IdA string | IdB string | labels int64 | mechanism string | effect string | score float64 | sentence string | signor_id string |
|---|---|---|---|---|---|---|---|
P17252 | O95644 | 1 | phosphorylation | down-regulates activity | 0.384 | Protein kinase A negatively modulates the nuclear accumulation of NF-ATc1. | Here we show that overexpression of PKA causes phosphorylation and cytoplasmic accumulation of NF-ATc1 in direct opposition to calcineurin by phosphorylating Ser-245, Ser-269, and Ser-294 in the conserved serine-proline repeat domain, and that mutation of these serines blocks the effect of PKA. Activation of endogenous PKA is similarly able to promote phosphorylation of these sites on NF-ATc1 in two lymphoid cell lines. | SIGNOR-249175 |
Q05397 | Q14247 | 1 | phosphorylation | down-regulates activity | 0.745 | FAK directly phosphorylates cortactin at Y421 and Y466 and over-expression of cortactin Y421, Y466, and Y482 mutated to phenylalanine (3YF) prevented FAK-enhanced FA turnover and cell motility.|GFP-FAK re-expression in FAK-/- MEFs enhances FA turnover (XREF_FIG) and cortactin knockdown slows FA turnover (XREF_FIG). | SIGNOR-278283 |
O15409 | Q8WXX7 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.325 | By interacting with CASK, TBR1 regulates several ASD candidate genes, such as GRIN2B, AUTS2 and RELN—all of which are recurrently mutated in ASD. In areas of the brain with overlapping expression patterns, such as in glutamatergic layer 6 neurons, the TBR1–FOXP2 interaction may result in co-ordinated regulation of common downstream targets. | SIGNOR-266832 |
Q63ZE4 | P20823 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.2 | Luciferase reporter gene constructs containing the OAT5 (SLC22A10) and OAT7 (SLC22A9) promoter regions were transactivated by HNF-1 in HepG2 cells. | SIGNOR-268983 |
P12931 | P11413 | 1 | phosphorylation | up-regulates activity | 0.274 | Here, we show that tyrosine kinase c-Src interacts with and phosphorylates G6PD at Tyr 112. This phosphorylation enhances catalytic activity of G6PD by dramatically decreasing its Km value and increasing its Kcat value for substrate glucose-6-phosphate. | SIGNOR-277550 |
O95786 | P62136 | 0 | dephosphorylation | up-regulates activity | 0.2 | We identified PP1alpha and PP1gamma as primary phosphatases responsible for MDA5 and RIG-I dephosphorylation, leading to their activation.|endogenous RIG-I and MDA5 that interacted with PP1 exhibited markedly decreased phosphorylation levels at S8 and S88, respectively | SIGNOR-264581 |
Q9HCP0 | O75581 | 1 | phosphorylation | up-regulates | 0.545 | Ck1gamma is associated with lrp6, which has multiple, modular ck1 phosphorylation sites. Wnt treatment induces the rapid ck1gamma-mediated phosphorylation of these sites within lrp6 | SIGNOR-143029 |
P29350 | Q14289 | 1 | dephosphorylation | down-regulates | 0.359 | Raftk binds constitutively to the protein tyrosine phosphatase shptp1.SHPTP1 Plays a negative role in pyk2/raftk signaling by dephosphorylating raftk on tyr-402, thereby inhibiting the interaction of the sh2 domain of c-src with raftk | SIGNOR-71414 |
O75030 | P49841 | 0 | phosphorylation | up-regulates quantity by stabilization | 0.435 | We also show that the MITF protein was stabilized by Wnt signaling, through the novel C-terminal GSK3 phosphorylations identified here. | SIGNOR-276476 |
P24588 | Q9UIJ5 | 0 | palmitoylation | up-regulates activity | 0.331 | Here, we report that the recycling endosome-resident palmitoyl acyltransferase DHHC2 interacts with and palmitoylates AKAP79/150 to regulate these plasticity signaling mechanisms | SIGNOR-261289 |
