| + |
PTEN | down-regulates activity 
dephosphorylation
|
CREB1 |
0.449 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248543 |
Ser119 |
EILSRRPsYRKILND |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 21385900 |
Our study demonstrates that PTEN can dephosphorylate CREB at Ser133 and that PTEN protein phosphatase activity is required for CREB dephosphoryation.|Moreover, we use both in vitro and in vivo experiments to show PTEN can dephosphorylate CREB in a phosphatase-dependent manner, suggesting that CREB is a substrate of PTEN nuclear phosphatase. Loss of Pten results in an elevated RNA level of multiple CREB transcriptional targets and increased cell proliferation, which can be reversed by a nonphosphorylatable CREB mutant or knockdown of CREB. These data reveal a mechanism for PTEN modulation of CREB-mediated gene transcription and cell growth. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Glioblastoma Multiforme, Malignant Melanoma, PI3K/AKT Signaling |
| + |
PTEN | down-regulates activity
dephosphorylation
|
DVL2 |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277035 |
Ser143 |
FHPNVSSsHENLEPE |
Homo sapiens |
|
| pmid |
sentence |
| 26399523 |
This showed that while both PTEN WT and the lipid phosphatase-inactive G129E mutant suppressed phosphorylation of DVL2 on serine 143 that accumulated upon PTEN knockdown, the C124S and Y138L mutants did not .|Finally, it is important to point out that while our studies show that PTEN can directly dephosphorylate DVL2 in vitro, it is possible that regulation of serine 143 phosphorylation of DVL2 by PTEN in cells may require additional protein factors, or post-translational modifications. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates quantity by destabilization
dephosphorylation
|
ABI1 |
0.243 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276949 |
Ser216 |
VPNDYMTsPARLGSQ |
Homo sapiens |
|
| pmid |
sentence |
| 32673396 |
After dephosphorylation by PTEN, Abi1 is degraded by calpains.|We demonstrate that PTEN dephosphorylation of Abi1 at Y213 and S216 results in Abi1 degradation through the calpain pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276948 |
Tyr213 |
PPTVPNDyMTSPARL |
Homo sapiens |
|
| pmid |
sentence |
| 32673396 |
After dephosphorylation by PTEN, Abi1 is degraded by calpains.|We demonstrate that PTEN dephosphorylation of Abi1 at Y213 and S216 results in Abi1 degradation through the calpain pathway. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates 
phosphorylation
|
PTEN |
0.643 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134851 |
Ser229 |
VKIYSSNsGPTRRED |
Homo sapiens |
|
| pmid |
sentence |
| 15793569 |
In addition, active rhoa is able to stimulate the phospholipid phosphatase activity of pten in human embryonic kidney cells and leukocytes, and this regulation seems to require rhoa's downstream effector, rhoa-associated kinase (rock). together with the observation that individual substitution of ser 229 and thr 223 restored some of the rescuing ability (fig. 4b), we conclude that effective regulation of pten by sdf-1 may require more than one of these residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134855 |
Thr232 |
YSSNSGPtRREDKFM |
Homo sapiens |
|
| pmid |
sentence |
| 15793569 |
In addition, active rhoa is able to stimulate the phospholipid phosphatase activity of pten in human embryonic kidney cells and leukocytes, and this regulation seems to require rhoa's downstream effector, rhoa-associated kinase (rock). together with the observation that individual substitution of ser 229 and thr 223 restored some of the rescuing ability (fig. 4b), we conclude that effective regulation of pten by sdf-1 may require more than one of these residues. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Hindbrain |
| + |
PTEN | down-regulates activity
dephosphorylation
|
IRS1 |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277078 |
Ser307 |
TRRSRTEsITATSPA |
Mus musculus |
|
| pmid |
sentence |
| 25645159 |
In contrast, IRS-1 level were significantly decreased and phosphorylation of IRS-1 at Ser 307 was strongly enhanced by PTEN knockdown, suggesting that both reduction in IRS-1 level and increase in IRS-1 phosphorylation at Ser307 upon HCV infection occurred in a PTEN dependent manner.|In contrast, IRS-1 level were significantly decreased and phosphorylation of IRS-1 at Ser-307 was strongly enhanced by PTEN knockdown, suggesting that both reduction in IRS-1 level and increase in IRS-1 phosphorylation at Ser307 upon Hepatitis C virus infection occurred in a PTEN-dependent manner. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Insulin Signaling, Luminal Breast Cancer, MTOR Signaling |
| + |
CSNK2A1 | down-regulates activity
phosphorylation
|
PTEN |
0.667 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89818 |
Ser370 |
TSVTPDVsDNEPDHY |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152348 |
Ser380 |
EPDHYRYsDTTDSDP |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89822 |
Ser385 |
RYSDTTDsDPENEPF |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250940 |
Thr366 |
ASSSTSVtPDVSDNE |
in vitro |
|
| pmid |
sentence |
| 12297295 |
We used mass spectrometric methods to identify Ser(370) and Ser(385) as in vivo phosphorylation sites of PTEN. These sites also are phosphorylated by CK2 in vitro, and phosphorylation inhibits PTEN activity towards its substrate, PIP3. We also identify a novel in vivo phosphorylation site, Thr(366). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89826 |
Thr382 |
DHYRYSDtTDSDPEN |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89830 |
Thr383 |
HYRYSDTtDSDPENE |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Publications: |
6 |
Organism: |
Homo Sapiens, In Vitro |
| + |
PLK3 | down-regulates activity
phosphorylation
|
PTEN |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168469 |
Ser370 |
TSVTPDVsDNEPDHY |
Homo sapiens |
|
| pmid |
sentence |
| 20940307 |
Plk3 phosphorylates pten on thr-366 and ser-370. Plk3-mediated phosphorylation facilitates pten stabilization, thereby negatively regulating the pi3k/pdk1/akt1 signaling axis |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168473 |
Thr366 |
ASSSTSVtPDVSDNE |
Homo sapiens |
|
| pmid |
sentence |
| 20940307 |
Plk3 phosphorylates pten on thr-366 and ser-370. Plk3-mediated phosphorylation facilitates pten stabilization, thereby negatively regulating the pi3k/pdk1/akt1 signaling axis |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK2A2 | down-regulates activity
phosphorylation
|
PTEN |
0.693 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251025 |
Ser370 |
TSVTPDVsDNEPDHY |
in vitro |
|
| pmid |
sentence |
| 12297295 |
We used mass spectrometric methods to identify Ser(370) and Ser(385) as in vivo phosphorylation sites of PTEN. These sites also are phosphorylated by CK2 in vitro, and phosphorylation inhibits PTEN activity towards its substrate, PIP3. We also identify a novel in vivo phosphorylation site, Thr(366). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251027 |
Ser385 |
RYSDTTDsDPENEPF |
in vitro |
|
| pmid |
sentence |
| 12297295 |
We used mass spectrometric methods to identify Ser(370) and Ser(385) as in vivo phosphorylation sites of PTEN. These sites also are phosphorylated by CK2 in vitro, and phosphorylation inhibits PTEN activity towards its substrate, PIP3. We also identify a novel in vivo phosphorylation site, Thr(366). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251026 |
Thr366 |
ASSSTSVtPDVSDNE |
in vitro |
|
| pmid |
sentence |
| 12297295 |
We used mass spectrometric methods to identify Ser(370) and Ser(385) as in vivo phosphorylation sites of PTEN. These sites also are phosphorylated by CK2 in vitro, and phosphorylation inhibits PTEN activity towards its substrate, PIP3. We also identify a novel in vivo phosphorylation site, Thr(366). |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PTEN | up-regulates activity
dephosphorylation
|
PTEN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248544 |
Ser380 |
EPDHYRYsDTTDSDP |
Homo sapiens |
|
| pmid |
sentence |
| 22413754 |
Overall, our results suggest that PTEN autodephosphorylation may be a critical event in this process; thus a major protein substrate for PTEN may be PTEN itself.|Various studies have demonstrated that PTEN is itself a phosphoprotein, and that the major sites of phosphorylation are found in an acidic stretch (DHYRYSDTTDSDPENE) near the C-terminus [1]. This prompted us to consider whether PTEN may autodephosphorylate these sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248546 |
Thr382 |
DHYRYSDtTDSDPEN |
Homo sapiens |
|
| pmid |
sentence |
| 22413754 |
Overall, our results suggest that PTEN autodephosphorylation may be a critical event in this process; thus a major protein substrate for PTEN may be PTEN itself.|Various studies have demonstrated that PTEN is itself a phosphoprotein, and that the major sites of phosphorylation are found in an acidic stretch (DHYRYSDTTDSDPENE) near the C-terminus [1]. This prompted us to consider whether PTEN may autodephosphorylate these sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248545 |
Thr383 |
HYRYSDTtDSDPENE |
Homo sapiens |
|
| pmid |
sentence |
| 22413754 |
Overall, our results suggest that PTEN autodephosphorylation may be a critical event in this process; thus a major protein substrate for PTEN may be PTEN itself.|Various studies have demonstrated that PTEN is itself a phosphoprotein, and that the major sites of phosphorylation are found in an acidic stretch (DHYRYSDTTDSDPENE) near the C-terminus [1]. This prompted us to consider whether PTEN may autodephosphorylate these sites |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML, B-cell activation, Colorectal Carcinoma, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, Malignant Melanoma, MTOR Signaling, Prostate Cancer, PI3K/AKT Signaling, Thyroid cancer |
| + |
STK11 | down-regulates activity
phosphorylation
|
PTEN |
0.624 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161118 |
Ser380 |
EPDHYRYsDTTDSDP |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161122 |
Thr382 |
DHYRYSDtTDSDPEN |
Homo sapiens |
|
| pmid |
sentence |
