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UniProtKB - P60484 (PTEN_HUMAN)

Entry version 206 (25 May 2022)
Sequence version 1 (16 Feb 2004)
Previous versions | rss
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Protein

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

Gene

PTEN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:26504226, PubMed:16824732).

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 MAGI2 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.

2 Publications

Functional kinase, like isoform 1 it antagonizes the PI3K-AKT/PKB signaling pathway. Plays a role in mitochondrial energetic metabolism by promoting COX activity and ATP production, via collaboration with isoform 1 in increasing protein levels of PINK1.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Enzymatic activity is enhanced in the presence of phosphatidylserine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei124Phosphocysteine intermediatePROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.3.16, 2681
3.1.3.67, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P60484

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1660499, Synthesis of PIPs at the plasma membrane
R-HSA-1855204, Synthesis of IP3 and IP4 in the cytosol
R-HSA-199418, Negative regulation of the PI3K/AKT network
R-HSA-202424, Downstream TCR signaling
R-HSA-5628897, TP53 Regulates Metabolic Genes
R-HSA-5674404, PTEN Loss of Function in Cancer
R-HSA-5689880, Ub-specific processing proteases
R-HSA-5689896, Ovarian tumor domain proteases
R-HSA-8943723, Regulation of PTEN mRNA translation
R-HSA-8948747, Regulation of PTEN localization
R-HSA-8948751, Regulation of PTEN stability and activity
R-HSA-8986944, Transcriptional Regulation by MECP2

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P60484

SIGNOR Signaling Network Open Resource

More...SIGNORi		P60484

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000849

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC:3.1.3.161 Publication, EC:3.1.3.482 Publications, EC:3.1.3.673 Publications)
Alternative name(s):
Mutated in multiple advanced cancers 1
Phosphatase and tensin homolog
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PTEN
Synonyms:MMAC1, TEP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9588, PTEN

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601728, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P60484

