IdA string | IdB string | labels int64 | mechanism string | effect string | score float64 | sentence string | signor_id string |
|---|---|---|---|---|---|---|---|
P34947 | P61073 | 1 | phosphorylation | down-regulates quantity | 0.459 | Conversely, GRK5 knock-down in cells with low WIP1 expression inhibited CXCR4 phosphorylation, increased cell membrane expression of CXCR4, and promoted medulloblastoma growth.|Transfection of GRK5 into D556-WIP1 cells increased Ser339 phosphorylation of CXCR4 and reduced proliferation. | SIGNOR-279740 |
O96017 | Q13362 | 1 | phosphorylation | up-regulates | 0.322 | Found that chk2 associated with the b' regulatory subunit of protein phosphatase pp2a. In vitro kinase assays showed that b'gamma3 was a potent chk2 substrate. This phosphorylation increased the catalytic phosphatase activity of pp2a. | SIGNOR-129255 |
P38435 | P22891 | 1 | carboxylation | up-regulates activity | 0.507 | Gamma-carboxylation is essential in the activation and proper functioning of multiple VK-dependent proteins (VKDP), the most well-known of which are involved in blood clotting, including coagulation factors (FII, FVII, FIX and FX) and natural anti-clotting agents (protein C, protein S (ProS; OMIM*176880) and protein Z | SIGNOR-265926 |
Q04760 | P12931 | 0 | phosphorylation | up-regulates activity | 0.2 | We show that Glo1 activity is promoted by phosphorylation on Tyrosine 136 via multiple kinases. Glo1 Y136 is phosphorylated by multiple different kinases including all members of the Src family. Depletion of multiple different kinases led to a partial reduction in Glo1(Y136) phosphorylation. These included members of t... | SIGNOR-276189 |
Q16832 | P12931 | 0 | phosphorylation | up-regulates | 0.38 | Here, using baculoviral co-expression of the ddr2 cytosolic domain and src, we show that src targets three tyrosine residues (tyr-736, tyr-740, and tyr-741) in the activation loop of ddr2 for phosphorylation. This phosphorylation by src stimulates ddr2 cis-autophosphorylation of additional tyrosine residues. | SIGNOR-140767 |
P04839 | P15976 | 0 | transcriptional regulation | up-regulates quantity | 0.279 | These results suggest that GATA-1 is an activator and that GATA-2 is a relative competitive inhibitor of GATA-1 in the expression of the gp91(phox) gene in human eosinophils. | SIGNOR-259947 |
P06400 | O14757 | 0 | phosphorylation | up-regulates activity | 0.422 | These results suggest that ser612 is phosphorylated by chk1/2 after dna damage, leading to the formation of prb-e2f-1. phosphorylation of prb at ser612 enhanced the formation of a complex between prb and e2f-1 | SIGNOR-153904 |
P49748 | P17612 | 0 | phosphorylation | up-regulates activity | 0.2 | As shown in Fig. 2C, an in vitro kinase assay carried out using PKA and a GST fusion protein containing the COOH-terminal 258 amino acids showed the protein to be efficiently phosphorylated in a time-dependent manner. |Furthermore, a phosphorylation-negative mutant (S586A) VLCAD shows reduced electron transfer activity... | SIGNOR-264422 |
P27361 | Q9UJY1 | 1 | phosphorylation | up-regulates activity | 0.34 | Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate t... | SIGNOR-107680 |
Q13882 | Q13017 | 1 | phosphorylation | up-regulates | 0.2 | Breast tumor kinase phosphorylates p190rhogap to regulate rho and ras and promote breast carcinoma growth, migration, and invasion. Brk phosphorylates p190 at the y(1105) residue both in vitro and in vivo, thereby promoting the association of p190 with p120rasgap (p120). As a consequence, brk stimulates p190 and attenu... | SIGNOR-181452 |
Q9UKB1 | Q9Y2X9 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.2 | E3 ligase the beta-transducin repeat-containing protein 2 (beta-TrCP2) governs the ubiquitination and degradation of ZNF281. In human CRC specimens, endogenous beta-TrCP2 were inversely correlated with ZNF281. | SIGNOR-264897 |
