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Protein

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

Gene

pteN

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity). Negative regulator of PI3K chemotaxis pathways. Overexpression leads to a suppression of a PI3K-dependent activation of pkbA, and these cells exhibit chemotaxis defects consistent with a reduction in PI3K activity.By similarity7 Publications

Catalytic activityi

Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei124Phosphocysteine intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • actin filament polymerization Source: dictyBase
  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: dictyBase
  • aggregation involved in sorocarp development Source: dictyBase
  • cell motility Source: dictyBase
  • chemotaxis Source: dictyBase
  • chemotaxis to cAMP Source: dictyBase
  • establishment of cell polarity Source: dictyBase
  • mitotic cytokinesis Source: dictyBase
  • negative chemotaxis Source: dictyBase
  • negative regulation of protein serine/threonine kinase activity Source: dictyBase
  • phosphatidylinositol 3-kinase signaling Source: dictyBase
  • phosphatidylinositol dephosphorylation Source: dictyBase
  • phosphatidylinositol-mediated signaling Source: dictyBase
  • positive regulation of cellular component movement Source: dictyBase
  • protein localization to trailing edge Source: dictyBase
  • protein localization to uropod Source: dictyBase
  • pseudopodium assembly Source: dictyBase
  • regulation of adenylate cyclase activity Source: dictyBase
  • regulation of cell morphogenesis Source: dictyBase
  • regulation of pseudopodium assembly Source: dictyBase
  • uropod retraction Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Chemotaxis, Lipid metabolism

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-DDI-1660499. Synthesis of PIPs at the plasma membrane.
R-DDI-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-DDI-199418. Negative regulation of the PI3K/AKT network.
R-DDI-202424. Downstream TCR signaling.
R-DDI-5689880. Ub-specific processing proteases.
R-DDI-5689896. Ovarian tumor domain proteases.

Names & Taxonomyi

Protein namesi
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):
Pten 3-phosphoinositide phosphatase alpha
Gene namesi
Name:pteN
Synonyms:ptenA
ORF Names:DDB_G0286557
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0286557. pten.

Subcellular locationi

GO - Cellular componenti

  • cell cortex of cell tip Source: dictyBase
  • cell trailing edge Source: dictyBase
  • cell trailing edge membrane Source: dictyBase
  • cytosol Source: dictyBase
  • equatorial cell cortex Source: dictyBase
  • plasma membrane Source: dictyBase
  • uropod Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Growth defect. Failure to aggregate. Slower migration. Leads to increased F-actin polymerization. Unable to suppress lateral pseudopod formation and turning. Having a direct on PI(3,4,5)P3/PI(3,4)P2 levels. Significant increase in chemoattractant-mediated activation of pkbA and a decrease in chemotaxis speed.5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003768251 – 533Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENAdd BLAST533

Proteomic databases

PaxDbiQ8T9S7.

Expressioni

Developmental stagei

In chemotaxing cells, is on the plasma membrane along the lateral sides and posterior of the cell but is absent or the level is significantly reduced at the leading edge.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi1250719. 3 interactors.
STRINGi44689.DDB0191093.

Structurei

3D structure databases

ProteinModelPortaliQ8T9S7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 185Phosphatase tensin-typePROSITE-ProRule annotationAdd BLAST172
Domaini271 – 406C2 tensin-typePROSITE-ProRule annotationAdd BLAST136

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi237 – 240Poly-Lys4
Compositional biasi266 – 272Poly-Gln7
Compositional biasi455 – 463Poly-Asn9
Compositional biasi471 – 475Poly-Thr5

Sequence similaritiesi

Contains 1 C2 tensin-type domain.PROSITE-ProRule annotation
Contains 1 phosphatase tensin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2283. Eukaryota.
COG2453. LUCA.
InParanoidiQ8T9S7.
KOiK01110.
OMAiWKNTEDS.
PhylomeDBiQ8T9S7.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
SMARTiSM01326. PTEN_C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8T9S7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNLLRVAVS KQKRRYQKNG YDLDLAYITD NIVAMGFPSE KVEGVFRNPM
60 70 80 90 100
KDVQRFLDQY HKDHFKVYNL CSERVYDHSK FYGRVGYYPF DDHNAPQFEM
110 120 130 140 150
IDAFCRDVDA WMKEDSKNIA VIHCKAGKGR TGLMICCWLM YCGMWKNTED
160 170 180 190 200
SLRFYAALRT YNQKGVTIPS QIRYVGYFGR SIRESIKYVP RNVTLKKIVL
210 220 230 240 250
RPLPKEINLS EVQFNISVGK NCVFNSKEHN MNVVISKKKK TVVDKNKKDP
260 270 280 290 300
KKKLTKENSE KNIDSQQQQQ SQSSLSQSQQ GQSSPNMQSL SASGTISSGS
310 320 330 340 350
NVGTVNGNTL HQLGGSQFSL SDLADGNTIG NDEYISFEIG ALSLAGDIRI
360 370 380 390 400
EFTNKQDDRM FMFWVNTSFV QQLEIIPKSG LDKAHKDKNH KAFPEDFHVE
410 420 430 440 450
LTFDQLDQQQ SHTTVVASAE EQTNNQHYPQ SSNNVATSSS HHDNITVVAS
460 470 480 490 500
DAPQNNNNNN NLNSSNSNNA TTTTTKNNIS LASSQSNPVQ QESNPSTTTQ
510 520 530
VSEENSAPKV EAEKIENSNA SANDSETSSN SSS
Length:533
Mass (Da):59,831
Last modified:June 1, 2002 - v1
Checksum:i9922F7887D6F9F6A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti515I → N in AAL99958 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF467431 mRNA. Translation: AAL75566.1.
AF483827 mRNA. Translation: AAL99958.1.
AAFI02000089 Genomic DNA. Translation: EAL64034.1.
RefSeqiXP_637576.1. XM_632484.1.

Genome annotation databases

EnsemblProtistsiEAL64034; EAL64034; DDB_G0286557.
GeneIDi8625716.
KEGGiddi:DDB_G0286557.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF467431 mRNA. Translation: AAL75566.1.
AF483827 mRNA. Translation: AAL99958.1.
AAFI02000089 Genomic DNA. Translation: EAL64034.1.
RefSeqiXP_637576.1. XM_632484.1.

3D structure databases

ProteinModelPortaliQ8T9S7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1250719. 3 interactors.
STRINGi44689.DDB0191093.

Proteomic databases

PaxDbiQ8T9S7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL64034; EAL64034; DDB_G0286557.
GeneIDi8625716.
KEGGiddi:DDB_G0286557.

Organism-specific databases

dictyBaseiDDB_G0286557. pten.

Phylogenomic databases

eggNOGiKOG2283. Eukaryota.
COG2453. LUCA.
InParanoidiQ8T9S7.
KOiK01110.
OMAiWKNTEDS.
PhylomeDBiQ8T9S7.

Enzyme and pathway databases

ReactomeiR-DDI-1660499. Synthesis of PIPs at the plasma membrane.
R-DDI-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-DDI-199418. Negative regulation of the PI3K/AKT network.
R-DDI-202424. Downstream TCR signaling.
R-DDI-5689880. Ub-specific processing proteases.
R-DDI-5689896. Ovarian tumor domain proteases.

Miscellaneous databases

PROiQ8T9S7.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PfamiPF00782. DSPc. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]
SMARTiSM01326. PTEN_C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTEN_DICDI
AccessioniPrimary (citable) accession number: Q8T9S7
Secondary accession number(s): Q54LI5, Q8T658
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: June 1, 2002
Last modified: November 30, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.