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000171862

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Cowden syndrome 1 (CWS1)21 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00873333Missing in CWS1. 1 PublicationCorresponds to variant dbSNP:rs1554893765Ensembl.1
Natural variantiVAR_00873434A → D in CWS1. 2 Publications1
Natural variantiVAR_00803635M → R in CWS1. 1 PublicationCorresponds to variant dbSNP:rs121909225EnsemblClinVar.1
Natural variantiVAR_01158747R → G in CWS1. 1 PublicationCorresponds to variant dbSNP:rs786204855EnsemblClinVar.1
Natural variantiVAR_00746167I → R in CWS1. 1
Natural variantiVAR_00746268Y → H in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes. 4 PublicationsCorresponds to variant dbSNP:rs398123317EnsemblClinVar.1
Natural variantiVAR_01810270L → P in CWS1. 1 PublicationCorresponds to variant dbSNP:rs121909226EnsemblClinVar.1
Natural variantiVAR_02625471C → Y in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. 1 Publication1
Natural variantiVAR_02625593H → Y in CWS1. 1 PublicationCorresponds to variant dbSNP:rs786204927EnsemblClinVar.1
Natural variantiVAR_026256105C → F in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. 1 Publication1
Natural variantiVAR_008735105C → Y in CWS1. 2 PublicationsCorresponds to variant dbSNP:rs587782343EnsemblClinVar.1
Natural variantiVAR_026257107D → Y in CWS1 and glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4. 2 PublicationsCorresponds to variant dbSNP:rs57374291EnsemblClinVar.1
Natural variantiVAR_007807112L → P in CWS1 and LDD; loss of phosphatase activity towards Ins(1,3,4,5)P4. 3 PublicationsCorresponds to variant dbSNP:rs121909230EnsemblClinVar.1
Natural variantiVAR_007463123H → R in CWS1. 2 PublicationsCorresponds to variant dbSNP:rs121909222EnsemblClinVar.1
Natural variantiVAR_007464124C → R in CWS1. 3 PublicationsCorresponds to variant dbSNP:rs121909223EnsemblClinVar.1
Natural variantiVAR_018104124C → S in CWS1; phosphatase-dead protein with neither lipid nor protein phosphatase activity. 2 PublicationsCorresponds to variant dbSNP:rs121909223EnsemblClinVar.1
Natural variantiVAR_007465129G → E in CWS1; no lipid phosphatase activity but retains protein phosphatase activity; retains ability to inhibit focal adhesion formation. 5 PublicationsCorresponds to variant dbSNP:rs121909218EnsemblClinVar.1
Natural variantiVAR_007467130R → L in CWS1 and endometrial hyperplasia; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. 2 PublicationsCorresponds to variant dbSNP:rs121909229EnsemblClinVar.1
Natural variantiVAR_007468130R → Q in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. 2 PublicationsCorresponds to variant dbSNP:rs121909229EnsemblClinVar.1
Natural variantiVAR_008736135I → V in CWS1. 2 PublicationsCorresponds to variant dbSNP:rs587782360EnsemblClinVar.1
Natural variantiVAR_007808136C → Y in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P3. 2 PublicationsCorresponds to variant dbSNP:rs786204859EnsemblClinVar.1
Natural variantiVAR_008737137A → AN in CWS1. 1 Publication1
Natural variantiVAR_026263155Y → C in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. 1 PublicationCorresponds to variant dbSNP:rs1060500126EnsemblClinVar.1
Natural variantiVAR_008739165G → E in CWS1. 1 Publication1
Natural variantiVAR_008738165G → V in CWS1. Corresponds to variant dbSNP:rs786204863EnsemblClinVar.1
Natural variantiVAR_007470170S → R in CWS1; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4. 5 PublicationsCorresponds to variant dbSNP:rs121909221EnsemblClinVar.1
Natural variantiVAR_008740246P → L in CWS1. 1 PublicationCorresponds to variant dbSNP:rs587782350EnsemblClinVar.1
Natural variantiVAR_008741289K → E in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes; predominantly nuclear. 3 PublicationsCorresponds to variant dbSNP:rs562015640EnsemblClinVar.1
Natural variantiVAR_026275331D → G in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. 1 Publication1
Natural variantiVAR_026276341F → V in CWS1; loss of interaction with NOP53; decreased phosphorylation at S-380; decreased stability; loss of phosphatase activity towards Ins(1,3,4,5)P4. 2 PublicationsCorresponds to variant dbSNP:rs1554825652EnsemblClinVar.1
Natural variantiVAR_026277342K → 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. 1 PublicationCorresponds to variant dbSNP:rs398123314EnsemblClinVar.1
Natural variantiVAR_008742343V → E in CWS1; loss of interaction with NOP53; decreased phosphorylation at S-380; decreased stability; loss of phosphatase activity towards Ins(1,3,4,5)P4. 3 Publications1
Natural variantiVAR_008743347F → L in CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4. 2 Publications1
