A0A8V8TQX2 · A0A8V8TQX2_HUMAN
- ProteinPhosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- GenePTEN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids388 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for PtdIns(3,4,5)P3.
Catalytic activity
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphateThis reaction proceeds in the forward direction.
- 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 109 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | dendritic spine | |
Cellular Component | PML body | |
Cellular Component | postsynaptic density | |
Molecular Function | inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity | |
Molecular Function | phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity | |
Molecular Function | phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity | |
Molecular Function | phosphatidylinositol-3-phosphate phosphatase activity | |
Molecular Function | protein tyrosine phosphatase activity | |
Biological Process | apoptotic process | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | nervous system development | |
Biological Process | phosphatidylinositol dephosphorylation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A8V8TQX2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,016 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 351 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 355 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-170 | Phosphatase tensin-type | ||||
Sequence: RRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVSCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNH | ||||||
Domain | 87-158 | Tyrosine specific protein phosphatases | ||||
Sequence: KPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRR | ||||||
Domain | 175-335 | C2 tensin-type | ||||
Sequence: PVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKT | ||||||
Region | 337-388 | Disordered | ||||
Sequence: EEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV | ||||||
Compositional bias | 338-355 | Polar residues | ||||
Sequence: EPSNPEASSSTSVTPDVS | ||||||
Compositional bias | 356-370 | Basic and acidic residues | ||||
Sequence: DNEPDHYRYSDTTDS |
Sequence similarities
Belongs to the PTEN phosphatase protein family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length388
- Mass (Da)45,195
- Last updated2022-12-14 v1
- ChecksumA2CB4139D5698596
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P60484 | PTEN_HUMAN | PTEN | 403 | ||
A0AAQ5BGY7 | A0AAQ5BGY7_HUMAN | PTEN | 83 | ||
A0AAQ5BH13 | A0AAQ5BH13_HUMAN | PTEN | 434 | ||
A0AA34QVZ8 | A0AA34QVZ8_HUMAN | PTEN | 344 | ||
A0A9L9PYJ2 | A0A9L9PYJ2_HUMAN | PTEN | 44 | ||
A0A8V8TPK6 | A0A8V8TPK6_HUMAN | PTEN | 434 | ||
A0A8V8TP77 | A0A8V8TP77_HUMAN | PTEN | 172 | ||
A0A8I5KSF9 | A0A8I5KSF9_HUMAN | PTEN | 576 | ||
A0A8I5KR36 | A0A8I5KR36_HUMAN | PTEN | 73 | ||
A0A8I5KVQ8 | A0A8I5KVQ8_HUMAN | PTEN | 190 | ||
A0A087X033 | A0A087X033_HUMAN | PTEN | 344 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 338-355 | Polar residues | ||||
Sequence: EPSNPEASSSTSVTPDVS | ||||||
Compositional bias | 356-370 | Basic and acidic residues | ||||
Sequence: DNEPDHYRYSDTTDS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC063965 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF455271 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |