IdA string | IdB string | labels int64 | mechanism string | effect string | score float64 | sentence string | signor_id string |
|---|---|---|---|---|---|---|---|
O14757 | Q92934 | 1 | phosphorylation | down-regulates activity | 0.2 | Chkl binds and phosphorylates BAD protein.|Taken together, our results suggest that Chk1 may inactivate BAD by associating with and phosphorylating residues critical for BAD function in response to DNA damage. | SIGNOR-279159 |
P17252 | Q92686 | 1 | phosphorylation | up-regulates activity | 0.394 | Phosphorylation of RC3 by PKC alpha, beta, or gamma was stimulated by Ca2+, phospholipid, and diacylglycerol. A single site, Ser36, which is adjacent to the predicted calmodulin (CaM)-binding domain, was phosphorylated by these enzymes. Phosphorylation of RC3 by PKC or PKM, a protease-degraded PKC, was inhibited by CaM. The effect of CaM apparently targets at RC3, as phosphorylation of protamine sulfate by PKM was not inhibited by CaM. | SIGNOR-248913 |
P10636 | O60285 | 0 | phosphorylation | up-regulates quantity | 0.249 | These results confirm that the effect of Nuak1 over tau levels is mainly due to tau phosphorylation at Ser356 by Nuak1.|Western blot analysis revealed that a 50% reduction in Nuak1 was sufficient to decrease tau levels in the brain (XREF_FIG). | SIGNOR-279306 |
Q96J02 | P46531 | 1 | ubiquitination | down-regulates | 0.644 | Itch binds to the n-terminal portion of the notch intracellular domain via its ww domains and promotes ubiquitination of notch through its hect ubiquitin ligase domain. | SIGNOR-80702 |
Q9P0U3 | P31749 | 1 | desumoylation | down-regulates quantity by destabilization | 0.28 | Although multiple sites on Akt could be SUMOylated, K276 was identified as a major SUMO acceptor site. K276R or E278A mutation reduced SUMOylation of Akt but had little effect on its ubiquitination. Strikingly, these mutations also completely abolished Akt kinase activity. In support of these results, we found that expression of PIAS1 and SUMO1 increased Akt activity, whereas expression of SENP1 reduced Akt1 activity. | SIGNOR-252736 |
P23443 | O60346 | 0 | dephosphorylation | down-regulates activity | 0.572 | Here we report the identification of ribosomal protein S6 kinase 1 (S6K1) as a novel substrate of PHLPP. | SIGNOR-237454 |
P05129 | P48058 | 1 | phosphorylation | up-regulates | 0.702 | We found that pka phosphorylation of the ampa receptor subunits glur4 and glur1 directly controlled the synaptic incorporation of ampa receptors in organotypic slices from rat hippocampus. | SIGNOR-97558 |
Q15796 | Q9Y5K5 | 0 | deubiquitination | up-regulates | 0.378 | Here, we report a novel interaction between smads and ubiquitin c-terminal hydrolase uch37, a deubiquitinating enzyme that could potentially reverse smurf-mediated ubiquitination. In gst pull down experiments, uch37 bound weakly to smad2 and smad3, and bound very strongly to smad7 in a region that is distinct from the -py- motif in smad7 that interacts with smurf ubiquitin ligases | SIGNOR-138876 |
Q99704 | Q13882 | 0 | phosphorylation | down-regulates activity | 0.494 | BRK downregulates Dok1 via proteasomal degradation.|BRK phosphorylates Dok1 at tyrosine 362. | SIGNOR-278301 |
Q96PY5 | P17252 | 0 | phosphorylation | up-regulates activity | 0.2 | PKCα associates with and phosphorylates FMNL2 at S1072 within its Diaphanous autoregulatory region, leading to the release of formin autoinhibition. | SIGNOR-273796 |
P68400 | Q08945 | 1 | phosphorylation | down-regulates activity | 0.703 | CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity. | we identified serines 510, 657, and 688 as phosphorylation targets of CK2 in vitro. Mutagenesis of the three serines revealed that serine 510 was more important for the regulation of SSRP1 DNA-binding activity. | SIGNOR-250961 |
P18669 | Q13153 | 0 | phosphorylation | down-regulates | 0.2 | Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. | SIGNOR-91594 |
P30305 | Q14680 | 0 | phosphorylation | down-regulates activity | 0.533 | In the present study we show that the human pEg3 kinase is able to specifically phosphorylate CDC25B in vitro. One phosphorylation site was identified and corresponded to serine 323[Ä] Taken together these results suggest that pEg3 is a potential regulator of the G2/M progression and may act antagonistically to the CDC25B phosphatase | SIGNOR-255655 |
Q6UXI9 | Q5H8C1 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.366 | The loss of QBRICK significantly diminished the expression of nephronectin, an integrin α8β1 ligand necessary for renal development. In vivo, nephronectin associated with QBRICK and localized at the sublamina densa region, where QBRICK was also located. Collectively, these findings indicate that QBRICK facilitates the integrin α8β1-dependent interactions of cells with basement membranes by regulating the basement membrane assembly of nephronectin and explain why renal defects occur in Fraser syndrome. | SIGNOR-253308 |
P11717 | Q7Z6M1 | 0 | relocalization | up-regulates activity | 0.385 | P40 is a very potent transport factor in that the pure, recombinant protein can stimulate, significantly, an in vitro transport assay that measures transport of mannose 6-phosphate receptors from endosomes to the trans-Golgi network. The functional importance of p40 is confirmed by the finding that anti-p40 antibodies inhibit in vitro transport. Finally, p40 shows synergy with Rab9 in terms of its ability to stimulate mannose 6-phosphate receptor transport. These data are consistent with a model in which p40 and Rab9 act together to drive the process of transport vesicle docking. | SIGNOR-253090 |
Q8NBP7 | P36956 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.427 | Expression of nuclear forms of sterol-regulatory element binding protein-1 (SREBP-1) and SREBP-2 dramatically increased the promoter activity of PCSK9. | SIGNOR-255222 |
P05112 | O95644 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.549 | Recombinant NFAT1 can mediate transcription of the interleukin-2, interleukin-4, tumor necrosis factor alpha, and granulocyte-macrophage colony-stimulating factor promoters in T cells, suggesting that NFAT1 contributes to the CsA-sensitive transcription of these genes during the immune response. | SIGNOR-254498 |
Q6ZMU5 | P35568 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.477 | Here, we demonstrate that MG53 induces IRS-1 ubiquitination with the help of the E2 enzyme UBE2H during skeletal myogenesis by examining MG53 disrupted skeletal muscle cells and tissues.|The IRS-1 protein level was decreased by MG53 in a concentration dependent manner and was restored by the addition of MG132, a proteasome inhibitor (XREF_FIG; XREF_SUPPLEMENTARY). | SIGNOR-278520 |
Q00987 | P11309 | 0 | phosphorylation | up-regulates | 0.388 | Additionally, the pim kinases phosphorylate mdm2 in vitro and in cultured cells at ser166 and ser186, two previously identified targets of other signaling pathways, including akt. | SIGNOR-178619 |
Q02156 | Q8WV44 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.2 | RINCK induces the ubiquitination of PKC both in vitro and in cells. Overexpression of RINCK reduces the levels of PKC in cells, whereas genetic knockdown of endogenous RINCK increases the levels of PKC. The RINCK-mediated ubiquitination is likely to be polyubiquitination, because the ubiquitinated PKCβII was detected as a high molecular weight smear. | SIGNOR-271668 |
P37231 | P25874 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.533 | NFIA binds to and activates the brown-fat-specific enhancers even before differentiation and later facilitates the binding of PPARgamma|NFIA has at least three functions on the transcriptional regulation of brown fat [2]. First, NFIA activates adipogenesis per se, through activating the transcription of Pparg, which encodes PPARgamma. Second, NFIA also activates the brown-fat-specific gene expression (such as Ucp1 and Ppargc1a) independent of the degree of adipocyte differentiation, through facilitating the binding of PPARgamma to the brown-fat-specific enhancers. Third, NFIA represses myogenesis through suppression of myogenic transcription factors such as Myod1 as well as Myog, | SIGNOR-263985 |
