 | P24385 | 2 | binding | up-regulates | 0.469 | Cyclin d1 bound hdac in vivo and preferentially physically associated with hdac1, hdac2, hdac3, and hdac5. | SIGNOR-134053 |
P06241 | P17612 | 2 | phosphorylation | up-regulates | 0.459 | The serine 21 (s21) residue of fyn is a protein kinase a (pka) recognition site within an rxxs motif of the amino terminal sh4 domain of fyn. In addition, s21 is critical for fyn kinase-linked cellular signaling. Mutation of s21a blocks pka phosphorylation of fyn and alters its tyrosine kinase activity. | SIGNOR-167147 |
Q9UN86 | Q13283 | 2 | binding | up-regulates activity | 0.459 | Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) is a component of SGs that initiates the assembly of SGs by forming a multimer. In this study, we examined the role of G3BP2, a close relative of G3BP1, in SG formation. Although single knockdown of either G3BP1 or G3BP2 in 293T cells partially reduced ... | SIGNOR-260862 |
Q13283 | Q9UN86 | 2 | binding | up-regulates activity | 0.459 | Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) is a component of SGs that initiates the assembly of SGs by forming a multimer. In this study, we examined the role of G3BP2, a close relative of G3BP1, in SG formation. Although single knockdown of either G3BP1 or G3BP2 in 293T cells partially reduced ... | SIGNOR-260863 |
P17612 | P06241 | 2 | phosphorylation | up-regulates activity | 0.459 | We found that the Src family kinase Fyn phosphorylates the catalytic subunit of PKA (PKA-C) at Y69, thereby increasing PKA kinase activity. | SIGNOR-277410 |
P31749 | Q01860 | 2 | transcriptional regulation | down-regulates quantity by repression | 0.457 | Furthermore, in ECCs, unphosphorylated Oct4 bound to the AKT1 promoter and repressed its transcription. | SIGNOR-252635 |
Q01860 | P31749 | 2 | phosphorylation | up-regulates quantity by stabilization | 0.457 | Here we show that in ECCs, Akt phosphorylated the master pluripotency factor Oct4 at threonine 235, and that the levels of phosphorylated Oct4 in ECCs correlated with resistance to apoptosis and tumorigenic potential. Phosphorylation of Oct4 increased its stability and facilitated its nuclear localization and its inter... | SIGNOR-252545 |
Q5S007 | Q14155 | 2 | binding | up-regulates | 0.456 | Arhgef7 is interacting with lrrk2 in vitro and in vivo. Gtpase activity of full-length lrrk2 increases in the presence of recombinant arhgef7. Arhgef7 might act as a guanine nucleotide exchange factor for lrrk2 | SIGNOR-169217 |
O15146 | O96014 | 2 | binding | up-regulates | 0.456 | Musk has an extracellular region with homology to the frizzled crd,binding of which by wnt11 stimulates a pcp-like pathway during neuromuscolar development. Here, we show that in vivo, wnt11r and wnt4a initiate musk translocation from muscle membranes to recycling endosomes we provide evidence that wnt9a and wnt11 bind... | SIGNOR-199641 |
Q14155 | Q5S007 | 2 | phosphorylation | up-regulates | 0.456 | Arhgef7 is interacting with lrrk2 in vitro and in vivo. Lrrk2 phosphorylates arhgef7 in vitro.Two Threonine residues, t107 and t143, within the arhgef7 n-terminus were identified with high confidence | SIGNOR-169221 |
O96014 | O15146 | 2 | binding | up-regulates | 0.456 | Like ror, musk has an extracellular region with homolgogy to the frizzled crd, binding of which by wnt11 stimulates a pcp-like pathway during neuromuscular development | SIGNOR-199518 |
P24941 | P22674 | 2 | binding | up-regulates activity | 0.453 | Phosphorylation of cyclin O, a novel cyclin family protein containing a cyclin-like domain, is involved in the activation of cyclin-dependent kinase 2|This activity was reduced in cells overexpressing cyclin O, in which the 81st serine had been replaced with alanine (S81A). These results suggest that cyclin O is a nove... | SIGNOR-275616 |
P22674 | P24941 | 2 | phosphorylation | up-regulates activity | 0.453 | Phosphorylation of cyclin O, a novel cyclin family protein containing a cyclin-like domain, is involved in the activation of cyclin-dependent kinase 2|This activity was reduced in cells overexpressing cyclin O, in which the 81st serine had been replaced with alanine (S81A). These results suggest that cyclin O is a nove... | SIGNOR-275615 |
Q9ULJ6 | P46531 | 2 | binding | up-regulates activity | 0.452 | The N-terminal domain (NTD) is critical for Zmiz1 to function as a Notch collaborator. Zmiz1 and Notch1 cooperatively recruit each other to chromatin through the TPR domain. The N-terminal domain (NTD) of Zmiz1 is important for enhancing Notch reporter activity and contains tetratricopeptide repeats (TPR) that mediate ... | SIGNOR-263937 |
