IdA string | IdB string | labels int64 | mechanism string | effect string | score float64 | sentence string | signor_id string |
|---|---|---|---|---|---|---|---|
P27816 | P33981 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.2 | We further uncovered that Mps1 is a kinase of MAP4, and E7-MAP4 binding blocks Mps1 phosphorylation of MAP4, thereby interrupting phosphorylation-dependent MAP4 degradation. | SIGNOR-277458 |
P19793 | P49841 | 0 | phosphorylation | up-regulates activity | 0.275 | GSK3β-induced RXRα phosphorylation decreased for RXRα-S49A, RXRα-S66A and RXRα-S78A in HEK293 cells compared with RXRα WT by western blot analysis. | SIGNOR-277371 |
Q16635 | O95835 | 0 | phosphorylation | down-regulates activity | 0.387 | When the inhibitory Hippo kinase module is ' on ', LATS1 and LATS2 phosphorylate and inactivate YAP and TAZ, and the output gene production is therefore turned off.|When the inhibitory Hippo kinase module is \u2018on\u2019, LATS1 and LATS2 phosphorylate and inactivate YAP and TAZ, and the output gene production is therefore turned off. | SIGNOR-279200 |
P78527 | Q9GZU7 | 0 | dephosphorylation | up-regulates activity | 0.2 | CTDSP1 activates DNA-PKcs and enhances DNA-PKcs dependent topoI degradation in response to irinotecan .|Our novel finding indicates that CTDSP1 dephosphorylates DNA-PKcs, changes its kinase activity, and regulates irinotecan-induced topoI degradation. | SIGNOR-277101 |
P23467 | P29474 | 1 | dephosphorylation | down-regulates activity | 0.267 | VE-PTP interacts with eNOS and dephosphorylates Tyr81 | SIGNOR-277521 |
P57073 | O14965 | 0 | phosphorylation | up-regulates activity | 0.2 | Therefore, Aurora-A not only directly phosphorylates SOX8 but also promotes SOX8 transcription indirectly by regulating c-Myc protein. | SIGNOR-280189 |
Q9NZQ7 | P46977 | 0 | glycosylation | up-regulates quantity by stabilization | 0.2 | Together, these results support a notion that the two STT3 isoforms regulate EMT-mediated PD-L1 induction through PD-L1 protein N-glycosylation and stabilization. | SIGNOR-274975 |
P04049 | P17252 | 0 | phosphorylation | down-regulates | 0.558 | Pka can inhibit raf-1 function directly via phosphorylation of the raf-1 kinase domain | SIGNOR-34761 |
Q12959 | P24941 | 0 | phosphorylation | up-regulates | 0.282 | We also show that dlg1 is phosphorylated by both cdk1 and cdk2 on ser158 and ser442. These phosphorylated sites together affect the nuclear localisation of the protein, and implicate the role of phosphorylation on ser158 and ser442 in its putative nuclear functions as a tumour suppressor. phosphorylation on ser158 and ser442 enhances nuclear expression of dlg1 | SIGNOR-182765 |
Q9P286 | Q9BY11 | 1 | phosphorylation | up-regulates activity | 0.2 | We identified two novel Pak5 substrates, Pacsin1 and Synaptojanin1, proteins that directly interact with one another to regulate synaptic vesicle endocytosis and recycling. Pacsin1 and Synaptojanin1 were phosphorylated by Pak5 and the other group II Paks in vitro, and Pak5 phosphorylation promoted Pacsin1-Synaptojanin1 binding both in vitro and in vivo. | SIGNOR-263025 |
Q9Y5Y9 | Q96PU5 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.32 | The control of Nav density at the cell membrane is crucial to ensuring normal neuronal excitability. Navs are subject to posttranslational modifications that may influence their cell membrane availability. Ubiquitylation is a key process that orchestrates the internalization and subsequent degradation or recycling of Navs. This is accomplished by ubiquitin protein ligases, such as NEDD4-2 (neuronal precursor cell expressed developmentally downregulated-4 type 2). | SIGNOR-253463 |
P29034 | Q9UNE7 | 0 | polyubiquitination | down-regulates quantity by destabilization | 0.318 | S100 protein itself is ubiquitinated by CHIP in a Ca2+-dependent manner.Ubiquitylated S100 proteins are shown as (Ub)n-S100A2 and (Ub)n-S100P. The association of the S100 proteins with CHIP provides a Ca2+-dependent regulatory mechanism for the ubiquitination and degradation of intracellular proteins by the CHIP-proteasome pathway. | SIGNOR-272918 |
P10636-2 | Q02156 | 0 | phosphorylation | down-regulates activity | 0.271 | 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 somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs. | SIGNOR-275444 |
Q6NUN9 | P00519 | 0 | phosphorylation | up-regulates activity | 0.313 | C-Abl-mediated phosphorylation of PARIS at Y137 (within the Krüppel-associated box domain) drives its association with KAP1 and the repression of genes with diverse functions in pathways such as chromatin remodelling and p53-dependent cell death. | SIGNOR-277626 |
P04114 | Q9UKV5 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.29 | In physiological condition, the unnecessary apoB is usually ubiquitinated by E3 ligase AMFR, and subsequently degraded by ubiquitination proteasomes. | SIGNOR-278685 |
Q9UK17 | P12931 | 0 | phosphorylation | up-regulates activity | 0.337 | These results indicate that Y108 (for Src-family kinases) and Y136 (for EGFR kinase) are involved in the tyrosine phosphorylation of hKv4.3 channels. | SIGNOR-276393 |
P00533 | P46108 | 1 | phosphorylation | down-regulates activity | 0.74 | To address these questions, we have developed an antibody that specifically recognizes the CrkII protein phosphorylated on Tyr221, and we found that the EGF receptor directly phosphorylates CrkII on Tyr221. Furthermore, we observed that the phosphorylation of Tyr221 of CrkII correlated with its dissociation from the EGF receptor, implicating the phosphorylation of Tyr221 in the negative feedback of binding to the EGF receptor. | SIGNOR-251091 |
Q15276 | Q15139 | 0 | phosphorylation | up-regulates activity | 0.382 | PKD phosphorylates Rabaptin-5 at Ser407, and this controls alphavbeta3 and alpha5beta1 integrin and EGFR recycling. | SIGNOR-278192 |
Q13464 | P42574 | 0 | cleavage | up-regulates | 0.734 | Rock i is cleaved by casp3 at a conserved detd1113/g sequence and its carboxy-terminal inhibitory domain is removed, resulting in deregulated and constitutive kinase activity. | SIGNOR-106546 |
Q92830 | P68431 | 1 | acetylation | down-regulates activity | 0.2 | The HAT module within the SAGA and ADA complexes acetylates histone H3, mainly on residues K9 and K14. | SIGNOR-269602 |
Q9H1A4 | P53350 | 0 | phosphorylation | up-regulates | 0.524 | Our analysis revealed an unexpected and unprecedented complexity of mitotic phosphorylation sites and suggests that other kinases than cdk1 and plk1 also contribute to apc phosphorylation. | SIGNOR-119881 |
Q8WV44 | Q8N884 | 1 | ubiquitination | up-regulates activity | 0.2 | Our finding that RINCK positively regulates cGAS activation by mediating the monoubiquitination of cGAS uncovers the function of RINCK in cGAS mediated innate immunity.|Together, these data suggest that RINCK mediates cGAS monoubiquitination. | SIGNOR-278794 |
Q9Y6R1 | Q9UEW8 | 0 | phosphorylation | down-regulates activity | 0.348 | SPAK phosphorylates the transporters to reduce their surface expression and thus their activity and consequently inhibits ductal secretion to stabilize the resting state. PP1 reverses the effect of SPAK. Molecular analysis revealed that the WNK kinases acted as scaffolds to recruit SPAK, which phosphorylated CFTR and NBCe1-B, reducing their cell surface expression. | SIGNOR-263133 |
O60353 | Q9ULT6 | 0 | ubiquitination | down-regulates quantity | 0.614 | Here we show that the cell-surface transmembrane E3 ubiquitin ligase zinc and ring finger 3 (ZNRF3) and its homologue ring finger 43 (RNF43) are negative feedback regulators of Wnt signalling. ZNRF3 is associated with the Wnt receptor complex, and inhibits Wnt signalling by promoting the turnover of frizzled and LRP6. | SIGNOR-260114 |
P00519 | P04040 | 1 | phosphorylation | up-regulates activity | 0.403 | 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-101302 |
P37840 | P53350 | 0 | phosphorylation | down-regulates activity | 0.351 | Polo-like kinase (plk) family (plk1, plk2, and plk3) phosphorylate alpha-syn and beta-syn specifically at ser-129 and ser-118, respectively. Polo-like kinase 2 (plk2) phosphorylates alpha-synuclein at serine 129 in central nervous system. The membrane association of pd-linked mutant alpha -synuclein, but not wild-type -synuclein, was increased by serine 129 phosphorylation. | SIGNOR-189045 |
P48729 | O60716 | 1 | phosphorylation | up-regulates activity | 0.2 | Moreover, CK1α phosphorylates p120-catenin on Ser268 and Ser269, releasing this protein from the signalosome and facilitating the subsequent phosphorylation of cadherin and the disruption of this cadherin interaction with LRP5/6 | SIGNOR-277893 |
P21802 | Q04760 | 1 | 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 the Src family (Src, Yes1, FGR, and the related Abl1), and of the FAK, EPHA, FGFR, and VEGFR families (Figure 2B), suggesting phosphorylation of Glo1 on Y136 by multiple different kinases. In vitro kinase assays revealed that all the members of the Src family, as well as Epha5 and VEGFR3, can efficiently phosphorylate recombinant Glo1 on Y136 (Figure 2C–D). | SIGNOR-276184 |
P17661 | P23409 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.242 | Desmin, the muscle specific intermediate filament (IF) protein, is expressed at low levels in myoblasts and at the onset of differentiation its expression increases several fold. In an effort to explore the mechanism involved in the tissue-specific and developmentally regulated expression of desmin, we have isolated the mouse desmin gene.Co-transfection of myoD, myogenin, MRF4 and Myf5, with the desmin-CAT construct into 10T-1/2 cells demonstrated that all these factors could transactivate desmin gene expression | SIGNOR-241497 |
P26045 | P55072 | 1 | dephosphorylation | down-regulates activity | 0.478 | Identification of VCP as a substrate of PTPH1in vivo.|The tyrosines (Tyr796 and Tyr805) at the C terminus of VCP have been reported to be the major sites of phosphorylation, with Tyr805 accounting for more than 90% of the tyrosine phosphorylation on the protein |The Y796F/Y805F VCP mutant was not associated with any of the PTPH1 constructs. | SIGNOR-248460 |
Q2TAL8 | Q9UGM6 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.2 | QRICH1 promotes the expression of translation-related genes. our combined ChIP-seq and RNA-seq analyses identified that QRICH1 and ATF4 were enriched at the promoters of these specific tRNA synthetases, and that ER stress positively regulated their transcription (Fig. 4I). Together, these findings suggest that QRICH1 and ATF4 modulate tRNA metabolic processes to promote secreted protein synthesis during ER stress. | SIGNOR-269411 |
P08631 | P08151 | 1 | phosphorylation | up-regulates activity | 0.299 | These results suggest that the interaction between Gli1 and Hck or the phosphorylation of Gli1 by Hck disrupts Sufu-Gli1 interaction.|We showed that tyrosine kinase Hck activates Gli1 and the kinase activity is required for its maximum effect. | SIGNOR-279374 |
P45983 | P08047 | 1 | phosphorylation | up-regulates | 0.705 | In addition, for mutation of the jnk-1 phosphorylated residues of sp1, namely, sp1(t278/739a) and sp1(t278/739d), the effect of ga on sp1 stability was reversed. | SIGNOR-184194 |
O96017 | P62380 | 1 | phosphorylation | down-regulates activity | 0.291 | In vitro, TRF2 was phosphorylated by recombinant Chk2 ( Figure\u00a04 C) on residues located in the first 350 aa ( Figure\u00a0S11 ).|To evaluate whether Chk2 activity affected the binding of TRF2 for telomeric TTAGGG repeats in duplex DNA, electrophoretic mobility shift assays (EMSA) were performed in the presence of ATP to allow phosphorylation and found that in contrast to Chk2 KD, Chk2 WT decreased the binding of TRF2 to DNA. | SIGNOR-280227 |
O00712 | Q9Y6N7 | 1 | transcriptional regulation | up-regulates quantity | 0.246 | For example, within the NFI targetome, we identified 6 collagen genes, 13 genes encoding potassium channel or glutamate receptor subunits and a range of factors related to axon guidance (e.g. Slit1, Robo1, Epha4, Epha5, Epha8) | SIGNOR-268900 |
O60346 | P05771 | 1 | dephosphorylation | down-regulates quantity | 0.341 | Here we show that the two PHLPP isoforms, PHLPP1 and PHLPP2, also dephosphorylate the hydrophobic motif on PKC betaII, an event that shunts PKC to the detergent-insoluble fraction, effectively terminating its life cycle | SIGNOR-237047 |
O76050 | P78504 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.707 | We find that NEDD4 targets an RNA-binding protein, NANOS2, in spermatogonia to destabilize it, leading to cell differentiation.|Jagged1 is also regulated by the E3 ligase Neuralized-like1 (Neurl1), which induces the monoubiquitination of membrane tethered Jagged1 in the C-terminal region. | SIGNOR-278772 |
P49959 | P09874 | 0 | relocalization | up-regulates activity | 0.2 | PARP1 collaborates with Mre11 to promote replication fork restart after release from replication blocks, most likely by recruiting Mre11 to the replication fork to promote resection of DNA. | SIGNOR-272478 |
Q02156 | O15530 | 0 | phosphorylation | up-regulates | 0.573 | In the present study, we analysed the contribution of the phosphoinositide-dependent kinase 1 (pdk-1) and pkcepsilon kinase activity in controlling the phosphorylation of thr(566) and ser(729). pdk-1 phosphorylation of the activation loop triggers autophosphorylation of the hydrophobic motif | SIGNOR-117320 |
O43791 | P10071 | 1 | ubiquitination | down-regulates quantity | 0.704 | RNAi knockdown of Spop (a substrate-binding adaptor for the cullin3-based ubiquitin E3 ligase) in Sufu mutant mouse embryonic fibroblasts (MEFs) can restore the levels of Gli2 and Gli3 full-length proteins | SIGNOR-268861 |
P02679 | P45452 | 0 | cleavage | down-regulates quantity by destabilization | 0.2 | Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-matrix metalloproteinase (MT1-MMP, MMP-14) in the degradation of fibrinogen and Factor XII of the plasma clotting system.|MMP-13 27YVATRDN g-chain| 20ADSGEGD a-chain| 124RNSVDXLNXN b-chain| 442LRTGKEKV a-chain | SIGNOR-263614 |
Q14164 | P10914 | 1 | phosphorylation | down-regulates activity | 0.35 | We demonstrated that IKK-ε phosphorylated the transcription factor IFN regulatory factor 1 (IRF-1) at amino acid (aa) 215/219/221 in primary CD4(+) T cells and blocked its transcriptional activity. | SIGNOR-276480 |
Q8WWK9 | Q96GD4 | 0 | phosphorylation | up-regulates | 0.296 | Here, we report that tmap is a novel substrate of the aurora b kinase. Ser627 of tmap was specifically phosphorylated by aurora b both in vitro and in vivo. Nearly all mutations at the phosphorylation motif had dramatic effects on the subcellular localization of tmap. | SIGNOR-165410 |
Q9UQM7 | P49593 | 0 | dephosphorylation | down-regulates | 0.331 | Ppm1f specifically dephosphorylates the phospho-thr-286 in autophosphorylated camkii substrate and thus deactivates the camkii in vitro. | SIGNOR-124309 |
O14492 | P31749 | 0 | phosphorylation | up-regulates activity | 0.4 | This study identifies APS as a novel physiological substrate for PKB and the first serine phosphorylation site on APS | SIGNOR-252557 |
Q9H6Y7 | Q96BI1 | 1 | polyubiquitination | down-regulates quantity by destabilization | 0.525 | Here, we present evidences indicating that RING105, a novel conserved RING-finger protein with a PA (protease-associated) domain and a PEST sequence, is a ubiquitin ligase for TSSC5 that can function in concert with the ubiquitin-conjugating enzyme UbcH6. The polyubiquitin target site on TSSC5 was mapped to a region in the 6th hydrophilic loop. | SIGNOR-271551 |
Q13418 | Q8TAE6 | 1 | phosphorylation | up-regulates activity | 0.546 | Pka predominantly phosphorylated a site distinct from the inhibitory t73 in kepi. Integrin-linked kinase phosphorylated KEPI (T73) and this dramatically increased inhibition of PP1c | SIGNOR-101835 |
P26640 | Q2TAL8 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.2 | QRICH1 promotes the expression of translation-related genes. our combined ChIP-seq and RNA-seq analyses identified that QRICH1 and ATF4 were enriched at the promoters of these specific tRNA synthetases, and that ER stress positively regulated their transcription (Fig. 4I). Together, these findings suggest that QRICH1 and ATF4 modulate tRNA metabolic processes to promote secreted protein synthesis during ER stress. | SIGNOR-269408 |
Q6UVJ0 | Q969U6 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.536 | We identify the centriolar protein HsSAS-6 (refs 4,5) as a critical substrate of the SCF-FBXW5 complex. FBXW5 binds HsSAS-6 and promotes its ubiquitylation in vivo. |expression of the wild-type form of FBXW5 accelerated the degradation of HsSAS-6 to a half-life of less than two hours | SIGNOR-275478 |
O75030 | P28482 | 0 | phosphorylation | down-regulates | 0.705 | The current study reveals that c-kit signaling triggers two phosphorylation events on mi, which up-regulate transactivation potential yet simultaneously target mi for ubiquitin-dependent proteolysis. The specific activation/degradation signals derive from mapk/erk targeting of serine 73the results suggested that s1p reduced melanin synthesis via s1p(3) receptor-mediated erk and rsk-1 activation, and subsequent mitf dual phosphorylation and degradation. | SIGNOR-75030 |
Q96HP0 | P63000 | 1 | guanine nucleotide exchange factor | up-regulates activity | 0.528 | Dock6 is a guanine nucleotide exchange factor (GEF) that activates the Rho family guanosine triphosphatases Rac1 and Cdc42 to regulate the actin cytoskeleton. | SIGNOR-275670 |
P53350 | Q7L2Z9 | 1 | phosphorylation | down-regulates quantity by destabilization | 0.588 | Notably, although Plk1 did not alter the level of PBIP1 and CENP-Q ubiquitination, Plk1-dependent phosphorylation and delocalization of these proteins from kinetochores appeared to indirectly lead to their degradation in the cytosol. From these analyses, we identified nine CENP-Q residues (Thr-123, Thr-135, Ser-138, Ser-139, Ser-248, Ser-249, Ser-253, Ser-255, and Thr-256) that were phosphorylated in both in vitro and in vivo samples (Fig. 4B), suggesting that Plk1 phosphorylates these sites. | SIGNOR-265227 |
O15297 | O96017 | 1 | dephosphorylation | up-regulates activity | 0.572 | an in vitro phosphatase assay revealed that Wip1 (WT), but not Wip1 (D314A), dephosphorylates Thr68 on phosphorylated Chk2 in vitro, resulting in the inhibition of Chk2 kinase activity toward glutathione S-transferase-Cdc25C. | SIGNOR-248318 |
P53350 | O95251 | 1 | phosphorylation | up-regulates | 0.503 | Here, we show that the interaction between plk1 and hbo1 is mitosis-specific and that plk1 phosphorylates hbo1 on ser-57 in vitro and in vivo. During mitosis, cdk1 phosphorylates hbo1 on thr-85/88, creating a docking site for plk1 to be recruited. Significantly, the overexpression of hbo1 mutated at the plk1 phosphorylation site (s57a) leads to cell-cycle arrest in the g1/s phase, inhibition of chromatin loading of the minichromosome maintenance (mcm) complex, and a reduced dna replication rate. | SIGNOR-160751 |
O15264 | P46734 | 0 | phosphorylation | up-regulates activity | 0.607 | p38-δ is activated by environmental stress, extracellular stimulants, and MAPK kinase-3, -4, -6, and -7. we investigated whether this Thr180-Gly-Tyr182 motif was essential for p38-δ activation. Taken together, these results suggest that the dual phosphorylation TGY motif is required for p38-δ activation. | SIGNOR-273950 |
Q00535 | P37231 | 1 | phosphorylation | down-regulates activity | 0.574 | CDK5 in turn phosphorylates PPARgamma at Ser273 and prevents the transcription of specific PPARgamma target genes that have anti-diabetic effects . | SIGNOR-278189 |
P12931 | O95297 | 1 | phosphorylation | up-regulates | 0.468 | Indeed, our studies indicated that cross-linking of pzr by cona lead to activation of c-src, which may be responsible for phosphorylation of pzr and possibly other proteins. Phosphorylation of pzr in turn recruits shp-2, which by itself is an essential signal transducertyrosine residues 241 and 263 embedded in the itims are responsible for the tyrosine phosphorylation of pzr | SIGNOR-113410 |
O14867 | P09601 | 1 | transcriptional regulation | down-regulates quantity | 0.361 | These results indicate that ho-1 regulation involves a competition between the activator Nrf2 and the Bach1 repressor for interactions with the small Maf proteins. | SIGNOR-259336 |
P43354 | Q9UPW6 | 0 | transcriptional regulation | down-regulates quantity | 0.295 | Satb2 represses the transcription of Nr4a2. The misexpression of Nr4a2 together with Ctip2 induces expression of SubC-specific genes in wild-type Rsp, and simultaneous knockdown of these two genes in Rsp Satb2-mutant cells prevents their fate transition to SubC identity. Thus, Satb2 serves as a determinant gene in the Rsp regionalization by repressing Nr4a2 and Ctip2 during cortical development | SIGNOR-268930 |
O15554 | P22392 | 0 | phosphorylation | up-regulates | 0.419 | We previously showed that nucleoside diphosphate kinase beta (ndpk-b), a mammalian histidine kinase, is required for kca3.1 channel activation in human cd4 t lymphocytes. | SIGNOR-181083 |
P11413 | O60502 | 0 | deglycosylation | down-regulates activity | 0.2 | O-GlcNAcylation of G6PD promotes the pentose phosphate pathway and tumor growth|O-GlcNAcylation of G6PD activates enzyme activity|G6PD is dynamically modified by O-GlcNAc at serine 84|In cells, a single set of antagonistic enzymes-O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase are responsible for the addition and removal of GlcNAc moiety, respectively. | SIGNOR-267605 |
O43524 | O75874 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.248 | We identify FOXOs as transcriptional activators of IDH1. FOXOs promote IDH1 expression and thereby maintain the cytosolic levels of α-ketoglutarate and NADPH. | SIGNOR-260100 |
P14921 | Q9Y458 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.2 | TBX22 is an X-linked gene, which encodes a T-box-containing transcription factor. Loss-of-function mutation in the X-linked TBX22 promoter disrupts an ETS-1 binding site and leads to cleft palate. We first link the transcription factor ETS-1 to TBX22 pathway during embryonic palatogenesis. | SIGNOR-265565 |
P42566 | O60260 | 0 | ubiquitination | up-regulates | 0.2 | Treatment of cells with egf stimulates parkin binding to both eps15 and the egfr and promotes parkin-mediated ubiquitination of eps15 | SIGNOR-148218 |
P10916 | Q15746 | 0 | phosphorylation | up-regulates activity | 0.72 | MLCK directly phosphorylates MLC2 and is a substrate for ERK1/2 ( ), thus providing a direct link between the Raf-MEK1/2-ERK1/2 module and MLC2.|These findings strongly suggest that the phosphorylation of MLC2 stimulated by MLCK and ROCK1/2 is an integral component of the biochemical signal transduction program that promotes noninvasive motility. | SIGNOR-279233 |
O43164 | P31321 | 1 | polyubiquitination | down-regulates quantity by destabilization | 0.2 | Praja2 controls the stability of PKA regulatory subunits. Praja2 ubiquitylates RIIα/β subunits. Subunits | SIGNOR-271857 |
P17612 | O14649 | 1 | phosphorylation | up-regulates activity | 0.2 | Mutation of the ser393 to alanine, which can neither be phosphorylated nor mimic a phosphorylated residue, resulted in the channel failing to pass current all of our findings support the conclusion that camp-dependent protein kinase is responsible for the phosphorylation of the terminal serine in both k2p3.1 and k2p9.1. | SIGNOR-172430 |
P42229 | Q9BZS1 | 1 | null | up-regulates | 0.48 | We demonstrate that the signal transducer and activator of transcription 5 (STAT5)-signaling cytokines, IL-2, IL-15 and to a lesser extent IL-7, induce FOXP3 up-regulation in vitro in activated human Teff cell | SIGNOR-254301 |
P02686 | P28482 | 0 | phosphorylation | down-regulates | 0.553 | Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence. | SIGNOR-22420 |
P45983 | Q16621 | 1 | phosphorylation | down-regulates quantity by destabilization | 0.411 | Through use of different approaches including nano-scale proteomics, we show that activated-JNK, or Phospho-JNK (P-JNK), physically interacts with p45/NF-E2 and phosphorylates its Ser157 residue. This reaction leads to the poly-ubiquitination of p45/NF-E2 at one or more of six Lys residues, one of which being also a sumoylation site, and its degradation through the proteasome pathway. | SIGNOR-275552 |
P04004 | P05771 | 0 | phosphorylation | up-regulates quantity by stabilization | 0.303 | Phosphorylation of vitronectin on Ser362 by protein kinase C attenuates its cleavage by plasmin. | SIGNOR-248963 |
Q15633 | Q9UBS0 | 0 | phosphorylation | up-regulates activity | 0.333 | We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. | SIGNOR-274066 |
O60260 | Q07817 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.2 | In cells, we found BCL-XL levels were reduced by overexpression of PARK2, but this catalytic activity was blocked by the proteasome inhibitor MG132, suggesting degradation of BCL-XL protein by PARK2 is dependent on the proteasome system (XREF_FIG A).|PARK2 directly binds to and ubiquitinates BCL-XL. | SIGNOR-278661 |
Q05655 | P07108 | 1 | phosphorylation | up-regulates | 0.2 | Acyl coenzyme a-binding protein (acbp) is phosphorylated following protein kinase c activation. | SIGNOR-160393 |
O95786 | P36873 | 0 | dephosphorylation | up-regulates activity | 0.2 | We identified PP1alpha and PP1gamma as primary phosphatases responsible for MDA5 and RIG-I dephosphorylation, leading to their activation.|endogenous RIG-I and MDA5 that interacted with PP1 exhibited markedly decreased phosphorylation levels at S8 and S88, respectively | SIGNOR-264580 |
P46695 | Q00987 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.349 | FHL2 stimulates MDM2 mediated ubiquitination of IER3 by forming a ternary complex.|Scaffold protein FHL2 facilitates MDM2 mediated degradation of IER3 to regulate proliferation of cervical cancer cells. | SIGNOR-278824 |
P49815 | Q05086 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.629 | An in vivo ubiquitination assay was done to reveal that E6AP promoted the ubiquitination of TSC2 independent of HPV16 E6. We further found that TSC2 bound E6AP in the presence as well as in the absence of HPV16 E6. The binding regions on E6AP and TSC2 have been identified as amino acid (aa) 260-316, aa 428-500 and aa 1-175, aa 1251-1807, respectively. Taken together, degradation of TSC2 is mediated by E6AP ubiquitin ligase. | SIGNOR-271396 |
Q9HCP0 | Q12778 | 1 | phosphorylation | down-regulates activity | 0.494 | Phosphorylation of Ser319 forms a consensus sequence for phosphorylation by CK1, allowing it to phosphorylate Ser322, which in turn primes the CK1-catalysed phosphorylation of Ser325 | Multisite phosphorylation of the region containing Ser319, Ser322, Ser325 and Ser329 provides a signal for the nuclear exclusion of FKHR | SIGNOR-250822 |
Q9HD43 | P06213 | 1 | dephosphorylation | down-regulates | 0.27 | These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase | SIGNOR-76072 |
Q9NQU5 | P53667 | 1 | phosphorylation | up-regulates activity | 0.2 | PAK6 bound to LIMK1 and activated it via phosphorylation at Thr-508.|These data indicated that PAK6 directly phosphorylated LIMK1 at Thr-508. | SIGNOR-278970 |
P27361 | P25098 | 1 | phosphorylation | down-regulates | 0.2 | Erk1 phosphorylates grk2 at ser(670). Inhibition of erk activity in hek293 cells potentiates grk2 activity, whereas, conversely, erk activation inhibits grk2 activity. | SIGNOR-72582 |
Q7Z569 | Q9UNH5 | 1 | polyubiquitination | up-regulates activity | 0.337 | Brap2 promotes Lys-63 linked ubiquitination of HsCdc14A. Collectively, these results support the idea that Brap2 facilitates Lys-63 linked ubiquitin modification of HsCdc14A, which may not be targeted for degradation, but mainly for protein–protein interactions or other regulatory functions. | SIGNOR-271777 |
P16220 | Q15418 | 0 | phosphorylation | up-regulates activity | 0.747 | The rsks phosphorylate the trascription factor creb at serine 133 to promote cell survival. | SIGNOR-72117 |
P06493 | O00311 | 1 | phosphorylation | up-regulates | 0.535 | Hucdc7 and ask proteins can also be phosphorylated by cdks in vitro. Among four possible cdk phosphorylation sites of hucdc7, replacement of thr-376, corresponding to the activating threonine of cdk, with alanine (t376a mutant) dramatically reduces kinase activity, indicative of kinase activation by phosphorylation of this residue. | SIGNOR-78311 |
Q63HR2 | P30530 | 0 | phosphorylation | up-regulates quantity | 0.2 | In this study, however, we demonstrate for the first time that Axl directly binds to and phosphorylates TNS2 at Y483.|Overall these results suggest that Axl positively regulates TNS2 expression. | SIGNOR-278471 |
P34947 | O75581 | 1 | phosphorylation | up-regulates | 0.548 | we found that g protein-coupled receptor kinases 5 and 6 (grk5/6), traditionally known to phosphorylate and desensitize 7tm g protein-coupled receptors, directly phosphorylate the pppsp motifs on single transmembrane lrp6 and regulate wnt/lrp6 signaling | SIGNOR-23330 |
Q9Y6N7 | O00712 | 0 | transcriptional regulation | up-regulates quantity | 0.246 | For example, within the NFI targetome, we identified 6 collagen genes, 13 genes encoding potassium channel or glutamate receptor subunits and a range of factors related to axon guidance (e.g. Slit1, Robo1, Epha4, Epha5, Epha8) | SIGNOR-268900 |
Q9UN86 | P25963 | 1 | relocalization | down-regulates activity | 0.342 | IkappaBalpha interacts with G3BP2 both in vivo and in vitrothrough the IkappaBalpha CRS. Overexpression of G3BP2 directly promotes retention of IkappaBalpha in the cytoplasm. | SIGNOR-260985 |
Q05655 | P49815 | 1 | phosphorylation | down-regulates activity | 0.2 | In vivo kinase analysis further indicated that both S932 and S939 are phosphorylated in response to translation inhibitors. Finally, phosphorylation defective TSC2 mutants (S932A and S939A single mutants and a S932A/S939A double mutant) failed to upregulate mTORC1 activity in the presence of translation inhibitors, suggesting that activation of mTORC1 by translation inhibitors is mediated by PKC-δ phosphorylation of TSC2 at S932/S939, which inactivates TSC. | SIGNOR-277427 |
P49841 | Q9UKT6 | 1 | phosphorylation | up-regulates activity | 0.2 | GSK-3beta phosphorylates FBXL21 and TCAP to activate FBXL21-mediated, phosphodegron-dependent TCAP degradation.|These results show direct GSK-3beta phosphorylation of TCAP S157 and FBXL21 T33 sites. | SIGNOR-264851 |
Q00987 | Q13469 | 1 | ubiquitination | down-regulates quantity | 0.306 | MDM2 negatively regulates NFATc2 and T cell activation.|The E3 ubiquitin ligase MDM2 is known to induce NFATc2 ubiquitination in a breast cancer cell line 24. | SIGNOR-278657 |
Q9HC98 | Q8TD19 | 0 | phosphorylation | up-regulates activity | 0.69 | Nercc1/nek9 activates the nek6 and nek7 kinases. Nercc1 catalyzes the direct phosphorylation of prokaryotic recombinant nek6 at ser206 in vitro concomitant with 20-25-fold activation of nek6 activity. | SIGNOR-102996 |
P27361 | Q86UR1 | 1 | phosphorylation | down-regulates | 0.267 | Accumulating evidence indicates that protein phosphorylation regulates nox activity. In this report, we show that serine282 residue of nox activator 1 (noxa1) is phosphorylated by erk in response to egf resulting in desensitization of nox1 activity | SIGNOR-164231 |
P00734 | P38435 | 0 | carboxylation | up-regulates activity | 0.669 | We analyzed the number of glutamic acid (Glu) residues and their positions in the Gla domain (GD) of DCP to investigate the gamma-carboxylation mechanism of VK-dependent carboxylase. Several DCPs were found in each subject studied. The 10 Gla residues of human prothrombin were carboxylated in order from the N-terminal (residues 26, 25, 16, 29, 20, 19, 14, 32, 7 and 6)|In the absence of VK or in the presence of VK antagonists, hepatic VKdependent carboxylase activity is inhibited and des-g-carboxyprothrombin (abnormal prothrombin or PIVKA; protein induced by vitamin K antagonist, prothrombin) is released into the blood. | SIGNOR-263676 |
Q9H6Y7 | Q15836 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.328 | Here, we show that Godzilla/RNF167 regulates endosome recycling by the ubiquitylation of VAMP3 on Lys66, Lys68 and Lys77; namely, two adjacent Lys residues on the both sides of the critical interface of SNARE complex are ubiquitylated. In agreement with VAMP3 being a target for Goliath family ubiquitin ligases, we show that recycling endosome trafficking is abrogated in response to their activity. While we observed ubiquitylation of VAMP3 by Godzilla, we are unable to describe the nature of this ubiquitination, be it mono-ubiquitin or extended ubiquitin chains. | SIGNOR-272093 |
P09238 | O00755 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.2 | We first proved that Wnt7a activated the canonical Wnt pathway through direct regulation of the MMP10 gene. | SIGNOR-278867 |
Q00532 | P06400 | 1 | phosphorylation | up-regulates activity | 0.2 | We also proved that as a downstream molecule of the P15 pathway, Rb is inhibited after CDKL1 knockdown. Rb is a well-known tumor suppressor in cell cycle regulation.28 Phosphorylation of Rb negatively regulates the cell cycle through E2F repression.29–31 However, Rb contains 13 conserved sites that are phosphorylated by the CDK–P15 complex in cycling cells and phosphorylation will cause site-specific and diverse conformational changes in the complex.32,33 Further studies need to be conducted to decipher the phosphorylated site of Rb related to CDKL1 knockdown. | SIGNOR-273863 |
Q13315 | Q9UQR1 | 1 | phosphorylation | up-regulates | 0.36 | Here we found that zbp-89 is phosphorylated by atm kinase in vitro and in vivo. Disruption of the atm phosphorylation motif (202)sq within the zinc finger domain of zbp-89 attenuated its ability to enhance p21(waf1) activation by butyrate. Moreover, disruption of the atm phosphorylation site abrogated the ability of zbp-89 to potentiate butyrate induction of endogenous p21(waf1) expression. | SIGNOR-155634 |
Q13627 | P55211 | 1 | phosphorylation | down-regulates activity | 0.388 | Depletion of DYRK1A from human cells by short interfering RNA inhibits the basal phosphorylation of caspase 9 at an inhibitory site, Thr125. DYRK1A-dependent phosphorylation of Thr125 is also blocked by harmine, confirming the use of this beta-carboline alkaloid as a potent inhibitor of DYRK1A in cells.|When co-expressed in cells, DYRK1A interacts with caspase 9, strongly induces Thr125 phosphorylation and inhibits caspase 9 auto-processing. | SIGNOR-279326 |
Q13263 | P09467 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.31 | In this study, we demonstrated that the tripartite motif-containing protein 28 (TRIM28) binds directly to and promotes FBP1 for ubiquitination and degradation. MAGE-A3 and MAGE-C2, which are known to be overexpressed in HCC, can enhance TRIM28-dependent degradation of FBP1 by forming ubiquitin ligase complexes with TRIM28. | SIGNOR-267591 |
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