Relation Results

Summary

Name PTEN
Full Name Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Synonyms Mutated in multiple advanced cancers 1, Phosphatase and tensin homolog | MMAC1, TEP1
Primary ID P60484
Links - -
Type protein
Relations 101
Pathways Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML, B-cell activation, Colorectal Carcinoma, Glioblastoma Multiforme, GPCR_CRC, GPCR_HCC, Hepatocellular Tumor, Insulin Signaling, Luminal Breast Cancer, Malignant Melanoma, MTOR Signaling, Prostate Cancer, PI3K/AKT Signaling, Thyroid cancer
Function Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also act ...
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Type: Score: Layout: SPV 
0.4410.320.4740.2420.6560.5810.6790.3370.7030.6090.20.5080.20.3760.5850.2570.4460.4270.2710.4570.4460.5410.3760.4310.4290.5960.420.8210.5410.20.3380.7170.670.4060.640.620.3590.3090.2790.3270.3860.20.3070.5720.20.20.3570.2970.2570.7320.3760.80.4240.6320.5180.2910.4610.4740.6630.3960.6890.5360.620.4420.6290.4450.2980.5540.640.2750.6830.20.7410.20.426PTENCREB1DVL2PINK1ABI1ROCK1IRS1CSNK2A1PLK3CSNK2A2STK11PBKPFKPRAB7AARIRF3NKX3-1GSK3BNCLKIF11INSRSRCLCKFGFR2FGFR3FRKPTK6PTK2BCR-ABLKDM5CPI3KMAST2SALL4AKTPREX2ABTB1PPM1ASL1 complexDUSP1MAPTNFIL3EGR2MAST3HCLS1SH2B2GLI1PTP4A3NR5A1PIK3CATET1PIP3SP1INPP4BMAST1KDM5APPARGPIK3C3NDRG1XIAPRPS6KB1STAT5AWWP2CFL1GRIN2BBMI1AKT1LIMK2PIK3CBTRIM10USP7SYVN1MKRN1

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ down-regulates activity img/direct_inhibition.png dephosphorylation CREB1 0.441
Identifier Residue Sequence Organism Cell Line
SIGNOR-248543 Ser119 EILSRRPsYRKILND Mus musculus MEF Cell
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation DVL2 0.32
Identifier Residue Sequence Organism Cell Line
SIGNOR-277035 Ser143 FHPNVSSsHENLEPE Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.474
Identifier Residue Sequence Organism Cell Line
SIGNOR-277915 Ser179 RRYVYYYsYLLKNHL Homo sapiens SKOV-3 Cell
pmid sentence
PINK1 interacts with and phosphorylates PTEN at Serine179, resulting in the activation of AKT and the inhibition of PTEN nuclear import. 
Publications: 1 Organism: Homo Sapiens
+ down-regulates quantity by destabilization img/direct_inhibition.png dephosphorylation ABI1 0.242
Identifier Residue Sequence Organism Cell Line
SIGNOR-276949 Ser216 VPNDYMTsPARLGSQ Homo sapiens
pmid sentence
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
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
+ up-regulates img/direct-activation.png phosphorylation PTEN 0.656
Identifier Residue Sequence Organism Cell Line
SIGNOR-134851 Ser229 VKIYSSNsGPTRRED Homo sapiens
pmid sentence
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
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation IRS1 0.581
Identifier Residue Sequence Organism Cell Line
SIGNOR-277078 Ser307 TRRSRTEsITATSPA Mus musculus
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.679
Identifier Residue Sequence Organism Cell Line
SIGNOR-89818 Ser370 TSVTPDVsDNEPDHY Homo sapiens
pmid sentence
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
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
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
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
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
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.337
Identifier Residue Sequence Organism Cell Line
SIGNOR-168469 Ser370 TSVTPDVsDNEPDHY Homo sapiens
pmid sentence
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
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.703
Identifier Residue Sequence Organism Cell Line
SIGNOR-251025 Ser370 TSVTPDVsDNEPDHY in vitro
pmid sentence
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
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
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.609
Identifier Residue Sequence Organism Cell Line
SIGNOR-161118 Ser380 EPDHYRYsDTTDSDP Homo sapiens
pmid sentence
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
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
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
