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14
Q9NY61
Q07812
1
transcriptional regulation
down-regulates quantity
0.2
We identify the transcriptional regulator apoptosis-antagonizing transcription factor (AATF)/Che-1 as a critical regulator of the cellular outcome of the p53 response. Upon genotoxic stress, AATF is phosphorylated by the checkpoint kinase MK2. Phosphorylation results in the release of AATF from cytoplasmic MRLC3 and su...
SIGNOR-259916
P47900
Q03113
1
binding
up-regulates activity
0.2
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-257394
P20339
Q9GZQ3
1
binding
up-regulates activity
0.2
The N terminus of COMMD5 binds to the endosomal Rab5, and its C terminus, including the COMMD domain, binds to the cytoskeletal scaffolding.
SIGNOR-261691
P17612
Q9NRD9
1
phosphorylation
up-regulates
0.2
We analyzed the duox1 phosphorylation state with an anti-rxx(ps/pt) antibody that could potentially recognize phosphorylation on ser955 and ser1217 but not on thr1007. duox1 but not duox2 activity is stimulated by forskolin (ec50 = 0.1 _m) via protein kinase a-mediated duox1 phosphorylation on serine 955. duox1 is po...
SIGNOR-183449
Q8IZL9
Q15910
1
phosphorylation
up-regulates activity
0.2
In addition to the transcriptional feedback loop, we also identified a feed-forward loop in which CCRK induces EZH2 phosphorylation, thereby promoting p-EZH2 Ser21 -AR physical interaction for CCRK promoter co-occupancy and transcriptional activation.
SIGNOR-279017
Q96GD4
P68431
1
phosphorylation
down-regulates activity
0.2
Histone code pathway involving h3 s28 phosphorylation and k27 acetylation activates transcription and antagonizes polycomb silencingaurora-b phosphorylates histone h3 at serine28 with regard to the mitotic chromosome condensation
SIGNOR-171717
P22612
Q6PIY7
1
phosphorylation
down-regulates activity
0.2
We found that Gld2 activity is regulated by site-specific phosphorylation in its disordered N-terminal domain. We identified two phosphorylation sites (S62, S110) where phosphomimetic substitutions increased Gld2 activity and one site (S116) that markedly reduced activity. Using mass spectrometry, we confirmed that HEK...
SIGNOR-259404
O14965
P68431
1
phosphorylation
up-regulates activity
0.2
Phosphorylation at ser-11 (h3s10ph) by aurkb is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. Phosphorylation at ser-11 (h3s10ph) by aurkb is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis.
SIGNOR-98289
Q13434
Q8IVH8
1
ubiquitination
down-regulates quantity
0.2
MKRN4 ubiquitinated GLK at Lys650 residue.|Remarkably, MKRN4 overexpression induced GLK protein degradation in HEK293T cells and Jurkat T cells (figure 5A and B).
SIGNOR-278658
P01178-PRO_0000020496
P01178-PRO_0000020495
1
binding
up-regulates quantity
0.2
 Neurophysins I and II (NPI and NPII) serve in the neurosecretory granules of the posterior pituitary as carrier proteins for the neurophyseal hormones oxytocin (OT) and vasopressin (VP), respectively, until the latter are released into blood. 
SIGNOR-270351
Q02156
O60716
1
phosphorylation
down-regulates
0.2
We find that ctnnd1/p120ctn phosphorylation at serine 268 (p-s268) occurs in a strictly pkc_-dependent manner,serine/threonine phosphorylation of p120-ctn has been reported to affect the integrity of ajs [12], [24] and [25]. Xia et al. (2003) reported that several residues (ser122, ser252, ser268, ser288, thr310, ser31...
SIGNOR-201600
Q96QT6
Q04727
1
binding
up-regulates activity
0.2
We have cloned and characterized a new member of the PHD zinc finger family called Pf1 that interacts with two global transcription corepressors: mSin3A and TLE. Pf1 interacts with TLE. The Groucho/TLE proteins are members of an abundant corepressor family, and we hypothesized that Pf1 might interact with TLE family m...
SIGNOR-266989
P17252
Q96AX2
1
phosphorylation
down-regulates activity
0.2
We also show that Rab37 is phosphorylated by protein kinase Cα (PKCα) at threonine 172 (T172), leading to attenuation of its GTP-bound state, and impairment of the Rab37-mediated exocytosis of TIMP1, and thus reduces its suppression activity on lung cancer cell motility. 
SIGNOR-273803
Q96QB1
P35579
1
binding
down-regulates activity
0.2
Our study has shown that Dlc1 interacts with non-muscle myosin heavy chain II-A (Myh9), plectin and spectrin proteins in different multiprotein complexes. Overexpression of Dlc1 led to increased phosphorylation of Myh9 protein and activation of Rac1 GTPase. Dlc1 interacts with phosphorylated Myh9 (Ser-1943). This asso...
SIGNOR-269283
P62714
Q13153
1
dephosphorylation
down-regulates activity
0.2
Both sites were dephosphorylated with the same kinetics; the anti-Ser(P)198 antibody was subsequently used as it exhibited lower background staining. Direct comparison of PP2Cα with purified PP1 and PP2A lead us to conclude that at the same molar ratio PP2Cα was the most efficient in dephosphorylating PAK1 (Fig. 1D). I...
SIGNOR-248600
P39900
P02671
1
cleavage
down-regulates quantity by destabilization
0.2
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII| We have now investigated the role of collagenase-2 (MMP-8), macrophage elastase (MMP-12), collagenase-3 (MMP-13), and membrane type 1-mat...
SIGNOR-263622
Q13418
Q13418
2
phosphorylation
up-regulates activity
0.2
Although ilk has been shown to autophosphorylate serine 343 (s343) is in the hydrophobic motif fsf within the activation loop of the kinase domain and has previously been suggested to be the target of autophosphorylation (9). Mutation of serine 343 to alanine (s343a) resulted in the inability of ilk to stimulate phosph...
SIGNOR-106838
O60502
P17858
1
deglycosylation
up-regulates activity
0.2
Our previous investigation on O-GlcNAcylation of PFK1 has demonstrated that O-GlcNAcylation inhibits PFK1 enzyme activity|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-267608
O14965
O14965
2
phosphorylation
up-regulates
0.2
The upstream pak1 kinase can phosphorylate aurora a at t288, autophosphorylation appears to be the essential mode of activation. Our experiments suggest that phosphorylation of t288 is important for regulation of the aurora2 kinase both for its activity and its stability
SIGNOR-205106
Q9HBM1
Q9BRS2
1
binding
up-regulates activity
0.2
This study demonstrates that SPC25 acts as a molecular scaffold, mediating SPC25/RIOK1/MYH9 complex formation and triggering the RIOK1‐mediated phosphorylation of MYH9 at Ser1943.Taken together, these results suggested that SPC25 increases MYH9 phosphorylation at Ser1943, enhancing the nuclear accumulation of MYH9 and ...
SIGNOR-278893
Q9HBM1
P35579
1
binding
up-regulates activity
0.2
This study demonstrates that SPC25 acts as a molecular scaffold, mediating SPC25/RIOK1/MYH9 complex formation and triggering the RIOK1‐mediated phosphorylation of MYH9 at Ser1943.Taken together, these results suggested that SPC25 increases MYH9 phosphorylation at Ser1943, enhancing the nuclear accumulation of MYH9 and ...
SIGNOR-278894
Q16584
Q16584
2
phosphorylation
up-regulates
0.2
These residues within the activation loop are critical for mlk-3 autophosphorylation and activation. In addition, when the thr277 and ser281 residues were mutated to negatively charged glutamic acid to mimic phosphorylated serine/threonine residues, the resulting mutants were fully functional, implying that these two r...
SIGNOR-83407
P16104
O60934
1
binding
up-regulates
0.2
Nbs1 physically interacts with ?-H2ax to form nuclear foci at dna damage sites. The inhibition of this interaction by introduction of anti-?-H2ax antibody into cells abolishes nbs1 foci formation in response to dna damage.
SIGNOR-133020
O15550
Q01543
1
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 phas...