P46531 | Q9ULJ6 | 2 | binding | up-regulates activity | 0.452 | The N-terminal domain (NTD) is critical for Zmiz1 to function as a Notch collaborator. Zmiz1 and Notch1 cooperatively recruit each other to chromatin through the TPR domain. The N-terminal domain (NTD) of Zmiz1 is important for enhancing Notch reporter activity and contains tetratricopeptide repeats (TPR) that mediate ... | SIGNOR-263936 |
P49757 | Q00987 | 2 | ubiquitination | down-regulates | 0.444 | These data strongly suggest thatmdm2functions as the ubiquitin ligase toward hnumb and that it induces its degradation in intact cells. | SIGNOR-99497 |
Q00987 | P49757 | 2 | binding | down-regulates | 0.444 | Numb interacts with mdm2, and inhibits its ubiquitin-ligase function on tp53 (which in itself is inhibitory for tp53), thus numb activates (b) tp53 | SIGNOR-168454 |
Q00987 | P32121 | 2 | binding | up-regulates quantity by stabilization | 0.434 | Our current results demonstrated that the binding of Mdm2 to beta-arrestin 2 was significantly enhanced by stimulation of GPCRs. Activation of GPCRs led to formation of a ternary complex of Mdm2, beta-arrestin 2, and GPCRs and thus recruited Mdm2 to GPCRs at plasma membrane. Moreover, the binding of beta-arrestin 2 to ... | SIGNOR-272592 |
P32121 | Q00987 | 2 | ubiquitination | down-regulates quantity | 0.434 | Indeed, the ubiquitination of \u03b2-arrestin2 by Mdm2 H457S was severely reduced in comparison to Mdm2 wt ( xref ).|Loss of Mdm2 E3 ligase activity causes dominant nuclear localization of beta-arrestin2. | SIGNOR-278760 |
P10827 | P10276 | 2 | binding | up-regulates | 0.432 | We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. | SIGNOR-133231 |
P10276 | P10827 | 2 | binding | up-regulates | 0.432 | We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. | SIGNOR-133240 |
P67775 | P12931 | 2 | phosphorylation | down-regulates | 0.43 | We found that ?-Syn gene overexpression in sk-n-sh cells and primary neurons led to pp2a/c phosphorylation at y307, a known target of src kinase, and consequent phosphatase inhibition. | SIGNOR-202192 |
P12931 | P67775 | 2 | dephosphorylation | down-regulates activity | 0.43 | We show that PR55gamma binds c-SRC and modulates the phosphorylation of serine 12 of c-SRC, a residue we demonstrate to be required for JNK activation by c-SRC | SIGNOR-247970 |
P00533 | P30530 | 2 | phosphorylation | up-regulates activity | 0.43 | AXL trans-actives EGFR in a ligand independent manner and induces phosphorylation of EGFR on tyrosine 1173.|In our models AXL seems to induce a re-wiring of the EGFR signaling towards the PLCgamma-PKC axis by receptor phosphorylation at tyrosine 1173. | SIGNOR-279141 |
P30530 | P00533 | 2 | phosphorylation | up-regulates activity | 0.43 | In this study, we have identified for the first time a direct interaction between EGFR and Axl RTKs, with EGF and EGFR induced activation of Axl as a novel signalling pathway to invasion in cancer cells.|The activation of Axl was shown to occur through direct phosphorylation by EGFR of Axl tyrosine 779, one of the key ... | SIGNOR-279734 |
Q12933 | P61088 | 2 | ubiquitination | up-regulates activity | 0.428 | Intact ring and zinc finger domains are required for tnfalfa-induced traf2 ubiquitination, which is also dependent on ubc13. Traf2 ubiquitination coincides with its translocation to the insoluble cellular fraction, resulting in selective activation of jnk. Ubc13 expression by rnai resulted in tnfalfa-induced traf2 tran... | SIGNOR-121274 |
P61088 | Q12933 | 2 | binding | up-regulates activity | 0.428 | Traf2, ubc13, and ikkgamma were required for complex assembly and activation of mekk1 and mapk cascades. | SIGNOR-179479 |
P14921 | Q99684 | 2 | binding | down-regulates activity | 0.426 | Co-immunoprecipitation analyses and glutathione-S-transferase pull-down assays revealed that ETS1 bound directly to GFI1 via its Ets domain, and GFI1 bound to ETS1 via its zinc-finger domain. Luciferase (Luc) assays using artificial reporters showed that GFI1 repressed ETS1-mediated transcriptional activation and ETS1 ... | SIGNOR-254201 |
Q99684 | P14921 | 2 | binding | down-regulates activity | 0.426 | Co-immunoprecipitation analyses and glutathione-S-transferase pull-down assays revealed that ETS1 bound directly to GFI1 via its Ets domain, and GFI1 bound to ETS1 via its zinc-finger domain. Luciferase (Luc) assays using artificial reporters showed that GFI1 repressed ETS1-mediated transcriptional activation and ETS1 ... | SIGNOR-254202 |
P53350 | P78527 | 2 | phosphorylation | up-regulates activity | 0.425 | DNA-PKcs Promotes Plk1 Activation.|Further analysis revealed that DNA-PKcs could directly phosphorylate the C-terminal PBD domain of Plk1 (lane 8). | SIGNOR-279562 |
P78527 | P53350 | 2 | phosphorylation | up-regulates activity | 0.425 | Moreover, PLK1 phosphorylates DNA-PKcs directly on Ser 3205 invitro, suggesting that DNA-PKcs Ser 3205 is a direct target of PLK1 in mitosis. | SIGNOR-278188 |
P27361 | Q13362 | 2 | binding | down-regulates | 0.42 | B56-containing pp2a dephosphorylate erk and their activity is controlled by the early gene iex-1 and erk | SIGNOR-144328 |
Q13362 | P27361 | 2 | phosphorylation | down-regulates | 0.42 | Iex-1 binds to b56 subunits and perk independently, enhances b56 phosphorylation by erk at a conserved ser/pro site in this complex and triggers dissociation from the catalytic subunit. | SIGNOR-144317 |
P13631 | P10827 | 2 | binding | up-regulates | 0.419 | We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. | SIGNOR-133246 |
P10827 | P13631 | 2 | binding | up-regulates | 0.419 | We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs | SIGNOR-133237 |
P10827 | P10826 | 2 | binding | up-regulates | 0.416 | We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs | SIGNOR-133234 |
P10826 | P10827 | 2 | binding | up-regulates | 0.416 | Ee report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs | SIGNOR-133243 |
O75592 | P01106 | 2 | transcriptional regulation | down-regulates quantity by repression | 0.415 | We identified several E3 ligases as strong candidates responsible for AR and MYC protein loss as HECTD4, MYCBP2, and TRIM49. HECTD4 and MYCBP2 target AR and MYC for degradation while TRIM49 appears to promote AR and MYC stability. We have shown that these E3 ligases in turn are directly regulated by MYC. MYC in turn r... | SIGNOR-267145 |
P01106 | O75592 | 2 | ubiquitination | down-regulates quantity by destabilization | 0.415 | We identified several E3 ligases as strong candidates responsible for AR and MYC protein loss as HECTD4, MYCBP2, and TRIM49. HECTD4 and MYCBP2 target AR and MYC for degradation while TRIM49 appears to promote AR and MYC stability. We have shown that these E3 ligases in turn are directly regulated by MYC. MYC in turn r... | SIGNOR-267147 |
P06733 | P01106 | 2 | transcriptional regulation | up-regulates quantity | 0.411 | C-Myc directly transactivates genes encoding GLUT1, phosphofructokinase, and enolase and increases glucose uptake in Rat1 fibroblasts. Nuclear run-on studies confirmed that the GLUT1 transcriptional rate is elevated by c-Myc. Our findings suggest that overexpression of the c-Myc oncoprotein deregulates glycolysis throu... | SIGNOR-259989 |
P01106 | P06733 | 2 | transcriptional regulation | down-regulates quantity by repression | 0.411 | This result suggests that MBP-1 in vivo acts as a sequence-specific repressor. | SIGNOR-261594 |
O75843 | P46934 | 2 | monoubiquitination | up-regulates activity | 0.401 | Gamma2-Adaptin is a putative member of the clathrin adaptor protein family with unknown physiological function. We previously reported that gamma2-adaptin acts as a ubiquitin receptor by virtue of its ubiquitin-interacting motif. Here we demonstrate that this motif mediates a specific physical interaction with the ubiq... | SIGNOR-272634 |
P46934 | O75843 | 2 | binding | up-regulates activity | 0.401 | Gamma2-Adaptin is a putative member of the clathrin adaptor protein family with unknown physiological function. We previously reported that gamma2-adaptin acts as a ubiquitin receptor by virtue of its ubiquitin-interacting motif. Here we demonstrate that this motif mediates a specific physical interaction with the ubiq... | SIGNOR-272636 |
P00519 | P16333 | 2 | binding | down-regulates activity | 0.4 | 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 site... | SIGNOR-109672 |
P16333 | P00519 | 2 | phosphorylation | up-regulates | 0.4 | 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 tyrosi... | SIGNOR-196043 |
P28360 | Q07687 | 2 | binding | down-regulates activity | 0.399 | We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperati... | SIGNOR-240918 |
Q07687 | P28360 | 2 | binding | down-regulates activity | 0.399 | We demonstrate that dimerization by Msx and Dlx proteins is mediated through their homeodomains and that the residues required for this interaction correspond to those necessary for DNA binding. Unlike most other known examples of homeoprotein interactions, association of Msx and Dlx proteins does not promote cooperati... | SIGNOR-240929 |
P06241 | P10586 | 2 | dephosphorylation | down-regulates | 0.396 | Regulation of lck and fyn tyrosine kinase activities by transmembrane protein tyrosine phosphatase leukocyte common antigen-related molecule. | SIGNOR-96768 |
P10586 | P06241 | 2 | phosphorylation | up-regulates activity | 0.396 | LAR PTPase domain 2 was tyrosine phosphorylated by Fyn tyrosine kinase. we confirmed that LAR dephosphorylated the phosphorylated tyrosine residues of Lck and Fyn, and tyrosine residue(s) in LAR PTPase D2 was phosphorylated by Fyn to supply Fyn SH2 binding site. | SIGNOR-251180 |
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