Reviewed,
UniProtKB/Swiss-Prot Q9PUT6 (PTEN_XENLA)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN EC=3.1.3.67 EC=3.1.3.16 EC=3.1.3.48 Alternative name(s): Phosphatase and tensin homolog Mutated in multiple advanced cancers 1 | ||
| Gene names |
| ||
| Organism | Xenopus laevis (African clawed frog) | ||
| Taxonomic identifier | 8355 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Protein attributes
| Sequence length | 402 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue By similarity. UniProtKB P60484 UniProtKB O08586 |
| Catalytic activity | Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate. UniProtKB P60484 A phosphoprotein + H2O = a protein + phosphate. UniProtKB P60484 Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. UniProtKB P60484 |
| Cofactor | Magnesium By similarity. UniProtKB P60484 |
| Subunit structure | Monomer By similarity. UniProtKB P60484 |
| Subcellular location | Cytoplasm By similarity. UniProtKB P60484 |
| Sequence similarities | Contains 1 C2 tensin-type domain. Contains 1 phosphatase tensin-type domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 402 | 402 | Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN | PRO_0000227539 | |||||
Regions | |||||||||
| Domain | 14 – 184 | 171 | Phosphatase tensin-type | ||||||
| Domain | 189 – 349 | 161 | C2 tensin-type | ||||||
| Motif | 400 – 402 | 3 | PDZ-binding | ||||||
Sites | |||||||||
| Active site | 123 | 1 | Phosphocysteine intermediate Potential | ||||||
Sequences
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References
| [1] | "Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association." Lee J.-O., Yang H., Georgescu M.-M., Di Cristofano A., Maehama T., Shi Y., Dixon J.E., Pandolfi P., Pavletich N.P. Cell 99:323-334(1999) [PubMed: 10555148] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis. |
Cross-references
Sequence databases | |
|---|---|
| AF144732 mRNA. Translation: AAD46165.1. | |
| RefSeq | NP_001083831.1. |
| UniGene | Xl.561 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1D5R based on UniProtKB P60484. |
| SMR | Q9PUT6. Positions 14-350. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 399142. |
| KEGG | xla:399142. |
Organism-specific databases | |
| Xenbase | XB-FEAT-491432. pten. |
Phylogenomic databases | |
| HOVERGEN | Q9PUT6. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.16. 648. 3.1.3.48. 648. 3.1.3.67. 648. |
Family and domain databases | |
| InterPro | IPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN. IPR014019. Phosphatase_tensin-typ. IPR014020. Tensin_phosphatase_C2-dom. IPR000340. Tyr_Pase_dual_specific. [Graphical view] |
| Pfam | PF00782. DSPc. 1 hit. PF10409. PTEN_C2. 1 hit. [Graphical view] |
| PIRSF | PIRSF038025. PTEN. 1 hit. |
| PROSITE | PS51182. C2_TENSIN. 1 hit. PS51181. PPASE_TENSIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PTEN_XENLA | ||||||||
| Accession | Primary (citable) accession number: Q9PUT6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Xenopus annotation project | ||||||||

Clusters with


