Reviewed, UniProtKB/Swiss-Prot Q9PUT6 (PTEN_XENLA)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
    EC=3.1.3.67
    EC=3.1.3.16
    EC=3.1.3.48
Alternative name(s):
    Phosphatase and tensin homolog
    Mutated in multiple advanced cancers 1

Gene names

Name:

pten

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. 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. UniProtKB P60484
Sequence similarities	Contains 1 C2 tensin-type domain. Contains 1 phosphatase tensin-type domain.

Ontologies

Keywords
Biological process	Cell cycle Lipid metabolism
Cellular component	Cytoplasm
Ligand	Lipid-binding
Molecular function	Anti-oncogene Hydrolase Protein phosphatase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW inositol phosphate dephosphorylation Inferred from sequence or structural similarity. 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 Inferred from sequence or structural similarity. 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
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)
	Q9PUT6-1 [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: 10555148] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF144732 mRNA. Translation: AAD46165.1.
RefSeq	NP_001083831.1.
UniGene	Xl.561
3D structure databases
HSSP	HSSP built from PDB template 1D5R based on UniProtKB P60484.
SMR	Q9PUT6. Positions 14-350.
ModBase	Search...
Genome annotation databases
GeneID	399142.
KEGG	xla:399142.
Organism-specific databases
Xenbase	XB-FEAT-491432. pten.
Phylogenomic databases
HOVERGEN	Q9PUT6.
Enzyme and pathway databases
BRENDA	3.1.3.16. 648. 3.1.3.48. 648. 3.1.3.67. 648.
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...

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:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project