Q05655 | P61073 | 1 | phosphorylation | down-regulates activity | 0.2 | Therefore, internalization of CXCR4 in response to PMA appears to be mediated by activation of protein kinase C | However, mutation of the dileucine motif or the serines at positions 324, 325, 338, and 339 profoundly decreased internalization. | SIGNOR-260898 |
P41743 | Q15334 | 1 | phosphorylation | up-regulates activity | 0.632 | This finding indicates that both mLgl-2 and mLgl-1 are phosphorylated in vivo in an aPKC lambda activity-dependent manner. | SIGNOR-263179 |
Q99523 | Q13177 | 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 serin... | SIGNOR-273717 |
P05771 | Q16820 | 1 | phosphorylation | down-regulates quantity | 0.2 | These findings suggest that activation of a protein kinase, presumably PKC, mediates PMA-induced hmeprinβ shedding. By labeling COS-1 cells transfected with mutant constructs lacking the potential phosphorylation sites, we identified Ser687 as the main 32P-acceptor. These data provide evidence that the cytoplasmic doma... | SIGNOR-263173 |
P31751 | P15336 | 1 | phosphorylation | up-regulates activity | 0.426 | Taken together, these data suggest that AMPK regulates EC migration through phosphorylation of AKT2, which promotes ATF2 transactivation of MMP-2 during EC migration.|Within this subgroup, we chose AKT2 for analysis because AKT2 phosphorylates activating transcription factor 2 (ATF2) [ xref , xref ]. | SIGNOR-280178 |
P98170 | O15294 | 1 | ubiquitination | down-regulates quantity | 0.2 | These results demonstrate that XIAP acts as an E3 ubiquitin ligase and ubiquitinates OGT in HCT116 colon cancer cells.|XIAP promotes the ubiquitin-dependent proteasomal degradation of OGT. | SIGNOR-278800 |
P28482 | P20749 | 1 | phosphorylation | up-regulates activity | 0.474 | Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregul... | SIGNOR-277361 |
P06493 | P10415 | 1 | phosphorylation | up-regulates activity | 0.345 | Using synthetic peptides and mutant cell lines, we identified threonine 56, one of two consensus sites for cdc2 within the bcl-2 sequence, as a residue phosphorylated by cdc2. Mutation at threonine 56 abrogated the cell cycle inhibitory effect of bcl-2 without affecting anti-apoptotic function.Taken together, our prese... | SIGNOR-76837 |
Q8NG68 | Q9BQE3 | 1 | tyrosination | down-regulates | 0.473 | 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-176918 |
P42684 | P04040 | 1 | phosphorylation | up-regulates activity | 0.34 | C-abl and arg phosphorylated catalase at tyr231 and tyr386 in vitrocatalase is a major effector in the defense of aerobic cells against oxidative stress. Recent studies have shown that catalase activity is stimulated by the c-abl and arg tyrosine kinases | SIGNOR-101306 |
P31749 | P41279 | 1 | phosphorylation | up-regulates activity | 0.558 | Akt-dependent phosphorylation of Cot occurs exclusively on serines 400 and 413. Akt to phosphorylate Cot at two sites in the carboxy-terminal domain, at least one of which may promote binding of substrates or coactivators to Cot, or alternatively may relieve binding of a negative regulator. | SIGNOR-252572 |
P35813 | P24941 | 1 | dephosphorylation | down-regulates activity | 0.292 | Moreover, purified recombinant PP2C alpha and PP2C beta 2 proteins efficiently dephosphorylated monomeric Cdk2/Cdk6 in vitro. | SIGNOR-277107 |
P23246 | P49840 | 0 | phosphorylation | down-regulates | 0.2 | Psf is directly phosphorylated by gsk3, thus promoting interaction of psf with trap150, which prevents psf from binding cd45 pre-mrna. / threonine phosphorylation of psf by gsk3 primarily occurs on residue t687 | SIGNOR-168385 |
P11802 | Q9BQA1 | 1 | phosphorylation | up-regulates activity | 0.7 | Phosphorylation of MEP50 on Thr 5 by D1T286A and CDK4 is necessary and sufficient to increase the intrinsic methyltransferase activity of PRMT5, resulting in increased H4R3 and H3R8 methylation and repression of the CUL4A/B expression. | SIGNOR-279019 |
