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 |
|---|---|---|---|---|---|---|---|
O60573 | Q9Y4X5 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.678 | Human homologue of Drosophila ariadne (HHARI) is a RING-IBR-RING domain protein identified through its ability to bind the human ubiquitin-conjugating enzyme, UbcH7. Thus, by promoting the ubiquitin-mediated degradation of 4EHP, HHARI may have a role in both protein degradation and protein translation. | SIGNOR-268848 |
O14733 | Q13387 | 0 | binding | up-regulates | 0.678 | Thus, both jip1 and jip2 selectively bind the mapkk isoform mkk7. | SIGNOR-59944 |
Q8WU20 | P07949 | 0 | binding | up-regulates | 0.678 | Tyrosine 1062 in ret provides a site for the interaction of multiple signaling molecules and that the balance of shc and snt/frs2 binding may affect the nature of the intracellular signaling for cell proliferation, differentiation and survival induced by activated ret | SIGNOR-108244 |
P38398 | P24941 | 0 | phosphorylation | up-regulates | 0.677 | However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. | SIGNOR-187607 |
P60953 | Q96HP0 | 0 | guanine nucleotide exchange factor | up-regulates activity | 0.677 | Dock6 is a guanine nucleotide exchange factor (GEF) that activates the Rho family guanosine triphosphatases Rac1 and Cdc42 to regulate the actin cytoskeleton. | SIGNOR-275671 |
O14543 | P42224 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.677 | Expression of SOCS1 and SOCS3 is regulated primarily by activation of STAT1 and STAT3, respectively, although their expression can be mediated through other signaling cascades, including the mitogen activated protein kinase (MAPK) and nuclear factor-kappa B (NF-kappaB) pathways. | SIGNOR-249565 |
P29353 | P43403 | 0 | phosphorylation | up-regulates | 0.677 | The syk-family kinases (syk and zap-70) were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site on shc1 (iso2). | SIGNOR-59659 |
P04637 | Q05655 | 0 | phosphorylation | up-regulates | 0.677 | Here, we show that the pro-apoptotic kinase, protein kinase c delta (pkcdelta), is involved in phosphorylation of p53 on ser(46). pkcdelta potentiates p53-dependent apoptosis by ser(46) phosphorylation in response to genotoxic stress. | SIGNOR-143382 |
P31749 | P12931 | 0 | phosphorylation | up-regulates activity | 0.677 | Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity. | SIGNOR-252623 |
Q9Y572 | Q13490 | 0 | polyubiquitination | up-regulates activity | 0.677 | CIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).Together, our results demonstrate that depleting cIAP1/2 inhibits RIP1-4 mediated NF-kB activation without affecting RIP auto-phosphorylation. | SIGNOR-272711 |
Q16611 | P10415 | 0 | binding | down-regulates | 0.677 | Bcl-2 bind to bax or five other pro-apoptotic relatives (bak, bad, bik, bid or bim) | SIGNOR-55546 |
Q92985 | P19474 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.677 | Furthermore, this Ro52 mediated degradation of IRF7 was inhibited in the presence of MG132, a proteasome inhibitor, indicating that IRF7 is targeted to the proteasome for degradation (XREF_FIG).|Ro52 ubiquitinates IRF7 in a dose dependent manner. | SIGNOR-278619 |
Q12933 | O75460 | 0 | binding | up-regulates activity | 0.677 | Activated IRE1 has been demonstrated to recruit TRAF2 and ASK1 on the ER membrane and thus to activate ASK1|ASK1 was found to associate with IRE1 only in the presence of TRAF2 and SOD1mut (Fig. 4B), suggesting that SOD1mut induces formation of an IRE1–TRAF2–ASK1 complex on the ER membrane and thus activates ASK1 by triggering ER stress-induced IRE1 activation. | SIGNOR-262790 |
Q96A54 | Q15848 | 0 | binding | up-regulates | 0.677 | Two adiponectin receptors, adipor1 and adipor2, have recently been identified. | SIGNOR-146170 |
Q00653 | Q99558 | 0 | phosphorylation | up-regulates activity | 0.677 | NIK-induced p100 processing requires phosphorylation of p100 at serines 866 and 870 | SIGNOR-105553 |
P38398 | O14965 | 0 | phosphorylation | up-regulates | 0.677 | Previous studies have shown that the brca1 breast cancer tumor suppressor also localizes to the centrosome and that brca1 inactivation results in loss of the g(2)-m checkpoint. We demonstrate here that aurora-a physically binds to and phosphorylates brca1. We propose that brca1 phosphorylation by aurora-a plays a role in g(2) to m transition of cell cycle | SIGNOR-123065 |
Q12933 | Q9NQC7 | 0 | deubiquitination | down-regulates activity | 0.677 | Cyld also interacts directly with tumour-necrosis factor receptor (tnfr)-associated factor 2 (traf2), an adaptor molecule involved in by members of the family of tnf/nerve growth factor receptors. (articolo-abstract) | SIGNOR-117860 |
Q15437 | Q9NR31 | 0 | binding | up-regulates quantity | 0.677 | 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-265298 |
P42229 | P18031 | 0 | dephosphorylation | down-regulates activity | 0.676 | A Cytosolic Protein-tyrosine Phosphatase PTP1B Specifically Dephosphorylates and Deactivates Prolactin-activated STAT5a and STAT5b | SIGNOR-248428 |
P51636 | P12931 | 0 | phosphorylation | down-regulates | 0.676 | Here, we show that cav-2 is phosphorylated at both tyrosines 19 and 27. We reconstituted this phosphorylation event by recombinantly coexpressing c-src and cav-2.Further functional analysis revealed that tyrosine phosphorylation of cav-2 has no effect on its targeting to lipid rafts, but clearly disrupts the hetero-oligomerization of cav-2 with cav-1. | SIGNOR-129961 |
P51692 | P18031 | 0 | dephosphorylation | down-regulates activity | 0.676 | A Cytosolic Protein-tyrosine Phosphatase PTP1B Specifically Dephosphorylates and Deactivates Prolactin-activated STAT5a and STAT5b | SIGNOR-248429 |
P0C0L5 | P48740 | 0 | cleavage | up-regulates activity | 0.676 | The classical complement activation pathway, like the MELinitiated pathway, involves the generation of a C3-converting complex, C4b2b, through enzymatic activation of C4 and C2. In the C1 complex (C1qr2s2), this specific protease activity is exhibited by C1s after activation of this enzyme by C1r. When C4 is activated, its reactive thiol ester is exposed and C4b binds covalently to nearby amino or hydroxyl groups. The C4-activating abilities of MASP-1 and MASP-2 were compared.|Activation of C4 by Ct sand MASP-2 on western blots. | SIGNOR-263426 |
O75581 | Q03135 | 0 | binding | up-regulates | 0.676 | Overall, our data suggest that wnt-3a triggers the interaction of lrp6 with caveolin and promotes recruitment of axin to lrp6 phosphorylated by glycogen synthase kinase-3beta and that caveolin thereby inhibits the binding of beta-catenin to axin. | SIGNOR-148665 |
P23458 | P40189 | 0 | null | up-regulates | 0.676 | Il-6 family members typically signal through the common gp130 receptor, with the janus kinase/signal transducer and activator of transcription (jak/stat) pathway being the major intracellular mediator of their effects. | SIGNOR-202036 |
P42701 | P29460 | 0 | binding | up-regulates | 0.676 | Characterization of the p40 proteins for binding and bioactivity showed that both the p40 monomer and dimer inhibited 125i-labeled il-12 binding to il-12r, but the 80-kda species, having a 50% inhibitory concentration (ic50) of 20 to 70 ng/ml, was at least 20-fold more effective than the monomer. The results suggest that the il-12 p40 subunit contains the essential epitopes for receptor binding. | SIGNOR-27690 |
Q9Y6H5 | Q8IUQ4 | 0 | ubiquitination | down-regulates | 0.676 | Siah proteins ubiquitylate synphilin-1 and promote its degradation through the ubiquitin proteasome system | SIGNOR-140612 |
P14138 | P23276 | 0 | cleavage | up-regulates activity | 0.676 | These data demonstrate that the Kell blood group protein is a proteolytic enzyme that processes big ET-3, generating ET-3, a potent bioactive peptide with multiple biological roles. | SIGNOR-256354 |
Q14765 | O60674 | 0 | phosphorylation | up-regulates | 0.676 | Janus family tyrosine kinases jak2 and tyk2, which in turn phosphorylate stat4 on tyrosine 693. The p38 mitogen-activated protein kinase (mapk) signaling pathway is also activated in response to il-12, followed by phosphorylation of stat4 on serine 721, which is required for stat4 full transcriptional activity | SIGNOR-142736 |
P49023 | P45983 | 0 | phosphorylation | up-regulates activity | 0.676 | JNK1 phosphorylates serine 178 on paxillin, a focal adhesion adaptor, both in vitro and in intact cells. NBT-II cells expressing the Ser 178 --> Ala mutant of paxillin (Pax(S178A)) formed focal adhesions and exhibited the limited movement associated with such contacts in both single-cell-migration and wound-healing assays. In contrast, cells expressing wild-type paxillin moved rapidly and retained close contacts as the predominant adhesion. | SIGNOR-250129 |
Q13485 | P05412 | 0 | binding | up-regulates activity | 0.676 | Our analysis of the regulation of dpc4 transcriptional activity by c-jun was consistent with the possibility that c-jun and dpc4 could interact and produce trans-activation of the 3tp-lux reporter. | SIGNOR-236139 |
P84022 | Q92831 | 0 | binding | up-regulates | 0.676 | P/caf was found to interact directly with smad3 in vitro. Moreover, smad2 and smad3 interacted with p/caf upon tgf-beta type i receptor activation in cultured mammalian cells. these results demonstrate the co-activator function of p/caf for smad2 and smad3. | SIGNOR-83607 |
P19174 | P35968 | 0 | binding | up-regulates | 0.675 | (vegfr) phosphorylated y1175 creates a binding site for phospholipase cgamma1 (plc-gamma1) | SIGNOR-147870 |
P48551 | P01574 | 0 | binding | up-regulates | 0.675 | 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-105934 |
Q13813 | P42574 | 0 | cleavage | down-regulates | 0.675 | Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. | SIGNOR-57891 |
P29353 | Q05209 | 0 | dephosphorylation | down-regulates | 0.675 | The shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (y239/240) that mediate protein-protein interactions. | SIGNOR-44361 |
Q13485 | Q99717 | 0 | phosphorylation | up-regulates | 0.675 | Whereas alk5 signalling is mediated by phosphorylation of smad2 and smad3 proteins, alk1 signalling is mediated by smad1, smad5, and smad8. Activated smads form a complex with the common smad (co-smad; smad4 in mammals) and shuttle into the nucleus. | SIGNOR-168737 |
P61586 | Q8N5V2 | 0 | guanine nucleotide exchange factor | up-regulates activity | 0.675 | 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-260562 |
Q96B36 | P31751 | 0 | phosphorylation | down-regulates | 0.674 | Insulin-stimulated phosphorylation of pras40 by akt/pkb suppresses its mtorc1 inhibitory activity. | SIGNOR-153931 |
O75197 | P56706 | 0 | binding | up-regulates | 0.674 | 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-131981 |
P29353 | Q05397 | 0 | phosphorylation | up-regulates activity | 0.674 | In vitro, FAK directly phosphorylated Shc Tyr-317 to promote Grb2 binding. FAK can associate and directly phosphorylate Shc at Tyr-317 to promote Grb2 binding and low-level signaling to ERK2. | SIGNOR-259854 |
Q13480 | P08581 | 0 | phosphorylation | up-regulates activity | 0.674 | Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. | SIGNOR-250290 |
P42226 | Q9UHD2 | 0 | phosphorylation | up-regulates | 0.674 | We now show that stat6 is required for innate immune signaling in response to virus infection. Viruses or cytoplasmic nucleic acids trigger sting (also named mita/eris) to recruit stat6 to the endoplasmic reticulum, leading to stat6 phosphorylation on ser(407) by tbk1 and tyr(641), independent of jaks. Phosphorylated stat6 then dimerizes and translocates to the nucleus to induce specific target genes responsible for immune cell homing. | SIGNOR-176775 |
Q16526 | Q9UNS1 | 0 | binding | up-regulates activity | 0.674 | We performed a detailed molecular characterization of TIM interactions with the core clock protein CRY1 and the DNA damage signal transducer CHK1, and found that the N-terminus of TIM is required for association with both proteins, as well as for homodimerization. | SIGNOR-268053 |