Q15796 | P24941 | 0 | phosphorylation | down-regulates activity | 0.488 | Moreover, CDK2 is the predominant CDK that phosphorylates Smad2 on T8 in myeloma cells, leading to inhibition of Smad2-Smad4 association that precludes transcriptional regulation by Smad2.|Moreover, CDK2 is the predominant cyclin-dependent kinase that phosphorylates Smad2 on T8 in myeloma cells, leading to inhibition of Smad2-Smad4 association that precludes transcriptional regulation by Smad2. | SIGNOR-279678 |
Q86YT6 | P34925 | 1 | ubiquitination | down-regulates | 0.327 | We discovered that ryk both physically and functionally interacts with the e3 ubiquitin ligase mind bomb 1 (mib1).We Found that overexpressed ryk and mib1 colocalized and that the overexpression of mib1 leads to the loss of surface ryk expression. In addition, biochemical studies revealed that mib1 promotes the ubiquitination and degradation of ryk. Endogenous ryk and mib1 were required for the wnt-dependent activation of wnt/ctnnb1 signaling | SIGNOR-176282 |
P49841 | O43623 | 1 | phosphorylation | down-regulates activity | 0.423 | GSK3beta controls epithelial-mesenchymal transition and tumor metastasis by CHIP mediated degradation of Slug.|Phosphorylation of Slug by GSK3beta promotes CHIP binding and ubiquitin mediated proteolysis. | SIGNOR-279414 |
O00141 | P10636 | 1 | phosphorylation | down-regulates | 0.331 | Second, sgk1 indirectly depolymerized mts through the phosphorylation of tau at ser214 | SIGNOR-161288 |
Q14232 | P20042 | 1 | guanine nucleotide exchange factor | up-regulates activity | 0.78 | EIF2B converts the protein synthesis initiation factor 2 (eIF2) from an inactive GDP-bound form to an active eIF2-GTP complex owing to its guanine nucleotide exchange factor (GEF) activity. | SIGNOR-269129 |
O75955 | P12931 | 0 | phosphorylation | up-regulates activity | 0.335 | Taken together, we conclude that mitochondrial c-Src phosphorylates flotillin-1 at Tyr56 and Tyr149, and that these phosphorylations are required for its interaction with CxII and the prevention of ROS production. | SIGNOR-273805 |
Q16584 | Q02750 | 1 | phosphorylation | up-regulates activity | 0.335 | Here we report that MLK3 can phosphorylate and activate MEK-1 directly in vitro and also can induce MEK phosphorylation on its activation sites in vivo in COS-7 cells. | SIGNOR-280019 |
P53350 | P13693 | 1 | phosphorylation | down-regulates | 0.716 | Plk phosphorylates tctp on two serine residues. These results suggest that phosphorylation decreases the microtubule-stabilizing activity of tctp and promotes the increase in microtubule dynamics that occurs after metaphase | SIGNOR-91348 |
Q5H8C1 | Q6UXI9 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.366 | The loss of QBRICK significantly diminished the expression of nephronectin, an integrin α8β1 ligand necessary for renal development. In vivo, nephronectin associated with QBRICK and localized at the sublamina densa region, where QBRICK was also located. Collectively, these findings indicate that QBRICK facilitates the integrin α8β1-dependent interactions of cells with basement membranes by regulating the basement membrane assembly of nephronectin and explain why renal defects occur in Fraser syndrome. | SIGNOR-253308 |
P24752 | Q9P0J1 | 1 | acetylation | down-regulates activity | 0.34 | We previously reported that the mitochondrial fraction of FLT3 activates acetyl-CoA acetyltransferase ACAT1 in mitochondria via Y407 phosphorylation to acetylate and inhibit mitochondrial pyruvate dehydrogenase A (PDHA) and PDH phosphatase 1 (PDP1) | SIGNOR-267635 |
Q9UKT4 | P53350 | 0 | phosphorylation | down-regulates | 0.783 | We propose that the balance of evi5 and polo-like kinase activities determines the timely accumulation of emi1 and cyclin, ensuring mitotic fidelity. | SIGNOR-142949 |
Q02952 | P06493 | 0 | phosphorylation | up-regulates activity | 0.322 | Mass spectrometry, molecular, and cellular approaches show that CDK1/Cyclin B1 phosphorylates Gravin on threonine 766 to prime the recruitment of the polo-like kinase Plk1 at defined phases of mitosis. | SIGNOR-271839 |
O00141 | Q13164 | 0 | phosphorylation | up-regulates | 0.388 | Bmk1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinasebmk1 activates sgk by phosphorylation at serine 78. | SIGNOR-105728 |
