Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9PUT6

- PTEN_XENLA

UniProt

Q9PUT6 - PTEN_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

Gene

pten

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate.By similarity
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.By similarity

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei123 – 1231Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity Source: UniProtKB
  2. lipid binding Source: UniProtKB-KW
  3. magnesium ion binding Source: InterPro
  4. PDZ domain binding Source: UniProtKB
  5. phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity Source: UniProtKB
  6. phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity Source: UniProtKB
  7. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
  8. protein serine/threonine phosphatase activity Source: UniProtKB
  9. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
  10. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. inositol phosphate dephosphorylation Source: UniProtKB
  3. negative regulation of cell migration Source: UniProtKB
  4. negative regulation of cell proliferation Source: UniProtKB
  5. negative regulation of focal adhesion assembly Source: UniProtKB
  6. negative regulation of protein kinase B signaling Source: UniProtKB
  7. peptidyl-tyrosine dephosphorylation Source: GOC
  8. phosphatidylinositol dephosphorylation Source: UniProtKB
  9. protein dephosphorylation Source: UniProtKB
  10. protein kinase B signaling Source: UniProtKB
  11. regulation of neuron projection development Source: UniProtKB
  12. regulation of protein stability Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Apoptosis, Lipid metabolism, Neurogenesis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ptenImported
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-491437. pten.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. NucleusPML body By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENPRO_0000227539Add
BLAST

Post-translational modificationi

Monoubiquitinated. Deubiquitinated (By similarity).By similarity

Keywords - PTMi

Ubl conjugation

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9PUT6.
SMRiQ9PUT6. Positions 14-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 184171Phosphatase tensin-typePROSITE-ProRule annotationAdd
BLAST
Domaini189 – 349161C2 tensin-typePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi400 – 4023PDZ-binding

Sequence similaritiesi

Contains 1 C2 tensin-type domain.PROSITE-ProRule annotation
Contains 1 phosphatase tensin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG000239.
KOiK01110.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR017361. 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]
PfamiPF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
PIRSFiPIRSF038025. PTEN. 1 hit.
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9PUT6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTAIIKEFVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI
60 70 80 90 100
DDVVRFLDSK HKNHYKIYNL CAERHYDTNK FSCRVAQYPF EDHNPPQLEL
110 120 130 140 150
IKPFCEDLDQ LLSENENVAA IHCKAGKGRT GVMICAYLLH RGKFPRAQEA
160 170 180 190 200
LDFYGEVRTR DKKGVTIPSQ RRYVYYYSYL LKNSLEYRPV PLLFHKIEFE
210 220 230 240 250
TIPMFSGSTC NPQFVVYQLK VKIFTSTAGP KRAEKLMYFD FPQPLPVCGD
260 270 280 290 300
IKVEFFHKQN KVMKKEKMFH FWVNTFFIPG PEEYSEKVEN GTLVGEQELD
310 320 330 340 350
GIYSTERSDN DKEYLTLALT KNDLDKANKD KANRLFSPNF KVKLFFTKTV
360 370 380 390 400
EESSNSEASS STSVTPDVSD NEPDHYRYSD TTDSDPENEP FDEDQITQIT

KV
Length:402
Mass (Da):46,878
Last modified:May 1, 2000 - v1
Checksum:iE61315E2DAB0850F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144732 mRNA. Translation: AAD46165.1.
RefSeqiNP_001083831.1. NM_001090362.1.
UniGeneiXl.561.

Genome annotation databases

GeneIDi399142.
KEGGixla:399142.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144732 mRNA. Translation: AAD46165.1 .
RefSeqi NP_001083831.1. NM_001090362.1.
UniGenei Xl.561.

3D structure databases

ProteinModelPortali Q9PUT6.
SMRi Q9PUT6. Positions 14-350.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 399142.
KEGGi xla:399142.

Organism-specific databases

CTDi 5728.
Xenbasei XB-GENE-491437. pten.

Phylogenomic databases

HOVERGENi HBG000239.
KOi K01110.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR017361. 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 ]
Pfami PF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view ]
PIRSFi PIRSF038025. PTEN. 1 hit.
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEi PS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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: TestisImported.

Entry informationi

Entry nameiPTEN_XENLA
AccessioniPrimary (citable) accession number: Q9PUT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3