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 |
|---|---|---|---|---|---|---|---|
P52564 | O43318 | 0 | phosphorylation | up-regulates activity | 0.764 | The activity of tak1 to phosphorylate mkk6, which activates the jnk-p38 kinase pathway, is directly regulated by k63-linked polyubiquitination | SIGNOR-109497 |
P18545 | P11488 | 0 | binding | down-regulates activity | 0.764 | In the dark, PDE6 activity is suppressed by its inhibitory γ-subunit (Pγ). Rhodopsin-catalyzed activation of the G protein, transducin, relieves this inhibition and enhances PDE6 catalysis. | SIGNOR-260008 |
Q03135 | P12931 | 0 | phosphorylation | down-regulates activity | 0.764 | Caveolin-1 is phosphorylated on tyr(14) in response to both oxidative and hyperosmotic stress. In the present paper, we show that this phosphorylation requires activation of the src family kinase fyn | SIGNOR-118007 |
O95786 | Q8IUD6 | 0 | ubiquitination | up-regulates activity | 0.764 | Our data suggest that Riplet/RNF135 is a novel factor of the RIG-I pathway that is involved in the evoking of human innate immunity against RNA virus infection, and activates RIG-I through ubiquitination of its C-terminal region. | SIGNOR-265569 |
P27037 | P18075 | 0 | binding | up-regulates | 0.764 | We show that bmp7 and activin bind to the same type ii receptors, actrii and iib, but recruit distinct type i receptors into heteromeric receptor complexes | SIGNOR-60237 |
P10636 | Q00535 | 0 | phosphorylation | down-regulates activity | 0.763 | We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. | SIGNOR-249321 |
P98177 | P31749 | 0 | phosphorylation | down-regulates | 0.763 | Foxo4 transcription factor, also referred to afx, contains three putative phosphorylation motif sites for protein kinase b (pkb), thr32, ser197, and ser262, and it is proposed that phosphorylated foxo4 stays in the cytosol and is imported to the nucleus through dephosphorylation to induce target gene expression | SIGNOR-252486 |
P10275 | P07900 | 0 | binding | up-regulates activity | 0.763 | The unliganded AR resides predominately in the cytoplasm as a heteromeric complex with hsp90 and other chaperone proteins. These chaperone proteins maintain AR in a form that is receptive to ligand binding. Regulation of gene expression by androgen-activated AR occurs through receptor nuclear translocation, dimerization, and binding to androgen response elements (AREs) in the DNA of target genes. | SIGNOR-251536 |
P34925 | P56704 | 0 | binding | up-regulates | 0.763 | Here, we report that ryk directly binds wnt-1 and wnt-3a via its wif domain and is required for the tcf. | SIGNOR-129580 |
Q9HCM2 | Q14563 | 0 | binding | up-regulates activity | 0.763 | We provide evidence suggesting that, in endothelial cells and glioblastoma cells, plexin-A4 is a required component of both Sema3A and Sema3B receptor complexes and inhibition of its expression nullifies both Sema3A and Sema3B signaling. The specificity for Sema3A or Sema3B is determined by the presence of plexin-A1 in Sema3A receptors and plexin-A2 in Sema3B receptors, and silencing each abrogates signaling by the appropriate semaphorin. | SIGNOR-261811 |
P49190 | Q96A98 | 0 | binding | up-regulates | 0.763 | Subsequent efforts led to the isolation and definition of the primary structure of a novel peptide, referred to as tip39, from bovine hypothalamus and the synthetic peptide was shown to efficiently activate human, rat, and zebrafish pth2 receptors | SIGNOR-115124 |
P01106 | Q969H0 | 0 | ubiquitination | down-regulates quantity | 0.762 | We now show that the F-box protein Fbw7 interacts with and thereby destabilizes c-Myc in a manner dependent on phosphorylation of MB1. Whereas wild-type Fbw7 promoted c-Myc turnover in cells, an Fbw7 mutant lacking the F-box domain delayed it. | SIGNOR-243545 |
Q01201 | Q00653 | 0 | binding | up-regulates activity | 0.762 | The map3k14-activated chuk/ikka homodimer phosphorylates nfkb2/p100 associated with relb, inducing its proteolytic processing to nfkb2/p52 and the formation of nf-kappa-b relb-p52 complexes. The nf-kappa-b heterodimeric relb-p52 complex is a transcriptional activator. | SIGNOR-182835 |
