pten

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0016314 phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic inference of PIP3 3-phosphatase activity is the defining and experimentally corroborated core molecular function of PTEN in Dictyostelium. Reason: The lipid phosphatase activity of PTEN toward PIP3 is well established and is the physiologically dominant activity of this enzyme, directly antagonizing PI3-kinase during chemotaxis. Supporting Evidence: PMID:14764604 the lipid phosphatase activity of PTEN mediates chemotaxis and that the sharp localization of PI(3,4,5)P3 requires localization of PTEN to the rear of the cell
GO:0051726 regulation of cell cycle	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Retain the broad inherited cell-cycle-regulation role while distinguishing division control from a claim about a specific nuclear checkpoint. Reason: The PTHR12305 IBD is at PTN000959472, and GO:0051726 is an existing IBA, contrary to the focused report. Its definition covers modulation of progression through the cell cycle and does not require a mammalian nuclear checkpoint or tumor-suppressor mechanism. PTEN-dependent cortical signaling, cytokinesis and proliferation control provide a compatible target regulatory context. Continued nuclear division in a cytokinesis mutant does not exclude regulation of another cell-cycle stage. The report also overstates PMID:15809030: its abstract describes cells lacking both enzymatic activities, not simply PTEN loss with intact PI3K. Preserve the inference as non-core without asserting an untested S-phase or checkpoint mechanism. PMID:19515202 directly reports multinucleation after PTEN loss and reduced furrow myosin II, supporting a target division-control role; this does not establish a particular nuclear checkpoint. Supporting Evidence: PMID:38940195 AprA requires both PTEN and CnrN to increase PI(4,5)P2 levels, decrease PI(3,4,5)P3 levels, inhibit proliferation, decrease myosin II phosphorylation and increase filopod sizes PMID:15809030 Then, as the spindle and cell elongate, PI3 kinases and PTEN move to and function at the poles and furrow, respectively. PMID:19515202 PTEN knockout (pten(-)) cells became multinucleated
GO:0005634 nucleus	IBA GO_REF:0000033	UNDECIDED	Summary: The focused report raises a nuclear-import conservation question but does not demonstrate loss of nuclear localization in Dictyostelium. Reason: The nuclear IBD at PTN000959472 includes worm as well as mammalian experimental descendants. Membrane/cortex imaging is positive evidence for those pools and is not an exclusion assay for conditional nuclear occupancy. The report claims a K289-equivalent glutamate from a low-confidence pairwise alignment but delivers no code or alignment artifact; it also assumes the human import mechanism is obligatory in Dictyostelium. PMID:17218261 shows the human K289E import defect can be overcome by forced monoubiquitination, so even the human residue effect is context dependent. The sequence lead merits structural/multiple-alignment and endogenous localization follow-up; it is insufficient to convert this IBA to REMOVE or NOT. Keep UNDECIDED without requesting a duplicate report. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000959472 · PTN000959472 UNRESOLVED PAINT includes a worm nuclear-localization source, so the source is not mammal-only. The focused report provides a speculative import-site divergence lead with missing computational provenance, not verified target loss. Supporting Evidence: PMID:12062103 Exogenously expressed PTEN-GFP localized to the surface membrane at the rear of the cell PMID:17218261 their mutation leads to a constitutive shuttling defect that can be overcome by forced mono-ubiquitination. file:DICDI/pten/pten-hypotheses/nuclear-localization-and-cell-cycle/openscientist.md the exact single-residue call is low-confidence
GO:0005886 plasma membrane	IBA GO_REF:0000033	ACCEPT	Summary: Plasma membrane localization is strongly supported by direct evidence; PTEN is a peripheral membrane protein enriched at the rear and lateral sides of chemotaxing cells. Reason: PTEN functions as a peripheral membrane phosphatase acting on membrane PIP3, and its rear/lateral plasma-membrane localization is directly observed. Supporting Evidence: PMID:12062103 Exogenously expressed PTEN-GFP localized to the surface membrane at the rear of the cell
GO:0051896 regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IBA GO_REF:0000033	ACCEPT	Summary: PTEN regulates PI3K/PKB signaling by degrading PIP3. The direction is negative (see GO:0051898), but this general regulation term is not incorrect. Reason: By dephosphorylating PIP3, PTEN is a bona fide regulator of the PI3K/PKB (PkbA) pathway; loss of PTEN elevates and prolongs PKB substrate phosphorylation. Supporting Evidence: PMID:21169559 The polarity defects in pten- cells correlate with elevated phosphorylations of PKB substrates
GO:0005829 cytosol	IBA GO_REF:0000033	ACCEPT	Summary: A cytosolic pool of PTEN exists and is directly observed; PTEN redistributes between the plasma membrane and the cytosol during signaling. Reason: PTEN cycles on and off the membrane and has a genuine cytosolic pool, supported by direct imaging and consistent with its soluble inositol-phosphatase activity. Supporting Evidence: PMID:23132928 redistribution of PTEN to the cytosol
GO:0004725 protein tyrosine phosphatase activity	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Protein tyrosine (dual-specificity) phosphatase activity is a family-level attribute inherited from the PTEN/tensin catalytic fold. It is a biochemical capability of PTEN but is not the physiologically dominant activity, which is lipid PIP3 phosphatase. Reason: The PTEN active site can dephosphorylate phosphotyrosine in vitro, but no protein-phosphatase substrate or physiological role has been demonstrated for Dictyostelium PTEN. Retain as a non-core catalytic capability.