P19532 | P11802 | 0 | phosphorylation | up-regulates activity | 0.2 | CDK4 and CDK6 interact with TFEB and TFE3 in the nucleus We next investigated how CDK4 and CDK6 activate TFEB and TFE3 .|We found that CDK4 and CDK6 interact with and phosphorylate nuclear TFEB and TFE3, thereby promoting their shuttling to the cytoplasm. | SIGNOR-279514 |
Q9H8V3 | P61586 | 1 | guanine nucleotide exchange factor | up-regulates activity | 0.712 | 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... | SIGNOR-260550 |
Q15116 | P06493 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.2 | We demonstrated that cyclin-dependent kinase 1-mediated phosphorylation of Ser261 residue primes PD-1 protein nucleus translocation and binding with FBW7. | SIGNOR-277605 |
P45983 | Q969R2 | 1 | phosphorylation | up-regulates activity | 0.2 | CK1a1, JNK1 and CDK1 had the highest site-specific activity for ORP4L, while CDK1, GSK3a, CK1a1 and GSK3b showed the highest specificity for the site when corrected for background activity with ORP4L-S4A. Because of the complexity of the serine/proline-rich site, we did not determine which serine(s) in ORP4L were phosp... | SIGNOR-264876 |
P12931 | Q13002 | 1 | phosphorylation | up-regulates activity | 0.372 | GluK2 binds to Src, and the tyrosine residue at position 590 (Y590) on GluK2 is a major site of phosphorylation by Src kinases. GluK2 phosphorylation at Y590 is responsible for increases in whole-cell currents and calcium influx in response to transient kainate stimulation. | SIGNOR-276850 |
P24941 | Q9H3D4 | 1 | phosphorylation | down-regulates | 0.246 | Atm kinase is a master switch for the delta np63 alpha phosphorylation/degradation in human head and neck squamous cell carcinoma cells upon dna damage. We previously found that the pro-apoptotic dna damaging agent, cisplatin, mediated the proteasome-dependent degradation of delta np63 alpha associated with its increas... | SIGNOR-180759 |
P61586 | Q12802 | 0 | guanine nucleotide exchange factor | up-regulates activity | 0.744 | 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... | SIGNOR-260527 |
P62987 | P15374 | 0 | cleavage | up-regulates quantity | 0.801 | 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, ... | SIGNOR-270827 |
P35568 | Q12923 | 0 | dephosphorylation | down-regulates activity | 0.466 | Finally, we report that PTPL1 expression is sufficient to block the IRS-1/phosphatidylinositol 3-kinase/Akt signaling pathway, to inhibit the insulin-like growth factor-I effect on cell survival, and to induce apoptosis.|We first show by complementary approaches that PTPL1 specifically dephosphorylates insulin receptor... | SIGNOR-277053 |
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 |
Q05655 | P41594 | 1 | phosphorylation | up-regulates activity | 0.348 | Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839. | SIGNOR-249287 |
P11309 | Q13309 | 1 | phosphorylation | up-regulates activity | 0.34 | We found that expression of Pim-1 increases the level of Skp2 through direct binding and phosphorylation of multiple sites on this protein. Along with known Skp2 phosphorylation sites including Ser(64) and Ser(72), we have identified Thr(417) as a unique Pim-1 phosphorylation target. Phosphorylation of Thr(417) control... | SIGNOR-259819 |
P17812 | P49841 | 0 | phosphorylation | down-regulates activity | 0.2 | We found that low serum conditions increased phosphorylation of endogenous CTPS1 and this phosphorylation was inhibited by the glycogen synthase kinase 3 (GSK3) inhibitor indirubin-3'-monoxime and GSK3beta short interfering RNAs, demonstrating the involvement of GSK3 in phosphorylation of endogenous human CTPS1. Separa... | SIGNOR-276069 |
Q14451 | P45983 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.262 | Our data show that phosphorylation of Grb7 protein on the Ser194-Pro motif by c-Jun N-terminal kinase facilitates its binding with the WW domain of Pin1. Subsequently, Grb7 is degraded by the ubiquitin- and proteasome-dependent proteolytic pathway. I | SIGNOR-277280 |
O14965 | Q15398 | 1 | phosphorylation | up-regulates quantity by stabilization | 0.751 | Phosphorylation and stabilization of HURP by Aurora-A. Four phosphorylated residues were identified, namely, HURP-S627, -S725, -S757, and -S830, with 65% amino acid sequence coverage. we propose here that Aurora-A may phosphorylate HURP and this probably attenuates the negative impact of cdk1 phosphorylation and by in... | SIGNOR-262651 |
Q9Y6D6 | P84077 | 1 | guanine nucleotide exchange factor | up-regulates activity | 0.6 | Brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) is an approximately 200-kDa brefeldin A-inhibited guanine nucleotide-exchange protein that preferentially activates ADP-ribosylation factor 1 (ARF1) and ARF3. | SIGNOR-272147 |
P49715 | P35638 | 0 | transcriptional regulation | down-regulates quantity | 0.519 | We find that expression of CHOP, a nuclear protein that dimerizes avidly with C/EBP isoforms alpha and beta and directs the resulting heterodimer away from classic C/EBP-binding sites, markedly inhibits this differentiation process. | SIGNOR-255913 |
Q92918 | Q13094 | 1 | phosphorylation | up-regulates | 0.778 | The serine/threonine kinase hpk-1 phosphorylates serine 376 of slp-76 and induces the interaction with 14-3-3 proteins | SIGNOR-153613 |
P53350 | Q13127 | 1 | phosphorylation | down-regulates activity | 0.309 | Mass spectrometry revealed that PLK1 phosphorylates REST on serine-1030 ( xref and xref ).|Notably, PLK1 depletion significantly increased REST protein half-life (XREF_FIG, XREF_SUPPLEMENTARY), indicating PLK1 antagonizes REST abundance by restraining REST protein stability. | SIGNOR-279380 |
P16220 | Q92911 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.267 | CREB recognized and bound to the promoter of SLC5A5 to facilitate its transcription. | SIGNOR-267137 |
O43318 | Q12933 | 0 | ubiquitination | up-regulates activity | 0.597 | Tumor necrosis factor receptor-associated factors 2 and 6 (traf2 and -6) act as the ubiquitin e3 ligases to mediate lys63-linked tak1 polyubiquitination at the lys158 residue in vivo and in vitro. Lys(63)-linked TAK1 polyubiquitination at the Lys(158) residue is required for TAK1-mediated IKK complex recruitment. | SIGNOR-162638 |
P06493 | P48200 | 1 | phosphorylation | down-regulates | 0.353 | Irp2 ser-157 is phosphorylated by cdk1/cyclin b1 during g(2)/m / ser-157 phosphorylation during g(2)/m reduces irp2 rna-binding activity | SIGNOR-179171 |
Q9UPP1 | P68400 | 0 | phosphorylation | up-regulates activity | 0.2 | The CK2 kinase is responsible for PHF8 phosphorylation at Ser854. PHF8 is phosphorylated by CK2, which regulates binding of PHF8 to TopBP1. The Ser854 residue of PHF8 is required for its interaction with TopBP1. | SIGNOR-273628 |
P06239 | Q06830 | 1 | phosphorylation | down-regulates activity | 0.2 | Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. To determine whether Prxs are phosphorylated, we subjected recombinant human PrxI and II to an in vitro kinase assay with two nonreceptor PTKs, Lck and Abl, in the presence of [γ-32P]ATP. Both PTKs phosphorylat... | SIGNOR-276277 |
P36956 | P49336 | 0 | phosphorylation | up-regulates activity | 0.474 | Biochemical analyses reveal that SREBP-1c can be directly phosphorylated by CDK8 at the conserved Threonine-402 residue (T402) in vitro and in cultured mammalian cells ( xref ).|Therefore, the mechanism of CDK8 regulating SREBP functions is primarily through the phosphorylation initiated control of nuclear SREBP-1 prot... | SIGNOR-279688 |
Q13315 | Q9NY61 | 1 | phosphorylation | up-regulates quantity by stabilization | 0.355 | The checkpoint kinases ATM/ATR and Chk2 interact with Che-1 and promote its phosphorylation and accumulation in response to DNA damage. These Che-1 modifications induce a specific recruitment of Che-1 on the TP53 and p21 promoters. |DNA damage stabilizes Che-1 protein|In addition, substitution of Che-1 Ser187 with an a... | SIGNOR-264415 |