| 21779440 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161126 |
Thr383 |
HYRYSDTtDSDPENE |
Homo sapiens |
|
| pmid |
sentence |
| 18321849 |
The C-terminal tail of PTEN is also the target of mutations in tumors. As mentioned, this region contains the main phosphorylation sites mapped to residues Ser362, Thr366, Ser370, Ser380, Thr382, Thr383, and Ser385, and the kinases involved are casein kinase 2 (CK2), GSK3_, LKB1, and MAST.84,97-101 The phosphorylation of the tail has been shown to enhance PTEN stability but at the same time decrease its phosphatase activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PBK | down-regulates activity
phosphorylation
|
PTEN |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271472 |
Ser380 |
EPDHYRYsDTTDSDP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 24012691 |
PTEN is phosphorylated by TOPK and is required for mitotic entry. In addition, reduced PTEN phosphorylation levels upon TOPK knockdown correlated with decreased Akt activation (Fig. 4e) suggesting that TOPK mediated phosphorylation may lead to PTEN inactivation. By using various PTEN mutants in a kinase assay we concluded that TOPK phosphorylates PTEN at S380 residue in vitro (Fig. 4c). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK11 |
phosphorylation
|
PTEN |
0.624 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247446 |
Ser385 |
RYSDTTDsDPENEPF |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 15987703 |
We provide evidence suggesting that LKB1 phosphorylates PTEN at residue S385 in combination either with S380, T382 or T383 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity 
dephosphorylation
|
PFKP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277118 |
Ser386 |
AVRLRGRsFAGNLNT |
Homo sapiens |
|
| pmid |
sentence |
| 29038421 |
In addition, AKT phosphorylation and PFKP S386 phosphorylation and PFKP expression levels were inversely correlated with PTEN expression levels, suggesting that PTEN inhibits PFKP S386 phosphorylation and reduces PFKP stability through inhibition of AKT.|These results indicate that AKT activation resulted from PTEN loss or EGFR dependent PI3K activation induces PFKP upregulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates activity
dephosphorylation
|
RAB7A |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276960 |
Ser72 |
AGQERFQsLGVAFYR |
Homo sapiens |
|
| pmid |
sentence |
| 26869029 |
PTEN dephosphorylates Rab7 on two conserved residues S72 and Y183, which are necessary for GDP dissociation inhibitor (GDI)-dependent recruitment of Rab7 on to late endosomes and subsequent maturation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276959 |
Tyr183 |
QETEVELyNEFPEPI |
in vitro |
|
| pmid |
sentence |
| 26869029 |
PTEN dephosphorylates Rab7 on two conserved residues S72 and Y183, which are necessary for GDP dissociation inhibitor (GDI)-dependent recruitment of Rab7 on to late endosomes and subsequent maturation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, In Vitro |
| + |
PTEN | up-regulates activity 
dephosphorylation
|
AR |
0.599 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277077 |
Ser83 |
QQQQQETsPRQQQQQ |
Homo sapiens |
|
| pmid |
sentence |
| 24480624 |
Furthermore, PTEN depletion increased AR protein instability, and this effect was further enhanced by p300 silencing in LAPC4 cells .|Our data demonstrate that loss of PTEN increases AR phosphorylation at Ser81 and that Ser81 phosphorylation acts as a molecular beacon that is required for the binding of p300, a key event that subsequently leads to AR acetylation, inhibition of AR ubiquitination and AR stabilization (XREF_FIG). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Prostate Cancer |
| + |
PTEN | up-regulates activity
dephosphorylation
|
IRF3 |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277025 |
Ser97 |
LRLAEDRsKDPHDPH |
Homo sapiens |
|
| pmid |
sentence |
| 32394474 |
PTEN can dephosphorylate IRF-3 S97 residue and facilitate its nuclear import for the IFN signaling pathway (7).|PTEN expression directly increases activated IRF-3 nuclear import and subsequent interferon (IFN) synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates quantity by stabilization
dephosphorylation
|
NKX3-1 |
0.455 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277026 |
Thr179 |
FQNRRYKtKRKQLSS |
Homo sapiens |
|
| pmid |
sentence |
| 31213464 |
Loss of PTEN Accelerates NKX3.1 Degradation to Promote Prostate Cancer Progression.|PTEN was also able to dephosphorylate NKX3.1 at threonine 179, a target of protein kinase C, but not threonine residues 89 and 93, targeted by casein kinase 2 . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Prostate Cancer |
| + |
GSK3B | down-regulates activity
phosphorylation
|
PTEN |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236641 |
Thr366 |
ASSSTSVtPDVSDNE |
Homo sapiens |
|
| pmid |
sentence |
| 16107342 |
Gsk3beta Phosphorylates pten at thr-366 in intact cells phosphorylation of pten at thr-366 reduces the activity of pten in cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Insulin Signaling, MTOR Signaling, PI3K/AKT Signaling |
