Reviewed, UniProtKB/Swiss-Prot O08586 (PTEN_MOUSE)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN
    EC=3.1.3.67
Alternative name(s):
    Mutated in multiple advanced cancers 1

Gene names

Name:	Pten
Synonyms:	Mmac1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Potential tumor suppressor. Acts as a phosphoinositide 3-phosphatase by regulating PtdIns(3,4,5)P3 levels. Involved in regulation of the AKT1 signaling pathway. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Ref.4
Catalytic activity	Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate.
Cofactor	Magnesium.
Subunit structure	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.
Post-translational modification	Phosphorylation results in an inhibited activity towards PIP3 By similarity.
Sequence similarities	Contains 1 C2 tensin-type domain. Contains 1 phosphatase tensin-type domain.

Ontologies

Keywords
Biological process	Cell cycle
Molecular function	Anti-oncogene Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	angiogenesis Inferred from mutant phenotype. Source: MGI cardiac muscle tissue development Inferred from mutant phenotype. Source: MGI cell cycle Inferred from electronic annotation. Source: UniProtKB-KW central nervous system development Inferred from mutant phenotype. Source: MGI endothelial cell migration Inferred from mutant phenotype. Source: MGI induction of apoptosis Inferred from mutant phenotype. Source: MGI inositol phosphate dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of apoptosis Ref.4 Inferred from mutant phenotype. Source: UniProtKB negative regulation of cell cycle Inferred from electronic annotation. Source: UniProtKB-KW 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 focal adhesion formation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein kinase B signaling cascade Ref.4 Inferred from mutant phenotype. Source: UniProtKB phosphoinositide dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein stability Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay. Source: MGI
Molecular function	PDZ 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 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

With	Entry	#Exp.	IntAct	Notes
Cenpc1	P49452	1	EBI-1186266,EBI-1186252
PTEN	P60484	1	EBI-1186266,EBI-696162	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 403	403	Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase PTEN		PRO_0000215905
Regions
	Domain	14 – 185	172	Phosphatase tensin-type
	Domain	190 – 350	161	C2 tensin-type
Sites
	Active site	124	1	Phosphocysteine intermediate Potential
Amino acid modifications
	Modified residue	366	1	Phosphothreonine By similarity
	Modified residue	370	1	Phosphoserine Ref.5
	Modified residue	385	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O08586-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 75F97C3DD6843BA9	FASTA	403	47,152
	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

References

	« Hide 'large scale' referencesShow '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: 9090379] [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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: 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: 15489334] [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: 10339565] [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: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-385, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U92437 mRNA. Translation: AAC53118.1. AK076980 mRNA. Translation: BAC36545.1. AK088717 mRNA. Translation: BAC40525.1. BC021445 mRNA. Translation: AAH21445.1.
IPI	IPI00114410.
RefSeq	NP_032986.1.
UniGene	Mm.245395
3D structure databases
HSSP	HSSP built from PDB template 1D5R based on UniProtKB O00633.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08586. 3 interactions.
PTM databases
PhosphoSite	O08586.
Proteomic databases
PRIDE	O08586.
Genome annotation databases
Ensembl	ENSMUSG00000013663. Mus musculus. [Contig view]
GeneID	19211.
KEGG	mmu:19211.
Organism-specific databases
MGI	MGI:109583. Pten.
Phylogenomic databases
HOGENOM	O08586.
HOVERGEN	O08586.
OMA	O08586. NEPFDEE.
Enzyme and pathway databases
BRENDA	3.1.3.67. 244.
Gene expression databases
ArrayExpress	O08586.
Bgee	O08586.
CleanEx	MM_PTEN.
GermOnline	ENSMUSG00000013663. Mus musculus.
Family and domain databases
InterPro	IPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN. IPR014019. Phosphatase_tensin-typ. IPR014020. Tensin_phosphatase_C2-dom. IPR000340. Tyr_Pase_dual_specific. [Graphical view]
Pfam	PF00782. DSPc. 1 hit. PF10409. PTEN_C2. 1 hit. [Graphical view]
PIRSF	PIRSF038025. PTEN. 1 hit.
PROSITE	PS51182. C2_TENSIN. 1 hit. PS51181. PPASE_TENSIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	295956.
SOURCE	Search...

Entry information

Entry name

PTEN_MOUSE

Accession

Primary (citable) accession number: O08586
Secondary accession number(s): Q542G1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)