P28482 | P10636 | 1 | phosphorylation | down-regulates activity | 0.566 | Using nanoelectrospray mass spectrometry, we have undertaken an extensive comparison of phosphorylation in vitro by several candidate tau kinases, namely, JNK, p38, ERK2, and glycogen synthase kinase 3beta (GSK3beta). Between 10 and 15 sites were identified for each kinase. The three MAP kinases phosphorylated Ser202 and Thr205 but not detectably Ser199, whereas conversely GSK3beta phosphorylated Ser199 but not detectably Ser202 or Thr205. Phosphorylated Ser404 was found with all of these kinases except JNK. The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser185, Thr245, Ser305, and Ser356, whereas ERK2 was the most strict. All of the sites detected except Thr245 and Ser305 are known or suspected phosphorylation sites in paired helical filament-tau extracted from Alzheimer brains. Thus, the three MAP kinases and GSK3beta are importantly all strong candidates as tau kinases that may be involved in the pathogenic hyperphosphorylation of tau in Alzheimer's disease. | SIGNOR-249416 |
P53779 | Q5JR12 | 1 | phosphorylation | down-regulates | 0.2 | Specific phosphorylation of pp2czeta at ser (92) by stress-activated jnk attenuates its phosphatase activity in cells. | SIGNOR-178926 |
Q08345 | Q06124 | 1 | relocalization | up-regulates activity | 0.373 | Overexpression of DDR1a/b increased the interaction of DDR1 with SHP-2 and up-regulated the tyrosine phosphatase activity of SHP-2. | SIGNOR-272403 |
O00257 | O60315 | 1 | sumoylation | down-regulates quantity by destabilization | 0.331 | Pc2 can act directly as an E3 ligase for SIP1 sumoylation.SIP1 sumoylation having a negative effect on its repression of E-cadherin transcription. | SIGNOR-268955 |
Q15208 | Q9UBF8 | 1 | phosphorylation | up-regulates activity | 0.267 | We identified 5 potential NDR1 substrates in the mouse brain and chose two for functional validation. We show that one NDR1 substrate is another kinase, AP-2 associated kinase-1 (AAK1) which regulates dendritic branching as a result of NDR1 phosphorylation. Another substrate is the Rab8 guanine nucleotide exchange factor (GEF) Rabin8 (a Sec2p homolog) which we find is involved in spine synapse formation. | SIGNOR-263033 |
Q96GD4 | Q9UPY8 | 1 | phosphorylation | up-regulates | 0.472 | Phosphorylation of eb3 at s176 by aurora b ensures successful cytokinesis completion by promoting midbody mt stability and midbody stabilization. | SIGNOR-202130 |
P27361 | P08047 | 1 | phosphorylation | up-regulates | 0.653 | We showed that perifosine activates the mitogen-activated protein/extracellular signal-regulated kinase pathway, and this activation promotes the phosphorylation of sp1 in known mitogen-activated protein kinase residues (threonine 453 and 739), thereby leading to increased sp1 binding and enhanced p21(waf1/cip1) transcription. | SIGNOR-248062 |
Q8N122 | P53350 | 0 | phosphorylation | up-regulates activity | 0.329 | Of note, MYC-PLK1 (WT) overexpression strongly enhanced MTOR and RPTOR signals in PLK1 IPs, whereas the LAMP2 signal was strongly decreased (XREF_FIG).|Thus, we conclude that PLK1 can directly phosphorylate RPTOR in vitro. | SIGNOR-279346 |
P27361 | P46527 | 1 | phosphorylation | down-regulates | 0.376 | These data suggest that increased signaling by erbb receptors up-regulates mapk activity, which, in turn, phosphorylates and destabilizes p27, thus contributing to dysregulated cell cycle progression. | SIGNOR-80234 |
Q2M3R5 | Q8IXL6 | 0 | phosphorylation | up-regulates activity | 0.2 | Notably, phosphorylation of Stim1 by Fam20C enhances Stim1 activation and store-operated Ca 2+ entry.|We feel that the western blot shows an appropriate range of contrast to support the conclusion that Stim1 can be activated by Fam20C under high calcium conditions. | SIGNOR-280012 |
P03372 | Q16539 | 0 | phosphorylation | up-regulates | 0.625 | Conversely, constitutively active mkk6 induced p38 mapk activation that recapitulated the effects of polyphenols by inducing eralpha phosphorylation and downstream activation of akt, and enos. The key role of eralpha ser-118 phosphorylation was confirmed in enos-transfected cos-7 cells | SIGNOR-136950 |
