IdA
string
IdB
string
labels
int64
mechanism
string
effect
string
score
float64
sentence
string
signor_id
string
P06493
Q15910
1
phosphorylation
down-regulates
0.575
Cdk1, which phosphorylates ezh2 at threonines 345 and 487.Phosphorylation of thr-345 and thr-487 promotes ezh2 ubiquitination and subsequent degradation by the proteasome
SIGNOR-174058
O75461
O14757
0
phosphorylation
down-regulates activity
0.574
the checkpoint kinase Chk1 phosphorylates E2F6 leading to its dissociation from promoters.
SIGNOR-266371
P42574
P38398
1
cleavage
down-regulates quantity by destabilization
0.473
We demonstrate the cleavage and the consequential downregulation of full-length BRCA1 by caspase-3 during UV-induced apoptosis. Finally, mutation of a caspase-3 specific cleavage site (D/A1154) rendered BRCA1 non-cleavable.
SIGNOR-256326
Q99541
P35790
0
phosphorylation
down-regulates quantity by destabilization
0.2
In addition, as a protein kinase, CHKalpha2 phosphorylates PLIN2 at Tyrosine 232 and PLIN3 at Tyrosine 251. Phosphorylated PLIN2 and PLIN3 are separated from lipid droplets and degraded by Hsc70-mediated autophagy, thereby promoting lipid droplet lipolysis, fatty acid oxidation and glioblastoma growth 
SIGNOR-267649
Q969H0
P23771
1
ubiquitination
down-regulates quantity by destabilization
0.403
Fbw7 promotes degradation of GATA3 in a Thr-156-dependent manner. 
SIGNOR-276635
O14490
Q9UPX8
1
relocalization
up-regulates activity
0.827
SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3).
SIGNOR-264587
Q9P2R6
Q07812
1
relocalization
up-regulates activity
0.2
We detected RERE protein mainly in the nucleus, where it colocalizes with the promyelocytic leukemia protein in promyelocytic leukemia oncogenic domains (PODs). Overexpression of RERE recruits a fraction of the proapoptotic protein BAX to PODS: This observation correlates with RERE-induced apoptosis, which occurs in a caspase-dependent manner.
SIGNOR-264485
Q9BUB5
P47712
1
phosphorylation
up-regulates activity
0.577
The results suggest that MNK1 or a closely related kinase is responsible for in vivo phosphorylation of cPLA2 on Ser-727.
SIGNOR-226633
Q16875
P53778
0
phosphorylation
up-regulates quantity
0.2
KRAS transformation and overexpression of p38gamma increased expression of PFKFB3 and glucose transporter GLUT2
SIGNOR-279539
P51955
P04637
1
phosphorylation
down-regulates
0.318
NEK2 Phosphorylates p53 at Ser315 and Reduces Its Stability.|These results are consistent with NEK2 inhibiting p53 transcriptional activation functions.
SIGNOR-278488
P22681
P27986
1
ubiquitination
down-regulates
0.694
Cbl-b, a ring-type e3 ubiquitin protein ligase, is implicated in setting the threshold of t lymphocyte activation. The p85 regulatory subunit of phosphatidylinositol 3 kinase (pi3k) was identified as a substrate for cbl-b. We have shown that cbl-b negatively regulated p85 in a proteolysis-independent manner.
SIGNOR-110060
P00751
P00746
0
cleavage
up-regulates activity
0.804
The resulting proconvertase C3bB is subsequently cleaved by factor D (FD), generating the AP C3 convertase C3bBb
SIGNOR-263488
Q96PM5
O14579
1
polyubiquitination
down-regulates quantity by destabilization
0.471
PIRH2 promotes the ubiquitylation of epsilon-COP in vitro and in vivo and consequently promotes the degradation of epsilon-COP. 
SIGNOR-272630
O60664
P51151
0
null
up-regulates activity
0.591
Rab9-dependent transport from late endosomes to the Golgi requires the Rab9 effectors p40 (Diaz et al., 1997) and TIP47 (Diaz and Pfeffer, 1998), a protein that recognizes the cytoplasmic domains of the two types of MPRs and packages them into nascent transport vesicles (Carroll et al., 2001). MPR recycling also utilizes a TGN-localized coiled-coil protein named GCC185 that is also a Rab9 effector
SIGNOR-253089
Q14493
Q5TEC6
1
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 cytoplasm, where SLBP participates in translation of the histone mRNA|We used radiolabeled probes generated by PCR targeting the open reading frame (ORF) to detect histones H2A, H2B, H3, H4, and H1 and used 7SK snRNA as a loading control (Fig. 2A). The abundance of histone H2A, H2B, H3, and H4 mRNAs is reduced to 37% to 70% of control levels in the SLBP knockdown cells when compared to the C2 control.