| + |
PTEN | up-regulates activity
dephosphorylation
|
NCL |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277166 |
Thr84 |
PAKKAAVtPGKKAAA |
Homo sapiens |
|
| pmid |
sentence |
| 28332494 |
The fact that PTEN\u03b2 interacts with nucleolin and dephosphorylates nucleolin at Thr84 raised a question as to whether nucleolin mediates PTEN\u03b2 regulation of rDNA transcription, and thus represents a direct mechanism by which PTEN\u03b2 controls ribosomal biogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates activity
dephosphorylation
|
KIF11 |
0.467 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277000 |
Thr926 |
LDIPTGTtPQRKSYL |
Homo sapiens |
|
| pmid |
sentence |
| 27492783 |
PTEN significantly reduces EG5 phosphorylation at Thr926 (XREF_FIG), suggesting PTEN may target this EG5 site for dephosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INSR | down-regulates activity
phosphorylation
|
PTEN |
0.455 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276471 |
Tyr174 |
TIPSQRRyVYYYSYL |
in vitro |
|
| pmid |
sentence |
| 23995781 |
Our results show that the kinase region of IRβ subunit physically binds to PTEN and phosphorylates on Y27 and Y174. In the current study, we discovered that IR also downregulates PTEN through tyrosine phosphorylation and suggest that Y27 and 174 are the two key tyrosines. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276470 |
Tyr27 |
GFDLDLTyIYPNIIA |
in vitro |
|
| pmid |
sentence |
| 23995781 |
Our results show that the kinase region of IRβ subunit physically binds to PTEN and phosphorylates on Y27 and Y174. In the current study, we discovered that IR also downregulates PTEN through tyrosine phosphorylation and suggest that Y27 and 174 are the two key tyrosines. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Insulin Signaling, Luminal Breast Cancer, MTOR Signaling |
| + |
SRC | up-regulates activity
phosphorylation
|
PTEN |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275982 |
Tyr240 |
RREDKFMyFEFPQPL |
Homo sapiens |
U-251MG Cell |
| pmid |
sentence |
| 11948419 |
MMAC/PTEN is tyrosine phosphorylated. U251 glioblastoma cells were cotransfected with MMAC/PTEN and either Src Lck expression plasmids.Reduced tyrosine phosphorylation of MMAC/PTEN was observed when tyrosine 240 or 315 mutants were mutated to nonphosphorylated residues (Figure 1e). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275981 |
Tyr315 |
RADNDKEyLVLTLTK |
Homo sapiens |
U-251MG Cell |
| pmid |
sentence |
| 11948419 |
MMAC/PTEN is tyrosine phosphorylated. U251 glioblastoma cells were cotransfected with MMAC/PTEN and either Src Lck expression plasmids.Reduced tyrosine phosphorylation of MMAC/PTEN was observed when tyrosine 240 or 315 mutants were mutated to nonphosphorylated residues (Figure 1e). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FGFR2 |
phosphorylation
|
PTEN |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191793 |
Tyr240 |
RREDKFMyFEFPQPL |
Homo sapiens |
|
| pmid |
sentence |
| 22891331 |
Fgfrs phosphorylate pten at tyrosine 240 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGFR3 |
phosphorylation
|
PTEN |
0.437 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191797 |
Tyr240 |
RREDKFMyFEFPQPL |
Homo sapiens |
Glioblastoma Cell |
| pmid |
sentence |
| 22891331 |
Fgfrs phosphorylate pten at tyrosine 240 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK | up-regulates activity
phosphorylation
|
PTEN |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275984 |
Tyr240 |
RREDKFMyFEFPQPL |
Homo sapiens |
U-251MG Cell |
| pmid |
sentence |
| 11948419 |
MMAC/PTEN is tyrosine phosphorylated. U251 glioblastoma cells were cotransfected with MMAC/PTEN and either Src Lck expression plasmids.Reduced tyrosine phosphorylation of MMAC/PTEN was observed when tyrosine 240 or 315 mutants were mutated to nonphosphorylated residues (Figure 1e). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275983 |
Tyr315 |
RADNDKEyLVLTLTK |
Homo sapiens |
U-251MG Cell |
| pmid |
sentence |
| 11948419 |
MMAC/PTEN is tyrosine phosphorylated. U251 glioblastoma cells were cotransfected with MMAC/PTEN and either Src Lck expression plasmids.Reduced tyrosine phosphorylation of MMAC/PTEN was observed when tyrosine 240 or 315 mutants were mutated to nonphosphorylated residues (Figure 1e). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LCK | up-regulates
phosphorylation
|
PTEN |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116499 |
Tyr315 |
RADNDKEyLVLTLTK |
Homo sapiens |
|
| pmid |
sentence |
| 11948419 |
Thus, y240a and y315a are involved in the ability of mmac/pten to dephosphorylate ptdins and regulate tumor cell growth in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FRK | up-regulates quantity by stabilization
phosphorylation
|
PTEN |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275458 |
Tyr336 |
NKDKANRyFSPNFKV |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 19345329 |
Rak phosphorylates PTEN on Tyr 336 to prevent its protein degradation. In this study, we demonstrate that the Rak tyrosine kinase physically interacts with PTEN and phosphorylates PTEN on Tyr336. Knockdown of Rak enhanced the binding of PTEN to its E3 ligase NEDD4-1 and promoted PTEN polyubiquitination, leading to PTEN protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
dephosphorylation
|
PTK6 |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276975 |
Tyr342 |
RLIKEDVyLSHDHNI |
in vitro |
|
| pmid |
sentence |
| 29142193 |
PTEN inhibits PTK6 activity and downstream signaling in prostate cancer cells.|Using an in vitro phosphatase assay, we observed that PTEN was able to dephosphorylate PTK6 at tyrosine residue 342 in a dose dependent manner. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTEN | down-regulates activity
dephosphorylation
|
PTK2 |
0.815 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248547 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 10400703 |
The tumor suppressor PTEN is a phosphatase with sequence homology to tensin. PTEN dephosphorylates phosphatidylinositol 3,4, 5-trisphosphate (PIP3) and focal adhesion kinase (FAK), and it can inhibit cell growth, invasion, migration, and focal adhesions. We investigated molecular interactions of PTEN and FAK in glioblastoma and breast cancer cells lacking PTEN. The PTEN trapping mutant D92A bound wild-type FAK, requiring FAK autophosphorylation site Tyr397 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
dephosphorylation
|
SRC |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277009 |
Tyr419 |
RLIEDNEyTARQGAK |
Homo sapiens |
|
| pmid |
sentence |
| 22482061 |
Antisense- or shRNA mediated downregulation of PTEN induced SRC Tyr416 phosphorylation, SRC activation, and ultimately elevated TZMB resistance, whereas induction of PTEN phosphatase activity directly dephosphorylated SRC Tyr416 residue and so abolished SRC activity .|These observations indicate that the loss of PTEN phosphatase activity induces SRC activation and so implicates SRC in shaping de novo TZMB resistance in PTEN deficient cells . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | down-regulates
phosphorylation
|
PTEN |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103721 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12869565 |
Activated src reduces the ability of pten to dephosphorylate phosphatidylinositols in micelles and promotes akt translocation to cellular plasma membranes but does not alter pten activity toward water-soluble phosphatidylinositols. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
HCLS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260052 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
PINK1 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260056 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
|
PIK3CA |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209856 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18794881 |
The pten tumour suppressor is a lipid and protein phosphatase that inhibits phosphoinositide 3-kinase (pi3k)-dependent by dephosphorylating phosphatidylinositol 3,4,5-trisphosphate (ptdinsp(3)). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Colorectal Carcinoma, Glioblastoma Multiforme, Luminal Breast Cancer, Malignant Melanoma, MTOR Signaling, Prostate Cancer |
| + |
MAST3 | up-regulates
binding
|
PTEN |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138077 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15951562 |
Pten binds to and is phosphorylated by mast kinases./ Pdz domain-mediated binding to pten facilitates its phosphorylation by mast kinases / pdz domain binding increases pten protein stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TET1 | up-regulates quantity by expression
transcriptional regulation
|
PTEN |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259096 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27121319 |
We also found that TET1 directly binds to the promoter region of PTEN and activates its transcription through demethylation of CpG islands |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
dephosphorylation
|
SP1 |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277119 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21603612 |
Moreover, PTEN downregulates p75NTR expression by decreasing DNA-binding activity of Sp1 .|PTEN dephosphorylates the Sp1 transcription factor , the phosphorylation status of which directly impacts its ability to bind to some DNA promoter regions , . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
MAST2 | up-regulates
phosphorylation
|
PTEN |
0.687 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138051 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15951562 |
We further demonstrate that binding of pten to specific pdz domains diminishes its degradation rate and facilitates its phosphorylation by mast kinases. Our results suggest a regulatory role of pdz domain binding on pten function by controlling its stability and phosphorylation status. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
|
PI3K |
0.707 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252725 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18794881 |