Q06210 | Q9UQM7 | 0 | phosphorylation | up-regulates | 0.2 | Amp-activated protein kinase and calcium/calmodulin-dependent kinase ii were identified to phosphorylate specifically ser243 in vitro. Phosphorylation by these two kinases results in an increase of enzymatic activity by 1.4-fold. These findings suggest for the first time that hgfat1 may be regulated by kinases other than pka. | SIGNOR-158486 |
O75385 | Q9Y4K3 | 0 | ubiquitination | up-regulates quantity by stabilization | 0.548 | AMBRA1, interacting with the E3-ligase TRAF6, supports ULK1 ubiquitylation by LYS-63-linked chains, and its subsequent stabilization, self-association and function. | SIGNOR-273000 |
Q9Y2Z4 | Q2TAL8 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.2 | QRICH1 promotes the expression of translation-related genes. our combined ChIP-seq and RNA-seq analyses identified that QRICH1 and ATF4 were enriched at the promoters of these specific tRNA synthetases, and that ER stress positively regulated their transcription (Fig. 4I). Together, these findings suggest that QRICH1 and ATF4 modulate tRNA metabolic processes to promote secreted protein synthesis during ER stress. | SIGNOR-269413 |
P08069 | Q00987 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.66 | We could prove that Mdm2 physically associates with IGF-1R and that Mdm2 causes IGF-1R ubiquitination in an in vitro assay. | SIGNOR-278571 |
P49959 | P53350 | 0 | phosphorylation | down-regulates activity | 0.2 | Plk1 phosphorylates Mre11 at S649.Mre11 phosphorylation at S649/S688 inhibits its binding to dsDNA and antagonizes the ATM signaling. | SIGNOR-265943 |
P16403 | O76064 | 0 | polyubiquitination | down-regulates | 0.2 | ITCH interacts with and ubiquitinates linker histone H1.2 at K46. ITCH biochemically competes with RNF168 and RNF8 to polyubiquitinate histone H1.2. | SIGNOR-272928 |
O75385 | P62820 | 0 | relocalization | up-regulates activity | 0.532 | 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-261299 |
P48729 | P11308 | 1 | phosphorylation | down-regulates quantity by destabilization | 0.2 | Using in vitro kinase assays, we further demonstrated that deletion of degron 1 largely abolished CKI-mediated phosphorylation of ERG (Figure S5B), indicating that serine residues within degron 1 are the major CKI phosphorylation sites. | SIGNOR-276935 |
P78536 | P15514 | 1 | cleavage | up-regulates activity | 0.448 | ADAM17 is involved in the release and activation of several growth factors and cytokine receptor ligands. Among the growth factors activated by ADAM17 are TGF-alpha, amphiregulin, epiregulin and HB-EGF | SIGNOR-259842 |
P0CG48 | P09936 | 0 | cleavage | up-regulates quantity | 0.864 | These data suggest that the physiological role of UCH is to hydrolyze small adducts of ubiquitin and to generate free monomeric ubiquitin from ubiquitin proproteins, but not to deubiquitinate ubiquitin-protein conjugates or disassemble polyubiquitin chains | SIGNOR-249693 |
P17252 | Q05586 | 1 | phosphorylation | up-regulates activity | 0.417 | Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms. The results show that PKC alpha phosphorylates preferentially S896 and PKC gamma preferentially S890. | SIGNOR-263177 |
P49841 | P12830 | 1 | phosphorylation | up-regulates activity | 0.558 | Phosphorylation of the E-cadherin Cytoplasmic Domain by CKII and GSK-3β Increases the Binding to β-catenin. pre-phosphorylation by CKII at Ser-855 and/or Ser-853 of E-cadherin is required before GSK-3β can phosphorylate at Ser-849. | SIGNOR-251225 |
P17948 | P63096 | 1 | phosphorylation | up-regulates activity | 0.257 | RTKs directly phosphorylate Gαi on Y154, 155, and Y320. | SIGNOR-277230 |
Q04759 | Q9BXL7 | 1 | phosphorylation | up-regulates activity | 0.775 | NF-kappaB activation is triggered by PKCteta-dependent phosphorylation of Carma1 after TCR/CD28 co-stimulation. PKCteta-phosphorylated Carma1 was suggested to function as a molecular scaffold that recruits preassembled Bcl10-Malt1 complexes to the membrane|we demonstrate that PP2A removes PKCteta-dependent phosphorylation of Ser645 in Carma1, and show that maintenance of this phosphorylation is correlated with increased T-cell activation. | SIGNOR-249193 |
Q9HCE7 | Q5VWQ8 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.262 | DAB2IP protein levels can be negatively regulated by the activity of the E3-ubiquitin ligases Fbw7, Skp2, and Smurf1 | SIGNOR-254776 |
Q14938 | A8MYZ6 | 1 | transcriptional regulation | down-regulates quantity | 0.2 | By integrating transcriptomic profiling (RNA-seq) of Nfia- and Nfix-deficient GNPs with epigenomic profiling (ChIP-seq against NFIA, NFIB and NFIX, and DNase I hypersensitivity assays), we reveal that these transcription factors share a large set of potential transcriptional targets, suggestive of complementary roles for these NFI family members in promoting neural development | SIGNOR-268887 |
Q92900 | P31749 | 0 | phosphorylation | up-regulates activity | 0.257 | AKT-Mediated UPF1 Phosphorylation at T151 Promotes UPF1 Helicase Activity | SIGNOR-277597 |
P31249 | P08648 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.25 | The homeobox transcription factor Hox D3 promotes integrin alpha5beta1 expression and function during angiogenesis. | SIGNOR-261649 |
P12931 | Q14118 | 1 | phosphorylation | down-regulates | 0.55 | Tyrosine 892 is now thought to be the principal site for recognition by the c-src tyrosine kinase;. We show that upon tyrosine phosphorylation, beta-dystroglycan undergoes a profound change in its sub-cellular localization (e.g., from the plasma membrane to an internal membrane compartment). One possibility is that the net negative charge at position 892 causes the redistribution of beta-dystroglycan to this intracellular vesicular location | SIGNOR-101655 |
Q9H422 | Q13158 | 1 | phosphorylation | down-regulates activity | 0.436 | FIST/HIPK3 causes FADD phosphorylation, thereby promoting FIST/HIPK3-FADD-Fas interaction.  Phosphorylation occurs on Ser194 close to the COOH terminus of human FADD| Fas ligand-induced activation of Jun NH(2)-terminal kinase is impaired by overexpressed active FIST/HIPK3 | SIGNOR-251272 |
O15151 | Q93009 | 0 | deubiquitination | up-regulates | 0.757 | Subsequently, hausp was shown to deubiquitinate mdm2 and mdmx, thereby stabilizing these proteins. | SIGNOR-139453 |
Q01484 | O00533 | 0 | relocalization | up-regulates quantity | 0.409 | Neurofascin, L1, NrCAM, NgCAM, and neuroglian are membrane-spanning cell adhesion molecules with conserved cytoplasmic domains that are believed to play important roles in development of the nervous system. This report presents biochemical evidence that the cytoplasmic domains of these molecules associate directly with ankyrins, a family of spectrin-binding proteins located on the cytoplasmic surface of specialized plasma membrane domains. | SIGNOR-266722 |
P17252 | P27987 | 1 | null | down-regulates activity | 0.359 | However, when assayed in the presence of calcium/calmodulin, the activity of the B isoform was decreased following phosphorylation by either protein kinase. | SIGNOR-248990 |
P12931 | O60716 | 1 | phosphorylation | up-regulates activity | 0.922 | Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 | SIGNOR-246484 |
Q9NZV8 | P78411 | 0 | transcriptional regulation | down-regulates quantity by repression | 0.487 | Irx5 Directly Represses the Kcnd2 Promoter | SIGNOR-266045 |
P56524 | Q13950 | 1 | deacetylation | down-regulates activity | 0.524 | HDAC4 and HDAC5 deacetylate Runx2, allowing the protein to undergo Smurf-mediated degradation | SIGNOR-227547 |
P49815 | Q13131 | 0 | phosphorylation | up-regulates activity | 0.682 | However, AMP-activated protein kinase (AMPK), an essential cellular energy sensor, phosphorylates and activates TSC2 [ xref ]. | SIGNOR-278981 |
Q86UE8 | Q9Y294 | 1 | phosphorylation | up-regulates quantity by stabilization | 0.668 | We found that only S192A in hASF1a and S198A in hASF1b significantly affected phosphorylation by hTLK2 | Consistent | SIGNOR-260787 |
O14746 | P00519 | 0 | phosphorylation | down-regulates activity | 0.66 | These findings indicate that phosphorylation of hTERT by c-Abl is associated with inhibition of telomerase activity.|We also found that c-Abl phosphorylates hTERT and inhibits hTERT activity. | SIGNOR-279354 |
Q9ULW0 | O14965 | 0 | phosphorylation | up-regulates activity | 0.965 | Here we show that TPX2, a microtubule-bundling protein and activator of Aurora A, plays an important role. TPX2 was phosphorylated by Aurora A during mitosis. Its phospho-null mutant caused short metaphase spindles coupled with low microtubule flux rate. Interestingly, phosphorylation of TPX2 regulated its interaction with CLASP1 but not Kif2a.|This suggests that TPX2 phosphorylation positively regulates the function of CLASP1.| This is in accord with a phosphoproteomics study that identified S121 and S125 as potential phosphorylation sites for Aurora A in mitotic HeLa cells | SIGNOR-265089 |
