Q9PUT6 (PTEN_XENLA) 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

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity. UniProtKB P60484 UniProtKB O08586
Catalytic activity	Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate. UniProtKB P60484 A phosphoprotein + H2O = a protein + phosphate. UniProtKB P60484 Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. UniProtKB P60484
Cofactor	Magnesium By similarity. UniProtKB P60484
Subunit structure	Monomer By similarity. UniProtKB P60484
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Nucleus › PML body By similarity UniProtKB P60484.
Post-translational modification	Monoubiquitinated. Deubiquitinated By similarity.
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
Ligand	Lipid-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Ubl conjugation
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW inositol phosphate dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB 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 assembly Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB regulation of neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein stability Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
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 lipid binding Inferred from electronic annotation. Source: UniProtKB-KW 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 402	402	Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN		PRO_0000227539
Regions
	Domain	14 – 184	171	Phosphatase tensin-type
	Domain	189 – 349	161	C2 tensin-type
	Motif	400 – 402	3	PDZ-binding
Sites
	Active site	123	1	Phosphocysteine intermediate Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9PUT6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E61315E2DAB0850F	FASTA	402	46,878
	10 20 30 40 50 60 MTAIIKEFVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK 70 80 90 100 110 120 HKNHYKIYNL CAERHYDTNK FSCRVAQYPF EDHNPPQLEL IKPFCEDLDQ LLSENENVAA 130 140 150 160 170 180 IHCKAGKGRT GVMICAYLLH RGKFPRAQEA LDFYGEVRTR DKKGVTIPSQ RRYVYYYSYL 190 200 210 220 230 240 LKNSLEYRPV PLLFHKIEFE TIPMFSGSTC NPQFVVYQLK VKIFTSTAGP KRAEKLMYFD 250 260 270 280 290 300 FPQPLPVCGD IKVEFFHKQN KVMKKEKMFH FWVNTFFIPG PEEYSEKVEN GTLVGEQELD 310 320 330 340 350 360 GIYSTERSDN DKEYLTLALT KNDLDKANKD KANRLFSPNF KVKLFFTKTV EESSNSEASS 370 380 390 400 STSVTPDVSD NEPDHYRYSD TTDSDPENEP FDEDQITQIT KV

References

[1]

"Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association." Lee J.-O., Yang H., Georgescu M.-M., Di Cristofano A., Maehama T., Shi Y., Dixon J.E., Pandolfi P., Pavletich N.P. Cell 99:323-334(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF144732 mRNA. Translation: AAD46165.1.
RefSeq	NP_001083831.1. NM_001090362.1.
UniGene	Xl.561.
3D structure databases
ProteinModelPortal	Q9PUT6.
SMR	Q9PUT6. Positions 14-350.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	399142.
KEGG	xla:399142.
Organism-specific databases
CTD	5728.
Xenbase	XB-GENE-491437. pten.
Phylogenomic databases
HOVERGEN	HBG000239.
KO	K01110.
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...

Entry information

Entry name

PTEN_XENLA

Accession

Primary (citable) accession number: Q9PUT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program