IdA string | IdB string | labels int64 | mechanism string | effect string | score float64 | sentence string | signor_id string |
|---|---|---|---|---|---|---|---|
Q13153 | O95747 | 0 | phosphorylation | down-regulates activity | 0.382 | OSR1 phosphorylated threonine 84 in the N-terminal regulatory domain of PAK1. phosphorylation of PAK1 by OSR1 desensitizes PAK1 to activation by small G proteins, providing a modulatory input to PAK1 activity. | SIGNOR-250210 |
Q07955 | O43187 | 0 | phosphorylation | down-regulates activity | 0.348 | IRAK2 phosphorylates SRSF1 and thereby reduces SRSF1 binding to the target mRNAs. | SIGNOR-278406 |
P49023 | P12931 | 0 | phosphorylation | up-regulates activity | 0.808 | Here, we demonstrate that Src kinase directly phosphorylates Y88 paxillin|In this study, we also show how pY88 paxillin transduces a signal to activate Akt | SIGNOR-263977 |
P02545 | P06493 | 0 | phosphorylation | up-regulates | 0.536 | Phosphorylation by mitotic cdc2 kinase at ser-22, ser-390, and ser-392 residues on lamin a/c, or by protein kinase c (pkc) during apoptosis, leads to the depolymerization of lamin (disassembly of the nuclear lamina), which may lead to their release from the inm | SIGNOR-181314 |
P52945 | P01308 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.643 | In conclusion, Pdx1 confers the expression of pancreatic β-cell-specific genes, such as genes encoding insulin, islet amyloid polypeptide, Glut2, and Nkx6.1. | SIGNOR-255541 |
Q00987 | P31749 | 0 | phosphorylation | up-regulates quantity by stabilization | 0.811 | Mitogen-induced activation of phosphatidylinositol 3-kinase (pi3-kinase) and its downstream target, the akt/pkb serine-threonine kinase, results in phosphorylation of mdm2 on serine 166 and serine 186. Phosphorylation on these sites is necessary for translocation of mdm2 from the cytoplasm into the nucleus.Both akt expression and serum treatment induced phosphorylation of mdm2 at ser186. | SIGNOR-116270 |
P26038 | Q13464 | 0 | phosphorylation | up-regulates activity | 0.688 | Rho-associated kinase (Rho-kinase), which is activated by the small GTPase Rho, phosphorylates moesin at Thr558 in vitro. Here, using a site- and phosphorylation state-specific antibody, we found that the expression of dominant active RhoA in COS7 cells induced moesin phosphorylation and the formation of microvilli-like structures at apical membranes where the Thr558-phosphorylated moesin accumulated, whereas the expression of dominant negative Rho-kinase inhibited both of these processes. | SIGNOR-249014 |
P04150 | Q13887 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.292 | We show that in addition, DEX-bound GR directly promotes the expression of adipogenic TFs, including C/EBPβ, Klf5, Klf9, and C/EBPα | SIGNOR-256118 |
Q9UGP8 | P68400 | 0 | phosphorylation | up-regulates activity | 0.291 | Sec63 was identified as a novel substrate and binding partner of protein kinase CK2. We identified serine 574, serine 576 and serine 748 as CK2 phosphorylation sites. Phosphorylation of Sec63 by CK2 enhanced its binding to Sec62. | SIGNOR-265267 |
Q04759 | P41594 | 1 | phosphorylation | up-regulates activity | 0.291 | Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839. | SIGNOR-249290 |
Q15437 | Q969U6 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.2 | SCFFBXW5 interacts with SEC23B and targets it for ubiquitylation and proteasome-mediated degradation. | SIGNOR-265286 |
P27361 | P42702 | 1 | phosphorylation | down-regulates | 0.299 | Thus, our results identify the human lifr as a substrate for mapk and suggest a mechanism of heterologous receptor regulation of lifr signaling occurring at ser-1044. | SIGNOR-32757 |
P28482 | Q15349 | 1 | phosphorylation | up-regulates | 0.717 | Erk-activates the rsk family of serine/threonine kinases,rsk1, rsk2, and rsk3. | SIGNOR-161515 |
Q8WVD3 | Q13315 | 0 | phosphorylation | up-regulates activity | 0.2 | We further confirm that RNF138 is phosphorylated by ATM at Ser124. | SIGNOR-279505 |