GO:0004722 protein serine/threonine phosphatase activity	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: Serine/threonine (dual-specificity) protein phosphatase activity derives from EC 3.1.3.16 mapping to the PTEN catalytic domain. It is a possible in-vitro capability but not a demonstrated physiological function. Reason: PTEN is a dual-specificity phosphatase by similarity, but its dominant physiological role is lipid PIP3 dephosphorylation; no protein ser/thr substrate is documented in Dictyostelium.
GO:0004725 protein tyrosine phosphatase activity	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: Duplicate protein tyrosine phosphatase assignment from automated EC mapping; same rationale as the IBA protein tyrosine phosphatase annotation. Reason: A biochemical capability of the PTEN fold, not the core physiological activity in Dictyostelium.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: General cytoplasmic localization from UniProt subcellular-location mapping; consistent with PTEN's cytosolic and cortical pools. Reason: PTEN is a cytoplasmic (peripheral membrane/cytosolic) protein, directly supported by imaging. Supporting Evidence: PMID:23132928 redistribution of PTEN to the cytosol
GO:0005886 plasma membrane	IEA GO_REF:0000044	ACCEPT	Summary: Plasma membrane localization from UniProt mapping, strongly corroborated by direct imaging of PTEN-GFP at the rear membrane. Reason: PTEN is a peripheral plasma-membrane protein acting on membrane PIP3. Supporting Evidence: PMID:12062103 Exogenously expressed PTEN-GFP localized to the surface membrane at the rear of the cell
GO:0005938 cell cortex	IEA GO_REF:0000044	ACCEPT	Summary: Cortical localization from UniProt mapping; PTEN is constitutively localized in the cortex of polarized cells. Reason: Directly supported experimental cortical localization in polarized cells. Supporting Evidence: PMID:17623773 PTEN, which is constitutively localized in the cortex of polarized cells
GO:0016314 phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity	IEA GO_REF:0000120	ACCEPT	Summary: Automated assignment of the core PIP3 3-phosphatase activity; redundant with and consistent with the IBA/ISS/experimental support. Reason: This is the defining core molecular function of PTEN. Supporting Evidence: PMID:14764604 the lipid phosphatase activity of PTEN mediates chemotaxis
GO:0016791 phosphatase activity	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: Grandparent-level generic phosphatase term from InterPro2GO. Not incorrect, but uninformative given the specific PIP3 3-phosphatase activity is annotated. Reason: The specific term GO:0016314 (PIP3 3-phosphatase activity) captures the core function; the generic phosphatase term is redundant and low-information.
GO:0030351 inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity	IEA GO_REF:0000116	KEEP AS NON CORE	Summary: Soluble inositol-polyphosphate 3-phosphatase activity toward Ins(1,3,4,5,6)P5, assigned by Rhea mapping and by similarity to human PTEN. Plausible but not experimentally demonstrated in Dictyostelium. Reason: PTEN can act as a cytosolic inositol 3-phosphatase by similarity, but this is a secondary activity relative to its core lipid PIP3 phosphatase role.
GO:0031038 myosin II filament organization	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: PTEN promotes cortical/posterior myosin II accumulation, so involvement in myosin II organization is supported, but this is a downstream consequence of PIP3 regulation rather than a core molecular function. Reason: PTEN acts upstream to localize myosin II; a genuine but downstream process, not the core activity. Supporting Evidence: PMID:19515202 PTEN and myosin II co-localized at the posterior of migrating cells and furrow region of dividing cells
GO:0031152 aggregation involved in sorocarp development	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: pten- cells fail to aggregate normally, so a developmental role in aggregation is supported (also annotated by IMP), but this is a downstream developmental phenotype, not a core molecular function. Reason: Aggregation defects are a downstream consequence of impaired chemotaxis/polarity; retain as non-core developmental role. Supporting Evidence: PMID:25247494 Deletion of ptenA results in defects in motility, chemotaxis, aggregation and multicellular morphogenesis
GO:0046580 negative regulation of Ras protein signal transduction	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: PTEN (with CnrN) locally inhibits Ras activation, supporting this process; consistent with the IMP annotation from the same phenomenon. Reason: Supported downstream process; PTEN restrains Ras activity, but this is a pathway-level effect of PIP3 regulation rather than a core molecular activity. Supporting Evidence: PMID:38940195 require both PTEN and CnrN to locally inhibit Ras activation
GO:0050793 regulation of developmental process	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Very general developmental regulation term inferred by ARBA; pten- has developmental (aggregation/morphogenesis) defects but this term is too broad to be informative. Reason: More specific developmental terms (aggregation involved in sorocarp development) capture the phenotype; this broad term is non-core. Supporting Evidence: PMID:25247494 Deletion of ptenA results in defects in motility, chemotaxis, aggregation and multicellular morphogenesis
GO:0051489 regulation of filopodium assembly	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: PTEN influences filopod size/formation, supporting a role in filopodium regulation, but as a downstream cytoskeletal effect of PIP3 control. Reason: Downstream cytoskeletal regulation; retain as non-core. Supporting Evidence: PMID:38940195 AprA requires both PTEN and CnrN to increase PI(4,5)P2 levels, decrease PI(3,4,5)P3 levels, inhibit proliferation, decrease myosin II phosphorylation and increase filopod sizes
GO:0051717 inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity	IEA GO_REF:0000116	KEEP AS NON CORE	Summary: Soluble inositol-phosphate 3-phosphatase activity toward Ins(1,3,4,5)P4, assigned by Rhea mapping and by similarity. Plausible secondary activity, not demonstrated in Dictyostelium. Reason: Secondary soluble inositol-phosphatase capability by similarity; not the core lipid phosphatase function.
GO:0051898 negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IEA GO_REF:0000117	ACCEPT	Summary: PTEN negatively regulates PI3K/PKB signaling by degrading PIP3; this is a core biological role, also supported by IMP. Reason: Loss of PTEN elevates and prolongs PKB (PkbA) substrate phosphorylation, directly demonstrating negative regulation of this pathway. Supporting Evidence: PMID:21169559 The polarity defects in pten- cells correlate with elevated phosphorylations of PKB substrates
GO:0052866 phosphatidylinositol phosphate phosphatase activity	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: General phosphatidylinositol-phosphate phosphatase term; a parent of the specific PIP3 3-phosphatase activity. Reason: The specific PIP3 3-phosphatase term is the informative core function; this parent term is redundant.
GO:0140986 G protein-coupled chemorepellent receptor signaling pathway	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: PTEN is required for AprA-induced chemorepulsion, supporting involvement in chemorepellent GPCR signaling (also annotated by IMP). Reason: Genuine but specialized downstream signaling role; not the core molecular function. Supporting Evidence: PMID:38940195 Dictyostelium discoideum cells require both PTEN and CnrN to induce chemorepulsion of cells away from the secreted chemorepellent protein AprA
GO:1903665 negative regulation of asexual reproduction	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: PTEN participates in density/polyphosphate-dependent proliferation inhibition, supporting negative regulation of asexual reproduction (proliferation), also annotated by IMP. Reason: Supported downstream role in proliferation control; not a core molecular activity. Supporting Evidence: PMID:34154396 Polyphosphate upregulates IP3, and this requires GrlD, GefA, PTEN, PLC, and PiaA
GO:0004722 protein serine/threonine phosphatase activity	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Serine/threonine protein phosphatase activity transferred by sequence similarity from human PTEN. A dual-specificity capability, not the core role. Reason: Biochemical capability by similarity; the physiological function is lipid PIP3 dephosphorylation.
GO:0004725 protein tyrosine phosphatase activity	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Protein tyrosine phosphatase activity transferred by similarity from human PTEN; a capability of the PTEN fold, not the dominant activity. Reason: Non-core dual-specificity capability by similarity.
