| + |
PPP4C | down-regulates activity 
dephosphorylation
|
PLK1 |
0.426 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277076 |
Ser137 |
LELCRRRsLLELHKR |
Homo sapiens |
|
| pmid |
sentence |
| 35546066 |
PPP4C dephosphorylated PLK1 at the S137 site, negatively regulating its activity in the DSB response in early embryonic cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP4C | up-regulates activity 
dephosphorylation
|
TP53BP1 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264451 |
Ser1618 |
LTKAADIsLDNLVEG |
in vitro |
|
| pmid |
sentence |
| 24703952 |
Here we show that 53BP1 is phosphorylated during mitosis on two residues, T1609 and S1618, located in its well-conserved ubiquitination-dependent recruitment (UDR) motif.|Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks |Depletion of PP4C, or PP4R3beta, causes persistence of phospho-T1609 and phospho-S1618 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264450 |
Thr1609 |
LGPYEAVtPLTKAAD |
in vitro |
|
| pmid |
sentence |
| 24703952 |
Here we show that 53BP1 is phosphorylated during mitosis on two residues, T1609 and S1618, located in its well-conserved ubiquitination-dependent recruitment (UDR) motif.|Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks |Depletion of PP4C, or PP4R3beta, causes persistence of phospho-T1609 and phospho-S1618 |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PPP4C | up-regulates
dephosphorylation
|
BANF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144779 |
Ser4 |
sQKHRDFV |
Homo sapiens |
|
| pmid |
sentence |
| 16495336 |
Herein, we demonstrate we demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. We have identified the major phosphatase responsible for dephosphorylation of ser-4 to be protein phosphatase 4 catalytic subunit. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203281 |
Ser4 |
sQKHRDFV |
Homo sapiens |
|
| pmid |
sentence |
| 24265311 |
Herein, we demonstrate we demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. We have identified the major phosphatase responsible for dephosphorylation of ser-4 to be protein phosphatase 4 catalytic subunit. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PPP4C | down-regulates activity
dephosphorylation
|
HDAC3 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248548 |
Ser424 |
DHDNDKEsDVEI |
Homo sapiens |
|
| pmid |
sentence |
| 15805470 |
Here we demonstrate that, in addition to protein-protein interactions with NCoR/SMRT, the activity of HDAC3 is regulated by both phosphorylation and dephosphorylation. A protein kinase CK2 phosphoacceptor site in the HDAC3 protein was identified at position Ser424, which is a nonconserved residue among the class I HDACs. Mutation of this residue was found to reduce deacetylase activity.|Significantly, both overexpression and siRNA knock-down approaches, and analysis of cells devoid of PP4c, unequivocally show that HDAC3 activity is inversely proportional to the cellular abundance of PP4(c). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP4C | up-regulates activity
dephosphorylation
|
ACACA |
0.243 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267724 |
Ser80 |
LHIRSSMsGLHLVKQ |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 25050742 |
PP4 was also found to directly interact with pACC1‑Ser79 in human HepG2 cells. In conclusion, the present study showed that PP4 may be a novel regulator in hepatic lipogenesis through dephosphorylating ACC1 on serine 79, suggesting that PP4 may be a promising therapeutic target in lipid metabolism disorders. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP4C | down-regulates activity
dephosphorylation
|
NDEL1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248550 |
Thr219 |
ASLSLPAtPVGKGTE |
Homo sapiens |
|
| pmid |
sentence |
| 18347064 |
Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and microtubule organization via NDEL1 dephosphorylation|PP4c selectively dephosphorylates NDEL1 at Cdk1 sites. We also demonstrate that PP4c negatively regulates Cdk1 activity at the centrosome.|We next examined the ability of PP4c to dephosphorylate a Cdk1 phosphorylation site, phospho-T219 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP4C | up-regulates activity
dephosphorylation
|
RELA |
0.368 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248549 |
Thr435 |
PTQAGEGtLSEALLQ |
Homo sapiens |
|
| pmid |
sentence |
| 15073167 |
Suppression of MEK/ERK signaling pathway enhances cisplatin-induced NF-kappaB activation by protein phosphatase 4-mediated NF-kappaB p65 Thr dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP4C | down-regulates activity
dephosphorylation
|
CDK1 |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277162 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18347064 |
PP4c efficiently dephosphorylates Cdk1 sites of NDEL1 but does not dephosphorylate the Aurora A site.|We also found that PP4c negatively regulates Cdk1 activity in interphase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP4C | down-regulates activity
dephosphorylation
|
TRIM28 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277163 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22732494 |
PP4 dephosphorylated pKAP1 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP4R3A | up-regulates
binding
|
PPP4C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180244 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18715871 |
Our data demonstrate that pp4r4 forms a novel cytosolic complex with pp4c, independent from the complexes containing pp4r1, pp4r2.PP4R3, and alpha4, and that the regulatory subunits of pp4c have evolved different modes of interaction with the catalytic subunit. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PPP4C
- 
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