O08586 (PTEN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Pten
Synonyms:	Mmac1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 phosphoprotein + H2O = a protein + 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. Nucleus › PML 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 process	Apoptosis Lipid metabolism Neurogenesis
Cellular component	Cytoplasm Nucleus
Disease	Tumor suppressor
Molecular function	Hydrolase Protein phosphatase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of mitotic anaphase-promoting complex activity Inferred from mutant phenotype PubMed 21241890. Source: BHF-UCL angiogenesis Inferred from mutant phenotype PubMed 16107612. Source: MGI apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara cardiac muscle tissue development Inferred from mutant phenotype PubMed 16107612. 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 induction of apoptosis Inferred from mutant phenotype PubMed 9778245. 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 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 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 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 Inferred from electronic annotation. Source: Compara 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 protein kinase B signaling cascade 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 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: Compara positive regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara 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 kinase B signaling cascade Inferred from mutant phenotype Ref.9. Source: UniProtKB protein stabilization Inferred from electronic annotation. Source: Compara regulation of B cell apoptotic process Inferred from mutant phenotype PubMed 9990064. Source: MGI regulation of myeloid cell apoptotic process Inferred from mutant phenotype PubMed 9990064. Source: MGI regulation of protein stability Inferred from sequence or structural similarity. Source: UniProtKB 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 maturation Inferred from mutant phenotype PubMed 18082964. Source: BHF-UCL
Cellular_component	PML 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 internal side of plasma membrane Inferred from electronic annotation. Source: Compara 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
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	2	EBI-1186266,EBI-1186252

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 and dual-specificity protein phosphatase PTEN		PRO_0000215905
Regions
	Domain	14 – 185	172	Phosphatase tensin-type
	Domain	190 – 350	161	C2 tensin-type
	Region	401 – 403	3	PDZ domain-binding By similarity
Sites
	Active site	124	1	Phosphocysteine intermediate Potential
Amino acid modifications
	Modified residue	336	1	Phosphotyrosine; by FRK By similarity
	Modified residue	366	1	Phosphothreonine; by GSK3-beta and PLK3 Ref.9
	Modified residue	370	1	Phosphoserine; by CK2 and PLK3 Ref.5 Ref.9
	Modified residue	380	1	Phosphoserine; by ROCK1 Ref.8
	Modified residue	382	1	Phosphothreonine; by ROCK1 Ref.8
	Modified residue	383	1	Phosphothreonine; by ROCK1 Ref.8
	Modified residue	385	1	Phosphoserine; by CK2 By similarity
	Modified residue	401	1	Phosphothreonine By similarity
	Cross-link	13		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	289		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Sequence conflict	50	1	Missing in BAE28651. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O08586 [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] [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]	"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-370 AND SER-385, MASS SPECTROMETRY. 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.
IPI	IPI00114410.
RefSeq	NP_032986.1. NM_008960.2.
UniGene	Mm.245395.
3D structure databases
ProteinModelPortal	O08586.
SMR	O08586. Positions 14-351.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38740N.
IntAct	O08586. 3 interactions.
MINT	MINT-128418.
PTM databases
PhosphoSite	O08586.
Proteomic databases
PaxDb	O08586.
PRIDE	O08586.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000013807; ENSMUSP00000013807; ENSMUSG00000013663.
GeneID	19211.
KEGG	mmu:19211.
UCSC	uc008hfr.1. mouse.
Organism-specific databases
CTD	5728.
MGI	MGI:109583. Pten.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00620000087779.
HOGENOM	HOG000008008.
HOVERGEN	HBG000239.
InParanoid	Q3UFB0.
KO	K01110.
OMA	TRREDKH.
OrthoDB	EOG434W64.
Gene expression databases
ArrayExpress	O08586.
Bgee	O08586.
CleanEx	MM_PTEN.
Genevestigator	O08586.
GermOnline	ENSMUSG00000013663. Mus musculus.
Family and domain databases
InterPro	IPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR000340. Dual-sp_phosphatase_cat-dom. IPR014019. Phosphatase_tensin-typ. IPR014020. Tensin_phosphatase_C2-dom. IPR016130. Tyr_Pase_AS. [Graphical view]
Pfam	PF00782. DSPc. 1 hit. PF10409. PTEN_C2. 1 hit. [Graphical view]
PIRSF	PIRSF038025. PTEN. 1 hit.
SUPFAM	SSF49562. C2_CaLB. 1 hit.
PROSITE	PS51182. C2_TENSIN. 1 hit. PS51181. PPASE_TENSIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PTEN. mouse.
NextBio	295956.
SOURCE	Search...

Entry information

Entry name

PTEN_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program