O60674 | P08575 | 0 | dephosphorylation | down-regulates activity | 0.472 | Src homology-2 (SH2) containing tyrosine phosphatase and CD45 tyrosine phosphatase play a major role in modulating JAK-STAT pathway. SH2 containing tyrosine phosphatases include SHP1 and SHP2 (shatterproof 1 & 2). Their SH2 domains allow attachment to the phospho-tyrosine residues present on activated receptors, JAKs o... | SIGNOR-255679 |
Q16877 | Q9Y6Q9 | 1 | phosphorylation | up-regulates activity | 0.326 | PFKFB4, a regulatory enzyme that synthesizes an allosteric stimulator of glycolysis2, was found to be a robust stimulator of SRC-3 that co-activates estrogen receptor (ER). PFKFB4 phosphorylates SRC-3 at serine 857 (S857) enhancing its transcriptional activity, whereas either suppression of PFKFB4 or ectopic expression... | SIGNOR-267269 |
P63000 | Q6ZNL6 | 0 | guanine nucleotide exchange factor | up-regulates activity | 0.2 | 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... | SIGNOR-260555 |
P01160 | Q15327 | 0 | transcriptional regulation | down-regulates quantity by repression | 0.326 | In vitro calpain-mediated degradation assays, coupled to reporter gene analysis in transfected HeLa cells, strongly suggested that this mutation enhances both the stability of the ANKRD1/CARP protein and its transcriptional repression activity upon the cardiac-specific atrial natriuretic factor (ANF) promoter. | SIGNOR-253647 |
Q70Z35 | P62136 | 0 | dephosphorylation | up-regulates activity | 0.2 | PREX2 is dephosphorylated by PP1α and PP2A.PAK-mediated phosphorylation of PREX2 reduced GEF activity toward Rac1 by inhibiting PREX2 binding to PIP3 and Gβγ. | SIGNOR-277183 |
P12931 | Q9UN19 | 1 | phosphorylation | up-regulates activity | 0.586 | Src family kinases mediate receptor-stimulated, phosphoinositide 3-kinase-dependent, tyrosine phosphorylation of dual adaptor for phosphotyrosine and 3-phosphoinositides-1 in endothelial and B cell linesyrosine phosphorylation of DAPP-1 appears important for appropriate intracellular targeting and creates a potential b... | SIGNOR-247119 |
O60216 | P11308 | 1 | relocalization | down-regulates activity | 0.2 | Large-scale AML genome re-sequencing efforts have identified novel recurrently mutated genes, including the members of the cohesin complex (RAD21, SMC3, SMC1A, and STAG2), implicated in the pathogenesis of this disease.Using ATAC-seq, we determined that mutant cohesin lead to a state of elevated chromatin accessibility... | SIGNOR-261515 |
P10636 | Q13131 | 0 | phosphorylation | down-regulates activity | 0.2 | We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates so... | SIGNOR-275439 |
Q99880 | Q14493 | 0 | translation regulation | up-regulates quantity by expression | 0.2 | Synthesis of mature histone mRNA requires only a single processing reaction: an endonucleolytic cleavage between a conserved stem-loop and a purine-rich downstream element to form the 3' end. The stem-loop binding protein (SLBP) is required for processing, and following processing, histone mRNA is transported to the cy... | SIGNOR-265389 |
P35626 | P21731-2 | 1 | phosphorylation | down-regulates activity | 0.2 | These data suggest a model whereby agonist-induced PKC phosphorylation of Ser(145) partially impairs TPbeta signalling while GRK2/3 phosphorylation at both Ser(239) and Ser(357) within its IC(3) and C-tail domains, respectively, sterically inhibits G-protein coupling, profoundly desensitizing signalling, and promotes ... | SIGNOR-274091 |
P53779 | O95644 | 1 | phosphorylation | down-regulates | 0.445 | We show that jnk, erk, and p38 physically associate with the nfatc n-terminal regulatory domain and can directly phosphorylate functionally important residues involved in regulating nfatc subcellular localization, namely ser(172) and the conserved nfatc ser-pro repeats. | SIGNOR-74556 |
O43896 | P20340 | 1 | relocalization | up-regulates quantity | 0.409 | Here, we identify Bicaudal-D-related protein 1 (BICDR-1) as an effector of the small GTPase Rab6 and key component of the molecular machinery that controls secretory vesicle transport in developing neurons. BICDR-1 interacts with kinesin motor Kif1C, the dynein/dynactin retrograde motor complex, regulates the pericentr... | SIGNOR-266877 |
