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 |
|---|---|---|---|---|---|---|---|
Q03468 | Q96FI4 | 1 | binding | up-regulates activity | 0.344 | CSB stimulates NEIL1 incision activity in vitro, and CSB and NEIL1 co-immunoprecipitate and co-localize in HeLa cells. | SIGNOR-251931 |
Q05655 | P61978 | 1 | phosphorylation | down-regulates | 0.344 | Ser302 is a major k protein site phosphorylated by pkcdelta in vitrothe ability of pkc_ to inducibly bind and phosphorylate k protein may serve not only to alter the activity of k protein itself, but k protein may also provide an avenue for pkc_ to engage in a cross-talk with other k protein molecular partners in response to specific changes in the extracellular environment | SIGNOR-67515 |
Q9UKA1 | Q9BQ15 | 1 | binding | down-regulates quantity by destabilization | 0.344 | Here, we report that hSSB1 is the bona fide substrate for an Fbxl5-containing SCF (Skp1-Cul1-F box) E3 ligase. Fbxl5 interacts with and targets hSSB1 for ubiquitination and degradation, which could be prevented by ATM-mediated hSSB1 T117 phosphorylation. | SIGNOR-271655 |
P53350 | Q9Y5T5 | 1 | phosphorylation | up-regulates activity | 0.344 | Plk1 phosphorylates and activates Usp16. In vitro phosphorylation of Usp16 with single (S330A, S386A, or S486A) or collective 3A (S330A/S386A/S486A) mutation showed that Plk1 phosphorylated Usp16 at all three sites (Fig. S2 D). | SIGNOR-274015 |
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 |
Q9Y613 | P60709 | 1 | binding | up-regulates quantity by stabilization | 0.344 | Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation | SIGNOR-276613 |
P78368 | Q13330 | 1 | phosphorylation | up-regulates activity | 0.344 | CKI-gamma2 could further potentiate the ER corepressive function of metastasis-associated protein-1 short form.|These findings identified metastasis-associated protein-1 short form as a target of CKI-gamma2, and provided new evidence to suggest that CKI-gamma2 phosphorylates and modulates the functions of metastasis-associated protein-1 short form, and that these extranuclear effects of estrogen might have important implications in regulating the functions of metastasis-associated protein-1 short form in human mammary epithelial and cancer cells. | SIGNOR-280236 |
P68400 | Q13351 | 1 | phosphorylation | up-regulates activity | 0.344 | Regulation of erythroid Krppel-like factor (EKLF) transcriptional activity by phosphorylation of a protein kinase casein kinase II site within its interaction domain. the transactivation capability of EKLF is augmented by co-transfection of CKIIalpha. in vitro assays demonstrate that CKIIalpha interacts with EKLF, and that the EKLF interaction domain is phosphorylated by CKII only at Thr-41 | SIGNOR-241361 |
O14672 | P04626 | 1 | cleavage | up-regulates activity | 0.344 | The ADAM proteases are best known for their role in shedding the extracellular domain of transmembrane proteins. Among the transmembrane proteins shed by ADAM10 are notch, HER2, E-cadherin, CD44, L1 and the EGFR ligands, EGF and betacellulin. | SIGNOR-259845 |
P50406 | P50148 | 1 | binding | up-regulates activity | 0.344 | Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. | SIGNOR-257340 |
P11940 | Q12986 | 2 | binding | up-regulates activity | 0.344 | We identifiednew protein partners of NFX1-123, including several cytoplasmic poly(A) binding proteins (PABPCs) thatinteracted with NFX1-123 through its N-terminal PAM2 motif. Central to our findings were our observations that PABPCs copurify with NFX1-123, that a PAM2 motif is present in NFX1, and this motif and the PABPCs are important in the enhancement of hTERT activity by NFX1-123. | SIGNOR-261052 |
Q9NPG1 | P61586 | 1 | binding | up-regulates activity | 0.344 | Upon ligand binding, non-canonical wnt signaling controls tissue polarity and cell movement through the activation of rhoa, c-jun n-terminal kinase (jnk), and nemo-like kinase (nlk) signaling cascades. | SIGNOR-167865 |
P51610 | Q13105 | 1 | binding | down-regulates activity | 0.344 | We show here that HCF-1 directly binds to the Myc-interacting protein Miz-1. HCF-1 Represses Gal4-Miz-1-mediated Transcriptional Activation | SIGNOR-223590 |