Q08050 | P06493 | 0 | phosphorylation | up-regulates | 0.762 | A conserved phosphorylation site within the forkhead domain of foxm1b is required for its activation by cyclin-cdk1further analysis reveals that the leu-641 residue within an lxl motif is required for the recruitment of the cyclin-cdk complex, and the thr-596 residue is a critical cdk1 phosphorylation site within the activation domain of foxm1b. Cdk-dependent phosphorylation stimulates the foxm1b transcriptional activity | SIGNOR-187880 |
P28482 | Q13115 | 0 | dephosphorylation | down-regulates activity | 0.762 | Dephosphorylation and Inactivation of ERKs|A single protein kinase, MEK, activates ERK2 by phosphorylating threonine 183 and tyrosine 185 | SIGNOR-248718 |
Q12866 | Q14393 | 0 | binding | up-regulates | 0.762 | We also found that gas6 stimulated tyrosine phosphorylation of axl, sky, and mer receptors ectopically expressed in chinese hamster ovary cells. Taken together, these findings suggest that gas6 is a common ligand for axl, sky, and mer, all known members of an axl/sky receptor subfamily. | SIGNOR-44953 |
Q13163 | Q9Y2U5 | 0 | phosphorylation | up-regulates | 0.762 | Mekk2 and mekk3 are mapk kinase kinases that bind, phosphorylate and activate mek5. | SIGNOR-104634 |
P04049 | P30086 | 0 | binding | down-regulates | 0.762 | Suppression of raf-1 kinase activity and map kinase by rkip. Rkip binds to raf-1, mek and erk, but not to ras. | SIGNOR-70838 |
P29353 | P43405 | 0 | phosphorylation | up-regulates | 0.762 | The syk-family kinases (syk and zap-70) were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site on sch1 (iso2). | SIGNOR-59635 |
P54753 | P98172 | 0 | binding | up-regulates | 0.762 | The activation of eph receptors by their ligands, which are membrane-anchored molecules, involves a cell-cell recognition event that often causes cell repulsion. | SIGNOR-52517 |
P34981 | P20396 | 0 | binding | up-regulates activity | 0.762 | When TRH reaches the pars distalis of the pituitary, it regulates cells that express TRH receptor-1 (TRH-R1), such as the thyrotrophs. These cell types are subject to a multifactorial regulation that determines the extent and specificity of their response to TRH. | SIGNOR-267200 |
O60609 | Q5T4W7 | 0 | binding | up-regulates | 0.762 | Here, we report the identification of artemin, a novel member of the gdnf family, and demonstrate that it is the ligand for the former orphan receptor gfralpha3-ret. Artemin can also activate the gfralpha1-ret complex. | SIGNOR-63009 |
P20336 | Q9UQ26 | 0 | relocalization | up-regulates activity | 0.762 | N-terminal interactions of RIMs with RAB3 and MUNC13 regulate DCV fusion. Through N-terminal interactions, RIMs position MUNC13 and recruit DCVs via RAB3, which is located on the vesicle | SIGNOR-264377 |
O95235 | P53350 | 0 | phosphorylation | up-regulates activity | 0.761 | MKlp2 treated with Plk1 did not form the regular microtubule bundles seen with MKlp2 only; many single microtubules were seen instead, and the bundles that were formed were loose parallel arrays rather than the dense bundles seen with untreated MKlp2.|We propose that phosphorylation of MKlp2 by Plk1 is necessary for the spatial restriction of Plk1 to the central spindle during anaphase and telophase, and the complex of these two proteins is required for cytokinesis. | SIGNOR-278201 |
Q03431 | P12272 | 0 | binding | up-regulates activity | 0.761 | Prostate-specific antigen was found to specifically cleave PTHrP 1-141 in a time- and dose-dependent manner.|The preferred PSA cleavage site of PTHrP 1-141 was determined to be at the carboxyl-terminus of phenylalanine 23, consistent with chymotryptic-like enzymatic activity of PSA. Cleavage of PTHrP by PSA completely abolished the ability of PTHrP to stimulate cAMP production. | SIGNOR-270549 |
P15502 | Q9UBX5 | 0 | binding | up-regulates activity | 0.761 | The binding of tropoelastin fragments to fibulin-5 was directly proportional to their propensity to coacervate. Furthermore, the addition of fibulin-5 to tropoelastin facilitated coacervation. Taken together, the present study shows that fibulin-5 enhances elastic fiber formation in part by improving the self-association properties of tropoelastin. | SIGNOR-252137 |
P06213 | Q14449 | 0 | binding | down-regulates activity | 0.761 | Growth factor receptor-bound protein 14 (Grb14) interacts with insulin receptor (IR) through the between PH and SH2 (BPS) domain. Grb14-IR complex formation is initiated by insulin stimulation, and the binding event results in the inhibition of insulin signalling. | SIGNOR-264873 |
P63000 | P52735 | 0 | guanine nucleotide exchange factor | up-regulates | 0.761 | Vav2 activates rac1 / vav2 is an exchange factor for rho family gtpases. | SIGNOR-81645 |
P35222 | P12931 | 0 | phosphorylation | down-regulates activity | 0.761 | beta-catenin is a good substrate of pp60c- srctyrosine kinase in vitro;this kinase modifies specifically tyr-86 and tyr-654although consistently detected, this negative effect of tyr-86 phosphorylation on tbp binding was clearly less important than the positive effect observed after tyr-654 phosphorylation. | SIGNOR-106458 |
Q9BXW9 | O94782 | 0 | deubiquitination | down-regulates activity | 0.761 | The deubiquitinating enzyme USP1 controls the cellular levels of the DNA damage response protein Ub-FANCD2|The level of monoubiquitinated FANCD2 protein increases in response to various types of DNA damage in mammalian cells | SIGNOR-263273 |
Q16763 | Q9UM11 | 0 | binding | up-regulates activity | 0.761 | Ube2S depends on the cell cycle-dependent association with the APC/C activators Cdc20 and Cdh1 for its activity | SIGNOR-265081 |
P00533 | Q9ULV8 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.761 | In summary, we have shown that CBLC and AIP4 can interact and that these two E3 ligases could contribute to down-regulate EGFR signaling by ubiquitination. | SIGNOR-272605 |
Q07817 | Q9BXH1 | 0 | binding | down-regulates activity | 0.761 | Only bimbh3 and bbc3 had comparable strong affinities for all the prosurvival proteins. The members that promote cell survival, including mammalian bcl-2, bcl-xl,bcl-w, mcl-1, and a1.Puma promotes bax translocation by both by directly interacting with bax and by competitive binding to bcl-x(l) in uv-induced apoptosis. | SIGNOR-133811 |
P42702 | P15018 | 0 | binding | up-regulates | 0.76 | Lif binds at low-affinity to lifr, the structure of which is closely related to that of gp130 (42). Lifr then becomes heterodimerized with gp130 to form the high-affinity and signaling-competent complex (43). Osm utilizes this type of heterodimer, i.e. the lifr/gp130 complex (43, 44). | SIGNOR-139102 |
Q9UJU2 | Q9UBE8 | 0 | phosphorylation | down-regulates | 0.76 | Regulation of lymphoid enhancer factor 1/t-cell factor by mitogen-activated protein kinase-related nemo-like kinase-dependent phosphorylation in wnt/beta-catenin signaling.Nlk phosphorylates lef-1/tcf on two serine/threonine residues located in its central region. Mutation of both residues to alanine enhanced lef-1 transcriptional activity and rendered it resistant to inhibition by nlk. | SIGNOR-97812 |
Q13480 | P00533 | 0 | phosphorylation | up-regulates | 0.76 | Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). | SIGNOR-236400 |
P04637 | Q8IW41 | 0 | phosphorylation | up-regulates | 0.76 | Furthermore, we show that prak activates p53 by direct phosphorylation. prak phosphorylates p53 at ser37 | SIGNOR-152847 |
P29474 | P07900 | 0 | binding | up-regulates | 0.76 | The binding of hsp90 to enos enhances the activation of enos. | SIGNOR-57211 |
P31749 | O60346 | 0 | dephosphorylation | down-regulates | 0.76 | Here, we identify a protein_ phosphatase, ph domain leucine-rich repeat protein_ phosphatase_ (phlpp), that specifically_ dephosphorylates_ the hydrophobic motif of_ akt_ (ser473 in akt1), triggering_ apoptosis_ and suppressing_ tumor_ growth. | SIGNOR-252601 |
