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14
Q96PY6
Q9UKI8
0
phosphorylation
up-regulates activity
0.29
TLK1 phosphorylated NEK1 at T141, which lies in the kinase domain, and caused an increase in its activity. 
SIGNOR-275840
P05204
P51812
0
phosphorylation
down-regulates activity
0.29
We report here that the NBD of the HMGN1 and -N2 protein family is highly and specifically phosphorylated during mitosis and that this phosphorylation has a major functional consequence: it abolishes the interaction of the proteins with its chromatin targets.
SIGNOR-249102
Q9Y2J4
Q9H0M0
0
ubiquitination
up-regulates activity
0.29
AMOTL2 mono-ubiquitination by WWP1 promotes contact inhibition by facilitating LATS activation|Here, we provide evidence that the E3 ligase WWP1 (WW-domain containing protein 1) mono-ubiquitinates AMOTL2 (angiomotin-like 2) at K347 and K408.
SIGNOR-271873
P46527
P36888
0
phosphorylation
down-regulates activity
0.29
FLT3 and FLT3-ITD phosphorylate and inactivate the cyclin-dependent kinase inhibitor p27 Kip1 in acute myeloid leukemia|P27Kip1 (p27) can prevent cell proliferation by inactivating cyclin-dependent kinases. This function is impaired upon phosphorylation of p27 at tyrosine residue 88.
SIGNOR-269208
Q5JVS0
P05771
0
phosphorylation
down-regulates activity
0.29
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This s...
SIGNOR-249247
P05204
P17252
0
phosphorylation
down-regulates
0.29
Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a...
SIGNOR-76320
Q96P20
P07948
0
phosphorylation
down-regulates
0.29
Lyn phosphorylates NLRP3 at Tyr 918 and controls NLRP3 ubiquitination.|Therefore, our data collectively indicate that Lyn inhibits the NLRP3 inflammasome in vivo.
SIGNOR-278485
Q92974
P27361
0
phosphorylation
up-regulates
0.29
Activates rhoa and as a result regulates actin assembly.
SIGNOR-160420
P13611
P04637
0
transcriptional regulation
up-regulates quantity by expression
0.29
By using in vitro and in vivo assays, we showed CSPG2 to be directly transactivated by p53.
SIGNOR-255441
P40337
P12931
0
phosphorylation
down-regulates quantity by destabilization
0.29
We have found that elevated Src can trigger a drastic reduction in VHL stability even under normoxic conditions, through phosphorylation of VHL tyrosine residue 185, leading to ubiquitination and proteasome mediated degradation of VHL.
SIGNOR-279125
P46531
P51608
0
transcriptional regulation
down-regulates quantity by repression
0.29
As the first step to reveal how MeCP2 phosphorylation may regulate Notch signaling, we conducted chromatin immunoprecipitation (ChIP) experiment to determine whether the phosphor-mutant MeCP2 protein has altered promoter occupancy at the promoters of Dll1 and Notch1. We found increased binding of the phosphor-mutant pr...
SIGNOR-264675
Q8TD08
P67775
0
dephosphorylation
down-regulates
0.289
Erk8 (extracellular-signal-regulated protein kinase 8) expressed in escherichia coli or insect cells was catalytically active and phosphorylated at both residues of the thr-glu-tyr motif. Dephosphorylation of the threonine residue by pp2a (protein serine/threonine phosphatase 2a) decreased erk8 activity by over 95% in ...
SIGNOR-142977
P46527
P49336
0
phosphorylation
down-regulates
0.289
As a consequence, CDK8 overexpression promoted p27 degradation, whereas CDK8 knockdown reduced it.|We also show that CDK8 promotes phosphorylation of p27 at T187 and then induces p27 ubiquitination and degradation in a Skp2-dependent manner.
SIGNOR-278513
P15056
Q9Y243
0
phosphorylation
down-regulates
0.289
We show that phosphorylation of b-raf by akt occurs at multiple residues within its aminoterminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity.
SIGNOR-78693
P35222
Q13554
0
phosphorylation
down-regulates
0.289
Camkii represses transcriptionally active _-catenin to mediate acute ethanol neurodegeneration and can phosphorylate _-catenincamkii can directly phosphorylate _-catenin. Using targeted mutagenesis we identified camkii phosphorylation sites within human _-catenin at t332, t472, and s552.
