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Protein

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

Gene

Pten

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

Catalytic activityi

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.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • activation of APC-Cdc20 complex activity Source: BHF-UCL
  • adult behavior Source: CACAO
  • aging Source: Ensembl
  • angiogenesis Source: MGI
  • apoptotic process Source: UniProtKB-KW
  • brain morphogenesis Source: BHF-UCL
  • canonical Wnt signaling pathway Source: MGI
  • cardiac muscle tissue development Source: MGI
  • cell migration Source: MGI
  • cellular response to decreased oxygen levels Source: MGI
  • cellular response to hypoxia Source: MGI
  • central nervous system development Source: MGI
  • central nervous system myelin maintenance Source: BHF-UCL
  • central nervous system neuron axonogenesis Source: BHF-UCL
  • dendritic spine morphogenesis Source: BHF-UCL
  • dentate gyrus development Source: BHF-UCL
  • endothelial cell migration Source: MGI
  • forebrain morphogenesis Source: BHF-UCL
  • heart development Source: MGI
  • inositol phosphate dephosphorylation Source: UniProtKB
  • learning or memory Source: BHF-UCL
  • locomotor rhythm Source: BHF-UCL
  • locomotory behavior Source: BHF-UCL
  • long term synaptic depression Source: Ensembl
  • long-term synaptic potentiation Source: BHF-UCL
  • male mating behavior Source: BHF-UCL
  • maternal behavior Source: BHF-UCL
  • memory Source: Ensembl
  • multicellular organismal response to stress Source: BHF-UCL
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of axonogenesis Source: BHF-UCL
  • negative regulation of cell aging Source: BHF-UCL
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of cell size Source: BHF-UCL
  • negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: MGI
  • negative regulation of dendritic spine morphogenesis Source: BHF-UCL
  • negative regulation of epithelial cell proliferation Source: MGI
  • negative regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
  • negative regulation of focal adhesion assembly Source: UniProtKB
  • negative regulation of G1/S transition of mitotic cell cycle Source: MGI
  • negative regulation of myelination Source: MGI
  • negative regulation of organ growth Source: BHF-UCL
  • negative regulation of phagocytosis Source: Ensembl
  • negative regulation of protein kinase B signaling Source: UniProtKB
  • negative regulation of protein phosphorylation Source: MGI
  • negative regulation of ribosome biogenesis Source: BHF-UCL
  • negative regulation of synaptic vesicle clustering Source: BHF-UCL
  • neuron-neuron synaptic transmission Source: BHF-UCL
  • peptidyl-tyrosine dephosphorylation Source: MGI
  • phosphatidylinositol dephosphorylation Source: UniProtKB
  • platelet-derived growth factor receptor signaling pathway Source: Ensembl
  • positive regulation of apoptotic signaling pathway Source: MGI
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
  • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • postsynaptic density assembly Source: BHF-UCL
  • prepulse inhibition Source: BHF-UCL
  • presynaptic membrane assembly Source: BHF-UCL
  • prostate gland growth Source: MGI
  • protein dephosphorylation Source: UniProtKB
  • protein kinase B signaling Source: UniProtKB
  • protein stabilization Source: MGI
  • regulation of axon regeneration Source: MGI
  • regulation of B cell apoptotic process Source: MGI
  • regulation of cell cycle Source: MGI
  • regulation of cellular component size Source: BHF-UCL
  • regulation of cellular localization Source: CACAO
  • regulation of myeloid cell apoptotic process Source: MGI
  • regulation of neuron projection development Source: UniProtKB
  • regulation of protein stability Source: UniProtKB
  • regulation of synaptic transmission, GABAergic Source: MGI
  • response to arsenic-containing substance Source: Ensembl
  • response to ATP Source: Ensembl
  • response to drug Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to glucose Source: Ensembl
  • response to nutrient Source: Ensembl
  • response to zinc ion Source: Ensembl
  • rhythmic synaptic transmission Source: BHF-UCL
  • social behavior Source: BHF-UCL
  • synapse assembly Source: BHF-UCL
  • synapse maturation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Apoptosis, Lipid metabolism, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.
REACT_280649. Downstream TCR signaling.
REACT_284913. Negative regulation of the PI3K/AKT network.
REACT_321652. Synthesis of IP3 and IP4 in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC:3.1.3.16, EC:3.1.3.48, EC:3.1.3.67)
Alternative name(s):
Mutated in multiple advanced cancers 1
Phosphatase and tensin homolog
Gene namesi
Name:Pten
Synonyms:Mmac1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:109583. Pten.

Subcellular locationi

  • 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.By similarity1 Publication

GO - Cellular componenti

  • cell projection Source: MGI
  • cytoplasm Source: UniProtKB
  • cytoplasmic side of plasma membrane Source: MGI
  • dendritic spine Source: Ensembl
  • mitochondrion Source: Ensembl
  • myelin sheath adaxonal region Source: BHF-UCL
  • neuron projection Source: BHF-UCL
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • PML body Source: UniProtKB-SubCell
  • postsynaptic membrane Source: Ensembl
  • Schmidt-Lanterman incisure Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 403402Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENPRO_0000215905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Cross-linki13 – 13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki289 – 289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei336 – 3361Phosphotyrosine; by FRKBy similarity
Modified residuei366 – 3661Phosphothreonine; by GSK3-beta and PLK31 Publication
Modified residuei370 – 3701Phosphoserine; by CK2 and PLK31 Publication
Modified residuei380 – 3801Phosphoserine; by ROCK11 Publication
Modified residuei382 – 3821Phosphothreonine; by ROCK11 Publication
Modified residuei383 – 3831Phosphothreonine; by ROCK11 Publication
Modified residuei385 – 3851Phosphoserine; alternate1 Publication
Modified residuei385 – 3851Phosphoserine; by CK2; alternateBy similarity
Modified residuei401 – 4011PhosphothreonineBy similarity

Post-translational modificationi

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.By similarity3 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 (By similarity). Ubiquitinated by XIAP/BIRC4.By similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO08586.
PaxDbiO08586.
PRIDEiO08586.

PTM databases

PhosphoSiteiO08586.

Expressioni

Gene expression databases

BgeeiO08586.
CleanExiMM_PTEN.
ExpressionAtlasiO08586. baseline and differential.
GenevisibleiO08586. MM.

Interactioni

Subunit structurei

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. Interacts with STK11; the interaction phosphorylates PTEN (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CenpcP494522EBI-1186266,EBI-1186252
Slc9a3r2Q9JHL13EBI-1186266,EBI-538451
Tp53P023404EBI-1186266,EBI-474016

Protein-protein interaction databases

BioGridi202449. 8 interactions.
DIPiDIP-38740N.
IntActiO08586. 8 interactions.
MINTiMINT-128418.
STRINGi10090.ENSMUSP00000013807.

Structurei

3D structure databases

ProteinModelPortaliO08586.
SMRiO08586. Positions 14-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 185172Phosphatase tensin-typePROSITE-ProRule annotationAdd
BLAST
Domaini190 – 350161C2 tensin-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni401 – 4033PDZ domain-bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000008008.
HOVERGENiHBG000239.
InParanoidiO08586.
KOiK01110.
OMAiRSINENK.
OrthoDBiEOG7R2BJ5.
PhylomeDBiO08586.
TreeFamiTF324513.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
IPR000008. C2_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
PIRSFiPIRSF038025. PTEN. 1 hit.
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08586-1 [UniParc]FASTAAdd to basket

« 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 PFDEDQHSQI

TKV
Length:403
Mass (Da):47,152
Last modified:July 1, 1997 - v1
Checksum:i75F97C3DD6843BA9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501Missing in BAE28651 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29753.1.
RefSeqiNP_032986.1. NM_008960.2.
UniGeneiMm.245395.

Genome annotation databases

EnsembliENSMUST00000013807; ENSMUSP00000013807; ENSMUSG00000013663.
GeneIDi19211.
KEGGimmu:19211.
UCSCiuc008hfr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29753.1.
RefSeqiNP_032986.1. NM_008960.2.
UniGeneiMm.245395.

3D structure databases

ProteinModelPortaliO08586.
SMRiO08586. Positions 14-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202449. 8 interactions.
DIPiDIP-38740N.
IntActiO08586. 8 interactions.
MINTiMINT-128418.
STRINGi10090.ENSMUSP00000013807.

PTM databases

PhosphoSiteiO08586.

Proteomic databases

MaxQBiO08586.
PaxDbiO08586.
PRIDEiO08586.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000013807; ENSMUSP00000013807; ENSMUSG00000013663.
GeneIDi19211.
KEGGimmu:19211.
UCSCiuc008hfr.1. mouse.

Organism-specific databases

CTDi5728.
MGIiMGI:109583. Pten.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000008008.
HOVERGENiHBG000239.
InParanoidiO08586.
KOiK01110.
OMAiRSINENK.
OrthoDBiEOG7R2BJ5.
PhylomeDBiO08586.
TreeFamiTF324513.

Enzyme and pathway databases

ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.
REACT_280649. Downstream TCR signaling.
REACT_284913. Negative regulation of the PI3K/AKT network.
REACT_321652. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

ChiTaRSiPten. mouse.
NextBioi295956.
PROiO08586.
SOURCEiSearch...

Gene expression databases

BgeeiO08586.
CleanExiMM_PTEN.
ExpressionAtlasiO08586. baseline and differential.
GenevisibleiO08586. MM.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
IPR000008. C2_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
PIRSFiPIRSF038025. PTEN. 1 hit.
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiPTEN_MOUSE
AccessioniPrimary (citable) accession number: O08586
Secondary accession number(s): Q3UFB0, Q542G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: June 24, 2015
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.