Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O08586 (PTEN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

EC=3.1.3.16
EC=3.1.3.48
EC=3.1.3.67
Alternative name(s):
Mutated in multiple advanced cancers 1
Phosphatase and tensin homolog
Gene names
Name:Pten
Synonyms:Mmac1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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

In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement By similarity. 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. Ref.4 Ref.7

Catalytic activity

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

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

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Cofactor

Magnesium.

Subunit structure

Monomer. The unphosphorylated form interacts with the second PDZ domain of AIP1. Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5; interaction with MAGI2 increases protein stability By similarity. Interacts with NEDD4. Interacts with NDFIP1 and NDFIP2; in the presence of NEDD4 or ITCH, this interaction promotes PTEN ubiquitination By similarity. Interacts (via C2 domain) with FRK By similarity. Interacts with USP7; the interaction is direct By similarity. Interacts with ROCK1. Interacts with XIAP/BIRC4. Ref.6 Ref.8

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. NucleusPML body By similarity. Note: Monoubiquitinated form is nuclear By similarity. Nonubiquitinated form is cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies. XIAP/BIRC4 promotes its nuclear localization. Ref.6

Post-translational modification

Constitutively phosphorylated by CK2 under normal conditions. 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 By similarity. Phosphorylation by PLK3 promotes its stability and prevents its degradation by the proteasome. Phosphorylation by ROCK1 is essential for its stability and activity. Ref.8 Ref.9

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 By similarity. Ubiquitinated by XIAP/BIRC4. Ref.6

Sequence similarities

Contains 1 C2 tensin-type domain.

Contains 1 phosphatase tensin-type domain.

Ontologies

Keywords
   Biological processApoptosis
Lipid metabolism
Neurogenesis
   Cellular componentCytoplasm
Nucleus
   DiseaseTumor suppressor
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of mitotic anaphase-promoting complex activity

Inferred from mutant phenotype PubMed 21241890. Source: BHF-UCL

aging

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from mutant phenotype PubMed 16107612. Source: MGI

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

brain morphogenesis

Inferred from mutant phenotype PubMed 19208814. Source: BHF-UCL

canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

cardiac muscle tissue development

Inferred from mutant phenotype PubMed 16107612. Source: MGI

cell migration

Inferred from mutant phenotype PubMed 12091320. Source: MGI

central nervous system development

Inferred from mutant phenotype PubMed 12091320. Source: MGI

central nervous system myelin maintenance

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

central nervous system neuron axonogenesis

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

dendritic spine morphogenesis

Inferred from mutant phenotype PubMed 18082964PubMed 21411674. Source: BHF-UCL

dentate gyrus development

Inferred from mutant phenotype PubMed 17706614. Source: BHF-UCL

endothelial cell migration

Inferred from mutant phenotype PubMed 16107612. Source: MGI

forebrain morphogenesis

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

heart development

Inferred from mutant phenotype PubMed 15755804. Source: MGI

inositol phosphate dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

learning or memory

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

locomotor rhythm

Inferred from mutant phenotype PubMed 17706614. Source: BHF-UCL

locomotory behavior

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

long term synaptic depression

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

male mating behavior

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

maternal behavior

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

memory

Inferred from electronic annotation. Source: Ensembl

multicellular organismal response to stress

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.4. Source: UniProtKB

negative regulation of axonogenesis

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

negative regulation of cell aging

Inferred from mutant phenotype PubMed 21241890. Source: BHF-UCL

negative regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell size

Inferred from mutant phenotype PubMed 16675393PubMed 21411674. Source: BHF-UCL

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

Inferred from electronic annotation. Source: Ensembl

negative regulation of dendritic spine morphogenesis

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 15994948. Source: MGI

negative regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 21411674. Source: BHF-UCL

negative regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of myelination

Inferred from mutant phenotype PubMed 20448149. Source: MGI

negative regulation of organ growth

Inferred from mutant phenotype PubMed 19208814. Source: BHF-UCL

negative regulation of phagocytosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase B signaling

Inferred from mutant phenotype Ref.4. Source: UniProtKB

negative regulation of ribosome biogenesis

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

negative regulation of synaptic vesicle clustering

Inferred from mutant phenotype PubMed 16675393PubMed 18082964. Source: BHF-UCL

neuron-neuron synaptic transmission

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

phosphatidylinositol dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

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 mutant phenotype PubMed 9778245. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 21241890. Source: BHF-UCL

positive regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

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

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

postsynaptic density assembly

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

prepulse inhibition

Inferred from mutant phenotype PubMed 16675393PubMed 19208814. Source: BHF-UCL

presynaptic membrane assembly

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

prostate gland growth

Inferred from mutant phenotype PubMed 15994948. Source: MGI

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein stabilization

Inferred from electronic annotation. Source: Ensembl

regulation of B cell apoptotic process

Inferred from mutant phenotype PubMed 9990064. Source: MGI

regulation of cell cycle

Inferred from genetic interaction PubMed 18332125. Source: MGI

regulation of cellular component size

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

regulation of myeloid cell apoptotic process

Inferred from mutant phenotype PubMed 9990064. Source: MGI

regulation of neuron projection development

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of protein stability

Inferred from sequence or structural similarity. 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 mutant phenotype PubMed 17706614. Source: BHF-UCL

social behavior

Inferred from mutant phenotype PubMed 16675393PubMed 19208814. Source: BHF-UCL

synapse assembly

Inferred from mutant phenotype PubMed 16675393. Source: BHF-UCL

synapse maturation

Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

Schmidt-Lanterman incisure

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

myelin sheath adaxonal region

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

neuron projection

Inferred from direct assay PubMed 21664258. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 14522255PubMed 18332125PubMed 18562292. Source: MGI

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionPDZ domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

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

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16456542PubMed 18190691. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 403402Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
PRO_0000215905

Regions

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

Sites

Active site1241Phosphocysteine intermediate Potential

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue3361Phosphotyrosine; by FRK By similarity
Modified residue3661Phosphothreonine; by GSK3-beta and PLK3 Ref.9
Modified residue3701Phosphoserine; by CK2 and PLK3 Ref.9
Modified residue3801Phosphoserine; by ROCK1 Ref.8
Modified residue3821Phosphothreonine; by ROCK1 Ref.8
Modified residue3831Phosphothreonine; by ROCK1 Ref.8
Modified residue3851Phosphoserine; alternate Ref.5
Modified residue3851Phosphoserine; by CK2; alternate By similarity
Modified residue4011Phosphothreonine By similarity
Cross-link13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict501Missing in BAE28651. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O08586 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 75F97C3DD6843BA9

FASTA40347,152
        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 PFDEDQHSQI TKV 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Sympathetic ganglion, Testis and Thymus.
[3]"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].
Strain: Czech II.
Tissue: Mammary gland.
[4]"PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway."
Sun H., Lesche R., Li D.M., Liliental J., Zhang H., Gao J., Gavrilova N., Mueller B., Liu X., Wu H.
Proc. Natl. Acad. Sci. U.S.A. 96:6199-6204(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"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.
[7]"DISC1 regulates new neuron development in the adult brain via modulation of AKT-mTOR signaling through KIAA1212."
Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N., Kang E., Song H., Ming G.L.
Neuron 63:761-773(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"ROCK1 functions as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability."
Vemula S., Shi J., Hanneman P., Wei L., Kapur R.
Blood 115:1785-1796(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-380; THR-382 AND THR-383, INTERACTION WITH ROCK1.
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92437 mRNA. Translation: AAC53118.1.
AK076980 mRNA. Translation: BAC36545.1.
AK088717 mRNA. Translation: BAC40525.1.
AK148736 mRNA. Translation: BAE28651.1.
BC021445 mRNA. Translation: AAH21445.1.
CCDSCCDS29753.1.
RefSeqNP_032986.1. NM_008960.2.
UniGeneMm.245395.

3D structure databases

ProteinModelPortalO08586.
SMRO08586. Positions 14-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202449. 6 interactions.
DIPDIP-38740N.
IntActO08586. 8 interactions.
MINTMINT-128418.

PTM databases

PhosphoSiteO08586.

Proteomic databases

MaxQBO08586.
PaxDbO08586.
PRIDEO08586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000013807; ENSMUSP00000013807; ENSMUSG00000013663.
GeneID19211.
KEGGmmu:19211.
UCSCuc008hfr.1. mouse.

Organism-specific databases

CTD5728.
MGIMGI:109583. Pten.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00620000087779.
HOGENOMHOG000008008.
HOVERGENHBG000239.
InParanoidQ3UFB0.
KOK01110.
OMAKEYLILT.
OrthoDBEOG7R2BJ5.
PhylomeDBO08586.
TreeFamTF324513.

Gene expression databases

ArrayExpressO08586.
BgeeO08586.
CleanExMM_PTEN.
GenevestigatorO08586.

Family and domain databases

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

Other

ChiTaRSPTEN. mouse.
NextBio295956.
PROO08586.
SOURCESearch...

Entry information

Entry namePTEN_MOUSE
AccessionPrimary (citable) accession number: O08586
Secondary accession number(s): Q3UFB0, Q542G1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot