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P60484 (PTEN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:MMAC1, TEP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement. Ref.1 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.21 Ref.25 Ref.31

Catalytic activity

Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate. Ref.1 Ref.12 Ref.13 Ref.14

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.1 Ref.12 Ref.13 Ref.14

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.1 Ref.12 Ref.13 Ref.14

Cofactor

Magnesium.

Subunit structure

Monomer. The unphosphorylated form interacts with the second PDZ domain of AIP1 and with DLG1 and MAST2 in vitro. Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5. Interaction with MAGI2 increases protein stability. Interacts with NEDD4. Interacts with NDFIP1 and NDFIP2; in the presence of NEDD4 or ITCH, this interaction promotes PTEN ubiquitination. Interacts (via C2 domain) with FRK. Interacts with USP7; the interaction is direct. Interacts with ROCK1 By similarity. Interacts with XIAP/BIRC4. Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.33

Subcellular location

Cytoplasm. Nucleus. NucleusPML body. Note: Monoubiquitinated form is nuclear. Nonubiquitinated form is cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies. XIAP/BIRC4 promotes its nuclear localization. Ref.1 Ref.25 Ref.27

Tissue specificity

Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas. Ref.2

Induction

Down-regulated by TGFB1. Ref.1

Domain

The C2 domain binds phospholipid membranes in vitro in a Ca2+-independent manner; this binding is important for its tumor suppressor function. Ref.16 Ref.33

Post-translational modification

Constitutively phosphorylated by CK2 under normal conditions. Phosphorylated in vitro by MAST1, MAST2 and MAST3. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding to NEDD4. Phosphorylation by ROCK1 is essential for its stability and activity. Phosphorylation by PLK3 promotes its stability and prevents its degradation by the proteasome. Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.26 Ref.28

Monoubiquitinated; monoubiquitination is increased in presence of retinoic acid. Deubiquitinated by USP7; leading to its nuclear exclusion. Monoubiquitination of one of either Lys-13 and Lys-289 amino acid is sufficient to modulate PTEN compartmentalization. Ubiquitinated by XIAP/BIRC4. Ref.25 Ref.27

Involvement in disease

Cowden syndrome 1 (CWS1) [MIM:158350]: An autosomal dominant hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.14 Ref.34 Ref.35 Ref.37 Ref.38 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.51 Ref.54 Ref.56

Lhermitte-Duclos disease (LDD) [MIM:158350]: A rare disease characterized by the occurrence of a slowly enlarging mass within the cerebellar cortex corresponding histologically to a cerebellar hamartoma. It manifests, most commonly in the third and fourth decades of life, with increased intracranial pressure, headache, nausea, cerebellar dysfunction, occlusive hydrocephalus, ataxia, visual disturbances and other cranial nerve palsies. Various associated abnormalities may be present such as megalencephaly, microgyria, hydromyelia, polydactyly, partial gigantism, macroglossia. LDD is part of the PTEN hamartoma tumor syndromes spectrum that also includes Cowden syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Bannayan-Riley-Ruvalcaba syndrome (BRRS) [MIM:153480]: A rare hamartomatous disorder characterized by macrocephaly and multiple hemangiomas as well as subcutaneous and visceral lipomas. It belongs to the family of hamartomatous polyposis syndromes that includes Peutz Jeghers syndrome, juvenile polyposis, and Cowden syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.39 Ref.43 Ref.50 Ref.51 Ref.56

Squamous cell carcinoma of the head and neck (HNSCC) [MIM:275355]: A non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.58

Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

PTEN mutations are found in a subset of patients with Proteus syndrome, a genetically heterogeneous condition. The molecular diagnosis of PTEN mutation positive cases classifies Proteus syndrome patients as part of the PTEN hamartoma syndrome spectrum. As such, patients surviving the early years of Proteus syndrome are likely at a greater risk of developing malignancies.

Glioma 2 (GLM2) [MIM:613028]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

VACTERL association with hydrocephalus (VACTERL-H) [MIM:276950]: VACTERL is an acronym for vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia, and other limb defects.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Prostate cancer (PC) [MIM:176807]: A malignancy originating in tissues of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Macrocephaly/autism syndrome (MCEPHAS) [MIM:605309]: Patients have autism spectrum disorders and macrocephaly, with head circumferences ranging from +2.5 to +8 SD for age and sex (average head circumference +4.0 SD).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.60

A microdeletion of chromosome 10q23 involving BMPR1A and PTEN is a cause of chromosome 10q23 deletion syndrome, which shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome.

Sequence similarities

Contains 1 C2 tensin-type domain.

Contains 1 phosphatase tensin-type domain.

Ontologies

Keywords
   Biological processApoptosis
Lipid metabolism
Neurogenesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Tumor suppressor
   LigandLipid-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

activation of mitotic anaphase-promoting complex activity

Inferred from direct assay PubMed 21241890. Source: BHF-UCL

aging

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

brain morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

canonical Wnt signaling pathway

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

cardiac muscle tissue development

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

cell proliferation

Traceable author statement PubMed 10918569. Source: UniProtKB

central nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

central nervous system myelin maintenance

Inferred from sequence or structural similarity. Source: BHF-UCL

central nervous system neuron axonogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

dentate gyrus development

Inferred from sequence or structural similarity. Source: BHF-UCL

endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

forebrain morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

heart development

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

inositol phosphate dephosphorylation

Inferred from direct assay Ref.13. Source: UniProtKB

inositol phosphate metabolic process

Traceable author statement. Source: Reactome

learning or memory

Inferred from sequence or structural similarity. Source: BHF-UCL

locomotor rhythm

Inferred from sequence or structural similarity. Source: BHF-UCL

locomotory behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

long term synaptic depression

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

male mating behavior

Inferred from electronic annotation. Source: Ensembl

maternal behavior

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

multicellular organismal response to stress

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 21241890. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of axonogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cell aging

