Identifiers
HUGO:PTEN
phosphatase and tensin homolog
HUGO:PTEN hgnc_id:HGNC:9588 HGNC:9588 ENTREZ:5728 UNIPROT:P60484
phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
HUGO:PTEN, HGNC:9588, ENTREZ:5728, UNIPROT:P60484, GENECARDS:GC10P089613
HUGO:PTEN HGNC:9588 ENTREZ:5728 UNIPROT:P60484
HUGO:PTEN HGNC:9588 ENTREZ:5728 UNIPROT:P60484 GENECARDS:PTEN REACTOME:62405 KEGG:5728 ATLASONC:PTENID158 WIKI:PTEN
phosphatase and tensin homologue
BZS, MHAM

Maps_Modules
HMC:AVOIDING_IMMUNE_DESTRUCTION
 Adaptive Immune Response   / TCR_SIGNALING 
HMC:TUMOR_PROMOTING_INFLAMMATION
HMC:ACTIVATING_INVASION_AND_METASTASIS
 Cancer Associated Fibroblasts   / CAF_INHIBITION_ANTITUMOR 
 Cancer Associated Fibroblasts   / CORE 
 EMT Senescence   / EMT_REGULATORS 
 EMT Senescence   / MITOCHONDRIA_OXIDATIVE_STRESS 
 EMT Senescence   / SENESCENCE 
HMC:RESISTING_CELL_DEATH
 Regulated Cell Death   / APOPTOSIS 
 Regulated Cell Death   / STARVATION_AUTOPHAGY 
 Regulated Cell Death   / DEATH_RECEPTOR_PATHWAYS 
 Regulated Cell Death   / DEPENDANCE_RECEPTORS 
 Regulated Cell Death   / RCD_GENES 
HMC:EVADING_GROWTH_SUPPRESSORS
 Survival   / PI3K_AKT_MTOR 
 Survival   / WNT_NON_CANONICAL 
 RECON2 

References
PMID:16982858 PMID:23732914
PMID:24254977
PMID:19847259
Fibroblast-speci???c deletion
of Pten in this manner resulted in increased primary tumour growth
the authors linked Pten loss
in ???broblasts to increased Ras???Akt signalling, as well
as increased activity of the Ets-2 transcription factor
and associated increases in expression of MMP9, an
Ets-2 target genes.
PMID:10753747
Pten regulates PI3K pathway via its phosphatase activity on phosphatidylinositol (PI) 3,4,5-trisphosphate (PI(3,4,5)P3), a product of PI 3-kinase.
Pten-deficient fibroblasts migrate faster than wild type.
there are marked increases of the GTP-bound forms of Rac1 and Cdc42 in logarithmically growing Pten???/??? cells compared to wild-type cells, although the total protein levels are not affected by the Pten status.
similar to Akt, Rac1 and Cdc42 activation in Pten???/??? cells is downstream of PI 3-kinase.
PMID:11747822
phosphorylation of Akt is elevated in the PTEN-deficient mouse embryonic fibroblasts (PTEN???/??? MEFs) compared to the level in PTEN+/??? MEFs (Figure 4b) and that the cell motility of the PTEN-deficient MEFs is higher than that of PTEN+/??? MEFs
PMID:25364523
We cultured cardiac fibroblasts of mice were in hypoxia or normoxia conditions for 12, 24 and 48 hours. At all the time points, caveolin-1 and PTEN expression were gradually reduced, whereas, ??-SMA was gradually increased.
PMID:22179046
MiR-320 is a Pten target in fibroblasts that suppresses tumor growth
Ets2 is a direct target of miR-320 in fibroblasts
Mmp9 and Emilin2 are directly regulated by miR-320 via their 3??? UTR target sequences
PMID:15721744
PMID:22465479
PMID:12040186
PMID:16288286
PMID:17218262

References
mo_re1:( motility  ) PMID:21084277 PMID:19440036 PMID:19945467 PMID:20609352 PMID:26597054 PMID:17409395 PMID:27328425 PMID:27572739 PMID:24030100

References
mo_re195:( motility  ) PMID:22677902

References
mo_re227:( motility  ) PMID:25897829

Maps_Modules
HMC:RESISTING_CELL_DEATH
 Regulated Cell Death   / APOPTOSIS 
 Regulated Cell Death   / STARVATION_AUTOPHAGY 
 Regulated Cell Death   / DEATH_RECEPTOR_PATHWAYS 
 Regulated Cell Death   / DEPENDANCE_RECEPTORS 
 Regulated Cell Death   / RCD_GENES 

References
s_akt1_re81( Survival  ):
PMID:17444818
ANNOTATION:PTEN is destabilized by phosphorylation on T366 followed by phosphorylation on S370 by GSK3beta.

References
s_akt1_re16( Survival  ):
PMID:17218261
PMID:17218260

References
s_akt1_re14( Survival  ):
PMID:17218261
PMID:17218260

References
s_akt1_re15( Survival  ):
PMID:17218261
PMID:17218260

References
s_akt1_re25( Survival  ):
PMID:17218261
PMID:17218260

References
s_akt1_re26( Survival  ):
PMID:17218261
PMID:17218260

References
s_akt1_re82( Survival  ):
PMID:17444818
ANNOTATION:PTEN is destabilized by phosphorylation on T366 followed by phosphorylation on S370 by GSK3beta.
s_akt1_re12( Survival  ):
PMID:19652529
PMID:19597351

References
s_akt1_re147( Survival  ):
PMID:11707428
phospho- rylation of the PTEN tail negatively regulates PTEN activity
PMID:11035045
phosphorylation of PTEN by CK2 is important for PTEN protein stability to proteasome-mediated degradation

References
s_akt2_re14:( Survival  ) PMID:18716620
s_akt2_re18( Survival  ):
PMID:17218262
PMID:17218252

References
s_akt2_re14:( Survival  ) PMID:18716620

1. PTEN@Autopagosome

1. PTEN@Cytoplasm
2. PTEN@Cytoplasm
3. PTEN|​emp@Cytoplasm
4. PTEN|​ubi@Cytoplasm
5. PTEN|​ubi@Cytoplasm
6. PTEN|​K13_ubi@Cytoplasm
7. PTEN|​K289_ubi@Cytoplasm
8. PTEN|​S370_pho@Cytoplasm
9. PTEN|​K289_ubi|​K13_ubi@Cytoplasm
10. PTEN|​S370_pho|​T366_pho@Cytoplasm
11. PTEN|​S370_pho|​S380_pho|​T382_pho|​T383_pho|​S385_pho@Cytoplasm

1. PTEN@Cytosol
2. PTEN|​pho|​active@Cytosol

1. PTEN@Nucleus
2. PTEN|​emp@Nucleus
3. PTEN|​ubi@Nucleus
4. PTEN|​ubi@Nucleus
5. PTEN|​K13_ubi@Nucleus
6. PTEN|​K289_ubi@Nucleus
7. PTEN|​pho|​active@Nucleus