P18206 | P12931 | 0 | phosphorylation | down-regulates activity | 0.76 | The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreadingWhen phosphorylated, the vinculin tail exhibited significantly less binding to the vinculin head domain than the unphosphorylated tail. | SIGNOR-247424 |
P00533 | Q13191 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.76 | Here we describe that overexpression of cbl-b, a homologue of the c-cbl protooncogene, inhibits EGFR-induced apoptosis in MDA-MB-468 breast cancer cells. Overexpression of cbl-b results in a shortened duration of EGFR activation upon EGF stimulation. This is demonstrated by decreased amounts of phosphorylated EGFR as well as by inhibition of multiple downstream signaling pathways. The inhibition of signaling by cbl-b results from increased ubiquitination and degradation of the activated EGFR. | SIGNOR-272934 |
P55211 | Q13489 | 0 | binding | down-regulates | 0.76 | Xiap, birc2 and birc3 were shown to bind pro-casp9. Iaps may suppress casp9 by direct auto-activation of pro-caspase-11 | SIGNOR-56481 |
P27361 | Q16690 | 0 | dephosphorylation | down-regulates | 0.76 | Extracellular regulated kinases (erk) 1 and erk2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase vhr. A novel role in down-regulating the erk pathway | SIGNOR-67358 |
P15311 | P61586 | 0 | phosphorylation | up-regulates activity | 0.76 | Rev-erbα interacted with OPHN-1, promoted RhoA activity and phosphorylation of ERM. etection of phosphorylated ezrin (Thr567)/radixin (Thr564)/moesin (Thr558)(p-ERM) in Rev-erbαfl/flCre− and Rev-erbαfl/flPF4Cre+ platelets using phospho-specific antibodies. | SIGNOR-268429 |
P35222 | P33151 | 0 | binding | up-regulates activity | 0.76 | At its C-terminus, cadherin interacts with β-catenin, which dynamically associates with α-catenin, a direct binding partner of filamentous actin | SIGNOR-265867 |
Q9HBX9 | P04090 | 0 | binding | up-regulates | 0.76 | Lgr7 and lgr8, are capable of mediating the action of relaxin through an adenosine 3',5'-monophosphate (camp)-dependent pathway | SIGNOR-114549 |
O95999 | Q9H257 | 0 | binding | up-regulates quantity by stabilization | 0.76 | To identify upstream signaling partners of BCL10, we performed a mammalian two-hybrid analysis and identified CARD9 as a novel CARD-containing protein that interacts selectively with the CARD activation domain of BCL10. When expressed in cells, CARD9 binds to BCL10 and activates NF-kappaB. | SIGNOR-257602 |
P10275 | P12931 | 0 | phosphorylation | up-regulates activity | 0.76 | In addition to the ability of Src to promotes castration resistant progression and AR activation, Src is involved in regulating prostate cancer cell migration, invasion, and metastasis and affects bone remodeling.|These data suggest that downstream of cell surface receptors, Ack1 mediates AR tyrosine phosphorylation at Tyr 267 and Src mediates AR tyrosine phosphorylation at Tyr 534. | SIGNOR-278168 |
P46108 | P00519 | 0 | phosphorylation | down-regulates activity | 0.76 | Negative regulation of crk by abl is essential for the antitumorigenic effects of ephrinb2,similar pathways may operate for crkl | SIGNOR-175135 |
P04637 | Q96S44 | 0 | phosphorylation | up-regulates | 0.76 | The intrinsic transcriptional activity of p53 was up-regulated by a transient transfection of prpk to cos-7 cells. Prpk was shown to bind to p53 and to phosphorylate p53 at ser-15. | SIGNOR-157471 |
P29474 | P0DP23 | 0 | binding | up-regulates activity | 0.76 | Electrons flow from the C-terminal reductase domain of one NOS monomer to the N-terminal oxygenase domain of the other NOS monomer (Siddhanta et al., 1998). The primary mode of enzyme activation is the binding of calcium-bound calmodulin to the N-terminal CaM-binding domain. This facilitates a structure change and the flow of electrons from NADPH through the flavins to the oxygenase domain of the other eNOS monomer | SIGNOR-251615 |