+ up-regulates activity img/direct-activation.png dephosphorylation PTEN 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-248544 Ser380 EPDHYRYsDTTDSDP Homo sapiens
pmid sentence
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
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
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.508
Identifier Residue Sequence Organism Cell Line
SIGNOR-271472 Ser380 EPDHYRYsDTTDSDP Homo sapiens HeLa Cell
pmid sentence
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
+ img/unknown.png phosphorylation PTEN 0.609
Identifier Residue Sequence Organism Cell Line
SIGNOR-247446 Ser385 RYSDTTDsDPENEPF Homo sapiens U2-OS Cell
pmid sentence
We provide evidence suggesting that LKB1 phosphorylates PTEN at residue S385 in combination either with S380, T382 or T383
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/indirect_inhibition.png dephosphorylation PFKP 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277118 Ser386 AVRLRGRsFAGNLNT Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png dephosphorylation RAB7A 0.376
Identifier Residue Sequence Organism Cell Line
SIGNOR-276960 Ser72 AGQERFQsLGVAFYR Homo sapiens
pmid sentence
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
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
+ up-regulates activity img/indirect-activation.png dephosphorylation AR 0.585
Identifier Residue Sequence Organism Cell Line
SIGNOR-277077 Ser83 QQQQQETsPRQQQQQ Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png dephosphorylation IRF3 0.257
Identifier Residue Sequence Organism Cell Line
SIGNOR-277025 Ser97 LRLAEDRsKDPHDPH Homo sapiens
pmid sentence
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
+ up-regulates quantity by stabilization img/direct-activation.png dephosphorylation NKX3-1 0.446
Identifier Residue Sequence Organism Cell Line
SIGNOR-277026 Thr179 FQNRRYKtKRKQLSS Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.427
Identifier Residue Sequence Organism Cell Line
SIGNOR-236641 Thr366 ASSSTSVtPDVSDNE Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png dephosphorylation NCL 0.271
Identifier Residue Sequence Organism Cell Line
SIGNOR-277166 Thr84 PAKKAAVtPGKKAAA Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png dephosphorylation KIF11 0.457
Identifier Residue Sequence Organism Cell Line
SIGNOR-277000 Thr926 LDIPTGTtPQRKSYL Homo sapiens
pmid sentence
PTEN significantly reduces EG5 phosphorylation at Thr926 (XREF_FIG), suggesting PTEN may target this EG5 site for dephosphorylation.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.446
Identifier Residue Sequence Organism Cell Line
SIGNOR-276471 Tyr174 TIPSQRRyVYYYSYL in vitro
pmid sentence
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
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
+ up-regulates activity img/direct-activation.png phosphorylation PTEN 0.541
Identifier Residue Sequence Organism Cell Line
SIGNOR-275982 Tyr240 RREDKFMyFEFPQPL Homo sapiens U-251MG Cell
pmid sentence
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
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
+ up-regulates activity img/direct-activation.png phosphorylation PTEN 0.376
Identifier Residue Sequence Organism Cell Line
SIGNOR-275984 Tyr240 RREDKFMyFEFPQPL Homo sapiens U-251MG Cell
pmid sentence
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
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
+ img/unknown.png phosphorylation PTEN 0.431
Identifier Residue Sequence Organism Cell Line
SIGNOR-191793 Tyr240 RREDKFMyFEFPQPL Homo sapiens
pmid sentence
Fgfrs phosphorylate pten at tyrosine 240
Publications: 1 Organism: Homo Sapiens
+ img/unknown.png phosphorylation PTEN 0.429
Identifier Residue Sequence Organism Cell Line
SIGNOR-191797 Tyr240 RREDKFMyFEFPQPL Homo sapiens Glioblastoma Cell
pmid sentence
Fgfrs phosphorylate pten at tyrosine 240
Publications: 1 Organism: Homo Sapiens
+ up-regulates img/direct-activation.png phosphorylation PTEN 0.376
Identifier Residue Sequence Organism Cell Line
SIGNOR-116499 Tyr315 RADNDKEyLVLTLTK Homo sapiens
pmid sentence
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
+ up-regulates quantity by stabilization img/direct-activation.png phosphorylation PTEN 0.596
Identifier Residue Sequence Organism Cell Line
SIGNOR-275458 Tyr336 NKDKANRyFSPNFKV Homo sapiens MCF-7 Cell
pmid sentence
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
+ up-regulates activity img/direct-activation.png phosphorylation PTEN 0.596
Identifier Residue Sequence Organism Cell Line
SIGNOR-278244 Tyr336 NKDKANRyFSPNFKV Homo sapiens
pmid sentence
Rak Phosphorylates PTEN on Tyrosine Residue 336.|Together, these results suggested that phosphorylation on Y336 by Rak prevents PTEN degradation; loss of Rak markedly decreased the ability of PTEN to inhibit tumor cell growth.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/direct_inhibition.png dephosphorylation PTK6 0.42
Identifier Residue Sequence Organism Cell Line
SIGNOR-276975 Tyr342 RLIKEDVyLSHDHNI in vitro
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation PTK2 0.821
Identifier Residue Sequence Organism Cell Line
SIGNOR-248547 Tyr397 SVSETDDyAEIIDEE Homo sapiens Breast Cancer Cell Line
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation SRC 0.541
Identifier Residue Sequence Organism Cell Line
SIGNOR-277009 Tyr419 RLIEDNEyTARQGAK Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation BCR-ABL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260080 Homo sapiens Chronic Myeloid Leukemia Cell
pmid sentence
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
+ down-regulates quantity by repression img/indirect_inhibition.png transcriptional regulation PTEN 0.338
Identifier Residue Sequence Organism Cell Line
SIGNOR-264312 Homo sapiens
pmid sentence
KDM5C performs its oncogenic function by suppressing PTEN epigenetically.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/indirect_inhibition.png PI3K 0.717
Identifier Residue Sequence Organism Cell Line
SIGNOR-252725 Homo sapiens Neuron
pmid sentence
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
+ up-regulates img/direct-activation.png phosphorylation PTEN 0.67
Identifier Residue Sequence Organism Cell Line
SIGNOR-138051 Homo sapiens
pmid sentence
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
+ down-regulates quantity by repression img/indirect_inhibition.png transcriptional regulation PTEN 0.406
Identifier Residue Sequence Organism Cell Line
SIGNOR-255126 Homo sapiens
pmid sentence
Stem cell factor SALL4 represses the transcriptions of PTEN and SALL1 through an epigenetic repressor complex.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/indirect_inhibition.png AKT 0.64
Identifier Residue Sequence Organism Cell Line
SIGNOR-244439 Homo sapiens DU-145 Cell
pmid sentence
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
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
+ down-regulates activity img/direct_inhibition.png binding PTEN 0.62
Identifier Residue Sequence Organism Cell Line
SIGNOR-259189 Homo sapiens HEK-293 Cell
pmid sentence
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
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation ABTB1 0.359
Identifier Residue Sequence Organism Cell Line
SIGNOR-260050 Homo sapiens
pmid sentence
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
+ up-regulates img/direct-activation.png binding PPM1A 0.309
Identifier Residue Sequence Organism Cell Line
SIGNOR-178643 Homo sapiens
pmid sentence
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
+ down-regulates quantity by destabilization img/indirect_inhibition.png SL1 complex 0.279
Identifier Residue Sequence Organism Cell Line
SIGNOR-269645
pmid sentence
PTEN represses RNA Polymerase I transcription by disrupting the SL1 complex
Publications: 1
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation DUSP1 0.327
Identifier Residue Sequence Organism Cell Line
SIGNOR-260053 Homo sapiens
pmid sentence
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
+ up-regulates activity img/direct-activation.png dephosphorylation MAPT 0.386
Identifier Residue Sequence Organism Cell Line
SIGNOR-277079 Homo sapiens
pmid sentence
Reduced phosphorylation of PTEN can dramatically increase tau phosphorylation and impair the ability of tau to bind to microtubules .
Publications: 1 Organism: Homo Sapiens
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation NFIL3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260055 Homo sapiens
pmid sentence
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
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation EGR2 0.307
Identifier Residue Sequence Organism Cell Line
SIGNOR-260049 Homo sapiens
pmid sentence
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
+ img/unknown.png phosphorylation PTEN 0.572
Identifier Residue Sequence Organism Cell Line
SIGNOR-138080 Homo sapiens
pmid sentence
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
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation HCLS1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260052 Homo sapiens
pmid sentence
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
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation SH2B2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260051 Homo sapiens
pmid sentence
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
+ down-regulates img/indirect_inhibition.png GLI1 0.357
Identifier Residue Sequence Organism Cell Line
SIGNOR-157776 Homo sapiens
pmid sentence
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
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
+ down-regulates quantity by destabilization img/direct_inhibition.png dephosphorylation PTEN 0.297
Identifier Residue Sequence Organism Cell Line
SIGNOR-277010 Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation NR5A1 0.257
Identifier Residue Sequence Organism Cell Line
SIGNOR-277117 Homo sapiens
pmid sentence
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
+ down-regulates activity img/indirect_inhibition.png PIK3CA 0.732
Identifier Residue Sequence Organism Cell Line
SIGNOR-209856 Homo sapiens
pmid sentence
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
+ up-regulates quantity by expression img/direct-activation.png transcriptional regulation PTEN 0.376
Identifier Residue Sequence Organism Cell Line
SIGNOR-259096 Homo sapiens
pmid sentence
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
+ down-regulates quantity img/direct_inhibition.png chemical modification PIP3 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-228145 Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation SP1 0.424
Identifier Residue Sequence Organism Cell Line
SIGNOR-277119 Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation PTEN 0.632
Identifier Residue Sequence Organism Cell Line
SIGNOR-277018 Homo sapiens
pmid sentence
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
+ down-regulates img/direct_inhibition.png phosphorylation PTEN 0.518
Identifier Residue Sequence Organism Cell Line
SIGNOR-138003 Homo sapiens
pmid sentence
Mast1 was found to associate to pten.
Publications: 1 Organism: Homo Sapiens
+ down-regulates quantity by destabilization img/direct_inhibition.png transcriptional regulation PTEN 0.291
Identifier Residue Sequence Organism Cell Line
SIGNOR-260079 Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png PTEN 0.461
Identifier Residue Sequence Organism Cell Line
SIGNOR-251997 Homo sapiens
pmid sentence
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
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation PINK1 0.474
Identifier Residue Sequence Organism Cell Line
SIGNOR-260056 Homo sapiens
pmid sentence
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
+ up-regulates img/direct-activation.png binding PTEN 0.663
Identifier Residue Sequence Organism Cell Line
SIGNOR-164075 Homo sapiens HeLa Cell
pmid sentence
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
+ up-regulates quantity by expression img/indirect-activation.png transcriptional regulation NDRG1 0.396
Identifier Residue Sequence Organism Cell Line
SIGNOR-260054 Homo sapiens
pmid sentence
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
+ down-regulates quantity img/direct_inhibition.png ubiquitination PTEN 0.689
Identifier Residue Sequence Organism Cell Line
SIGNOR-278751 Homo sapiens
pmid sentence
Finally, we found that XIAP can directly ubiquitinate PTEN in vitro.|Overexpression of XIAP induces polyubiquitination of PTEN and proteasome dependent decrease of PTEN protein levels.
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/indirect_inhibition.png dephosphorylation RPS6KB1 0.536
Identifier Residue Sequence Organism Cell Line
SIGNOR-277080 Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png binding PREX2 0.62
Identifier Residue Sequence Organism Cell Line
SIGNOR-259190 Homo sapiens HEK-293 Cell
pmid sentence
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
+ down-regulates img/direct_inhibition.png dephosphorylation STAT5A 0.442
Identifier Residue Sequence Organism Cell Line
SIGNOR-166481 Homo sapiens
pmid sentence
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
+ down-regulates quantity by destabilization img/direct_inhibition.png ubiquitination PTEN 0.629
Identifier Residue Sequence Organism Cell Line
SIGNOR-278650 Homo sapiens
pmid sentence
We have shown that WWP2 interacts with and ubiquitylates PTEN, promoting its degradation.
