IdA
string
IdB
string
labels
int64
mechanism
string
effect
string
score
float64
sentence
string
signor_id
string
Q01484
Q9UJW0
1
relocalization
up-regulates quantity
0.625
We present evidence for an ankyrin-based mechanism for sarcolemmal localization of dystrophin and beta-DG. Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4.
SIGNOR-266713
Q12923
P06213
1
dephosphorylation
down-regulates
0.26
We demonstrate that ptpl1, like ptp1b, interacts with and dephosphorylates a bis-phosphorylated insulin receptor peptide more efficiently than monophosphorylated peptides, indicating that ptpl1 may down-regulate the phosphatidylinositol 3-kinase pathway, by dephosphorylating insulin or growth factor receptors that contain tandem phosphotyrosines.
SIGNOR-132555
Q92529
Q9UM73
0
phosphorylation
up-regulates
0.44
Anaplastic lymphoma kinase (alk), which turned out to be one of these phosphoproteins, was constitutively activated and associated with the ptb domain of shcc in three neuroblastoma cells. In vitro kinase assay revealed that shcc is a potent substrate of the activated alk kinase. The alk gene locus was significantly amplified in both of these cell lines, suggesting that gene amplification leads to constitutive activation of the alk kinase, which results in hyperphosphorylation of shcc.
SIGNOR-91537
P04908
Q9H3R0
0
demethylation
down-regulates activity
0.2
As one member of the Jumonji-C histone demethylase family, JMJD2C has the ability to demethylate tri- or di-methylated histone 3 and 2 in either K9 (lysine residue 9) or K36 (lysine residue 36) sites by an oxidative reaction, thereby affecting heterochromatin formation, genomic imprinting, X-chromosome inactivation, and transcriptional regulation of genes.JMJD2C has been proved to be a demethylase for H3K9 methylation, in the manner of catalyzing the demethylation of H3K9me3/me2 (the known repressive markers of gene regulation), a histone mark found in heterochromatin associated with euchromatic transcriptional silencing and heterochromatin formation
SIGNOR-263862
P60321
P46934
0
ubiquitination
down-regulates quantity by destabilization
0.2
We find that NEDD4 targets an RNA-binding protein, NANOS2, in spermatogonia to destabilize it, leading to cell differentiation.|To examine whether complex formation of NEDD4 and NDFIP2 promotes NANOS2 ubiquitination in vivo, FLAG tagged NANOS2 was expressed in HEK293 cells with or without MYC-NEDD4 and MYC-NDFIP2.
SIGNOR-278770
O43781
Q96B36
1
phosphorylation
down-regulates
0.34
When dyrk3 is active, it allows stress granule dissolution, releasing mtorc1 for signaling and promoting its activity by directly phosphorylating the mtorc1 inhibitor pras40
SIGNOR-201002
Q12888
O15264
0
phosphorylation
down-regulates activity
0.2
Here we show that 53BP1 is phosphorylated during mitosis on two residues, T1609 and S1618, located in its well-conserved ubiquitination-dependent recruitment (UDR) motif.|Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks |phosphorylation of T1609 is likely to be mediated by p38 MAPK
SIGNOR-264449
Q13131
Q9UBK2
1
phosphorylation
up-regulates activity
0.575
Ampk phosphorylates pgc-1alpha directly both in vitro and in cells. These direct phosphorylations of the pgc-1alpha protein at threonine-177 and serine-538.
SIGNOR-156780
Q9Y243
P67775
0
dephosphorylation
down-regulates activity
0.738
Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes
SIGNOR-248654
P15923
Q15759
0
phosphorylation
up-regulates
0.436
Here we show that p38 mapk, whose activity is essential for myogenesis, regulates myod/e47 heterodimerization. Phosphorylation of e47 at ser140 by p38 induces myod/e47 association and activation of muscle-specific transcription, while the nonphosphorylatable e47 mutant ser140ala fails to heterodimerize with myod and displays impaired myogenic potentia
SIGNOR-134190
P11171
P00533
0
phosphorylation
down-regulates
0.4
The phosphorylation site has been localized to the 8-kda domain, which has one tyrosine, tyrosine-418. The 8-kda region is required for the assembly of the spectrin/actin complex, and phosphorylation by egfr reduced the ability of protein 4.1 to promote the assembly of the spectrin/actin/protein 4.1 ternary complex
SIGNOR-20452
P17858
O15294
0
glycosylation
down-regulates activity
0.277
O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia. Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway| O-GlcNAc transferase (OGT) catalyzes the transfer of N-acetylglucosamine from uridine diphospho-N-acetylglucosamine (UDP-GlcNAc) to serine or threonine residues
SIGNOR-267585
O15182
Q15154
0
relocalization
up-regulates
0.297
Rna silencing of pcm-1 leads to reduced assembly of centrin, pericentrin, and ninein at the centrosome
SIGNOR-95016
O75385
Q7Z3C6
1
phosphorylation
up-regulates activity
0.582
Src phosphorylates mATG9 at Tyr8 to maintain its endocytic and constitutive trafficking in unstressed conditions. In response to starvation, phosphorylation of mATG9 at Tyr8 by Src and at Ser14 by ULK1 functionally cooperate to promote interactions between mATG9 and the AP1/2 complex, leading to redistribution of mATG9 from the plasma membrane and juxta-nuclear region to the peripheral pool for autophagy initiation.