P06493 | Q01196 | 1 | phosphorylation | up-regulates | 0.341 | Phosphorylation of runx1 on ser-303 by cdks leads its ubiquitin-mediated degradation during g2/m (19). We developed additional evidence that cdks phosphorylate ser-303 and found that ser-48 and ser-424 are also substrates of cdk1/cyclin b and cdk6/cyclin d3. Moreover, we demonstrated that phosphorylation of ser-48, ser-303, and ser-424 strengthens the ability of runx1 to activate transcription and to stimulate proliferation of the ba/f3 hematopoietic cell line (20). | SIGNOR-169322 |
Q15154 | Q12798 | 1 | relocalization | up-regulates | 0.406 | Rna silencing of pcm-1 leads to reduced assembly of centrin, pericentrin, and ninein at the centrosome | SIGNOR-94947 |
P51813 | P56945 | 1 | phosphorylation | up-regulates quantity | 0.506 | Recombinant Bmx kinase was found to effectively phosphorylate the wt CAS SH3 domain on Tyr-12 (Figure 2B). A novel phosphorylation site on CAS, Tyr-12 (Y12) within the ligand-binding hydrophobic pocket of the CAS SH3 domain, was identified and found to be enriched in Src-transformed cells and invasive human carcinoma cells. | SIGNOR-276384 |
P31749 | Q96GX5 | 1 | phosphorylation | up-regulates activity | 0.2 | Here, we report that AKT phosphorylates MASTL at residue T299, which plays a critical role in its activation. | SIGNOR-277515 |
P15559 | Q9Y4A8 | 0 | transcriptional regulation | down-regulates quantity by repression | 0.338 | Deletion mutation analysis revealed that Nrf3 repression of NQO1 gene expression required heterodimerization and DNA binding domains but not transcriptional activation domain of Nrf3. | SIGNOR-268976 |
P08631 | Q13444 | 1 | phosphorylation | up-regulates | 0.355 | Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling. | SIGNOR-112919 |
P55011 | Q9UEW8 | 0 | phosphorylation | up-regulates activity | 0.6 | This phosphorylation event activates PASK, which in turn phosphorylates and activates NKCC1 | SIGNOR-264642 |
Q9Y6M1 | P42345 | 0 | phosphorylation | up-regulates activity | 0.2 | IGF2BP2 can be activated by mTOR and promotes its binding to IGF2 mRNA of IGF2 thereby leading to diabetes mellitus [ xref , xref ].|In addition, phosphorylation of IGF2BP2 in the linker region between RRM2 and KH1 by mTOR promotes its binding to the IGF leader 3 mRNA 5\u2032-UTR, enhancing the initiation of IGF2 translation through eIF-4E- and 5\u2032 cap-independent internal ribosomal entry [ xref ]. | SIGNOR-280046 |
P04275 | Q76LX8 | 0 | cleavage | down-regulates activity | 0.599 | Proteolytic degradation of VWF by ADAMTS-13 downregulates the proinflammatory potential of VWF. | SIGNOR-251966 |
P62714 | Q12933 | 1 | dephosphorylation | down-regulates activity | 0.2 | We show that the Thr117 residue in TRAF2 is phosphorylated following TNFalpha stimulation. This phosphorylation process is modulated by PP2A and is required for TRAF2 functional activity. | SIGNOR-248597 |
P11912 | P06241 | 0 | phosphorylation | up-regulates activity | 0.596 | Lyn and Fyn phosphorylated the CD79a cytoplasmic portion of the fusion proteins well, with >80% of phosphorylation occurring at Y182. CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM). | SIGNOR-251153 |
P11308 | P04628 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.2 | Interestingly, our data showed that ERG drastically induced Wnt ligand gene expression. | SIGNOR-261597 |
O75592 | P46060 | 0 | relocalization | down-regulates quantity by destabilization | 0.315 | SUMOylated RanGAP1 Inhibits MYCBP2 Activity and Mediates Its Transport to the Nucleus. Surprisingly, we did not find MYCBP2-dependent ubiquitylation of SUMOylated RanGAP1 but instead a strong inhibition of the ubiquitin ligase activity of MYCBP2 in the presence of SUMOylated RanGAP1, as determined by the presence of ubiquitylated proteins. this effect was specific for SUMOylated RanGAP1, because the unmodified form of RanGAP1 did not affect MYCBP2-dependent protein ubiquitylation. , SUMOylated RanGAP1 inhibited the ubiquitin ligase activity of MYCBP2, and it is tempting to speculate that SUMOylated RanGAP1 inhibits the ubiquitin ligase activity of MYCBP2 to ensure MYCBP2 silencing during its transport to the nucleus | SIGNOR-261203 |
P01106 | P17480 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.356 | MAD1 and c-MYC regulate UBF and rDNA transcription during granulocyte differentiation|MAD1 repressed and c-MYC activated rDNA transcription in nuclear run-on assays. Repression of rDNA transcription by MAD1 was associated with its ability to interact directly with the promoter of upstream binding factor (UBF), an rDNA regulatory factor. Conversely, c-MYC activated transcription from the UBF promoter. | SIGNOR-269644 |
O15234 | O95271 | 0 | ADP-ribosylation | down-regulates quantity by destabilization | 0.2 | Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling. RNF146 promotes Wnt signalling by mediating tankyrase-dependent degradation of axin. Mechanistically, RNF146 directly interacts with poly(ADP-ribose) through its WWE domain, and promotes degradation of PARsylated proteins. Using proteomics approaches, we have identified BLZF1 and CASC3 as further substrates targeted by tankyrase and RNF146 for degradation. | SIGNOR-263383 |
Q9H4B4 | Q16143 | 1 | phosphorylation | down-regulates activity | 0.38 | Polo-like kinase (plk) family (plk1, plk2, and plk3) phosphorylate alpha-syn and beta-syn specifically at ser-129 and ser-118, respectively. Polo-like kinase 2 (plk2) phosphorylates alpha-synuclein at serine 129 in central nervous system. The membrane association of pd-linked mutant alpha -synuclein, but not wild-type -synuclein, was increased by serine 129 phosphorylation. | SIGNOR-189057 |
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, mTORC2 activity, but not mTORC1, was required for the insulin-induced phosphorylation of Elp1 S1174 | SIGNOR-275541 |
P19021 | P01178-PRO_0000020495 | 1 | cleavage | up-regulates activity | 0.2 | Nevertheless, overall the results of this study show that peptide sequence recognition is an important aspect of the interactions of the prohormone substrates prooxytocin (3d) and procalcitonin (7e) with PAM, which is mirrored in the potency of analogous peptidomimetic glycolate inhibitors of the enzyme. | SIGNOR-268551 |
O15297 | Q13315 | 1 | dephosphorylation | down-regulates | 0.488 | The negative regulator wip1 plays an important role in inhibiting atm, resulting in a pulse of atm activity. | SIGNOR-185135 |
P00533 | Q16539 | 0 | phosphorylation | down-regulates | 0.508 | In conclusion, the use of pharmacological agents suggests that p38 mapk is the enzyme involved in egfr phosphorylation, as well as internalization, following exposure of cells to various stress-inducing conditions. | SIGNOR-149089 |
P04049 | O75914 | 0 | phosphorylation | up-regulates | 0.556 | The protein kinase pak3 positively regulates raf-1 activity through phosphorylation of serine 338. | SIGNOR-62043 |
Q5VWQ8 | P01112 | 1 | gtpase-activating protein | down-regulates activity | 0.6 | The GAP domain of DAB2IP is homologous to other Ras-GAPs, such as GAP120 and neurofibromin (NF1), and can stimulate the GTPase activity of RAS proteins both in vitro and in cancer cell lines. DAB2IP is able to stimulate in vitro and in vivo the GTPase activity of RAS proteins (H-Ras, K-Ras, and N-Ras) facilitating GTP hydrolysis to GDP. | SIGNOR-254745 |
Q8TEU7 | P01112 | 1 | guanine nucleotide exchange factor | up-regulates | 0.336 | Gefs catalyse the transition from gdp-bound, inactive ras to gtp-bound, active ras. | SIGNOR-183796 |
P17252 | P08670 | 1 | phosphorylation | down-regulates quantity by destabilization | 0.284 | We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. | SIGNOR-248880 |
Q02779 | P15923 | 1 | phosphorylation | down-regulates | 0.2 | Mlk2 inhibits e47 transactivation activity on the trkb promote | SIGNOR-161544 |
Q7Z6Z7 | Q13105 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.327 | Previously, we reported that K48 linked polyubiquitination of Miz1 by Mule triggers its proteasomal degradation, thereby relieving Miz1 suppression on TNF induced JNK activation and apoptosis. | SIGNOR-278697 |