The pten tumour suppressor is a lipid and protein phosphatase that inhibits phosphoinositide 3-kinase (pi3k)-dependent by dephosphorylating phosphatidylinositol 3,4,5-trisphosphate (ptdinsp(3)). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML, B-cell activation, Hepatocellular Tumor, PI3K/AKT Signaling |
| + |
PREX2 | down-regulates activity
binding
|
PTEN |
0.606 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259189 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24367090 |
Here, we report that P-REX2 interacts with PTEN via two interfaces. In summary, P-REX2 docks to the PDZ-BD of PTEN through its C-terminal domain, reads the phosphorylation state of the PTEN tail via the DH domain, and inhibits PTEN activity by unleashing the PH domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates activity
dephosphorylation
|
MAPT |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277079 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27221467 |
Reduced phosphorylation of PTEN can dramatically increase tau phosphorylation and impair the ability of tau to bind to microtubules . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
SH2B2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260051 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
dephosphorylation
|
BCR-ABL |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260080 |
|
|
Homo sapiens |
Chronic Myeloid Leukemia Cell |
| pmid |
sentence |
| 31374292 |
PTEN targets the protein phosphatase activity of BCR-ABL. PTEN has the same function as PTP1B, which can regulate BCR-ABL dephosphorylation [13]. However, whether PTEN can mediate BCR-ABL dephosphorylation remains unknown. We found that under-expression of PTEN significantly upregulated phosphorylation level of BCR-ABL. In order to verify the mechanisms, co-IP assays were applied, demonstrating the ways in which PTEN and BCR-ABL interact with each other. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML |
| + |
PTEN | down-regulates activity
dephosphorylation
|
RPS6KB1 |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277080 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19436944 |
Expression of WT-PTEN also caused decreased activation of Akt, p70 S6K, and Erk signaling pathways.|This may potentially be a result of PTEN inhibition of p70 S6K phosphorylation and may explain the mechanism by which PTEN inhibits proliferation of HSCs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Insulin Signaling, MTOR Signaling |
| + |
MAST3 |
phosphorylation
|
PTEN |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138080 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15951562 |
Furthermore, binding of PTEN to the PDZ domains from microtubule-associated serine/threonine kinases facilitated PTEN phosphorylation at its C terminus by these kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
|
AKT |
0.656 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244439 |
|
|
Homo sapiens |
DU-145 Cell |
| pmid |
sentence |
| 19903340 |
PTEN-mediated suppression of the PI3K/AKT pathway is well established, accumulating evidence suggests that nuclear PTEN also plays a critical role in tumor suppression |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166478 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 20596030 |
Exposure of eol-1r cells to imatinib failed to dephosphorylate akt, erk and stat5, although pdgfralpha was effectively inactivated. The forced expression of pten negatively regulated these signal pathways and sensitized eol-1r cells to imatinib. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, B-cell activation, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, Malignant Melanoma, MTOR Signaling, Prostate Cancer, PI3K/AKT Signaling, Thyroid cancer |
| + |
PTEN | down-regulates
|
GLI1 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157776 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17845852 |
Moreover, suppressors of ras akt function, such as the tumor-suppressor pten, and the attenuation of ras signaling involved in senescence, could be thus viewed as modulators of the gli code |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151134 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17157787 |
Moreover, suppressors of ras akt function, such as the tumor-suppressor pten, and the attenuation of ras signaling involved in senescence, could be thus viewed as modulators of the gli code |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
KDM5C | down-regulates quantity by repression
transcriptional regulation
|
PTEN |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264312 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30921702 |
KDM5C performs its oncogenic function by suppressing PTEN epigenetically. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
|
AKT1 |
0.656 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189105 |
|
|
Homo sapiens |
DU-145 Cell |
| pmid |
sentence |
| 19903340 |