P23467 | P06213 | 1 | dephosphorylation | down-regulates | 0.344 | Identification of tyrosine phosphatases that dephosphorylate the insulin receptor. | SIGNOR-75997 |
P68400 | P09629 | 1 | phosphorylation | down-regulates activity | 0.344 | Thus, we concluded that CKII can phosphorylate HOXB7 in vitro and that this phosphorylation occurs at both of the CKII target sites, S133 and T204. | Wild-type HOXB7 inhibited the differentiation of 32D cells, whereas mutations in the Pbx-binding pentapeptide motif or the DNA-binding homeodomain, as well as internal deletions of the N-terminal unique region, blocked this effect. Interestingly, mutations eliminating two target sites for casein kinase II, the glutamate-rich C terminus, or the first 14 amino acids of HOXB7, led to enhanced 32D differentiation. | SIGNOR-250896 |
Q05209 | Q14161 | 1 | dephosphorylation | down-regulates | 0.344 | Conversely, a gfp-pkl phosphorylation mutant, y286/392/592f (gfp-pkl triple yf) (brown et al., 2005), was not phosphorylated during adhesion and the addition of ptp-pest had no effect, suggesting one or more of these tyrosine residues are dephosphorylated by ptppest. Taken together, these data strongly suggest pkl as a direct substrate for ptp-pest. | SIGNOR-142719 |
P00519 | P40692 | 1 | phosphorylation | up-regulates quantity by stabilization | 0.344 | We also observed phosphorylation of MLH1 by ABL1 in an in vitro kinase assay with purified recombinant ABL1 and MLH1, confirming there is a direct phosphorylation between ABL1 and the MLH1 component of the MLH1-PMS2 heterodimer.|we propose that ABL1 prevents MLH1 from being targeted for degradation by the chaperone Hsp70 and that in the absence of ABL1 activity at least a portion of MLH1 is degraded. | SIGNOR-279581 |
O00141 | P15056 | 1 | phosphorylation | down-regulates activity | 0.344 | Serum- and glucocorticoid-inducible kinase SGK phosphorylates and negatively regulates B-Raf.|We observed that SGK inhibits B-Raf activity. | SIGNOR-279110 |
P06493 | Q14807 | 1 | phosphorylation | up-regulates activity | 0.344 | Cdc2-mediated phosphorylation of kid controls its distribution to spindle and chromosomes. We identify ser427 and thr463 as m phase-specific phosphorylation sites and cdc2-cyclin b as a thr463 kinase. Kid with a thr463 to alanine mutation fails to be localized on chromosomes and is only detected along spindles, although it retains the ability to bind dna or chromosomes | SIGNOR-100964 |
O00192 | P33151 | 1 | binding | up-regulates quantity by stabilization | 0.344 | To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. | SIGNOR-252129 |
Q7KZI7 | Q8WUI4 | 1 | phosphorylation | down-regulates | 0.344 | We further show that emk and c-tak1 phosphorylate class iia hdacs on one of their multiple 14-3-3 binding sites and alter their subcellular localization and repressive function | SIGNOR-149583 |
P68400 | P35638 | 1 | phosphorylation | down-regulates activity | 0.344 | CHOP transcription factor phosphorylation by casein kinase 2 inhibits transcriptional activation. | The serine to alanine substituted site CHOP mutant was not phosphorylated by CK2, indicating that serines 14–15 and 30–31 of CHOP are the CK2 phosphoacceptor sites | SIGNOR-250850 |
Q12986 | P11940 | 2 | binding | up-regulates activity | 0.344 | NFX1-123 augments the activation of hTERT expression through interactions with PABPCs | SIGNOR-226011 |
O00311 | Q99459 | 1 | phosphorylation | down-regulates activity | 0.344 | During SPOC, Dbf4 binds to Cdc5 and promotes Cdc7-mediated phosphorylation of Cdc5, which then presumably prevents Cdc5 from recognizing its substrates in the MEN pathway . | SIGNOR-280203 |
Q9H0H3 | P53396 | 1 | binding | down-regulates quantity by destabilization | 0.344 | Here, we found that CUL3 interacts with ACLY through its adaptor protein, KLHL25 (Kelch-like family member 25), to ubiquitinate and degrade ACLY in cells. | SIGNOR-272333 |
Q5T0W9 | P48729 | 1 | binding | up-regulates quantity | 0.344 | We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or required for the association of CK1 with FAM83 proteins. Our findings imply that the DUF1669 domains of FAM83 proteins anchor CK1 α, α-like, δ, and ε isoforms in specific subcellular compartments and potentially mediate their association with substrates. | SIGNOR-273746 |