P35372 | P01213 | 0 | chemical activation | up-regulates activity | 0.674 | Accordingly, for the OTDP, the binding affinity and activity of a large number of opiate compounds have been tested at μ-, δ-, and κ-opiate receptors. Binding studies were originally conducted in guinea pig brain membranes, and subsequent studies have been carried out in CHO cells transfected with human receptors. Table 7 shows a biochemical method for determining activity and potency of opioid compounds, stimulation of [35S]GTPγS binding in membranes from cells transfected with human μ, δ, or κ receptors. | SIGNOR-258414 |
P15260 | O15524 | 0 | binding | down-regulates | 0.674 | Suppressor of cytokine signaling (socs)-1, the key negative regulator of interferon (ifn)-gamma-dependent signaling, is induced in response to ifngamma. Socs-1 binds to and inhibits the ifngamma receptor-associated kinase janus-activated kinase (jak) 2 and inhibits its function in vitrothe binding of socs-1 to tyr441 also blocks the access of stat1 to tyr419 and that this effect may be the principal mechanism of inhibition of downstream signaling | SIGNOR-180140 |
Q08379 | P06493 | 0 | phosphorylation | down-regulates | 0.674 | Cdc2 kinase directly phosphorylates the cis-golgi matrix protein gm130 and is required for golgi fragmentation in mitosis. Mitotic fragmentation of the golgi apparatus can be largely explained by disruption of the interaction between gm130 and the vesicle-docking protein p115. Here we identify a single serine (ser-25) in gm130 as the key phosphorylated target and cdc2 as the responsible kinase | SIGNOR-60281 |
O14793 | O95633 | 0 | binding | down-regulates | 0.674 | Fstl3 inhibits myostatin via its n-terminal domain. | SIGNOR-199063 |
Q12772 | O43462 | 0 | cleavage | up-regulates activity | 0.673 | In order to activate transcription, the NH2-terminal domain of the SREBP must be released from the membrane so that it can enter the nucleus. This release has been studied most extensively for one of the SREBPs, namely, SREBP-2. However, the mechanism appears to be similar for the other SREBPs (SREBP-1a and -1c) (1). Release of the NH2-terminal domain is accomplished by a two-step proteolytic event that is regulated by sterols (3). In sterol-depleted mammalian cells, this proteolysis is initiated by the Site-1 protease (S1P), which cleaves human SREBP-2 between the Leu522-Ser523 bond in the sequence RSVL S (4). This cleavage requires formation of a complex between SREBP and SCAP, a polytopic membrane protein of the ER, and it is prevented when this complex is disrupted | SIGNOR-267498 |
Q9BXW9 | Q13535 | 0 | phosphorylation | up-regulates | 0.673 | In the present study, we identify two novel dna damage-inducible phosphorylation sites on fancd2, threonine 691 and serine 717. Atr phosphorylates fancd2 on these two sites, thereby promoting fancd2 monoubiquitination and enhancing cellular resistance to dna cross-linking agents | SIGNOR-149305 |
P01111 | Q06124 | 0 | dephosphorylation | up-regulates activity | 0.673 | Here we identify SHP2 as the ubiquitously expressed tyrosine phosphatase that preferentially binds to and dephosphorylates Ras to increase its association with Raf and activate downstream proliferative Ras/ERK/MAPK signalling. | SIGNOR-255754 |
O00422 | Q9UMX1 | 0 | binding | up-regulates | 0.673 | Here we report that the mouse homolog of su(fu) [msu(fu)] specifically interacts with sap18, a component of the msin3 and histone deacetylase complex. In addition, we demonstrate that msu(fu) functionally cooperates with sap18 to repress transcription by recruiting the sap18-msin3 complex to promoters containing the gli-binding element. | SIGNOR-117311 |
O14746 | Q9NUX5 | 0 | binding | up-regulates | 0.673 | We find that tpp1 and pot1 form a complex with telomeric dna that increases the activity and processivity of the human telomerase core enzyme. | SIGNOR-152327 |
Q07955 | P49759 | 0 | phosphorylation | up-regulates activity | 0.673 | In a previous study, we showed that CLK1 phosphorylates SRSF1 to a greater extent than SRPK1, inducing a hyper-phosphorylated state that can be readily detected by a gel shift on SDS-PAGE. xref In xref , the phosphorylation of SRSF1 in single turnover experiments using SRPK1 and CLK1 is shown.|Unlike SRPK1, CLK1 induces a unique structural form of SRSF1 observed by SDS-PAGE that is exclusively the result of Ser-Pro rather than Arg-Ser phosphorylation. | SIGNOR-279608 |
P07585 | P08254 | 0 | cleavage | down-regulates quantity by destabilization | 0.673 | Degradation of decorin by matrix metalloproteinases. These data indicate proteolytic degradation of DCN by MMP-2, MMP-3 and MMP-7, and suggest the possibility that, under pathophysiological conditions, the digestion by the MMPs may induce tissue reactions mediated by TGF-beta1 released from DCN in the connective tissues. | SIGNOR-256353 |
O75581 | P09544 | 0 | binding | up-regulates | 0.673 | 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-131730 |
P08151 | Q6PHR2 | 0 | phosphorylation | up-regulates activity | 0.673 | We show that ULK3 is able to phosphorylate three mammalian GLI proteins in vitro. | Our data suggest that serine/threonine kinase ULK3 is involved in the SHH pathway as a positive regulator of GLI proteins. | SIGNOR-260797 |
O00451 | P39905 | 0 | binding | up-regulates | 0.673 | Gdnf mediates its actions through a multicomponent receptor system composed of a ligand-binding glycosyl-phosphatidylinositol (gpi)-linked protein (designated gdnfr-alpha). | SIGNOR-49184 |
P12318 | P43405 | 0 | phosphorylation | up-regulates activity | 0.673 | To identify the FcgammaRII-phosphorylating protein tyrosine kinase (PTK), we used the combination of an in vitro and an in vivo approach. In an in vitro assay using recombinant cytoplasmic tails of the different FcgammaRII isoforms as well as tyrosine exchange mutants, we show that each of the BCR-associated PTKs (Lyn, Blk, Fyn, and Syk) shows different phosphorylation patterns with regard to the different FcgammaR isoforms and pointFyn and Blk definitely phosphorylate Y-282 in the ITAM of Fc_RIIa/c, whereas the non-ITAM tyrosine residue (Y-275) becomes phosphorylated by Syk, as the phosphorylation of double point mutants shows. In addi-tion to these tyrosine residues, Fyn, Blk, and Syk might phosphorylate the most C-terminal tyrosine residue (Y-298) because altering this tyrosine residue together with one of the tyrosine residues clearly shown to be phosphorylated by the respective PTK results in the abrogation of phosphorylation. | SIGNOR-247590 |
Q00987 | Q9UER7 | 0 | binding | up-regulates | 0.673 | The optimal function of mdm2 requires daxx, which stabilizes mdm2 through the deubiquitinase hausp/usp7 and also directly promotes mdm2's ubiquitin ligase activity towards p53. | SIGNOR-200892 |
Q99836 | O60603 | 0 | binding | up-regulates activity | 0.673 | To initiate the innate immune response, Toll-like receptors (TLRs) associate with cytoplasmic adaptor proteins through TIR (Toll/interleukin-1 receptor) domain interactions. The four principal signaling adaptor proteins include MyD88, MAL, TRIF and TRAM, and the fifth protein SARM, involved in negative regulation of TLR pathways, is usually considered a part of the TIR domain-containing adaptor protein group | SIGNOR-266740 |
P17275 | P45984 | 0 | binding | down-regulates | 0.673 | Jnk targets junb ubiquitination | SIGNOR-53827 |
P60953 | Q2M1Z3 | 0 | gtpase-activating protein | down-regulates activity | 0.673 | 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-260490 |
P22455 | P08620 | 0 | binding | up-regulates | 0.672 | Our results establish an fgf binding profile for fgfr-4 with afgf having the highest affinity, followed by k-fgf/hst-1 and bfgf. In addition, fgf-6 was found to bind to fgfr-4 in ligand competition experiments. Ligands binding to fgfr-4 induced receptor autophosphorylation and phosphorylation of a set of cellular polypeptides. | SIGNOR-18567 |
O60353 | O96014 | 0 | binding | up-regulates activity | 0.672 | Human wnt5a, wnt5b and wnt11 are non-canonical wnt ligands transducing pcp signals through fzd3 or fzd6 receptors. | SIGNOR-141431 |
P40259 | P06241 | 0 | phosphorylation | up-regulates activity | 0.672 | CD79b cytoplasmic tail-containing GST fusion proteins were phosphorylated in vitro by baculovirus-produced Fyn, >80% of phosphorylation occurred on the N-terminal ITAM tyrosine. CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM). pY195 and pY206 in CD79b | SIGNOR-251154 |
