Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-265749	Leu309	RRTPDYFl	in vitro
pmid	sentence
18394995	Methylation of the carboxy-terminal Leu309 in a conserved TPDYFL309 motif of the C subunit has been shown to enhance the affinity of the PP2A core enzyme for some, but not all, regulatory subunits \|The PP2A core enzyme was methylated by a PP2A-specific leucine carboxyl methyltransferase (LCMT1)

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-265748	Leu309	RRTPDYFl	in vitro
pmid	sentence
18394995	Methylation of the carboxy-terminal Leu309 in a conserved TPDYFL309 motif of the C subunit has been shown to enhance the affinity of the PP2A core enzyme for some, but not all, regulatory subunits \|Demethylation and negative regulation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to humans.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-277881	Ser109	NKFAAHIsPAQGSPK	in vitro
pmid	sentence
29945972	MS analysis revealed that PP2A dephosphorylates TFEB at several residues, including Ser-109, Ser-114, Ser-122, and Ser-211, thus facilitating TFEB activation.

Identifier	Residue	Sequence	Organism
SIGNOR-277880	Ser114	HISPAQGsPKPPPAA	in vitro
pmid	sentence
29945972	MS analysis revealed that PP2A dephosphorylates TFEB at several residues, including Ser-109, Ser-114, Ser-122, and Ser-211, thus facilitating TFEB activation.

Identifier	Residue	Sequence	Organism
SIGNOR-277878	Ser122	PKPPPAAsPGVRAGH	in vitro
pmid	sentence
29945972	MS analysis revealed that PP2A dephosphorylates TFEB at several residues, including Ser-109, Ser-114, Ser-122, and Ser-211, thus facilitating TFEB activation.

Identifier	Residue	Sequence	Organism
SIGNOR-277879	Ser211	LVGVTSSsCPADLTQ	in vitro
pmid	sentence
29945972	MS analysis revealed that PP2A dephosphorylates TFEB at several residues, including Ser-109, Ser-114, Ser-122, and Ser-211, thus facilitating TFEB activation.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277184	Ser1107	DTISNRDsYSDCNSN	Homo sapiens	HEK-293 Cell
pmid	sentence
26438819	PREX2 is dephosphorylated by PP1α and PP2A.PAK-mediated phosphorylation of PREX2 reduced GEF activity toward Rac1 by inhibiting PREX2 binding to PIP3 and Gβγ.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275669	Ser1194	GQRSRLAsMLDSDTE
pmid	sentence
23462102	Akt and PP2A reciprocally regulate the guanine nucleotide exchange factor Dock6 to control axon growth of sensory neurons\|At later developmental stages, the abundance of the kinase Akt increased, resulting in the binding of Akt to Dock6 and the phosphorylation of Dock6 at Ser(1194). \| In dorsal root ganglion neurons from mice lacking Dock6, reintroduction of Dock6 with a nonphosphorylatable S1194A mutation rescued axon extension but not branch number, whereas reintroduction of Dock6 with a phosphomimetic S1194E mutation resulted in premature branching

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247970	Ser12	KSKPKDAsQRRRSLE	Homo sapiens	U2-OS Cell
pmid	sentence
18069897	We show that PR55gamma binds c-SRC and modulates the phosphorylation of serine 12 of c-SRC, a residue we demonstrate to be required for JNK activation by c-SRC

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248635	Ser129	NEAYEMPsEEGYQDY	Homo sapiens
pmid	sentence
21562258	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

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248646	Ser155	FPLRKTVsEPNLKLR	Homo sapiens
pmid	sentence
18339811	Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. \|Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs.\|we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions.

Identifier	Residue	Sequence	Organism
SIGNOR-248647	Ser181	NPLLRKEsAPPSLRR	Homo sapiens
pmid	sentence
18339811	Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. \|Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs.\|we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions.

Identifier	Residue	Sequence	Organism
SIGNOR-248648	Ser358	WPLSRTRsEPLPPSA	Homo sapiens
pmid	sentence
18339811	Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. \|Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs.\|we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions.

Identifier	Residue	Sequence	Organism
SIGNOR-248649	Ser486	RPLSRAQsSPAAPAS	Homo sapiens
pmid	sentence
18339811	Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. \|Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs.\|we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248644	Ser1981	SLAFEEGsQSTTISS	Homo sapiens
pmid	sentence
15510216	Ionizing radiation induces autophosphorylation of the ataxia-telangiectasia mutated (ATM) protein kinase on serine 1981; however, the precise mechanisms that regulate ATM activation are not fully understood. Here, we show that the protein phosphatase inhibitor okadaic acid (OA) induces autophosphorylation of ATM on serine 1981 in unirradiated cells at concentrations that inhibit protein phosphatase 2A-like activity in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248642	Ser199	PRPEHTKsVYTRSVI	Rattus norvegicus
pmid	sentence
18586681	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). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation.

Identifier	Residue	Sequence	Organism
SIGNOR-248641	Ser57	KKDRFYRsILPGDKT	Rattus norvegicus
pmid	sentence
18586681	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). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation.

Identifier	Residue	Sequence	Organism
SIGNOR-248643	Thr423	PEQSKRStMVGTPYW	Rattus norvegicus
pmid	sentence
18586681	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). In this case we monitored two autophosphorylation sites in the Pak1 N-terminal regulatory region (Ser57 and Ser198/203) using phosphospecific antibodies: both sites showed the same kinetics of inactivation.