P45984 | Q14934 | 1 | phosphorylation | up-regulates activity | 0.419 | Here, we showed that the nuclear factor of activated T3 (NFAT3) is phosphorylated by JNK1 or JNK2 at Ser(213) and Ser(217), which are located in the conserved SP motif.|Moreover, a 3xNFAT-luc reporter gene assay indicated that NFAT3 transcriptional activity was increased in a dose-dependent manner by JNK1 or JNK2. | SIGNOR-280036 |
P27361 | O75582 | 1 | phosphorylation | up-regulates | 0.585 | In the present study, we show that, in addition to being phosphorylated on thr-581 and ser-360 by erk1/2 or p38, msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. | SIGNOR-131379 |
P01579 | Q9UL17 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.475 | T-bet Transactivates the IFNγ Gene and Represses the IL-2 Gene in EL4 Cells | SIGNOR-266234 |
Q04206 | Q9Y6K9 | 0 | phosphorylation | up-regulates activity | 0.862 | Chromatographic fractionation of cell extracts allowed the identification of two distinct enzymatic activities phosphorylating ser-536. Peak 1 represents an unknown kinase, whereas peak 2 contained ikkalpha, ikkbeta, ikkepsilon, and tbk1. collectively, our results provide evidence for at least five kinases that converge on ser-536 of p65 and a novel function for this phosphorylation site in the recruitment of components of the basal transcriptional machinery to the interleukin-8 promoter. | SIGNOR-129947 |
P04637 | Q9H2X6 | 0 | phosphorylation | up-regulates | 0.797 | Based on all these observations, it is legitimate to suggest that axin and daxx seem to adopt both parallel routes and a convergent means to activate p53. In either case, hipk2 seems to be the protein kinase that catalyzes the ser46 phosphorylation. | SIGNOR-151930 |
P52945 | Q13043 | 0 | phosphorylation | down-regulates activity | 0.2 | MST1 directly phosphorylated PDX1 at Thr11, resulting in its ubiquitination, degradation and impaired insulin secretion.|Thus, kinase activity is required for MST1 induced PDX1 degradation. | SIGNOR-278303 |
P51608 | Q13224 | 1 | transcriptional regulation | down-regulates quantity by repression | 0.35 | The interaction of MeCP2 with the 2BI3 and 2BI5 sites was strikingly reduced in neurons maintained in the presence of TTX (Fig. 2C). This result is consistent with the classical view of MeCP2 as a general transcriptional repressor, in that the reduced association leads to increased expression of NR2B. | SIGNOR-264685 |
P35637 | P00533 | 0 | phosphorylation | up-regulates activity | 0.259 | Thus, EGFR appears to mediate FUS nuclear translocation by phosphorylating Y6 and Y296 in FUS. | SIGNOR-279168 |
Q14938 | Q13562 | 1 | transcriptional regulation | up-regulates quantity | 0.265 | 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-268904 |
P24588 | P17612 | 1 | relocalization | up-regulates activity | 0.561 | In this report, we demonstrate that glutamate receptors and PKA are recruited into a macromolecular signaling complex through direct interaction between the MAGUK proteins, PSD-95 and SAP97, and AKAP79/150 | SIGNOR-261292 |
P29323 | Q13224 | 1 | phosphorylation | up-regulates quantity | 0.443 | In addition, EPHB2 signaling leads to phosphorylation of GluN2B at tyrosine residue 1472 preventing clathrin dependent endocytosis, and increasing the surface retention of GluN2B containing NMDARs. | SIGNOR-279710 |
Q92833 | P15173 | 1 | transcriptional regulation | down-regulates quantity by repression | 0.2 | JARID2 is a direct target of the PAX3-FOXO1 fusion protein and inhibits myogenic differentiation of rhabdomyosarcoma cells|Addition of Differentiation Media (DM) to human myoblasts was associated with the induction of MYOG, MYOD and MYL1 and a decrease in JARID2 RNA expression|Furthermore, we that showed JARID2 binds to and alters the methylation status of histone H3 lysine 27 in the promoter regions of MYOG and MYL1 and that the interaction of JARID2 at these promoters is dependent upon EED, a core component of the Polycomb Repressive Complex 2 (PRC2). Therefore JARID2 is a downstream effector of PAX3-FOXO1 that maintains an undifferentiated myogenic phenotype that is characteristic of RMS | SIGNOR-249599 |