P42261 | P46934 | 0 | ubiquitination | down-regulates quantity | 0.419 | Finally, we show that ubiquitination of GluA1 by Nedd4-1 becomes more prevalent as neurons mature.|The ability of Nedd4-1 to reduce surface GluA1 levels required its ligase activity, since co-expression of a catalytically-inactive version of Nedd4-1 (Nedd4-1 CS) did not decrease surface GluA1 levels . | SIGNOR-278572 |
Q92993 | Q00987 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.654 | Furthermore, we provide evidence that Mdm2, the ubiquitin ligase of the p53 tumour suppressor, interacts physically with Tip60 and induces its ubiquitylation and proteasome-dependent degradation. | SIGNOR-272613 |
P45984 | P30307 | 1 | phosphorylation | down-regulates | 0.376 | Here we show that jnk directly phosphorylates cdc25c at serine 168 during g(2) phase of the cell cycle. Cdc25c phosphorylation by jnk negatively regulates its phosphatase activity and thereby cdk1 activation, enabling a timely control of mitosis onset. | SIGNOR-164093 |
P07910 | P68400 | 0 | phosphorylation | down-regulates activity | 0.357 | In contrast, hnRNP-C1 that was also modified at the CK1alpha phosphorylation sites exhibited a 14-500-fold decrease in binding affinity, demonstrating that CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C. | SIGNOR-133540 |
Q9HA47 | O95198 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.346 | We demonstrated that the ubiquitin E3 ligase KLHL2 interacted with UCK1 and mediated its polyubiquitination at the K81 residue and degradation. We showed that deubiquitinase USP28 antagonized KLHL2-mediated polyubiquitylation of UCK1. | SIGNOR-275962 |
Q02952 | P17252 | 1 | relocalization | up-regulates activity | 0.459 | A-kinase-anchoring protein 250 (AKAP250; gravin) acts as a scaffold that binds protein kinase A (PKA), protein kinase C and protein phosphatases, associating reversibly with the beta(2)-adrenergic receptor. | SIGNOR-271836 |
Q7KZI7 | Q05513 | 0 | phosphorylation | down-regulates | 0.266 | Hpar-1b is phosphorylated by apkc on threonine 595 importantly, phosphorylation of hpar-1b on t595 negatively regulates the kinase activity and plasma membrane localization of hpar-1b in vivo. | SIGNOR-124217 |
Q8IVH8 | Q13434 | 0 | ubiquitination | down-regulates quantity | 0.2 | MKRN4 ubiquitinated GLK at Lys650 residue.|Remarkably, MKRN4 overexpression induced GLK protein degradation in HEK293T cells and Jurkat T cells (figure 5A and B). | SIGNOR-278658 |
O14950 | Q12852 | 0 | phosphorylation | up-regulates | 0.2 | Zip kinase (hzipk) phosphorylated the regulatory light chain of myosin ii (mrlc) at both ser19 and thr18 in vitro. In this study, we demonstrate that hzipk also induces the diphosphorylation of mrlc in nonmuscle cells. | SIGNOR-113664 |
P18846 | O75582 | 0 | phosphorylation | up-regulates activity | 0.69 | Using embryonic fibroblasts derived from these mice we were able to demonstrate an important role for these enzymes in the activation of CREB and the closely related transcription factor ATF1. | Our results clearly demonstrate that MSK1 and MSK2 are the major, if not the only, protein kinases that mediate the phosphorylation of CREB at Ser133 and of ATF1 at Ser63 in fibroblasts | SIGNOR-249144 |
P23760 | P49841 | 0 | phosphorylation | up-regulates quantity | 0.334 | The ubiquitously expressed CK2 often provides the priming phosphorylation for GSK-3, however, we found that GSK-3beta alone was sufficient to phosphorylate PAX3 at both Ser205 and Ser197 and Ser201 in-vitro. | SIGNOR-278482 |
P16104 | Q99504 | 0 | dephosphorylation | down-regulates | 0.2 | Tyr142 is dephosphorylated by the tyr phosphatases eya1 and eya3. | SIGNOR-168927 |
P45983 | P10415 | 1 | phosphorylation | down-regulates | 0.582 | G(2)/m-phase cells proved more susceptible to death signals, and phosphorylation of bcl-2 appeared to be responsible, as a ser70ala substitution restored resistance to apoptosis. We noted that ask1 and jnk1 were normally activated at g(2)/m phase, and jnk was capable of phosphorylating bcl-2.. | SIGNOR-72361 |