SIGNOR-265415
P78536
P05067
1
cleavage
up-regulates activity
0.539
By the use of gene disruption (knockout), we now demonstrate that TACE (tumor necrosis factor alpha converting enzyme), a member of the ADAM family (a disintegrin and metalloprotease-family) of proteases, plays a central role in regulated alpha-cleavage of APP. Our data suggest that TACE may be the alpha-secretase responsible for the majority of regulated alpha-cleavage in cultured cells. 
SIGNOR-262829
P27361
Q9BR01
1
phosphorylation
down-regulates
0.2
The phosphorylation of sult4a1 allows interaction with pin1, which then promotes degradation of the sulfotransferase.
SIGNOR-168248
P98177
Q13627
0
phosphorylation
down-regulates
0.315
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity
SIGNOR-183677
O75531
Q86Y07
0
phosphorylation
down-regulates
0.502
We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. Coexpression of vrk1 and gfp-baf greatly diminishes the association of baf with the nuclear chromatin/matrix and leads to its dispersal throughout the cell
SIGNOR-143368
O60346
P17252
1
dephosphorylation
down-regulates quantity
0.25
In addition, knockdown of PHLPP expression reduces the rate of phorbol ester-triggered dephosphorylation of the hydrophobic motif, but not turn motif, of PKC alpha
SIGNOR-237043
P15311
P43405
0
phosphorylation
up-regulates activity
0.447
Phospho-SYK has also been shown to specifically activate ezrin upon CD81 engagement.|We found that the activated SYK led to a time dependent phosphorylation of ezrin (pY354 and pThr567) and radixin (pThr564) (XREF_FIG).
SIGNOR-279129
Q13501
O60260
0
ubiquitination
down-regulates quantity by destabilization
0.2
Once activated, parkin interacts with and subsequently ubiquitinates p62 at the K13 residue, resulting in the degradation of p62 via the proteasomal dependent pathway.
SIGNOR-278524
O75151
P68431
1
demethylation
down-regulates activity
0.2
PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation. This modification leads to targeting of the PHF2–ARID5B complex to its target promoters, where it removes the repressive H3K9Me2 mark.
SIGNOR-264521
Q5T197
P52630
1
ubiquitination
down-regulates activity
0.448
DCST1 promotes ubiquitination of STAT2.|The ability of DCST1 to degrade STAT2 levels was visible both in the presence and absence of IFNbetastimulation.|In our study, DCST1 was found to interact with and promote ubiquitination of STAT2, leading to reduced STAT2 expression and attenuated activation of the ISG induction pathway.
SIGNOR-278747
P04637
P25445
1
transcriptional regulation
up-regulates quantity by expression
0.605
In an attempt to understand how CD95 expression is regulated by p53, we identified a p53-responsive element within the first intron of the CD95 gene, as well as three putative elements within the promoter. The intronic element conferred transcriptional activation by p53 and cooperated with p53-responsive elements in the promoter of the CD95 gene. wt p53 bound to and transactivated the CD95 gene,
SIGNOR-62376
P62834
O95398
0
guanine nucleotide exchange factor
up-regulates activity
0.71
Epac1 (cAMP-GEFI) and Epac2 (cAMP-GEFII) are closely related guanine nucleotide exchange factors (GEFs) for the small GTPase Rap1, which are directly regulated by cAMP. Here we show that both GEFs efficiently activate Rap2 as well.
SIGNOR-263956
O14965
O75496
1
phosphorylation
up-regulates activity
0.51
Aurora-A controls pre-replicative complex assembly and DNA replication by stabilizing geminin in mitosis.|Thr25 of geminin is phosphorylated by Aurora-A.
SIGNOR-278509
P68400
Q9HA82
1
phosphorylation
up-regulates activity
0.2
Most of the phosphorylated residues conformed to a consensus motif for phosphorylation by casein kinase 2 (CK2), and treatment of cells with the CK2-specific inhibitor CX-4945 lowered the phosphorylation levels of CERS2, -4, -5, and -6. Phosphorylation of CERS2 was especially important for its catalytic activity, acting mainly by increasing itsVmaxvalue. 