PTEN-mediated suppression of the PI3K/AKT pathway is well established, accumulating evidence suggests that nuclear PTEN also plays a critical role in tumor suppression |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252638 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 20596030 |
Exposure of eol-1r cells to imatinib failed to dephosphorylate akt, erk and stat5, although pdgfralpha was effectively inactivated. The forced expression of pten negatively regulated these signal pathways and sensitized eol-1r cells to imatinib. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glioblastoma Multiforme |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
NFIL3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260055 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KDM5A | down-regulates quantity by destabilization
transcriptional regulation
|
PTEN |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260079 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31374292 |
The retinoblastoma binding protein 2 (RBP2) belongs to the KDM5 family, and is also known as JARID1A or KDM5A. We found that histone H3 lysine 4 (H3K4) demethylase RBP2 expression is negatively correlated with BCR-ABL expression, which suggests a regulatory link between these two genes. We also discovered that RBP2 mediates the dephosphorylation of BCR-ABL by directly downregulating PTEN expression, depending on histone demethylase activity, while PTEN targets protein phosphatase activity of BCR-ABL, a phosphatase which directly dephosphorylates BCR-ABL. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML |
| + |
PTEN | up-regulates activity
dephosphorylation
|
CFL1 |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276980 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22317922 |
Unexpectedly, cofilin-1 activation by PGE 2 was mediated by the protein phosphatase activity of PTEN (phosphatase and tensin homolog deleted on chromosome 10), with which it directly associated.|Unexpectedly, cofilin-1 dephosphorylation and activation in our model was mediated by the protein phosphatase activity of PTEN. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INPP4B | down-regulates activity
dephosphorylation
|
PTEN |
0.618 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277018 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26411369 |
In support, the increase in PTEN caused by INPP4B knockdown was associated with increased phosphorylation of the Ser380, Thr382, Thr383 and Ser385 cluster of the protein (XREF_FIG), which is known to increase PTEN half-life, in colon cancer cells.|Exogenous INPP4B could pull down and dephosphorylate endogenous PTEN, suggesting that effect of INPP4B on PTEN in colon cancer cells is not due to cell-type-specific characteristics of INPP4B per se.|INPP4B downregulates PTEN in colon cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAST1 | down-regulates
phosphorylation
|
PTEN |
0.53 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138003 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15951562 |
Mast1 was found to associate to pten. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
NDRG1 |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260054 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
USP7 | down-regulates activity
deubiquitination
|
PTEN |
0.731 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276533 |
|
|
|
|
| pmid |
sentence |
| 24317448 |
BCR-ABL disrupts PTEN nuclear-cytoplasmic shuttling through phosphorylation-dependent activation of HAUSP|hese data indicate that BCR-ABL phosphorylation of HAUSP modulates HAUSP’s deubiquitinase activity toward PTEN. |
|
| Publications: |
1 |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
ABTB1 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260050 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
|
PIK3CB |
0.671 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236663 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18794881 |
The pten tumour suppressor is a lipid and protein phosphatase that inhibits phosphoinositide 3-kinase (pi3k)-dependent by dephosphorylating phosphatidylinositol 3,4,5-trisphosphate (ptdinsp(3)). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Insulin Signaling |
| + |
PPARG | down-regulates activity
|
PTEN |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251997 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23128507 |
The PAX8-PPARγ rearrangement leads to strong induction of the PPARγ protein and the consequent abrogation of the normal PPARγ function. PPARγ overexpression abolishes the PTEN-inhibitory effect on immunoactive AKT, which in turn induces the PI3K signaling pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | MTOR Signaling, Prostate Cancer, Thyroid cancer |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
EGR2 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260049 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates
binding
|
PPM1A |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178643 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18482992 |
Upon complex formation with pten, ppm1a is protected from degradation induced by the tgf-? Signaling. this study establishes a novel role for nuclear pten in the stabilization of ppm1a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates quantity
chemical modification
|
PIP3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-228145 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11875759 |
PTEN dephosphorylates PI3P, lowering its cellular levels and resulting in the down-regulation of AKT. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, B-cell activation, Glioblastoma Multiforme, Hepatocellular Tumor, Insulin Signaling, Malignant Melanoma, MTOR Signaling, Prostate Cancer, PI3K/AKT Signaling, Thyroid cancer |
| + |
BMI1 | down-regulates quantity by repression
transcriptional regulation
|
PTEN |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189040 |
|
|
Homo sapiens |
Lymphoma Cell |
| pmid |
sentence |
| 19884659 |
Chromatin immunoprecipitation assays revealed the bmi-1 transcriptionally downregulated expression of the tumor suppressor pten in tumor cells through direct association with the pten locus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates
dephosphorylation
|
STAT5A |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166481 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20596030 |
The forced expression of pten in the eol-1r cells dephosphorylated akt, erk and stat5 /eol-1r cells showed epigenetic silencing of the phosphatase and tensin homolog deleted on chromosome ten (pten) gene. Exposure of eol-1r cells to imatinib failed to dephosphorylate akt, erk and stat5, although pdgfr? Was effectively inactivated. The forced expression of pten negatively regulated these signal pathways and sensitized eol-1r cells to imatinib. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML, B-cell activation |
| + |
PIK3C3 | up-regulates
binding
|
PTEN |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164075 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20212113 |
Direct positive regulation of pten by the p85 subunit of phosphatidylinositol 3-kinase.Thus p85 regulates both p110-pi3k and pten-phosphatase enzymes through direct interaction |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SALL4 | down-regulates quantity by repression
transcriptional regulation
|
PTEN |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255126 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19440552 |
Stem cell factor SALL4 represses the transcriptions of PTEN and SALL1 through an epigenetic repressor complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates quantity by expression
transcriptional regulation
|
DUSP1 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260053 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates quantity by destabilization
|
SL1 complex |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269645 |
|
|
|
|
| pmid |
sentence |
| 16055704 |
PTEN represses RNA Polymerase I transcription by disrupting the SL1 complex |
|
| Publications: |
1 |
| + |
PTEN | down-regulates activity
binding
|
PREX2 |
0.606 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259190 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25829446 |
Here, we used cell biology, biochemistry, and genetic approaches to show that PTEN suppresses cell movement by blocking PREX2 GEF–catalyzed activation of the GTPase RAC1. PTEN binds PREX2 and directly inhibits GEF activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
dephosphorylation
|
GRIN2B |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277165 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33348808 |
GluN2B Y1472 site is dephosphorylated by PTEN . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTP4A3 | down-regulates quantity by destabilization
dephosphorylation
|
PTEN |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277010 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29266303 |
As expected, PRL3 clearly reduced PTEN phosphorylation at the tyrosine residue and PTEN protein in PRL3 overexpressing LO2 and HepG2 cell lines, with no significant changes in PRL3 (C104S) mutant cells.|PRL3 down-regulates PTEN expression, a negative regulator of the Akt pathway.11 Phosphorylation of PTEN at Tyr336 is required for maintenance of PTEN protein stability and prevention of PTEN degradation.17 We therefore speculated that PRL3 might dephosphorylate PTEN at tyrosine sites and consequently reduce the PTEN protein level. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | down-regulates activity
dephosphorylation
|
NR5A1 |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277117 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27838257 |
The fact that SF-1 and PIP3 is robustly dephosphorylated by PTEN, yet SF-1 and PIP2 is resistant to phosphorylation by p110 PI3-kinases, suggests that nuclear proteins like SF-1 can help decouple PTEN signaling in the nucleus from p110 signaling.|We also showed that PTEN can dephosphorylate the SF-1 and PIP3 product of the IPMK reaction, and that PTEN inhibits SF-1 transcriptional activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTEN
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