IdA string | IdB string | labels int64 | mechanism string | effect string | score float64 | sentence string | signor_id string |
|---|---|---|---|---|---|---|---|
O43597 | Q13627 | 0 | phosphorylation | down-regulates | 0.304 | We identify dyrk1a as one of the protein kinases of sprouty2. We show that dyrk1a interacts with and regulates the phosphorylation status of sprouty2. Moreover, we identify thr75 on sprouty2 as a dyrk1a phosphorylation site in vitro and in vivo. | SIGNOR-179828 |
Q02156 | O94925 | 1 | phosphorylation | up-regulates activity | 0.2 | PKCε is the kinase that phosphorylates GAC at Ser314. | SIGNOR-277387 |
O75688 | O14920 | 1 | dephosphorylation | down-regulates activity | 0.404 | PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation|Overexpression of PPM1A or PPM1B results in dephosphorylation of IKKbeta at Ser177 and Ser181 and termination of IKKbeta-induced NF-kappaB activation. | SIGNOR-248343 |
P15336 | P28482 | 0 | phosphorylation | up-regulates | 0.733 | Here, we show that in fibroblasts, insulin, epidermal growth factor (egf) and serum activate atf2 via a so far unknown two-step mechanism involving two distinct ras effector pathways: the raf-mek-erk pathway induces phosphorylation of atf2 thr71, whereas subsequent atf2 thr69 phosphorylation requires the ral-ralgds-src-p38 pathway. | SIGNOR-90517 |
P17252 | P48050 | 1 | phosphorylation | down-regulates activity | 0.2 | These results therefore indicate that Kir2.3 is directly modulated by PKC phosphorylation of its channel protein and threonine 53 is the PKC phosphorylation site in Kir2.3. | SIGNOR-275965 |
P30291 | P63151 | 0 | dephosphorylation | up-regulates quantity by stabilization | 0.385 | Knockout of FAM122A results in activation of PP2A-B55α, a phosphatase that dephosphorylates the WEE1 protein and rescues WEE1 from ubiquitin-mediated degradation. in tumor cells with oncogene-driven replication stress, CHK1 can directly phosphorylate FAM122A, leading to activation of the PP2A-B55α phosphatase and increased WEE1 expression. | SIGNOR-266381 |
P08581 | P23470 | 0 | dephosphorylation | down-regulates activity | 0.317 | PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. | SIGNOR-254712 |
Q9P0L2 | P27816 | 1 | phosphorylation | down-regulates activity | 0.437 | Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. | SIGNOR-250171 |
P56524 | P12830 | 1 | transcriptional regulation | down-regulates quantity by repression | 0.287 | GATA1 is a new substrate of p21-activated kinase 5 (PAK5), which is phosphorylated on serine 161 and 187 (S161 and S187). GATA1 recruits HDAC3/4 to E-cadherin promoter, which is reduced by GATA1 S161A S187A mutant. These data indicate that phosphorylated GATA1 recruits more HDAC3/4 to promote transcriptional repression of E-cadherin, leading to the EMT of breast cancer cells. | SIGNOR-275663 |
Q9NRC8 | Q16695 | 1 | deacetylation | up-regulates activity | 0.2 | Besides confirming the previously reported histone H3K18 deacylation activity, our results revealed that SIRT7 has an astonishingly high activity to catalyze deacylation of H3K36 and is also catalytically active to deacylate H3K37. | SIGNOR-275876 |
P58753 | Q9NWF9 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.387 | Triad3A promotes proteolytic degradation of adapter proteins. A, Triad3A promotes down-regulation of TIRAP, TRIF, and RIP1 proteins. | SIGNOR-271607 |
O96017 | Q9NQS7 | 1 | phosphorylation | up-regulates activity | 0.261 | Also, inhibition of Chk2 by Chk2 inhibitor II in cytokinesis after release of cells from a nocodazole-induced prometaphase block diminished INCENP localization to the midbody center in late midbodies (Fig. 1, M and N).|In turn, active Chk2 phosphorylates human INCENP at the newly identified site Ser91 to promote INCENP binding to Mklp2, resulting in recruitment of the INCENP\u2013Mklp2 complex to the midbody center through Mklp2\u2019s interaction with the midbody protein Cep55 to delay abscission. | SIGNOR-279695 |
Q14790 | P42574 | 1 | cleavage | up-regulates activity | 0.726 | Triggering of the DISC leads to caspase-8 activation. Active caspase-8 cleaves caspase-3 which, in type I cells, leads to cell death induction. | SIGNOR-171767 |