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration

Inferred from mutant phenotype PubMed 17880912Ref.15. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.16PubMed 17880912. Source: UniProtKB

negative regulation of cell size

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 21241890. Source: BHF-UCL

negative regulation of dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of focal adhesion assembly

Inferred from mutant phenotype Ref.15. Source: UniProtKB

negative regulation of myelination

Inferred from electronic annotation. Source: Ensembl

negative regulation of organ growth

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of phagocytosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of phosphatidylinositol 3-kinase signaling

Traceable author statement PubMed 18082964. Source: BHF-UCL

negative regulation of protein kinase B signaling

Inferred from mutant phenotype Ref.19. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

negative regulation of ribosome biogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of synaptic vesicle clustering

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron-neuron synaptic transmission

Inferred from sequence or structural similarity. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.12. Source: GOC

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol dephosphorylation

Inferred from direct assay Ref.13Ref.14. Source: UniProtKB

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

platelet-derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 21241890. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 20123964. Source: BHF-UCL

postsynaptic density assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

prepulse inhibition

Inferred from sequence or structural similarity. Source: BHF-UCL

presynaptic membrane assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

prostate gland growth

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from direct assay Ref.12. Source: UniProtKB

protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

protein stabilization

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

regulation of B cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of cellular component size

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement PubMed 10918569. Source: UniProtKB

regulation of myeloid cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein stability

Inferred from mutant phenotype PubMed 10866658. Source: UniProtKB

response to ATP

Inferred from electronic annotation. Source: Ensembl

response to arsenic-containing substance

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

rhythmic synaptic transmission

Inferred from sequence or structural similarity. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

social behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

synapse assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

synapse maturation

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

Schmidt-Lanterman incisure

Inferred from sequence or structural similarity. Source: BHF-UCL

cell projection

Inferred from direct assay Ref.19. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.19PubMed 10940933Ref.1. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 10940933. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

myelin sheath adaxonal region

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron projection

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 17218261PubMed 21241890. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.19. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionPDZ domain binding

Inferred from physical interaction Ref.17Ref.19. Source: UniProtKB

anaphase-promoting complex binding

Inferred from physical interaction PubMed 21241890. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 16845383. Source: UniProtKB

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

Inferred from direct assay Ref.13. 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 direct assay Ref.13Ref.14. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity

Inferred from direct assay Ref.14. Source: UniProtKB

phosphatidylinositol-3-phosphatase activity

Inferred from direct assay Ref.14. Source: UniProtKB

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 21241890. Source: BHF-UCL

protein serine/threonine phosphatase activity

Inferred from direct assay Ref.12. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay Ref.12. 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

Initiator methionine11Removed Ref.32
Chain2 – 403402Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
PRO_0000215904

Regions

Domain14 – 185172Phosphatase tensin-type
Domain190 – 350161C2 tensin-type
Region401 – 4033PDZ domain-binding

Sites

Active site1241Phosphocysteine intermediate Potential

Amino acid modifications

Modified residue21N-acetylthreonine Ref.32
Modified residue3361Phosphotyrosine; by FRK Ref.26
Modified residue3661Phosphothreonine; by GSK3-beta and PLK3 Ref.22 Ref.28
Modified residue3701Phosphoserine; by CK2 and PLK3 Ref.20 Ref.22 Ref.28
Modified residue3801Phosphoserine; by ROCK1 and CK2 Ref.20
Modified residue3821Phosphothreonine; by ROCK1 and CK2 Ref.20
Modified residue3831Phosphothreonine; by ROCK1 and CK2 Ref.20
Modified residue3851Phosphoserine; by CK2 Ref.20 Ref.22
Modified residue4011Phosphothreonine Ref.17
Cross-link13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.25
Cross-link289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.25