Lhermitte-Duclos disease (LDD)
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007807112L → P in CWS1 and LDD; loss of phosphatase activity towards Ins(1,3,4,5)P4. 3 PublicationsCorresponds to variant dbSNP:rs121909230EnsemblClinVar.1
Squamous cell carcinoma of the head and neck (HNSCC)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018103121A → G in HNSCC. 1 PublicationCorresponds to variant dbSNP:rs121909237EnsemblClinVar.1
Endometrial cancer (ENDMC)
Disease susceptibility is associated with variants affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM
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)1 Publication
Disease susceptibility is associated with variants affecting the gene represented in this entry.
Disease descriptionGliomas 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018106234R → Q in GLM2; the patient also suffered from benign 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. 1 PublicationCorresponds to variant dbSNP:rs121909235EnsemblClinVar.1
Prostate cancer (PC)2 Publications
Disease susceptibility is associated with variants affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM
Macrocephaly/autism syndrome (MCEPHAS)3 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionPatients 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).
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07870565 – 403Missing in MCEPHAS. 1 PublicationAdd BLAST339
Natural variantiVAR_03263493H → R in MCEPHAS. 1 PublicationCorresponds to variant dbSNP:rs121909238EnsemblClinVar.1
Natural variantiVAR_076762131T → I in MCEPHAS. 1 PublicationCorresponds to variant dbSNP:rs397514560EnsemblClinVar.1
Natural variantiVAR_076763167T → N in MCEPHAS. 1 PublicationCorresponds to variant dbSNP:rs397514559EnsemblClinVar.1
Natural variantiVAR_032636241F → S in MCEPHAS. 1 PublicationCorresponds to variant dbSNP:rs121909240EnsemblClinVar.1
Natural variantiVAR_032637252D → G in MCEPHAS. 1 PublicationCorresponds to variant dbSNP:rs121909239EnsemblClinVar.1
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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1M → I: Expression is restricted to isoform alpha. 1 Publication1
Mutagenesisi13K → E: Nuclear. Cytoplasmic; when associated with E-289. Shows less tumor suppressive ability; when associated with E-289. 1 Publication1
Mutagenesisi92D → A: 700-fold reduction in phosphatase activity towards PtdIns(3,4,5)P3. Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation. 2 Publications1
Mutagenesisi93H → A: 75% reduction in phosphatase activity towards PtdIns(3,4,5)P3. Modest reduction in phosphatase activity towards PtdIns(3,4)P2. 1 Publication1
Mutagenesisi124C → A: Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation. 1 Publication1
Mutagenesisi125K → M: Reduced phosphatase activity towards PtdIns(3,4,5)P3, PtdIns(3,4)P2 and PtdIns(3)P. 1 Publication1
Mutagenesisi126A → P: Does not reduce phosphatase activity towards PtdIns(3,4,5)P3 and PtdIns(3,4)P2. 1 Publication1
Mutagenesisi126A → S: Does not reduce phosphatase activity towards PtdIns(3,4,5)P3 and PtdIns(3,4)P2. 1 Publication1
Mutagenesisi126A → V: Does not reduce phosphatase activity towards PtdIns(3,4,5)P3 and PtdIns(3,4)P2. 1 Publication1
Mutagenesisi128K → M: 85% reduction in phosphatase activity towards PtdIns(3,4,5)P3. 1 Publication1
Mutagenesisi128K → R: Does not reduce phosphatase activity towards PtdIns(3,4,5)P3. 1 Publication1
Mutagenesisi130R → M: Does not affect the ability to inhibit AKT/PKB activation. 1 Publication1
Mutagenesisi167T → A or D: 60% reduction in phosphatase activity towards PtdIns(3,4,5)P3. 1 Publication1
Mutagenesisi171Q → A or E: 75% reduction in phosphatase activity towards PtdIns(3,4,5)P3. 1 Publication1
Mutagenesisi263 – 269KMLKKDK → 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. 1 Publication7
Mutagenesisi289K → E: Cytoplasmic; when associated with E-13. Shows less tumor suppressive ability; when associated with E-13. 1 Publication1
Mutagenesisi327 – 335KANKDKANR → 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. 1 Publication9
Mutagenesisi336Y → F: Significantly lower phosphatase activity, reduced protein stability and decreased growth-inhibitory effect. 1 Publication1
Mutagenesisi366T → A: Decreased stability. 1 Publication1
Mutagenesisi370S → A: Decreased stability. 1 Publication1
Mutagenesisi401T → A: Loss of DLG1-binding. No effect on MAGI2- and MAST2-binding. 1
Mutagenesisi402K → A: No effect on MAGI2-, MAST2- and DLG1-binding. 1
Mutagenesisi402K → W: Loss of DLG1-, MAGI2-, MAGI3- and MAST2-binding. Decrease of protein stability. 1
Mutagenesisi403V → A: Loss of DLG1-, MAGI2-, MAGI3-, MAST1-, MAST2- and MAST3-binding. 1 Publication1

Keywords - Diseasei

Autism spectrum disorder, Disease variant, Tumor suppressor

Organism-specific databases

DisGeNET

More...DisGeNETi		5728

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		PTEN

MalaCards human disease database

More...MalaCardsi		PTEN
MIMi137800, phenotype
158350, phenotype
176807, phenotype
275355, phenotype
605309, phenotype
608089, phenotype
612242, phenotype
613028, phenotype

Open Targets

More...OpenTargetsi		ENSG00000171862

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		397596, Activated PI3K-delta syndrome
109, Bannayan-Riley-Ruvalcaba syndrome
101070, Bilateral frontoparietal polymicrogyria
201, Cowden syndrome
145, Hereditary breast and ovarian cancer syndrome
79076, Juvenile polyposis of infancy
65285, Lhermitte-Duclos disease
210548, Macrocephaly-intellectual disability-autism syndrome
744, Proteus syndrome
2969, Proteus-like syndrome
137608, Segmental outgrowth-lipomatosis-arteriovenous malformation-epidermal nevus syndrome
500481, Squamous cell carcinoma of salivary glands
494547, Squamous cell carcinoma of the hypopharynx
494550, Squamous cell carcinoma of the larynx
502366, Squamous cell carcinoma of the lip
500464, Squamous cell carcinoma of the nasal cavity and paranasal sinuses
502363, Squamous cell carcinoma of the oral cavity
500478, Squamous cell carcinoma of the oropharynx

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33942

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P60484, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2052032

Drug and drug target database

More...DrugBanki		DB04327, Phosphatidylethanolamine

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2497

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PTEN

Domain mapping of disease mutations (DMDM)

More...DMDMi		42560209

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002159042 – 403Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENAdd BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylthreonineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei294PhosphoserineBy similarity1
Modified residuei336Phosphotyrosine; by FRK1 Publication1
Modified residuei366Phosphothreonine; by GSK3-beta and PLK3Combined sources2 Publications1
Modified residuei370Phosphoserine; by CK2 and PLK33 Publications1
Modified residuei380Phosphoserine; by ROCK1 and CK21 Publication1
Modified residuei382Phosphothreonine; by ROCK1 and CK21 Publication1
Modified residuei383Phosphothreonine; by ROCK1 and CK21 Publication1
Modified residuei385Phosphoserine; by CK22 Publications1
Modified residuei401Phosphothreonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Constitutively phosphorylated by CK2 under normal conditions. Phosphorylated in vitro by MAST1, MAST2, MAST3 and STK11. 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.9 Publications
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/BIRC4.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P60484

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P60484

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P60484

MaxQB - The MaxQuant DataBase

More...MaxQBi		P60484

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P60484

PeptideAtlas

More...PeptideAtlasi		P60484

PRoteomics IDEntifications database

More...PRIDEi		P60484

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		57209 [P60484-1]

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P60484

DEPOD human dephosphorylation database

More...DEPODi		PTEN

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P60484

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P60484

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P60484

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed at a relatively high level in all adult tissues, including heart, brain, placenta, lung, liver, muscle, kidney and pancreas.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated by TGFB1.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000171862, Expressed in calcaneal tendon and 219 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P60484, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P60484, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000171862, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. The unphosphorylated form interacts with the second PDZ domain of MAGI2 and with DLG1 and MAST2 in vitro (PubMed:10646847, PubMed:10760291, PubMed:11707428).

Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5; interaction with MAGI2 increases protein stability (PubMed:10748157, PubMed:15951562).

Interacts with NEDD4 (PubMed:17218260).

Interacts with NDFIP1 and NDFIP2; in the presence of NEDD4 or ITCH, this interaction promotes PTEN ubiquitination (PubMed:25801959, PubMed:20534535).

Interacts (via C2 domain) with FRK (PubMed:19345329).

Interacts with USP7; the interaction is direct (PubMed:18716620).

Interacts with ROCK1 (By similarity).

Interacts with XIAP/BIRC4 (PubMed:19473982).

Interacts with STK11; the interaction phosphorylates PTEN (PubMed:15987703).

Interacts with PPP1R16B (PubMed:25007873).

Interacts with NOP53; regulates PTEN phosphorylation and increases its stability (PubMed:15355975).