Q09472 | Q6DJT9 | 1 | acetylation | up-regulates | 0.308 | Plag1 and plagl2 are also regulated by acetylation. They are acetylated and activated by p300 and deacetylated and repressed by hdac7. | SIGNOR-140915 |
P78536 | P01375 | 1 | cleavage | up-regulates quantity | 0.704 | We have now purified and cloned a metalloproteinase that specifically cleaves precursor TNF-alpha. [...]This enzyme (called the tnf-alpha-converting enzyme, or tace) is a new member of the family of mammalian adamalysins (or adams), for which no physiological catalytic function has previously been identified. | SIGNOR-46754 |
Q9NVD7 | P28482 | 0 | phosphorylation | up-regulates activity | 0.259 | Actopaxin (alpha-parvin) is a paxillin, integrin-linked kinase, and F-actin binding focal adhesion protein with several serine phosphorylation sites in the amino terminus that contribute to the regulation of cell spreading and migration.|Actopaxin phosphorylation of Ser4/8 enhances cell migration whereas a nonphosphorylatable (Quint) mutant suppresses migration in U2OS osteosarcoma cells (7). | SIGNOR-265759 |
O15105 | Q9H0M0 | 0 | relocalization | up-regulates activity | 0.731 | We found that WWP1 inhibited transcriptional activities induced by TGF-beta. Similar to Smurfs, WWP1 associated with Smad7 and induced its nuclear export, and enhanced binding of Smad7 to TGF-beta type I receptor to cause ubiquitination and degradation of the receptor. | SIGNOR-126578 |
Q8TCS8 | P78527 | 0 | phosphorylation | up-regulates activity | 0.2 | We also demonstrated that DNAPK phosphorylates PNPase at Ser-776, which is critical for its ribonuclease activity. | SIGNOR-263182 |
Q9Y478 | Q13131 | 0 | phosphorylation | up-regulates | 0.925 | Mutation of serine 108 to alanine, an autophosphorylation site within the glycogen binding domain of the beta1 subunit, almost completely abolishes activation of ampk by a-769662 in cells and in vitro, while only partially reducing activation by amp | SIGNOR-157553 |
Q8TEW0 | Q05513 | 0 | phosphorylation | up-regulates | 0.711 | These results imply that serine 827 in the apkc binding site of par-3 is a target of apkc and that the regulated interaction between a protein kinase, apkc, and its substrate, par-3, plays an essential role in the establishment of cell polarity | SIGNOR-94523 |
P17480 | P28482 | 0 | phosphorylation | down-regulates | 0.394 | Erk1/2 was found to phosphorylate the architectural transcription factor ubf at amino acids 117 and 201 within hmg boxes 1 and 2, preventing their interaction with dna | SIGNOR-112809 |
P23771 | Q99717 | 0 | transcriptional regulation | up-regulates quantity | 0.31 | Chromatin immunoprecipitation (ChIP) revealed a subset of the BIG (BMP4 induced genes) signature, including Satb2, Smad6, Hand1, Gadd45γ and Gata3, that was bound by Smad1/5 in the developing mandible, revealing direct Smad-mediated regulation | SIGNOR-268943 |
Q8N2W9 | Q05513 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.519 | In this study, we discovered a new protein isoform encoded by KIAA0317, termed fibrosis-inducing E3 ligase 1 (FIEL1), which potently stimulates the TGFbeta signaling pathway through the site-specific ubiquitination of PIAS4.FIEL1 targets PIAS4 using a double locking mechanism that is facilitated by the kinases PKCzeta and GSK3beta. Specifically, PKCzeta phosphorylation of PIAS4 and GSK3beta phosphorylation of FIEL1 are both essential for the degradation of PIAS4.|These experiments suggested that PKCzeta is an authentic regulator of PIAS4 protein stability; Q21 and phosphorylated S18 of PIAS4 are both required for FIEL1 interaction. | SIGNOR-275513 |
Q9H2X6 | P26367 | 1 | phosphorylation | up-regulates activity | 0.463 | HIPK2 phosphorylates the activation domain of Pax6, which augments Pax6 transactivation by enhancing its interaction with p300. Mass spectrometric analysis identified three Pax6 phosphorylation sites as threonines 281, 304, and 373. | SIGNOR-251271 |
Q9UNZ2 | P06493 | 0 | phosphorylation | down-regulates activity | 0.325 | Now, we have found that p47, which mainly localizes to the nucleus during interphase, is phosphorylated on serine-140 by cdc2 at mitosis. The phosphorylated p47 does not bind to golgi membranes. | SIGNOR-102350 |