SIGNOR-266369
P04150
P49716
1
transcriptional regulation
up-regulates quantity
0.315
We conclude that glucocorticoid-induced adipogenesis from bone marrow stromal cells is mediated through a reaction cascade in which dexamethasone transcriptionally activates C/EBPδ; C/EBPδ then binds to PPARγ2 promoter and transactivates PPARγ2 gene expression.
SIGNOR-253061
P10415
Q86UR1
0
null
down-regulates activity
0.2
BH3-only proteins containing only a single BH domain and including Puma, Noxa, Bid and Bad as well as other factors are particularly important for such neutralisation, binding and regulating the anti-apoptotic Bcl-2 proteins to promote apoptosis
SIGNOR-209684
Q9Y2U5
P45985
1
phosphorylation
up-regulates activity
0.612
Both mekk2 and mekk3 are able to activate the jun kinase pathway in vivo. However, following routine immunoprecipitation in triton x-100, mekk2 but not mekk3 is able to effectively phosphorylate both sek-1 and mek-1 and to undergo autophosphorylation
SIGNOR-107695
Q9Y6Q9
O15111
0
phosphorylation
up-regulates
0.395
Herein, we report the successful identification of six functional in vivo src-3 phosphorylation sites.
SIGNOR-196953
P30305
O14757
0
phosphorylation
down-regulates activity
0.785
Here, we show that cdc25b is phosphorylated by chk1 in vitro on multiple residues, including s230 and s563.We show that the s230-phosphorylated form of cdc25b is located at the centrosome from early s phase until mitosis. Furthermore, mutation of s230 to alanine increases the mitotic-inducing activity of cdc25b
SIGNOR-149898
Q13568
P07948
0
phosphorylation
down-regulates activity
0.329
Lyn Kinase Suppresses the Transcriptional Activity of IRF5. Here, we found that Lyn physically interacted with IRF5 to inhibit ubiquitination and phosphorylation of IRF5 in the TLR-MyD88 pathway, thereby suppressing the transcriptional activity of IRF5 in a manner independent of Lyn's kinase activity.
SIGNOR-277247
P30307
P38398
0
ubiquitination
down-regulates quantity by destabilization
0.464
BRCA1 mediates cyclin B and Cdc25C ubiquitination.|Thus, BRCA1 dependent proteasomal degradation of cyclin B and Cdc25C precede the subsequent BRCA1 dependent cell cycle arrest.
SIGNOR-278623
P52945
P11168
1
transcriptional regulation
up-regulates quantity by expression
0.522
In conclusion, Pdx1 confers the expression of pancreatic β-cell-specific genes, such as genes encoding insulin, islet amyloid polypeptide, Glut2, and Nkx6.1.
SIGNOR-255540
P06493
O00429
1
phosphorylation
up-regulates activity
0.466
Drp1 is phosphorylated at the Ser616 position and activated predominantly by CDK1.
SIGNOR-279394
P20248
Q86T82
0
deubiquitination
up-regulates quantity by stabilization
0.581
USP37 Binds, Deubiquitinates, and Stabilizes Cyclin A
SIGNOR-265052
Q13873
Q9HCE7
0
ubiquitination
down-regulates
0.56
Smurf1 and smurf2 are e3 ubiquitin ligases known to suppress tgf-beta signaling through degradation of smads and receptors for tgf-beta and bmps.
SIGNOR-153402
P04637
P38936
1
transcriptional regulation
up-regulates quantity by expression
0.876
The ability of p53 to activate transcription from specific sequences suggests that genes induced by p53 may mediate its biological role as a tumor suppressor. Using a subtractive hybridization approach, we identified a gene, named WAF1, whose induction was associated with wild-type but not mutant p53 gene expression in a human brain tumor cell line. The WAF1 gene was localized to chromosome 6p21.2, and its sequence, structure, and activation by p53 was conserved in rodents.
SIGNOR-37145
O76064
O14773
1
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
Q71DI3
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-276844
O15534
Q92973
0
relocalization
up-regulates activity
0.268
The non-classical nuclear import carrier Transportin 1 modulates circadian rhythms through its effect on PER1 nuclear localization
SIGNOR-262102
Q86U86
Q13049
0
ubiquitination
down-regulates quantity by destabilization
0.2
TRIM32 ubiquitination of PB1 leads to its protein degradation.
SIGNOR-278735
P29350
P14618
1
dephosphorylation
down-regulates activity
0.2
SHP-1 dephosphorylates PKM2 at Y105 to inhibit nuclear function of PKM2 and determines the efficacy of targeted drugs.|SHP-1 directly dephosphorylated PKM2 at Y105 and further decreased the proliferative activity of PKM2; similar effects were found in sorafenib-treated hepatocellular carcinoma cells.|SHP-1 dephosphorylates p-PKM2Y105 and further affects the nucleus-related cell proliferation.
SIGNOR-276997
Q9H2G2
P41161
1
phosphorylation
up-regulates activity
0.2
Here, we report that the direct activation of the three mammalian ERMs by the Ste20-like kinase (SLK) is crucial for guiding the mitotic spindle toward the expected orientation in two mammalian models of oriented cell division: micropatterned cells and apical progenitors of the mouse neocortex.|SLK directly phosphorylates mammalian ERMs and controls their cortical activation in mitosis.
SIGNOR-280126
P25098
Q8IXH6
1
phosphorylation
down-regulates activity
0.2
In conclusion, experimental results demonstrate that GRK2 chronically downregulates DOR functional competence at the PM in peripheral sensory neurons, as well as peripheral DOR anti-nociception in vivo.|These data demonstrate that BK does not affect GRK2 mediated phosphorylation of DOR at its primary desensitization site.
SIGNOR-279739
O15111
P49815
1
phosphorylation
down-regulates
0.296
Insulin activation of mtor requires akt in a manner that involves ikkalpha, preferentially to ikkbeta, and tsc2 phosphorylation
SIGNOR-178664
Q86Y13
P16104
1
monoubiquitination
up-regulates activity
0.2
 2A-HUB catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatoric component of the repression machinery required for specific gene regulation programs. Thus, 2A-HUB mediates a selective repression of a specific set of chemokine genes in macrophages, critically modulating migratory responses to TLR activation. H2A monoubiquitination acts to prevent FACT recruitment at the transcriptional promoter region, blocking RNA polymerase II release at the early stage of elongation.
SIGNOR-271752
P23409
Q14814
0
transcriptional regulation
up-regulates quantity by expression
0.573
Myogenin and MEF2 function synergistically to activate the MRF4 promoter during myogenesis.
SIGNOR-238715
P12931
Q08050
1
phosphorylation
up-regulates activity
0.324
Hence, c-Src-dependent phosphorylation of MPP2 could be part of a negative feedback loop within the circuitry that modulates c-Src activity by MPP2.
SIGNOR-279117
Q969H0
P41743
0
phosphorylation
down-regulates activity
0.267
Here, we report that Fbw7α, the only Fbw7 isoform detected in eggs, is phosphorylated by PKC (protein kinase C) at a key residue (S18) in a manner coincident with Fbw7α inactivation.
SIGNOR-277250
P31749
O43521
1
phosphorylation
down-regulates activity
0.567
Recombinant Akt could directly phosphorylate a GST-Bim(EL) fusion protein and identified the Akt phosphorylation site in the Bim(EL) domain as Ser(87). Further, we demonstrated that cytokine stimulation promotes Bim(EL) binding to 14-3-3 proteins. Finally, we show that mutation of Ser(87) dramatically increases the apoptotic potency of Bim(EL).
SIGNOR-252487
P00533
Q9HD43
0
dephosphorylation
down-regulates activity
0.288
We further found that PTPRH and PTPRB directly dephosphorylate EGFR and repress its downstream signaling.