Publications:

3

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-168306	Ser209	DTATKSGsTTKNRFV	Homo sapiens
pmid	sentence
20927323	A recent study using genetically engineered mouse models has clearly shown that mnk-mediated eif4e phosphorylation is absolutely required for eif4e's oncogenic action. Taken together, we conclude that pp2a negatively regulates eif4e phosphorylation and eif4f complex assembly through dephosphorylation of mnk and eif4e, thus suggesting a novel mechanism by which pp2a exerts its tumor-suppressive function.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, PI3K/AKT Signaling, SARS-CoV STRESS GRANULES

Identifier	Residue	Sequence	Organism
SIGNOR-134597	Ser23	PAPIRRRsSNYRAYA	Homo sapiens
pmid	sentence
15769444	The major phosphatase thought to dephosphorylate ctni and phospholamban is type 2a protein phosphatase (pp2a) [61]. Activation of pp2a and ensuing dephosphorylation of regulatory proteins is involved in the anti-adrenergic effects of adenosine and muscarinic receptor activation see also fig2.

Identifier	Residue	Sequence	Organism
SIGNOR-134601	Ser24	APIRRRSsNYRAYAT	Homo sapiens
pmid	sentence
15769444	The major phosphatase thought to dephosphorylate ctni and phospholamban is type 2a protein phosphatase (pp2a) [61]. Activation of pp2a and ensuing dephosphorylation of regulatory proteins is involved in the anti-adrenergic effects of adenosine and muscarinic receptor activation see also fig2.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-252973	Ser253	APRRRAVsMDNSNKY	Homo sapiens
pmid	sentence
20110348	Protein phosphatase 2a reactivates foxo3a through a dynamic interplay with 14-3-3 and aktpp2a-mediated dephosphorylation of t32/s253 is required for dissociation of 14-3-3, nuclear translocation, and transcriptional activation of foxo3a.

Identifier	Residue	Sequence	Organism
SIGNOR-252971	Ser253	APRRRAVsMDNSNKY	Homo sapiens
pmid	sentence
18593906	Pp2a-mediated dephosphorylation of t32/s253 is required for dissociation of 14-3-3, nuclear translocation, and transcriptional activation of foxo3a.

Identifier	Residue	Sequence	Organism
SIGNOR-252974	Thr32	QSRPRSCtWPLQRPE	Homo sapiens
pmid	sentence
20110348	Protein phosphatase 2a reactivates foxo3a through a dynamic interplay with 14-3-3 and aktpp2a-mediated dephosphorylation of t32/s253 is required for dissociation of 14-3-3, nuclear translocation, and transcriptional activation of foxo3a.

Publications:

3

Organism:

Homo Sapiens

Pathways:

PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-163680	Ser253	APRRRAVsMDNSNKY	Homo sapiens
pmid	sentence
20110348	Protein phosphatase 2a reactivates foxo3a through a dynamic interplay with 14-3-3 and aktpp2a-mediated dephosphorylation of t32/s253 is required for dissociation of 14-3-3, nuclear translocation, and transcriptional activation of foxo3a.

Identifier	Residue	Sequence	Organism
SIGNOR-163684	Thr32	QSRPRSCtWPLQRPE	Homo sapiens
pmid	sentence
20110348	Protein phosphatase 2a reactivates foxo3a through a dynamic interplay with 14-3-3 and aktpp2a-mediated dephosphorylation of t32/s253 is required for dissociation of 14-3-3, nuclear translocation, and transcriptional activation of foxo3a.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264858	Ser284	LTFARTPsVCK	in vitro
pmid	sentence
30766540	Furthermore, FcalphaRI activation is induced by protein phosphatase 2A (PP2A) after it dephosphorylates a single serine residue (S263) in the FcalphaRI intracellular tail

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-167385	Ser291	TYVNNSPsPGFNSSH	Homo sapiens
pmid	sentence
20682773	We previously established that phosphorylation of lsf in early g1 at ser-291 and ser-309 inhibits its transcriptional activity and that dephosphorylation later in g1 is required for its reactivation. This predominant cis conformation would also limit dephosphorylation of ser-291 and ser-309 by phosphatases such as pp2a

Identifier	Residue	Sequence	Organism
SIGNOR-167389	Ser309	SLGEGNGsPNHQPEP	Homo sapiens
pmid	sentence
20682773	We previously established that phosphorylation of lsf in early g1 at ser-291 and ser-309 inhibits its transcriptional activity and that dephosphorylation later in g1 is required for its reactivation. This predominant cis conformation would also limit dephosphorylation of ser-291 and ser-309 by phosphatases such as pp2a

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-159492	Ser298	ACSSAPGsGPSSPNN	Homo sapiens
pmid	sentence
18045992	Different signal-regulated serine/threonine kinases phosphorylate class ii histone deacetylases (hdacs) to promote nuclear export, cytosolic accumulation, and activation of gene transcriptionhere we show that hdac4 forms a complex with the pp2a holoenzyme c alpha, a alpha, b/pr55 alpha. In vitro and in vivo binding studies demonstrate that the n-terminus of hdac4 interacts with the catalytic subunit of pp2a. Hdac4 is dephosphorylated by pp2a

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276379	Ser31	LKLGSGPsIKALDGR	Homo sapiens	HeLa Cell
pmid	sentence
24781523	CaMKII phosphorylates securin at PP2A substrate site(s).Securin is destabilized by phosphorylation and stabilized by PP2A-dependent dephosphorylation on separase

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276378	Ser87	PLKQKQPsFSAKKMT	Homo sapiens	HeLa Cell
pmid	sentence
24781523	CaMKII phosphorylates securin at PP2A substrate site(s).Securin is destabilized by phosphorylation and stabilized by PP2A-dependent dephosphorylation on separase

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276380	Ser89	KQKQPSFsAKKMTEK	Homo sapiens	HeLa Cell
pmid	sentence
24781523	CaMKII phosphorylates securin at PP2A substrate site(s).Securin is destabilized by phosphorylation and stabilized by PP2A-dependent dephosphorylation on separase

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276376	Thr66	ATRKALGtVNRATEK	Homo sapiens	HeLa Cell
pmid	sentence
24781523	CaMKII phosphorylates securin at PP2A substrate site(s).Securin is destabilized by phosphorylation and stabilized by PP2A-dependent dephosphorylation on separase

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248616	Ser317	ENVKYSSsQPEPRTG	Homo sapiens
pmid	sentence
17015476	Phosphorylation of Chk1 by ATR is antagonized by a Chk1-regulated protein phosphatase 2A circuit\|In response to genotoxic stress, Chk1 is phosphorylated on serines 317 (S317) and 345 (S345) by the ataxia-telangiectasia-related (ATR) protein kinase. Phosphorylation of Chk1 on these C-terminal serine residues is used as an indicator of Chk1 activation in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-248615	Ser345	LVQGISFsQPTCPDH	Homo sapiens
pmid	sentence
17015476	Phosphorylation of Chk1 by ATR is antagonized by a Chk1-regulated protein phosphatase 2A circuit\|In response to genotoxic stress, Chk1 is phosphorylated on serines 317 (S317) and 345 (S345) by the ataxia-telangiectasia-related (ATR) protein kinase. Phosphorylation of Chk1 on these C-terminal serine residues is used as an indicator of Chk1 activation in vivo.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248619	Ser37	NVLSPLPsQAMDDLM	Homo sapiens
pmid	sentence
14712210	Phosphorylation of p53 at serine 37 is important for transcriptional activity and regulation in response to DNA damage\| Furthermore, in vitro phosphatase assays show that PP2A dephosphorylates p53 at S37.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-160398	Ser387	ETGLYRIsGCDRTVK	Homo sapiens
pmid	sentence
18201571	We report here that (i) mgcracgap is phosphorylated by aurora b and cdk1, (ii) pp2a dephosphorylates aurora b and cdk1 phosphorylated sites and (iii) inhibition of pp2a abrogates mgcracgap/ect2 interaction. Therefore, pp2a may regulate cytokinesis by dephosphorylating mgcracgap and its interacting partners.

Identifier	Residue	Sequence	Organism
SIGNOR-160402	Thr588	PEHQLLKtPSSSSLS	Homo sapiens
pmid	sentence
18201571	We report here that (i) mgcracgap is phosphorylated by aurora b and cdk1, (ii) pp2a dephosphorylates aurora b and cdk1 phosphorylated sites and (iii) inhibition of pp2a abrogates mgcracgap/ect2 interaction. Therefore, pp2a may regulate cytokinesis by dephosphorylating mgcracgap and its interacting partners.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277049	Ser394	EDAVHEDsGDEDGED	Homo sapiens
pmid	sentence
30050113	In contrast, in the present work, PPP2CA reduced HDAC2 S394 phosphorylation.\|We postulated that PPP2CA would negatively regulate phospho dependent HDAC2 activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248623	Ser432	SAYGGLTsPGLSYSL	Homo sapiens	HT-29 Cell
pmid	sentence
16554440	K8 Ser431-P is a physiologic substrate to PP2A during hyposmotic conditions and possibly other biologic contexts.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248652	Ser472	RPHFPQFsYSASGRE	Mus musculus
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Identifier	Residue	Sequence	Organism
SIGNOR-248653	Ser472	RPHFPQFsYSASGRE	Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Identifier	Residue	Sequence	Organism
SIGNOR-248654	Thr305	TDAATMKtFCGTPEY	Mus musculus
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Identifier	Residue	Sequence	Organism
SIGNOR-248651	Thr305	TDAATMKtFCGTPEY	Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Publications:

4

Organism:

Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252606	Ser473	RPHFPQFsYSASGTA	Mus musculus	NIH-3T3 Cell
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Identifier	Residue	Sequence	Organism
SIGNOR-248628	Ser473	RPHFPQFsYSASGTA	Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Identifier	Residue	Sequence	Organism
SIGNOR-248626	Thr308	KDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252614	Thr308	KDGATMKtFCGTPEY	Mus musculus	NIH-3T3 Cell
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Publications:

4

Organism:

Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248627	Ser473	RPHFPQFsYSASGTA	Mus musculus
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248629	Thr308	KDGATMKtFCGTPEY	Mus musculus	NIH-3T3 Cell
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Identifier	Residue	Organism
SIGNOR-248655		Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Publications:

3

Organism:

Mus Musculus, Homo Sapiens

Pathways:

COVID-19 Causal Network, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248631	Ser474	RTHFPQFsYSASIRE	Mus musculus	NIH-3T3 Cell
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Identifier	Residue	Sequence	Organism
SIGNOR-248632	Ser474	RTHFPQFsYSASIRE	Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Identifier	Residue	Sequence	Organism
SIGNOR-248630	Thr309	SDGATMKtFCGTPEY	Homo sapiens
pmid	sentence
18160256	Overexpression of BTBD10 increased phosphorylation levels of Akts at both Thr(308) and Ser(473) while the reduction of the endogenous BTBD10 level resulted in a decrease in the phosphorylation levels of Akts. In vitro analysis indicated that BTBD10 bound to protein phosphatase 2A (PP2A) and inhibited dephosphorylation of Akts by PP2A.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248633	Thr309	SDGATMKtFCGTPEY	Mus musculus	NIH-3T3 Cell
pmid	sentence
15367694	Protein phosphatase 2A negatively regulates insulin's metabolic signaling pathway by inhibiting Akt (protein kinase B) activity in 3T3-L1 adipocytes

Publications:

4

Organism:

Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-165229	Ser520	RLQTICMsGTGMRSV	Homo sapiens
pmid	sentence
20448038	Overexpression of pp2a catalytic subunit (pp2ac) beta-isoform results in dephosphorylation of mekk3 at thr-516 and ser-520 and termination of mekk3-mediated nf-kappab activation.

Identifier	Residue	Sequence	Organism
SIGNOR-165233	Ser526	MSGTGMRsVTGTPYW	Homo sapiens
pmid	sentence
20448038	Pp2ac binds to the phosphorylated mekk3 and subsequently dephosphorylate mekk3 at thr-516, ser-520, and ser-526 residues to terminate mekk3-mediated ikkbeta/Nf-kappaB Activation

Identifier	Residue	Sequence	Organism
SIGNOR-165237	Thr516	GASKRLQtICMSGTG	Homo sapiens
pmid	sentence
20448038	Overexpression of pp2a catalytic subunit (pp2ac) beta-isoform results in dephosphorylation of mekk3 at thr-516 and ser-520 and termination of mekk3-mediated nf-kappab activation.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248223	Ser59	GGQESQPsPLALLAA	Homo sapiens
pmid	sentence
24382322	These results indicate that the signals from TCDD or OP caused PP2A-mediated dephosphorylation of Sp1 at Ser-59 and induced CYP1A1 transcription

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-137963	Ser6	sKKRKFVA	Homo sapiens
pmid	sentence
15950189	We identified that pp2a interacts with wild-type rps3, but not with mutants (s6a/t221a) (fig. 8), and that it associates with the n-terminal region of rps3 (fig. 2). From our results presented here, we conclude that pp2a is involved in the dephosphorylation of phosphorylated rps3 by pkc, and that serine 6 on the n-terminal region of rps3 appears to mediate the pp2a recruitment.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248650	Ser644	NLMFRKFsLERPFRP	Homo sapiens
pmid	sentence
21157432	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.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248638	Ser645	LNEKARLsYSDKNLI	Homo sapiens
pmid	sentence
11959144	PP2A(c) displayed the highest specific activity towards PKCdelta. The role of PP2A(c) in the dephosphorylation of PKCdelta in cells was supported by the demonstration that these proteins could be co-immunoprecipitated from NIH3T3 cells.\|In conclusion, the evidence here indicates that PKCdelta de-phosphorylation and hence inactivation is effected by PP2A with which it forms a complex

Identifier	Residue	Sequence	Organism
SIGNOR-248639	Ser664	QSAFAGFsFVNPKFE	Homo sapiens
pmid	sentence
11959144	PP2A(c) displayed the highest specific activity towards PKCdelta. The role of PP2A(c) in the dephosphorylation of PKCdelta in cells was supported by the demonstration that these proteins could be co-immunoprecipitated from NIH3T3 cells.\|In conclusion, the evidence here indicates that PKCdelta de-phosphorylation and hence inactivation is effected by PP2A with which it forms a complex

Identifier	Residue	Sequence	Organism
SIGNOR-248637	Thr507	FGESRAStFCGTPDY	Homo sapiens
pmid	sentence
11959144	PP2A(c) displayed the highest specific activity towards PKCdelta. The role of PP2A(c) in the dephosphorylation of PKCdelta in cells was supported by the demonstration that these proteins could be co-immunoprecipitated from NIH3T3 cells.\|In conclusion, the evidence here indicates that PKCdelta de-phosphorylation and hence inactivation is effected by PP2A with which it forms a complex

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248621	Ser660	QSEFEGFsFVNSEFL	Rattus norvegicus
pmid	sentence
15880462	Inhibition of PP2A increased phosphorylation at Ser660 that determines calcium sensitivity and activity of PKCbetaII isoform

Identifier	Residue	Sequence	Organism
SIGNOR-248622	Thr641	TRHPPVLtPPDQEVI	Rattus norvegicus
pmid	sentence
8749392	Specifically, the threonine at position 500 (T500) on the activation loop, and T641 and S660 on the carboxyl terminus of protein kinase C beta II are phosphorylated in vivo. T500 and S660 are selectively dephosphorylated in vitro by protein phosphatase 2A to yield an enzyme that is still capable of lipid-dependent activation, whereas all three residues are dephosphorylated by protein phosphatase 1 to yield an inactive enzyme.

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-248645	Ser67	LKSTLAMsPRQRKKM	Rattus norvegicus
pmid	sentence
11278334	In vitro and in vivo studies indicated that phospho-Ser-67 inhibitor-1 was dephosphorylated by protein phosphatases-2A and -2B. \| However, inhibitor-1 phosphorylated at Ser-67 was a less efficient substrate for cAMP-dependent protein kinase. These results demonstrate regulation of a Cdk5-dependent phosphorylation site in inhibitor-1 and suggest a role for this site in modulating the amplitude of signal transduction events that involve cAMP-dependent protein kinase activation.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-262975	Ser711	NPAKEPTsVSENEGI	in vitro
pmid	sentence
11328814	Here we incubated a recombinant preparation of the phospholipase in vitro with several enzymes including protein kinase CK2 (CK2), extracellular signal-regulated kinase 2 (ERK2), and protein phosphatase 2A (PP2A) to identify effects that might be of regulatory importance in vivo.Major findings were that 1) CK2 phosphorylated the phospholipase on serines 93, 105, and 716; 2) ERK2 phosphorylated the enzyme on serine 730; 3) there was cross-antagonism between the reactions that phosphorylated serines 716 and 730; 4) PP2A selectively hydrolyzed phosphate groups that were esterified to serines 716 and 730. The results of two independent experiments with each type of assay indicated that the incubation caused a 50% loss of phospholipase activity (TableV). These results differed from those of corresponding incubation experiments with PA-PLA1α plus ERK2 and MgATP (see “Experimental Procedures”), which provided no evidence for complex formation or phosphorylation-dependent loss of phospholipase activity

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-262976	Ser727	TIPSPVTsPVLSRRH	in vitro
pmid	sentence
11328814	Here we incubated a recombinant preparation of the phospholipase in vitro with several enzymes including protein kinase CK2 (CK2), extracellular signal-regulated kinase 2 (ERK2), and protein phosphatase 2A (PP2A) to identify effects that might be of regulatory importance in vivo.Major findings were that 1) CK2 phosphorylated the phospholipase on serines 93, 105, and 716; 2) ERK2 phosphorylated the enzyme on serine 730; 3) there was cross-antagonism between the reactions that phosphorylated serines 716 and 730; 4) PP2A selectively hydrolyzed phosphate groups that were esterified to serines 716 and 730. The results of two independent experiments with each type of assay indicated that the incubation caused a 50% loss of phospholipase activity (TableV). These results differed from those of corresponding incubation experiments with PA-PLA1α plus ERK2 and MgATP (see “Experimental Procedures”), which provided no evidence for complex formation or phosphorylation-dependent loss of phospholipase activity

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence
SIGNOR-275803	Ser74	EFEELTMsQKNGGNV
pmid	sentence
24462681	Protein phosphatase 2A regulates deoxycytidine kinase activity via Ser-74 dephosphorylation\|Deoxycytidine kinase (dCK) is a critical enzyme for activation of anticancer nucleoside analogs. Its activity is controlled via Ser-74 phosphorylation. Here, we investigated which Ser/Thr phosphatase dephosphorylates Ser-74. In cells, the PP1/PP2A inhibitor okadaic acid increased both dCK activity and Ser-74 phosphorylation

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-248624	Ser87	AAAGPALsPVPPVVH	Homo sapiens
pmid	sentence
15225643	The phosphorylation of Bcl-2 resulted in a reduction in anti-apoptotic function, implying that dephosphorylation promoted the anti-apoptotic activity of Bcl-2 protein in human tumor cell lines. Thus, the present findings suggest that ERK and PP2A are physiological regulators of Bcl-2 phosphorylation, and these enzymes exert an influence on the anti-apoptotic function of Bcl-2.phosphorylation of Bcl2 at Ser70 is proposed to be a dynamic process regulated by the sequential action of an agonist-activated Bcl2 kinase and PP2A.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273794	Ser9	SFRAARLsMRNRRND	Homo sapiens	HEK-293 Cell
pmid	sentence
20110357	Using specific pharmacological and molecular tools combined with patch-clamp current recordings, we found that in heterologously expressed HEK-293 (human embryonic kidney) cells, TRPM8 channel is inhibited by the G(i) protein/adenylate cyclase (AC)/cAMP/protein kinase A (PKA) signaling cascade. We further identified the TRPM8 S9 and T17 as two key PKA phosphorylation sites regulating TRPM8 channel activity. the intracellular serine/threonine protein phosphatase 2A (PP2A) dephosphorylates TRPM8 Ser-9 and Thr-17 inhibiting the channel activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273793	Thr17	MRNRRNDtLDSTRTL	Homo sapiens	HEK-293 Cell
pmid	sentence
20110357	Using specific pharmacological and molecular tools combined with patch-clamp current recordings, we found that in heterologously expressed HEK-293 (human embryonic kidney) cells, TRPM8 channel is inhibited by the G(i) protein/adenylate cyclase (AC)/cAMP/protein kinase A (PKA) signaling cascade. We further identified the TRPM8 S9 and T17 as two key PKA phosphorylation sites regulating TRPM8 channel activity. the intracellular serine/threonine protein phosphatase 2A (PP2A) dephosphorylates TRPM8 Ser-9 and Thr-17 inhibiting the channel activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248640	Thr117	DGCTWKGtLKEYESC	Mus musculus
pmid	sentence
17188031	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.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-138428	Thr157	IRSKPPYtDYVSTRW	Homo sapiens	HEK-293T Cell
pmid	sentence
15988018	In addition, mass spectrometry showed that pp2a treatment completely abolished the dually phosphorylated form, leaving only the singly phosphorylated form (data not shown). We conclude that a portion of ick in unstimulated and asynchronized hek293t cells is dually phosphorylated on the tdy motif.

Identifier	Residue	Sequence	Organism
SIGNOR-138432	Tyr159	SKPPYTDyVSTRWYR	Homo sapiens
pmid	sentence
15988018	In addition, mass spectrometry showed that pp2a treatment completely abolished the dually phosphorylated form, leaving only the singly phosphorylated form (data not shown). We conclude that a portion of ick in unstimulated and asynchronized hek293t cells is dually phosphorylated on the tdy motif.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-142977	Thr175	GPEDQAVtEYVATRW	Homo sapiens
pmid	sentence
16336213	Erk8 (extracellular-signal-regulated protein kinase 8) expressed in escherichia coli or insect cells was catalytically active and phosphorylated at both residues of the thr-glu-tyr motif. Dephosphorylation of the threonine residue by pp2a (protein serine/threonine phosphatase 2a) decreased erk8 activity by over 95% in vitro, whereas complete dephosphorylation of the tyrosine residue by ptp1b (protein tyrosine phosphatase 1b) decreased activity by only 15-20%

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-201266	Thr180	DTMAKRNtVIGTPFW	Homo sapiens
pmid	sentence
23431053	Rassf1a apparently protects mst1/2 against inactivation by pp2a, the phosphatases that dephosphorylate the stimulatory thr-183 and thr-180 of mst1 andmst2, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-201270	Thr183	DTMAKRNtVIGTPFW	Homo sapiens
pmid	sentence
23431053	Rassf1a apparently protects mst1/2 against inactivation by pp2a , the phosphatases that dephosphorylate the stimulatory thr-183 and thr-180 of mst1 andmst2, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103159	Thr185	HDHTGFLtEYVATRW	Homo sapiens	Dermal Fibroblast
pmid	sentence
12840032	P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3).Mapk activity is tightly regulated by phosphorylation and dephosphorylation. The activation of the mapk activity requires the dual phosphorylation of the ser/thr and tyr residues in the txy kinase activation motif (1113), and deactivation occurs through the action of either ser/thr protein phosphatase

Identifier	Residue	Sequence	Organism
SIGNOR-248625	Thr185	HDHTGFLtEYVATRW	Rattus norvegicus
pmid	sentence
7780739	Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines\|Protein phosphatase-2A was the only vanadate-insensitive phosphatase acting on Thr 183 of p42mapk or on MAPKK to be detected in PC12 cell extracts.