SIGNOR-202833
P04049
P53350
0
phosphorylation
up-regulates activity
0.289
An in vitro kinase assay demonstrated that PLK1 directly phosphorylated CRAF at S338 and S339, but not at S621 (XREF_FIG).|These results demonstrate that PLK1 increases the stability of CRAF protein by preventing proteasome degradation.
SIGNOR-278190
P11831
Q09013
0
phosphorylation
up-regulates
0.289
Myotonic dystrophy protein kinase (DMPK), a muscle- and neuron-restricted kinase, enhanced SRF-mediated promoter activity of the skeletal and cardiac alpha-actin genes in C2C12 myoblasts as well as in nonmyogenic cells. | Threonine 159 in the MADS box alphaI coil was a specific phosphorylation target in vitro as well a...
SIGNOR-236982
O95863
Q9UNE7
0
ubiquitination
down-regulates quantity by destabilization
0.289
These results indicate that CHIP can ubiquitylate and degrade Snail in a GSK\u20103\u03b2\u2010independent manner.|These results suggest that CHIP negatively regulates the stability of Snail through inducing its proteasomal degradation.
SIGNOR-278545
P60484
P29375
0
transcriptional regulation
down-regulates quantity by destabilization
0.289
The retinoblastoma binding protein 2 (RBP2) belongs to the KDM5 family, and is also known as JARID1A or KDM5A. We found that histone H3 lysine 4 (H3K4) demethylase RBP2 expression is negatively correlated with BCR-ABL expression, which suggests a regulatory link between these two genes. We also discovered that RBP2 med...
SIGNOR-260079
P26678
P31749
0
phosphorylation
down-regulates activity
0.289
Akt interacts with and phosphorylates PLN at Thr(17), the Ca(2+)-calmodulin-dependent kinase IIdelta site, whereas silencing Akt signaling, through the knock-out of phosphatidylinositol-dependent kinase-1, resulted in reduced phosphorylation of PLN at Thr(17).
SIGNOR-252578
O95837
O60755
0
binding
up-regulates activity
0.289
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signali...
SIGNOR-257206
P52630
P49841
0
phosphorylation
down-regulates quantity by destabilization
0.289
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation.
SIGNOR-276764
P63096
P21918
0
binding
up-regulates activity
0.289
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signali...
SIGNOR-257043
P37231
P14373
0
ubiquitination
down-regulates quantity by destabilization
0.289
Mechanically, TRIM27 ubiquitinates and degrades PPARgamma, following induces cleaved Caspase-3 and IL-1beta expression.
SIGNOR-278734
P19086
P25103
0
binding
up-regulates activity
0.289
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signali...
SIGNOR-257316
Q14934
P27361
0
phosphorylation
up-regulates
0.289
The formation of rsk-nfatc4-dna transcription complex is also apparent upon adipogenesis. Bound rsk phosphorylates ser(676) and potentiates nfatc4 dna binding by escalating nfat-dna association. Ser(676) is also targeted by the erk map kinase, which interacts with nfat at a distinct region than rsk. Thus, integration o...
SIGNOR-133276
P38405
P41968
0
binding
up-regulates activity
0.289
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signali...
SIGNOR-256748
P04626
P23470
0
dephosphorylation
up-regulates activity
0.289
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and V...
SIGNOR-254701
P11233
P62714
0
dephosphorylation
down-regulates
0.289
Pp2a abeta-containing complexes dephosphorylate rala at ser183 and ser194, inactivating rala and abolishing its transforming function
SIGNOR-155349
P04792
P31751
0
phosphorylation
down-regulates
0.289
First, the akt1, akt2, and akt3 isoforms can bind directly to hsp27 and can be found in a complex with p38 mapk, mk2, and hsp27 [98_100]. Second, rane and colleagues showed that akt could phosphorylate hsp27 at ser-82, but not ser-15 or ser-78, in vitro, while co-expression of an active akt mutant and hsp27 in hek cell...
SIGNOR-186776
P61160
P18075
0
binding
up-regulates
0.289
The two ligands induce the formation of two ligand-receptor complexes, cbmp7 (blue) and ctgf-b (red), that share the type i receptor alk2
SIGNOR-144144
P42858
Q9UHD2
0
phosphorylation
up-regulates activity
0.289
Herein, we report the discovery and validation of a kinase, TANK-binding kinase 1 (TBK1), that efficiently phosphorylates full-length and N-terminal HTT fragments in vitro (at S13/S16), in cells (at S13) and in vivo. TBK1 expression in HD models (cells, primary neurons, and Caenorhabditis elegans) increases mutant HTT ...