Q9UPX8 | Q9Y2H0 | 0 | relocalization | up-regulates activity | 0.744 | 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-264596 |
O14773 | O76064 | 0 | ubiquitination | up-regulates activity | 0.302 | Our data demonstrate that RNF8 directly ubiquitylates and stabilizes TPP1 at telomeres.|Taken together, these results suggest that RNF8 dependent K63 linked, but not K48 linked ubiquitin chain formation on TPP1 is required to promote TPP1 stability and function at telomeres. | SIGNOR-278574 |
P60709 | O95631 | 0 | post transcriptional regulation | up-regulates quantity | 0.28 | Netrin-1 induces β-actin translation driven by its 3’UTR. | SIGNOR-268161 |
P68400 | Q92769 | 1 | phosphorylation | up-regulates | 0.619 | Protein kinase ck2-mediated phosphorylation of hdac2 regulates co-repressor formation, deacetylase activity and acetylation of hdac2 by cigarette smoke and aldehydesstudies using unfractionated cell extracts with ck2 inhibitors suggest that protein kinase ck2 is the major source of hdac2 kinase. Finally, and perhaps most interesting, hdac2 phosphorylation promotes enzymatic activity, selectively regulates complex formation, but has no effect on transcriptional repression. Together, our data indicate that like many hdacs, hdac2 is regulated by post-translational modification, particularly phosphorylation. | SIGNOR-164795 |
P54646 | Q92786 | 1 | phosphorylation | down-regulates quantity by destabilization | 0.2 | Furthermore, the Ser79 phosphorylation of PROX1 by AMPK enhances the recruitment of CUL4-DDB1 ubiquitin ligase to promote PROX1 degradation. | SIGNOR-277608 |
P54829 | P42262 | 1 | dephosphorylation | down-regulates activity | 0.412 | One study showed that stimulation of the metabotrophic glutamate receptor mGluR5 leads to a STEP mediated tyrosine dephosphorylation of GluA2 and internalization of GluA1 and GluA2, although the tyrosine residue on GluA2 that is dephosphorylated by STEP remains unidentified. | SIGNOR-277040 |
P35813 | O15169 | 1 | dephosphorylation | down-regulates | 0.435 | Pp2c utilizes axin as a substrate both in vitro and in vivo and decreases its half-life. These results indicate that pp2c is a positive regulator of wnt signal transduction and mediates its effects through the dephosphorylation of axin. | SIGNOR-74231 |
Q96BR1 | Q96PU5 | 1 | phosphorylation | down-regulates activity | 0.445 | Moreover, S422DSGK1, SGK1, and SGK3 also phosphorylated Nedd4-2 and thereby inhibited Nedd4-2 binding to its target. | SIGNOR-280125 |
Q15139 | O60602 | 1 | phosphorylation | up-regulates | 0.353 | Pkd phosphorylated the tlr5-derived target peptide in vitro, and phosphorylation of the putative target serine 805 in hek 293t cell-derived tlr5 was identified by mass spectrometry. These results demonstrate that both pkd1 and pkd2 are required for inflammatory responses following tlr2, tlr4, or tlr5 activation, although pkd1 is more strongly involved | SIGNOR-154473 |
Q12933 | P19438 | 0 | null | up-regulates | 0.832 | We found that TNF-R1-mediated IKK activation requires both RIP and TRAF2 proteins. Although TRAF2 or RIP can be independently recruited to the TNF-R1 complex, neither one of them alone is capable of transducing the TNF signal that leads to IKK activation | SIGNOR-256251 |
Q9UBS5 | Q9UQM7 | 0 | phosphorylation | down-regulates | 0.237 | Nmda-dependent internalization of gabab receptors requires activation of ca2+/calmodulin-dependent protein kinase ii (camkii), which associates with gabab receptors in vivo and phosphorylates serine 867 (s867) in the intracellular c terminus of the gabab1 subunit. | SIGNOR-166846 |
P68400 | P19447 | 1 | phosphorylation | down-regulates activity | 0.2 | Phosphorylation of S751 by CKII inhibits 5′ incision. | SIGNOR-276013 |
Q8N4X5 | P07949 | 0 | phosphorylation | up-regulates activity | 0.33 | RET/PTC induced robust tyrosine phosphorylation of XB130, which promoted its subsequent association with the p85alpha subunit of phosphatidylinositol 3-kinase (PI 3-kinase). We identified tyrosine 54 of XB130 as the major target of RET/PTC-mediated phosphorylation and a critical binding site for the SH2 domains of p85alpha. | SIGNOR-263192 |
