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UniProtKB/Swiss-Prot entry O08586


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PTEN_MOUSE
Primary accession number O08586
Secondary accession number Q542G1
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 84)
Name and origin of the protein
Protein name Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN
Synonyms EC 3.1.3.67
Mutated in multiple advanced cancers 1
Gene name
Name: Pten
Synonyms: Mmac1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/ng0497-356; PubMed=9090379 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers.";
Nat. Genet. 15:356-363(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Testis, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION.
DOI=10.1073/pnas.96.11.6199; PubMed=10339565 [NCBI, ExPASy, EBI, Israel, Japan]
Sun H., Lesche R., Li D.M., Liliental J., Zhang H., Gao J., Gavrilova N., Mueller B., Liu X., Wu H.;
"PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway.";
Proc. Natl. Acad. Sci. U.S.A. 96:6199-6204(1999).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-385, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U92437; AAC53118.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK076980; BAC36545.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088717; BAC40525.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021445; AAH21445.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_032986.1; -.
UniGene Mm.245395
3D structure databases
HSSP O00633; 1D5R. [HSSP ENTRY / PDB]
ModBase O08586.
Protein-protein interaction databases
IntAct O08586; 3.
PTM databases
PhosphoSite O08586; -.
Organism-specific databases
MGI MGI:109583; Pten.
Gene expression databases
ArrayExpress O08586; -.
CleanEx MM_PTEN; -.
GermOnline ENSMUSG00000013663; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
GO:0051717; Molecular function: inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0030165; Molecular function: PDZ domain binding (inferred from sequence or structural similarity from UniProtKB).
GO:0016314; Molecular function: phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0051800; Molecular function: phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004438; Molecular function: phosphatidylinositol-3-phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004722; Molecular function: protein serine/threonine phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004725; Molecular function: protein tyrosine phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008138; Molecular function: protein tyrosine/serine/threonine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0001525; Biological process: angiogenesis (inferred from mutant phenotype from MGI).
GO:0048738; Biological process: cardiac muscle development (inferred from mutant phenotype from MGI).
GO:0007417; Biological process: central nervous system development (inferred from mutant phenotype from MGI).
GO:0043542; Biological process: endothelial cell migration (inferred from mutant phenotype from MGI).
GO:0006917; Biological process: induction of apoptosis (inferred from mutant phenotype from MGI).
GO:0046855; Biological process: inositol phosphate dephosphorylation (inferred from sequence or structural similarity from UniProtKB).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0045786; Biological process: negative regulation of cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0030336; Biological process: negative regulation of cell migration (inferred from sequence or structural similarity from UniProtKB).
GO:0008285; Biological process: negative regulation of cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0051895; Biological process: negative regulation of focal adhesion formation (inferred from sequence or structural similarity from UniProtKB).
GO:0051898; Biological process: negative regulation of protein kinase B signaling cascade (inferred from mutant phenotype from UniProtKB).
GO:0046856; Biological process: phosphoinositide dephosphorylation (inferred from sequence or structural similarity from UniProtKB).
GO:0006470; Biological process: protein amino acid dephosphorylation (inferred from sequence or structural similarity from UniProtKB).
GO:0031647; Biological process: regulation of protein stability (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR017361; Bifunc_PIno_P3_Pase/Pase_PTEN.
IPR014019; Phosphatase_tensin.
IPR014020; Tensin_C2.
IPR000387; Tyr_Pase.
IPR000340; Tyr_Pase_dual_specific.
Graphical view of domain structure.
Pfam PF00782; DSPc; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF038025; PTEN; 1.
PROSITE PS51182; C2_TENSIN; 1.
PS51181; PPASE_TENSIN; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE O08586; -.
Genome annotation databases
Ensembl ENSMUSG00000013663; Mus musculus. [Contig view]
GeneID 19211; -.
KEGG mmu:19211; -.
Phylogenomic databases
HOGENOM O08586; -.
HOVERGEN O08586; -.
Other
NextBio 295956; -.
SOURCE Pten; Mus musculus.
ProtoNet O08586.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Anti-oncogene; Cell cycle; Hydrolase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   403  403     Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN. PRO_0000215905
DOMAIN   14   185  172     Phosphatase tensin-type. 
DOMAIN   190   350  161     C2 tensin-type. 
ACT_SITE   124   124        Phosphocysteine intermediate (Potential). 
MOD_RES   366   366        Phosphothreonine (By similarity). 
MOD_RES   370   370        Phosphoserine. 
MOD_RES   385   385        Phosphoserine. 
Sequence information
Length: 403 AA [This is the length of the unprocessed precursor] Molecular weight: 47152 Da [This is the MW of the unprocessed precursor] CRC64: 75F97C3DD6843BA9 [This is a checksum on the sequence]
        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 

O08586 in FASTA format

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View entry in raw text format (no links)
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