Natural variations

Natural variant101S → N Retains phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes. Ref.51
VAR_026248
Natural variant151R → S in glioma. Ref.2
VAR_007457
Natural variant161Y → C Loss of phosphatase activity towards Ins(1,3,4,5)P4; retains the ability to bind phospholipid membranes. Ref.51
VAR_026249
Natural variant191D → N in malignant melanoma; somatic mutation. Ref.53
VAR_018100
Natural variant201G → E Reduced phosphatase activity towards Ins(1,3,4,5)P4; retains phosphatase activity towards PtdIns(3,4,5)P3. Ref.51
VAR_026250
Natural variant271Y → S Loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026251
Natural variant331Missing in CWS1. Ref.49
VAR_008733
Natural variant341A → D in BRRS. Ref.50 Ref.56
VAR_008734
Natural variant351M → R in CWS1. Ref.46
VAR_008036
Natural variant361G → E in glioma. Ref.2
VAR_007458
Natural variant361G → R in endometrial hyperplasia. Ref.40
VAR_026252
Natural variant421L → R in glioma; retains phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes. Ref.2
VAR_007459
Natural variant471R → G in CWS1. Ref.56
VAR_011587
Natural variant571L → W in glioma; loss of protein phosphatase activity. Ref.2 Ref.12
VAR_007460
Natural variant611H → D in VATER. Ref.55
VAR_018101
Natural variant611H → R Loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026253
Natural variant671I → R in CWS1.
VAR_007461
Natural variant681Y → H in CWS1 and BRRS; loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes. Ref.42 Ref.50 Ref.51 Ref.56
VAR_007462
Natural variant701L → P in CWS1. Ref.45
VAR_018102
Natural variant711C → Y in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026254
Natural variant931H → R in MCEPHAS. Ref.60
VAR_032634
Natural variant931H → Y in CWS1. Ref.51
VAR_026255
Natural variant1051C → F in BRRS; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026256
Natural variant1051C → Y in BRRS. Ref.50 Ref.56
VAR_008735
Natural variant1071D → Y in BRRS and glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.36 Ref.51
VAR_026257
Natural variant1121L → P in CWS1 and LDD; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.42 Ref.48 Ref.51
VAR_007807
Natural variant1121L → R Loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026258
Natural variant1191V → L in multiple cancers. Ref.52
VAR_011588
Natural variant1211A → G in HNSCC. Ref.58
VAR_018103
Natural variant1211A → P in glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.36 Ref.51
VAR_026259
Natural variant1231H → R in CWS1. Ref.37 Ref.49
VAR_007463
Natural variant1231H → Y in endometrial cancer; loss of protein phosphatase activity. Ref.12
VAR_026260
Natural variant1241C → R in CWS1. Ref.37 Ref.49 Ref.51
VAR_007464
Natural variant1241C → S in CWS1; phosphatase-dead protein with neither lipid nor protein phosphatase activity. Ref.14 Ref.54
VAR_018104
Natural variant1291G → E in CWS1; no lipid phosphatase activity but retains protein phosphatase activity; retains ability to inhibit focal adhesion formation. Ref.14 Ref.15 Ref.38 Ref.51 Ref.54
VAR_007465
Natural variant1291G → R in glioblastoma; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.3 Ref.12 Ref.36 Ref.51
VAR_007466
Natural variant1301R → G Loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3. Ref.51
VAR_026261
Natural variant1301R → L in CWS1 and endometrial hyperplasia; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. Ref.40 Ref.51
VAR_007467
Natural variant1301R → Q in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. Ref.47 Ref.51
VAR_007468
Natural variant1321G → V in one patient with clinical findings suggesting hamartoma tumor syndrome. Ref.62
VAR_032635
Natural variant1331V → I Loss of phosphatase activity towards Ins(1,3,4,5)P3. Ref.51
VAR_026262
Natural variant1341M → L in prostate cancer; no effect on protein phosphatase activity; reduced phosphatase activity towards Ins(1,3,4,5)P3 but retains PtdIns(3,4,5)P3 phosphatase activity. Ref.3 Ref.12 Ref.51
VAR_007469
Natural variant1351I → V in BRRS. Ref.50 Ref.56
VAR_008736
Natural variant1361C → Y in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P3. Ref.44 Ref.51
VAR_007808
Natural variant1371A → AN in CWS1. Ref.34
VAR_008737
Natural variant1551Y → C in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026263
Natural variant1581V → L in multiple cancers. Ref.52
VAR_011589
Natural variant1651G → E in CWS1. Ref.49
VAR_008739
Natural variant1651G → R in glioblastoma; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. Ref.12 Ref.36 Ref.51
VAR_026264
Natural variant1651G → V in CWS1.
VAR_008738
Natural variant1671T → P in breast cancer; severely reduced protein phosphatase activity. Ref.12
VAR_026265
Natural variant1701S → N Loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. Ref.51
VAR_026266
Natural variant1701S → R in BRRS; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.12 Ref.39 Ref.50 Ref.51 Ref.56
VAR_007470
Natural variant1731R → C in endometrial hyperplasia; loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains ability to bind phospholipid membranes. Ref.40 Ref.51
VAR_026267
Natural variant1731R → H Loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026268
Natural variant1731R → P Loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026269
Natural variant1741Y → N Loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026270
Natural variant1911V → A in endometrial hyperplasia. Ref.40
VAR_026271
Natural variant2171V → I in malignant melanoma; somatic mutation. Ref.53
VAR_018105
Natural variant2271S → F Reduced phosphatase activity towards Ins(1,3,4,5)P4 but retains PtdIns(3,4,5)P3 phosphatase activity. Ref.51
VAR_026272
Natural variant2341R → Q in a patient with glioma and meningioma; not capable of inducing apoptosis; induced increased cell proliferation; led to high constitutive AKT1 activation which could not be increased further by stimulation with insulin. Ref.57
VAR_018106
Natural variant2411F → S in MCEPHAS. Ref.60
VAR_032636
Natural variant2461P → L in CWS1 and BRRS. Ref.50
VAR_008740
Natural variant2511G → C Loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. Ref.51
VAR_026273
Natural variant2521D → G in MCEPHAS. Ref.60
VAR_032637
Natural variant2891K → E in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. Ref.41 Ref.51
VAR_008741
Natural variant2901V → L. Ref.9
Corresponds to variant rs35600253 [ dbSNP | Ensembl ].
VAR_025167
Natural variant3191Missing in glioma; reduced tumor suppressor activity; fails to inactivate AKT/PKB. Ref.2 Ref.16
VAR_026274
Natural variant3311D → G in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. Ref.51
VAR_026275
Natural variant3411F → V in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.51
VAR_026276
Natural variant3421K → N in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4 but PtdIns(3,4,5)P3 phosphatase activity is similar to wild-type. Ref.51
VAR_026277
Natural variant3431V → E in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. Ref.35 Ref.51
VAR_008742
Natural variant3451L → Q in glioblastoma; reduced tumor suppressor activity; loss of phosphatase activity towards Ins(1,3,4,5)P4; reduced ability to inactivate AKT/PKB; retains ability to bind phospholipid membranes. Ref.16 Ref.36 Ref.51
VAR_026278
Natural variant3471F → L in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4. Ref.35 Ref.51
VAR_008743
Natural variant3481T → I in endometrial hyperplasia; reduced phosphatase activity towards PtdIns(3,4,5)P3; mildly reduced tumor suppressor activity; reduced ability to inactivate AKT/PKB. Ref.16 Ref.40
VAR_026279
Natural variant3691V → G Retains Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3 phosphatase activity; retains ability to bind phospholipid membranes. Ref.51
VAR_026280
Natural variant4011T → I Retains Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3 phosphatase activity; retains ability to bind phospholipid membranes. Ref.51
VAR_026281

Experimental info

Mutagenesis131K → E: Nuclear. Cytoplasmic; when associated with E-289. Shows less tumor suppressive ability; when associated with E-289. Ref.25
Mutagenesis921D → A: 700-fold reduction in phosphatase activity towards PtdIns(3,4,5)P3. Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation. Ref.15 Ref.33
Mutagenesis931H → A: 75% reduction in phosphatase activity towards PtdIns(3,4,5)P3. Modest reduction in phosphatase activity towards PtdIns(3,4)P2. Ref.33
Mutagenesis1241C → A: Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation. Ref.15
Mutagenesis1251K → M: Reduced phosphatase activity towards PtdIns(3,4,5)P3, PtdIns(3,4)P2 and PtdIns(3)P. Ref.33
Mutagenesis1281K → M: 85% reduction in phosphatase activity towards PtdIns(3,4,5)P3. Ref.33
Mutagenesis1281K → R: Does not reduce phosphatase activity towards PtdIns(3,4,5)P3. Ref.33
Mutagenesis1301R → M: Does not affect the ability to inhibit AKT/PKB activation. Ref.14
Mutagenesis1671T → A or D: 60% reduction in phosphatase activity towards PtdIns(3,4,5)P3. Ref.33
Mutagenesis1711Q → A or E: 75% reduction in phosphatase activity towards PtdIns(3,4,5)P3. Ref.33
Mutagenesis263 – 2697KMLKKDK → AAGAADA: Reduces the growth suppression activity and cells show anchorage-independent growth. Reduces binding to phospholipid membranes in vitro. Phosphatase activity towards PtdIns(3,4,5)P3 is not affected. Ref.33
Mutagenesis2891K → E: Nuclear. Cytoplasmic; when associated with E-13. Shows less tumor suppressive ability; when associated with E-13. Ref.25
Mutagenesis327 – 3359KANKDKANR → AAGADAANA: Reduces growth suppression activity and promotes anchorage-independent growth. Reduces binding to phospholipid membranes in vitro; phosphatase activity towards PtdIns(3,4,5)P3 is not affected. Ref.33
Mutagenesis3361Y → F: Significantly lower phosphatase activity, reduced protein stability and decreased growth-inhibitory effect. Ref.26
Mutagenesis3661T → A: Decreased stability. Ref.28
Mutagenesis3701S → A: Decreased stability. Ref.28
Mutagenesis4011T → A: Loss of DLG1-binding. No effect on MAGI2- and MAST2-binding.
Mutagenesis4021K → A: No effect on MAGI2-, MAST2- and DLG1-binding.
Mutagenesis4021K → W: Loss of DLG1-, MAGI2-, MAGI3- and MAST2-binding. Decrease of protein stability.
Mutagenesis4031V → A: Loss of DLG1-, MAGI2-, MAGI3-, MAST1-, MAST2- and MAST3-binding. Ref.23

Secondary structure

..................................................... 403
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60484 [UniParc].

Last modified February 16, 2004. Version 1.
Checksum: 75F97C3DD6802BA9

FASTA40347,166
        10         20         30         40         50         60 
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK 

        70         80         90        100        110        120 
HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA 

       130        140        150        160        170        180 
AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY 

       190        200        210        220        230        240 
LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY 

       250        260        270        280        290        300 
FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI 

       310        320        330        340        350        360 
DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS 

       370        380        390        400 
SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHTQI TKV 