P45983 | P17535 | 1 | phosphorylation | up-regulates | 0.796 | Menin binds the jun family transcription factor jund and inhibits its transcriptional activity. The menin-jund interaction blocks jun n-terminal kinase (jnk)-mediated jund phosphorylation and suppresses jund-induced transcription. We found a role for phosphorylation of the ser100 residue of jund;jund phosphorylation were prevented by inhibitors of calcium, calmodulin, or erk1/2 kinase. | SIGNOR-196038 |
Q9H2G2 | P04637 | 1 | phosphorylation | up-regulates activity | 0.256 | The Ste20 like kinase SLK promotes p53 transactivation and apoptosis.|Thus SLK induces p53 phosphorylation and transactivation, which enhances apoptosis after in vitro ischemia-reperfusion injury. | SIGNOR-279285 |
P09622 | Q9Y572 | 0 | phosphorylation | up-regulates activity | 0.2 | Here, we show that RIP3 activates the pyruvate dehydrogenase complex (PDC, also known as PDH), the rate-limiting enzyme linking glycolysis to aerobic respiration, by directly phosphorylating the PDC E3 subunit (PDC-E3) on T135. | SIGNOR-266372 |
P10275 | P16591 | 0 | phosphorylation | up-regulates | 0.259 | Fer is required for il-6 mediated ar activation by phosphorylating ar tyrosine 223 and binding via its sh2 domain. | SIGNOR-194749 |
P67775 | Q9BXL7 | 1 | dephosphorylation | down-regulates activity | 0.309 | NF-kappaB activation is triggered by PKCtheta-dependent phosphorylation of Carma1 after TCR/CD28 co-stimulation. PKCtheta-phosphorylated Carma1 was suggested to function as a molecular scaffold that recruits preassembled Bcl10-Malt1 complexes to the membrane|we demonstrate that PP2A removes PKCtheta-dependent phosphorylation of Ser645 in Carma1, and show that maintenance of this phosphorylation is correlated with increased T-cell activation. | SIGNOR-248650 |
P25440 | P62805 | 0 | relocalization | up-regulates activity | 0.2 | Thus, the TIP60 HAT complex is recruited to MYC-target genes and, probably with other other HATs, contributes to histone acetylation in response to mitogenic signals. | SIGNOR-262062 |
O95155 | P54252 | 1 | polyubiquitination | down-regulates quantity by destabilization | 0.578 | Mammalian E4B (UFD2a), a ubiquitin chain assembly factor (E4), copurified with the polyubiquitylation activity for ataxin-3. E4B interacted with, and thereby mediated polyubiquitylation of, ataxin-3. Collectively, these data suggest that E4B promotes the degradation of ataxin-3, and that this effect surmounts the stabilization of ataxin-3 conferred by expansion of the polyglutamine tract. | SIGNOR-271502 |
P36873 | P50750 | 1 | dephosphorylation | up-regulates | 0.2 | Pp1 is an activator of cdk9. Pp1 dephosphorylates cdk9 thr186. | SIGNOR-173454 |
Q13363 | P45983 | 0 | phosphorylation | down-regulates | 0.358 | In this study, we found that c-jun nh2-terminal kinase 1 activation triggered ctbp phosphorylation on ser-422 and subsequent degradation, | SIGNOR-149721 |
Q13309 | P01106 | 1 | ubiquitination | down-regulates quantity | 0.736 | The F-box protein Skp2 mediates c-Myc ubiquitylation by binding to the MB2 domain | SIGNOR-243548 |
P18887 | P68400 | 0 | phosphorylation | up-regulates | 0.395 | Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair | SIGNOR-165419 |
P04637 | O14920 | 0 | phosphorylation | up-regulates activity | 0.52 | Here , we show that IKKbeta modulates the activity of p53 in response to glutamine depletion to promote cancer cell adaptation .|Taken together, these results indicate that IKK\u03b2 phosphorylates p53 on Ser392 as an early response to glutamine deprivation and possibly later facilitates its phosphorylation at Ser15 and transcriptional activity. | SIGNOR-278516 |
Q86X55 | P23759 | 1 | methylation | up-regulates | 0.421 | Carm1 specifically methylates Pax7 at multiple arginine residues in the N terminus of Pax7 | SIGNOR-255898 |
Q13315 | Q8N0Z6 | 1 | phosphorylation | up-regulates activity | 0.538 | Here we report a new pathway in which ATM kinase signals the DNA damage response by targeting the transcriptional cofactor Strap. ATM phosphorylates Strap at a serine residue, stabilizing nuclear Strap and facilitating formation of a stress-responsive co-activator complex. | SIGNOR-262645 |
Q13315 | Q9HAU4 | 1 | phosphorylation | up-regulates activity | 0.2 | Using biochemical approaches and MS analysis, we show that upon the onset of the DNA-damage response, SMURF2 becomes phosphorylated at Ser384 by ataxia telangiectasia mutated (ATM) serine/threonine kinase, and this phosphorylation is required for its interaction with RNF20. | SIGNOR-277534 |
Q9Y2T7 | P31751 | 0 | phosphorylation | up-regulates quantity by stabilization | 0.2 | In this context, YBX2 is a dual substrate for both AMPK and Akt2. The phosphorylation at Thr115 by AMPK or at Ser137 by Akt2 facilitates YBX2 accumulation in brown adipocytes by decreasing ubiquitination-mediated degradation. | SIGNOR-277869 |
O75717 | Q13535 | 0 | phosphorylation | up-regulates activity | 0.539 | And-1 is phosphorylated at T826 by ATR following replication stress, and this phosphorylation is required for And-1 to accumulate at the damage sites, where And-1 promotes the interaction between Claspin and Chk1, thereby stimulating efficient Chk1 activation by ATR. | SIGNOR-262664 |
P27361 | Q15672 | 1 | phosphorylation | up-regulates | 0.328 | Phosphorylation of serine 68 of twist1 by mapks stabilizes twist1 protein and promotes breast cancer cell invasiveness. this ser 68 is phosphorylated by p38, c-jun n-terminal kinases (jnk), and extracellular signal-regulated kinases1/2 in vitro | SIGNOR-173413 |
P55211 | Q9Y243 | 0 | phosphorylation | down-regulates | 0.518 | Akt phosphorylated recombinant casp9 in vitro on serine-196 and inhibited its protease activity | SIGNOR-61565 |
Q53EL6 | P31749 | 0 | phosphorylation | down-regulates | 0.435 | Both akt and p70(s6k) phosphorylate pdcd4, allowing for binding of the e3-ubiquitin ligase beta-trcp and consequently ubiquitylation. | SIGNOR-252505 |
P31749 | P15056 | 1 | phosphorylation | down-regulates activity | 0.458 | Akt phosphorylates both S364 and S428. Akt downregulates B-Raf activity in vivo | SIGNOR-251472 |
Q13315 | P55957 | 1 | phosphorylation | down-regulates activity | 0.463 | Taken together, these results are consistent with the idea that at low levels of DNA damage ATM phosphorylates Bid to keep it away from the mitochondria resulting in low levels of ROS.|Thus, Bid accumulation at the mitochondria, which is negatively regulated by ATM, triggers a metabolic change in mitochondria that includes an increase in ROS and perhaps changes in other metabolites that signal back to the nucleus to regulate gene transcription leading to cell cycle progression (XREF_FIG). | SIGNOR-279790 |
Q15796 | Q13705 | 0 | phosphorylation | up-regulates activity | 0.776 | It has been suggested that binding of myostatin to the ActRIIB results in the phosphorylation of two serine residues of Smad2 or Smad3 at COOH domains | SIGNOR-254984 |
Q9UJW0 | Q01484 | 0 | relocalization | up-regulates quantity | 0.625 | We present evidence for an ankyrin-based mechanism for sarcolemmal localization of dystrophin and beta-DG. Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4. | SIGNOR-266713 |
Q13315 | Q96SD1 | 1 | phosphorylation | up-regulates | 0.619 | The artemis nuclease is defective in radiosensitive severe combined immunodeficiency patients and is required for the repair of a subset of ionising radiation induced dna double-strand breaks (dsbs) in an atm and dna-pk dependent process. Here, we show that artemis phosphorylation by atm and dna-pk in vitro is primarily attributable to s503, s516 and s645 and demonstrate atm dependent phosphorylation at serine 645 in vivo | SIGNOR-148315 |
O60315 | P50222 | 1 | transcriptional regulation | down-regulates quantity by repression | 0.318 | ZEB2 represses GAX transcription through multiple up- stream consensus binding sites. | SIGNOR-268951 |
P28482 | P17676 | 1 | phosphorylation | up-regulates | 0.716 | Phosphorylation of cebpb at thr(235) peaked at 16 hours in il-1beta-stimulated cells. The mek inhibitor u0126 inhibited this phosphorylation and reduced mmp-1 gene induction. | SIGNOR-187798 |
P31749 | Q15257 | 0 | dephosphorylation | down-regulates | 0.2 | Consistent with previous reports (2830), we found that expression of sv40st, suppression of either pp2a c or b resulted in elevated levels of akt phosphorylation (ser473) | SIGNOR-252607 |
O14920 | P42771 | 1 | phosphorylation | down-regulates | 0.396 | Ikkbeta specifically binds to p16 and phosphorylates ser8 of p16 phosphorylation at ser8 of p16 brings about a significant loss of its cyclin-dependent kinase (cdk) 4-inhibitory activity | SIGNOR-163801 |
P17947 | O15550 | 0 | transcriptional regulation | down-regulates quantity by repression | 0.252 | 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-260036 |
Q9HCE7 | Q12778 | 0 | transcriptional regulation | up-regulates quantity | 0.248 | FoxO factors are required for the transcriptional regulation of the ubiquitin ligases atrogin-1, also called muscle atrophy F-box (MAFbx) and muscle ring finger 1 (MuRF1), leading to the ubiquitylation of myosin and other muscle proteins (see below), and their degradation via the proteasome | SIGNOR-256268 |
Q96J02 | O15350 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.566 | Collectively, our present findings suggest that MDM2 promotes Itch-mediated degradation of p73 through the interaction with Itch in HeLa cells | SIGNOR-278699 |
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 |
O94986 | P24941 | 1 | relocalization | up-regulates activity | 0.278 | Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome. | SIGNOR-271724 |
P14618 | Q9P1W9 | 0 | phosphorylation | up-regulates quantity by stabilization | 0.37 | Here, we identified the protein-serine/threonine kinase PIM2, a known oncogene, as a novel binding partner of PKM2. The interaction between PIM2 and PKM2 was confirmed by multiple biochemical approaches in vitro and in cultured cells. Importantly, we found that PIM2 could directly phosphorylate PKM2 on the Thr-454 residue, resulting in an increase of PKM2 protein levels. Compared with wild type, PKM2 with the phosphorylation-defective mutation displayed a reduced effect on glycolysis | SIGNOR-267472 |
P78352 | Q02156 | 0 | phosphorylation | up-regulates quantity | 0.285 | PKCepsilon directly phosphorylated PSD-95 and JNK1 in vitro Inhibiting PKCepsilon, JNK, or calcium/calmodulin dependent kinase II activity prevented the effects of PKCepsilon activators on PSD-95 phosphorylation.|These results indicate that PKCepsilon promotes synaptogenesis by activating PSD-95 phosphorylation directly through JNK1 and calcium/calmodulin dependent kinase II and also by inducing expression of PSD-95 and synaptophysin. | SIGNOR-280087 |
P19474 | P49915 | 1 | ubiquitination | down-regulates | 0.326 | Cytoplasmic sequestration of gmps requires ubiquitylation by trim21, a ubiquitin ligase associated with autoimmune disease. | SIGNOR-204478 |
Q13315 | Q96J02 | 1 | phosphorylation | up-regulates activity | 0.264 | Here we uncover ATM as a novel positive modulator of ITCH E3-ubiquitin ligase activity. A single residue on ITCH protein, S161, which is part of an ATM SQ consensus motif, is required for ATM-dependent activation of ITCH. | SIGNOR-276488 |
O43293 | O14950 | 1 | phosphorylation | up-regulates | 0.511 | Hzipk phosphorylated the regulatory light chain of myosin ii (mrlc) at both ser19 and thr18 in vitro. Phosphorylation of mrlc is required to generate the driving force in the migration of the cells but not necessary for localization of myosin ii at the leading edge. | SIGNOR-16043 |