SIGNOR-270350
P04264
Q03405
0
binding
up-regulates activity
0.288
Cytokeratin 1 binds to both gC1qR and u-PAR. Our data suggest that formation of HK (and Factor XII) binding sites along endothelial cell membranes consists of bimolecular com-plexes of gC1qR-cytokeratin 1 and u-PAR-cytokeratin 1, with gC1qR binding being favored.
SIGNOR-251880
P30411
P32298
0
phosphorylation
down-regulates activity
0.288
Expression of GRK4α drastically increased the basal level of32P incorporation into B2R. GRK4α elevated the basal phosphorylation of Ser339 and Ser346/Ser348. phosphorylation of specific residues was correlated with the initiation of receptor internalization and the regulation of its desensitization.
SIGNOR-251193
P30411
P43250
0
phosphorylation
down-regulates activity
0.288
Ligand-induced phosphorylation is found at Ser339 and Ser346/Ser348 that could be executed by several G protein-coupled receptor kinases. 32P labeling of peptide 3 containing pS346/pS348 was enhanced 1.5–3-fold as compared with mock-transfected cells in the order GRK6 < GRK5 < GRK2 < GRK4α < GRK3. several endogenous GR...
SIGNOR-251207
O75581
Q9Y6M4
0
phosphorylation
up-regulates activity
0.288
Central to WNT signalosome formation is phosphorylation of LRP6 at multiple sites, with GSK3β phosphorylating LRP6 at S1490 and CK1 family members phosphorylating LRP6 at T1479 and T1493
SIGNOR-275401
O60716
P49674
0
phosphorylation
down-regulates
0.288
Moreover, in response to wnt3a, p120-catenin is phosphorylated at ser268, a modification dependent on ck1epsilon activity, which disrupts its interaction with e-cadherin and, subsequently, with lrp5/6, promoting the release of ck1epsilon/p120-catenin from the wnt receptor complex.
SIGNOR-24443
O14936
Q00535
0
phosphorylation
up-regulates activity
0.288
Cdk5 promotes synaptogenesis by regulating the subcellular distribution of the MAGUK family member CASK.|We found that Cdk5 phosphorylates and regulates CASK distribution to membranes.
SIGNOR-280216
Q92974
P63172
0
binding
down-regulates activity
0.288
Rho-Rac guanine nucleotide exchange factor 2 (ARHGEF2), which activates Ras homolog family member A (RHOA), is anchored to the microtubule network and sequestered in an inhibited state through binding to dynein light chain Tctex-1 type 1 (DYNLT1). We showed in mammalian cells that liver kinase B1 (LKB1) activated the m...
SIGNOR-277369
Q05586
Q8TBB1
0
ubiquitination
down-regulates quantity by destabilization
0.288
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous su...
SIGNOR-272901
Q01167
P57073
0
transcriptional regulation
up-regulates quantity by expression
0.288
We showed for the first time that Aurora-A interacts directly with SOX8 and phosphorylates the protein at Ser327 to further regulate the SOX8/FOXK1 axis, which modulates cell senescence and glycolysis, ultimately leading to cisplatin resistance.. Our results showed that SOX8 targets FOXK1, thereby regulating its transc...
SIGNOR-273613
O60879
Q96GD4
0
phosphorylation
up-regulates
0.288
The microtubule binding fh2 domain of mdia3 is phosphorylated by aurora b kinase in vitro, and cells expressing the nonphosphorylatable mdia3 mutant cannot position chromosomes at the metaphase plate
SIGNOR-172803
P31146
Q00535
0
phosphorylation
up-regulates activity
0.288
We here show that phosphorylation of coronin 1 on Thr(418/424) by cyclin-dependent kinase (CDK) 5 activity was responsible for coronin 1-G_s association and the modulation of cAMP production. Together these results show an essential role for CDK5 activity in promoting the coronin 1-dependent cAMP/PKA pathway.
SIGNOR-245187
P46531
Q92630
0
phosphorylation
down-regulates quantity by destabilization
0.288
We demonstrate that DYRK2 phosphorylates Notch1-IC in response to chemotherapeutic agents and facilitates its proteasomal degradation by FBXW7 ubiquitin ligase through a Thr-2512 phosphorylation-dependent mechanism.