Publications: 1 Organism: Homo Sapiens
+ up-regulates activity img/direct-activation.png dephosphorylation CFL1 0.445
Identifier Residue Sequence Organism Cell Line
SIGNOR-276980 Homo sapiens
pmid sentence
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
+ down-regulates activity img/direct_inhibition.png dephosphorylation GRIN2B 0.298
Identifier Residue Sequence Organism Cell Line
SIGNOR-277165 Homo sapiens
pmid sentence
GluN2B Y1472 site is dephosphorylated by PTEN .
Publications: 1 Organism: Homo Sapiens
+ down-regulates quantity by repression img/indirect_inhibition.png transcriptional regulation PTEN 0.554
Identifier Residue Sequence Organism Cell Line
SIGNOR-189040 Homo sapiens Lymphoma Cell
pmid sentence
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
+ down-regulates activity img/indirect_inhibition.png AKT1 0.64
Identifier Residue Sequence Organism Cell Line
SIGNOR-252638 Homo sapiens Leukemia Cell
pmid sentence
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.
Identifier Residue Sequence Organism Cell Line
SIGNOR-189105 Homo sapiens DU-145 Cell
pmid sentence
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
Publications: 2 Organism: Homo Sapiens
Pathways:Glioblastoma Multiforme
+ down-regulates activity img/direct_inhibition.png phosphorylation PTEN 0.275
Identifier Residue Sequence Organism Cell Line
SIGNOR-278363 Homo sapiens
pmid sentence
LIMK2 inhibits PTEN phosphatase activity in vitro and in cells.|PTEN phosphorylation and downregulation by LIMK2 promotes tumorigenesis and EMT in vivo.
Publications: 1 Organism: Homo Sapiens
+ down-regulates img/direct_inhibition.png phosphorylation PTEN 0.541
Identifier Residue Sequence Organism Cell Line
SIGNOR-103721 Homo sapiens Breast Cancer Cell
pmid sentence
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
+ down-regulates activity img/indirect_inhibition.png PIK3CB 0.683
Identifier Residue Sequence Organism Cell Line
SIGNOR-236663 Homo sapiens
pmid sentence
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
+ down-regulates quantity img/direct_inhibition.png ubiquitination PTEN 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-278729 Homo sapiens
pmid sentence
Collectively, these results indicate that TRIM10 may lead to ubiquitination and degradation of PTEN, which could be an underlying reason for AKT signalling inhibition in cardiac hypertrophy processes (Figure\u00a05D).4\n\nDISCUSSION.|In addition, we found that the effect regulated by TRIM10 was mediated by interactions with phosphatase and tensin homolog (PTEN); specifically, TRIM10 promoted PTEN ubiquitination, thus leading to AKT signalling activation.|The results showed that TRIM10 overexpression decreased PTEN expression, and MG132 reversed the reduction in PTEN (Figure\u00a05C).
Publications: 1 Organism: Homo Sapiens
+ down-regulates activity img/direct_inhibition.png deubiquitination PTEN 0.741
Identifier Residue Sequence Organism Cell Line
SIGNOR-276533
pmid sentence
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
+ down-regulates quantity by destabilization img/direct_inhibition.png ubiquitination PTEN 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-278724 Homo sapiens
pmid sentence
Secondly, HRD1 promotes PTEN ubiquitination and degradation.
Publications: 1 Organism: Homo Sapiens
+ up-regulates img/direct-activation.png binding PTEN 0.572
Identifier Residue Sequence Organism Cell Line
SIGNOR-138077 Homo sapiens
pmid sentence
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
+ down-regulates quantity by destabilization img/direct_inhibition.png ubiquitination PTEN 0.426
Identifier Residue Sequence Organism Cell Line
SIGNOR-278830 Homo sapiens
pmid sentence
EGFR/PI3K/AKT-mediated ubiquitination and degradation of PTEN are dependent on the MKRN1 E3 ligase.|In fact, epidermal growth factor-stimulated pAKT phosphorylates and subsequently stabilizes MKRN1, which then ubiquitinates and induces the degradation of PTEN.
Publications: 1 Organism: Homo Sapiens
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