Q13627 | P40763 | 1 | phosphorylation | up-regulates activity | 0.265 | DYRK1A overexpression promotes STAT3 activity by phosphorylating STAT3 at Ser727 and contributes to reduced neuronal production and increased astroglial generation in DS. | SIGNOR-279992 |
P54646 | Q92574 | 1 | phosphorylation | up-regulates | 0.551 | Under energy starvation conditions, the amp-activated protein kinase (ampk) phosphorylates tsc2 and enhances its activity. | SIGNOR-119541 |
P28482 | P17480 | 1 | phosphorylation | down-regulates | 0.394 | Erk1/2 was found to phosphorylate the architectural transcription factor ubf at amino acids 117 and 201 within hmg boxes 1 and 2, preventing their interaction with dna | SIGNOR-112809 |
P67775 | P31749 | 1 | dephosphorylation | down-regulates activity | 0.893 | Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes | SIGNOR-252614 |
O75874 | Q12778 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.258 | We identify FOXOs as transcriptional activators of IDH1. FOXOs promote IDH1 expression and thereby maintain the cytosolic levels of α-ketoglutarate and NADPH. | SIGNOR-260101 |
P31269 | P11309 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.2 | Thus Pim1 appears to be a direct transcriptional target of HOXA9 and a mediator of its antiapoptotic and proproliferative effects in early cells. | SIGNOR-261632 |
Q14653 | P13288 | 0 | phosphorylation | down-regulates activity | 0.2 | BGLF4 kinase interacts physically with and phosphorylates IRF3, which is the initial activator of transcription in the innate immune response. BGLF4 suppresses IRF3-dependent transcriptional activation. Data here suggest that Ser123, Ser173, and Thr180 contribute additively to the BGLF4-mediated repression of the IRF3 transactivation activity. | SIGNOR-266647 |
P06493 | Q9BZB8 | 1 | phosphorylation | up-regulates activity | 0.581 | Combined, our results suggest that XGef is involved in XRINGO and CDK1 mediated activation of CPEB and that an XGef, XRINGO, ERK2, and CPEB complex forms in ovo to facilitate this process.|Notably, specific inhibition of XRINGO and CDK1 activity in CPEB phosphorylation-competent extracts completely blocks phosphorylation of CPEB, which suggests that XRINGO and CDK1 directly phosphorylates CPEB. | SIGNOR-280205 |
P37840 | P67775 | 0 | dephosphorylation | down-regulates activity | 0.332 | α-Synuclein (α-Syn) is a key protein that accumulates as hyperphosphorylated aggregates in pathologic hallmark features of Parkinson's disease (PD) and other neurodegenerative disorders. Phosphorylation of this protein at serine 129 is believed to promote its aggregation and neurotoxicity, suggesting that this post-translational modification could be a therapeutic target. Here, we demonstrate that phosphoprotein phosphatase 2A (PP2A) dephosphorylates α-Syn at serine 129 | SIGNOR-248635 |
P60953 | Q8NF50 | 0 | guanine nucleotide exchange factor | up-regulates activity | 0.767 | Recently, DOCK8 was identified as a guanine-nucleotide exchange factor (GEF) for Cdc42 activation and has been associated with human mental retardation. | SIGNOR-268412 |
Q9HCK8 | P04818 | 1 | transcriptional regulation | up-regulates quantity by expression | 0.283 | In order to identify CHD8 target genes, we performed a transcriptomic analysis of CHD8-depleted cells, finding out that CHD8 controls the expression of cyclin E2 (CCNE2) and thymidylate synthetase (TYMS), two genes expressed in the G1/S transition of the cell cycle. CHD8 was also able to co-activate the CCNE2 promoter in transient transfection experiments. Chromatin immunoprecipitation experiments demonstrated that CHD8 binds directly to the 5' region of both CCNE2 and TYMS genes. | SIGNOR-268805 |
O43521 | P45984 | 0 | phosphorylation | up-regulates activity | 0.637 | 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-250134 |
Q9BX84 | Q96QT4 | 1 | phosphorylation | down-regulates quantity | 0.498 | We found TRPM6 and TRPM7 both autophosphorylate threonine residues, but only TRPM6 crossphosphorylates TRPM7, and not the reverse . | SIGNOR-279770 |
P36897 | P63000 | 1 | null | up-regulates activity | 0.28 | Thus, TGF-_1 rapidly stimulates activity of both RhoA and Rac1 and this activation requires ALK5/T_RI kinase activity. | SIGNOR-227496 |
Q9UII4 | P22392 | 1 | ubiquitination | up-regulates quantity by stabilization | 0.307 | HERC5 is required for ubiquitination of Nm23B. In summary, Nm23B ubiquitination is mediated by HERC5. Stable Nm23B protein in presence of HERC5 as well as proteasome-independent ubiquitination suggest that ubiquitination of Nm23B serves a different purpose than marking it for degradation. | SIGNOR-271778 |
Q00987 | P35790 | 0 | phosphorylation | down-regulates quantity by destabilization | 0.274 | The data presented here provides evidence for a molecular mechanism by which CKI-dependent phosphorylation of Mdm2 at multiple sites triggers SCF \u03b2-TRCP -mediated Mdm2 destruction ( xref ). | SIGNOR-279606 |
Q14896 | P17612 | 0 | phosphorylation | up-regulates | 0.275 | Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). | SIGNOR-163760 |
O15105 | Q96EB6 | 0 | deacetylation | down-regulates | 0.441 | Sirt1 reversed acetyl-transferase (p300)-mediated acetylation of two lysine residues (lys-64 and -70) on smad7. sirt1-mediated deacetylation of smad7 enhanced smad ubiquitination regulatory factor 1 (smurf1)-mediated ubiquitin proteasome degradation, which contributed to the low expression of smad7 in sirt1-overexpressing mesangial cells. | SIGNOR-150595 |
P37231 | Q00987 | 0 | ubiquitination | down-regulates quantity by destabilization | 0.389 | Here, we found that nuclear EGFR induced phosphorylation of PPARγ at Tyr-74 leading to PPARγ ubiquitination and degradation by mouse double minute 2 (MDM2) ubiquitin ligase. | SIGNOR-277191 |
Q6VVB1 | P35573 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.56 | The E3 ubiquitin ligase Malin interacts with and promotes the ubiquitination of AGL. | SIGNOR-271669 |
Q00535 | P49023 | 1 | phosphorylation | up-regulates activity | 0.377 | Thus, phosphorylation of paxillin is involved in NGF-induced neurite extension of PC-12 cells, probably through regulating focal adhesion organization.|cdk5 and p38MAPK phosphorylates Ser 85 on paxillin in vitro. | SIGNOR-278921 |
Q9Y314 | P67775 | 1 | ubiquitination | down-regulates quantity by destabilization | 0.338 | NOSIP mediates the monoubiquitination of the PP2A catalytic subunit and the loss of NOSIP results in an increase in PP2A activity in craniofacial tissue in NOSIP knockout mice. | SIGNOR-271498 |
Q86UR1 | P10415 | 1 | null | down-regulates activity | 0.2 | BH3-only proteins containing only a single BH domain and including Puma, Noxa, Bid and Bad as well as other factors are particularly important for such neutralisation, binding and regulating the anti-apoptotic Bcl-2 proteins to promote apoptosis | SIGNOR-209684 |
Q8TD19 | Q8TDX7 | 1 | phosphorylation | up-regulates activity | 0.715 | Nercc1 catalyzes the phosphorylation of nek6 (ser206) and the equivalent site on nek7 (ser195), resulting in a 20-25-fold activation of nek6/7 kinase activity | SIGNOR-103030 |
O15054 | Q16665 | 0 | transcriptional regulation | up-regulates quantity by expression | 0.266 | To this end, we confirm that KDM3A, KDM4B, KDM4C, KDM5B, KDM5C, and KDM62 are direct targets of HIF-1a while extent the list of known targets to KDM2A, KDM2B, KDM4D, KDM5A, and KDM6A. The results demonstrated that majority of the KDMs were similarly induced (KDM2A, KDM2B, KDM3A, KDM4B, KDM4C, KDM4D, KDM5A, KDM5B, KDM5C, KDM6B, and KDM7A) or repressed (KDM NO66 and KDM1A) by both HIF-1a and HIF-2a. | SIGNOR-271571 |
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