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Q9PUT6 (PTEN_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

EC=3.1.3.16
EC=3.1.3.48
EC=3.1.3.67
Alternative name(s):
Mutated in multiple advanced cancers 1
Phosphatase and tensin homolog
Gene names
Name:pten
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement By similarity. UniProtKB P60484 UniProtKB O08586

Catalytic activity

Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate. UniProtKB P60484

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

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. Nucleus By similarity. NucleusPML body By similarity UniProtKB P60484.

Post-translational modification

Monoubiquitinated. Deubiquitinated By similarity.

Sequence similarities

Contains 1 C2 tensin-type domain.

Contains 1 phosphatase tensin-type domain.

Ontologies

Keywords
   Biological processApoptosis
Lipid metabolism
Neurogenesis
   Cellular componentCytoplasm
Nucleus
   DiseaseTumor suppressor
   LigandLipid-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMUbl conjugation
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

inositol phosphate dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from sequence or structural similarity. Source: GOC

phosphatidylinositol dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein stability

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionPDZ domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
PRO_0000227539

Regions

Domain14 – 184171Phosphatase tensin-type
Domain189 – 349161C2 tensin-type
Motif400 – 4023PDZ-binding

Sites

Active site1231Phosphocysteine intermediate Potential

Sequences

Sequence LengthMass (Da)Tools
Q9PUT6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E61315E2DAB0850F

FASTA40246,878
        10         20         30         40         50         60 
MTAIIKEFVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK 

        70         80         90        100        110        120 
HKNHYKIYNL CAERHYDTNK FSCRVAQYPF EDHNPPQLEL IKPFCEDLDQ LLSENENVAA 

       130        140        150        160        170        180 
IHCKAGKGRT GVMICAYLLH RGKFPRAQEA LDFYGEVRTR DKKGVTIPSQ RRYVYYYSYL 

       190        200        210        220        230        240 
LKNSLEYRPV PLLFHKIEFE TIPMFSGSTC NPQFVVYQLK VKIFTSTAGP KRAEKLMYFD 

       250        260        270        280        290        300 
FPQPLPVCGD IKVEFFHKQN KVMKKEKMFH FWVNTFFIPG PEEYSEKVEN GTLVGEQELD 

       310        320        330        340        350        360 
GIYSTERSDN DKEYLTLALT KNDLDKANKD KANRLFSPNF KVKLFFTKTV EESSNSEASS 

       370        380        390        400 
STSVTPDVSD NEPDHYRYSD TTDSDPENEP FDEDQITQIT KV 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF144732 mRNA. Translation: AAD46165.1.
RefSeqNP_001083831.1. NM_001090362.1.
UniGeneXl.561.

3D structure databases

ProteinModelPortalQ9PUT6.
SMRQ9PUT6. Positions 14-350.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399142.
KEGGxla:399142.

Organism-specific databases

CTD5728.
XenbaseXB-GENE-491437. pten.

Phylogenomic databases

HOVERGENHBG000239.
KOK01110.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
IPR000008. C2_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamPF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
PIRSFPIRSF038025. PTEN. 1 hit.
SUPFAMSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTEN_XENLA
AccessionPrimary (citable) accession number: Q9PUT6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families