SIGNOR-277090
Q8TD19
P06493
0
phosphorylation
up-regulates activity
0.482
We now identify Plk1 as Nek9 direct activator and propose a two-step activation mechanism that involves Nek9 sequential phosphorylation by CDK1 and Plk1. while CDK1 activity is necessary for Nek9 phosphorylation in mitosis and the resulting change in electrophoretical mobility, Nek9 Thr210 phosphorylation and mitotic activation requires both CDK1 and Plk1.
SIGNOR-273889
P50222
O60315
0
transcriptional regulation
down-regulates quantity by repression
0.318
ZEB2 represses GAX transcription through multiple up- stream consensus binding sites.
SIGNOR-268951
Q13554
P16949
1
phosphorylation
down-regulates
0.515
Stimulation via cd2 activated multiple signal transduction pathways, resulting in phosphorylation of distinct sites of stathmin. Ser16 of recombinant human stathmin was phosphorylated also by purified cam kinase ii, and in vivo, cam kinase ii activity was indeed stimulated in cd2-triggered jurkat cells.
SIGNOR-59358
Q13043
P26927
0
phosphorylation
up-regulates
0.524
We directly show that okadaic acid induces phosphorylation in the activation loop of mst, and, once phosphorylated, mst is rapidly translocated to the nucleus. when thr183 in mst1 was mutated to ala, no band could be detected by oa treatment,2 indicating that thr183 was the site of phosphorylation.
SIGNOR-114289
P04049
Q9NQU5
0
phosphorylation
up-regulates activity
0.2
PAK5 phosphorylates Raf-1 on serine 338 and stimulates Raf-1 activity.
SIGNOR-278971
P21817
P17612
0
phosphorylation
up-regulates activity
0.326
PKA-mediated hyperphosphorylation of a conserved serine, Ser-2843 in skeletal RyR and Ser-2809 in cardiac RyR, results in an aberrant SR function during heart failure. hyperphosphorylated RyRs are leaky and therefore lead to a reduced SR Ca2+ load and impaired contractile function in heart failure
SIGNOR-250078
P14635
Q14774
0
transcriptional regulation
up-regulates quantity by expression
0.2
In this study, we have identified cell cycle regulatory genes as downstream targets of the homeobox gene HLX in cultured trophoblast cells, namely RB1, MYC, EGR1, CDKN1C, ELK1, CCNB1, and JUN. RB1 and MYC mRNA expression was increased with HLX inactivation, whereas EGR1, CDKN1C, ELK1, CCNB1, and JUN mRNA expression was decreased compared with mock-transfected control cells.
SIGNOR-261619
Q00535
P35712
1
phosphorylation
down-regulates quantity
0.366
GST-Sox6 was phosphorylated in vitro by Cdk5 and p35 (XREF_FIG).|Inhibition of Cdk5 activity by DN Cdk5 and roscovitine increases the Sox6 expression in primary cortical neurons.
SIGNOR-279365
P09917
P17612
0
phosphorylation
down-regulates activity
0.335
These results indicate that PKA phosphorylates 5-LO on Ser-523, which inhibits the catalytic activity of 5-LO and reduces cellular LT generation.
SIGNOR-264410
P09467
P17010
0
transcriptional regulation
down-regulates quantity by repression
0.2
For instance, nucleophosmin (NPM1) and zinc-finger protein X-linked (ZFX) bind to the E-box and ZFX binding site on the FBP1 promoter, respectively, and restrain FBP1 expression to facilitate aerobic glycolysis in PDAC and melanoma
SIGNOR-267595
P17252
P14136
1
phosphorylation
down-regulates activity
0.366
Glial fibrillary acidic protein (GFAP), the intermediate filament component of astroglial cells, can serve as an excellent substrate for both cAMP-dependent protein kinase and protein kinase C, in vitro. GFAP phosphorylated by each protein kinase does not polymerize, and the filaments that do polymerize tend to depolymerize after phosphorylation. Dephosphorylation of phospho-GFAP by phosphatase led to a recovery of the polymerization competence of GFAP. Most of the phosphorylation sites for cAMP-dependent protein kinase and protein kinase C on GFAP are the same, Ser-8, Ser-13, and Ser-34. cAMP-dependent protein kinase has one additional phosphorylation site, Thr-7.
SIGNOR-248862
P78527
P09874
1
phosphorylation
down-regulates activity
0.525
Therefore, through its interaction with Ku70/80 in the presence of dsDNA , DNA-PK phosphorylated PARP-1 at its catalytic CTD.
SIGNOR-280093
Q07812
P49841
0
phosphorylation
up-regulates
0.376
Glycogen synthase kinase-3beta phosphorylates bax and promotes its mitochondrial localization during neuronal apoptosis. Gsk-3beta directly phosphorylated bax(alpha) on ser163
SIGNOR-130141
P02686
P09543
0
null
down-regulates activity
0.455
We provide evidence that CNP directly associates with and organizes the actin cytoskeleton, thereby providing an intracellular strut that counteracts membrane compaction by myelin basic protein (MBP).
SIGNOR-269269
O43795
P29323
0
phosphorylation
up-regulates activity
0.2
EphB2 kinase activity is required for Myo1b-EphB2 interaction and induced Myo1b phosphorylation.
SIGNOR-279171
P68104
P36897
0
phosphorylation
down-regulates
0.343
Phosphorylation of eEF1A1 at Ser300 by T_R-I results in inhibition of mRNA translation
SIGNOR-167943
P10644
Q00536
0
phosphorylation
up-regulates activity
0.272
PCTK1 regulates spindle orientation in a kinase-dependent manner. Phosphoproteomic analysis together with an RNA interference screen revealed that PCTK1 regulates spindle orientation through phosphorylation of Ser83 on KAP0, a regulatory subunit of protein kinase A (PKA)
SIGNOR-273018
Q92990
P08581
0
relocalization
down-regulates
0.331
Significantly, nonphosphorylated hgf receptor prevents fap68 from stimulating p70s6k. fap68 binding to met requires the last 30 amino acids of the c-terminal tail, which are unique to the hgf receptor.
SIGNOR-110726
P22607
Q9UPZ9
1
phosphorylation
down-regulates activity
0.2
FGF signaling partially abolished ICK's kinase activity, through FGFR-mediated ICK phosphorylation at conserved residue Tyr15, which interfered with optimal ATP binding.
SIGNOR-277436
Q13009
P48729
0
phosphorylation
down-regulates quantity by destabilization
0.309
Phosphorylation of Ser329, Ser334, and Thr340 in Tiam1 is required for its interaction with βTrCP1. The proteolysis of Tiam1 is prevented by βTrCP silencing, inhibition of CK1 and MEK, or mutation of the Tiam1 degron site.
SIGNOR-276673
P49336
P84243
1
phosphorylation
down-regulates activity
0.2
However, within T/G-Mediator, cdk8 phosphorylates serine-10 on histone H3, which in turn stimulates H3K14 acetylation by GCN5L within the complex. Tandem phosphoacetylation of H3 correlates with transcriptional activation, and ChIP assays demonstrate co-occupancy of T/G-Mediator components at several activated genes in vivo.
SIGNOR-273173
Q05682
Q9UQM7
0
phosphorylation
down-regulates
0.2
Smooth muscle caldesmon was phosphorylated by smooth muscle calmodulin-dependent protein kinase. Ii
SIGNOR-22635
Q9UBS0
P42345
0
phosphorylation
up-regulates
0.834
In response to insulin and nutrients, mtorc1, consisting of mtor, raptor (regulatory-associated protein of mtor), and mlst8, is activated and phosphorylates eukaryotic initiation factor 4e-binding protein (4ebp) and p70 s6 kinase to promote protein synthesis and cell size.
SIGNOR-154821
P22087
Q9NRC8
0
deacetylation
up-regulates activity
0.271
Here, we show that FBL is acetylated at several lysine residues by the acetyltransferase CBP and deacetylated by SIRT7.|hyperacetylation impairs the interaction of FBL with histone H2A and chromatin, thereby compromising H2AQ104 methylation (H2AQ104me) and rDNA transcription. SIRT7-dependent deacetylation of FBL ensures H2AQ104me and high levels of rRNA synthesis during interphase. |Global acetylome studies have shown that FBL is acetylated at four conserved lysine residues (K102, K121, K205, and K206)
SIGNOR-275894
P00519
Q9Y6Q9
1
phosphorylation
up-regulates
0.348
Tyrosine phosphorylation of the nuclear receptor coactivator aib1/src-3 is enhanced by abl kinase and is required for its activity in cancer cellstyrosine kinase directly phosphorylates aib1/src-3 at y1357 and modulates the association of aib1 with c-abl, eralpha, the transcriptional cofactor p300,
SIGNOR-180571
P49841
P54132
1
phosphorylation
down-regulates quantity by destabilization
0.259
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates.
SIGNOR-276906
Q9NV58
P41180
1
ubiquitination
down-regulates quantity by destabilization
0.381
Coexpression with dorfin decreased the amount of total CaR protein and increased CaR ubiquitination, whereas a dominant negative fragment of dorfin had opposite effects. dorfin-mediated proteasomal degradation of immature CaR occurs from the endoplasmic reticulum. Because endogenous CaR in Madin-Darby canine kidney cells is also subject to degradation from the endoplasmic reticulum, dorfin-mediated ubiquitination may contribute to a general mechanism for CaR quality control during biosynthesis.
SIGNOR-271456
O15379
P12830
1
transcriptional regulation
down-regulates quantity by repression
0.257
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-275662
P24941
O60318
1
phosphorylation
up-regulates activity
0.2
To study the inducible regulation of GANP DNA-primase during cell activation, we examined phosphorylation induced by various kinds of kinases.We observed that the cell cycle-associated kinase Cdks induced phosphorylation of GANP in vitro. Examination of immunoprecipitates of Cdk2 from B cells revealed phosphorylation of GANP-PD at a consensus sequence of Cdk phosphorylation at Ser502 (S/T-P-X-K/R) (Fig. ​(Fig.1C1C Left; ref. 22).
SIGNOR-262734
Q13131
Q8IWQ3
0
phosphorylation
up-regulates
0.291
Ampka1 activators increased phosphorylation level and cytoplasmic localization (reduced nuclear/cytoplasmic ratio). Ampka1 activators reduced rna synthesis in the nucleoli.
SIGNOR-176594
Q9HAU4
P49910
0
transcriptional regulation
down-regulates quantity by repression
0.268
ZNF165 drives the unrestrained activation of transforming growth factor β (TGFβ) signalling by directly inactivating the expression of negative feedback pathway regulators, SMURF2, SMAD7 and PMEPA1.
SIGNOR-266095
P17252
Q96RI1
1
phosphorylation
up-regulates
0.325
Phosphorylation of farnesoid x receptor by protein kinase c promotes its transcriptional activity. pkcalpha phosphorylates in vitro fxr in its dna-binding domain on s135 and s154.
SIGNOR-180537
Q96RR4
Q00535
0
phosphorylation
down-regulates
0.2
Cdk5 and gsk3 phosphorylate ser-129, ser-133, and ser-137. Mutation of ser-129, ser-133, and ser-137 increases autonomous activity with little change in ca2 /cam-dependent activity.
SIGNOR-198111
Q16620
P19174
1
phosphorylation
up-regulates activity
0.647
Both Shc and PLCgamma1 are phosphorylated by TrkB, thereby initiating Shc/Ras/MAP kinase and PLCgamma1 signaling respectively.|We conclude that activation of pY783 PLCgamma1 is due mainly to TrkB activation in these models and that TrkB induced PLCgamma1 signaling promotes limbic epileptogenesis.
SIGNOR-279241
P0C0L5
O00187
0
cleavage
up-regulates activity
0.798
MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester. C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase (C4b2a).
SIGNOR-263422
P24941
P23511
1
phosphorylation
up-regulates activity
0.439
Cdk2 phosphorylates two serine residues near the DNA-binding domain of the YA subunit of NF-Y. Cyclin A-cdk2 appears to associate with NF-Y both in vitro and in vivo. Furthermore, YA protein is phosphorylated in parallel with a cell cycle-dependent activation of cdk2 kinase and cyclin A expression. YA phosphorylation is unnecessary for heterotrimer formation with the YB-YC dimer. However, NF-Y containing a phosphorylation-deficient mutant form of YA, YA-aa, has its DNA binding activity impaired. \ To examine whether cdk2 phosphorylates the two serine residues at positions 320 and 326 in YA, we replaced either or both with alanine by site-directed mutagenesis. In a kinase assay using purified GST fusion proteins in vitro, cdk2 phosphorylated the wild type and both of the single-mutant proteins (YA-as and -sa), but not the double-mutant protein (YA-aa)
SIGNOR-250742
P13349
P23759
0
transcriptional regulation
up-regulates quantity by expression
0.492
Together, these experiments indicate that Pax7 enforces satellite cell commitment by recruiting a HMT complex to Myf5, resulting in transcriptional activation.
SIGNOR-255641
Q96QB1
Q00535
0
phosphorylation
up-regulates activity
0.2
The CDK5 kinase phosphorylates four serines in DLC1 located N-terminal to the Rho-GAP domain. When not phosphorylated, this N-terminal region functions as an autoinhibitory domain that places DLC1 in a closed, inactive conformation by efficiently binding to the Rho-GAP domain. CDK5 phosphorylation reduces this binding and orchestrates the coordinate activation DLC1, including its localization to focal adhesions, its Rho-GAP activity, and its ability to bind tensin and talin. 
SIGNOR-276444
P42684
Q14653
1
phosphorylation
up-regulates activity
0.2
The data in this study show that IRF3 is physically associated with c-Abl in vivo and directly binds to c-Abl in vitro. IRF3 is phosphorylated by c-Abl and c-Abl-related kinase, Arg, mainly at Y292.
SIGNOR-277441
Q16512
Q9NYL2
1
phosphorylation
up-regulates
0.2
Phosphorylation of mltkalpha by pknalpha enhances its kinase activity
SIGNOR-152768
Q96SW2
Q9UKT9
1
ubiquitination
down-regulates quantity by destabilization
0.581
IMiD compounds cause selective ubiquitination and degradation of IKZF1 in CD34+ cells by the CRBN E3 ubiquitin ligase.
SIGNOR-272319
O43318
O14920
1
phosphorylation
up-regulates activity
0.755
Tak1 become activated and then phosphorylates and activates ikk2 which in turn now phosphorylates ikba, marking it for k48-ubiquitination and proteasomal degradation. tak1 kinase complex phosphorylates and activates ikk in a manner that depends on traf6 and ubc13-uev1a our studies suggests that tak1_ acts as an upstream activating kinase for ikkbeta.
SIGNOR-109490
Q07812
Q9ULZ3
0
relocalization
up-regulates
0.353
Asc directly induces bax-mediated apoptosis. Asc induces the translocation of bax to the mitochondria, bax-dependent cycs release from the mitochondria and casp9 activation.
SIGNOR-149522
P45984
P14778
0
phosphorylation
up-regulates activity
0.281
Il-1 binding to its receptor triggers a cascade of signaling events, including activation of the stress-activated mitogen-activated protein (map) kinases, c-jun nh2-terminal kinase (jnk) and p38 map kinase, as well as transcription factor nuclear factor kappab (nf-kappab
SIGNOR-249514
P41180
Q9NV58
0
ubiquitination
down-regulates quantity by destabilization
0.381
Coexpression with dorfin decreased the amount of total CaR protein and increased CaR ubiquitination, whereas a dominant negative fragment of dorfin had opposite effects. dorfin-mediated proteasomal degradation of immature CaR occurs from the endoplasmic reticulum. Because endogenous CaR in Madin-Darby canine kidney cells is also subject to degradation from the endoplasmic reticulum, dorfin-mediated ubiquitination may contribute to a general mechanism for CaR quality control during biosynthesis.
SIGNOR-271456
Q09472
Q9UK32
0
phosphorylation
down-regulates activity
0.253
Figure 2G shows that Ser89 phosphorylation of p300, an event that inhibits p300’s acetyltransferase activity (13), was decreased in RSK4-silenced A549 and T24 cells. Consequently, RSK4 may regulate the activity of the NFκB pathway by direct phosphorylation of p300, as recombinant RSK4 phosphorylates p300 on Ser89 in vitro 
SIGNOR-275796
P30874
P15884
0
transcriptional regulation
up-regulates quantity by expression
0.358
Activation of somatostatin receptor II expression by transcription factors MIBP1 and SEF-2 in the murine brain.
SIGNOR-261618
P22612
P46019
1
phosphorylation
down-regulates activity
0.325
Phosphorylation of the alpha and beta subunits by the 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) also relieves inhibition of the gamma subunit and thereby activates the enzyme.
SIGNOR-267414
P09619
P17706
0
dephosphorylation
down-regulates activity
0.564
The PDGF beta receptor is negatively regulated by protein tyrosine phosphatases (PTPs).|In summary, our findings identify TC-PTP as a previously unrecognized negative regulator of PDGF beta receptor signaling and support the general notion that PTPs display site selectivity in their action on tyrosine kinase receptors.The fact that two of the investigated PDGF β receptor sites, Y1021 and Y771, displayed a larger increase in phosphorylation than Y579 and Y751 in TC-PTP ko MEFs indicated that these two sites are preferred substrates for TC-PTP.
SIGNOR-248389
P53602
P31749
0
phosphorylation
up-regulates activity
0.2
Akt modulated the pathway by phosphorylating mevalonate diphosphate decarboxylase (MDD) at Ser96. These data suggest that Akt regulates Rac1 activity by directly phosphorylating MDD at Ser96, which augments Rac1 geranylgeranylation.
SIGNOR-265891
Q13153
Q70Z35
1
phosphorylation
down-regulates activity
0.367
P21-activated Kinases (PAKs) Mediate the Phosphorylation of PREX2 Protein to Initiate Feedback Inhibition of Rac1 GTPase. PAK-mediated phosphorylation of PREX2 reduced GEF activity toward Rac1 by inhibiting PREX2 binding to PIP3 and Gβγ.
SIGNOR-277181
Q02127
P01106
0
transcriptional regulation
up-regulates quantity by expression
0.346
PPAT, catalyzing the first step of purine synthesis, and DHODH, an enzyme generating uridine in the middle of the pyrimidine synthesis pathway, were validated as direct c-MYC target genes by all criteria.
SIGNOR-267382
P27361
P35228
1
phosphorylation
up-regulates
0.354
Erk phosphorylated inos on ser745. Mutation of ser745 to ala did not affect basal inos activity but eliminated inos phosphorylation and activation in response to b1r agonist.
SIGNOR-157711
Q14790
Q5T447
0
polyubiquitination
down-regulates activity
0.336
HECTD3, a new E3 ubiquitin ligase, interacts with caspase-8 death effector domains and ubiquitinates caspase-8 with K63-linked polyubiquitin chains that do not target caspase-8 for degradation but decrease the caspase-8 activation. HECTD3 ubiquitinates caspase-8 with K63-linked polyubiquitin chains at K215.
SIGNOR-272077
P60953
Q96N96
0
guanine nucleotide exchange factor
up-regulates activity
0.718
We therefore developed a screening-compatible live-cell imaging assay, using FRET-based biosensors for the prototype GTPases RHOA, RAC1 and CDC4215,19,20 (Extended Data Fig. 2 and Supplementary Note 1)|We found catalytic activities for 45/75 RhoGEFs and 48/63 RhoGAPs| Our data thus not only reveal extensive promiscuity among regulators, but also that the inactivating RhoGAPs are less selective than the activating RhoGEFs (p-value=0.02)(Supplementary Table 2).
SIGNOR-260576
Q13148
O14920
0
phosphorylation
down-regulates quantity by destabilization
0.2
IκB kinase phosphorylates cytoplasmic TDP-43 and promotes its proteasome degradation. Furthermore, we identified IKKβ-induced phosphorylation sites of TDP-43 and found that phosphorylation at Thr8 and Ser92 is important for the reduction of TDP-43 by IKK.
SIGNOR-277860
Q86V86
Q13200
1
phosphorylation
up-regulates activity
0.2
Seven of these kinases (PIM1/2/3, MAP4K1/2, PKA, and NEK6) directly and robustly phosphorylated recombinant GST-Rpn1 at S361 in vitro (Fig. 3D and SI Appendix, Fig. S3 A and B). 
SIGNOR-273897
Q8TD16
P49792
0
relocalization
up-regulates quantity
0.505
We show that the dynein/dynactin adaptor BICD2 is specifically recruited to the NPC in G2phase through a direct interaction with the NPC componentRanBP2.
SIGNOR-259122
Q12879
Q00535
0
phosphorylation
up-regulates activity
0.525
Here, we demonstrate that cyclin dependent kinase-5 (Cdk5) associates with and phosphorylates NR2A subunits at Ser-1232 in vitro and in intact cells. Moreover, we show that roscovitine, a selective Cdk5 inhibitor, blocks both long-term potentiation induction and NMDA-evoked currents in rat CA1 hippocampal neurons. These results suggest that Cdk5 plays a key role in synaptic transmission and plasticity through its up-regulation of NMDARs.
SIGNOR-250666
P35222
P16591
0
phosphorylation
down-regulates activity
0.72
Interaction of beta-catenin with alpha-catenin is regulated by the phosphorylation of beta-catenin Tyr-142. This residue can be phosphorylated in vitro by Fer or Fyn tyrosine kinases.  Transfection of these kinases to epithelial cells disrupted the association between both catenins.
SIGNOR-251131