By similarity15 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111700, 807 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3153, PTEN phosphatase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P60484

Database of interacting proteins

More...DIPi		DIP-35019N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P60484

Protein interaction database and analysis system

More...IntActi		P60484, 68 interactors

Molecular INTeraction database

More...MINTi		P60484

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000361021

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P60484

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P60484, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P60484

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P60484

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P60484

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini14 – 185Phosphatase tensin-typePROSITE-ProRule annotationAdd BLAST172
Domaini190 – 350C2 tensin-typePROSITE-ProRule annotationAdd BLAST161

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni338 – 348Required for interaction with NOP531 PublicationAdd BLAST11
Regioni352 – 403DisorderedSequence analysisAdd BLAST52
Regioni401 – 403PDZ domain-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi353 – 370Polar residuesSequence analysisAdd BLAST18
Compositional biasi371 – 385Basic and acidic residuesSequence analysisAdd BLAST15

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C2 domain binds phospholipid membranes in vitro in a Ca2+-independent manner; this binding is important for its tumor suppressor function.2 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PTEN phosphatase protein family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2283, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154335

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_020105_5_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P60484

Identification of Orthologs from Complete Genome Data

More...OMAi		HARTMNG

Database of Orthologous Groups

More...OrthoDBi		639380at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P60484

TreeFam database of animal gene trees

More...TreeFami		TF324513

Family and domain databases

Conserved Domains Database

More...CDDi		cd14509, PTP_PTEN, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.190.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR017361, Bifunc_PIno_P3_Pase/Pase_PTEN
IPR035892, C2_domain_sf
IPR029021, Prot-tyrosine_phosphatase-like
IPR045101, PTP_PTEN
IPR014020, Tensin_C2-dom
IPR029023, Tensin_phosphatase
IPR016130, Tyr_Pase_AS
IPR003595, Tyr_Pase_cat
IPR000387, Tyr_Pase_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10409, PTEN_C2, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF038025, PTEN, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01326, PTEN_C2, 1 hit
SM00404, PTPc_motif, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49562, SSF49562, 1 hit
SSF52799, SSF52799, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51182, C2_TENSIN, 1 hit
PS51181, PPASE_TENSIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P60484-1) [UniParc]FASTAAdd to basket
Also known as: 55kDa

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI 
        60         70         80         90        100
DDVVRFLDSK HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL 
       110        120        130        140        150
IKPFCEDLDQ WLSEDDNHVA AIHCKAGKGR TGVMICAYLL HRGKFLKAQE 
       160        170        180        190        200
ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY LLKNHLDYRP VALLFHKMMF 
       210        220        230        240        250
ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY FEFPQPLPVC 
       260        270        280        290        300
GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI 
       310        320        330        340        350
DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT 
       360        370        380        390        400
VEEPSNPEAS SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHTQI 

TKV
Length:403
Mass (Da):47,166
Last modified:February 16, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i75F97C3DD6802BA9
GO
Isoform alpha (identifier: P60484-2) [UniParc]FASTAAdd to basket
Also known as: 70kDa, PTEN-long

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MERGGEAAAA...FFFSHRLPDM

Note: Produced by alternative initiation at a CTG start codon of isoform 1. May contain a signal peptide at positions 1-21.Curated
Show »
Length:576
Mass (Da):64,882
Checksum:iE0A3C5E42AEC150D
GO
Isoform 3 (identifier: P60484-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-70: RFLDSKHKNHYKIYNL → S
     165-190: GVTIPSQRRYVYYYSYLLKNHLDYRP → ADPTGGIPDKGIIVIGDGSSMDVIAP
     191-403: Missing.

Show »
Length:175
Mass (Da):19,796
Checksum:iEB3BBB17D7302085
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087X033A0A087X033_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
PTEN
153Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A8I5KR36A0A8I5KR36_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
PTEN
30Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A8I5KSF9A0A8I5KSF9_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
PTEN
576Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A8I5KVQ8A0A8I5KVQ8_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
PTEN
190Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A8I5QKR2A0A8I5QKR2_HUMAN
Phosphatidylinositol 3,4,5-trisphos...
PTEN
44Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02624810S → N Retains phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes. 1 Publication1
Natural variantiVAR_00745715R → S in glioma. 1 PublicationCorresponds to variant dbSNP:rs1064794096EnsemblClinVar.1
Natural variantiVAR_02624916Y → C Loss of phosphatase activity towards Ins(1,3,4,5)P4; retains the ability to bind phospholipid membranes. 1 Publication1
Natural variantiVAR_01810019D → N in malignant melanoma; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121909233EnsemblClinVar.1
Natural variantiVAR_02625020G → E Reduced phosphatase activity towards Ins(1,3,4,5)P4; retains phosphatase activity towards PtdIns(3,4,5)P3. 1 PublicationCorresponds to variant dbSNP:rs1064795967EnsemblClinVar.1
Natural variantiVAR_02625127Y → S Loss of phosphatase activity towards Ins(1,3,4,5)P4. 1 PublicationCorresponds to variant dbSNP:rs886041877EnsemblClinVar.1
Natural variantiVAR_00873333Missing in CWS1. 1 PublicationCorresponds to variant dbSNP:rs1554893765Ensembl.1
Natural variantiVAR_00873434A → D in CWS1. 2 Publications1
Natural variantiVAR_00803635M → R in CWS1. 1 PublicationCorresponds to variant dbSNP:rs121909225EnsemblClinVar.1
Natural variantiVAR_00745836G → E in glioma. 1 PublicationCorresponds to variant dbSNP:rs1554893792EnsemblClinVar.1
Natural variantiVAR_02625236G → R in endometrial hyperplasia. 1 PublicationCorresponds to variant dbSNP:rs786204854EnsemblClinVar.1
Natural variantiVAR_00745942L → 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. 1 Publication1
Natural variantiVAR_01158747R → G in CWS1. 1 PublicationCorresponds to variant dbSNP:rs786204855EnsemblClinVar.1
Natural variantiVAR_00746057L → W in glioma; loss of protein phosphatase activity. 2 PublicationsCorresponds to variant dbSNP:rs786202398EnsemblClinVar.1
Natural variantiVAR_01810161H → D Foun in a patient with macrocephaly, ventriculomegaly, vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia and other limb defects; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121909236EnsemblClinVar.1
Natural variantiVAR_02625361H → R Loss of phosphatase activity towards Ins(1,3,4,5)P4. 1 PublicationCorresponds to variant dbSNP:rs398123316EnsemblClinVar.1
Natural variantiVAR_07870565 – 403Missing in MCEPHAS. 1 PublicationAdd BLAST339
Natural variantiVAR_00746167I → R in CWS1. 1
Natural variantiVAR_00746268Y → H in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes. 4 PublicationsCorresponds to variant dbSNP:rs398123317EnsemblClinVar.1
Natural variantiVAR_01810270L → P in CWS1. 1 PublicationCorresponds to variant dbSNP:rs121909226EnsemblClinVar.1
Natural variantiVAR_02625471C → Y in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. 1 Publication1
Natural variantiVAR_03263493H → R in MCEPHAS. 1 PublicationCorresponds to variant dbSNP:rs121909238EnsemblClinVar.1
Natural variantiVAR_02625593H → Y in CWS1. 1 PublicationCorresponds to variant dbSNP:rs786204927EnsemblClinVar.1
Natural variantiVAR_026256105C → F in CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4. 1 Publication1
Natural variantiVAR_008735105C → Y in CWS1. 2 PublicationsCorresponds to variant dbSNP:rs587782343EnsemblClinVar.1
Natural variantiVAR_026257107D → Y in CWS1 and glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4. 2 PublicationsCorresponds to variant dbSNP:rs57374291EnsemblClinVar.1
Natural variantiVAR_007807112L → P in CWS1 and LDD; loss of phosphatase activity towards Ins(1,3,4,5)P4. 3 PublicationsCorresponds to variant dbSNP:rs121909230EnsemblClinVar.1
Natural variantiVAR_026258112L → R Loss of phosphatase activity towards Ins(1,3,4,5)P4. 1 Publication1
Natural variantiVAR_011588119V → L in multiple cancers. 1 PublicationCorresponds to variant dbSNP:rs139767111EnsemblClinVar.1
Natural variantiVAR_018103121A → G in HNSCC. 1 PublicationCorresponds to variant dbSNP:rs121909237EnsemblClinVar.1
Natural variantiVAR_026259121A → P in glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4. 2 Publications1
Natural variantiVAR_007463123H → R in CWS1. 2 Publications