Q15831 | Q05513 | 0 | phosphorylation | up-regulates | 0.321 | Here, we have identified s307 as a novel phosphorylation site in lkb1 and provide evidence that, in multiple cell types, phosphorylation of this site by protein kinase c ? (pkc-?) Induces nucleocytoplasmic transport of lkb1. | SIGNOR-185640 |
Q96FW1 | P03372 | 1 | deubiquitination | down-regulates activity | 0.546 | OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity.|We show that OTUB1 negatively regulates transcription mediated by ERalpha in transient reporter gene assays and transcription mediated by endogenous ERalpha in Ishikawa endometrial cancer cells. | SIGNOR-276529 |
Q13586 | Q13131 | 0 | phosphorylation | down-regulates activity | 0.2 | STIM1 is a novel exercise‐regulated AMPK substrate. Phosphorylation of STIM1 by AMPK suppresses SOCE | SIGNOR-277299 |
P49815 | P31749 | 0 | phosphorylation | down-regulates activity | 0.817 | We demonstrate that, upon activation of PI3K, tuberin is phosphorylated on consensus recognition sites for PI3K-dependent S/T kinases. Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo. We also show that S939 and T1462 of tuberin are PI3K-regulated phosphorylation sites and that T1462 is constitutively phosphorylated in PTEN(-/-) tumor-derived cell lines. | SIGNOR-235515 |
Q96N16 | P33176 | 0 | relocalization | up-regulates activity | 0.2 | Marlin-1 is associated with kinesin-I and suggest that the movement of Marlin-1 is mediated by plus end microtubuledependent molecular motors | SIGNOR-260989 |
Q8IUC6 | Q9Y4K3 | 0 | polyubiquitination | up-regulates | 0.83 | Here, we show that the TRAF family proteins directly bind TICAM-1 and demonstrate that TRAF2 and TRAF6 bind different sites of the N-terminal TICAM-1 and accelerate its polyubiquitination. we speculate that polyubiquitination of TICAM-1 by TRAF2 and TRAF6 is required for TICAM-1 to induce IRF-3 and NF-κB activation. This is supported by the observation that polyubiquitination of TICAM-1 was required for TRAF3-binding to TICAM-1 | SIGNOR-271428 |
Q9UM73 | P23471 | 0 | dephosphorylation | down-regulates | 0.545 | Rptpbeta/zeta dephosphorylates alk at the site(s) in alk that is undergoing autophosphorylation through autoactivation. | SIGNOR-157227 |
P19532 | Q00534 | 0 | phosphorylation | up-regulates activity | 0.2 | CDK4 and CDK6 interact with TFEB and TFE3 in the nucleus We next investigated how CDK4 and CDK6 activate TFEB and TFE3 .|CDK4 and CDK6 phosphorylate TFEB and TFE3. | SIGNOR-279517 |
P00519 | P12931 | 0 | phosphorylation | up-regulates activity | 0.538 | c-Src-induced c-Abl activation involves phosphorylation of Y245 and Y412, two residues required for c-Abl mitogenic function. | SIGNOR-246311 |
Q6U7Q0 | Q01860 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.2 | Chromatin immunoprecipitation (ChIP) and dual-luciferase reporter assays revealed that Zfp322a binds to Pou5f1 and Nanog promoters and regulates their transcription. | SIGNOR-264900 |
P17542 | Q9UNE7 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.356 | Ubiquitination and degradation of Tal1/SCL are induced by notch signaling and depend on Skp2 and CHIP. CHIP promoted Tal1 degradation with both chaperone binding and ubiquitin ligase activities, which are mediated by its TPR domain and U box, respectively. | SIGNOR-271393 |
Q15067 | Q2T9J0 | 0 | cleavage | up-regulates activity | 0.694 | Here, we demonstrate that Tysnd1, a previously uncharacterized protein, is responsible both for the removal of the leader peptide from PTS2 proteins and for the specific processing of PTS1 proteins. All of the identified Tysnd1 substrates catalyze peroxisomal β-oxidation. In vitro cleavage of Acox1, Scp2 and prethiolase by recombinant Tysnd1. | SIGNOR-261057 |
Q9H257 | P68400 | 0 | phosphorylation | down-regulates activity | 0.346 | PVHL Acts as an Adaptor to Promote the Inhibitory Phosphorylation of the NF-κB Agonist Card9 by CK2 | SIGNOR-257601 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.