SIGNOR-273984
O15294
P11413
1
glycosylation
up-regulates activity
0.264
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-267582
P00533
Q38SD2
1
phosphorylation
down-regulates activity
0.343
In this study, we demonstrate that EGFR regulates the kinase activity of LRRK1 via tyrosine phosphorylation and that this is required for proper endosomal trafficking of EGFR. Phosphorylation of LRRK1 at Tyr-944 results in reduced LRRK1 kinase activity.
SIGNOR-262856
P25098
P08069
1
phosphorylation
down-regulates quantity by destabilization
0.2
GRK2 and GRK6 coimmunoprecipitate with IGF-1R and increase IGF-1R serine phosphorylation, promoting β-arrestin1 association. Using immunoprecipitation, confocal microscopy, and FRET analysis, we demonstrated β-arrestin/IGF-1R association to be transient for GRK2 and stable for GRK6. Using bioinformatic studies we identified serines 1248 and 1291 as the major serine phosphorylation sites of the IGF-1R. Targeted mutation of S1248 recapitulates GRK2 modulation, whereas S1291 mutation resembles GRK6 effects on IGF-1R signaling/degradation
SIGNOR-276413
Q01974
P49841
0
phosphorylation
down-regulates activity
0.312
We identify ror2 ser 864 as a critical residue phosphorylated by gsk3 and required for noncanonical receptor activation by wnt5a, analogous to the priming phosphorylation of low-density receptor-related protein 6 (lrp6) in response to wnt3a.
SIGNOR-169642
Q13224
P54829
0
dephosphorylation
down-regulates activity
0.547
 These previous results, together with the present findings, indicate that STEP61 dephosphorylates the NR2B subunit at its regulatory tyr1472 site, and dephosphorylation of this site leads to internalization of the NMDAR complex from neuronal surface membranes.
SIGNOR-265744
Q00987
Q16665
1
ubiquitination
down-regulates quantity by destabilization
0.643
We find that p53 promotes Mdm2-mediated ubiquitination and proteasomal degradation of the HIF-1alpha subunit of hypoxia-inducible factor 1 (HIF-1), a heterodimeric transcription factor that regulates cellular energy metabolism and angiogenesis in response to oxygen deprivation.
SIGNOR-271385
Q08493
P28482
0
phosphorylation
down-regulates
0.256
The short-form pde4b2 isoenzyme was activated by erk2 phosphorylation. sub-family selective actions in the ability of erk2 map kinase to phosphorylate and regulate the activity of pde4 cyclic amp-specific phosphodiesterases
SIGNOR-83187
P52564
Q99683
0
phosphorylation
up-regulates activity
0.613
A MAP kinase kinase kinase (MAPKKK), termed ASK1, was identified that activated two different subgroups of MAP kinase kinases (MAPKK), SEK1 (or MKK4) and MKK3/MAPKK6 (or MKK6), which in turn activated stress-activated protein kinase (SAPK, also known as JNK; c-Jun amino-terminal kinase) and p38 subgroups of MAP kinases, respectively.
SIGNOR-45353
Q96NT3
P46934
0
polyubiquitination
down-regulates quantity by destabilization
0.419
The E3 ligase NEDD4 regulates GUCD1 degradation. many polyubiquitinylated species of GUCD1 appeared as high molecular weight forms, suggesting that GUCD1 is degraded by the proteasome, after polyubiquitin chain formation, in the presence of NEDD4-1.
SIGNOR-272846
Q9Y243
O15111
1
phosphorylation
up-regulates
0.414
Although there are likely to be multiple levels of crosstalk between the pi3k-akt and nf-kb pathways, one mechanism has been attributed to direct phosphorylation of the amino acid residue t23 on ikb kinase alfa (ikkalfa) by akt, thereby leading to activation of this kinase upstream of nf-kb akt mediates ikkalpha phosphorylation at threonine 23 akt transiently associates in vivo with ikk and induces ikk activation. Akt mediates ikkalfa phosphorylation at threonine 23.Akt phosphorylates ikkalpha on t23, and this phosphorylation event is a prerequisite for the phosphorylation of p65 at s534 by ikkalpha and beta
SIGNOR-187062
P00533
P09211
1
phosphorylation
up-regulates
0.437
Taken together, these results and those of the ms/ms analyses confirmed tyr-3, tyr-7, and tyr-198 to be primary residues phosphorylated by egfr in the gstp1 protein. The phosphorylation increased gstp1 enzymatic activity significantly,
SIGNOR-184387
P78344
P68400
0
phosphorylation
up-regulates activity
0.226
DAP5(S902) is phosphorylated by CK2α. Phosphorylation of DAP5(S902) by CK2α is required for eIF2β binding.