O60260 | Q9NX47 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.2 | MITOL promotes cell survival by degrading Parkin during mitophagy.|Mechanistically, MITOL mediates ubiquitination of Parkin at lysine 220 residue, which promotes its proteasomal degradation, and thereby fine-tunes mitophagy by controlling the quantity of Parkin. | SIGNOR-278554 |
P52789 | P12931 | 0 | phosphorylation | up-regulates activity | 0.362 | Here we find that c-Src can interact with and phosphorylate hexokinases HK1 and HK2, the rate limiting enzymes in glycolysis.|Moreover, c-Src could efficiently stimulate the catalytic activities of HK1 and HK2, but failed to stimulate their corresponding mutants (XREF_FIG and XREF_SUPPLEMENTARY). | SIGNOR-278499 |
P04637 | P28482 | 0 | phosphorylation | up-regulates activity | 0.778 | In summary, our results suggest that phosphorylation of p53Thr55 by ERK2 is important for doxorubicin-induced p53 activation and cell death. | SIGNOR-279068 |
Q9Y4K3 | P03186 | 0 | deubiquitination | down-regulates activity | 0.2 | EBV-encoded BPLF1 interacts with and deubiquitinates TRAF6 to inhibit NF-κB signaling during lytic infection. Once lytic replication is induced, BPLF1 then deubiquitinates and inactivates TRAF6 to further block NF-κB signaling, promoting efficient viral genome replication. | SIGNOR-266739 |
P42768 | P07948 | 0 | phosphorylation | up-regulates activity | 0.378 | We demonstrated that WASP is phosphorylated on tyrosine 291 in macrophages, and the WASP phosphorylation is important for the phagocytic cup formation. In addition, we showed that WASP and WASP-interacting protein (WIP) form a complex at the phagocytic cup and that the WASP.WIP complex plays a critical role in the phagocytic cup formation. | SIGNOR-273959 |
Q13224 | P17612 | 0 | phosphorylation | up-regulates activity | 0.414 | Here we identify serine residue 1166 (Ser1166) in the carboxy-terminal tail of the NMDAR subunit GluN2B to be a direct molecular and functional target of PKA phosphorylation critical to NMDAR-dependent Ca(2+) permeation and Ca(2+) signaling in spines. | SIGNOR-276616 |
O95817 | Q05655 | 0 | phosphorylation | up-regulates | 0.251 | Pkc_-mediated phosphorylation of bag3 at ser187 site induces epithelial-mesenchymal transition and enhances invasiveness in thyroid cancer fro cells. we showed that bag3 was implicated in epithelial-mesenchymal transition (emt) procedure, and phosphorylation state at ser187 site had a critical role in emt regulation by bag3. | SIGNOR-199316 |
P62136 | P07737 | 1 | dephosphorylation | up-regulates | 0.247 | Knockdown of the catalytic subunit of pp1 (pp1c_), but not pp2a (pp2ac_), increased ps137-pfn1 levels. Pp1c_ binds pfn1 in cultured cells, and this interaction was increased by a phosphomimetic mutation of pfn1 at ser-137 (s137d). Together, these data define pp1 as the principal phosphatase for ser-137 of pfn1 | SIGNOR-196816 |
Q14469 | P53805 | 1 | transcriptional regulation | down-regulates quantity by repression | 0.2 | Increased Calcineurin/NFAT activity by Notch signaling involves downregulation of Calcipressin, an endogenous Calcineurin inhibitor, through a HES-1-dependent mechanism .... Chromatin immunoprecipitation (ChIP) analysis of keratinocytes overexpressing HES-1 showed that this protein can bind to the HES binding sites present in both distal and proximal promoters | SIGNOR-252026 |
Q9GZQ8 | Q9Y4P1 | 0 | cleavage | up-regulates | 0.803 | 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-125449 |
O60266 | Q13555 | 0 | phosphorylation | down-regulates activity | 0.353 | Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo. | Site-directed mutagenesis of a CaM kinase II consensus site (Ser-1076 to Ala-1076) in III-AC greatly reduced Ca2+-stimulated phosphorylation and inhibition of III-AC in vivo. | SIGNOR-250691 |
P55085 | P35030 | 0 | cleavage | up-regulates activity | 0.388 | Mass spectrometry studies of PAR2E predicted activation of PAR2 by trypsin through cleavage at the Arg36-Ser37 site, no effect of thrombin, and inactivation of the receptor by plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3. | SIGNOR-263604 |
Q96PU5 | Q9NRA0 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.2 | In this study, we found that NEDD4L interacted with SphK2 to ubiquitinate SphK2 protein.|NEDD4L Mediates the Degradation of SphK2 Protein Through the Ubiquitin-Proteasomal Pathway. | SIGNOR-278660 |