P55211 | P36507 | 0 | phosphorylation | down-regulates activity | 0.347 | Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK|The opposing protein kinase activity is overcome by treatment with the broad-specificity kinase inhibitor staurosporine or with inhibitors of MEK1/2 | SIGNOR-249386 |
P17844 | P00519 | 0 | phosphorylation | up-regulates | 0.357 | 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. | SIGNOR-149988 |
Q13887 | Q9H0M0 | 0 | ubiquitination | up-regulates activity | 0.459 | WWP1 and Smurf2 were adopted to induce ubiquitination of endogenous KLF5 protein in cells.|WWP1 or Smurf2 degrades KLF5 by ubiquitination to repress fracture healing. | SIGNOR-278683 |
P03209 | P01574 | 1 | transcriptional regulation | down-regulates quantity by repression | 0.2 | Epstein-Barr Virus BRLF1 Inhibits Transcription of IRF3 and IRF7 and Suppresses Induction of Interferon-β. These results suggest that EBV Rta is capable of regulating the activation of the IFN-β promoter. | SIGNOR-266646 |
Q15398 | Q9BYB0 | 1 | relocalization | up-regulates activity | 0.2 | SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3). | SIGNOR-264600 |
Q13794 | Q00535 | 0 | phosphorylation | down-regulates | 0.356 | We show that noxa is phosphorylated on a serine residue (s(13)) in the presence of glucose. Phosphorylation promotes its cytosolic sequestration and suppresses its apoptotic function. We identify cdk5 as the noxa kinase | SIGNOR-170357 |
Q96P20 | Q9Y2R2 | 0 | dephosphorylation | up-regulates activity | 0.356 | Further, this explains how loss of PTPN22 and subsequent enhanced NLRP3 phosphorylation mediate a decrease in NLRP3 inflammasome activation.|Upon NLRP3 activation, PTPN22 dephosphorylates NLRP3 and thereby protects it from degradation, allowing robust inflammasome activity (summarized in Fig.S6). | SIGNOR-277056 |
P07101 | P28482 | 0 | phosphorylation | up-regulates | 0.441 | Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylase in vitro at comparable rates to other proteins thought to be physiological substrates of these protein kinases.The effect on activity of phosphorylating both ser31 and ser40 was not additive. The possible roles of mapkap kinase-1, mapkap kinase-2 and map kinase in the regulation of tyrosine hydroxylase in vivo are discussed. | SIGNOR-34674 |
O75582 | Q92934 | 1 | phosphorylation | down-regulates activity | 0.344 | Phosphorylation of Bad at Ser112 in response to growth factors or cytokines is generally linked to cell survival. Knockdown of MSK1 suppressed Bad phosphorylation after calcium ionophore A23187 treatment in neuronal cells | SIGNOR-262990 |
P43250 | Q15722 | 1 | phosphorylation | down-regulates activity | 0.474 | Thr(308) is a major residue involved in GRK6-mediated desensitization of BLT1 signaling. | SIGNOR-251213 |
Q9BYP7 | Q9UHW9 | 1 | phosphorylation | down-regulates activity | 0.444 | WNK3, which inhibits the activity of KCC3, promoted phosphorylation of Ser-96 as well as Thr-991 and Thr-1048. | SIGNOR-260912 |
P20916 | P06241 | 0 | phosphorylation | up-regulates activity | 0.425 | Fyn constitutively binds to MAG in a latent form. Ligand stimulation of L-MAG would result in activation of Fyn kinase and phosphorylation of Tyr-620. Binding and activation of PLC y through this phosphotyrosine residue would contribute to the signaling pathway involved in the regulation of myelination. | SIGNOR-251178 |
Q9H4E7 | P06239 | 0 | phosphorylation | up-regulates activity | 0.5 | In vitro kinase assays indeed demonstrated that Lck can phosphorylate wild-type IBP but not the Y210F mutant. IBP Binds PI(3,4,5)P3 upon Phosphorylation by Lck | SIGNOR-251372 |
Q9NQB0 | Q8WVD3 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.325 | Here, we show that NARF induces the ubiquitylation of TCF/LEF in vitro and in vivo, and functions as an E3 ubiquitin-ligase that specifically cooperates with the E2 conjugating enzyme E2-25K. We found that NLK augmented NARF binding and ubiquitylation of TCF/LEF, and this required NLK kinase activity. The ubiquitylated TCF/LEF was subsequently degraded by the proteasome. | SIGNOR-271593 |