SIGNOR-266384
P17612
P05114
1
phosphorylation
down-regulates activity
0.307
PKA preferentially phosphorylates serine 6 in human HMGN1. specific phosphorylation of the NBD of HMGN proteins serves to prevent the interaction of these proteins with their chromatin targets during mitosis.
SIGNOR-249993
P55072
P31749
0
phosphorylation
up-regulates
0.509
Site-directed mutagenesis identified ser-351, ser-745, and ser-747 as akt phosphorylation sites on vcp. however, our study also suggests that other known biological activities of vcp, such as those related to intracellular trafficking, ubiquitin-mediated proteolysis, and activation of transcription (28), might be regulated by akt through the activation of vcp. I
SIGNOR-252491
Q06413
P51608
0
transcriptional regulation
down-regulates quantity by repression
0.346
MeCP2 binds to the promoter region of six target genes. ChIP with anti-MeCP2 antibody shows that MeCP2 binds to the promoter regions of activated targets Sst, Oprk1, Gamt, and Gprin1, and repressed targets Mef2c and A2bp1.
SIGNOR-264680
P09543
P02686
1
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
Q15717
Q05655
0
phosphorylation
up-regulates
0.637
Tandem phosphorylation of serines 221 and 318 by protein kinase cdelta coordinates mrna binding and nucleocytoplasmic shuttling of hurstabilization of mrna by the ubiquitous rna binding protein human antigen r (hur), a member of the embryonic lethal abnormal vision (elav) protein family, requires canonical binding to au-rich element (are)-bearing target mrna and export of nuclear hur-mrna complexes to the cytoplasm. In human mesangial cells (hmc) both processes are induced by angiotensin ii (angii) via protein kinase cdelta (pkcdelta)-triggered serine phosphorylation of hur.
SIGNOR-163524
O15392
Q96GD4
0
phosphorylation
down-regulates
0.795
Phosphorylation by aurora-b negatively regulates survivin function . hat survivin is phosphorylated at t117 during mitosis, and once phosphorylated, dephosphorylation is crucial for chromosome congression and progression into anaphaseduring mitosis
SIGNOR-154569
P35241
Q13464
0
phosphorylation
up-regulates activity
0.68
 A peak of the phosphopeptide, in which only T573 was phosphorylated, was not detected. Quantitative analyses revealed that _100% of T564, but at most _40% of T573, was phosphorylated when C-rad was incubated with Rho-Kc for 1 h. Then we concluded that the major and primary phosphorylation site of radixin by Rho-kinase was T564 and referred to the Rho-Kc€“phosphorylated C-rad as T564-phosphorylated C-rad. | In this study, we found that the T564 phosphorylation of radixin markedly suppressed its head-to-tail association. This suggests that the T564-phosphorylation of radixin (and probably also the phosphorylation of ezrin T567 and moesin T558) keeps them open and active.
SIGNOR-248994
O75116
Q16555
1
phosphorylation
up-regulates
0.383
Rho-kinase phosphorylated crmp-2 at thr-555 in vitro.we demonstrated that crmp-2 is phosphorylated by rho-kinase in drg neurons during lpa-induced growth cone collapse.
SIGNOR-77543
Q9HC98
P52732
1
phosphorylation
up-regulates activity
0.444
Nek6 phosphorylated Eg5 at several sites in vitro and one of these sites, Ser1033, is phosphorylated in vivo during mitosis. Whereas CDK1 phosphorylates nearly all Eg5 at Thr926 during mitosis, Nek6 phosphorylates approximately 3% of Eg5, primarily at the spindle poles. 
SIGNOR-273886
P51149
Q8NEB9
1
guanine nucleotide exchange factor
up-regulates activity
0.484
The p150 adapter protein is in a complex with rab7. The hVPS34/p150 complex colocalized with rab7 on late endosomes and hVPS34 activity was dependent on nucleotide cycling of rab7
SIGNOR-261302
Q92529
P62993
1
relocalization
up-regulates
0.819
In addition to direct binding of grb2 to phosphotyrosine residues of receptor kinases, grb2 can also be recruited to the receptor by binding to shc when shc is tyrosine phosphorylated as a result of receptor stimulation.
SIGNOR-146897
P40763
P14618
0
phosphorylation
up-regulates activity
0.443
PKM2 activates transcription of MEK5 by phosphorylating stat3 at Y705. In vitro phosphorylation assays show that PKM2 is a protein kinase using PEP as a phosphate donor
SIGNOR-267716
P40763
P53350
1
transcriptional regulation
up-regulates quantity by expression
0.306
Stat3 directly activated transcription of PLK1 in esophageal cancer cells and mouse embryonic fibroblast cell NIH3T3.
SIGNOR-271690
Q8TDC3
P20810
1
phosphorylation
up-regulates activity
0.2
Here, we show that an AZ cytomatrix protein CAST and an AZ-associated protein kinase SAD-B coordinately regulate STD by controlling reloading of the AZ with release-ready synaptic vesicles. SAD-B phosphorylates the N-terminal serine (S45) of CAST, and S45 phosphorylation increases with higher firing rate.
SIGNOR-263051
Q07817
Q9H4B4
0
phosphorylation
up-regulates
0.391
Polo kinase 3 (plk3) was implicated in bcl-xl(ser49) phosphorylation. These data indicate that, during g2 checkpoint, phospho-bcl-xl(ser49) is another downstream target of plk3, acting to stabilize g2 arrest.
SIGNOR-172230
P25963
Q9UN86
0
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
Q9UGI9
O75385
0
phosphorylation
down-regulates
0.406
Ulk1/2 in turn phosphorylates all three subunits of ampk and thereby negatively regulates its activity phosphorylation of ampk by ulk1 represents a negative feedback circuit.
SIGNOR-173053
Q8TAE6
Q13418
0
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
P17252
P48048
1
phosphorylation
down-regulates activity
0.2
The giant patch clamp together with site direct mutagenesis revealed that Thr-193 is the phosphorylation site on PKC that regulates the pH(i) sensitivity of ROMK1 channels. Mutation of PKC-induced phosphorylation sites (T193A) decreases the pH(i) sensitivity and increases the interaction of channel-PIP(2). 
SIGNOR-276389
Q13554
Q9UQD0
1
phosphorylation
up-regulates activity
0.272
CaMKII enhances voltage-gated sodium channel Nav1.6 activity and neuronal excitability|mmobilized peptide arrays and nanoflow LC-electrospray ionization/MS of Nav1.6 reveal potential sites of CaMKII phosphorylation, specifically Ser-561 and Ser-641/Thr-642 within the first intracellular loop of the channel.
SIGNOR-275788
Q14493
P23527
1
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 cytoplasm, where SLBP participates in translation of the histone mRNA|We used radiolabeled probes generated by PCR targeting the open reading frame (ORF) to detect histones H2A, H2B, H3, H4, and H1 and used 7SK snRNA as a loading control (Fig. 2A). The abundance of histone H2A, H2B, H3, and H4 mRNAs is reduced to 37% to 70% of control levels in the SLBP knockdown cells when compared to the C2 control.
SIGNOR-265379
Q9Y243
Q13043
1
phosphorylation
down-regulates
0.261
Full activation of mst1 requires an activation cleavage that is prevented by the phosphorylation of thr-387 by akt.
SIGNOR-201129
Q9BZS1
P49841
0
phosphorylation
down-regulates quantity by destabilization
0.285
Our previous study showed, by mass spectrometry analysis, that GSK-3β phosphorylates Foxp3 at Ser270 and Ser275
SIGNOR-277245
P35222
Q9NW38
0
ubiquitination
up-regulates activity
0.2
Here we provide evidence that FANCL increases the activity and expression of beta-catenin, a key pluripotency factor in hematopoietic stem cells.|We show that FANCL ubiquitinates \u03b2-catenin with atypical ubiquitin chain extension known to have nonproteolytic functions.
SIGNOR-278651
Q9C0C7
P42345
0
phosphorylation
down-regulates activity
0.471
We show that under non-autophagic conditions, mTOR inhibits AMBRA1 by phosphorylation, whereas on autophagy induction, AMBRA1 is dephosphorylated. In this condition, AMBRA1, interacting with the E3-ligase TRAF6, supports ULK1 ubiquitylation by LYS-63-linked chains, and its subsequent stabilization, self-association and function. As ULK1 has been shown to activate AMBRA1 by phosphorylation, the proposed pathway may act as a positive regulation loop, which may be targeted in human disorders linked to impaired autophagy.|mTOR phosphorylates AMBRA1 at Ser 52, inhibiting its role in ULK1 modification
SIGNOR-272986
Q08050
P06493
0
phosphorylation
up-regulates
0.762
A conserved phosphorylation site within the forkhead domain of foxm1b is required for its activation by cyclin-cdk1further analysis reveals that the leu-641 residue within an lxl motif is required for the recruitment of the cyclin-cdk complex, and the thr-596 residue is a critical cdk1 phosphorylation site within the activation domain of foxm1b. Cdk-dependent phosphorylation stimulates the foxm1b transcriptional activity
SIGNOR-187880
Q01543
O15550
0
transcriptional regulation
down-regulates quantity by repression
0.2
Our findings reveal a dual role for UTX in suppressing acute myeloid leukaemia via repression of oncogenic ETS and upregulation of tumor suppressive GATA programs. several ETS transcription factors, including Elf4, Etv6, Erg, Fli1, Ets2, Spi1 and Elk3 were upregulated immediately after Utx loss in the preleukaemic phase
SIGNOR-260034
Q04912
P31749
0
phosphorylation
up-regulates
0.559
Akt/pkb phosphorylates ron ser-1394, thus providing a docking site for 14-3-3based on these results, we propose a mechanism based on msp-ron-dependent phosphorylation and 14-3-3 association, whereby the function of alpha6beta4 switches from a mechanical adhesive device into a signaling component, and might be critically involved in human epidermal wound healing
SIGNOR-252471
O14757
Q9BXW9
1
phosphorylation
up-regulates activity
0.585
In vitro and in vivo experiments show that phosphorylation of s331 is mediated by chk1, the s-phase checkpoint kinase implicated in the fanconi anemia dna repair pathway. phosphorylation at this site is dependent on chk1, signifying the importance of the s-phase checkpoint in the activation of fanconi anemia pathway.
SIGNOR-107042
P40763
P15692
1
transcriptional regulation
up-regulates quantity by expression
0.786
Stat3 directly regulated the promoter of the VEGF gene. Blockade of activated Stat3 by ectopic expression of dominant-negative Stat3 significantly inhibited VEGF expression, and the growth and metastasis of human pancreatic cancer cells. 
SIGNOR-259456
Q8IWJ2
P11717
1
relocalization
up-regulates activity
0.529
Rab9-dependent transport from late endosomes to the Golgi requires the Rab9 effectors p40 (Diaz et al., 1997) and TIP47 (Diaz and Pfeffer, 1998), a protein that recognizes the cytoplasmic domains of the two types of MPRs and packages them into nascent transport vesicles (Carroll et al., 2001). MPR recycling also utilizes a TGN-localized coiled-coil protein named GCC185 that is also a Rab9 effector
SIGNOR-253085
P06748
P51452
0
dephosphorylation
down-regulates activity
0.2
In the absence of DUSP3, these three residues remain phosphorylated and favor the dissociation equilibrium of NPM homo-oligomerization and/or its association with ARF, therefore promoting an early nuc|Therefore, here we focused on the molecular mechanisms used by DUSP3-NPM interaction to affect the abovementioned cellular responses and found out that DUSP3 dephosphorylates three tyrosine residues (Y29, Y67, and Y271) of NPM.
SIGNOR-277005
P45983
Q13469
1
phosphorylation
down-regulates
0.752
Jnks directly phosphorylate nuclear factor of activated t-cell (nfat) transcription factors, thus antagonizing the effects of calcium-regulated signaling through the protein phosphatase calcineurin jnk directly regulated nuclear factor of activated t-cell (nfat) activation in culture and in transgenic mice containing an nfat-dependent luciferase reporter.