SIGNOR-260034
Q13554
Q9UBS5
1
phosphorylation
down-regulates quantity by destabilization
0.2
ERK1/2 and CaMKIIβ mediated phosphorylation of GABAB1 at serine 867 (S867) and threonine 872 (T872). We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to dire...
SIGNOR-277851
Q05655
Q9UQ13
1
phosphorylation
down-regulates quantity by destabilization
0.2
PKCalpha/delta phosphorylate Sur8 at Thr-71 and Ser-297, respectively. This phosphorylation is essential for polyubiquitin-dependent degradation of Sur8.
SIGNOR-275565
O14843
P08754
1
binding
up-regulates activity
0.2
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-256821
P62140
Q00987
1
dephosphorylation
up-regulates quantity by stabilization
0.2
Three phosphorylation sites identified are Ser342, Ser367, and Ser403. In the present study, we identify protein phosphatase 1 (PP1) as a negative regulator in the p53 signaling pathway. PP1 directly interacts with Mdmx and specifically dephosphorylates Mdmx at Ser367. The dephosphorylation of Mdmx increases its stabil...
SIGNOR-248577
P05771
P16949
1
phosphorylation
down-regulates
0.2
Op18 is multisite phosphorylated on four ser residues during mitosis;two of these ser residues, ser-25 and ser-38, are targets for cyclin-dependent protein kinases. our findings suggest that stathmin phosphorylation in reh6 cells could be in part mediated by pkc activation.
SIGNOR-50598
O60216
P11308
1
relocalization
down-regulates activity
0.2
Large-scale AML genome re-sequencing efforts have identified novel recurrently mutated genes, including the members of the cohesin complex (RAD21, SMC3, SMC1A, and STAG2), implicated in the pathogenesis of this disease.Using ATAC-seq, we determined that mutant cohesin lead to a state of elevated chromatin accessibility...
SIGNOR-261515
P68400
Q99808
1
phosphorylation
up-regulates activity
0.2
These data suggest that inhibition of CK2-mediated phosphorylation at Ser254 had the same effect on transporter function as the actual loss of Ser254 in mENT1a, implying that this site is constitutively phosphorylated by CK2. 
SIGNOR-276063
P36897
Q96JC1
1
binding
up-regulates activity
0.2
TLP interacts with TGF-β and activin receptors in vivo. Endogenous TLP associates with both active and kinase-deficient TGF-beta and activin type II receptors, but interacts with the common-mediator Smad4 only in the presence of TGF-beta/activin signaling.
SIGNOR-261375
P09619
P34947
1
phosphorylation
up-regulates activity
0.2
Purified GRK5 was tyrosine-phosphorylated by the wild-type PDGFRbeta to a stoichiometry of 0.8 mol phosphate/mol GRK5, an extent approximately 5 times greater than observed with a Y857F PDGFRbeta mutant that fails to phosphorylate exogenous substrates but autophosphorylates and activates Src normally.|We conclude that ...
SIGNOR-279642
Q96PU5
Q9C0H2
1
polyubiquitination
down-regulates quantity by destabilization
0.2
Our data indicate that Nedd4-2 binds to two family members, TTYH2 and TTYH3, which contain consensus PY ((L/P)PXY) binding sites for HECT type E3 ubiquitin ligases, but not to TTYH1, which lacks this motif. Consistently, Nedd4-2 ubiquitinates both TTYH2 and TTYH3. Importantly, we have shown that endogenous TTYH2 and Ne...
SIGNOR-272633
Q8NFZ3
P78352
1
relocalization
up-regulates activity
0.2
Like NRXNs, NLGNs bind to intracellular PDZ-domain proteins, but in contrast to NRXNs, NLGNs bind to class I PDZ domains such as those contained in PSD95, a postsynaptic MAGUK protein65. PSD95 and its homologues are centrally involved in recruiting glutamate receptors at postsynaptic sites66. Similarly to CASK, PSD95 b...
SIGNOR-264190
Q13131
P60891
1
phosphorylation
down-regulates activity
0.2
We demonstrate here that glucose deprivation or hypoxia results in the AMPK-mediated phosphorylation of phosphoribosyl pyrophosphate synthetase 1 (PRPS1) S180 and PRPS2 S183, leading to conversion of PRPS hexamers to monomers and thereby inhibiting PRPS1/2 activity, nucleotide synthesis, and nicotinamide adenine dinucl...