Q9BUB5 | Q16539 | 0 | phosphorylation | up-regulates | 0.672 | Mnk1, but not mnk2, also binds strongly to the stress-activated kinase, p38. | SIGNOR-48346 |
Q14653 | Q12899 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.672 | TRIM26 bound to IRF3 and promoted its K48-linked polyubiquitination and degradation in nucleus. | SIGNOR-272440 |
Q16543 | P53041 | 0 | dephosphorylation | down-regulates activity | 0.672 | Activation of protein kinase clients by the Hsp90 system is mediated by the cochaperone protein Cdc37. Cdc37 requires phosphorylation at Ser13|PP5/Ppt1 regulates phosphorylation of Ser13-Cdc37 in vivo, directly affecting activation of protein kinase clients by Hsp90-Cdc37. | SIGNOR-248539 |
P13569 | P11142 | 0 | binding | down-regulates quantity | 0.672 | JB12 cooperates with cytosolic Hsc70 and the ubiquitin ligase RMA1 to target CFTR and CFTRΔF508 for degradation. JB12 drives Hsc70 to associate with CFTR and the RMA1 E3 complex | SIGNOR-271492 |
Q9UN19 | Q06187 | 0 | phosphorylation | up-regulates activity | 0.672 | We present a number of lines of evidence that in vivo, Src-type tyrosine kinases are responsible for the phosphorylation of tyrosine 139 in DAPP-1. | Although Btk appears to phosphorylate DAPP-1 relatively efficiently both in Sf9 cells and in vitro, we find no evidence that in either B cells or PAE cells Btk family kinases phosphorylate DAPP-1. | SIGNOR-250602 |
P14921 | P27361 | 0 | phosphorylation | up-regulates | 0.672 | We found that hgf/sf activates the erk1 map kinase, leading to the phosphorylation of the threonine 38 residue of ets1 | SIGNOR-116494 |
Q13618 | Q9H2C0 | 0 | binding | up-regulates activity | 0.672 | Gigaxonin is the substrate-specific adaptor for a new Cul3-E3-ubiquitin ligase family that promotes the proteasome dependent degradation of its partners MAP1B, MAP8 and tubulin cofactor B. | SIGNOR-268944 |
P28482 | P51452 | 0 | dephosphorylation | down-regulates activity | 0.672 | 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.|Catalysis by VHR requires the native structure of ERK and is specific for tyrosine 185 of ERK2 | SIGNOR-248536 |
P48740 | O75636 | 0 | binding | up-regulates activity | 0.672 | H-ficolin binds to PSA, a polysaccharide produced by Aerococcus viridans. C4 was activated by H-ficolin preparations bound to PSA which had been coated on ELISA plates. These results indicate that H-ficolin is a second ficolin which is associated with MASPs and sMAP, and which activates the lectin pathway|Proteolytic activation of complement components by H-ficolin-MASP. | SIGNOR-263410 |
P38936 | P45983 | 0 | phosphorylation | up-regulates quantity by stabilization | 0.672 | The stress-activated protein kinases p38 alpha and jnk1 stabilize p21(cip1) by phosphorylation.|p38 alpha and JNK1 phosphorylated p21 in vivo, and both p38 alpha and JNK1 phosphorylated p21 at Ser(130) in vitro. | SIGNOR-89440 |
P35222 | P45984 | 0 | phosphorylation | up-regulates | 0.671 | Beta-catenin, upon entering the nucleus, in turn activates transcription of downstream target genes. Jnk2 phosphorylates Beta-catenin on critical residues (ser191 and ser605). Jnk activity is required for Beta-catenin nuclear localization in response to wnt. | SIGNOR-178258 |
Q13541 | O75582 | 0 | phosphorylation | down-regulates activity | 0.671 | In response to UV-B irradiation, the translation factor 4E-BP1 (eukaryotic initiation factor 4E [eIF4E]-binding protein 1) was phosphorylated at Thr36, Thr45, Ser64 and Thr69. Using either p38 MAPK inhibitors or the MSK inhibitor H89, UV-B-irradiation-induced phosphorylation was blocked [43]. 4E-BP1 binds to eIF4E in resting cells to prevent formation of a functional eIF4F complex, which is essential for cap-dependent initiation of translation. Phosphorylation of 4E-BP1 leads to dissociation from eIF4E | SIGNOR-262992 |
P10071 | Q9Y297 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.671 | Third, we and others have recently shown that only phosphorylated Ci/Gli3 are able to directly bind Slimb/BetaTrCP, that Gli3 is polyubiquitinated in the cell, and that mutations of 4 lysine residues, the putative ubiquitination sites in the Gli3 C-terminal region, inhibit Gli3 processing These observations further support the notion that Ci/Gli3 processing is carried out by the proteasome because the deletion of the cleavage site is expected to often disrupt the protease-mediated site-specific cleavage. | SIGNOR-145116 |
P03372 | P28482 | 0 | phosphorylation | up-regulates | 0.671 | In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo. | SIGNOR-156856 |
P04637 | Q86XK2 | 0 | neddylation | down-regulates | 0.671 | Fbxo11 promotes the neddylation of p53 and inhibits its transcriptional activity / we found that fbxo11 also neddylates p53 on two lysines, lys-320 and lys-321 | SIGNOR-150669 |
P04626 | Q99952 | 0 | dephosphorylation | down-regulates quantity by destabilization | 0.671 | PTPN18 knockdown selectively enhances the EGF-induced tyrosine phosphorylation of the HER2 Y1112, Y1196 and Y1248 sites. |Whereas the catalytic domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation of HER2 on pY(1112), the PEST domain of PTPN18 promotes K48-linked HER2 ubiquitination and its rapid destruction via the proteasome pathway and an HER2 negative feedback loop. | SIGNOR-262596 |
O00327 | P20393 | 0 | transcriptional regulation | down-regulates quantity by repression | 0.671 | In this study, we found that NPAS2, like BMAL1, is a direct target gene of RORα and REV-ERBα. it appears in the context of the NPAS2 promoter RORα functions as a transcriptional activator, but REV-ERBα may only function as an inhibitor of RORα activity by blocking binding. | SIGNOR-267983 |
Q13905 | P12931 | 0 | phosphorylation | up-regulates | 0.671 | C3g is activated upon phosphorylation at tyrosine 504 c3g is phosphorylated in vivo on y504 upon coexpression with src or hck, two members of the src family tyrosine kinases. | SIGNOR-128273 |
P42224 | P22607 | 0 | phosphorylation | up-regulates activity | 0.671 | Activation of Stat1 and Stat3 by FGFR derivatives. Lysates of 293T cells transfected as indicated were analysed by Western blotting using Phospho-Stat1 (Y701) antisera (top) or Stat1 antisera (bottom). (b) The same lysates in (a) were re-examined for phosphorylated Stat3 by Western blotting with Phospho-Stat3 (Y705) (top). all three FGFR family members examined here are able to lead to Stat activation. Expression of the 'TDII-like' derivatives of FGFR1, FGFR3, and FGFR4, as well as myrR1-WT, led to phosphorylation of both Stat1 and Stat3. | SIGNOR-251138 |
O95786 | Q96EQ8 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.671 | Here, we found that RIG-I undergoes proteasomal degradation after conjugation to ubiquitin by RNF125. Further, RNF125 conjugates ubiquitin to MDA5, a family protein of RIG-I as well as IPS-1, which is also a downstream protein of RIG-I signaling that results in suppressing the functions of these proteins. Because RNF125 is enhanced by IFN, these functions constitute a negative regulatory loop circuit for IFN production. | SIGNOR-271647 |
P0CG47 | Q96BN8 | 0 | cleavage | up-regulates quantity | 0.671 | Here we provide data suggesting that two of the four mammalian ubiquitin precursors, UBA52 and UBA80, are processed mostly post-translationally whereas the other two, UBB and UBC, probably undergo a combination of co- and post-translational processing. Using an unbiased biochemical approach we found that UCHL3, USP9X, USP7, USP5 and Otulin/Gumby/FAM105b are by far the most active DUBs acting on these precursors. | SIGNOR-270819 |
P31749 | O95988 | 0 | binding | up-regulates | 0.671 | In vivo, tcl1 forms trimers, which associate with akt. Tcl1 facilitates the oligomerization and activation of akt. Our data show that tcl1 is a novel akt kinase coactivator, which promotes akt-induced cell survival and proliferation. | SIGNOR-81713 |
Q9Y2T1 | Q9NTX7 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.671 | Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling. RNF146 promotes Wnt signalling by mediating tankyrase-dependent degradation of axin. Mechanistically, RNF146 directly interacts with poly(ADP-ribose) through its WWE domain, and promotes degradation of PARsylated proteins. Using proteomics approaches, we have identified BLZF1 and CASC3 as further substrates targeted by tankyrase and RNF146 for degradation. | SIGNOR-263336 |