P23443 | O94763 | 1 | phosphorylation | down-regulates activity | 0.344 | Here we report that the prefoldin chaperone URI represents a mitochondrial substrate of S6K1. In growth factor-deprived or rapamycin-treated cells, URI forms stable complexes with protein phosphatase (PP)1gamma at mitochondria, thereby inhibiting the activity of the bound enzyme. Growth factor stimulation induces disassembly of URI/PP1gamma complexes through S6K1-mediated phosphorylation of URI at serine 371. | SIGNOR-262943 |
Q14833 | P63092 | 1 | binding | up-regulates activity | 0.344 | MGluRs are members of the G-protein-coupled receptor (GPCR) superfamily, the most abundant receptor gene family in the human genome. GPCRs are membrane-bound proteins that are activated by extracellular ligands such as light, peptides, and neurotransmitters, and transduce intracellular signals via interactions with G proteins. The resulting change in conformation of the GPCR induced by ligand binding activates the G protein, which is composed of a heterotrimeric complex of α, β, and γ subunits. | SIGNOR-264082 |
P27216 | P46934 | 1 | relocalization | up-regulates quantity | 0.344 | Annexin XIII has two known isoforms, a and b, that are apically localized, although XIIIa is also found in the basolateral compartment. In vitro binding and coprecipitation experiments showed that the Nedd4-C2 domain interacts with both annexin XIIIa and b in the presence of Ca2+, and the interaction is direct and optimal at 1 μM Ca2+.These results suggest that the apical membrane localization of Nedd4 is mediated by an association of its C2 domain with the apically targeted annexin XIIIb. | SIGNOR-272571 |
Q13043 | Q96EB6 | 1 | phosphorylation | down-regulates activity | 0.344 | We found that MST1 increases p53 acetylation and transactivation by inhibiting the deacetylation of Sirtuin 1 (Sirt1) and its interaction with p53 and that Sirt1 can be phosphorylated by MST1 leading to the inhibition of Sirt1 activity. | SIGNOR-279574 |
Q9Y4K3 | P01106 | 1 | ubiquitination | down-regulates activity | 0.344 | We posited that TRAF6 ubiquitination of MYC at K148 prevents its acetylation, which results in diminished MYC activity ( xref ). | SIGNOR-278563 |
P62877 | P03372 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.344 | I3C-dependent activation of the aryl hydrocarbon receptor (AhR) initiates Rbx-1 E3 ligase-mediated ubiquitination and proteasomal degradation of ERalpha protein. | SIGNOR-271434 |
P17252 | Q13976 | 1 | phosphorylation | up-regulates | 0.344 | Antibodies generated against phosphorylated threonine 58 were used to demonstrate phosphorylation in response to pma treatment of the cells with kinetics similar to vasodilator-stimulated phosphoprotein phosphorylation. A phospho-mimetic mutation at this site (t58e) generated a partially activated pkg that was more sensitive to cgmp levels. A phospho- mutation (t58a) revealed that this residue is important but not sufficient for pkg activation by pkc. | SIGNOR-98803 |
Q9H0B6 | Q9BQS8 | 1 | binding | up-regulates activity | 0.344 | Interestingly, bead capture assays indicated that the middle part of FYCO1 (residues 585–1233) interacts directly with the KLC2 light chain of kinesin 1 (Fig. 3a and Extended Data Fig. 7a, b). Residues 735–773 of FYCO1 were found to be necessary for its kinesin-1 binding (Fig. 3c and Extended Data Fig. 7b, c), and FYCO1(Δ735–773)-positive LEs failed to translocate to the cell periphery (Extended Data Fig. 7e). | SIGNOR-260599 |
P06241 | Q04759 | 1 | phosphorylation | up-regulates | 0.344 | Further indications of direct interaction are that p59fyn potentiates ?PKC Catalytic activity and that ?PKC Is a substrate for tyrosine phosphorylation by p59fyn. | SIGNOR-68798 |
P19474 | Q9C035 | 1 | monoubiquitination | up-regulates quantity | 0.344 | Here, we show that TRIM5alpha functions as a RING-finger-type E3 ubiquitin ligase both in vitro and in vivo and ubiquitinates itself in cooperation with the E2 ubiquitin-conjugating enzyme UbcH5B. Thus, the ubiquitination of TRIM5alpha is catalyzed by itself and Ro52. Unexpectedly, although TRIM5alpha is ubiquitinated, our results have revealed that the proteasome inhibitors MG115 and MG132 do not stabilize it in HeLa cells, suggesting that the ubiquitination of TRIM5alpha does not lead to proteasomal degradation. Importantly, TRIM5alpha is clearly conjugated by a single ubiquitin molecule (monoubiquitination). Our monoubiquitin-fusion assay suggests that monoubiquitination is a signal for TRIM5alpha to translocate from cytoplasmic bodies to the cytoplasm. | SIGNOR-271672 |
Q01973 | P21860 | 1 | phosphorylation | up-regulates activity | 0.343 | Here we show that NKX2-1 induces the expression of the receptor tyrosine kinase-like orphan receptor 1 (ROR1), which in turn sustains a favorable balance between prosurvival PI3K-AKT and pro-apoptotic p38 signaling, in part through ROR1 kinase-dependent c-Src activation, as well as kinase activity-independent sustainment of the EGFR-ERBB3 association, ERBB3 phosphorylation, and consequential PI3K activation.|ROR1 knockdown decreased phosphorylations of ERBB3, c-Src, and AKT in NKX2-1 + / ROR1 + NCI-H1975, SK-LC-5, and NCI-H358 cells. | SIGNOR-279279 |
P06493 | Q13501 | 1 | phosphorylation | up-regulates | 0.343 | Here we show that cdk1 phosphorylates p62 in vitro and in vivo at t269 and s272, which is necessary for the maintenance of appropriate cyclin b1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis. | SIGNOR-169012 |
P53350 | O14920 | 1 | phosphorylation | down-regulates | 0.343 | Plk1 phosphorylates serines 733, 740, and 750 in the gammabd of ikkbeta in vitro. Phosphorylating gammabd with plk1 decreased its affinity for ikkgamma | SIGNOR-181802 |
P00519 | P42224 | 1 | phosphorylation | up-regulates activity | 0.343 | Our study unexpectedly found that c-Abl, another kinase other than JAKs, also contributes to STAT1 Y701 phosphorylation independently (XREF_FIG).|reported that c-Abl, but not Arg, could induce neuronal loss by prompting STAT1 activation and interferon production. | SIGNOR-279491 |
Q9UNE7 | Q99717 | 1 | ubiquitination | down-regulates | 0.343 | In ad-dition, some proteins (e.g. Chip, carboxyl terminus of hsc70-interacting protein) inhibit the signaling activi-ties of smad1/5 by recruiting smad1/5 from the functional r-/co-smad complex and further pro-moting the ubiquitination and degradation of smad1/5 in a chaperone-independent manne | SIGNOR-195690 |
O60674 | Q9UGK3 | 1 | phosphorylation | up-regulates activity | 0.343 | To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase |On the other hand, the phosphorylation levels of Y22F, Y310F, and Y322F by GST-JH1 were reduced to 8060% of the levels of wild-type STAP-2, which suggests that these three are potential phosphorylation sites by activated JAK2. | SIGNOR-249372 |
Q13043 | P00519 | 2 | phosphorylation | down-regulates | 0.343 | Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3 | SIGNOR-181060 |
P11229 | P08754 | 1 | binding | up-regulates activity | 0.343 | Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. | SIGNOR-256878 |
Q9BZR9 | O43318 | 1 | polyubiquitination | up-regulates activity | 0.343 | These results suggest that TRIM8 could mediate K63-linked polyubiquitination of TAK1 at residue K158.These results suggest that TRIM8 is involved in TNFα- and IL-1β–induced NF-κB activation by mediating K63-linked TAK1 polyubiquitination and subsequent activation. | SIGNOR-271890 |
P41743 | P50613 | 1 | phosphorylation | up-regulates activity | 0.343 | PKC\u03b9 activates CDK7 to promote glucose consumption.|PKC\u03b9 phosphorylates Thr170 on CDK7 in vitro, can associate with CDK7 in cells, and is activated downstream of PI3K signaling xref , xref \u2013 xref . | SIGNOR-280088 |
P17612 | Q15256 | 1 | phosphorylation | down-regulates activity | 0.343 | The PKA phosphorylation site on PTP-SL was identified as the Ser(231) residue. treatment of COS-7 cells with PKA activators, or overexpression of the Calpha catalytic subunit of PKA, inhibited the cytoplasmic retention of ERK2 and p38alpha by wild-type PTP-SL, but not by a PTP-SL S231A mutant.‚ | SIGNOR-250038 |
P19784 | Q13351 | 1 | phosphorylation | up-regulates activity | 0.343 | Regulation of erythroid Krppel-like factor (EKLF) transcriptional activity by phosphorylation of a protein kinase casein kinase II site within its interaction domain. the transactivation capability of EKLF is augmented by co-transfection of CKIIalpha. in vitro assays demonstrate that CKIIalpha interacts with EKLF, and that the EKLF interaction domain is phosphorylated by CKII only at Thr-41 | SIGNOR-241365 |
O14965 | Q13158 | 1 | phosphorylation | up-regulates | 0.343 | Here, we report that aur-a phosphorylates s203 of the fas associated with death domain protein (fadd)phosphorylation of s203 by aur-a serves to prime fadd for plk1-mediated phosphorylation at s194 | SIGNOR-176739 |
P54253 | P12830 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.343 | Overexpression of the CtBP2 protein enhanced the repression activity of the E-cadherin promoter in a dose-dependent manner, whereas overexpression of ataxin-1 increased the activity of the E-cadherin promoter in a dose-dependent manner | SIGNOR-261577 |
P36897 | O00459 | 1 | binding | up-regulates | 0.343 | These studies revealed that PI 3-kinase is associated in vivo with both TGF-_ receptor subtypes and that TGF-_1 stimulation enhances PI 3-kinase activity associated with type I TGF-_ receptor in hASM cells. | SIGNOR-227531 |
P31751 | Q92945 | 1 | phosphorylation | down-regulates | 0.343 | AKT phosphorylates the mRNA decay-promoting factor KSRP at a unique serine residue, induces its association with the multifunctional protein 14-3-3, and prevents KSRP interaction with the exoribonucleolytic complex exosome. This impairs KSRPs ability to promote rapid mRNA decay. | SIGNOR-151220 |
Q18PE1 | P46109 | 1 | binding | up-regulates activity | 0.343 | Here, we identify two tyrosine residues in Dok-7 that are phosphorylated by Agrin stimulation, and show that two proteins, Crk and Crk-L, are recruited to these phosphorylation sites in Dok-7. | SIGNOR-273848 |
Q13153 | P36871 | 1 | phosphorylation | up-regulates | 0.343 | The signaling kinase p21-activated kinase 1 (pak1) binds to, phosphorylates and enhances the enzymatic activity of phosphoglucomutase 1 (pgm), | SIGNOR-127135 |
Q7Z6Z7 | P15172 | 1 | ubiquitination | down-regulates quantity | 0.343 | Importantly, addition of WT HUWE1 to a proteolytic reaction mixture enhanced the degradation of MyoD.|Mass-spectrometry analyses show that HUWE1 can ubiquitinate MyoD at its N-terminal residue, though the preferred sites are - at least in a cell free system - the internal lysines of the protein. | SIGNOR-278694 |
Q9NXA8 | P54868 | 1 | post translational modification | up-regulates activity | 0.343 | We demonstrate that SIRT5 regu-lates succinylation of the rate-limiting ketogenicenzyme 3-hydroxy-3-methylglutaryl-CoA synthase 2(HMGCS2) both in vivo and in vitro.|Succinylation of Lysine Residues within the SubstrateBinding Pocket Inhibits HMGCS2 Activity|Here, we use a label-freequantitative proteomic approach to characterizethe lysine succinylome in liver mitochondria and itsregulation by the desuccinylase SIRT5 | SIGNOR-267641 |
P17252 | P19429 | 1 | phosphorylation | up-regulates activity | 0.343 | In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. | Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation. | SIGNOR-249066 |
P36897 | P68104 | 1 | phosphorylation | down-regulates | 0.343 | Phosphorylation of eEF1A1 at Ser300 by T_R-I results in inhibition of mRNA translation | SIGNOR-167943 |
Q96EV8 | Q9Y6W5 | 1 | binding | up-regulates activity | 0.343 | Dysbindin-1, WAVE2 and Abi-1 form a complex that regulates dendritic spine formation. Although dysbindin-1, WAVE2 and Abi-1 form a ternary complex, dysbindin-1 promoted the binding of WAVE2 to Abi-1. | SIGNOR-265659 |
Q02750 | P49841 | 1 | phosphorylation | up-regulates activity | 0.343 | In vitro kinase assay was carried out using a recombinant human active mek1 and we found that gsk-3beta was phosphorylated on tyr(216) by this kinase in a dose- and time-dependent manner. Further, the pretreatment of fibroblasts with u0126 inhibited serum-induced nuclear translocation of gsk-3beta. These results suggested that mek1/2 induces tyrosine phosphorylation of gsk-3beta and this cellular event might induce nuclear translocation of gsk-3beta. | SIGNOR-236622 |
P00519 | Q14847 | 1 | phosphorylation | up-regulates | 0.343 | C-abl activation by apoptotic agents specifically promotes phosphorylation of lasp-1 at tyrosine 171, which is associated with the loss of lasp-1 localization to focal adhesions and induction of cell death. Thus, lasp-1 is a dynamic focal adhesion protein necessary for cell migration and survival in response to growth factors and ecm proteins. | SIGNOR-124719 |
P29350 | O94916 | 1 | dephosphorylation | down-regulates activity | 0.343 | We confirmed that SHP-1 is inhibitory by overexpressing it, which reduces TonEBP/OREBP transcriptional activity at 500 mosmol/kg. SHP-1 dephosphorylates TonEBP/OREBP at a known regulatory site, Y143, both in vivo and in vitro. It inhibits TonEBP/OREBP by both reducing TonEBP/OREBP nuclear localization, which is Y143 dependent, and by lowering high NaCl-induced TonEBP/OREBP transactivating activity | SIGNOR-248467 |
P00533 | Q38SD2 | 1 | phosphorylation | down-regulates activity | 0.343 | In this study, we demonstrate that EGFR regulates the kinase activity of LRRK1 via tyrosine phosphorylation and that this is required for proper endosomal trafficking of EGFR. Phosphorylation of LRRK1 at Tyr-944 results in reduced LRRK1 kinase activity. | SIGNOR-262856 |
P24941 | P10644 | 1 | phosphorylation | up-regulates | 0.343 | In this context, we have identified rialpha as a novel substrate for the g(1)/s-cyclin-dependent kinase, cdk2/cyclin e, and found that rialpha is specifically phosphorylated at the serine residue. | SIGNOR-145577 |
P51149 | O14818 | 1 | binding | up-regulates activity | 0.343 | Rab7 Forms a Complex with the Proteasome -Subunit XAPC. In this study the proteasome alpha-subunit XAPC7 (also known as PSMA7, RC6-1, and HSPC in mammals) was identified to interact specifically with Rab7 and was recruited to multivesicular late endosomes through this interaction. | SIGNOR-261303 |
P68400 | Q02790 | 1 | phosphorylation | down-regulates activity | 0.343 | Thr-143 in the hinge I region was identified as the major phosphorylation site for CK2. | Most importantly, CK2-phosphorylated FKBP52 did not bind to HSP90 | SIGNOR-250865 |
P00519 | Q13043 | 2 | phosphorylation | up-regulates activity | 0.343 | In the present study, we demonstrate that the protein kinase c-Abl phosphorylates MST1 at Y433, which triggers the stabilization and activation of MST1. | SIGNOR-260927 |
P27361 | Q01860 | 1 | phosphorylation | down-regulates | 0.343 | Phosphorylation of this site downregulates nanog, sox2, rex1 and upregulates bmp4, gata6, ddlx5. | SIGNOR-192101 |
P12931 | P16662 | 1 | phosphorylation | up-regulates | 0.343 | Overexpression of regular or active src, but not dominant-negative src, in 2b7-transfected cos-1 cells increased 2b7 activity and phospho-y438-2b7 by 50% | SIGNOR-184613 |
P06241 | Q8TDQ1 | 1 | phosphorylation | up-regulates activity | 0.343 | Y236 (YVTM) and Y263 (YCNM) fit with the consensus motif reported to bind the p85α regulatory subunit of PI3K (16). |The association between IREM-1 and p85α was only perceived in the presence of c-Fyn, suggesting that tyrosine phosphorylation of IREM-1 cytoplasmic tail of IREM-1 was required for the interaction. | SIGNOR-275620 |
Q00341 | P07333 | 1 | transcriptional regulation | down-regulates quantity by repression | 0.342 | Vigilin (Vgl1) is essential for heterochromatin formation, chromosome segregation, and mRNA stability and is associated with autism spectrum disorders and cancer: vigilin, for example, can suppress proto-oncogene c-fms expression in breast cancer. | SIGNOR-266696 |
P68400 | P29590 | 1 | phosphorylation | down-regulates | 0.342 | Here we show that ck2 regulates pml protein levels by promoting its ubiquitin-mediated degradation dependent on direct phosphorylation at ser517. | SIGNOR-148306 |
Q13131 | P04049 | 1 | phosphorylation | down-regulates | 0.342 | Ampk also phosphorylated full-length, kinase-defective raf-1 (k375m) to generate two [32p]phosphopeptides, one co-migrating with synthetic tryptic peptide containing phospho-ser621 and the other with phospho-ser259. The catalytic subunit of PKA also phosphorylated Ser621 in vitro, while its overexpression in intact cells resulted in increased phosphorylation of Ser621 and decreased activity of Raf-1. These results suggest that phosphorylation of Ser621 inactivates Raf-1, but do not prove that PKA is responsible for this in vivo. | SIGNOR-47148 |
P16220 | Q9Y4H2 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.342 | Taken together, these results indicate that the IRS2 gene is a direct target for CREB action in vivo | SIGNOR-278145 |
P68400 | P06127 | 1 | phosphorylation | up-regulates | 0.342 | In this study, we use jurkat t cell transfectants of cd5 cytoplasmic tail mutants to reveal phosphorylation sites relevant to signal transduction. Our results show that casein kinase ii (ckii) is responsible for the constitutive phosphorylation of cd5 molecules at a cluster of three serine residues located at the extreme c terminus (s458, s459, and s461) | SIGNOR-62311 |
Q9Y297 | P47736 | 1 | ubiquitination | down-regulates | 0.342 | Here, we demonstrated that rap1gap is ubiquitinated and degraded through proteasome pathway in mitosis. Proteolysis of rap1gap requires the plk1 kinase and _-trcp ubiquitin ligase complex. | SIGNOR-203548 |
Q8TDX7 | P54274 | 1 | phosphorylation | up-regulates activity | 0.342 | Using KR-TRF2 to induce telomeric DNA damage, we found that TRF1 degradation was also exacerbated when ATM was inhibited after damage induction (55.2% of mock treated cells) (XREF_FIG), indicating that the ATM signal pathway is required for Nek7 mediated TRF1 stabilization.|We show that Nek7 phosphorylates TRF1 at Ser114 and in turn maintains stability of the shelterin complex at telomeres. | SIGNOR-278447 |
P09874 | P09884 | 1 | binding | up-regulates activity | 0.342 | We provide evidence that in proliferating cells: (i) PARP is physically associated with the catalytic subunit of the DNA polymerase α–primase tetramer, an association confirmed by confocal microscopy, demonstrating that both enzymes are co-localized at the nuclear periphery of HeLa cells.|(iii) PARP-deficient cells derived from PARP knock-out mice exhibited reduced DNA polymerase activity, | SIGNOR-261270 |
Q16236 | P08263 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.342 | In both models, the inducer-modified and Nrf2-bound Keap1 is inactivated and, consequently, newly synthesized Nrf2 proteins bypass Keap1 and translocate into the nucleus, bind to the ARE and drive the expression of Nrf2 target genes such as NAD(P)H quinone oxidoreductase 1 (NQO1), heme oxygenase 1 (HMOX1), glutamate-cysteine ligase (GCL) and glutathione S transferases (GSTs). | SIGNOR-256278 |
P12931 | Q7Z3C6 | 1 | phosphorylation | up-regulates activity | 0.342 | Src phosphorylates mATG9 at Tyr8 to maintain its endocytic and constitutive trafficking in unstressed conditions. In response to starvation, phosphorylation of mATG9 at Tyr8 by Src and at Ser14 by ULK1 functionally cooperate to promote interactions between mATG9 and the AP1/2 complex, leading to redistribution of mATG9 from the plasma membrane and juxta-nuclear region to the peripheral pool for autophagy initiation. | SIGNOR-266367 |
P24941 | P26358 | 1 | phosphorylation | up-regulates | 0.342 | We report that cyclin-dependent kinases (cdks) 1, 2 and 5 can phosphorylate ser154 of human dnmt1 in vitro. Further evidence of phosphorylation of endogenous dnmt1 at position 154 by cdks is also found in 293 cells treated with roscovitine, a specific inhibitor of cdk1, 2 and 5 | SIGNOR-173681 |
Q05655 | P49840 | 1 | phosphorylation | down-regulates | 0.342 | Convergence of multiple signaling cascades at glycogen synthase kinase 3: edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase c-dependent intracellular pathway. | SIGNOR-115722 |
Q15475 | P15311 | 1 | transcriptional regulation | up-regulates quantity | 0.342 | We now show that the gene encoding Ezrin is a direct transcriptional target of Six1. | SIGNOR-259374 |
P50552 | P31939 | 1 | phosphorylation | up-regulates activity | 0.342 | ATIC and VASP phosphorylation is dependent on NPM-ALK kinase activity. | SIGNOR-276172 |
P52564 | Q14765 | 1 | phosphorylation | up-regulates activity | 0.342 | MKK6, phosphorylate STAT4 on serine 721. IL-12 induces STAT4 phosphorylation on serine 721 and that mutation of serine 721 interferes with STAT4 transcriptional activity. | SIGNOR-251425 |
P41743 | P15311 | 1 | phosphorylation | up-regulates | 0.342 | Pkciota phosphorylated ezrin on t567 in vitro, and in sf9 cells that do not activate human ezrin. we conclude that, although other molecular mechanisms contribute to ezrin activation, apically localized phosphorylation by pkciota is essential for the activation and normal distribution of ezrin at the early stages of intestinal epithelial cell differentiation. | SIGNOR-160855 |