« Hide

References

« Hide 'large scale' references
[1]"TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor beta."
Li D.M., Sun H.
Cancer Res. 57:2124-2129(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
Tissue: Epithelium.
[2]"Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers."
Steck P.A., Pershouse M.A., Jasser S.A., Lin H., Yung W.K.A., Ligon A.H., Langford L.A., Baumgard M.L., Hattier T., Davis T., Frye C., Hu R., Swedlund B., Teng D.H.-F., Tavtigian S.V.
Nat. Genet. 15:356-363(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS GLIOMA SER-15; GLU-36; ARG-42; TRP-57 AND THR-319 DEL.
[3]"PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer."
Li J., Yen C., Liaw D., Podsypanina K., Bose S., Wang S.I., Puc J., Miliaresis C., Rodgers L., McCombie R., Bigner S.H., Giovanella B.C., Ittmann M., Tycko B., Hibshoosh H., Wigler M.H., Parsons R.
Science 275:1943-1947(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLIOBLASTOMA ARG-129 AND PROSTATE CANCER LEU-134.
[4]"The expression profile for the tumour suppressor gene PTEN and associated polymorphic markers."
Hamilton J.A., Stewart L.M.D., Ajayi L., Gray I.C., Gray N.E., Roberts K.G., Watson G.J., Kaisary A.V., Snary D.
Br. J. Cancer 82:1671-1676(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]Wang S., Li J., Liaw D., Bose S., Podsypanina K., Parsons R.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Genomic sequence of PTEN/MMAC1."
Jensen K., de la Bastide M., Parsons R., Parnell L.D., Dedhia N., Gottesman T., Gnoj L., Kaplan N., Lodhi M., Johnson A.F., Shohdy N., Hasegawa A., Haberman K., Huang E.N., Schutz K., Calma C., Granat S., Wigler M.H., McCombie W.R.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen.
[9]NIEHS SNPs program
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-290.
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[12]"P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase."
Myers M.P., Stolarov J.P., Eng C., Li J., Wang S.I., Wigler M.H., Parsons R., Tonks N.K.
Proc. Natl. Acad. Sci. U.S.A. 94:9052-9057(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS GLIOMA TRP-57; ENDOMETRIAL CANCER TYR-123; GLIOBLASTOMA ARG-129; CWS1 ARG-129; PROSTATE CANCER LEU-134; GLIOBLASTOMA ARG-165; BREAST CANCER PRO-167 AND BZ ARG-170.
[13]"The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate."
Maehama T., Dixon J.E.
J. Biol. Chem. 273:13375-13378(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[14]"The lipid phosphatase activity of PTEN is critical for its tumor suppressor function."
Myers M.P., Pass I., Batty I.H., Van der Kaay J., Stolarov J.P., Hemmings B.A., Wigler M.H., Downes C.P., Tonks N.K.
Proc. Natl. Acad. Sci. U.S.A. 95:13513-13518(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-130, CHARACTERIZATION OF VARIANTS CWS1 SER-124 AND CWS1 GLU-129.
[15]"Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN."
Tamura M., Gu J., Matsumoto K., Aota S., Parsons R., Yamada K.M.
Science 280:1614-1617(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-92 AND CYS-124, CHARACTERIZATION OF VARIANT GLU-129.
[16]"The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region."
Georgescu M.-M., Kirsch K.H., Akagi T., Shishido T., Hanafusa H.
Proc. Natl. Acad. Sci. U.S.A. 96:10182-10187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, CHARACTERIZATION OF VARIANTS THR-319 DEL; GLN-345 AND ILE-348.
[17]"Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding."
Adey N.B., Huang L., Ormonde P.A., Baumgard M.L., Pero R., Byreddy D.V., Tavtigian S.V., Bartel P.L.
Cancer Res. 60:35-37(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG1 AND MAST2, PHOSPHORYLATION AT THR-401.
[18]"Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase."
Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.
J. Biol. Chem. 275:21477-21485(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAGI3.
[19]"Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2."
Wu X., Hepner K., Castelino-Prabhu S., Do D., Kaye M.B., Yuan X.-J., Wood J., Ross C., Sawyers C.L., Whang Y.E.
Proc. Natl. Acad. Sci. U.S.A. 97:4233-4238(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AIP1.
[20]"The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation."
Torres J., Pulido R.
J. Biol. Chem. 276:993-998(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-370; SER-380; THR-382; THR-383 AND SER-385.
[21]"Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex."
Vazquez F., Grossman S.R., Takahashi Y., Rokas M.V., Nakamura N., Sellers W.R.
J. Biol. Chem. 276:48627-48630(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH AIP1.
[22]"Direct identification of PTEN phosphorylation sites."
Miller S., Lou D., Seldin D., Lane W., Neel B.
FEBS Lett. 528:145-153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-366; SER-370 AND SER-385.
[23]"Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases."
Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C., Antonarakis S.E., Pulido R.
J. Biol. Chem. 280:28936-28943(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAGI2; MAGI3; MAST1; MAST2 AND MAST3, MUTAGENESIS OF VAL-403, PHOSPHORYLATION.
[24]"NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN."
Wang X., Trotman L.C., Koppie T., Alimonti A., Chen Z., Gao Z., Wang J., Erdjument-Bromage H., Tempst P., Cordon-Cardo C., Pandolfi P.P., Jiang X.
Cell 128:129-139(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEDD4.
[25]"The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network."
Song M.S., Salmena L., Carracedo A., Egia A., Lo-Coco F., Teruya-Feldstein J., Pandolfi P.P.
Nature 455:813-817(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH USP7, UBIQUITINATION AT LYS-13 AND LYS-289, DEUBIQUITINATION BY USP7, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-13 AND LYS-289.
[26]"Rak functions as a tumor suppressor by regulating PTEN protein stability and function."
Yim E.-K., Peng G., Dai H., Hu R., Li K., Lu Y., Mills G.B., Meric-Bernstam F., Hennessy B.T., Craven R.J., Lin S.-Y.
Cancer Cell 15:304-314(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FRK, PHOSPHORYLATION AT TYR-336, MUTAGENESIS OF TYR-336.
[27]"X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization."
Van Themsche C., Leblanc V., Parent S., Asselin E.