P42229 | P28482 | 0 | phosphorylation | up-regulates | 0.76 | Gh treatment of chinese hamster ovary cells stably transfected with the gh receptor (choa cells) led to rapid and transient activation of both stat5a and erk1 and erk2. these observations show, for the first time, direct physical interaction between erk and stat5a and also clearly identify serine 780 as a target for erk. | SIGNOR-66239 |
Q01718 | Q8TCY5 | 0 | binding | up-regulates activity | 0.76 | We report that MRAP and MRAP2 can interact with all 5 MCRs. This interaction results in MC2R surface expression and signaling.We have previously identified MRAP as an accessory protein for MC2R, required for receptor trafficking to the cell surface and the formation of a functional MC2R. Here we have identified MRAP2 as a homologue of MRAP. Like MRAP, MRAP2 is able to support MC2R cell-surface expression, producing a functional ACTH-responsive receptor. | SIGNOR-252360 |
Q15418 | P28482 | 0 | phosphorylation | up-regulates activity | 0.759 | Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. | SIGNOR-219308 |
Q99717 | Q04771 | 0 | phosphorylation | up-regulates | 0.759 | Bmp7 stimulated phosphorylation of endogenous smad1 and 5, formation of complexes with smad4 and induced the promoter for the homeobox gene, tlx2 | SIGNOR-60171 |
O43521 | P45983 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.759 | Ser69 can also be phosphorylated by JNK and p38MAPK at least in vitro. Phosphorylation of BimEL on Ser69 promotes its ubiquitination. | SIGNOR-250132 |
Q9NQS7 | P06493 | 0 | phosphorylation | up-regulates | 0.759 | Here, we report that cdk1 phosphorylates thr 59 and thr 388 on inner centromere protein (incenp), which regulates the localization and kinase activity of aurora-b from prophase to metaphase. The replacement of endogenous incenp with t388a resulted in the delay of progression from metaphase to anaphase. | SIGNOR-143387 |
P78352 | Q8NFZ4 | 0 | relocalization | up-regulates activity | 0.759 | Like NRXNs, NLGNs bind to intracellular PDZ-domain proteins, but in contrast to NRXNs, NLGNs bind to class I PDZ domains such as those contained in PSD95, a postsynaptic MAGUK protein65. PSD95 and its homologues are centrally involved in recruiting glutamate receptors at postsynaptic sites66. Similarly to CASK, PSD95 binds to intracellular adaptor proteins, and especially to GKAP (a protein that binds to the guanylate-kinase domain of PSD95), which, in turn, binds to SHANK proteins (Fig. 1b). A possible role of these interactions is to recruit postsynaptic adaptor proteins to the site of synaptic junctions. | SIGNOR-264193 |
O00401 | P12931 | 0 | phosphorylation | up-regulates activity | 0.759 | An Src family tyrosine kinase, v-Src, phosphorylates and activates N-WASP. | SIGNOR-279487 |
P40763 | P48357 | 0 | binding | up-regulates activity | 0.759 | LRb signaling is initiated by leptin binding to the extracellular domain of the LRb dimer, leading to Jak2 transphosphorylation and activation. Activated Jak2 mediates the tyrosine phosphorylation of Tyr985 and Tyr1138of LRb. These phosphotyrosine residues immediately function as binding sites (double-ended lines) for SHP-2 and STAT3, both of which quickly become tyrosine-phosphorylated by Jak2. | SIGNOR-263495 |
P41968 | P01189 | 0 | binding | up-regulates activity | 0.759 | The melanocortin (MC) receptor family consists of five Gs-coupled receptors that control various physiological functions in response to four distinct agonists, adrenocorticotropic hormone (ACTH, also known as corticotrophin) and alpha, beta, and gamma melanocyte-stimulating hormone (MSH), which are derived from the proopiomelanocortin precursor protein, and two inverse agonists, agouti and agouti-related proteins | SIGNOR-268705 |
P01019 | Q9BYF1 | 0 | cleavage | up-regulates activity | 0.759 | The ACE2 hydrolytic activity is dependent on the C terminus sequence of the substrate, which is evident from the data with the angiotensin peptides. After 2 h, ACE2 hydrolyzes Ang I partially and Ang II completely, although there is no hydrolysis of angiotensin 1–9, angiotensin 1–7, and angiotensin 1–5, which possess the same N terminus. | SIGNOR-256315 |
P36402 | P35222 | 0 | binding | up-regulates | 0.759 | Activated dvl binds and inhibits the phosphorylation of beta catenin by gsk3beta/alfa, blocking beta catenin degradation (fig 2?2),), so that beta catenin accumulates and translocates to the nucleus, where it interacts with the t cell specific factor (tcf)/lymphoid enhancer binding factor 1 (lef-1) transcription factor and induces the transcription of target genes such as c-jun, c-myc, and cyclin d1 | SIGNOR-134282 |
P48382 | P33076 | 0 | binding | up-regulates activity | 0.759 | RFX5 can activate transcription only in cooperation with CIITA. RFX5 and CIITA associate to form a complex capable of activating transcription from class II major histocompatibility complex promoters. In this complex, promoter specificity is determined by the DNA binding domain of RFX5 and the general transcription apparatus is recruited by the acidic activation domain of CIITA. | SIGNOR-240980 |
P42338 | P01112 | 0 | binding | up-regulates activity | 0.759 | Grb2 binds and activates sos, which then activates ras, and this activates p110 independently of p85. it was also described that ras interacts with pi3k in a direct manner. | SIGNOR-175189 |
P78352 | O95886 | 0 | binding | up-regulates activity | 0.758 | SAPAPs are specifically expressed in neuronal cells and enriched in the PSD fraction. SAPAPs induce the enrichment of PSD-95/SAP90 to the plasma membrane in transfected cells. Thus, SAPAPs may have a potential activity to maintain the structure of PSD by concentrating its components to the membrane area. | SIGNOR-264211 |
O43561 | P06239 | 0 | phosphorylation | up-regulates | 0.758 | Evidence of lat as a dual substrate for lck and syk in t lymphocytes.Lat is a linker protein essential for activation of t lymphocytes. Its rapid tyrosine-phosphorylation upon t cell receptor (tcr) stimulation recruits downstream signaling molecules for membrane targeting and activation. | SIGNOR-149182 |
O75581 | P41221 | 0 | binding | up-regulates activity | 0.758 | Wnt proteins bind to the frizzled receptors and lrp5/6 co-receptors, and through stabilizing the critical mediator betBeta-catenin, initiate a complex signaling cascade that plays an important role in regulating cell proliferation and differentiation. | SIGNOR-131841 |
P25054 | P49841 | 0 | phosphorylation | up-regulates | 0.758 | Gsk-3beta-dependent phosphorylation of apc. | SIGNOR-75366 |
P21802 | P08620 | 0 | binding | up-regulates | 0.758 | The nine known fgf ligands and the four signaling fgf receptors (and their alternatively spliced variants) are expressed in specific spatial and temporal patterns. The activity of this signaling pathway is regulated by ligand binding specificity, heparan sulfate proteoglycans, and the differential signaling capacity of individual fgf receptors. | SIGNOR-42377 |
P48551 | P05000 | 0 | binding | up-regulates | 0.758 | Ifn-alpha, ifn-beta, and ifn-omega, induce somewhat different cellular effects but act through a common receptor complex, ifnar, composed of subunits ifnar-1 and ifnar-2. | SIGNOR-105982 |
Q13114 | Q96RJ3 | 0 | binding | down-regulates quantity by destabilization | 0.758 | Activation of br3 induces recruitment and degradation of traf3. | SIGNOR-168199 |
P84022 | P11802 | 0 | phosphorylation | down-regulates activity | 0.757 | We have mapped CDK4 and CDK2 phosphorylation sites to Thr 8, Thr 178 and Ser 212 in Smad3. Mutation of the CDK phosphorylation sites increases Smad3 transcriptional activity | SIGNOR-232142 |
Q9Y4H2 | P06213 | 0 | phosphorylation | down-regulates activity | 0.757 | Tyr624 and Tyr628 are involved in the interaction between the IR and the KRLB domain of IRS-2, including tyrosine phosphorylation, and Tyr628 seems to be more important than Tyr624 in this process. the binding between the insulin receptor and the KRLB domain of IRS-2 results in tyrosine phosphorylation of the KRLB domain, and this leads to decreased binding of IRS-2 to the insulin receptor. | SIGNOR-251319 |
O95166 | Q14596 | 0 | binding | up-regulates | 0.757 | We performed glutathione s-transferase (gst) pull-down assays using extracts from hek293 cells overexpressing an ha-tagged nbr1(d50r) mutant, which lacks the ability to bind p62 (lamark et al., 2003) (figures s1a and s1b, available online), and gst fusions of six human atg8 homologs: gabarap, gabarapl1, gabarapl2, lc3a, lc3b, and lc3c. Indeed, nbr1 interacted with all these members of the mammalian atg8 protein family | SIGNOR-184261 |
Q14790 | P28482 | 0 | phosphorylation | down-regulates | 0.757 | We demonstrate that perk 1/2 can phosphorylate pro-caspase-8 at s387 by knocking-down the endogenous pro-caspase-8 using rnai and replacing it with its non-phosphorylatable counterpart (s387a), a significant increase in caspase-8 activity | SIGNOR-203473 |
P46531 | Q8NES3 | 0 | binding | up-regulates | 0.757 | We demonstrate that egf 12, a portion of the ligand-binding site, is modified with o-fucose and that this site is evolutionarily conserved. We also show that endogenous fringe proteins in chinese hamster ovary cells (lunatic fringe and radical fringe) as well as exogenous manic fringe modify o-fucose on many but not all egf repeats of mouse notch1. | SIGNOR-96537 |
O76064 | Q14676 | 0 | relocalization | up-regulates | 0.757 | Rnf8 relocalizes to dna damage sites via a phospho-dependent interaction with mdc1 | SIGNOR-179820 |
P21730 | P01031 | 0 | binding | up-regulates activity | 0.757 | The chemotactic receptor for human C5a anaphylatoxin|The human C5a receptor was cloned from U937 and HL-60 cells and identified by high affinity binding when expressed in COS-7 cells. | SIGNOR-263457 |
Q9BXW4 | Q9Y4P1 | 0 | cleavage | up-regulates activity | 0.757 | Human atg4 homologues cleave the carboxyl termini of the three human atg8 homologues, microtubule-associated protein light chain 3 (lc3), gabarap, and gate-16. | SIGNOR-125489 |
O15151 | Q93009 | 0 | deubiquitination | up-regulates | 0.757 | Subsequently, hausp was shown to deubiquitinate mdm2 and mdmx, thereby stabilizing these proteins. | SIGNOR-139453 |
Q9UM11 | Q9UKT4 | 0 | ubiquitination | down-regulates | 0.756 | Emi1 binds cdh1 and inhibits apc-cdh1 activity. | SIGNOR-113385 |
Q00987 | Q13315 | 0 | phosphorylation | down-regulates activity | 0.756 | Dephosphorylation stabilizes mdm2 and increases its affinity for p53, inducing p53 degredation. ;phosphorylated s260 and s395 ands260d and s395d mutant peptides inhibited binding of binding of a specific monoclonal antibody raised to mdm2. Phosphorylation of mdm2 regulates p53 degradation. | SIGNOR-94268 |
Q13416 | P24941 | 0 | phosphorylation | up-regulates | 0.756 | We also found that horc2p is phosphorylated in vitro by cyclin a/cdk2, specifically at residues thr116 and thr226. These data combined strongly suggest that skp2 promotes horc1p turnover and that the n-terminal domain of horc1p, containing most of the phosphorylation sites and overlapping with one of the skp2-interacting domains, is a regulatory element for horc1p stability. | SIGNOR-116364 |
Q9Y566 | Q9P1A6 | 0 | relocalization | up-regulates activity | 0.756 | 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-264589 |
O95486 | Q9NR31 | 0 | binding | up-regulates quantity | 0.756 | Biogenesis of COPII vesicles is initiated by the activation of the small guanosine triphosphate (GTP)-binding protein secretion-associated Ras-related protein 1 (Sar1) at specialized subdomains of the ER, called ER exit sites (ERES) or transitional ER (tER). Membrane-bound Sar1 then recruits the inner COPII coat subcomplex, the Sec23/24 heterodimer. | SIGNOR-265303 |
Q04721 | Q96JK9 | 0 | binding | up-regulates | 0.756 | We report here the cloning and characterization of two new genes, maml2 and maml3, that also function as transcriptional coactivators for notch receptors. | SIGNOR-94097 |
P15336 | Q15759 | 0 | phosphorylation | up-regulates | 0.756 | Our results indicate that atf-2 not only directly binds to smad3/4 hetero-oligomers but also that atf-2 is phosphorylated by tgf-beta signaling via tak1 and p38. The two pathways, smad and tak1, synergistically enhance the activity of atf-2 which acts as their common nuclear target | SIGNOR-65586 |
P04637 | Q15831 | 0 | phosphorylation | up-regulates | 0.756 | We show that lkb1 physically associates with p53 in the nucleus and directly or indirectly phosphorylates p53 ser15 (previously shown to be phosphorylated by amp-dependent kinase) and p53 ser392 | SIGNOR-150830 |
Q92529-2 | Q16620 | 0 | phosphorylation | up-regulates activity | 0.755 | We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo. | SIGNOR-273917 |
P12830 | P12931 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.755 | Activated c-Src phosphorylated E-cadherin at the tyrosine 797 site to initiate RNF43-mediated E-cadherin ubiquitination at lysine 816 and subsequent degradation | SIGNOR-274048 |
P78352 | Q9NZ94 | 0 | relocalization | up-regulates activity | 0.755 | Like NRXNs, NLGNs bind to intracellular PDZ-domain proteins, but in contrast to NRXNs, NLGNs bind to class I PDZ domains such as those contained in PSD95, a postsynaptic MAGUK protein65. PSD95 and its homologues are centrally involved in recruiting glutamate receptors at postsynaptic sites66. Similarly to CASK, PSD95 binds to intracellular adaptor proteins, and especially to GKAP (a protein that binds to the guanylate-kinase domain of PSD95), which, in turn, binds to SHANK proteins (Fig. 1b). A possible role of these interactions is to recruit postsynaptic adaptor proteins to the site of synaptic junctions. | SIGNOR-264189 |
P00451 | P00734 | 0 | cleavage | up-regulates activity | 0.755 | Activation of factor VIII by thrombin occurs via limited proteolysis at R372, R740, and R1689. | SIGNOR-263640 |
Q92529 | Q16620 | 0 | binding | up-regulates | 0.755 | Our present study established that n-shc and sck are expressed in a region-specific manner in the brain and that n-shc is a higher affinity adapter molecule than sck for trka and trkb receptors | SIGNOR-55864 |
O14920 | O43318 | 0 | phosphorylation | up-regulates activity | 0.755 | Tak1 become activated and then phosphorylates and activates ikk2 which in turn now phosphorylates ikba, marking it for k48-ubiquitination and proteasomal degradation. tak1 kinase complex phosphorylates and activates ikk in a manner that depends on traf6 and ubc13-uev1a our studies suggests that tak1_ acts as an upstream activating kinase for ikkbeta. | SIGNOR-109490 |
Q92889 | Q8IY92 | 0 | binding | up-regulates | 0.755 | Slx4 is a tumor suppressor that stimulates the activity of the nuclease xpf-ercc1 in dna crosslink repair. | SIGNOR-204890 |
Q9UDY8 | Q9Y4K3 | 0 | ubiquitination | up-regulates | 0.755 | Traf6 associates with malt1 in response to t-cell activation and can function as an e3 ligase for malt1 in vitro and in vivo, mediating lysine 63-linked ubiquitination of malt1. Multiple lysine residues in the c-terminus of malt1 serve as acceptor sites for the assembly of polyubiquitin chains. (articolo-abstract) | SIGNOR-158554 |
P61586 | Q8N1W1 | 0 | guanine nucleotide exchange factor | up-regulates activity | 0.755 | We therefore developed a screening-compatible live-cell imaging assay, using FRET-based biosensors for the prototype GTPases RHOA, RAC1 and CDC4215,19,20 (Extended Data Fig. 2 and Supplementary Note 1)|We found catalytic activities for 45/75 RhoGEFs and 48/63 RhoGAPs| Our data thus not only reveal extensive promiscuity among regulators, but also that the inactivating RhoGAPs are less selective than the activating RhoGEFs (p-value=0.02)(Supplementary Table 2). | SIGNOR-260546 |
O75581 | Q9H461 | 0 | binding | up-regulates activity | 0.755 | Ligands such as Wnt1, Wnt3a, and Wnt8 couple the seven-transmembrane domain receptor Frizzled (Fzd) and the single-membrane-spanning low-density receptor-related protein 5/6 (LRP5/6) to activate WntBeta-catenin signaling. | SIGNOR-169638 |
Q13094 | P06241 | 0 | phosphorylation | down-regulates | 0.755 | P59fyn_phosphorylated slp-76 at intermediate levels but, significantly, this phosphorylation failed to induce vav?SLP-76 complex formation | SIGNOR-46851 |
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