Q13485 | Q15797 | 0 | phosphorylation | up-regulates | 0.671 | Whereas alk5 signalling is mediated by phosphorylation of smad2 and smad3 proteins, alk1 signalling is mediated by smad1, smad5, and smad8. Activated smads form a complex with the common(co-Smad; Smad4 in mammals) and shuttle into the nucleus. | SIGNOR-168734 |
Q9Y6R1 | O43865 | 0 | binding | up-regulates activity | 0.671 | IRBIT opposed the effects of WNKs and SPAK by recruiting PP1 to the complex to dephosphorylate CFTR and NBCe1-B, restoring their cell surface expression, in addition to stimulating their activities. | SIGNOR-263135 |
P04637 | Q92630 | 0 | phosphorylation | up-regulates | 0.67 | Here, we demonstrate that the dual-specificity tyrosine-phosphorylation-regulated kinase 2 (dyrk2) directly phosphorylates p53 at ser46. these findings indicate that dyrk2 regulates p53 to induce apoptosis in response to dna damage. | SIGNOR-153544 |
P42226 | O60674 | 0 | phosphorylation | up-regulates activity | 0.67 | Downstream intracellular signaling from the IL-4IL-4Rc complex involves activation of the Jak1 and Jak3 kinases, phosphorylation of the Stat6 transcription factor, and activation of the insulin receptor substrate (IRS)-2 and Dok2-signaling intermediates. IL-13 initially binds to IL-13R1 with intermediate affinity, and then heterodimerizes with IL-4R. The IL-13IL-13R1IL-4R complex activates the Tyk2, Jak2, and Jak1 kinases and Stat6. | SIGNOR-249532 |
O14920 | O15111 | 0 | phosphorylation | up-regulates activity | 0.67 | Our data indicate that IKKα stimulates IKKβ kinase activity for the IκBα substrate. Finally, we demonstrate that IKKα can phosphorylate IKKβ in in vitro kinase assays. | SIGNOR-250772 |
P46734 | Q9UL54 | 0 | binding | up-regulates activity | 0.67 | Cotransfection experiments suggested that tao2 selectively activates mek3 and mek6 but not meks 1, 4, or 7. | SIGNOR-70947 |
Q15256 | P27361 | 0 | phosphorylation | up-regulates activity | 0.67 | Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. | SIGNOR-249477 |
P10451 | P08254 | 0 | cleavage | up-regulates activity | 0.67 | In this study, we found a novel motif, LRSKSRSFQVSDEQY, in the C-terminal fragment of MMP-3/7-cleaved mouse OPN binds to α9β1 integrin. Importantly, this novel motif is involved in the development of anti-type II collagen antibody-induced arthritis (CAIA). This study provides the first in vitro and in vivo evidence that OPN cleavage by MMP-3/7 is an important regulatory mechanism for CAIA. | SIGNOR-253320 |
P27986 | P06213 | 0 | phosphorylation | up-regulates activity | 0.67 | The alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase is phosphorylated at tyrosines 368, 580, and 607 by the insulin receptor. | SIGNOR-251321 |
P04637 | Q92794 | 0 | acetylation | up-regulates | 0.67 | We show here that moz is an acetyltransferase of p53 at k120 and k382 and colocalizes with p53 in promyelocytic leukemia (pml) nuclear bodies following cellular stress. The moz-pml-p53 interaction enhances moz-mediated acetylation of p53, and this ternary complex enhances p53-dependent p21 expression | SIGNOR-201486 |
O43933 | Q13608 | 0 | binding | up-regulates activity | 0.67 | Pex26 recruits Pex6–Pex1 complexes to peroxisomes. Pex26 anchors Pex6 and Pex1 through Pex26–Pex6 and Pex6–Pex1 interactions. | SIGNOR-253615 |
P21860 | P00533 | 0 | phosphorylation | up-regulates | 0.67 | The erbb3 protein which possesses little or no intrinsic protein tyrosine kinase activiity is phosphorylated by the activated egf receptor protein tyrosine kinase on tyrosine residues within the yxxm sequence motif. These phosphorylated tyrosine residues interact with the p85 regulatory subunit of pi 3-kinase, which could result in the activation of the p110 catalytic subunit via a conformational mechanism. | SIGNOR-34748 |
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