Q15084 | O75460 | 1 | null | down-regulates activity | 0.317 | A resident ER protein disulfide isomerase, PDIA6, limits the duration of IRE1α activity by direct binding to cysteine148 in the luminal domain of the sensor, | SIGNOR-256536 |
Q13224 | P78352 | 0 | relocalization | up-regulates activity | 0.823 | The PDZ domains of PSD-95 and related proteins interact with the COOH-terminal sequences of K+channels and NMDA2 receptors (3). By these interactions, PSD-95 may mediate the clustering of K+ channels and NMDA receptors at synapses. | SIGNOR-264195 |
Q12834 | O60566 | 0 | phosphorylation | up-regulates activity | 0.993 | Furthermore, BUBR1 phosphorylates p55CDC in vitro, and the phosphorylation of p55CDC by BUBR1 appears to be correlated with spindle checkpoint activation. | SIGNOR-279507 |
P01178-PRO_0000020495 | P16870 | 0 | cleavage | up-regulates activity | 0.2 | First, OT preprohormone is produced, that will be cleaved and matured by successive enzymes. The OT gene encodes for the Pre-Pro-OT-Neurophysin I (pre-pro-hormone), which is cleaved by different enzymes to give rise to different OT intermediate forms and to the Neurophysin I, and finally to the mature amidated form tha... | SIGNOR-270338 |
Q13315 | Q5VTR2 | 1 | phosphorylation | up-regulates | 0.522 | E3 ubiquitin ligase, a heterodimeric complex of the ringfinger rfn20/rfn40 is phosphorylated by atm. | SIGNOR-174949 |
P32754 | Q9BYT3 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.2 | Decreased expression of 4-hydroxyphenylpyruvic acid dioxygenase (HPD), a key enzyme for tyrosine metabolism, is a cause of human tyrosinemia. However, the regulation of HPD expression remains largely unknown. Here, we demonstrate that molecular chaperone TTC36, which is highly expressed in liver, is associated with HPD... | SIGNOR-272958 |
Q15139 | Q05655 | 0 | phosphorylation | up-regulates | 0.269 | Here we show that activation of pkd in response to oxidative stress requires two sequential signaling events, i.e., phosphorylation of tyr463 by abl, which in turn promotes a second step, phosphorylation of the pkd activation loop (ser738/ser742). We show that this is mediated by pkcdelta (protein kinase cdelta) | SIGNOR-123453 |
Q00535 | Q13224 | 1 | phosphorylation | down-regulates quantity | 0.443 | Cdk5 phosphorylates NR2B at Ser1116 and controls surface level expression.|Reduction in Cdk5 activity, as well as disruption of Cdk5-NR2B interactions consistently increased NR2B surface levels and facilitated NMDA mediated synaptic function. | SIGNOR-278265 |
Q13153 | O15530 | 0 | phosphorylation | up-regulates activity | 0.357 | P21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1). We identify threonine 423, a conserved threonine in the activation loop of kinase subdomain VIII, as the PDK1 phosphorylation site on PAK1. | SIGNOR-250267 |
P04637 | Q15759 | 0 | phosphorylation | up-regulates | 0.611 | We show that prak activates p53 by direct phosphorylation. | SIGNOR-152843 |
Q12778 | Q14680 | 0 | phosphorylation | down-regulates quantity | 0.257 | Direct phosphorylation of FOXO1 and FOXO3 by MELK.|Our findings revealed that siRNA mediated MELK knockdown increased protein levels of FOXO1 and FOXO3, which might increase p21 transcriptional level in a p53 independent manner. | SIGNOR-279543 |
Q9NZ72 | P49841 | 0 | phosphorylation | up-regulates activity | 0.264 | Altogether, these results indicate that CDK5 phosphorylates similarly serines 68 and 73, whereas ERK2 targets mostly serine 68 and GSK-3beta mostly serine 60.|This observation may support the hypothesis of a specific localization of stathmin 3 depending on its phosphorylation by GSK-3beta | SIGNOR-264882 |
P04049 | Q5T447 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.2 | By western blot, we observed robust degradation of endogenous native CRAF in untransformed HEK293 cells treated with control siRNA 24 hr after the addition of AUY922, but this was substantially reduced in cells in which HECTD3 was knocked down, confirming that endogenous CRAF is a bona fide degradation target of HECTD... | SIGNOR-272328 |