P07355 | Q75N03 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.2 | By immunoprecipitation, we present evidence that Hakai interacts with Hsp90 chaperone complex in several epithelial cells and demonstrate that is a novel Hsp90 client protein. Interestingly, by overexpressing and knocking-down experiments with Hakai, we identified Annexin A2 as a Hakai-regulated protein. Interestingly, geldanamycin-induced Hakai degradation is accompanied by an increased expression of E-cadherin and Annexin A2. | SIGNOR-271473 |
Q13936 | P12931 | 0 | phosphorylation | up-regulates activity | 0.443 | Cotransfection of human embryonic kidney (HEK)-293 cells with hCa(v)1.2b and c-Src resulted in tyrosine phosphorylation of the calcium channel, which was prevented by nitration of tyrosine residues by peroxynitrite. Whole cell calcium currents were reduced by 58 + 5% by the Src kinase inhibitor PP2 and 64 + 6% by peroxynitrite. | SIGNOR-276081 |
O00213 | O00141 | 0 | phosphorylation | down-regulates activity | 0.345 | In the present study, we demonstrated that phosphorylation of FE65 Ser 610 by SGK1 attenuates the interaction between FE65 and APP (XREF_FIG).|In this regard, we demonstrated that phosphorylation of FE65 Ser 610 by SGK1 abolishes the effect of FE65 on APP processing and the amount of secreted Abeta is comparable to APP + Mock control (XREF_FIG). | SIGNOR-278220 |
P04637 | P50750 | 0 | phosphorylation | up-regulates | 0.535 | We recently demonstrated that through their physical interaction, cdk9 phosphorylates p53 on ser-392, leading to p53 stability and accumulation | SIGNOR-201935 |
Q04912 | P00533 | 0 | phosphorylation | up-regulates activity | 0.334 | This showed that EGFR activation transphosphorylated Ron.|Together, these data suggested that (1) Ron activation transphosphorylated EGFR and vice versa and (2) activated Ron biochemically interacted with EGFR. | SIGNOR-280000 |
P00519 | O60234 | 1 | phosphorylation | down-regulates activity | 0.2 | Acetylcholine stimulation also increased GMF-γ phosphorylation at Tyr-104. GMF-γ phosphorylation at this residue was mediated by c-Abl tyrosine kinase. The GMF-γ mutant Y104F (phenylalanine substitution at Tyr-104) had higher association with Arp2 in HASM cells upon contractile activation.Furthermore, expression of mutant Y104F GMF-γ attenuated actin polymerization and contraction in smooth muscle. | SIGNOR-273536 |
Q01726 | Q8IUH4 | 0 | palmitoylation | up-regulates activity | 0.274 | Collectively these results suggest that ZDHHC13 phosphorylation by ATR following UVB irradiation promotes its interaction with MC1R to stimulate MC1R palmitoylation.Activating MC1R palmitoylation rescues the defect of MC1R RHC variants | SIGNOR-273518 |
P06239 | Q05655 | 1 | phosphorylation | up-regulates activity | 0.526 | The tyrosine phosphorylation sites of PKC delta in the H(2)O(2)-treated cells were identified as Tyr-311, Tyr-332, and Tyr-512 by mass spectrometric analysis with the use of the precursor-scan method and by immunoblot analysis with the use of phosphorylation site-specific antibodies. Tyr-311 was the predominant modification site among them. In an in vitro study, phosphorylation at this site by Lck, a non-receptor-type tyrosine kinase, enhanced the basal enzymatic activity and elevated its maximal velocity in the presence of diacylglycerol. phosphorylation at Tyr-311 between the regulatory and catalytic domains is a critical step for generation of the active PKC delta in response to H(2)O(2). | SIGNOR-251386 |
Q16695 | Q9Y4C1 | 0 | demethylation | up-regulates activity | 0.2 | Using a biochemical assay coupled with chromatography, we have purified a JmjC domain-containing protein, JHDM2A, which specifically demethylates mono- and dimethyl-H3K9. | SIGNOR-276846 |
P23467 | P33151 | 1 | dephosphorylation | up-regulates activity | 0.581 | Because we had shown previously that VE-PTP supports VE-cadherin function when exogenously expressed in transfected cells, we expected it to be expressed at endothelial cell contacts.|Indeed, tyrosine phosphorylation of VE-cadherin is reduced by VE-PTP in COS-7 and CHO cells. | SIGNOR-277131 |
Q13627 | Q52LA3 | 1 | phosphorylation | up-regulates activity | 0.681 | Here we report that DYRK1A can specifically phosphorylate LIN52 on serine residue 28, and that this phosphorylation is required for DREAM assembly. | SIGNOR-262846 |
P48729 | Q9UGI0 | 1 | phosphorylation | up-regulates activity | 0.2 | Interestingly, ZRANB1 is phosphorylated at Thr35, and Ser209 residues by CSNK1A1, and this phosphorylation activates its deubiquitinating activity. | SIGNOR-273621 |
O00254 | Q15835 | 0 | phosphorylation | down-regulates activity | 0.2 | For example, RhoK phosphorylates and inhibits TIAM1, STEF, and PAR3; disrupts the polarity complex; and prevents Rac activation ( xref ). | SIGNOR-279993 |
Q9NVW2 | Q86U70 | 1 | polyubiquitination | down-regulates quantity by destabilization | 0.566 | Here we identify RLIM as a ubiquitin protein ligase that is able to target CLIM cofactors for degradation through the 26S proteasome pathway. | SIGNOR-272617 |
Q9Y6K9 | P06241 | 0 | phosphorylation | down-regulates activity | 0.357 | Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation. | SIGNOR-276371 |
O60936 | Q05086 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.2 | Incubation of transfected HEK293T cells with the proteasome inhibitor, MG132 blocked Ube3A mediated degradation of Arc suggesting that Ube3A degrades Arc via the ubiquitin proteasome system .|The ubiquitination of Arc by Ube3A was confirmed by mass spectrometry which revealed that Ube3A catalyzed the polyubiquitination of Arc on Lysine 268 and 269 ( xref ). | SIGNOR-278522 |
P54198 | P31749 | 0 | phosphorylation | up-regulates activity | 0.2 | Consistently, HIRA phosphorylation was effectively decreased by Akt1 knockdown and was completely eliminated by the depletion of both Akt1 and Akt2, suggesting that HIRA is phosphorylated primarily by Akt1 and that Akt2 seemed to contribute to HIRA phosphorylation as a supplementary kinase in myoblasts (XREF_FIG).|In this study, HIRA was more efficiently targeted by Akt1 in myoblasts. | SIGNOR-279584 |
O43521 | Q16539 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.32 | Ser69 can also be phosphorylated by JNK and p38MAPK at least in vitro. Phosphorylation of BimEL on Ser69 promotes its ubiquitination. | SIGNOR-260442 |
P21796 | O00141 | 0 | phosphorylation | down-regulates quantity | 0.2 | As hypothesized based upon our observation that activated SGK-1 reduces VDAC-1 protein levels, sgk-1 overexpression normalizes the shortened lifespan of vdac-1 transgenics .|Taken together, these data indicate that Ser104 phosphorylation of VDAC1 by SGK1 increases its ubiquitination and subsequent cellular clearance. | SIGNOR-278988 |
Q99523 | Q13153 | 0 | phosphorylation | down-regulates activity | 0.2 | PAKs specifically phosphorylate Ser15 of the sortilin-cd and alter its trafficking. It can be concluded that PAK1-3 may indeed instigate the phosphorylation of sortilin and that they target a single serine residue (Ser15) located in the kinase domain-binding site of the sortilin-cd. Full-length sortilins with the serine at position 793 (residue 15 in the cytoplasmic domain) (for the sequence, see Fig. 2). Phosphorylation (Ser15) downregulates the sortilin–AP-1 interaction. | SIGNOR-273718 |
P05067 | P11802 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.258 | These include a significant increase in APP phosphorylation at Thr 668 by cdk2, cdk4, and cdk5, which increases its beta-amyloid production and APP proteolysis by the activated caspases during cell cycle ( xref ; xref ; xref ; xref ). | SIGNOR-280214 |
Q13164 | P15056 | 0 | phosphorylation | up-regulates quantity | 0.292 | Our data indicate that oncogenic BRAF increases ERK5 protein level, phosphorylation at several residues and kinase activity.|Overexpression of oncogenic BRAF induced ERK5 phosphorylation at Thr218 and Tyr220, although to a lower level than that induced by MEK5DD. | SIGNOR-278353 |
P06493 | P51003 | 1 | phosphorylation | up-regulates activity | 0.258 | Once an oocyte resumes meiosis, activated CDK1 and ERK1/2 cooperatively mediate the phosphorylation of three serine residues of PAPalpha, 537, 545 and 558, thereby leading to increased activity. | SIGNOR-268338 |