Q00526 | Q5TKA1 | 1 | phosphorylation | up-regulates | 0.2 | In this report, we demonstrate that cyclin e1/cdk3 phosphorylates lin-9 on thr-96. Mutating thr-96 to alanine inhibits activation of cyclins a2 and b1 promoters, whereas a phosphomimetic asp mutant strongly activates their promoters and triggers accelerated entry into g2/m phase in 293t cells. | SIGNOR-204529 |
O60502 | P17858 | 1 | deglycosylation | up-regulates activity | 0.2 | Our previous investigation on O-GlcNAcylation of PFK1 has demonstrated that O-GlcNAcylation inhibits PFK1 enzyme activity|In cells, a single set of antagonistic enzymes-O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase are responsible for the addition and removal of GlcNAc moiety, respectively. | SIGNOR-267608 |
P08581 | Q6ZN28 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.394 | Human colon carcinoma SW480 cells express virtually no MACC1. MACC1 cDNA transfection led not only to strong increases in MACC1 mRNA expression (Fig. 3a), but also to a 40-fold upregulation of the HGF receptor MET mRNA expression (Fig. 3b). This was confirmed on the protein level | SIGNOR-266058 |
P49841 | Q15208 | 1 | phosphorylation | down-regulates activity | 0.278 | GSK-3β phosphorylated STK38 on residues S6 and T7 in vitro, depending largely on a PKA-mediated priming phosphorylation of STK38 on residues S10 and S11, respectively. Our results indicate that that GSK-3β inhibits STK38's full activation, and suggest that STK38 activation is required to prevent cell death in response to oxidative stress. | SIGNOR-276392 |
P41970 | P45984 | 0 | phosphorylation | down-regulates activity | 0.323 | JNK binds to the J box in the middle of the protein, and binding is required for phosphorylation of the adjacent EXport motif. Both the binding and phosphorylation sites (the JEX element) are important for Net export. | SIGNOR-250138 |
Q13485 | Q96JC1 | 0 | relocalization | down-regulates activity | 0.318 | The data demonstrating binding of TLP to TGF-β and activin type II receptors and selective inhibition of Smad3/Smad4 complex formation by deregulated TLP suggest that TLP is involved in localizing these receptors and Smad4 to specific intracellular compartments, where it regulates formation of Smad3/Smad4 but not Smad2/Smad4 complexes. | SIGNOR-261377 |
O00506 | Q9H4B6 | 1 | phosphorylation | down-regulates activity | 0.28 | STK25 inhibits the ability of SAV1 to counteract STRIPAK.|Using this antibody, we confirmed that SAV1 WT was indeed phosphorylated by STK25 at T26 in human cells (XREF_FIG). | SIGNOR-278369 |
Q5JTC6 | P49841 | 1 | relocalization | up-regulates activity | 0.419 | Amer1 binds ck1gamma, recruits axin and gsk3beta to the plasma membrane and promotes complex formation between axin and lrp6. | SIGNOR-171892 |
P07948 | Q06187 | 1 | phosphorylation | up-regulates | 0.545 | Phosphorylation at y551 requires lyn kinase activity, indicating that y551 is a transphosphorylation site \ this transphosphorylation at y551 is followed by phosphorylation at a second site, which is dependent on btk catalytic activity. | SIGNOR-41607 |
Q99590 | P49768 | 1 | cleavage | up-regulates activity | 0.294 | Remarkably, the caspases acting on PS1 could be subdivided in two groups. One group, containing caspase-8, -6 and -11, cleaved PS1 after residues ENDD329 and to a lesser extent after residues AQRD341. A second group consisting of caspase-3, -7 and -1 acted uniquely on AQRD341. Importantly, these two cleavage sites were also recognized by caspases in the C-terminal PS1 fragment produced by constitutive proteolysis. | SIGNOR-261758 |
Q9H2X6 | P51608 | 1 | phosphorylation | up-regulates activity | 0.478 | Here, we identify the homeodomain-interacting protein kinase 2 (HIPK2) as a kinase that binds MeCP2 and phosphorylates it at Ser 80 in vitro and in vivo. | SIGNOR-264549 |
Q04726 | P98170 | 0 | ubiquitination | up-regulates activity | 0.507 | These findings suggest that TLE3 ubiquitylation by XIAP may be required during Wnt pathway activation to facilitate its dissociation from TCF/Lef, allowing subsequent beta-catenin binding and transcriptional activation. | SIGNOR-278528 |
P46531 | Q00535 | 0 | phosphorylation | up-regulates activity | 0.32 | An in vitro kinase reaction demonstrated that T2132, S2136, and S2141 were CDK5\u2010phosphorylated sites in the Notch1 peptide (Figure\u00a02B, C, and D).|In conclusion, CDK5 positively regulates Notch1 function via phosphorylation, which in turn promotes cell proliferation and migration. | SIGNOR-279401 |
Q01094 | P17612 | 0 | phosphorylation | up-regulates activity | 0.2 | We confirmed the phosphorylation of T130, S235, and S364 by developing monoclonal antibodies against phospho-specific forms of these sites and showed that their phosphorylation is cell cycle-dependent. According to our results, PKA-mediated phosphorylation of E2F1 by PKA inhibits proliferation and glucose uptake and induces caspase-3 activation and senescence. | SIGNOR-277537 |
O95071 | Q96BY2 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.345 | We demonstrate that UBR5 interacts physically with MOAP-1, ubiquitylates MOAP-1 in vitro and inhibits MOAP-1 stability in cultured cells. | SIGNOR-278581 |
P20807 | Q15078 | 1 | cleavage | up-regulates activity | 0.261 | Calpains also modulate the activity of CDK5. Physiologically, CDK 5 is activated by p35 and its cleaved product p25. The latter has a longer half life than p35 and therefore it is a more potent activator of CDK5. The cleavage of p35 to p25 is mediated by calpain | SIGNOR-251604 |
O75122 | P49841 | 0 | phosphorylation | down-regulates activity | 0.515 | GSK-3beta directly phosphorylates CLASP2 at Ser533 and Ser537 within the region responsible for the IQGAP1 binding. Phosphorylation of CLASP2 results in the dissociation of CLASP2 from IQGAP1, EB1 and microtubules.| CLASPs were originally identified as CLIP-170-interacting proteins and later found to be required for microtubule stabilisation at the cortical regions of epithelial cells | SIGNOR-264826 |
P17612 | Q13002 | 1 | phosphorylation | up-regulates activity | 0.2 | GluR6 glutamate receptor, transiently expressed in mammalian cells, is directly phosphorylated by PKA, and that intracellularly applied PKA increases the amplitude of the glutamate response. Site-specific mutagenesis of the serine residue (Ser 684) representing a PKA consensus site completely eliminates PKA-mediated phosphorylation of this site as well as the potentiation of the glutamate response. | SIGNOR-250315 |
Q02447 | P62136 | 0 | dephosphorylation | down-regulates activity | 0.2 | Transcription factors Sp1 and Sp3 activate alpha-ENaC2 transcription through a GC-rich element (Sp1-binding site) in the promoter. Sp1 and Sp3 are essential for alpha-ENaC2 transcription in lung epithelial cells and that dephosphorylation of the Sp transcription factors by PP1 suppresses alpha-ENaC2 expression. | SIGNOR-251953 |
Q5S007 | P53805 | 1 | phosphorylation | up-regulates activity | 0.371 | LRRK2 Directly Phosphorylates RCAN1. | SIGNOR-278340 |
Q86UR5 | Q9UQM7 | 0 | phosphorylation | up-regulates | 0.347 | Two serine residues in rim1 (ser-241 and ser-287) and one serine residue in rim2 (ser-335) were required for 14-3-3 binding. Incubation with ca2+/calmodulin-dependent protein kinase ii greatly stimulated the interaction of recombinant n-terminal rim but not the s241/287a mutant with 14-3-3, | SIGNOR-103890 |
Q01082 | Q8NG27 | 0 | ubiquitination | down-regulates | 0.403 | The present study indicates that praja, a ring finger e3 ubiquitin ligase, interacts with elf and ubiquitinates it. | SIGNOR-141216 |
P46527 | P00519 | 0 | phosphorylation | down-regulates quantity | 0.595 | 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 | SIGNOR-245293 |
P60484 | Q93009 | 0 | deubiquitination | down-regulates activity | 0.741 | BCR-ABL disrupts PTEN nuclear-cytoplasmic shuttling through phosphorylation-dependent activation of HAUSP|hese data indicate that BCR-ABL phosphorylation of HAUSP modulates HAUSP’s deubiquitinase activity toward PTEN. | SIGNOR-276533 |
Q6VVB1 | P43004 | 1 | ubiquitination | up-regulates activity | 0.2 | On the contrary, overexpression of the laforin/malin complex promotes the retention of GLT-1 at the plasma membrane.|This is due to a direct ubiquitination of GLT-1 by laforin and malin and/or to changes in the dynamics of its Nedd4.2-mediated endocytosis, which is assisted by specific adaptors (\u03b1- and \u03b2-arrestins). | SIGNOR-278586 |
Q12888 | Q8IYW5 | 0 | ubiquitination | up-regulates quantity | 0.822 | E3 ligase RNF168-mediated 53BP1 ubiquitination through activated the mechanistic target of rapamycin (mTOR)-ribosomal S6 kinase (S6K) signaling and increased 53BP1 protein stability in response to IR|We further found that overexpression of RNF168 enhanced 53BP1 ubiquitination inhibited by G0S2 overexpression in U87 and LN229 cells in response to IR (Fig. xref f). | SIGNOR-278777 |
Q14451 | Q06124 | 0 | dephosphorylation | up-regulates activity | 0.435 | Dephosphorylation of Grb7 was blocked by the SHP inhibitor NSC-87877 (Zhan et al., 2009), supporting the specificity of SHP-2 in dephosphorylating Grb7.|Nuclear SHP-2 mediates the formation of an EGF induced complex of Grb7, HuR, and CRM1.|Using the \u03ba\u2013opioid receptor (OR [KOR]) as a model, we demonstrate that EGF activates nuclear SHP-2 (Src homology region 2\u2013containing tyrosine phosphatase), which dephosphorylates Grb7 in the nucleus. | SIGNOR-277169 |
O14757 | P06400 | 1 | phosphorylation | up-regulates activity | 0.422 | These results suggest that ser612 is phosphorylated by chk1/2 after dna damage, leading to the formation of prb-e2f-1. phosphorylation of prb at ser612 enhanced the formation of a complex between prb and e2f-1 | SIGNOR-153904 |
P16104 | Q9UIG0 | 0 | phosphorylation | up-regulates | 0.2 | We show that wstf phosphorylates tyr 142 of h2a.x, and that wstf activity has an important role in regulating several events that are critical for the dna damage response | SIGNOR-182831 |
Q9BY66 | P68431 | 1 | demethylation | up-regulates activity | 0.2 | KDM5 subfamily is capable of removing tri‐ and di‐ methyl marks from lysine 4 on histone H3 (H3K4). Depending on the methylation site, its effect on transcription can be either activating or repressing. | SIGNOR-264308 |
Q8IW41 | P25685 | 1 | phosphorylation | up-regulates | 0.463 | Phosphorylation of heat shock protein 40 (hsp40/dnajb1) by mitogen-activated protein kinase-activated protein kinase 5 (mk5/prak). Mk5 phosphorylates hsp40/dnajb1 in vivo at ser-149 or/and ser-151 and ser-171 in the c-terminal domain of hsp40/dnajb1. Mk5 modestly stimulates the atp hydrolyse activity of hsp40/hsp70 complex and enhances the repression of heat shock factor 1 driven transcription by hsp40/dnajb1. | SIGNOR-203464 |
Q9HD90 | Q14938 | 0 | transcriptional regulation | up-regulates quantity | 0.2 | For example, within the NFI targetome, we identified 6 collagen genes, 13 genes encoding potassium channel or glutamate receptor subunits and a range of factors related to axon guidance (e.g. Slit1, Robo1, Epha4, Epha5, Epha8) | SIGNOR-268905 |
P38484 | P23458 | 0 | phosphorylation | up-regulates activity | 0.66 | The activation of this signaling pathway involves the binding of IFN-g to two IFN-g receptor (IFN-gR) subunits, made up of respective IFNgR1:IFNgR2 pairs, which dimerize upon IFN-g binding to form the IFN-gR complex. Two JAKs, JAK1and JAK2,which bind to each IFN-gR subunits, respectively through their N-terminal domains, both become activated by tyrosine phosphorylation in a JAK2-dependent process. | SIGNOR-249491 |
Q8NG68 | Q9NY65 | 1 | tyrosination | down-regulates | 0.31 | Tubulin tyrosine ligase (ttl) adds a c-terminal tyr to __tubulin as part of a tyrosination/detyrosination cycle present in most eukaryotic cells. / ttl inhibits spontaneous tubulin polymerization | SIGNOR-176930 |
Q9GZT9 | Q13131 | 0 | phosphorylation | down-regulates activity | 0.373 | Mechanistically, AMPKα1 directly phosphorylated prolyl hydroxylase domain-containing (PHD)2 at serines 61 and 136, which suppressed PHD2-dependent hydroxylation of hypoxia-inducible factor (HIF)1α and subsequent regulation of hepatic hepcidin-related iron signalling. | SIGNOR-277592 |
Q9UGL1 | P68431 | 1 | demethylation | up-regulates activity | 0.2 | KDM5 subfamily is capable of removing tri‐ and di‐ methyl marks from lysine 4 on histone H3 (H3K4). Depending on the methylation site, its effect on transcription can be either activating or repressing. | SIGNOR-264302 |
Q13490 | Q01094 | 1 | ubiquitination | up-regulates activity | 0.336 | The ability of cIAP1 to promote wt E2F1 transcriptional activity was retained by all E2F1 mutants, except the K161R/164R mutant for which cIAP1 was completely inactive and the K185R whose basal transactivation activity was weakly enhanced by cIAP1 (XREF_FIG).|Here, we demonstrated that the E3-ubiquitin ligase cellular inhibitor of apoptosis 1 (cIAP1) increases E2F1 K63-poly-ubiquitination on the lysine residue 161/164 cluster, which is associated with the transcriptional factor stability and activity. | SIGNOR-278688 |
Q6PCD5 | P04637 | 1 | ubiquitination | up-regulates quantity by stabilization | 0.361 | RFWD3 is a positive regulator of p53 abundance and regulates the G1 checkpoint in response to IR. We found that an E3 ubiquitin ligase RFWD3 (RNF201/FLJ10520) forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and is required to stabilize p53 in the late response to DNA damage. | SIGNOR-271944 |
P12724 | P11678 | 0 | post translational modification | up-regulates activity | 0.477 | Human eosinophils are bone marrow-derived, non-dividing granulocytes of the innate immune system, which store the highly cationic proteins eosinophil peroxidase (EPO), major basic protein (MBP), eosinophil-derived neurotoxin (EDN), and eosinophil cationic protein (ECP) in secondary granules. we demonstrated that Tyr nitration of the eosinophil granule proteins is exclusively mediated by EPO, in the presence of functional NADPH oxidase and minute amounts of NOx. EPO appears to nitrate itself via an autocatalytic mechanism. | SIGNOR-261705 |
P78527 | P00519 | 1 | phosphorylation | up-regulates activity | 0.513 | We show that DNA-PK phosphorylates and activates c-Abl in vitro. | SIGNOR-279268 |
Q8TBB1 | Q96KB5 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.375 | We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo. | SIGNOR-272898 |
Q15910 | Q8NG27 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.488 | Biochemical and genetic evidence demonstrates that the MYOD-induced E3 ubiquitin ligase Praja1 (PJA1) is involved in regulating EZH2 levels upon p38α activation. EZH2 premature degradation in proliferating myoblasts is prevented by low levels of PJA1, its cytoplasmic localization and the lower activity towards unphosphorylated EZH2 | SIGNOR-255664 |
Q09013 | P11831 | 1 | phosphorylation | up-regulates | 0.289 | Myotonic dystrophy protein kinase (DMPK), a muscle- and neuron-restricted kinase, enhanced SRF-mediated promoter activity of the skeletal and cardiac alpha-actin genes in C2C12 myoblasts as well as in nonmyogenic cells. | Threonine 159 in the MADS box alphaI coil was a specific phosphorylation target in vitro as well as in vivo of both DMPK and protein kinase C-alpha. | SIGNOR-236982 |
Q07889 | P62993 | 0 | relocalization | up-regulates activity | 0.912 | Interaction domains of sos1/grb2 are finely tuned for cooperative control of embryonic stem cell fate. | SIGNOR-235773 |
P31749 | Q5UE93 | 1 | phosphorylation | up-regulates activity | 0.45 | P84 forms a negative regulatory complex with p110gamma to control PI3Kgamma signalling during cell migration|However, phosphorylation at this site was confirmed using an in vitro kinase assay in which Akt kinase was shown to readily phosphorylate Thr607 using a p84 peptide (Figure 1e), where Thr607 in conjunction with surrounding residues forms an Akt kinase consensus sequence|In contrast, although p84-T607A exhibited basal p110γ dimerisation, this interaction could not be further induced with stimulation | SIGNOR-275722 |
P61073 | Q86V86 | 0 | phosphorylation | up-regulates quantity | 0.263 | Pim-1 and Pim-3 enhance phosphorylation and cell surface expression of CXCR4.|The intracellular tail of CXCR4 can be phosphorylated in vitro at Ser339 by Pim-1 kinase and by Pim-3, as shown here, but not by Pim-2. | SIGNOR-279092 |
Q13546 | O00429 | 1 | phosphorylation | up-regulates activity | 0.51 | RIPK1 also activates DRP1 by phosphorylating DRP1 at Ser616 in a RIPK3-dependent fashion independent of MLKL. | SIGNOR-280104 |
P10070 | Q8N752 | 0 | phosphorylation | up-regulates | 0.333 | Gli2 is phosphorylated by gsk3 and ck1 for the fbxw11 (betatrcp2)-mediated degradation ci is phosphorylated by pka at multiple sites priming phosphorylation by both gsk3 and cki, leading to partial proteolysis. The pka, gsk3, and cki sites are conserved in gli2 and gli3, vertebrate homologs of ci that are similarly processed | SIGNOR-179972 |
P22626 | P01106 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.356 | We also demonstrate that the oncogenic transcription factor c-Myc upregulates transcription of PTB, hnRNPA1 and hnRNPA2, | SIGNOR-268691 |
P14635 | P30307 | 0 | dephosphorylation | up-regulates activity | 0.832 | Cdc25C is an activator of Cdc2 kinase and dephosphorylates and activates the CyclinB-Cdc2 complex shortly before the entry into the mitosis. | SIGNOR-277099 |
P00519 | P33981 | 0 | phosphorylation | down-regulates | 0.279 | Ttk phosphorylation of thr735 was associated with partial inhibition of nuclear targeting of c-abl. | SIGNOR-181064 |
P29375 | Q16665 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.273 | To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. | SIGNOR-271565 |
Q14469 | P17252 | 0 | phosphorylation | down-regulates activity | 0.329 | Endogenous HES-1 DNA-binding activity is post-translationally inhibited during NGF signaling in vivo, and phosphorylation of PKC consensus sites in the HES-1 DNA-binding domain inhibits DNA binding by purified HES-1 in vitro. | SIGNOR-248993 |
Q16566 | P09429 | 1 | phosphorylation | up-regulates activity | 0.285 | Collectively, our results demonstrate that CaMKIV promotes the nucleocytoplasmic shuttling of HMGB1 and suggest that the process may be mediated through CaMKIV-dependent serine phosphorylation of HMGB1. | SIGNOR-278510 |
P35222 | P48729 | 0 | phosphorylation | down-regulates | 0.791 | Specifically, ck1_ phosphorylates _-catenin at s45, which primes this n-terminal region for subsequent phosphorylations by gsk3 at t41, s37 and s33 [7]. These latter two phosphorylations are recognized by the e3-ligase component, _-trcp, for ultimate ubiquitylation and destruction by the proteosome | SIGNOR-165022 |
Q9UD71 | P49674 | 0 | phosphorylation | up-regulates activity | 0.322 | CKIepsilon phosphorylates and activates DARPP-32, a key molecule in various complex signaling pathways, including dopamine and glutamine signaling, which have both been demonstrated to be main pathways in substance dependence. | SIGNOR-279701 |
P15514 | P12931 | 0 | cleavage | up-regulates | 0.345 | Ep2 can also promote the transactivation of epidermal growth factor receptor (egfr) expressed in colon cancer cells through src, which activates the proteolytic release of the egfr ligands amphiregulin (ar) and transforming growth factor-alfa (tgfalfa)125, thereby stimulating the egfr- network. | SIGNOR-236537 |
P68363 | Q9BYW2 | 0 | methylation | up-regulates activity | 0.244 | The histone methyltransferase SET-domain-containing 2 (SETD2), which is responsible for H3 lysine 36 trimethylation (H3K36me3) of histones, also methylates α-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy | SIGNOR-269090 |
Q16620 | Q06124 | 0 | dephosphorylation | down-regulates activity | 0.707 | Conversely, PTPN11 knockdown lead to increased Y 515 phosphorylation of TrkB compared to the scramble control in the neuronal cells.|This study established that TrkB activation as demonstrated by receptor phosphorylation at Tyr 515 in the SH-SY5Y cells is negatively regulated by PTPN11 actions. | SIGNOR-277123 |
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