Q96LB2 | P50148 | 1 | binding | up-regulates activity | 0.342 | Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. | SIGNOR-257384 |
Q09472 | Q10571 | 2 | binding | up-regulates | 0.342 | Our results indicate that mn1 is a transcription coactivator rather than a sequence-specific transcription factor, and that it may stimulate rar/rxr-mediated transcription through interaction with p160 and p300. | SIGNOR-97899 |
P24941 | Q02535 | 1 | phosphorylation | down-regulates | 0.342 | We now show that an analogous cell-cycle-regulated phosphorylation of id3 alters the specificity of id3 for abrogating both e-box-dependent bhlh homo- or heterodimer complex formation in vitro and e-box-dependent reporter gene function in vivo._ | SIGNOR-53306 |
Q10571 | Q09472 | 2 | binding | up-regulates activity | 0.342 | Taken together, our results indicate that MN1 is a transcription coactivator rather than a sequence-specific transcription factor, and that it may stimulate RAR/RXR-mediated transcription through interaction with p160 and p300. | SIGNOR-256020 |
Q14678 | Q9UQB8 | 1 | binding | down-regulates activity | 0.342 | In this study, we report that Kank disrupts the function of active Rac1 through IRSp53. The binding between IRSp53 and Kank inhibits the association of active Rac1 with IRSp53 rather than the association of active cdc42 with IRSp53. Kank inhibits the formation of lamellipodia and membrane ruffles induced by active Rac1 in NIH3T3 cells. Kank interacts with IRSp53 through their coiled-coil domains. Kank affected the interaction between IRSp53 and Rac1 and partially affected that between IRSp53 and cdc42 (Fig. 3). | SIGNOR-265553 |
O15379 | O15105 | 1 | binding | up-regulates | 0.342 | We show here that smad7 can form a complex with endogenous histone deacetylase proteins hdac-1 and hdac-3 in nih 3t3 mouse fibroblast cells | SIGNOR-199967 |
P55210 | P49768 | 1 | cleavage | up-regulates activity | 0.342 | 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-261757 |
Q9BZE9 | Q9H867 | 1 | binding | up-regulates | 0.342 | In the case of vcp, methylation by mettl21d was stimulated by the addition of the ubx cofactor aspscr1, which we show directly interacts with the methyltransferase. | SIGNOR-200572 |
Q96L73 | P10163 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.342 | We here demonstrate that NSD1 could bind to the promoter regions of PRB4 and activate promoter activity by reducing the binding of H3K27me2 and increasing the binding of H3K36me2 on PRB4 promoter. | SIGNOR-268459 |
P10586 | P31749 | 1 | dephosphorylation | down-regulates | 0.342 | Knock-down of lar by the l3 sirna probe markedly inhibited the insulin-stimulated increase in the phosphorylation of protein kinase b (pkb, also called akt) on serine 473 by >90% | SIGNOR-137246 |
O43293 | Q00987 | 1 | phosphorylation | up-regulates quantity by stabilization | 0.342 | Zip kinase was able to phosphorylate mdm2 at ser166, a site previously reported to be modified by akt kinase, thus demonstrating that zip kinase is a bona fide mdm2-binding protein. | SIGNOR-123159 |
Q07912 | O00308 | 1 | phosphorylation | up-regulates activity | 0.342 | ACK1 phosphorylates WWP2 at the 2, 3-linker and partially activates the ubiquitination ligase activity.|Activation of E3 ubiquitin ligase WWP2 by non-receptor tyrosine kinase ACK1. | SIGNOR-279302 |
Q12772 | Q7KZF4 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.342 | These findings reveal that SREBP-2 and SREBP-1 bind to specific sites in SND1 promoter and regulate SND1 transcription in opposite ways; it is induced by SREBP-2 activating conditions and repressed by SREBP-1 overexpression. | SIGNOR-259136 |
P08253 | P98164 | 1 | binding | up-regulates quantity | 0.342 | We show that megalin/LRP-2 acts as an endocytic receptor for proMMP-2:TIMP-2 complex. We found that RAP, an antagonist of the LDL receptor family18, competed with binding of proMMP-2:TIMP-2 complex onto rat BN16 epithelial cells. | SIGNOR-265255 |
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