SIGNOR-118217
P40818
P08581
1
destabilization
down-regulates quantity
0.456
Degradation of acutely stimulated receptor tyrosine kinases, epidermal growth factor receptor and Met, is strongly inhibited in UBPY knockdown cells suggesting that UBPY function is essential for growth factor receptor down-regulation.
SIGNOR-266903
Q8NB16
P30530
0
phosphorylation
up-regulates quantity by stabilization
0.2
TAM kinases phosphorylate MLKL to promote necroptosis. MLKL is then recruited to the plasma membrane, where TAM kinases phosphorylate MLKL at Tyr376 (Figure 5G, step 5), promoting its oligomerization and formation of membrane-rupturing pores that result in necrotic cell death (Figure 5G, step 6).
SIGNOR-274119
P05771
Q16625
1
phosphorylation
up-regulates activity
0.455
Protein kinase C regulates the phosphorylation and cellular localization of occludin. Ser(338) of occludin was identified as an in vitro protein kinase C phosphorylation site using peptide mass fingerprint analysis and electrospray ionization tandem mass spectroscopy. Both the phosphorylation of occludin and its incorporation into tight junctions induced by calcium switch were markedly inhibited by the PKC inhibitor GF-109203X.
SIGNOR-249106
Q92570
Q9BXH1
1
transcriptional regulation
up-regulates quantity by expression
0.2
Over-expression of NR4A3 attenuated proliferation of cancer cells and promoted apoptosis by augmenting the expression of pro-apoptotic genes, PUMA and Bax.
SIGNOR-259396
P28482
Q14686
1
phosphorylation
up-regulates activity
0.2
In vitro phosphorylation studies with His-tagged TRBP (795–931) suggested that S884 can be phosphorylated by MAPK (ERK2) in vitro (Fig. 10A).Analysis of in vitro and in vivo receptor interactions with TRBP suggested that S884 allowed selective interactions for ERβ, TR, and RXR vs. ERα.
SIGNOR-265882
Q13555
Q9Y618
1
phosphorylation
down-regulates
0.2
The kinase activity of camkii was essential for the activation of notch signaling. We also determined that camkii could enhance the association between notch1-ic and rbp-jk. Furthermore, the physical association between rbp-jk and smrt was substantially suppressed by camkii. We demonstrated that camkii directly bound and phosphorylated smrt at ser-1407, thereby facilitating smrt translocation from the nucleus to the cytoplasm and proteasome-dependent degradation.
SIGNOR-191777
Q16620
P12931
0
phosphorylation
up-regulates activity
0.46
Indeed, activated Src can directly phosphorylate recombinant TrkB protein in a cell-free system.|We found that both exogenous H 2 O 2 and endogenous ROS activate TrkB signaling by a Src family kinase dependent but brain derived neurotrophic factor independent mechanism in cultured rat cortical neurons.
SIGNOR-280130
Q9HBY8
O43524
1
phosphorylation
down-regulates activity
0.521
Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)|However, SGK and Akt display differences with respect to the efficacy with which they phosphorylate the three regulatory sites on FKHRL1. While both kinases can phosphorylate Thr-32, SGK displays a marked preference for Ser-315 whereas Akt favors Ser-253. These findings suggest that SGK and Akt may coordinately regulate the function of FKHRL1 by phosphorylating this transcription factor at distinct sites. The efficient phosphorylation of these three sites on FKHRL1 by SGK and Akt appears to be critical to the ability of growth factors to suppress FKHRL1-dependent transcription, thereby preventing FKHRL1 from inducing cell cycle arrest and apoptosis.
SIGNOR-249130
P24941
O60934
1
phosphorylation
up-regulates activity
0.507
Nbs1 is phosphorylated by Cdk2 on Ser432 in human whole-cell extracts.
SIGNOR-279500
Q01860
P26358
1
transcriptional regulation
up-regulates quantity by expression
0.437
Oct4 and Nanog upregulate Dnmt1 through direct binding to its promoter, thereby leading to the repressed expression of p16 and p21 and genes associated with development and lineage differentiation
SIGNOR-253158
P42574
Q9BQQ3
1
cleavage
up-regulates activity
0.396
In contrast, Caspase‐3 cleavage of GRASP‐1 releases the C‐terminal fragment, which in turn activates JNK signaling by serving as a scaffold protein
SIGNOR-260613
Q96RR4
Q13131
1
phosphorylation
up-regulates
0.604
Ampka1 activators increased phosphorylation level and cytoplasmic localization (reduced nuclear/cytoplasmic ratio). Ampka1 activators reduced rna synthesis in the nucleoli.
SIGNOR-176602
Q00613
P27361
0
phosphorylation
down-regulates
0.631
Sequential phosphorylation of hsf1 by mitogen-activated protein kinase and glycogen synthase kinase 3 at ser-303 and ser-307 represses transcriptional activation by heat shock factor-1.
SIGNOR-44999
O43521
P53779
0
phosphorylation
up-regulates activity
0.689
JNKs specifically phosphorylate BIMEL at Ser55, 65, and/or 73. several observations demonstrate that the phosphorylation of BIMEL is a physiologically important mechanism for enhancing its proapoptotic activity.
SIGNOR-250130
P17252
P13726
1
phosphorylation
up-regulates
0.2
We previously showed that the phosphorylation of ser253 within the cytoplasmic domain of human tissue factor (tf) initiates the incorporation and release of this protein into cell-derived microparticles. Furthermore, subsequent phosphorylation of ser258 terminates this process. The phosphorylation of ser253 is known to be mediated by protein kinase c_
SIGNOR-199872
P14679
P05771
0
phosphorylation
up-regulates
0.441
We conclude that pkc-beta activates tyrosinase directly by phosphorylating serine residues at positions 505 and 509 in the cytoplasmic domain of this melanosome-associated protein. our results strongly suggest that direct phosphorylation of tyrosinase by pkc-_ leads to its activation.
SIGNOR-67870
Q9BUB5
O00141
0
phosphorylation
down-regulates activity
0.2
We show that SGK1 phosphorylates MNK1 at a conserved site, which represses its activity. 
SIGNOR-277357
O75385
Q96PU5
0
ubiquitination
down-regulates quantity by destabilization
0.361
NEDD4L ubiquitylates ULK1 at lysine 925 and lysine 933.|Next, we found that down-regulation of the ULK1 protein by NEDD4L is blocked by proteasome inhibitors (MG132 and lactacystin), but not by lysosomal inhibitors (leupeptin and Clq; XREF_FIG and S2 C), indicating that NEDD4L triggers ULK1 degradation exclusively through the proteasome pathway.
SIGNOR-278523
P24941
P98177
1
phosphorylation
down-regulates
0.518
Additionally, ck1, dyrk1a, and cdk2 also phosphorylate foxos at various sites to inhibit foxos activity
SIGNOR-183655
P25098
P17612
0
phosphorylation
up-regulates activity
0.2
PKA directly phosphorylates GRK2 on serine 685. This modification increases G subunit binding to GRK2 and thus enhances the ability of the kinase to translocate to the membrane and phosphorylate the receptor.
SIGNOR-250334
P20823
P05019
1
transcriptional regulation
up-regulates quantity by expression
0.301
Growth hormone induces insulin-like growth factor-I gene transcription by a synergistic action of STAT5 and HNF-1α
SIGNOR-251720
Q13315
O95863
1
phosphorylation
up-regulates activity
0.482
ATM-mediated Snail Serine 100 phosphorylation regulates cellular radiosensitivity.
SIGNOR-279587
P18031
P19235
1
dephosphorylation
down-regulates activity
0.459
In vivo interaction between EPO-R and PTP1B suggested that PTP1B dephosphorylates the EPO-R intracellularly.|Protein tyrosine phosphatase 1B participates in the down-regulation of erythropoietin receptor signalling.
SIGNOR-276994
O96017
P53350
0
phosphorylation
up-regulates
0.492
Plk1 overexpression enhances phosphorylation of chk2 at thr-68.
SIGNOR-96637
Q13950
Q09472
0
acetylation
up-regulates quantity
0.453
Bmp-induced non-smad erk signaling pathway cooperatively regulates osteoblast differentiation, in part, through increasing the stability and transcriptional activity of runx2 or increasing runx2 acetylation by p300.
SIGNOR-195579
Q92538
P84077
1
guanine nucleotide exchange factor
up-regulates activity
0.719
GBF1 Stimulates Production of Arf-GTP In Vivo
SIGNOR-277400
P01116
P49356
0
null
up-regulates activity
0.419
Major investments have been made to target Ras through indirect routes. Inhibition of farnesyl transferase to block Ras maturation has failed in large clinical trials.
SIGNOR-242556