J. Biol. Chem. 284:20462-20466(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY XIAP/BIRC4, SUBCELLULAR LOCATION, INTERACTION WITH XIAP/BIRC4.
[28]"Regulation of PTEN stability and activity by Plk3."
Xu D., Yao Y., Jiang X., Lu L., Dai W.
J. Biol. Chem. 285:39935-39942(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-366 AND SER-370, MUTAGENESIS OF THR-366 AND SER-370.
[29]"Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2."
Mund T., Pelham H.R.
Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NDFIP1 AND NDFIP2.
[30]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling."
Stohr N., Kohn M., Lederer M., Glass M., Reinke C., Singer R.H., Huttelmaier S.
Genes Dev. 26:176-189(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
[32]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[33]"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: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 8-353 IN COMPLEX WITH L(+)-TARTRATE, SUBUNIT, DOMAIN, MUTAGENESIS OF ASP-92; HIS-93; LYS-125; LYS-128; THR-167; GLN-171; 263-LYS--ALA-269 AND 327-LYS--ALA-335.
[34]"The role of MMAC1 mutations in early-onset breast cancer: causative in association with Cowden syndrome and excluded in BRCA1-negative cases."
Tsou H.C., Teng D.H.-F., Ping X.L., Brancolini V., Davis T., Hu R., Xie X.X., Gruener A.C., Schrager C.A., Christiano A.M., Eng C., Steck P., Ott J., Tavtigian S.V., Peacocke M.
Am. J. Hum. Genet. 61:1036-1043(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1 ASN-137 INS.
[35]"Inherited mutations in PTEN that are associated with breast cancer, Cowden disease, and juvenile polyposis."
Lynch E.D., Ostermeyer E.A., Lee M.K., Arena J.F., Ji H., Dann J., Swisshelm K., Suchard D., MacLeod P.M., Kvinnsland S., Gjertsen B.T., Heimdal K., Lubs H., Moeller P., King M.-C.
Am. J. Hum. Genet. 61:1254-1260(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CWS1 GLU-343 AND LEU-347.
[36]"Somatic mutations of PTEN in glioblastoma multiforme."
Wang S.I., Puc J., Li J., Bruce J.N., Cairns P., Sidransky D., Parsons R.
Cancer Res. 57:4183-4186(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLIOBLASTOMA TYR-107; PRO-121; ARG-129; ARG-165 AND GLN-345.
[37]"Germline mutations in the PTEN/MMAC1 gene in patients with Cowden disease."
Nelen M.R., van Staveren W.C.G., Peeters E.A.J., Ben-Hassel M., Gorlin R.J., Hamm H., Lindboe C.F., Fryns J.-P., Sijmons R.H., Woods D.G., Mariman E.C.M., Padberg G.W., Kremer H.
Hum. Mol. Genet. 6:1383-1387(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CWS1 ARG-123 AND ARG-124.
[38]"Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome."
Liaw D., Marsh D.J., Li J., Dahia P.L.M., Wang S.I., Zheng Z., Bose S., Call K.M., Tsou H.C., Peacocke M., Eng C., Parsons R.
Nat. Genet. 16:64-67(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1 GLU-129.
[39]"Germline mutations in PTEN are present in Bannayan-Zonana syndrome."
Marsh D.J., Dahia P.L.M., Zheng Z., Liaw D., Parsons R., Gorlin R.J., Eng C.
Nat. Genet. 16:333-334(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BRRS ARG-170.
[40]"Mutation of the PTEN tumor suppressor gene in endometrial hyperplasias."
Maxwell G.L., Risinger J.I., Gumbs C., Shaw H., Bentley R.C., Barrett J.C., Berchuck A., Futreal P.A.
Cancer Res. 58:2500-2503(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ENDOMETRIAL HYPERPLASIA ARG-36; LEU-130; CYS-173; ALA-191 AND ILE-348.
[41]"Mutational abrogation of the PTEN/MMAC1 gene in gastrointestinal polyps in patients with Cowden disease."
Chi S.-G., Kim H.-J., Park B.-J., Min H.-J., Park J.-H., Kim Y.-W., Dong S.-H., Kim B.-H., Lee J.-I., Chang Y.-W., Chang R., Kim W.-K., Yang M.-H.
Gastroenterology 115:1084-1089(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1 GLU-289.
[42]"The genetic basis of Cowden's syndrome: three novel mutations in PTEN/MMAC1/TEP1."
Tsou H.C., Ping X.L., Xie X.X., Gruener A.C., Zhang H., Nini R., Swisshelm K., Sybert V., Diamond T.M., Sutphen R., Peacocke M.
Hum. Genet. 102:467-473(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CWS1 HIS-68 AND PRO-112.
[43]"Mutation spectrum and genotype-phenotype analyses in Cowden disease and Bannayan-Zonana syndrome, two hamartoma syndromes with germline PTEN mutation."
Marsh D.J., Coulon V., Lunetta K.L., Rocca-Serra P., Dahia P.L.M., Zheng Z., Liaw D., Caron S., Duboue B., Lin A.Y., Richardson A.-L., Bonnetblanc J.-M., Bressieux J.-M., Cabarrot-Moreau A., Chompret A., Demange L., Eeles R.A., Yahanda A.M. expand/collapse author list , Fearon E.R., Fricker J.-P., Gorlin R.J., Hodgson S.V., Huson S., Lacombe D., Leprat F., Odent S., Toulouse C., Olopade O.I., Sobol H., Tishler S., Woods C.G., Robinson B.G., Weber H.C., Parsons R., Peacocke M., Longy M., Eng C.
Hum. Mol. Genet. 7:507-515(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CWS1 AND BRRS.
[44]"Novel mutation of the PTEN gene in an Italian Cowden's disease kindred."
Scala S., Bruni P., Lo Muzio L., Mignogna M., Viglietto G., Fusco A.
Int. J. Oncol. 13:665-668(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1 TYR-136.
[45]"Germline PTEN mutations in Cowden syndrome-like families."
Marsh D.J., Dahia P.L.M., Caron S., Kum J.B., Frayling I.M., Tomlinson I.P.M., Hughes K.S., Eeles R.A., Hodgson S.V., Murday V.A., Houlston R., Eng C.
J. Med. Genet. 35:881-885(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1 PRO-70.
[46]"PTEN germ-line mutations in juvenile polyposis coli."
Olschwang S., Serova-Sinilnikova O.M., Lenoir G.M., Thomas G.
Nat. Genet. 18:12-14(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1 ARG-35.
[47]"Variant manifestation of Cowden disease in Japan: hamartomatous polyposis of the digestive tract with mutation of the PTEN gene."
Kurose K., Araki T., Matsunaka T., Takada Y., Emi M.
Am. J. Hum. Genet. 64:308-310(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1 GLN-130.
[48]"Severe Lhermitte-Duclos disease with unique germline mutation of PTEN."
Sutphen R., Diamond T.M., Minton S.E., Peacocke M., Tsou H.C., Root A.W.
Am. J. Med. Genet. 82:290-293(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1/LDD PRO-112.
[49]"Novel PTEN mutations in patients with Cowden disease: absence of clear genotype-phenotype correlations."
Nelen M.R., Kremer H., Konings I.B.M., Schoute F., van Essen A.J., Koch R., Woods C.G., Fryns J.-P., Hamel B.C.J., Hoefsloot L.H., Peeters E.A.J., Padberg G.W.