Q9NQU5 | P04049 | 1 | phosphorylation | up-regulates activity | 0.2 | PAK5 phosphorylates Raf-1 on serine 338 and stimulates Raf-1 activity. | SIGNOR-278971 |
P06241 | P05067 | 1 | phosphorylation | up-regulates quantity | 0.451 | Fyn induced phosphorylation of APP at Tyr-757 of the (757)YENPTY(762) motif and increased cell surface expression of APP. | SIGNOR-278378 |
Q13464 | P48436 | 1 | phosphorylation | up-regulates | 0.305 | Rho kinase-dependent activation of sox9 in chondrocytes. In vitro, rock directly phosphorylated sox9 at ser(181), and the overexpression of rock or the activation of the rhoa pathway in sw1353 chondrosarcoma cells increased sox9(ser181) phosphorylation | SIGNOR-162643 |
P06493 | P67870 | 1 | phosphorylation | up-regulates | 0.459 | In cells, the casein kinase ii beta-subunit is phosphorylated at an autophosphorylation site and at a site (ser-209) that is maximally phosphorylated in mitotic cells. These studies provide strong biochemical evidence that p34cdc2 is the enzyme that phosphorylates ser-209 on the beta-subunit of ckii in mitotic cells. | SIGNOR-29462 |
P42768 | Q06187 | 0 | phosphorylation | up-regulates activity | 0.743 | These results demonstrate that WASP, under this experimental condition, can be tyrosine-phosphorylated by the kinase activity of Btk and that the direct interaction between WASP and the SH3 domain of Btk is required for this phosphorylation to occur. | SIGNOR-273958 |
Q9BT67 | Q9H0M0 | 0 | ubiquitination | down-regulates quantity | 0.381 | Accordingly, the ubiquitination assays were performed and the results revealed that knockdown of WWP1 reduced the ubiquitination of NDFIP1 in HuCCT1 and vice versa in HCCC-9810 and RBE (Fig. 7E).|In addition, we found that WWP1 could reduce the protein level of NDFIP1 via ubiquitination. | SIGNOR-278796 |
Q13315 | Q9BQ15 | 1 | phosphorylation | up-regulates activity | 0.501 | Ataxia telangiectasia mutated (ATM) kinase phosphorylates hSSB1 in response to DNA double-strand breaks (DSBs). This phosphorylation event is required for DNA damage-induced stabilization of hSSB1. | SIGNOR-262639 |
P17252 | P28698 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.384 | The luciferase reporter assay results revealed that the presence of both MZF-1 and Elk-1 significantly contributed to the upregulation of PKCα gene transcription activity. | SIGNOR-256337 |
Q8NG68 | Q6PEY2 | 1 | tyrosination | down-regulates | 0.46 | Tubulin tyrosine ligase (ttl) adds a c-terminal tyr to __tubulin as part of a tyrosination/detyrosination cycle present in most eukaryotic cells. / ttl inhibits spontaneous tubulin polymerization | SIGNOR-176924 |
Q5VT25 | P53667 | 1 | phosphorylation | up-regulates activity | 0.404 | Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha. \ In vitro, MRCKalpha phosphorylated the protein kinase domain of LIM kinases, and the site in LIMK2 phosphorylated by MRCKalpha proved to be threonine 505 within the activation segment. | SIGNOR-250721 |
Q13542 | P42345 | 0 | phosphorylation | down-regulates | 0.661 | Here, we show that cancer cells acquire resistance to astori by downregulating eukaryotic translation initiation factor (eif4e)-binding proteins (4e-bps-eif4ebp1, eif4ebp2). | SIGNOR-122014 |
Q92519 | Q9HCE7 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.41 | In this study, we found that TRIB2 was up-regulated and exhibited high stability in liver cancer cells compared with other cells. We performed a structure-function analysis of TRIB2 and identified a domain (amino acids 1-5) at the N terminus that interacted with the E3 ubiquitin ligase Smurf1 and was critical for protein stability. Deletion of this domain extended TRIB2 half-life time accompanied with a more significant malignant property compared with wild type TRIB2. | SIGNOR-275432 |
O75581 | Q9H0K1 | 0 | phosphorylation | up-regulates activity | 0.2 | Mechanistically, SIK2, phosphorylated by CK1α, directly phosphorylated LRP6 in a SIK2 kinase activity-dependent manner, leading to Wnt/β-catenin signaling pathway activation. | SIGNOR-275399 |
P07384 | P10636 | 1 | cleavage | down-regulates activity | 0.333 | Besides tau phosphorylation, calpain activation might play a role in tau-mediated neurodegeneration by inducing tau cleavage. In vitro studies have shown that both fetal and adult tau isoforms are rapidly proteolyzed by calpains | SIGNOR-251584 |
O14965 | O43379 | 1 | phosphorylation | up-regulates activity | 0.352 | AURKA activity promotes WDR62 spindle localization|We next purified recombinant full-length WDR62 (GST–WDR62-FL) for in vitro kinase assays with active AURKA and demonstrated that WDR62 was a direct phosphorylation target of AURKA|In addition, our quantitative phosphoproteomic analysis of in-vitro-phosphorylated WDR62 identified S32 and S33 as significantly phosphorylated in the presence of active AURKA|Alanine replacement of the five putative phosphorylation sites (S32/S33/S49/T50/S52-AAAAA) of WDR62 attenuated interphase microtubule association induced by AURKA coexpression | SIGNOR-271713 |
P48729 | O15534 | 1 | phosphorylation | down-regulates quantity by destabilization | 0.318 | CKI\u03b1-Dependent Phosphorylation and Degradation of PER1. | SIGNOR-279700 |
P47712 | P27361 | 0 | phosphorylation | up-regulates | 0.658 | Activated map kinase phosphorylates cpla2 at ser-505, causing increased enzymatic activity of cpla2, which is only realized upon translocation of cpla2 to the membrane. | SIGNOR-38434 |
Q05655 | Q99808 | 1 | phosphorylation | up-regulates activity | 0.2 | Phosphorylation of hENT1 by PKC has effects on both the function and subcellular trafficking of hENT1 | SIGNOR-260888 |
P19634 | P51812 | 0 | phosphorylation | up-regulates activity | 0.414 | In pressured arteries, RSK2 dependent activation of NHE-1 was associated with increased intracellular Ca 2+ transients, which would be expected to increase MLCK activity, thereby contributing to basal tone and myogenic responses.|Together, these data indicate that Ser 703 in NHE-1 is phosphorylated by RSK2, that RSK2 is associated with NHE-1, and that the time course of NHE-1 phosphorylation in response to intraluminal pressure is fast enough for this phosphorylation event to contribute to myogenic vasoconstriction. | SIGNOR-280119 |
P23771 | P42226 | 0 | null | up-regulates | 0.662 | GATA-3 plays a central role in regulating Th1 and Th2 cell differentiation. Upon interleukin (IL)-4 binding to its receptor, GATA-3 is induced through the action of Stat6 | SIGNOR-254299 |
Q15306 | O15054 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.422 | JMJD3 seems to function by controlling expression of the transcription factor IRF4, which in turn is required for M2 polarization of macrophages in vitro and in vivo. Although this pathway is strongly supported by genetic. | SIGNOR-249540 |
P32245 | P25098 | 0 | phosphorylation | down-regulates activity | 0.2 | Mutagenesis studies revealed that Thr312 and Ser329/330 in the C-terminal tail are potential sites for PKA and GRK phosphorylation and may play an essential role in the recruitment of beta-arrestin to the activated receptor. | SIGNOR-247770 |
P27708 | P27361 | 0 | phosphorylation | up-regulates | 0.2 | Cad is a multifunctional protein that initiates and regulates mammalian de novo pyrimidine biosynthesis. The activation of the pathway required for cell proliferation is a consequence of the phosphorylation of cad thr-456 by mitogen-activated protein (map) kinase.Activated map kinase (erk1/2), the enzyme responsible for the phosphorylation of thr-456, was also present in larger amounts in the nucleus than the cytosol | SIGNOR-137179 |
P98170 | P31749 | 0 | phosphorylation | up-regulates quantity by stabilization | 0.618 | Akt, including akt1 and akt2, interacts with and phosphorylates x-linked inhibitor of apoptosis protein (xiap) at residue serine-87 in vitro and in vivo. Phosphorylation of xiap by akt protects xiap from ubiquitination and degradation in response to cisplatin. | SIGNOR-119488 |
Q00613 | P68400 | 0 | phosphorylation | up-regulates activity | 0.37 | Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. | SIGNOR-250898 |
P32121 | Q14940 | 1 | relocalization | down-regulates activity | 0.397 | Internalization of the Na(+)/H(+) exchanger NHE5 into recycling endosomes is enhanced by the endocytic adaptor proteins beta-arrestin1 and -2, best known for their preferential recognition of ligand-activated G protein-coupled receptors (GPCRs) | SIGNOR-275506 |
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