GleghornLab/Signor_processed · Datasets at Hugging Face

IdA stringlengths 6 21	IdB stringlengths 6 21	labels float64 0 2	mechanism stringclasses 40 values	effect stringclasses 10 values	score float64 0.1 0.99 ⌀	sentence stringlengths 10 1.63k ⌀	signor_id stringlengths 12 14
P42680	P42680	2	phosphorylation	up-regulates	0.2	Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. Here, we could confirm that y223 is the only site in the btk-sh3 domain being detectably phosphorylated	SIGNOR-98098
Q13315	O94874	2	ubiquitination	up-regulates activity	0.2	UFM1 specific ligase 1 (UFL1), an ufmylation E3 ligase, is important for ATM activation. UFL1 is recruited to double strand breaks by the MRE11/RAD50/NBS1 complex, and monoufmylates histone H4 following DNA damage.	SIGNOR-265073
Q13489	Q13489	2	ubiquitination	down-regulates activity	0.2	Ciap1 and ciap2 undergo autoubiquitination and degradation upon binding to the iap antagonist second mitochondrial activator of caspases (smac)/direct iap-binding protein with low pi (diablo), which is released from the mitochondria.	SIGNOR-121880
Q96JA1	Q9ULV8	2	ubiquitination	down-regulates	0.2	Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation	SIGNOR-127292
P00519	Q13188	2	phosphorylation	down-regulates	0.2	Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3	SIGNOR-181056
Q14289	Q14289	2	phosphorylation	up-regulates	0.2	Overexpression of pyk2 alone led to its spontaneous activation and tyrosine phosphorylation, resulting in activation of stat5b, indicated by the reporter gfp-stat5b. These effects were completely dependent upon tyr(402), the autophosphorylation site of pyk2, which allows recruitment of src family members for further activating phosphorylations at other sites on pyk2.	SIGNOR-124339
Q13557	Q13557	2	phosphorylation	up-regulates	0.2	Upon binding of the Ca2+/calmodulin complex to the binding domain of CaMKII, it is activated via autophosphorylation, then remaining active independent of of Ca2+ levels.	SIGNOR-255954
Q13131	Q13131	2	phosphorylation	down-regulates activity	0.2	We show that AMPK α-Ser485/491 can be a site for autophosphorylation, which may play a role in limiting AMPK activation in response to energy depletion or other regulators	SIGNOR-256114
Q02750	Q02750	2	phosphorylation	up-regulates activity	0.2	MEK1 and MEK2 can also be activated by autophosphorylation. Tyrosine 304 may be a candidate for the autophosphorylation site in MEK1.	SIGNOR-251415
Q06187	Q06187	2	phosphorylation	up-regulates	0.2	Overexpression of btk with a src family kinase increases tyrosine phosphorylation and catalytic activity of btk. This occurs by transphosphorylation at y551 in the btk catalytic domain and the enhancement of btk autophosphorylation at a second site. We mapped the major btk autophosphorylation site to y223 within the sh3 domain	SIGNOR-41480
O43829	O43829	2	binding	up-regulates activity	0.2	ZF5, which we have cloned as a transcriptional repressor on the mouse c-myc promoter, has the POZ domain at the amino-terminus and the Kruppel-type zinc finger domain at the carboxy-terminus. We demonstrated that the POZ domain has a function mediating homomeric protein-protein interaction and this interaction requires the zinc finger domain.	SIGNOR-220534
O00206	O00206	2	binding	up-regulates	0.2	Upon activation, tlrs hetero- or homodimerize inducing the recruitment of adaptor proteins via the cytoplasmic tir domain	SIGNOR-203484
O60858	O60858	2	polyubiquitination	down-regulates quantity by destabilization	0.2	In this study, we showed that the N-degron pathway mediates ubiquitin (Ub)-dependent reticulophagy. During this 2-step process, the ER transmembrane E3 ligase TRIM13 undergoes auto-ubiquitination via lysine 63 (K63) linkage chains and acts as a ligand for the autophagic receptor SQSTM1/p62 (sequestosome 1).	SIGNOR-272219
P12643	P12643	2	binding	up-regulates	0.2	Bmps are dimeric proteins with a single interchain disulfide bond. The dimeric conformation is an absolute requirement for the biological action and interaction with receptors	SIGNOR-236166
P80192	P80192	2	phosphorylation	up-regulates activity	0.2	We present here biochemical and biophysical evidence that MLK1 is activated by autophosphorylation in (or near) the activation loop. The activation loops of the MLK family are highly homologous, and so one might predict that the same residues would be key to their activation. Functional data presented here, however, demonstrate that the key residue for activation of MLK1, Thr312, differs from the key residue for activation of MLK3.	SIGNOR-249388
P16591	P16591	2	phosphorylation	up-regulates activity	0.2	Mutation analysis unveiled a tyrosine (Tyr(616)) embedded in the Hsp90 recognition loop, which is required for the kinase activity of Fer. Replacement of this tyrosine by phenylalanine (Y616F) disabled the auto-phosphorylation activity of Fer and abolished its ability to phosphorylate Stat3.	SIGNOR-276236
P24941	P24941	2	phosphorylation	up-regulates	0.2	Our results demonstrate that cdk2 is capable of autophosphorylation at thr160.	SIGNOR-153636
O00712	O00712	2	binding	down-regulates activity	0.2	Coexpression of NFI-B3 with other isoforms of the NFI-B, -C, and -X family, however, led to a strong reduction of transcriptional activation compared with the expression of these factors alone. NFI-B3 apparently forms heterodimers with other NFI proteins thereby interfering with their function.	SIGNOR-240883
Q14012	Q14012	2	phosphorylation	up-regulates activity	0.2	CaM kinase I was autophosphorylated in a Ca2+/CaM-dependent manner at a threonyl residue (Thr-177) which is located at a position equivalent to that of the threonyl residue (Thr-197) autophosphorylated in cAMP-dependent protein kinase.	SIGNOR-250612
P41240	P41240	2	phosphorylation	up-regulates activity	0.2	Taken together these results indicate that Csk can be phosphorylated in vivo at Tyr-184 by an as yet unknown tyrosine kinase, and that autophosphorylation of Tyr-304 occurs only at abnormally high Csk concentrations in vitro. Furthermore, Tyr-304 is required for the maintenance of the structure of the Csk kinase domain.	SIGNOR-250778
Q12809	P05556	2	binding	up-regulates activity	0.2	One such mechanism is operant in colorectal cancer (CRC) cells. On integrin-dependent CRC cell adhesion, the Kv11.1/β1 integrin complex recruits the PI3K p85 subunit, which stimulates AKT phosphorylation and thus regulates autophagy	SIGNOR-277614
Q96FA3	P00533	2	phosphorylation	up-regulates activity	0.2	EGFR is positively correlated with PELI1 expression in breast cancers, and its activation led to the phosphorylation of PELI1 at Tyr154 and Thr264, which subsequently activated its E3 ubiquitin ligase.	SIGNOR-277874
Q04759	Q04759	2	phosphorylation	up-regulates activity	0.2	Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes.	SIGNOR-249298
P25098	P09619	2	phosphorylation	up-regulates activity	0.2	The platelet-derived growth factor receptor-beta phosphorylates and activates G protein-coupled receptor kinase-2.\|We conclude that the activated PDGFRbeta itself phosphorylates GRK2 tyrosyl residues and thereby activates GRK2, which then serine phosphorylates and desensitizes the PDGFRbeta.	SIGNOR-278972
O94874	Q13315	2	phosphorylation	up-regulates activity	0.2	Furthermore, ATM phosphorylates UFL1 at serine 462, enhancing UFL1 E3 ligase activity and promoting ATM activation in a positive feedback loop.	SIGNOR-265075
P98170	O43236	2	binding	down-regulates quantity	0.2	The mitochondrial ARTS protein promotes apoptosis through targeting XIAP.\|Binding of ARTS to XIAP is direct, as recombinant ARTS and XIAP proteins can bind to each other in vitro. ARTS binding to XIAP is specific and related to its pro-apoptotic function, as mutant forms of ARTS (or related septins) that fail to bind XIAP failed to induce apoptosis. ARTS leads to decreased XIAP protein levels and caspase activation. Our data suggest that ARTS induces apoptosis by antagonizing IAPs.	SIGNOR-267671
Q13554	Q13554	2	phosphorylation	up-regulates activity	0.2	Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity.	SIGNOR-250640
Q15645	P00533	2	phosphorylation	up-regulates quantity	0.2	Reciprocally, TRIP13 was phosphorylated at tyrosine(Y) 56 by EGFRvIII and EGF-activated EGFR. Abrogating TRIP13 Y56 phosphorylation dramatically attenuated TRIP13 expression-enhanced EGFR signaling and GBM cell growth.	SIGNOR-265083
P17861	P17861	2	binding	up-regulates activity	0.2	E4BP4, ATF-6, OASIS, and XBP-1 all formed strong homodimeric associations on the array Transcription factor dimerization can increase the selectivity of protein-DNA interactions and generate a large amount of DNA binding diversity from a relatively small number of proteins	SIGNOR-224199
Q8NHY2	Q13330	2	binding	down-regulates quantity by destabilization	0.2	MTA1 destabilizes COP1 by promoting its autoubiquitination. in addition to polyubiquitination of its substrates, COP1 also catalyzes its autoubiquitination for degradation as a part of an autoregulatory mechanism	SIGNOR-271892
Q8N0X7	Q96J02	2	binding	up-regulates activity	0.2	SPG20 Protein Spartin Is Recruited to Midbodies by ESCRT-III Protein Ist1 and Participates in Cytokinesis. Spartin colocalizes with Ist1 at the midbody, and depletion of Ist1 in cells significantly decreases the number of cells where spartin is present at midbodies.	SIGNOR-261308
Q9ULV8	Q96JA1	2	binding	up-regulates	0.2	Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation	SIGNOR-127301
Q9H765	O14920	2	phosphorylation	up-regulates activity	0.2	We found that ASB8 was phosphorylated at the N-terminal Ser-31 by host IkappaB kinase beta (IKKbeta). In turn, ASB8 facilitated K48-linked ubiquitination and degradation of IKKbeta via the ubiquitin-proteasome pathway, resulting in remarkable inhibition of I-kappa-B-alpha (IkappaBalpha) and of p65 phosphorylation, consequently suppressing NF-kappaB activity.	SIGNOR-272242
P10721	Q13239	2	ubiquitination	down-regulates quantity by destabilization	0.2	In this report, we show that SLAP associates with both wild-type and oncogenic c-Kit (c-Kit-D816V). The association involves the SLAP SH2 domain and receptor phosphotyrosine residues different from those mediating Src interaction. Association of SLAP triggers c-Kit ubiquitylation which, in turn, is followed by receptor degradation	SIGNOR-263143
Q9NTX7	Q9NTX7	2	ubiquitination	down-regulates quantity	0.2	We show that RNF146, tankyrase, and Axin form a protein complex, and that RNF146 mediates ubiquitylation of all three proteins to target them for proteasomal degradation.	SIGNOR-260006
Q08345	Q08345	2	phosphorylation	up-regulates activity	0.2	The discoidin domain receptor tyrosine kinases are activated by collagen \| Here, we present evidence that stimulating DDR1- and DDR2-expressing cells with various types of collagen induces receptor autophosphorylation.	SIGNOR-251086
P61296	P61296	2	binding	up-regulates activity	0.2	The basic helix-loop-helix factor, HAND2, functions as a transcriptional activator by binding to E-boxes as a heterodimer	SIGNOR-223476
P20265	P20265	2	binding	up-regulates activity	0.2	These experiments lead to the conclusion that the full-length Brn-2 protein can interact with full-length Brn-2. Assay of homodimerization properties of Brn-2 protein on the b2s1 dimer recognition sequence also demonstrated cooperativity, indicating that protein-protein contacts would be important for synergistic interactions between the Brn-2 subunits.	SIGNOR-221824
Q2T9J0	Q2T9J0	2	cleavage	down-regulates activity	0.2	Self-cleavage of Tysnd1 in the active oligomer most likely inactivates its protease activity. Subsequently, the cleaved products are degraded by PsLon and removed from the Tysnd1 oligomer.	SIGNOR-261053
P51956	P51956	2	phosphorylation	down-regulates activity	0.2	Autophosphorylation at Thr-165 is required for NEK3 kinase activity in vitro.	SIGNOR-260919
Q9BYF1	P01019-PRO_0000032457	2	binding	up-regulates activity	0.2	At first, ACE2 has been demonstrated to induce conversion of Ang I into Ang (1–7) by means of intermediate production of Ang (1–9), a fragment with unknown function.	SIGNOR-260226
O43236	P98170	2	ubiquitination	down-regulates quantity	0.2	Fig. 1 D revealed that co-transfection of ARTS and full length XIAP strongly reduces the levels of ARTS, while co-transfection of ARTS and XIAPdelRING does not change ARTS protein levels.\|In this study we show that XIAP also promotes the ubiquitination and degradation of its antagonist ARTS.	SIGNOR-278801
Q9Y4K3	Q9Y4K3	2	ubiquitination	up-regulates activity	0.2	Here we report that the ubiquitin ligase (e3) traf6 interacts with a consensus motif present in tbetari. The tbetari-traf6 interaction is required for tgf-beta-induced autoubiquitylation of traf6 and subsequent activation of the tak1-p38/jnk pathway, which leads to apoptosis.	SIGNOR-180562
P49715	P49715	2	transcriptional regulation	up-regulates quantity	0.2	Here, we demonstrate that C/EBPα indeed activates its promoter in transient transfection assays in myeloid cells.	SIGNOR-255673
Q9UL17	Q9UL17	2	null	up-regulates	0.2	In turn, T-bet is an IFN-gamma activator (Szabo et al., 2000), thus creating an indirect positive feedback. Furthermore, it has been shown that ectopic T-bet is able to induce the transcription of its own gene	SIGNOR-254294
Q8IYM9	Q8IYM9	2	polyubiquitination	down-regulates quantity by destabilization	0.2	Importantly, TRIM22 was conjugated with poly-ubiquitin chains and stabilized by the proteasome inhibitor in 293T cells, suggesting that TRIM22 targeted itself for proteasomal degradation through the poly-ubiquitylation. We also found that TRIM22 was located in the nucleus, indicating that TRIM22 might function as a nuclear E3 ubiquitin ligase.	SIGNOR-271780
Q9C026	Q9C026	2	ubiquitination	down-regulates quantity by destabilization	0.2	Collectively, these results indicated that TRIM9 is an E3 ligase for its self-ubiquitination and that the ubiquitination of TRIM9 likely serves as a signal for proteasomal degradation. As shown in Fig. 1A, TRIM9 was ubiquitinated by itself when incubated with UbcH5b. In contrast, ubiquitination was observed when incubated with other E2 enzymes. These results suggest that TRIM9 cooperates with UbcH5b for its self-ubiquitination. N	SIGNOR-271419
O14920	Q9H765	2	ubiquitination	down-regulates quantity by destabilization	0.2	In turn, ASB8 facilitated K48-linked ubiquitination and degradation of IKKbeta via the ubiquitin-proteasome pathway, resulting in remarkable inhibition of I-kappa-B-alpha (IkappaBalpha) and of p65 phosphorylation, consequently suppressing NF-kappaB activity.	SIGNOR-272253
P00533	Q15645	2	binding	up-regulates quantity by stabilization	0.2	Mechanistically, TRIP13 enhanced EGFR protein abundance in part by preventing Cbl-mediated ubiquitination and proteasomal degradation.	SIGNOR-265084
P15173	P15173	2	transcriptional regulation	up-regulates	0.2	Upon the expression of myogenin, myogenin, mef2d, and brg1 localize to the myogenin promoter to maintain myogenin expression./ Swi/snf chromatin-remodeling activity is required for myogenin expression in differentiated skeletal muscle	SIGNOR-151694
O15146	O15146	2	phosphorylation	up-regulates activity	0.2	AGRN is released by the nerve and binds to LRP4, which then binds to MuSK. This interaction leads to MuSK autophosphorylation and activation of its kinase function, leading to anterograde signalling by subsequent phosphorylation of DOK7 (not shown), which binds MuSK as a dimer.	SIGNOR-273851
P10275	P10275	2	binding	up-regulates activity	0.2	The unliganded AR resides predominately in the cytoplasm as a heteromeric complex with hsp90 and other chaperone proteins. These chaperone proteins maintain AR in a form that is receptive to ligand binding. Regulation of gene expression by androgen-activated AR occurs through receptor nuclear translocation, dimerization, and binding to androgen response elements (AREs) in the DNA of target genes.	SIGNOR-251537
P27708	P27708	2	phosphorylation	up-regulates activity	0.2	Autophosphorylation resulted in a 2-fold increase in CPSase activity, an increased sensitivity to the feedback inhibitor UTP, and decreased allosteric activation by 5-phosphoribosyl-1-pyrophosphate	SIGNOR-250610
O00625	Q16236	2	transcriptional regulation	up-regulates quantity by expression	0.2	The activation of NFE2L2 is pivotal in protecting cells from ferroptotic death. To achieve this protective function, NFE2L2 regulates a broad spectrum of genes involved in multiple cellular pathways, including those that modulate ROS, detoxify harmful agents, and repair damaged proteins. In human pancreatic cancer cell lines, the expression of PIR is upregulated by NFE2L2 in response to ferroptosis-inducing agents (erastin or RSL3)	SIGNOR-279850
P07948	P07948	2	phosphorylation	up-regulates activity	0.2	Lyn is a member of the Src family of protein-tyrosine kinases that can readily undergo autophosphorylation in vitro. The site of autophosphorylation is Tyr397. Autophosphorylation results in a 17-fold increase in protein-tyrosine kinase activity.	SIGNOR-251402
Q96EP0	P29466	2	cleavage	down-regulates activity	0.2	We show that LUBAC interacted with caspase-1 via HOIP and modified its CARD domain with linear polyubiquitin and that depletion of HOIP or Sharpin resulted in heightened caspase-1 activation and cell death in response to inflammasome activation, unlike what is observed in macrophages. Reciprocally, caspase-1, as well as caspase-8, regulated LUBAC activity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death.	SIGNOR-272193