Eur. J. Hum. Genet. 7:267-273(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CWS1 ILE-33 DEL; ARG-123; ARG-124 AND GLU-165.
[50]"PTEN mutation spectrum and genotype-phenotype correlations in Bannayan-Riley-Ruvalcaba syndrome suggest a single entity with Cowden syndrome."
Marsh D.J., Kum J.B., Lunetta K.L., Bennett M.J., Gorlin R.J., Ahmed S.F., Bodurtha J., Crowe C., Curtis M.A., Dasouki M., Dunn T., Feit H., Geraghty M.T., Graham J.M. Jr., Hodgson S.V., Hunter A., Korf B.R., Manchester D. expand/collapse author list , Miesfeldt S., Murday V.A., Nathanson K.L., Parisi M., Pober B., Romano C., Tolmie J.L., Trembath R., Winter R.M., Zackai E.H., Zori R.T., Weng L.-P., Dahia P.L.M., Eng C.
Hum. Mol. Genet. 8:1461-1472(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BRRS ASP-34; HIS-68; TYR-105; VAL-135; ARG-170 AND LEU-246.
[51]"Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay."
Han S.-Y., Kato H., Kato S., Suzuki T., Shibata H., Ishii S., Shiiba K., Matsuno S., Kanamaru R., Ishioka C.
Cancer Res. 60:3147-3151(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ASN-10; CYS-16; GLU-20; SER-27; ARG-61; HIS-68; CWS1 TYR-71; CWS1 TYR-93; BRRS PHE-105; BRRS TYR-107; PRO-112; ARG-112; PRO-121; ARG-124; ARG-129; GLU-129; GLY-130; CWS1 LEU-130; GLN-130; ILE-133; LEU-134; TYR-136; CYS-155; ARG-165; ASN-170; ARG-170; CYS-173; HIS-173; PRO-173; ASN-174; PHE-227; CYS-251; GLU-289; GLY-331; VAL-341; ASN-342; GLU-343; GLN-345; LEU-347; GLY-369 AND ILE-401.
[52]"Novel germline mutations in the PTEN tumour suppressor gene found in women with multiple cancers."
De Vivo I., Gertig D.M., Nagase S., Hankinson S.E., O'Brien R., Speizer F.E., Parsons R., Hunter D.J.
J. Med. Genet. 37:336-341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MULTIPLE CANCERS LEU-119 AND LEU-158.
[53]"Identification of PTEN mutations in metastatic melanoma specimens."
Celebi J.T., Shendrik I., Silvers D.N., Peacocke M.
J. Med. Genet. 37:653-657(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MALIGNANT MELANOMA ASN-19 AND ILE-217.
[54]"PTEN coordinates G1 arrest by down-regulating cyclin D1 via its protein phosphatase activity and up-regulating p27 via its lipid phosphatase activity in a breast cancer model."
Weng L.-P., Brown J.L., Eng C.
Hum. Mol. Genet. 10:599-604(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS CWS1 SER-124 AND GLU-129.
[55]"A novel germline mutation of the PTEN gene in a patient with macrocephaly, ventricular dilatation, and features of VATER association."
Reardon W., Zhou X.-P., Eng C.
J. Med. Genet. 38:820-823(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VATER ASP-61.
[56]"Rapid mutation scanning of genes associated with familial cancer syndromes using denaturing high-performance liquid chromatography."
Marsh D.J., Theodosopoulos G., Howell V., Richardson A.-L., Benn D.E., Proos A.L., Eng C., Robinson B.G.
Neoplasia 3:236-244(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CWS1 GLY-47, VARIANTS BRRS ASP-34; HIS-68; TYR-105; VAL-135 AND ARG-170.
[57]"A novel germline mutation of PTEN associated with brain tumours of multiple lineages."
Staal F.J.T., van der Luijt R.B., Baert M.R.M., van Drunen J., van Bakel H., Peters E., de Valk I., van Amstel H.K.P., Taphoorn M.J.B., Jansen G.H., van Veelen C.W.M., Burgering B., Staal G.E.J.
Br. J. Cancer 86:1586-1591(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT GLN-234.
[58]"Detection of new PTEN/MMAC1 mutations in head and neck squamous cell carcinomas with loss of chromosome 10."
Poetsch M., Lorenz G., Kleist B.
Cancer Genet. Cytogenet. 132:20-24(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HNSCC GLY-121.
[59]"Germline mutation of the tumour suppressor PTEN in Proteus syndrome."
Smith J.M., Kirk E.P.E., Theodosopoulos G., Marshall G.M., Walker J., Rogers M., Field M., Brereton J.J., Marsh D.J.
J. Med. Genet. 39:937-940(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF PTEN INVOLVEMENT IN PROTEUS SYNDROME.
[60]"Subset of individuals with autism spectrum disorders and extreme macrocephaly associated with germline PTEN tumour suppressor gene mutations."
Butler M.G., Dasouki M.J., Zhou X.-P., Talebizadeh Z., Brown M., Takahashi T.N., Miles J.H., Wang C.H., Stratton R., Pilarski R., Eng C.
J. Med. Genet. 42:318-321(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MCEPHAS ARG-93; SER-241 AND GLY-252.
[61]"Recurrent 10q22-q23 deletions: a genomic disorder on 10q associated with cognitive and behavioral abnormalities."
Balciuniene J., Feng N., Iyadurai K., Hirsch B., Charnas L., Bill B.R., Easterday M.C., Staaf J., Oseth L., Czapansky-Beilman D., Avramopoulos D., Thomas G.H., Borg A., Valle D., Schimmenti L.A., Selleck S.B.
Am. J. Hum. Genet. 80:938-947(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CHROMOSOME 10Q23 DELETION SYNDROME.
[62]"A germline PTEN mutation with manifestations of prenatal onset and verrucous epidermal nevus."
Tekin M., Hismi B.O., Fitoz S., Yalcinkaya F., Ekim M., Kansu A., Ertem M., Deda G., Tutar E., Arsan S., Zhou X.-P., Pilarski R., Eng C., Akar N.
Am. J. Med. Genet. A 140:1472-1475(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-132.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96180 mRNA. Translation: AAB66902.1.
U92436 mRNA. Translation: AAC51182.1.
U93051 mRNA. Translation: AAC51183.1.
AF143315 expand/collapse EMBL AC list , AF143312, AF143313, AF143314 Genomic DNA. Translation: AAD38372.1.
AF000734 expand/collapse EMBL AC list , AF000726, AF000727, AF000728, AF000729, AF000730, AF000731, AF000732, AF000733 Genomic DNA. Translation: AAC08699.1.
AF067844 Genomic DNA. Translation: AAD13528.1.
CR450306 mRNA. Translation: CAG29302.1.
AK313581 mRNA. Translation: BAG36351.1.
DQ073384 Genomic DNA. Translation: AAY57327.1.
CH471066 Genomic DNA. Translation: EAW50174.1.
BC005821 mRNA. Translation: AAH05821.1.
RefSeqNP_000305.3. NM_000314.4.
UniGeneHs.500466.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D5RX-ray2.10A8-353[»]
2KYLNMR-B391-403[»]
ProteinModelPortalP60484.
SMRP60484. Positions 14-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111700. 84 interactions.
DIPDIP-35019N.
IntActP60484. 38 interactions.
MINTMINT-127351.
STRING9606.ENSP00000361021.

Chemistry

ChEMBLCHEMBL2052032.

PTM databases

PhosphoSiteP60484.

Polymorphism databases

DMDM42560209.

Proteomic databases

PaxDbP60484.
PRIDEP60484.

Protocols and materials databases

DNASU5728.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371953; ENSP00000361021; ENSG00000171862.
GeneID5728.
KEGGhsa:5728.
UCSCuc001kfb.3. human.

Organism-specific databases

CTD5728.
GeneCardsGC10P089613.
HGNCHGNC:9588. PTEN.
HPACAB004076.
HPA031335.
MIM137800. phenotype.
153480. phenotype.
158350. phenotype.
176807. phenotype.
275355. phenotype.
276950. phenotype.
601728. gene.
605309. phenotype.
608089. phenotype.
612242. phenotype.
613028. phenotype.
neXtProtNX_P60484.
Orphanet109. Bannayan-Riley-Ruvalcaba syndrome.
201. Cowden syndrome.
145. Hereditary breast and ovarian cancer syndrome.
79076. Juvenile polyposis of infancy.
65285. Lhermitte-Duclos disease.
210548. Macrocephaly-autism syndrome.
744. Proteus syndrome.
2969. Proteus-like syndrome.
137608. Segmental outgrowth - lipomatosis - arteriovenous malformation - epidermal nevus.
67037. Squamous cell carcinoma of head and neck.
PharmGKBPA33942.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000008008.
HOVERGENHBG000239.
InParanoidP60484.
KOK01110.
OMAKEYLILT.
OrthoDBEOG7R2BJ5.
PhylomeDBP60484.
TreeFamTF324513.

Enzyme and pathway databases

BioCycMetaCyc:HS10404-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP60484.

Gene expression databases

ArrayExpressP60484.
BgeeP60484.
CleanExHS_PTEN.
HS_TEP1.
GenevestigatorP60484.

Family and domain databases

InterProIPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
IPR000008. C2_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR014020. Tensin_C2-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.
PROSITEPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTEN. human.
EvolutionaryTraceP60484.
GeneWikiPTEN_(gene).
GenomeRNAi5728.
NextBio22282.
PMAP-CutDBP60484.
PROP60484.
SOURCESearch...

Entry information

Entry namePTEN_HUMAN
AccessionPrimary (citable) accession number: P60484
Secondary accession number(s): B2R904 expand/collapse secondary AC list , O00633, O02679, Q6ICT7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM