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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: -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)DescriptionActionsGraphical viewLength
Active sitei123Phosphocysteine intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processApoptosis, Lipid metabolism, Neurogenesis
LigandLipid-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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002275391 – 402Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENAdd BLAST402

Post-translational modificationi

Monoubiquitinated. Deubiquitinated (By similarity).By similarity

Keywords - PTMi

Ubl conjugation

Interactioni

Subunit structurei

Monomer.By similarity

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliQ9PUT6
SMRiQ9PUT6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 184Phosphatase tensin-typePROSITE-ProRule annotationAdd BLAST171
Domaini189 – 349C2 tensin-typePROSITE-ProRule annotationAdd BLAST161

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi400 – 402PDZ-binding3

Phylogenomic databases

HOVERGENiHBG000239
KOiK01110

Family and domain databases

Gene3Di3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR017361 Bifunc_PIno_P3_Pase/Pase_PTEN
IPR000340 Dual-sp_phosphatase_cat-dom
IPR029021 Prot-tyrosine_phosphatase-like
IPR014020 Tensin_C2-dom
IPR029023 Tensin_phosphatase
IPR016130 Tyr_Pase_AS
IPR003595 Tyr_Pase_cat
PfamiView protein in Pfam
PF00782 DSPc, 1 hit
PF10409 PTEN_C2, 1 hit
PIRSFiPIRSF038025 PTEN, 1 hit
SMARTiView protein in SMART
SM01326 PTEN_C2, 1 hit
SM00404 PTPc_motif, 1 hit
SUPFAMiSSF52799 SSF52799, 1 hit
PROSITEiView protein in PROSITE
PS51182 C2_TENSIN, 1 hit
PS51181 PPASE_TENSIN, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPTEN_XENLA
AccessioniPrimary (citable) accession number: Q9PUT6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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