Publications:

2

Organism:

Homo Sapiens, Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-143052	Thr185	HDHTGFLtEYVATRW	Homo sapiens
pmid	sentence
16456541	B56-containing pp2a dephosphorylate erk and their activity is controlled by the early gene iex-1 and erk

Identifier	Residue	Organism
SIGNOR-166655		Homo sapiens
pmid	sentence
20626350	In particular, p38 mapk activity stimulates the physical association between ppa2 and mkk1/2- erk1/2 complex, leading to mkk1/2 dephosphorilation by pp2a . p38 mapks activity stimulates the physical association between pp2a and erk complex, leading to mkk1/2 dephosphorylation by pp2a.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-150369	Thr187	CDIQTHMtNNKGSAA	Homo sapiens
pmid	sentence
17079228	Our results demonstrate that pp6 specifically down-regulates tak1 through dephosphorylation of thr-187 in the activation loop, which is likely important for suppressing inflammatory responses via tak1 signaling pathways.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism
SIGNOR-144322	Thr202	HDHTGFLtEYVATRW	Homo sapiens
pmid	sentence
16456541	B56-containing pp2a dephosphorylate erk and their activity is controlled by the early gene iex-1 and erk

Identifier	Residue	Organism
SIGNOR-103162		Homo sapiens
pmid	sentence
12840032	P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248636	Thr216	RSSSSEStGTPSNPD	Mus musculus
pmid	sentence
11983168	cyclin G also binds in vivo and in vitro to Mdm2 and markedly stimulates the ability of PP2A to dephosphorylate Mdm2 at T216. Consistent with these data, cyclin G null cells have both Mdm2 that is hyperphosphorylated at T216 and markedly higher levels of p53 protein when compared to wild-type cells

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-248634	Thr231	CPKYIKWtQREKGIF	Homo sapiens
pmid	sentence
18714041	Elf-1 enhances the expression of CD3zeta, whereas it suppresses the expression of FcRgamma gene and lupus T cells have decreased amounts of DNA-binding 98 kDa form of Elf-1. We show that the aberrantly increased PP2A in lupus T cells dephosphorylates Elf-1 at Thr-231. Dephosphorylation results in limited expression and binding of the 98 kDa Elf-1 form to the CD3zeta and FcRgamma promoters. Suppression of the expression of the PP2A leads to increased expression of CD3zeta and decreased expression of FcRgamma genes and correction of the early signaling response

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-168310	Thr250	NSCTPITtPELTTPC	Homo sapiens
pmid	sentence
20927323	Moreover, a dephosphorylation assay revealed that pp2a could directly dephosphorylate mnk1 and eif4e.

Identifier	Residue	Sequence	Organism
SIGNOR-168314	Thr255	ITTPELTtPCGSAEY	Homo sapiens
pmid	sentence
20927323	Moreover, a dephosphorylation assay revealed that pp2a could directly dephosphorylate mnk1 and eif4e.

Publications:

2

Organism:

Homo Sapiens

Pathways:

PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-163688	Thr32	QSRPRSCtWPLQRPE	Homo sapiens
pmid	sentence
20110348	Pp2a-mediated dephosphorylation of t32/s253 is required for dissociation of 14-3-3, nuclear translocation, and transcriptional activation of foxo3a.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-114767	Thr450	TAQMITItPPDQDDS	Homo sapiens
pmid	sentence
11839802	Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2a and dephosphorylation of akt and glycogen synthase kinase 3 beta

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-252616	Thr450	TAQMITItPPDQDDS	Homo sapiens
pmid	sentence
11839802	Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2a and dephosphorylation of akt and glycogen synthase kinase 3 beta

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248620	Thr500	WDGVTTKtFCGTPDY	Rattus norvegicus
pmid	sentence
8749392	Specifically, the threonine at position 500 (T500) on the activation loop, and T641 and S660 on the carboxyl terminus of protein kinase C beta II are phosphorylated in vivo. T500 and S660 are selectively dephosphorylated in vitro by protein phosphatase 2A to yield an enzyme that is still capable of lipid-dependent activation, whereas all three residues are dephosphorylated by protein phosphatase 1 to yield an inactive enzyme.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-248618	Thr55	DDIEQWFtEDPGPDE	Homo sapiens
pmid	sentence
17245430	A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55\| In this study, we reported that the specific B regulatory subunits of PP2A B56gamma1 and B56gamma3 mediate dephosphorylation of p53 at Thr55. Ablation of the B56gamma protein by RNAi, which abolishes the Thr55 dephosphorylation in response to DNA damage, reduces p53 stabilization, Bax expression and cell apoptosis

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-38561	Thr57	RAGETRFtDTRKDEQ	Homo sapiens
pmid	sentence
8386634	Protein phosphatases-2a and -2c (pp-2a and pp-2c) can each efficiently dephosphorylate phosphorylated eef-2

Identifier	Residue	Sequence	Organism
SIGNOR-38566	Thr59	GETRFTDtRKDEQER	Homo sapiens
pmid	sentence
8386634	Protein phosphatases-2a and -2c (pp-2a and pp-2c) can each efficiently dephosphorylate phosphorylated eef-2

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248617	Thr68	SSLETVStQELYSIP	Homo sapiens	Ovary Cancer Cell
pmid	sentence
16596250	Protein phosphatase 2A interacts with Chk2 and regulates phosphorylation at Thr-68 after cisplatin treatment of human ovarian cancer cells\|In response to DNA damage, Chk2 is initially phosphorylated at Thr-68, which leads to its full activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-202192	Tyr307	VTRRTPDyFL	Homo sapiens	Neuron
pmid	sentence
23796501	We found that ?-Syn gene overexpression in sk-n-sh cells and primary neurons led to pp2a/c phosphorylation at y307, a known target of src kinase, and consequent phosphatase inhibition.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-182637		Homo sapiens
pmid	sentence
19061640	In the absence of the wt apc protein, phosphorylated beta-catenin is rapidly dephosphorylated by serine/threonine protein phosphatase 2a (pp2a). phosphorylated beta-catenin associated with the wild-type apc protein is recruited to the scf(beta-trcp) complex, ubiquitin conjugated, and degraded.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-265583		Homo sapiens	HEK-293 Cell
pmid	sentence
30453012	CLN8 interacts with ceramide binding proteins PP2A and I2PP2A. We showed that the phosphorylation levels of several substrates of PP2A, namely Akt, S6 kinase, and GSK3β, were decreased in CLN8 disease patient fibroblasts. This reduction can be reversed by inhibiting PP2A phosphatase activity with cantharidin, suggesting a higher PP2A activity in CLN8-deficient cells. The phosphorylation levels of PP2A substrates are decreased in the absence of CLN8.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-129752		Homo sapiens
pmid	sentence
15467457	Pocket protein family consists of the retinoblastoma tumor suppressor protein (prb) and the functionally and structurally related proteins p107 and p130./dephosphorylation of p130 and p107 in cell extracts is inhibited by concentrations of okadaic acid known to inhibit pp2a, but not pp1. Finally, the pp2a catalytic subunit pp2a/c) specifically interacts with both p130 and p107 / the cell cycle repressor activity of pocket proteins is inactivated by cdk mediated phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-260944		Homo sapiens
pmid	sentence
24726876	RACK1 Negatively Regulates the Type I IFN pathway. Here we report that IRF3 is deactivated via dephosphorylation mediated by the serine and threonine phosphatase PP2A and its adaptor protein RACK1. The PP2A-RACK1 complex negatively regulated the IRF3 pathway after LPS or poly(I:C) stimulation or Sendai virus (SeV) infection.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, SARS-CoV STRESS GRANULES

Identifier	Residue	Organism
SIGNOR-141170		Homo sapiens
pmid	sentence
16239230	Both pp2a holoenzymes were found to associate with raf1 and catalyze dephosphorylation of inhibitory phospho-ser-259. Together these findings indicate that pp2a abalphac and abdeltac holoenzymes function as positive regulators of raf1-mek1/2-erk1/2 signaling by targeting raf1.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Pathways:

COVID-19 Causal Network

Identifier	Residue	Organism
SIGNOR-166649		Homo sapiens
pmid	sentence
20626350	In particular, p38 mapk activity stimulates the physical association between ppa2 and mkk1/2- erk1/2 complex, leading to mkk1/2 dephosphorilation by pp2a.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-271467		Homo sapiens	Embryonic Fibroblast
pmid	sentence
11685209	MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-271498		Mus musculus
pmid	sentence
25546391	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.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-243442		Homo sapiens
pmid	sentence
23454242	[PP2A] ... is multifarious as it is composed of catalytic, scaffold and regulatory subunits. The catalytic and scaffold subunits have two isoforms and the regulatory subunit has four different families containing different isoforms. The regulatory subunit is the most diverse with temporal and spatial specificity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-75398		Homo sapiens
pmid	sentence
10702384	This dephosphorylation returns prb to its active, growth suppressive state.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-261698		Mus musculus	Neuron
pmid	sentence
29802198	The striatin family proteins interact with the structural (A) and catalytic (C) subunits of the protein phosphatase, PP2A, and are also termed the B‴ family of PP2A subunits (4). Within heterotrimeric PP2A complexes, striatins function as one of many regulatory B subunits thought to be responsible for substrate selection and localization of PP2A isoforms

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-243433		Homo sapiens
pmid	sentence
23454242	[PP2A] ... is multifarious as it is composed of catalytic, scaffold and regulatory subunits. The catalytic and scaffold subunits have two isoforms and the regulatory subunit has four different families containing different isoforms. The regulatory subunit is the most diverse with temporal and spatial specificity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-175719		Homo sapiens
pmid	sentence
21806989	Here we report that both the amino terminal fragment (i(2ntf);aa 1-175) and the carboxy terminal fragment (i(2ctf);aa 176-277) of i(2)(pp2a) inhibit pp2a by binding to its catalytic subunit pp2ac

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-217875		Homo sapiens
pmid	sentence
19114990	Since B_ suppresses the association of the catalytic C and regulatory A subunits of protein phosphatase 2A [94], the B_ interaction with the receptor is expected to result in enhanced protein phosphatase 2A activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-261697		Mus musculus	Neuron
pmid	sentence
29802198	The striatin family proteins interact with the structural (A) and catalytic (C) subunits of the protein phosphatase, PP2A, and are also termed the B‴ family of PP2A subunits (4). Within heterotrimeric PP2A complexes, striatins function as one of many regulatory B subunits thought to be responsible for substrate selection and localization of PP2A isoforms

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-269918		Homo sapiens
pmid	sentence
12840032	P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3).

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, PI3K/AKT Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-240719		Homo sapiens	JURKAT Cell
pmid	sentence
15897879	HOX11 also inhibited PP2A serine/threonine phosphatase activity concomitant with stimulation of the AKT/PKB signaling cascade.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-23575		Homo sapiens
pmid	sentence
2826472	Protein phosphatase 2a inactivates the mitogen-stimulated s6 kinase from swiss mouse 3t3 cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-268155		Homo sapiens
pmid	sentence
7592815	We have identified by two-hybrid interaction a new human gene family encoding PP2A B subunits. This family, denoted B56, contains three distinct genes, one of which is differentially spliced.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-129749		Homo sapiens
pmid	sentence
15467457	Pocket protein family consists of the retinoblastoma tumor suppressor protein (prb) and the functionally and structurally related proteins p107 and p130./dephosphorylation of p130 and p107 in cell extracts is inhibited by concentrations of okadaic acid known to inhibit pp2a, but not pp1. Finally, the pp2a catalytic subunit pp2a/c) specifically interacts with both p130 and p107 / the cell cycle repressor activity of pocket proteins is inactivated by cdk mediated phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-138883		Homo sapiens
pmid	sentence
16039140	Pr65/a acts as a scaffold protein for binding pp2ac and regulatory b subunits in a heterotrimeric holoenzyme

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-166652		Homo sapiens
pmid	sentence
20626350	In particular, p38 mapk activity stimulates the physical association between ppa2 and mkk1/2- erk1/2 complex, leading to mkk1/2 dephosphorilation by pp2a.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-167480		Homo sapiens
pmid	sentence
20704570	Accordingly, smad3-associated pp2a activity was found under hypoxic conditions. Hypoxia attenuated the nuclear accumulation of tgf-beta-induced smad3 but did not affect smad2. Moreover, the influence of tgf-beta on a set of smad3-activated genes was attenuated by hypoxia, and this was reversed by chemical pp2a inhibition. Our data demonstrate the existence of a smad3-specific phosphatase and identify a novel role for pp2a.

Identifier	Residue	Organism
SIGNOR-161919		Homo sapiens
pmid	sentence
19951945	Accordingly, smad3-associated pp2a activity was found under hypoxic conditions. Hypoxia attenuated the nuclear accumulation of tgf-beta-induced smad3 but did not affect smad2. Moreover, the influence of tgf-beta on a set of smad3-activated genes was attenuated by hypoxia, and this was reversed by chemical pp2a inhibition. Our data demonstrate the existence of a smad3-specific phosphatase and identify a novel role for pp2a.

Publications:

2

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Organism
SIGNOR-105783		Homo sapiens
pmid	sentence
11259586	This together with the rapid kinetics of pp1-pp2a activation following p38 activation suggests that pp1 and/or pp2a complexes are direct targets for p38-mediated phosphorylation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-153772		Homo sapiens
pmid	sentence
17374643	The alpha-isoform of the regulatory subunit a of protein phosphatase 2a (pr65alpha) as a new interaction partner of hrsl3 / we demonstrate that hrsl3 binds to the endogenous pr65alpha, thereby partially sequestering the catalytic subunit pr36 from the pr65 protein complex, and inhibiting pp2a catalytic activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-260945		Homo sapiens
pmid	sentence
24726876	RACK1 Mediates the Formation of the IRF3-RACK1-PP2A Complex and Promotes the Dephosphorylation of IRF3.Here we report that IRF3 is deactivated via dephosphorylation mediated by the serine and threonine phosphatase PP2A and its adaptor protein RACK1. The PP2A-RACK1 complex negatively regulated the IRF3 pathway after LPS or poly(I:C) stimulation or Sendai virus (SeV) infection.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, SARS-CoV STRESS GRANULES

Identifier	Residue	Organism	Cell Line
SIGNOR-217421		Homo sapiens	Melanoma Cell
pmid	sentence
11591705	Rela was dephosphorylated by a purified pp2a core enzyme, a heterodimer formed by the catalytic subunit of pp2a (pp2ac) and pr65, in a concentration-dependent manner.These data suggest that the constitutive activation of rela in melanoma cells could be due, at least in part, to the deficiency of pp2a, which exhibits decreased dephosphorylation of nf-kappa b/rela.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, SARS-CoV STRESS GRANULES

Identifier	Residue	Organism	Cell Line
SIGNOR-110959		Homo sapiens	Melanoma Cell
pmid	sentence
11591705	Rela was dephosphorylated by a purified pp2a core enzyme, a heterodimer formed by the catalytic subunit of pp2a (pp2ac) and pr65, in a concentration-dependent manner.These data suggest that the constitutive activation of rela in melanoma cells could be due, at least in part, to the deficiency of pp2a, which exhibits decreased dephosphorylation of nf-kappa b/rela.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-243424		Homo sapiens
pmid	sentence
23454242	[PP2A] ... is multifarious as it is composed of catalytic, scaffold and regulatory subunits. The catalytic and scaffold subunits have two isoforms and the regulatory subunit has four different families containing different isoforms. The regulatory subunit is the most diverse with temporal and spatial specificity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-269896		Homo sapiens
pmid	sentence
12840032	P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-271930		in vitro
pmid	sentence
25207814	Here we report that MID1 catalyzes the in vitro ubiquitination of the catalytic subunit of PP2A (PP2Ac) in the absence of alpha4. In the presence of alpha4, the level of PP2Ac ubiquitination is reduced.The high molecular weight smear pattern was not as obvious, suggesting that domains within the C-terminal half of MID1 may contribute to the polyubiquitination of PP2Ac.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-217872		Homo sapiens
pmid	sentence
19114990	Since B_ suppresses the association of the catalytic C and regulatory A subunits of protein phosphatase 2A [94], the B_ interaction with the receptor is expected to result in enhanced protein phosphatase 2A activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-244941		Homo sapiens
pmid	sentence
20626350	In particular, p38 mapk activity stimulates the physical association between ppa2 and mkk1/2- erk1/2 complex, leading to mkk1/2 dephosphorilation by pp2a.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, PI3K/AKT Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-279981		Homo sapiens	HEK-293 Cell
pmid	sentence
31694919	We also found that the miR-183 cluster activates the IFN pathway and inhibits vesicular stomatitis virus infection by directly targeting several negative regulators of IRF3 and STAT1 activities, including protein phosphatase 2A (PPP2CA) and tripartite motif-containing 27 (TRIM27).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-269940		Homo sapiens
pmid	sentence
23431053	Rassf1a apparently protects mst1/2 against inactivation by pp2a, the phosphatases that dephosphorylate the stimulatory thr-183 and thr-180 of mst1 andmst2, respectively.

Publications:

1

Organism:

Homo Sapiens

Name	PPP2CA View Modifications
Full Name	Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Synonyms	PP2A-alpha, Replication protein C, RP-C
Primary ID	P67775
Links	- -
Type	protein
Relations	136
Pathways	COVID-19 Causal Network, PI3K/AKT Signaling, SARS-CoV STRESS GRANULES, YAP/TAZ regulation
Function	PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259' (PubMed:10801873). Mediates dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint (PubMed:33108758).

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