SIGNOR-279035
P28329
Q05513
0
phosphorylation
up-regulates
0.288
Finally, basal chat phosphorylation in neurons is mediated predominantly by pkc at ser-476, with pkc activation increasing phosphorylation at ser-440 and enhancing chat activity.
SIGNOR-129340
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
P60953
P52306
0
binding
up-regulates
0.288
Smggds has been previously shown to activate a wide variety of small gtpases, including the ras family members rap1a, rap1b, and k-ras, as well as the rho family members cdc42, rac1, rac2, rhoa, and rhob
SIGNOR-171412
Q6PKG0
P31749
0
phosphorylation
down-regulates activity
0.288
LARP1 is a direct substrate of Akt/S6K1 and mTORC1. Akt is a physiologically relevant primary kinase for S770/S979 phosphorylation of LARP1|Importantly, phosphorylation of LARP1 by mTORC1 and Akt/S6K1 dissociates it from 5’UTRs and relieves its inhibitory activity on RP mRNA translation.
SIGNOR-260992
P49841
Q96RG2
0
phosphorylation
down-regulates activity
0.288
In vitro, PASK directly phosphorylates GSK3\u03b2 on its inactivating phosphorylation site Ser(9).|We conclude that PASK phosphorylates and inactivates GSK3\u03b2, thereby preventing PDX-1 serine phosphorylation and alleviating GSK3\u03b2-mediated PDX-1 protein degradation in pancreatic \u03b2-cells.
SIGNOR-279639
O43829
Q96RE7
0
binding
up-regulates activity
0.288
NAC1 potentiated ZF5 mediated repression in Gal4-DBD fusion transient assays. GST pulldown assays further confirmed protein–protein interactions between these proteins and NAC1.
SIGNOR-226443
P30679
O43603
0
binding
up-regulates activity
0.288
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signali...
SIGNOR-257226
Q99683
P30307
0
dephosphorylation
down-regulates activity
0.288
At the interval CDC25C inhibits ASK1, dephosphorylating pThr838 in its activation loop.|CDC25C dephosphorylates ASK1 to inhibit its activity during the interphase.
SIGNOR-277100
Q15831
Q15418
0
phosphorylation
down-regulates activity
0.288
Negative regulation of the LKB1/AMPK pathway by ERK in human acute myeloid leukemia cellsBRAFV600E activates downstream molecules, including ERK and p90 ribosomal S6 kinase (RSK), and leads to the phosphorylation of LKB-1 at Ser428 by these kinases. This cascade results in the dissociation of LKB1 from AMPK.
SIGNOR-209871
Q8WWK9
P06493
0
phosphorylation
up-regulates
0.288
Among these, thr-622 was specifically phosphorylated by cdk1-cyclin b1 both in vitro and in vivo. these findings suggest that cdk1-cyclin b1-mediated phosphorylation of tmap is important for and contributes to proper regulation of microtubule dynamics and establishment of functional bipolar spindles during mitosis.
SIGNOR-185317
Q13144
Q92837
0
binding
up-regulates activity
0.288
In contrast to the GS‐1 peptide, glycogen synthase and the eIF2B peptide, the GSK3‐catalysed phosphorylation of Tau was completely inhibited by FRATtide|This prevents GSK3 from phosphorylating and inhibiting glycogen synthase [2, 3] and protein synthesis initiation factor eIF2B
SIGNOR-262835
P15336
Q02156
0
phosphorylation
up-regulates
0.288
Pkc_ phosphorylation of atf2 on thr52. Pkc_ promotes oncogenic functions of atf2 in the nucleus while blocking its apoptotic function at mitochondria
SIGNOR-195761
Q9NRD5
Q6ZN44
0
binding
up-regulates activity
0.288
Recently, our laboratory showed that UNC5A is coimmunoprecipitated with PICK1 and PKCα. Moreover, we demonstrated that the association of PKCα with UNC5A depends on the activation of PKCα and the ability of UNC5A to bind PICK1
SIGNOR-268181
Q9UI33
Q96PU5
0
ubiquitination
down-regulates quantity by destabilization
0.288
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 ...
SIGNOR-253462
P35222
Q9H251
0
binding
up-regulates activity
0.288
At its C-terminus, cadherin interacts with β-catenin, which dynamically associates with α-catenin, a direct binding partner of filamentous actin
SIGNOR-265861
P00390
Q13131
0
phosphorylation
up-regulates activity
0.288
Mechanistically, AMPKα1 regulate the glutathione reductase (GSR) phosphorylation possibly through residue Thr507 which enhances its activity. 
SIGNOR-273734
Q96PX1
P24941
0
phosphorylation
up-regulates activity
0.287
CDK2 promotes phosphorylation of RNF157 at the same Ser 660-663 residues that become phosphorylated downstream of combined PI3K and MAPK pathway activity.
SIGNOR-279016
P36956
P06493
0
phosphorylation
up-regulates
0.287
Cdk1/cyclin b-mediated phosphorylation stabilizes srebp1 during mitosis.
SIGNOR-148354
P05976
P27361
0
phosphorylation
up-regulates
0.287
Activation of raf/mek/erk cascade can also result in the phosphorylation of the antiapoptotic mcl-1 protein and the pro-apoptotic bim protein.
SIGNOR-148002
P48735
P24752
0
acetylation
down-regulates activity
0.287
Mitochondrial acetyltransferase ACAT1 and deacetylase SIRT3 are responsible for acetylation and deacetylation, respectively, at K413 of mIDH2|K413 acetylation inhibits mIDH2 by simultaneously attenuating dimer formation from monomers and destabilizing dimers for conversion to monomers
SIGNOR-267627
O43524
Q96KS0
0
hydroxylation
down-regulates activity
0.287
Prolyl hydroxylation by EglN2 destabilizes FOXO3a by blocking its interaction with the USP9x deubiquitinase.|Here we report that EglN2 can hydroxylate FOXO3a on two specific prolyl residues in vitro and in vivo. Hydroxylation of these sites prevents the binding of USP9x deubiquitinase, thereby promoting the proteasomal...
SIGNOR-261998
Q9ULU4
P25440
0
relocalization
up-regulates activity
0.287
ZMYND8 and BRD2 therefore work together to protect H4Ac domains from HDAC activity.|Further, when BRD2 was depleted, ZMYND8 accumulation was lost (Fig. 2e), indicating that either BRD2, or the underlying H4Ac, is required for ZMYND8 loading.
SIGNOR-262036
O60674
P23470
0
dephosphorylation
down-regulates activity
0.287
Deeper examination shows that JAKs are critically involved in integrin-mediated monocyte adhesion and that PTPRG activation leads to JAK2 dephosphorylation on the critical 1007–1008 phosphotyrosine residues, implying JAK2 inhibition and thus explaining the antiadhesive role of PTPRG.
SIGNOR-254690
Q92985
P63279
0
sumoylation
down-regulates activity
0.287
One mechanism by which LMP1 regulates cellular activation is through the induction of protein posttranslational modifications. We have now identified a specific target of LMP1-induced sumoylation, interferon regulatory factor 7 (IRF7). We hypothesize that during EBV latency, LMP1 induces the sumoylation of IRF7, limiti...
SIGNOR-266837
P46531
O00629
0
relocalization
up-regulates
0.287
Nicd binds via one of its four potential nuclear localization signals to importins alfa3, alfa4, and alfa7.
SIGNOR-165314
Q9GZM8
P28482
0
phosphorylation
up-regulates activity
0.287
In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively,...
SIGNOR-274076
Q00613
Q02750
0
phosphorylation
up-regulates activity
0.287
This study indicates that mTORC1, MEK1, p38 and DYRK2 induce HSF1 activity to a similar level but phosphorylate HSF1 primarily at S326 as well as S363, a known inhibitory site [71,72], S221, also thought to be an inhibitory site [70], or at S241 and S344, which are two novel phosphorylation sites with unknown function....
SIGNOR-279208
P18564
O14713
0
binding
down-regulates activity
0.287
Integrins also bind to many PTBdomain-containing proteins (Calderwood et al., 2003) – including Dok1 and integrincytoplasmic-domain-associated protein 1 (ICAP1) – and these can compete with talin for binding to integrin and so can impair activation
SIGNOR-257662
P26010
O14713
0
binding
down-regulates activity
0.287
Integrins also bind to many PTBdomain-containing proteins (Calderwood et al., 2003) – including Dok1 and integrincytoplasmic-domain-associated protein 1 (ICAP1) – and these can compete with talin for binding to integrin and so can impair activation
SIGNOR-257664
P12830
P56524
0
transcriptional regulation
down-regulates quantity by repression
0.287
GATA1 is a new substrate of p21-activated kinase 5 (PAK5), which is phosphorylated on serine 161 and 187 (S161 and S187). GATA1 recruits HDAC3/4 to E-cadherin promoter, which is reduced by GATA1 S161A S187A mutant. These data indicate that phosphorylated GATA1 recruits more HDAC3/4 to promote transcriptional repression...
SIGNOR-275663
P05067
P53355
0
phosphorylation
up-regulates quantity
0.287
DAPK1, but not its kinase deficient mutant (K42A), significantly increased human Aβ secretion in neuronal cell culture models. Moreover, knockdown of DAPK1 expression or inhibition of DAPK1 catalytic activity significantly decreased Aβ secretion. Furthermore, DAPK1, but not K42A, triggered Thr668 phosphorylation of A...
SIGNOR-279518
Q13568
P42229
0
transcriptional regulation
up-regulates quantity by expression
0.287
The GM-CSF receptor forms a dodecamer structure and recruits JAK2, leading to the activation of STAT5, extracellular signal-regulated kinase (ERK), V-Akt murine thymoma viral oncogene homolog 1 (AKT), and the nuclear translocation of NF-kappaB and IRF5
SIGNOR-249508
P36406
O14920
0
phosphorylation
down-regulates activity
0.287
Phosphorylation of ARD1 by IKKbeta reduced its growth suppression effect.
SIGNOR-279337
P29350
P24941
0
phosphorylation
down-regulates quantity by destabilization
0.287
Interaction between SHP-1 and Cdk2 was confirmed by co-immunoprecipitations whereby co-precipitated Cdk2 phosphorylated SHP-1 protein.
SIGNOR-279147
P10721
O96017
0
phosphorylation
up-regulates
0.286
In this report, we characterize the binding of sh2(chk) to specific phosphotyrosine sites on the c-kit protein sequence. the sh2(chk) binding to the two sites is direct and not through phosphorylated intermediates such as fyn or shc. this indicates that chk binds to the same site on c-kit to which fyn binds, possibly...
SIGNOR-197281
P04637
P62140
0
dephosphorylation
down-regulates activity
0.286
Protein serine/threonine phosphatase-1 dephosphorylates p53 at Ser-15 and Ser-37 to modulate its transcriptional and apoptotic activities|In addition, our results reveal that one of the molecular mechanisms by which PP-1 promotes cell survival is to dephosphorylate p53, and thus negatively regulate p53-dependent death ...
SIGNOR-248572
Q9H2S1
Q05086
0
ubiquitination
up-regulates activity
0.286
UBE3A directly ubiquitinates SK2 in the C-terminal domain, which facilitates endocytosis.
SIGNOR-278527
P28329
P05771
0
phosphorylation
up-regulates
0.286
Protein kinase c isoforms differentially phosphorylate human choline acetyltransferase regulating its catalytic activity.
SIGNOR-129288
Q6JBY9
P45983
0
phosphorylation
down-regulates activity
0.286
CapZIP was also phosphorylated rapidly by SAPK3/p38γ and SAPK4/p38δ, and even faster and more extensively by JNK1α1, these protein kinases phosphorylating CapZIP in vitro to >3, approx. 2 and >5 mol of phosphate/mol of protein respectively within a few minutes. Following tryptic digestion and C18 chromatography, furthe...
SIGNOR-263085
P25490
P68400
0
phosphorylation
up-regulates
0.286
More recently, we identified and mapped multiple phosphorylation sites in yy1, including, threonine 39, serine 118, serine 247, threonine 348 and threonine 378. The first kinase proven to phosphorylate yy1 in vivo was plk1, which phosphorylates threonine 39 during g2/m stage of the cell cycle [25]. Ck2_ is another kina...
SIGNOR-200083
P55957
P19784
0
phosphorylation
up-regulates activity
0.286
Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. | These results suggest that residues S61, S64, and to a much lesser extent T58 are site...
SIGNOR-250978
P55957
P67870
0
phosphorylation
up-regulates activity
0.286
Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. | These results suggest that residues S61, S64, and to a much lesser extent T58 are site...
SIGNOR-251054
P08235
P28482
0
phosphorylation
down-regulates quantity by destabilization
0.286
 Taken together, these data suggest that ERK1/2 directly phosphorylates the MR on several serine residues present in its NTD, that the upward shift of MR is mainly due to receptor phosphorylation, and finally that these sites represent the major aldosterone-inducible targets for MR phosphorylation.MR phosphorylation li...
SIGNOR-276101
O95983
O14965
0
phosphorylation
up-regulates
0.286
These results suggest that the biochemical changes of mbd3 may be intimately related to the targeting of mbd3 to centrosomes. aurora-a phosphorylates mbd3
SIGNOR-93693
P04792
Q9Y243
0
phosphorylation
down-regulates
0.286
First, the akt1, akt2, and akt3 isoforms can bind directly to hsp27 and can be found in a complex with p38 mapk, mk2, and hsp27 [98_100]. Second, rane and colleagues showed that akt could phosphorylate hsp27 at ser-82, but not ser-15 or ser-78, in vitro, while co-expression of an active akt mutant and hsp27 in hek cell...
SIGNOR-186780
Q8WYL5
O94806
0
phosphorylation
down-regulates activity
0.286
Active PKD Isoforms Phosphorylate and Inactivate SSH1L|Here, we show that active PKD3 also mediates SSH1L phosphorylation at Ser-978 and binding to 14-3-3, further confirming the involvement of all three PKD isoforms in negatively regulating this phosphatase
SIGNOR-275938
Q13683
P15172
0
transcriptional regulation
up-regulates quantity by expression
0.286
Only myogenin and MyoD were able to efficiently trans-activate the alpha7 promoter-CAT construct (Fig. 7). Myogenin trans-activated the promoter by _2-fold whereas MyoD was able to trans-activate by nearly 4-fold, indicating that both of these factors may play a role in alpha7 gene expression during muscle development.
SIGNOR-241518
P55957
P48729
0
phosphorylation
up-regulates activity
0.286
Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. | These results suggest that residues S61, S64, and to a much lesser extent T58 are site...
SIGNOR-250785
P24844
Q05397
0
phosphorylation
up-regulates activity
0.286
It indicates that FAK positively regulates the phosphorylation of MLC2.
SIGNOR-280098
P62140
Q96C90
0
binding
down-regulates activity
0.286
We conclude that ILK may activate smooth-muscle contraction both directly, via phosphorylation of myosin, and indirectly, via phosphorylation and activation of CPI-17 and PHI-1, leading to inhibition of MLCP.|CPI-17 and PHI-1 thiophosphorylated by ILK at Thr(38) or Thr(57) respectively inhibited myosin light-chain phos...
SIGNOR-265743
P04637
Q9UEE5
0
phosphorylation
up-regulates
0.286
Genetic and biochemical studies have shown that ser20 phosphorylation in the transactivation domain of p53 mediates p300-catalyzed dna-dependent p53 acetylation and b-cell tumor suppression. a cell-free ser20 phosphorylation site assay was used to identify a broad range of calcium calmodulin kinase superfamily members...
SIGNOR-153532
P22415
P49841
0
phosphorylation
up-regulates activity
0.286
 Both MITF and USF1 were activated by glycogen synthase kinase (GSK) 3, with GSK3 phosphorylation sites on USF1 identified as the previously described activating site threonine 153 as well as serine 186.
SIGNOR-276355
P50148
P34998
0
binding
up-regulates activity
0.286
Previous studies have indicated that CRHR could couple to multiple Galpha proteins including Gs, Gi, and Gq/11 and then go on to induce changes in AC activity and activation of PLC-beta3
SIGNOR-268619
P31269
O43189
0
transcriptional regulation
down-regulates quantity by repression
0.286
These data support the proposed regulatory impact of particular PRC2-proteins in expression of HOXA9 and HOXA10 in NK/T-cells. In mammalian cells knockdown of PRC2 components EZH2 or PHF1 led to upregulated HOXA gene expression.
SIGNOR-260069
P15172
P00519
0
phosphorylation
down-regulates activity
0.286
We have found that c-Abl can phosphorylate MyoD at a conserved N-terminal tyrosine (Tyr30) that is located within the transactivation domain. Mutation of Tyr30 to Phe does not interfere with the function of MyoD, but theTyr30Phe mutant becomes resistant to the inhibitory effect of DNA damage.
SIGNOR-253055
Q86VP3
Q13489
0
polyubiquitination
down-regulates quantity by destabilization
0.286
Under basal conditions, PACS-2 underwent K48-linked poly-ubiquitination, resulting in PACS-2 proteasomal degradation. Biochemical assays showed cIAP-1 and cIAP-2 interacted with PACS-2 in vitro and co-immunoprecipitation studies demonstrated that the two cIAPs bound PACS-2 in vivo. More importantly, both cIAP-1 and cIA...
SIGNOR-272852