SIGNOR-265729
O00410
Q8TD84
1
relocalization
up-regulates activity
0.2
DSCAM and DSCAML1 specifically interacted with the importin beta IPO5, whereas deletion of the identified NLSs abolished this specific interaction and suppressed nuclear translocation of the DSCAM/L1 ICDs in cell lines and cultured neurons. This suggests a direct role of IPO5 in the nuclear import of the DSCAM/L1 ICDs.
SIGNOR-264274
P0C6X7-PRO_0000037312
O75348
1
cleavage
down-regulates activity
0.2
Cleavage of the V-ATPase G1 fusion protein by SARS-CoV 3CLpro was found in this study (Fig. 3), implying that 3CLpro potentially cleaves the cellular V-ATPase G1, and affects the function of vacuolar H(+)-ATPase. Meanwhile, a significant intracellular acidification has been demonstrated in the 3CLpro-expressing cells (...
SIGNOR-260264
P32121
Q92835
1
binding
up-regulates activity
0.2
We identified a new adaptor beta-arrestin 2 that associates with phosphorylated TIGIT and mediates recruitment of inositol phosphatase SHIP1 through the ITT-like motif (Fig. 7). Finally, SHIP1 impairs TRAF6 autoubiquitination to abolish NF-kappaB activation, leading to inhibition of IFN- gamma production in NK cells.
SIGNOR-261428
Q86YJ5
P15151
1
ubiquitination
down-regulates quantity by destabilization
0.2
MARCH9, a member of the RING-CH family of transmembrane E3 ubiquitin ligases, down-regulates CD4, major histocompatibility complex-I (MHC), and ICAM-1 in lymphoid cells. To identify novel MARCH9 substrates, we used high throughput flow cytometry and quantitative mass spectrometry by stable isotope labeling by amino aci...
SIGNOR-271530
Q96G91
P63096
1
binding
up-regulates activity
0.2
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-257060
Q96RU2
P12830
1
deubiquitination
up-regulates quantity by stabilization
0.2
Usp28 deubiquitylates and consequently stabilizes Claspin in response to DNA damage
SIGNOR-274057
P17612
Q9GZU1
1
phosphorylation
down-regulates
0.2
The stimulatory effect of h89 on mcoln1 function was not observed when ser(557) and ser(559) were mutated to alanine residues, indicating that these two residues are essential for pka-mediated negative regulation of mcoln1.
SIGNOR-158946
P68400
Q06265
1
phosphorylation
up-regulates
0.2
Indeed recombinant pmscl1 undergoes ck2-mediated phosphorylation in vitro at various serine residues, including serines 409 and 411, which reside within the phosphosim region. the exchange of hydrophobic core residues or serines 409 and 411 to alanine attenuates binding of sumo to the phosphosim-containing fragment of ...
SIGNOR-184031
Q8IWT3
Q9BQL6
1
ubiquitination
down-regulates quantity by destabilization
0.2
M-phase-specific CDK1–cyclin B1 complex directly binds KIND1 and KIND2 and phosphorylates a conserved proline-directed CDK1 consensus motif in the flexible and intrinsically disordered loop of the F1 domain. This then results in the recruitment of the CUL9–FBXL10 complex, modification with K48-linked polyubiquitin chai...
SIGNOR-276718
Q9Y6X9
Q9H0A0
1
binding
up-regulates activity
0.2
MORC2 directly interacts with PARP1. MORC2 mediates the interaction between PARP1 and NAT10 and thereby promotes NAT10-mediated PARP1 acetylation at K949, which blocks CHFR-mediated ubiquitination and degradation of PARP1.
SIGNOR-273716
P04201
P21333
1
binding
up-regulates activity
0.2
We further determined that GPCRs, AT1R, and MAS directly recruited FLNa and promoted its phosphorylation by cellular S/T kinases in an agonist-dependent manner. Our studies thus provide a structural framework for filamin in GPCR signaling, potentially regulating a variety of cellular responses. MAS likely binds filamin...
SIGNOR-260627
Q8TD08
Q8TD08
2
phosphorylation
up-regulates
0.2
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.Our results suggest that the activity of erk8 in transfected hek-293 cells depends on the relative rates of erk8 autophosphorylation
SIGNOR-142969
Q14934
Q9Y625
1
transcriptional regulation
up-regulates quantity by expression
0.2
NFAT transcriptionally regulates GPC6 induction in breast cancer cells and binds to three regulatory elements in the GPC6 proximal promoter. Expression of GPC6 in response to NFAT signalling promotes invasive migration, whereas GPC6 silencing with shRNA (small-hairpin RNA) potently blocks this phenotype.
SIGNOR-264023
O15393
P14210
1
transcriptional regulation
up-regulates quantity by expression
0.2
we identified pro-hepatocyte growth factor (HGF) as a TMPRSS2 substrate and confirmed that HGF and it’s cognate receptor c-Met are activated in prostate cancers expressing TMPRSS2, a finding that also associated with the acquisition of a pro-invasive mesenchymal gene expression program.
SIGNOR-263657
Q05513
O43315
1
phosphorylation
up-regulates
0.2
Wt-pkc_-mediated phosphorylation of wt aqp9 in vitro. In the experiments, substitution of ser11 to ala markedly inhibited phosphorylation. the s11a mutation in fibroblasts caused a smoother cell periphery with fewer aqp9-induced filopodia
SIGNOR-176278
O15297
P16104
1
dephosphorylation
down-regulates
0.2
Wild-type p53-induced phosphatase 1 dephosphorylates histone variant gamma-h2ax and suppresses dna double strand break repair. Here, we demonstrate that the wild-type p53-induced phosphatase 1 (wip1) also dephosphorylates gamma-h2ax at serine 139 in vitro and in vivo.
SIGNOR-163693
Q9UPC5
P09471
1
binding
up-regulates activity
0.2
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-256967
Q15751
P62195
1
ubiquitination
down-regulates quantity
0.2
HERC1 interacts with and ubiquitinates nascent PSMC5.|PSMC5 produced in the absence of PAAF1 is presumably misfolded (consistent with its aggregation in the PURE system), triggering PSMC5 degradation by a HERC1-independent pathway.
SIGNOR-278812
Q8N4C8
Q15797
1
phosphorylation
down-regulates activity
0.2
Msn kinases directly phosphorylate α-helix 1 of Smad. we have identified Misshapen (Msn) and the mammalian orthologs TNIK, MINK1, and MAP4K4 as the kinases responsible for α-helix 1 phosphorylation. 
SIGNOR-276336
P43405
O14986
1
phosphorylation
down-regulates activity
0.2
We identified spleen tyrosine kinase (Syk), which is activated by oxidants, as a candidate PIP5Kbeta kinase in this pathway, and mapped the oxidant-sensitive tyrosine phosphorylation site to residue 105. The PIP5KbetaY105E phosphomimetic is catalytically inactive and cytosolic, whereas the Y105F non-phosphorylatable mu...
SIGNOR-276227
P00519
Q04760
1
phosphorylation
up-regulates activity
0.2
We show that Glo1 activity is promoted by phosphorylation on Tyrosine 136 via multiple kinases. Glo1 Y136 is phosphorylated by multiple different kinases including all members of the Src family. Depletion of multiple different kinases led to a partial reduction in Glo1(Y136) phosphorylation. These included members of t...
SIGNOR-276187
P42684
P42684
2
phosphorylation
up-regulates quantity by stabilization
0.2
The results show that Arg is stabilized in response to 0.1 mM H2O2 by autophosphorylation of Y-261, consistent with involvement of the Arg kinase function in regulating Arg levels. The results further demonstrate that c-Abl-mediated phosphorylation of Arg on Y-261 similarly confers Arg stabilization.. These findings in...
SIGNOR-276033
P51608
P18031
1
transcriptional regulation
down-regulates quantity by repression
0.2
In this study, we have demonstrated that the PTPN1 gene, which encodes PTP1B, was a direct target of MECP2 and that PTP1B protein levels were dramatically increased in Mecp2-mutant mice and in fibroblasts derived from patients with RTT.
SIGNOR-264546
P17612
O75899
1
phosphorylation
down-regulates activity
0.2
Here we show that the functional coupling of GABA(B)R1/GABA(B)R2 receptors to inwardly rectifying K(+) channels rapidly desensitizes. This effect is alleviated after direct phosphorylation of a single serine residue (Ser892) in the cytoplasmic tail of GABA(B)R2 by cyclic AMP (cAMP)-dependent protein kinase (PKA).
SIGNOR-263150
Q9Y2H1
Q9Y2H1
2
phosphorylation
up-regulates
0.2
Ndr1/ndr2 protein kinase is activated by phosphorylation on the activation loop phosphorylation site ser281/ser282 and the hydrophobic motif phosphorylation site thr444/thr442. Autophosphorylation of ndr is responsible for phosphorylation on ser281/ser282, whereas thr444/thr442 is targeted by an upstream kinase. Here w...
SIGNOR-142518
P48730
P43629
1
phosphorylation
up-regulates
0.2
In this study, we have mapped constitutive phosphorylation sites for casein kinases, protein kinase c, and an unidentified kinase on the kir cytoplasmic domain. Three of these phosphorylation sites are highly conserved in human inhibitory kir. Functional studies of the wild-type receptor and serine/threonine mutants in...
SIGNOR-158125
Q9BXC1
P38405
1
binding
up-regulates activity
0.2
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-256900
P53779
P54259
1
phosphorylation
down-regulates activity
0.2
Dentatorubral-pallidoluysian atrophy protein is phosphorylated by c-jun nh2-terminal kinase. serine 734 of the drpla protein is a phospho-acceptor site by jnk. The phosphorylation may be coupled to the activation of a protease. The molecular size of drpla protein detected in the rat brain with the specific phosphopepti...
SIGNOR-102394
Q9Y463
Q9Y463
2
phosphorylation
up-regulates
0.2
Mirk kinase is activated by autophosphorylation on tyrosine at the y271/y273 site
SIGNOR-79810
P43146
O00555
1
null
up-regulates activity
0.2
DCC activation by a netrin-1 gradient creates a high-level [Ca2+]i gradient by triggering LCC activity and by stimulating the cAMP–PKA pathway, which further activates LCC in the plasma membrane (PM) and Ca2+ channels in the ER.
SIGNOR-268293
Q86UY5
P49674
1
binding
up-regulates quantity
0.2
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or req...
SIGNOR-273761
P30153
P10636
1
dephosphorylation
down-regulates
0.2
Galpha12 directly interacts with pp2a: evidence for galpha12-stimulated pp2a phosphatase activity and dephosphorylation of microtubule-associated protein, tau.
SIGNOR-130136
Q13043
P42336
1
phosphorylation
down-regulates activity
0.2
MST1/2 and HGK inhibit catalytic activity of p110α through phosphorylation at T1061 
SIGNOR-277920
O43791
Q27J81
1
binding
down-regulates activity
0.2
SPOP acts as an adaptor protein of the CUL3-RBX1 E3 ubiquitin ligase complex that generally recruits substrates for ubiquitination and subsequent degradation. Here, we revealed that SPOP recognizes a Ser/Thr (S/T)-rich motif in the C-terminal region of INF2 and triggers atypical polyubiquitination of INF2. These ubiqui...
SIGNOR-272798
P42345
O95163
1
phosphorylation
up-regulates activity
0.2
Human ELP1 S1174 phosphorylation was triggered by insulin treatment, as shown by the specific phosphorylated (p)ELP1 (S1174) antibody, and addition of a phosphorylation-mutant variant of the ELP1 protein (ELP1(S1174A)) to ELP1-depleted BRAFV600E melanoma cells failed to rescue cell survival |In line with these findings...
SIGNOR-275541
Q99986
P16104
1
phosphorylation
up-regulates activity
0.2
In response to DNA damage induced by ionizing radiation, histone H2AX is phosphorylated in Ser139 by VRK1.