Q96J02	Q8N0X7	2	binding	up-regulates activity	0.2	Cytosolic endogenous spartin is mono-ubiquitinated and we demonstrate that it interacts via a PPXY motif with the ubiquitin E3 ligases AIP4 [atrophin-interacting protein 4; ITCH (itchy E3 ubiquitin protein ligase homologue] [corrected] and AIP5 (WWP1). Surprisingly, the PPXY motif, AIP4 and AIP5 are not required for spartin's ubiquitination, and so we propose that spartin acts as an adaptor for these proteins.	SIGNOR-261306
Q86SG6	Q86SG6	2	phosphorylation	up-regulates activity	0.2	Multimerization and autophosphorylation of Nek8 are important for its activation.Our data suggests that one site for Nek8 autophosphorylation may be Thr-210 within the activation loop.	SIGNOR-250298
O43524	O43524	2	transcriptional regulation	up-regulates quantity	0.2	We show that FOXO3 binds and activates its own promoter via a positive autoregulatory feedback loop	SIGNOR-255757
Q9C035	Q9C035	2	monoubiquitination	up-regulates quantity	0.2	Here, we show that TRIM5alpha functions as a RING-finger-type E3 ubiquitin ligase both in vitro and in vivo and ubiquitinates itself in cooperation with the E2 ubiquitin-conjugating enzyme UbcH5B. Thus, the ubiquitination of TRIM5alpha is catalyzed by itself and Ro52. Unexpectedly, although TRIM5alpha is ubiquitinated, our results have revealed that the proteasome inhibitors MG115 and MG132 do not stabilize it in HeLa cells, suggesting that the ubiquitination of TRIM5alpha does not lead to proteasomal degradation. Importantly, TRIM5alpha is clearly conjugated by a single ubiquitin molecule (monoubiquitination). Our monoubiquitin-fusion assay suggests that monoubiquitination is a signal for TRIM5alpha to translocate from cytoplasmic bodies to the cytoplasm.	SIGNOR-271671
Q9Y572	Q9Y572	2	phosphorylation	up-regulates activity	0.2	This suggests that Thr182 is a likely auto-phosphorylation target and may be involved in RIP3 activity.	SIGNOR-277396
Q96EP1	Q96EP1	2	ubiquitination	down-regulates quantity by destabilization	0.2	In this study, we identified USP7 (also known as HAUSP), which is a member of a family of proteins that cleave polyubiquitin chains and/or ubiquitin precursors, as an interacting protein with Chfr by immunoaffinity purification and mass spectrometry, and their interaction greatly increases the stability of Chfr. In fact, USP7 can remove ubiquitin moiety from the autoubiquitinated Chfr both in vivo and in vitro, which results in the accumulation of Chfr in the cell. USP7 mediates deubiquitination of Chfr.	SIGNOR-271461
Q02930	Q02930	2	binding	up-regulates activity	0.2	CRE-BPa specifically binds to CRE as a homodimer or heterodimer with c-Jun or CRE-BP1. In CAT cotransfection experiments using CV-1 cells, transient expression of each of four CRE-BPa proteins caused a 1.6- to 3.4-fold increase of CRE-dependent transcription	SIGNOR-219602
Q96GX5	Q96GX5	2	phosphorylation	up-regulates activity	0.2	After this priming step, Gwl can intramolecularly phosphorylate its C-terminal tail at pS883; this site probably plays a role similar to that of the tail/Z motif of other AGC kinases.	SIGNOR-243409
P04049	P04049	2	phosphorylation	up-regulates activity	0.2	We show that phosphorylation of s621 turns over rapidly and is enriched in the activated pool of endogenous raf-1. The phosphorylation on this site can be mediated by raf-1 itself but also by other kinase(s)	SIGNOR-235770
O15151	O15151	2	ubiquitination	down-regulates quantity by destabilization	0.2	Here we demonstrate that MdmX acts as a ubiquitin ligase in vitro, being capable of autoubiquitination, as well as mediating the ubiquitination of p53.	SIGNOR-271390
P06239	P06239	2	phosphorylation	up-regulates activity	0.2	They also demonstrate that replacement of the major site of autophosphorylation of p56lck (tyrosine 394) by a phenylalanine residue abolishes the ability to activate p56lck by CD4 cross-linking, implying that this residue is critical for the positive regulation of the Lck tyrosine kinase activity by CD4.	SIGNOR-81372
Q14164	Q14164	2	phosphorylation	up-regulates activity	0.2	As previously reported, IKKε underwent rapid activation by auto-phosphorylation on T501 upon IFNβ treatment of control A549 cells, which was impaired by TRIM6si (Figure 4D)	SIGNOR-276637
Q9UM73	Q9UM73	2	phosphorylation	up-regulates activity	0.2	ALK SelectiVely Phosphorylates the First Tyrosine in Its A-Loop Peptide.	SIGNOR-250575
P00533	Q96FA3	2	polyubiquitination	up-regulates quantity by stabilization	0.2	EGFR is positively correlated with PELI1 expression in breast cancers, and its activation led to the phosphorylation of PELI1 at Tyr154 and Thr264, which subsequently activated its E3 ubiquitin ligase. Simultaneously, PELI1 physically interacted with and enhanced the stability of EGFR via the K63-linked polyubiquitination in reverse.	SIGNOR-277875
Q12851	Q12851	2	phosphorylation	up-regulates activity	0.2	MAP4K2 is autophosphorylated at S170 for activation	SIGNOR-277826
P49959	Q13315	2	phosphorylation	up-regulates	0.2	In this report, we showed that atm phosphorylates a p95 peptide (ser-343) and a mre11 peptide (ser-264) in vitro, suggesting that atm may regulate the function of p95?Mre11? Rad50 repair complex in response to dna damage.	SIGNOR-73366
Q86YT6	Q86YT6	2	polyubiquitination	down-regulates quantity by destabilization	0.2	The RING finger motifs of DIP-1 have E3 ligase activity that can auto-ubiquitinate DIP-1 in vitro. In vivo, DIP-1 is detected as a polyubiquitinated protein, suggesting that the intracellular levels of DIP-1 are regulated by the ubiquitin-proteasome system.	SIGNOR-272603
O15530	P00558	2	phosphorylation	up-regulates activity	0.2	PGK1 is an important enzyme in the metabolic glycolysis pathway, but PGK1 also phosphorylates and activates PDK1 through its protein kinase activity ( xref ).\|PGK1 is an important enzyme in the metabolic glycolysis pathway, but PGK1 also phosphorylates and activates PDK1 through its protein kinase activity.	SIGNOR-280064

P42680

2

phosphorylation

up-regulates

0.2

Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. Here, we could confirm that y223 is the only site in the btk-sh3 domain being detectably phosphorylated

SIGNOR-98098

Q13315

O94874

2

ubiquitination

up-regulates activity

0.2

UFM1 specific ligase 1 (UFL1), an ufmylation E3 ligase, is important for ATM activation. UFL1 is recruited to double strand breaks by the MRE11/RAD50/NBS1 complex, and monoufmylates histone H4 following DNA damage.

SIGNOR-265073

Q13489

2

ubiquitination

down-regulates activity

0.2

Ciap1 and ciap2 undergo autoubiquitination and degradation upon binding to the iap antagonist second mitochondrial activator of caspases (smac)/direct iap-binding protein with low pi (diablo), which is released from the mitochondria.

SIGNOR-121880

Q96JA1

Q9ULV8

2

ubiquitination

down-regulates

0.2

Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation

SIGNOR-127292

P00519

Q13188

2

phosphorylation

down-regulates

0.2

Here, we identify clk1, clk4, mst1, mst2 and ttk (also known as mps1) as novel thr735 kinases in vitro / phosphorylation of thr735 in c-abl is critical for binding to 14-3-3

SIGNOR-181056

Q14289

2

phosphorylation

up-regulates

0.2

Overexpression of pyk2 alone led to its spontaneous activation and tyrosine phosphorylation, resulting in activation of stat5b, indicated by the reporter gfp-stat5b. These effects were completely dependent upon tyr(402), the autophosphorylation site of pyk2, which allows recruitment of src family members for further activating phosphorylations at other sites on pyk2.

SIGNOR-124339

Q13557

2

phosphorylation

up-regulates

0.2

Upon binding of the Ca2+/calmodulin complex to the binding domain of CaMKII, it is activated via autophosphorylation, then remaining active independent of of Ca2+ levels.

SIGNOR-255954

Q13131

2

phosphorylation

down-regulates activity

0.2

We show that AMPK α-Ser485/491 can be a site for autophosphorylation, which may play a role in limiting AMPK activation in response to energy depletion or other regulators

SIGNOR-256114

Q02750

2

phosphorylation

up-regulates activity

0.2

MEK1 and MEK2 can also be activated by autophosphorylation. Tyrosine 304 may be a candidate for the autophosphorylation site in MEK1.

SIGNOR-251415

Q06187

2

phosphorylation

up-regulates

0.2

Overexpression of btk with a src family kinase increases tyrosine phosphorylation and catalytic activity of btk. This occurs by transphosphorylation at y551 in the btk catalytic domain and the enhancement of btk autophosphorylation at a second site. We mapped the major btk autophosphorylation site to y223 within the sh3 domain

SIGNOR-41480

O43829

2

binding

up-regulates activity

0.2

ZF5, which we have cloned as a transcriptional repressor on the mouse c-myc promoter, has the POZ domain at the amino-terminus and the Kruppel-type zinc finger domain at the carboxy-terminus. We demonstrated that the POZ domain has a function mediating homomeric protein-protein interaction and this interaction requires the zinc finger domain.

SIGNOR-220534

O00206

2

binding

up-regulates

0.2

Upon activation, tlrs hetero- or homodimerize inducing the recruitment of adaptor proteins via the cytoplasmic tir domain

SIGNOR-203484

O60858

2

polyubiquitination

down-regulates quantity by destabilization

0.2

In this study, we showed that the N-degron pathway mediates ubiquitin (Ub)-dependent reticulophagy. During this 2-step process, the ER transmembrane E3 ligase TRIM13 undergoes auto-ubiquitination via lysine 63 (K63) linkage chains and acts as a ligand for the autophagic receptor SQSTM1/p62 (sequestosome 1).

SIGNOR-272219

P12643

2

binding

up-regulates

0.2

Bmps are dimeric proteins with a single interchain disulfide bond. The dimeric conformation is an absolute requirement for the biological action and interaction with receptors

SIGNOR-236166

P80192

2

phosphorylation

up-regulates activity

0.2

We present here biochemical and biophysical evidence that MLK1 is activated by autophosphorylation in (or near) the activation loop. The activation loops of the MLK family are highly homologous, and so one might predict that the same residues would be key to their activation. Functional data presented here, however, demonstrate that the key residue for activation of MLK1, Thr312, differs from the key residue for activation of MLK3.

SIGNOR-249388

P16591

2

phosphorylation

up-regulates activity

0.2

Mutation analysis unveiled a tyrosine (Tyr(616)) embedded in the Hsp90 recognition loop, which is required for the kinase activity of Fer. Replacement of this tyrosine by phenylalanine (Y616F) disabled the auto-phosphorylation activity of Fer and abolished its ability to phosphorylate Stat3.

SIGNOR-276236

P24941

2

phosphorylation

up-regulates

0.2

Our results demonstrate that cdk2 is capable of autophosphorylation at thr160.

SIGNOR-153636

O00712

2

binding

down-regulates activity

0.2

Coexpression of NFI-B3 with other isoforms of the NFI-B, -C, and -X family, however, led to a strong reduction of transcriptional activation compared with the expression of these factors alone. NFI-B3 apparently forms heterodimers with other NFI proteins thereby interfering with their function.

SIGNOR-240883

Q14012

2

phosphorylation

up-regulates activity

0.2

CaM kinase I was autophosphorylated in a Ca2+/CaM-dependent manner at a threonyl residue (Thr-177) which is located at a position equivalent to that of the threonyl residue (Thr-197) autophosphorylated in cAMP-dependent protein kinase.

SIGNOR-250612

P41240

2

phosphorylation

up-regulates activity

0.2

Taken together these results indicate that Csk can be phosphorylated in vivo at Tyr-184 by an as yet unknown tyrosine kinase, and that autophosphorylation of Tyr-304 occurs only at abnormally high Csk concentrations in vitro. Furthermore, Tyr-304 is required for the maintenance of the structure of the Csk kinase domain.

SIGNOR-250778

Q12809

P05556

2

binding

up-regulates activity

0.2

One such mechanism is operant in colorectal cancer (CRC) cells. On integrin-dependent CRC cell adhesion, the Kv11.1/β1 integrin complex recruits the PI3K p85 subunit, which stimulates AKT phosphorylation and thus regulates autophagy

SIGNOR-277614

Q96FA3

P00533

2

phosphorylation

up-regulates activity

0.2

EGFR is positively correlated with PELI1 expression in breast cancers, and its activation led to the phosphorylation of PELI1 at Tyr154 and Thr264, which subsequently activated its E3 ubiquitin ligase.

SIGNOR-277874

Q04759

2

phosphorylation

up-regulates activity

0.2

Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes.

SIGNOR-249298

P25098

P09619

2

phosphorylation

up-regulates activity

0.2

The platelet-derived growth factor receptor-beta phosphorylates and activates G protein-coupled receptor kinase-2.|We conclude that the activated PDGFRbeta itself phosphorylates GRK2 tyrosyl residues and thereby activates GRK2, which then serine phosphorylates and desensitizes the PDGFRbeta.

SIGNOR-278972

O94874

Q13315

2

phosphorylation

up-regulates activity

0.2

Furthermore, ATM phosphorylates UFL1 at serine 462, enhancing UFL1 E3 ligase activity and promoting ATM activation in a positive feedback loop.

SIGNOR-265075

P98170

O43236

2

binding

down-regulates quantity

0.2

The mitochondrial ARTS protein promotes apoptosis through targeting XIAP.|Binding of ARTS to XIAP is direct, as recombinant ARTS and XIAP proteins can bind to each other in vitro. ARTS binding to XIAP is specific and related to its pro-apoptotic function, as mutant forms of ARTS (or related septins) that fail to bind XIAP failed to induce apoptosis. ARTS leads to decreased XIAP protein levels and caspase activation. Our data suggest that ARTS induces apoptosis by antagonizing IAPs.

SIGNOR-267671

Q13554

2

phosphorylation

up-regulates activity

0.2

Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity.

SIGNOR-250640

Q15645

P00533

2

phosphorylation

up-regulates quantity

0.2

Reciprocally, TRIP13 was phosphorylated at tyrosine(Y) 56 by EGFRvIII and EGF-activated EGFR. Abrogating TRIP13 Y56 phosphorylation dramatically attenuated TRIP13 expression-enhanced EGFR signaling and GBM cell growth.

SIGNOR-265083

P17861

2

binding

up-regulates activity

0.2

E4BP4, ATF-6, OASIS, and XBP-1 all formed strong homodimeric associations on the array Transcription factor dimerization can increase the selectivity of protein-DNA interactions and generate a large amount of DNA binding diversity from a relatively small number of proteins

SIGNOR-224199

Q8NHY2

Q13330

2

binding

down-regulates quantity by destabilization

0.2

MTA1 destabilizes COP1 by promoting its autoubiquitination. in addition to polyubiquitination of its substrates, COP1 also catalyzes its autoubiquitination for degradation as a part of an autoregulatory mechanism

SIGNOR-271892

Q8N0X7

Q96J02

2

binding

up-regulates activity

0.2

SPG20 Protein Spartin Is Recruited to Midbodies by ESCRT-III Protein Ist1 and Participates in Cytokinesis. Spartin colocalizes with Ist1 at the midbody, and depletion of Ist1 in cells significantly decreases the number of cells where spartin is present at midbodies.

SIGNOR-261308

Q9ULV8

Q96JA1

2

binding

up-regulates

0.2

Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation

SIGNOR-127301

Q9H765

O14920

2

phosphorylation

up-regulates activity

0.2

We found that ASB8 was phosphorylated at the N-terminal Ser-31 by host IkappaB kinase beta (IKKbeta). In turn, ASB8 facilitated K48-linked ubiquitination and degradation of IKKbeta via the ubiquitin-proteasome pathway, resulting in remarkable inhibition of I-kappa-B-alpha (IkappaBalpha) and of p65 phosphorylation, consequently suppressing NF-kappaB activity.

SIGNOR-272242

P10721

Q13239

2

ubiquitination

down-regulates quantity by destabilization

0.2

In this report, we show that SLAP associates with both wild-type and oncogenic c-Kit (c-Kit-D816V). The association involves the SLAP SH2 domain and receptor phosphotyrosine residues different from those mediating Src interaction. Association of SLAP triggers c-Kit ubiquitylation which, in turn, is followed by receptor degradation

SIGNOR-263143

Q9NTX7

2

ubiquitination

down-regulates quantity

0.2

We show that RNF146, tankyrase, and Axin form a protein complex, and that RNF146 mediates ubiquitylation of all three proteins to target them for proteasomal degradation.

SIGNOR-260006

Q08345

2

phosphorylation

up-regulates activity

0.2

The discoidin domain receptor tyrosine kinases are activated by collagen | Here, we present evidence that stimulating DDR1- and DDR2-expressing cells with various types of collagen induces receptor autophosphorylation.

SIGNOR-251086

P61296

2

binding

up-regulates activity

0.2

The basic helix-loop-helix factor, HAND2, functions as a transcriptional activator by binding to E-boxes as a heterodimer

SIGNOR-223476

P20265

2

binding

up-regulates activity

0.2

These experiments lead to the conclusion that the full-length Brn-2 protein can interact with full-length Brn-2. Assay of homodimerization properties of Brn-2 protein on the b2s1 dimer recognition sequence also demonstrated cooperativity, indicating that protein-protein contacts would be important for synergistic interactions between the Brn-2 subunits.

SIGNOR-221824

Q2T9J0

2

cleavage

down-regulates activity

0.2

Self-cleavage of Tysnd1 in the active oligomer most likely inactivates its protease activity. Subsequently, the cleaved products are degraded by PsLon and removed from the Tysnd1 oligomer.

SIGNOR-261053

P51956

2

phosphorylation

down-regulates activity

0.2

Autophosphorylation at Thr-165 is required for NEK3 kinase activity in vitro.

SIGNOR-260919

Q9BYF1

P01019-PRO_0000032457

2

binding

up-regulates activity

0.2

At first, ACE2 has been demonstrated to induce conversion of Ang I into Ang (1–7) by means of intermediate production of Ang (1–9), a fragment with unknown function.

SIGNOR-260226

O43236

P98170

2

ubiquitination

down-regulates quantity

0.2

Fig. 1 D revealed that co-transfection of ARTS and full length XIAP strongly reduces the levels of ARTS, while co-transfection of ARTS and XIAPdelRING does not change ARTS protein levels.|In this study we show that XIAP also promotes the ubiquitination and degradation of its antagonist ARTS.

SIGNOR-278801

Q9Y4K3

2

ubiquitination

up-regulates activity

0.2

Here we report that the ubiquitin ligase (e3) traf6 interacts with a consensus motif present in tbetari. The tbetari-traf6 interaction is required for tgf-beta-induced autoubiquitylation of traf6 and subsequent activation of the tak1-p38/jnk pathway, which leads to apoptosis.

SIGNOR-180562

P49715

2

transcriptional regulation

up-regulates quantity

0.2

Here, we demonstrate that C/EBPα indeed activates its promoter in transient transfection assays in myeloid cells.

SIGNOR-255673

Q9UL17

2

null

up-regulates

0.2

In turn, T-bet is an IFN-gamma activator (Szabo et al., 2000), thus creating an indirect positive feedback. Furthermore, it has been shown that ectopic T-bet is able to induce the transcription of its own gene

SIGNOR-254294

Q8IYM9

2

polyubiquitination

down-regulates quantity by destabilization

0.2

Importantly, TRIM22 was conjugated with poly-ubiquitin chains and stabilized by the proteasome inhibitor in 293T cells, suggesting that TRIM22 targeted itself for proteasomal degradation through the poly-ubiquitylation. We also found that TRIM22 was located in the nucleus, indicating that TRIM22 might function as a nuclear E3 ubiquitin ligase.

SIGNOR-271780

Q9C026

2

ubiquitination

down-regulates quantity by destabilization

0.2

Collectively, these results indicated that TRIM9 is an E3 ligase for its self-ubiquitination and that the ubiquitination of TRIM9 likely serves as a signal for proteasomal degradation. As shown in Fig. 1A, TRIM9 was ubiquitinated by itself when incubated with UbcH5b. In contrast, ubiquitination was observed when incubated with other E2 enzymes. These results suggest that TRIM9 cooperates with UbcH5b for its self-ubiquitination. N

SIGNOR-271419

O14920

Q9H765

2

ubiquitination

down-regulates quantity by destabilization

0.2

In turn, ASB8 facilitated K48-linked ubiquitination and degradation of IKKbeta via the ubiquitin-proteasome pathway, resulting in remarkable inhibition of I-kappa-B-alpha (IkappaBalpha) and of p65 phosphorylation, consequently suppressing NF-kappaB activity.

SIGNOR-272253

P00533

Q15645

2

binding

up-regulates quantity by stabilization

0.2

Mechanistically, TRIP13 enhanced EGFR protein abundance in part by preventing Cbl-mediated ubiquitination and proteasomal degradation.

SIGNOR-265084

P15173

2

transcriptional regulation

up-regulates

0.2

Upon the expression of myogenin, myogenin, mef2d, and brg1 localize to the myogenin promoter to maintain myogenin expression./ Swi/snf chromatin-remodeling activity is required for myogenin expression in differentiated skeletal muscle

SIGNOR-151694

O15146

2

phosphorylation

up-regulates activity

0.2

AGRN is released by the nerve and binds to LRP4, which then binds to MuSK. This interaction leads to MuSK autophosphorylation and activation of its kinase function, leading to anterograde signalling by subsequent phosphorylation of DOK7 (not shown), which binds MuSK as a dimer.

SIGNOR-273851

P10275

2

binding

up-regulates activity

0.2

The unliganded AR resides predominately in the cytoplasm as a heteromeric complex with hsp90 and other chaperone proteins. These chaperone proteins maintain AR in a form that is receptive to ligand binding. Regulation of gene expression by androgen-activated AR occurs through receptor nuclear translocation, dimerization, and binding to androgen response elements (AREs) in the DNA of target genes.

SIGNOR-251537

P27708

2

phosphorylation

up-regulates activity

0.2

Autophosphorylation resulted in a 2-fold increase in CPSase activity, an increased sensitivity to the feedback inhibitor UTP, and decreased allosteric activation by 5-phosphoribosyl-1-pyrophosphate

SIGNOR-250610

O00625

Q16236

2

transcriptional regulation

up-regulates quantity by expression

0.2

The activation of NFE2L2 is pivotal in protecting cells from ferroptotic death. To achieve this protective function, NFE2L2 regulates a broad spectrum of genes involved in multiple cellular pathways, including those that modulate ROS, detoxify harmful agents, and repair damaged proteins. In human pancreatic cancer cell lines, the expression of PIR is upregulated by NFE2L2 in response to ferroptosis-inducing agents (erastin or RSL3)

SIGNOR-279850

P07948

2

phosphorylation

up-regulates activity

0.2

Lyn is a member of the Src family of protein-tyrosine kinases that can readily undergo autophosphorylation in vitro. The site of autophosphorylation is Tyr397. Autophosphorylation results in a 17-fold increase in protein-tyrosine kinase activity.

SIGNOR-251402

Q96EP0

P29466

2

cleavage

down-regulates activity

0.2

We show that LUBAC interacted with caspase-1 via HOIP and modified its CARD domain with linear polyubiquitin and that depletion of HOIP or Sharpin resulted in heightened caspase-1 activation and cell death in response to inflammasome activation, unlike what is observed in macrophages. Reciprocally, caspase-1, as well as caspase-8, regulated LUBAC activity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death.

SIGNOR-272193

Q96J02

Q8N0X7

2

binding

up-regulates activity

0.2

Cytosolic endogenous spartin is mono-ubiquitinated and we demonstrate that it interacts via a PPXY motif with the ubiquitin E3 ligases AIP4 [atrophin-interacting protein 4; ITCH (itchy E3 ubiquitin protein ligase homologue] [corrected] and AIP5 (WWP1). Surprisingly, the PPXY motif, AIP4 and AIP5 are not required for spartin's ubiquitination, and so we propose that spartin acts as an adaptor for these proteins.

SIGNOR-261306

Q86SG6

2

phosphorylation

up-regulates activity

0.2

Multimerization and autophosphorylation of Nek8 are important for its activation.Our data suggests that one site for Nek8 autophosphorylation may be Thr-210 within the activation loop.

SIGNOR-250298

O43524

2

transcriptional regulation

up-regulates quantity

0.2

We show that FOXO3 binds and activates its own promoter via a positive autoregulatory feedback loop

SIGNOR-255757

Q9C035

2

monoubiquitination

up-regulates quantity

0.2

Here, we show that TRIM5alpha functions as a RING-finger-type E3 ubiquitin ligase both in vitro and in vivo and ubiquitinates itself in cooperation with the E2 ubiquitin-conjugating enzyme UbcH5B. Thus, the ubiquitination of TRIM5alpha is catalyzed by itself and Ro52. Unexpectedly, although TRIM5alpha is ubiquitinated, our results have revealed that the proteasome inhibitors MG115 and MG132 do not stabilize it in HeLa cells, suggesting that the ubiquitination of TRIM5alpha does not lead to proteasomal degradation. Importantly, TRIM5alpha is clearly conjugated by a single ubiquitin molecule (monoubiquitination). Our monoubiquitin-fusion assay suggests that monoubiquitination is a signal for TRIM5alpha to translocate from cytoplasmic bodies to the cytoplasm.

SIGNOR-271671

Q9Y572

2

phosphorylation

up-regulates activity

0.2

This suggests that Thr182 is a likely auto-phosphorylation target and may be involved in RIP3 activity.

SIGNOR-277396

Q96EP1

2

ubiquitination

down-regulates quantity by destabilization

0.2

In this study, we identified USP7 (also known as HAUSP), which is a member of a family of proteins that cleave polyubiquitin chains and/or ubiquitin precursors, as an interacting protein with Chfr by immunoaffinity purification and mass spectrometry, and their interaction greatly increases the stability of Chfr. In fact, USP7 can remove ubiquitin moiety from the autoubiquitinated Chfr both in vivo and in vitro, which results in the accumulation of Chfr in the cell. USP7 mediates deubiquitination of Chfr.

SIGNOR-271461

Q02930

2

binding

up-regulates activity

0.2

CRE-BPa specifically binds to CRE as a homodimer or heterodimer with c-Jun or CRE-BP1. In CAT cotransfection experiments using CV-1 cells, transient expression of each of four CRE-BPa proteins caused a 1.6- to 3.4-fold increase of CRE-dependent transcription

SIGNOR-219602

Q96GX5

2

phosphorylation

up-regulates activity

0.2

After this priming step, Gwl can intramolecularly phosphorylate its C-terminal tail at pS883; this site probably plays a role similar to that of the tail/Z motif of other AGC kinases.

SIGNOR-243409

P04049

2

phosphorylation

up-regulates activity

0.2

We show that phosphorylation of s621 turns over rapidly and is enriched in the activated pool of endogenous raf-1. The phosphorylation on this site can be mediated by raf-1 itself but also by other kinase(s)

SIGNOR-235770

O15151

2

ubiquitination

down-regulates quantity by destabilization

0.2

Here we demonstrate that MdmX acts as a ubiquitin ligase in vitro, being capable of autoubiquitination, as well as mediating the ubiquitination of p53.

SIGNOR-271390

P06239

2

phosphorylation

up-regulates activity

0.2

They also demonstrate that replacement of the major site of autophosphorylation of p56lck (tyrosine 394) by a phenylalanine residue abolishes the ability to activate p56lck by CD4 cross-linking, implying that this residue is critical for the positive regulation of the Lck tyrosine kinase activity by CD4.

SIGNOR-81372

Q14164

2

phosphorylation

up-regulates activity

0.2

As previously reported, IKKε underwent rapid activation by auto-phosphorylation on T501 upon IFNβ treatment of control A549 cells, which was impaired by TRIM6si (Figure 4D)

SIGNOR-276637

Q9UM73

2

phosphorylation

up-regulates activity

0.2

ALK SelectiVely Phosphorylates the First Tyrosine in Its A-Loop Peptide.

SIGNOR-250575

P00533

Q96FA3

2

polyubiquitination

up-regulates quantity by stabilization

0.2

EGFR is positively correlated with PELI1 expression in breast cancers, and its activation led to the phosphorylation of PELI1 at Tyr154 and Thr264, which subsequently activated its E3 ubiquitin ligase. Simultaneously, PELI1 physically interacted with and enhanced the stability of EGFR via the K63-linked polyubiquitination in reverse.

SIGNOR-277875

Q12851

2

phosphorylation

up-regulates activity

0.2

MAP4K2 is autophosphorylated at S170 for activation

SIGNOR-277826

P49959

Q13315

2

phosphorylation

up-regulates

0.2

In this report, we showed that atm phosphorylates a p95 peptide (ser-343) and a mre11 peptide (ser-264) in vitro, suggesting that atm may regulate the function of p95?Mre11? Rad50 repair complex in response to dna damage.

SIGNOR-73366

Q86YT6

2

polyubiquitination

down-regulates quantity by destabilization

0.2

The RING finger motifs of DIP-1 have E3 ligase activity that can auto-ubiquitinate DIP-1 in vitro. In vivo, DIP-1 is detected as a polyubiquitinated protein, suggesting that the intracellular levels of DIP-1 are regulated by the ubiquitin-proteasome system.

SIGNOR-272603

O15530

P00558

2

phosphorylation

up-regulates activity

0.2

PGK1 is an important enzyme in the metabolic glycolysis pathway, but PGK1 also phosphorylates and activates PDK1 through its protein kinase activity ( xref ).|PGK1 is an important enzyme in the metabolic glycolysis pathway, but PGK1 also phosphorylates and activates PDK1 through its protein kinase activity.

SIGNOR-280064