1. PTEN@T_cell
2. PTEN|​pho@T_cell

1. PTEN|​pho|​pho|​pho|​pho:​_beta_-Arrestin*@Cytoplasm

1. NHERF1*:​PTEN|​pho@Cytosol

1. NHERF1*:​PTEN|​pho@Nucleus

1. PTEN@T_cell → T-cell_anergy@T_cell
2. PTEN@T_cell → PTEN|​pho@T_cell
3. PTEN@Cytosol → NEGATIVE_REGULATORS OF_CAF@Cytosol
4. rPTEN@Cytosol → PTEN@Cytosol
5. PTEN@Cytosol → PTEN|​pho|​active@Cytosol
6. rPTEN@Nucleus → PTEN@Cytosol
7. PTEN|​pho|​active@Cytosol → PTEN@Cytosol
8. rPTEN@Nucleus → PTEN@Nucleus
9. PTEN@Nucleus → PTEN@Cytosol
10. NHERF1*@Nucleus + PTEN|​pho|​active@Nucleus → NHERF1*:​PTEN|​pho@Nucleus
11. NHERF1*:​PTEN|​pho@Nucleus → NHERF1*:​PTEN|​pho@Cytosol
12. PTEN|​pho|​active@Cytosol → PTEN|​pho|​active@Nucleus
13. NHERF1*:​PTEN|​pho@Cytosol → Akt activation@Cytosol
14. rPTEN@Nucleus → PTEN@Cytosol
15. PTEN@Cytoplasm → PTEN@Cytoplasm
16. PTEN@Cytoplasm → PTEN|​K13_ubi@Cytoplasm
17. PTEN@Cytoplasm → PTEN|​S370_pho|​S380_pho|​T382_pho|​T383_pho|​S385_pho@Cytoplasm
18. PTEN|​K13_ubi@Cytoplasm → PTEN|​K13_ubi@Nucleus
19. PTEN|​K13_ubi@Nucleus → PTEN@Nucleus
20. PTEN|​K289_ubi@Nucleus → PTEN@Nucleus
21. PTEN@Nucleus → PTEN@Cytoplasm
22. PTEN@Cytoplasm → PTEN|​K289_ubi|​K13_ubi@Cytoplasm
23. PTEN@Cytoplasm → PTEN|​K289_ubi@Cytoplasm
24. PTEN|​K289_ubi@Cytoplasm → PTEN|​K289_ubi@Nucleus
25. PTEN@Cytoplasm → PTEN|​S370_pho@Cytoplasm
26. PTEN|​S370_pho@Cytoplasm → PTEN|​S370_pho|​T366_pho@Cytoplasm
27. PTEN|​ubi@Nucleus → PTEN|​emp@Nucleus
28. PTEN|​ubi@Nucleus → PTEN|​emp@Nucleus
29. PTEN|​emp@Nucleus → PTEN|​emp@Cytoplasm
30. PTEN|​ubi@Nucleus → Chromosome integrity and DSB repair@Nucleus
31. PTEN|​ubi@Nucleus → Chromosome integrity and DSB repair@Nucleus
32. PTEN|​ubi@Cytoplasm → PTEN|​ubi@Nucleus
33. PTEN|​ubi@Cytoplasm → PTEN|​ubi@Nucleus
34. PTEN|​pho|​pho|​pho|​pho:​_beta_-Arrestin*@Cytoplasm → PI3K AKT MTOR pathway@Cytoplasm
35. _beta_-Arrestin*@Cytoplasm + PTEN@Cytoplasm → PTEN|​pho|​pho|​pho|​pho:​_beta_-Arrestin*@Cytoplasm
36. PTEN|​pho|​pho|​pho|​pho:​_beta_-Arrestin*@Cytoplasm → Cell migration@Nucleus

1. PIP3*@T_cell → PIP2*@T_cell
2. PIP3*@Cytosol → PIP2*@Cytosol
3. gETS2@Cytosol → rETS2@Cytosol
4. gMIR320A@Cytosol → arMIR320A@Cytosol
5. PI(3)P@Cytosol → PI@Cytosol
6. AKT1@Cytosol → AKT1@Cytosol
7. PIP3@Cytosol → PIP2@Cytosol
8. AKT1|​ser473_pho|​active@Nucleus → AKT1@Nucleus
9. PIP3*@Cytosol → PIP2*@Cytosol
10. PIP3*@Autopagosome → PIP2@Autopagosome
11. p110*:​p85*@Cytoplasm + GRB2:​SOS*@Cytoplasm + PI3,4,5-P3@Lipid Raft + RTK*@Cytoplasm + GF@default + RAS*@Cytoplasm + GAB1|​Y977_pho|​Y989_pho@Cytoplasm → GAB1|​Y977_pho|​Y989_pho:​GF:​GRB2:​PI3,4,5-P3:​RAS*:​RTK*|​pho|​pho|​hm2:​SOS*:​p110*:​p85*@Lipid Raft
12. PTEN@Cytoplasm → PTEN@Cytoplasm
13. PI3,4,5-P3@Lipid Raft → PtdIns(4,5)-P2@Lipid Raft
14. gRAD51@Nucleus → rRAD51@Nucleus