SIGNOR-278370
O15552
Q03113
1
binding
up-regulates activity
0.2
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-257342
Q92831
P84243
1
acetylation
down-regulates activity
0.2
The HAT module within the SAGA and ADA complexes acetylates histone H3, mainly on residues K9 and K14.
SIGNOR-269620
P04629
P04629
2
phosphorylation
up-regulates
0.2
In vitro studies indicate that trka autophosphorylates at tyrosines 490, 670, 674, 675, and 785
SIGNOR-47171
Q8IZL9
Q9UPZ9
1
phosphorylation
up-regulates
0.2
Recombinant cak1p phosphorylates thr-157 in the tdy motif of recombinant ick and activates its activity in vitro.
SIGNOR-138420
O43638
P48023
1
transcriptional regulation
down-regulates quantity by repression
0.2
As we expected, Fkhl18 suppressed, dose-dependently,human and mouseFasLpromoter in bovine vascularsmooth muscle cells
SIGNOR-261612
Q99683
O14548
1
phosphorylation
up-regulates activity
0.2
Phosphorylation of EB1 by ASK1 promotes the binding of EB1 to CLIP-170 and p150 glued.
SIGNOR-278341
P31751
P55265
1
phosphorylation
down-regulates activity
0.2
AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Coimmunoprecipitation studies and in vitro kinase assays revealed that AKT-1, -2, and -3 interact with both ADAR1p110 and ADAR2 and phosphorylate these RNA editases. Using site-directed mutagenesis of suspected AKT phos...
SIGNOR-276192
P19525
Q9H3R0
1
phosphorylation
down-regulates quantity by destabilization
0.2
In the absence of Wnt3a, protein kinase R phosphorylated KDM4C at Ser918, inducing KDM4C ubiquitination and degradation.
SIGNOR-277497
P49841
O00159
1
phosphorylation
up-regulates activity
0.2
Here, we report that at early G1 the glycogen synthase kinase 3\u03b2 phosphorylates and stabilizes Nuclear myosin 1c, allowing for Nuclear myosin 1c association with the chromatin.
SIGNOR-279184
P13674
Q01581
1
transcriptional regulation
up-regulates quantity by expression
0.2
In this study, we found that the prolyl 4-hydroxylase (P4H) subunit P4HA1 protects NPC cells from erastin-induced ferroptosis by activating HMGCS1, a key enzyme in the mevalonate pathway. Our results show that HMGCS1 and HMGCR are regulated by P4HA subunits at the transcriptional level (Fig. S4).
SIGNOR-279853
Q92520
P42702
1
binding
up-regulates activity
0.2
Interleukin-like EMT inducer (ILEI) a cytokine from the FAM3 family, also functions as a ligand for LIFR-gp130 heterodimer and mediates intracellular signal through STAT activation.
SIGNOR-277986
P16234
P16234
2
phosphorylation
up-regulates activity
0.2
We have identified two autophosphorylation sites, Tyr-988 and Tyr-1018, in the platelet-derived growth factor (PDGF) alpha-receptor carboxyl-terminal tail, which are involved in binding of phospholipase C-gamma (PLC-gamma). We conclude that phosphorylated Tyr-988 and Tyr-1018 in the PDGF α-receptor carboxyl-terminal t...
SIGNOR-250252
Q04759
P15407
1
phosphorylation
up-regulates activity
0.2
PKCθ-induced phosphorylations, in part at T217 and T227 residues, strongly and specifically increased Fra-1 transcriptional activity through the stimulation of Fra-1 transactivation domain, without affecting JUN factors.
SIGNOR-260879
Q96QT6
Q04724
1
binding
up-regulates activity
0.2
We have cloned and characterized a new member of the PHD zinc finger family called Pf1 that interacts with two global transcription corepressors: mSin3A and TLE. Pf1 interacts with TLE. The Groucho/TLE proteins are members of an abundant corepressor family, and we hypothesized that Pf1 might interact with TLE family m...
SIGNOR-266994
Q9NR19
Q14457
1
transcriptional regulation
up-regulates quantity by expression
0.2
As expected, we found that glucose deprivation induced the binding of TFEB (Figure S4C) and ACSS2 (Figure S4D) to the promoter regions of MAP1LC3B, ATG3, and WIPI-1 as well as mRNA (Figure 3H) and protein (Figure 3I) expression of these genes;
SIGNOR-276561
P55286
Q14653
1
transcriptional regulation
up-regulates quantity
0.2
CHD8 binds to histone H3 di- and trimethylated on lysine 4. It resides on the human U6 promoter as well as the mRNA IRF3 promoter in vivo and contributes to efficient transcription from both these promoters
SIGNOR-266898
P47710
Q04206
1
phosphorylation
up-regulates
0.2
Phosphorylation of serine 529 of p65 is mediated by casein kinase ii, but is prevented in nonstimulated cells by the interaction with ikba
SIGNOR-171222
P49840
Q07869
1
phosphorylation
up-regulates activity
0.2
GSK-3alpha phosphorylates PPARalpha at Ser280, located in the ligand binding domain.|These results suggest that GSK-3alpha positively regulates PPARalpha activity through Ser280 phosphorylation.
SIGNOR-278515
P51812
O60825
1
phosphorylation
up-regulates activity
0.2
Heart 6-phosphofructo-2-kinase activation by insulin results from ser-466 and ser-483 phosphorylation and requires 3-phosphoinositide-dependent kinase-1, but not protein kinase b.
SIGNOR-23753
P30411
Q14344
1
binding
up-regulates activity
0.2
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-257399
Q9C0A6
P68431
1
methylation
up-regulates activity
0.2
SETD5 Exhibits Intrinsic Methyltransferase Activity on H3K36. This assay showed that SETD5 has specific histone methyltransferase activity toward K36 but not for other residues such as K4 and K27 (Figure 8B). we revealed that SETD5 is endowed with H3K36 methyltransferase, which is necessary for RNA elongation and proce...
SIGNOR-264620
Q86UY5
P48729
1
binding
up-regulates quantity
0.2
We identified members of the FAM83 family of proteins as partners of CK1 in cells. All eight members of the FAM83 family (FAM83A–H) interacted with the α and α-like isoforms of CK1; FAM83A, -B, -E, and -H also interacted with the δ and ε isoforms of CK1. The intrinsic catalytic activity of CK1 is not affected by or req...
SIGNOR-273748
P27361
Q8NET8
1
phosphorylation
up-regulates activity
0.2
We observed that ERK-mediated phosphorylation of TRPV3 alters its responsiveness to repeated chemical stimuli. Among several putative ERK phosphorylation sites, we identified threonine 264 in the N-terminal ankyrin repeat domain as the most critical site for the ERK-dependent modulation of TRPV3 channel activity. Of no...
SIGNOR-273672
P55085
P63096
1
binding
up-regulates activity
0.2
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-256895
P68400
P49321
1
phosphorylation
down-regulates activity
0.2
Here, we show that somatic nuclear autoantigenic sperm protein (sNASP) binds to TRAF6 to prevent TRAF6 autoubiquitination in unstimulated macrophages. Following LPS stimulation, a complex consisting of sNASP, TRAF6, IRAK4, and casein kinase 2 (CK2) is formed. CK2 phosphorylates sNASP at serine 158, allowing sNASP to di...
SIGNOR-273627
Q9UEW8
O95863
1
phosphorylation
up-regulates activity
0.2
In this study, we found that STK39 also enhances SNAI1 stability by its phosphorylation at T203.|STK39 interacts with SNAI1 and phosphorylates SNAI1 on T203.
SIGNOR-279128
Q14004
Q86VE9
1
phosphorylation
down-regulates quantity by destabilization
0.2
In addition, CDK13-KD disrupted Nef downregulation of SERINC5 from the cell surface, whereas CDK12-KD did not (Figures 2D and 2E).|Thus, S360 phosphorylation increases interactions between Nef and SERINC5 and initiates the destruction of SERINC5 by the endocytic machinery.|Thus, we conclude that CycK/CDK13 phosphorylat...
SIGNOR-278918
Q9UIK4
Q9UIK4
2
phosphorylation
down-regulates activity
0.2
Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding. | It comprises a single autophosphorylation event mapped to Ser308 within the CaM regulatory domain.
SIGNOR-251084