P00519 | P78352 | 1 | phosphorylation | up-regulates activity | 0.441 | Moreover, c-Abl phosphorylates PSD-95 at tyrosine 533.|c-Abl modulates the synaptic contact number and PSD-95 clustering. | SIGNOR-278391 |
P11362 | O60506 | 1 | phosphorylation | down-regulates | 0.2 | Novel in vivo tyrosine phosphorylation sites were found in the fgfr-1, phospholipase cgamma, p90 ribosomal s6 kinase, cortactin, and ns-1-associated protein-1. Syncrip, was very recently found to be phosphorylated in response to insulin treatment of 3t3-l1 adipocytes (32). Phosphorylation of syncrip was accommodated by... | SIGNOR-98704 |
P17612 | Q14344 | 1 | phosphorylation | down-regulates activity | 0.366 | PKA directly phosphorylates Galpha(13). Galpha(13)-T203A mutant (in COS-7 cells) could not be phosphorylated by PKA. PKA blocks Rho activation by phosphorylation of Galpha(13) Thr(203). | SIGNOR-249985 |
Q13153 | Q13586 | 1 | phosphorylation | up-regulates activity | 0.354 | Taken together, our data demonstrate that PAK1 interacts with STIM1 and phosphorylates specific STIM1 cytosolic domains. | SIGNOR-279244 |
O14965 | P68431 | 1 | phosphorylation | up-regulates activity | 0.2 | Phosphorylation at ser-11 (h3s10ph) by aurkb is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. Phosphorylation at ser-11 (h3s10ph) by aurkb is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. | SIGNOR-98289 |
P62826 | O75592 | 0 | guanine nucleotide exchange factor | up-regulates activity | 0.296 | MYCBP2 Is a Nuclear GEF for Ran in DRG Neurons—Next, we studied whether or not MYCBP2 modulates the interaction between Ran/RanGAP1. MYCBP2 contains an N-terminal RCC1-like domain (Fig. 8C) (13), and RCC1 is a known GEF for Ran, indicating a potential functional interaction between MYCBP2 and Ran. | SIGNOR-261204 |
O15524 | P12931 | 0 | phosphorylation | down-regulates activity | 0.45 | SOCS1 is phosphorylated on Y80 by SRC family kinase members SRC and YES1. | SIGNOR-276857 |
Q99459 | O96017 | 0 | phosphorylation | down-regulates activity | 0.304 | Remarkably, however, the activation of the DDC triggers a Rad53-dependent phosphorylation of Cdc5 that inhibits the polo-like kinase, thus favoring Cdh1 activity and subsequently also restraining spindle elongation and anaphase progression [34,54] (Figure 1). | SIGNOR-279694 |
P17252 | O60928 | 1 | phosphorylation | down-regulates | 0.2 | After pharmacological pkc activation, kir7.1 currents were strongly inhibited. Co-application of pkc inhibitors attenuated this effect. Inactivation of pkc consensus sites also strongly attenuated the effect with a single site ((201)s) being essential for almost the total pkc sensitivity. | SIGNOR-181863 |
P23467 | P27361 | 1 | dephosphorylation | up-regulates | 0.432 | When cells are stimulated with various ligands such as growth factors, hormones, neurotransmitters, or tumor promoters, erk1/2 is activated through dualphosphorylation at the -ptepy-motif. Subsequently, p-erk1/2 translocates into the nucleus and phosphorylates elk-1, thereby acting as a transcription factor for cell pr... | SIGNOR-103165 |
P62805 | Q92585 | 0 | acetylation | down-regulates activity | 0.2 | We speculated that maml1, in addition to recruiting p300, might directly interact with histones to facilitate histone acetylation. We had observed acetylation of the histones h3 and h4. | SIGNOR-153041 |
P08047 | P60484 | 0 | dephosphorylation | down-regulates activity | 0.421 | Moreover, PTEN downregulates p75NTR expression by decreasing DNA-binding activity of Sp1 .|PTEN dephosphorylates the Sp1 transcription factor , the phosphorylation status of which directly impacts its ability to bind to some DNA promoter regions , . | SIGNOR-277119 |
P31749 | O15327 | 0 | dephosphorylation | down-regulates activity | 0.374 | Further, we show that INPP4B but not PTEN is able to reduce tyrosine phosphorylation of Akt1 and both the lipid and PTP activity of INPP4B likely contribute to the reduction of Akt1 phosphorylation.|Further, we show that INPP4B but not PTEN is able to reduce tyrosine phosphorylation of Akt1 and both the lipid and prote... | SIGNOR-277106 |
Q15746 | P24844 | 1 | phosphorylation | up-regulates | 0.838 | More than a dozen kinases have been reported to phosphorylate the rlcs of nm ii (fig. 2), including myosin light chain kinase (mlck;also known as mylk), rho-associated, coiled coil-containing kinase (rock), citron kinase, leucine zipper interacting kinase (zipk;also known as dapk3) and myotonic dystrophy kinase-related... | SIGNOR-188797 |
P84022 | Q09472 | 0 | acetylation | up-regulates quantity by stabilization | 0.736 | Smad proteins are crucial for the intracellular signaling of transforming growth factor-beta (TGF-beta). Upon their receptor-induced activation, Smad proteins are phosphorylated and translocated to the nucleus to activate the transcription of a select set of target genes. Here, we show that the co-activator p300/CBP bo... | SIGNOR-260431 |
Q00987 | P10914 | 1 | ubiquitination | down-regulates quantity | 0.388 | HIV-1 Tat Recruits HDM2 E3 Ligase To Target IRF-1 for Ubiquitination and Proteasomal Degradation.|IRF-1 ubiquitination by HDM2 is specifically increased during HIV-1 infection in the presence of increasing amounts of Tat and is mediated by the formation of a trimeric complex between Tat, IRF-1, and HDM2, as demonstrate... | SIGNOR-278590 |
O95835 | P49593 | 0 | dephosphorylation | down-regulates activity | 0.2 | POPX2 is capable of dephosphorylating LATS1 at Thr1079 (Figure xref ), which is a residue critical for LATS1 activity.|POPX2 might negatively regulate the activities of MST1 and LATS1 through dephosphorylation.|We found that POPX2 could dephosphorylate LATS1 on Threonine-1079, leading to inactivation of LATS1 kinase. | SIGNOR-276989 |
Q12888 | O75925 | 0 | sumoylation | up-regulates | 0.494 | Pias1 and pias4 are recruited to dna-damage sites and mediate 53bp1 recruitment and sumoylation. | SIGNOR-162156 |
P31749 | P51812 | 1 | phosphorylation | down-regulates activity | 0.265 | Akt interacts with and phosphorylates RSK2 at S19. | SIGNOR-277548 |
P15407 | P05412 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.826 | Members of the AP1 family distinctly regulated the fra-1 promoter. In particular, coexpression of c-Jun, Jun-D, and Fra-2 up-regulated fra-1 transcription. | SIGNOR-261604 |
P00519 | Q14247 | 1 | phosphorylation | up-regulates activity | 0.424 | Because phosphorylation by c-Abl augments nmMLCK-cortactin interaction to a greater degree than does pp60src phosphorylation, it is likely that phosphorylation sites on nmMLCK unique to c-Abl (i.e., other than Y464 and Y846) are responsible for this enhanced protein-protein interaction.|Moreover, our data indicate that... | SIGNOR-278504 |
P59595 | P16220 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.2 | The transcription factors c-Fos, FosB, CREB-1, and ATF2 were all activated by the addition of SARS-CoV N protein to the sample well | SIGNOR-260729 |
P04637 | P14672 | 1 | transcriptional regulation | down-regulates quantity by repression | 0.335 | P53 regulates basal expression of AIF and SCO2 and facilitates oxidative phosphorylation. The expression of GLUT1, GLUT4, and HK2 is negatively regulated by p53, whereas TIGAR expression is induced by p53. The net result of p53-mediated regulation of these glycolytic enzymes is the suppression of glycolysis. In additio... | SIGNOR-267465 |
P27540 | P68400 | 0 | phosphorylation | down-regulates | 0.34 | Here, we show that arnt and alt arnt proteins are differentially phosphorylated by protein kinase ckii in vitro. Phosphorylation had an inhibitory effect on dna-binding to an e-box probe by alt arnt, but not arnt, homodimers. This inhibitory phosphorylation occurs through ser77. | SIGNOR-140034 |
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