GO:0016314 phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity	ISS GO_REF:0000024	ACCEPT	Summary: Core PIP3 3-phosphatase activity transferred by sequence similarity from human PTEN and corroborated experimentally in Dictyostelium. Reason: This is the defining core molecular function of PTEN. Supporting Evidence: PMID:14764604 the lipid phosphatase activity of PTEN mediates chemotaxis
GO:0030351 inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Soluble Ins(1,3,4,5,6)P5 3-phosphatase activity by similarity; a plausible secondary activity. Reason: Secondary soluble inositol-phosphatase capability, not the core lipid phosphatase function.
GO:0051717 inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Soluble Ins(1,3,4,5)P4 3-phosphatase activity by similarity; a plausible secondary activity. Reason: Secondary soluble inositol-phosphatase capability, not the core function.
GO:0031273 negative regulation of pseudopodium assembly	IMP PMID:38940195 PTEN and the PTEN-like phosphatase CnrN have both distinct a...	ACCEPT	Summary: Suppression of pseudopod formation is a hallmark PTEN function; by degrading PIP3 at the sides and rear, PTEN restrains lateral pseudopod assembly, which is central to directed migration and chemorepulsion. Reason: A well-supported core biological role of PTEN; pten- cells cannot suppress lateral pseudopods, and PTEN is required for AprA-induced pseudopod inhibition. Supporting Evidence: PMID:17623773 PTEN, therefore, plays a fundamental role in the suppression of lateral pseudopod formation
GO:0051490 negative regulation of filopodium assembly	IMP PMID:38940195 PTEN and the PTEN-like phosphatase CnrN have both distinct a...	KEEP AS NON CORE	Summary: PTEN affects filopod size/number in the AprA chemorepulsion pathway; supported downstream cytoskeletal regulation. Reason: Genuine but downstream cytoskeletal effect of PIP3 control; non-core. Supporting Evidence: PMID:38940195 AprA requires both PTEN and CnrN to increase PI(4,5)P2 levels, decrease PI(3,4,5)P3 levels, inhibit proliferation, decrease myosin II phosphorylation and increase filopod sizes
GO:0046580 negative regulation of Ras protein signal transduction	IMP PMID:38940195 PTEN and the PTEN-like phosphatase CnrN have both distinct a...	KEEP AS NON CORE	Summary: PTEN (together with CnrN) is required to locally inhibit Ras activation, a genuine signaling role demonstrated by mutant analysis, though it is a downstream pathway effect rather than the core molecular function. Reason: Experimentally supported: pten- cells fail to locally inhibit Ras activation, linking PTEN to negative regulation of Ras signaling; this is a downstream signaling consequence of PIP3 restriction, kept consistent with the IEA annotation to the same term. Supporting Evidence: PMID:38940195 require both PTEN and CnrN to locally inhibit Ras activation
GO:0031038 myosin II filament organization	IMP PMID:38940195 PTEN and the PTEN-like phosphatase CnrN have both distinct a...	KEEP AS NON CORE	Summary: PTEN influences myosin II phosphorylation/organization; a downstream cytoskeletal consequence of PIP3 regulation. Reason: Supported downstream role in myosin II regulation; not a core molecular activity. Supporting Evidence: PMID:38940195 AprA requires both PTEN and CnrN to increase PI(4,5)P2 levels, decrease PI(3,4,5)P3 levels, inhibit proliferation, decrease myosin II phosphorylation and increase filopod sizes
GO:1903665 negative regulation of asexual reproduction	IMP PMID:38940195 PTEN and the PTEN-like phosphatase CnrN have both distinct a...	KEEP AS NON CORE	Summary: PTEN is required for AprA-mediated inhibition of proliferation, linking it to negative regulation of asexual reproduction. Reason: Supported downstream role in proliferation control; non-core. Supporting Evidence: PMID:38940195 AprA requires both PTEN and CnrN to increase PI(4,5)P2 levels, decrease PI(3,4,5)P3 levels, inhibit proliferation, decrease myosin II phosphorylation and increase filopod sizes
GO:0051898 negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IMP PMID:21169559 Disruption of PKB signaling restores polarity to cells lacki...	ACCEPT	Summary: Directly supported core role; disruption of PTEN elevates and prolongs PKB (PkbA) substrate phosphorylation, and the polarity defects track with this hyperphosphorylation. Reason: Strong experimental support for PTEN as a negative regulator of the PI3K/PKB pathway in Dictyostelium. Supporting Evidence: PMID:21169559 The polarity defects in pten- cells correlate with elevated phosphorylations of PKB substrates
GO:0051896 regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IMP PMID:20562345 Self-organization of the phosphatidylinositol lipids signali...	ACCEPT	Summary: PTEN, with PI3K, regulates the spatiotemporal dynamics of PtdIns lipids and is essential for self-organized PIP3 waves underlying migration. Reason: Experimentally supported regulatory role in the PI3K/PIP3 signaling system; PTEN is essential for the lipid wave dynamics. Supporting Evidence: PMID:20562345 regulators for PtdIns lipid concentrations along the membrane, were essential for wave generation
GO:0001931 uropod	IDA PMID:19515202 PTEN is a mechanosensing signal transducer for myosin II loc...	ACCEPT	Summary: PTEN localizes to the posterior (uropod) of migrating cells, directly observed by fluorescence imaging, consistent with its rear-restricted role. Reason: Direct imaging places PTEN at the posterior/uropod of migrating cells. Supporting Evidence: PMID:19515202 PTEN and myosin II co-localized at the posterior of migrating cells and furrow region of dividing cells
GO:0005829 cytosol	TAS PMID:15473840 Chemoattractant signaling in dictyostelium discoideum.	ACCEPT	Summary: A cytosolic pool of PTEN is described; PTEN cycles between the plasma membrane and cytosol during chemoattractant signaling. Reason: Consistent with directly observed cytosolic redistribution of PTEN. Supporting Evidence: PMID:23132928 redistribution of PTEN to the cytosol
GO:0031254 cell trailing edge	IDA PMID:19011688 Ordered patterns of cell shape and orientational correlation...	ACCEPT	Summary: PTEN is directly observed to localize at the rear/trailing edge of spontaneously migrating cells, where it restricts excess pseudopod formation. Reason: Direct imaging localizes PTEN to the cell rear/trailing edge. Supporting Evidence: PMID:19011688 phosphatase and tensin homolog, (PTEN), is simultaneously localized at the rear
GO:0031257 cell trailing edge membrane	IDA PMID:12062104 Spatial and temporal regulation of 3-phosphoinositides by PI...	ACCEPT	Summary: PTEN shows a distribution reciprocal to PI3K, occupying the plasma membrane along the lateral sides and posterior of chemotaxing cells. Reason: Directly supported rear-membrane localization; PTEN's reciprocal distribution to PI3K places it on the trailing-edge membrane. Supporting Evidence: PMID:12062104 PTEN, a negative regulator of PI3K pathways, exhibits a reciprocal pattern of localization
GO:0032154 cleavage furrow	IDA PMID:19515202 PTEN is a mechanosensing signal transducer for myosin II loc...	ACCEPT	Summary: PTEN localizes to the furrow region of dividing cells, directly observed together with myosin II. Reason: Direct imaging places PTEN at the cleavage furrow during cytokinesis. Supporting Evidence: PMID:19515202 PTEN and myosin II co-localized at the posterior of migrating cells and furrow region of dividing cells
GO:0051285 cell cortex of cell tip	IDA PMID:17623773 PTEN plays a role in the suppression of lateral pseudopod fo...	ACCEPT	Summary: PTEN is constitutively localized in the cortex of polarized cells, including at cell tips/pseudopod-suppressing cortical regions. Reason: Directly supported constitutive cortical localization in polarized cells. Supporting Evidence: PMID:17623773 PTEN, which is constitutively localized in the cortex of polarized cells
GO:1990753 equatorial cell cortex	IDA PMID:19515202 PTEN is a mechanosensing signal transducer for myosin II loc...	ACCEPT	Summary: During division PTEN accumulates at the equatorial/furrow cortex, where it contributes to myosin II accumulation and cytokinesis. Reason: Direct imaging localizes PTEN to the equatorial cortex/furrow of dividing cells. Supporting Evidence: PMID:19515202 PTEN and myosin II co-localized at the posterior of migrating cells and furrow region of dividing cells
GO:0140986 G protein-coupled chemorepellent receptor signaling pathway	IMP PMID:30462573 An endogenous chemorepellent directs cell movement by inhibi...	KEEP AS NON CORE	Summary: PTEN localizes myosin II to the rear during chemorepulsion; it is part of the AprA chemorepellent GPCR signaling response. Reason: Genuine but specialized downstream signaling role in chemorepulsion. Supporting Evidence: PMID:30462573 PTEN to localize myosin II to the rear of a cell
GO:0030010 establishment of cell polarity	IMP PMID:21169559 Disruption of PKB signaling restores polarity to cells lacki...	ACCEPT	Summary: By restricting PIP3, PTEN establishes and maintains front-rear polarity required for cytokinesis and chemotaxis; a core biological role. Reason: Strongly supported; loss of PTEN causes loss of polarity, and PTEN is required to maintain the polarity underlying directed migration and division. Supporting Evidence: PMID:21169559 tumor suppressor PTEN not only controls cell growth but also maintains cell polarity required for cytokinesis and chemotaxis
GO:0036052 protein localization to uropod	IMP PMID:19515202 PTEN is a mechanosensing signal transducer for myosin II loc...	KEEP AS NON CORE	Summary: PTEN acts upstream to recruit/localize myosin II to the posterior (uropod), accumulating there prior to myosin II. Reason: Downstream effect of PTEN's rear localization and PIP3 restriction; not the core molecular activity. Supporting Evidence: PMID:19515202 During pseudopod retraction and cell aspiration by microcapillary, PTEN accumulated at the tips of pseudopods and aspirated lobes prior to the accumulation of myosin II
GO:0080025 phosphatidylinositol-3,5-bisphosphate binding	IDA PMID:35186938 Gradients of PI(4,5)P(2) and PI(3,5)P(2) Jointly Participate...	KEEP AS NON CORE	Summary: In vitro, PTEN preferentially bound liposomes containing PI(4,5)P2 and PI(3,5)P2, indicating PI(3,5)P2 binding capacity that may contribute to back (rear) membrane localization. Reason: Directly demonstrated lipid-binding property that supports membrane targeting to the back, but distinct from the core catalytic function. Supporting Evidence: PMID:35186938 Pten preferentially bound to liposomes containing PI(4,5)P2 and PI(3,5)P2
GO:0005829 cytosol	IDA PMID:23132928 Delineating the core regulatory elements crucial for directe...	ACCEPT	Summary: Direct imaging shows PTEN redistributing to the cytosol upon stimulation and residing in the cytoplasm when membrane PI(4,5)P2 is depleted. Reason: Directly supported cytosolic pool of PTEN. Supporting Evidence: PMID:23132928 redistribution of PTEN to the cytosol
GO:1903665 negative regulation of asexual reproduction	IMP PMID:34154396 An Autocrine Negative Feedback Loop Inhibits Dictyostelium d...	KEEP AS NON CORE	Summary: PTEN is required for polyphosphate-mediated inhibition of proliferation, acting within a density-sensing autocrine feedback loop. Reason: Supported downstream role in density-dependent proliferation control; non-core. Supporting Evidence: PMID:34154396 Polyphosphate upregulates IP3, and this requires GrlD, GefA, PTEN, PLC, and PiaA
GO:0032060 bleb assembly	IMP PMID:26317626 Microtubule-Mediated Inositol Lipid Signaling Plays Critical...	KEEP AS NON CORE	Summary: PTEN-null cells extend fewer blebs, implicating PTEN in bleb regulation via inositol lipid metabolism. Reason: Supported downstream role in blebbing through PIP3/PIP2 balance; not the core molecular activity. Supporting Evidence: PMID:26317626 PTEN-null cells extended fewer blebs
GO:0005546 phosphatidylinositol-4,5-bisphosphate binding	IDA PMID:32111929 Single-molecule imaging of PI(4,5)P(2) and PTEN in vitro rev...	ACCEPT	Summary: PTEN binds its enzymatic product PI(4,5)P2, which stabilizes its membrane binding in a basic-residue-dependent, positive-feedback manner and drives its posterior accumulation. Reason: Directly demonstrated PI(4,5)P2 binding is central to PTEN's rear membrane targeting mechanism and to restricting PIP3 to the anterior. Supporting Evidence: PMID:32111929 the enzymatic product, PI(4,5)P2, stabilizes PTEN's membrane-binding
GO:0034485 phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity	IDA PMID:14764604 Novel mechanism of PTEN regulation by its phosphatidylinosit...	UNDECIDED	Summary: This annotation assigns 5-phosphatase activity (the reaction catalyzed by SHIP-type enzymes, yielding PI(3,4)P2), which conflicts with PTEN's well-established mechanism as a D3 (3-position) phosphatase. The cited abstract does not describe 5-phosphatase activity and the full text is not available to verify the experimental basis. Reason: PTEN is defined mechanistically as a PIP3 3-phosphatase; a 5-phosphatase activity is inconsistent with this. As the relevant full text cannot be accessed to confirm the assay, this is flagged UNDECIDED rather than removed, per policy on unverifiable experimental annotations.
GO:0051800 phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity	IDA PMID:14764604 Novel mechanism of PTEN regulation by its phosphatidylinosit...	KEEP AS NON CORE	Summary: PTEN also dephosphorylates PtdIns(3,4)P2 at the 3-position, consistent with its D3 phosphatase mechanism and with UniProt substrate annotation. This is a genuine but secondary activity relative to the preferred PIP3 substrate. Reason: PI(3,4)P2 is a documented secondary substrate of PTEN; the core activity is PIP3 3-phosphatase, so this is retained as non-core.
GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction	IMP PMID:12062104 Spatial and temporal regulation of 3-phosphoinositides by PI...	KEEP AS NON CORE	Summary: PTEN acts within the PI3K/PKB pathway; disruption prolongs and broadens PIP3-dependent (PH-domain) responses. The negative-regulation aspect is better captured by GO:0051898. Reason: PTEN acts upstream within this pathway as its negative regulator; the specific negative-regulation term is the more informative core annotation. Supporting Evidence: PMID:12062103 Disruption of the PI 3-phosphatase, PTEN, in Dictyostelium discoideum dramatically prolonged and broadened the PH domain relocation and actin polymerization responses
GO:0005886 plasma membrane	IDA PMID:12062103 Tumor suppressor PTEN mediates sensing of chemoattractant gr...	ACCEPT	Summary: PTEN-GFP directly localizes to the plasma membrane at the rear of the cell; membrane localization requires the PI(4,5)P2-binding motif. Reason: Directly observed plasma-membrane localization essential for function. Supporting Evidence: PMID:12062103 Exogenously expressed PTEN-GFP localized to the surface membrane at the rear of the cell
GO:0030041 actin filament polymerization	IMP PMID:12062103 Tumor suppressor PTEN mediates sensing of chemoattractant gr...	KEEP AS NON CORE	Summary: Loss of PTEN broadens and prolongs actin polymerization responses; PTEN acts upstream of actin dynamics via PIP3 restriction rather than directly polymerizing actin. Reason: Downstream cytoskeletal consequence of PIP3 regulation; not a core molecular activity. Supporting Evidence: PMID:12062103 Disruption of the PI 3-phosphatase, PTEN, in Dictyostelium discoideum dramatically prolonged and broadened the PH domain relocation and actin polymerization responses
GO:0031269 pseudopodium assembly	IMP PMID:12062103 Tumor suppressor PTEN mediates sensing of chemoattractant gr...	KEEP AS NON CORE	Summary: PTEN regulates pseudopod formation; its normal role is to restrict pseudopods to the front, and loss leads to broadened/excess pseudopod responses. Reason: Downstream morphogenetic process controlled via PIP3; the negative regulation of pseudopodia is the more informative aspect. Non-core. Supporting Evidence: PMID:12062103 Disruption of the PI 3-phosphatase, PTEN, in Dictyostelium discoideum dramatically prolonged and broadened the PH domain relocation and actin polymerization responses
GO:0043327 chemotaxis to cAMP	IMP PMID:12062103 Tumor suppressor PTEN mediates sensing of chemoattractant gr...	ACCEPT	Summary: PTEN is required for efficient cAMP chemotaxis; pten- cells follow circuitous routes toward the attractant. A core biological role. Reason: Strongly supported; PTEN-mediated gradient sensing/polarity is required for directional migration toward cAMP. Supporting Evidence: PMID:12062103 causing the cells lacking PTEN to follow a circuitous route toward the attractant
GO:0000281 mitotic cytokinesis	IMP PMID:19515202 PTEN is a mechanosensing signal transducer for myosin II loc...	ACCEPT	Summary: PTEN is required for cytokinesis; pten- cells become multinucleated and show reduced furrow myosin II. A core biological role. Reason: Directly supported; loss of PTEN causes cytokinesis failure and multinucleation. Supporting Evidence: PMID:19515202 PTEN knockout (pten(-)) cells became multinucleated, and myosin II significantly decreased in amount at the furrow
GO:0034461 uropod retraction	IMP PMID:19515202 PTEN is a mechanosensing signal transducer for myosin II loc...	KEEP AS NON CORE	Summary: PTEN accumulates at retracting pseudopods/aspirated lobes prior to myosin II, acting upstream in tail (uropod) retraction. Reason: Supported downstream contractile process dependent on PTEN-mediated myosin II localization; non-core. Supporting Evidence: PMID:19515202 During pseudopod retraction and cell aspiration by microcapillary, PTEN accumulated at the tips of pseudopods and aspirated lobes prior to the accumulation of myosin II
GO:0048870 cell motility	IMP PMID:17623773 PTEN plays a role in the suppression of lateral pseudopod fo...	KEEP AS NON CORE	Summary: PTEN contributes to efficient motility by suppressing lateral pseudopods; pten- cells are less efficient in locomotion. Reason: General motility term; the informative core roles are chemotaxis and pseudopod suppression. Non-core. Supporting Evidence: PMID:17623773 the fundamental incapacity of pten(-) cells to suppress lateral pseudopod formation and turning
GO:0048870 cell motility	IGI PMID:17462897 Chemotaxis in the absence of PIP3 gradients.	KEEP AS NON CORE	Summary: In a PI3K1-5/PTEN sextuple mutant, chemotaxis is near-normal but there is a consistent defect in movement speed, implicating PTEN/PIP3 in motility efficiency rather than directional sensing. Reason: Genetic-interaction evidence links PTEN to movement speed; a general motility contribution, non-core. Supporting Evidence: PMID:17462897 There is, however, a consistent defect in movement speed in chemotaxis and especially in random movement
GO:0031152 aggregation involved in sorocarp development	IMP PMID:25247494 PTEN redundancy: overexpressing lpten, a homolog of Dictyost...	KEEP AS NON CORE	Summary: Deletion of ptenA impairs aggregation and multicellular morphogenesis; these developmental defects are rescuable by the homolog lpten. Reason: Downstream developmental phenotype secondary to chemotaxis/polarity defects; non-core. Supporting Evidence: PMID:25247494 Deletion of ptenA results in defects in motility, chemotaxis, aggregation and multicellular morphogenesis
GO:0036051 protein localization to trailing edge	IDA PMID:21169559 Disruption of PKB signaling restores polarity to cells lacki...	KEEP AS NON CORE	Summary: PTEN, itself a rear/trailing-edge protein, contributes to localizing cytoskeletal/PKB-substrate components to the trailing edge. Reason: Downstream localization role tied to PTEN's rear positioning; non-core. Supporting Evidence: PMID:21169559 tumor suppressor PTEN not only controls cell growth but also maintains cell polarity required for cytokinesis and chemotaxis
GO:0000281 mitotic cytokinesis	IMP PMID:21169559 Disruption of PKB signaling restores polarity to cells lacki...	ACCEPT	Summary: PTEN maintains the polarity required for cytokinesis; loss causes cytokinesis defects that are suppressed by disrupting downstream PKB signaling. Reason: Directly supported role in cytokinesis via PIP3/PKB control. Supporting Evidence: PMID:21169559 tumor suppressor PTEN not only controls cell growth but also maintains cell polarity required for cytokinesis and chemotaxis
GO:0043327 chemotaxis to cAMP	IMP PMID:21169559 Disruption of PKB signaling restores polarity to cells lacki...	ACCEPT	Summary: PTEN is required for efficient cAMP chemotaxis; pten- cells are poorly polarized and move slowly on circuitous routes, a defect suppressed by reducing PKB signaling. Reason: Strongly supported core role in directed migration toward cAMP. Supporting Evidence: PMID:21169559 tumor suppressor PTEN not only controls cell growth but also maintains cell polarity required for cytokinesis and chemotaxis
GO:0022604 regulation of cell morphogenesis	IMP PMID:19011688 Ordered patterns of cell shape and orientational correlation...	KEEP AS NON CORE	Summary: PTEN (with PI3K and F-actin) shapes the ordered patterns of cell deformation during migration by restricting excess pseudopods. Reason: General cell-shape regulation downstream of PIP3 control; non-core. Supporting Evidence: PMID:19011688 phosphatase and tensin homolog, (PTEN), is simultaneously localized at the rear
GO:0031272 regulation of pseudopodium assembly	IMP PMID:19011688 Ordered patterns of cell shape and orientational correlation...	KEEP AS NON CORE	Summary: PTEN restricts the formation of excess pseudopodia during spontaneous migration, regulating pseudopod assembly. Reason: Downstream morphogenetic regulation; the negative-regulation aspect is the core function. Non-core here. Supporting Evidence: PMID:19011688 phosphatase and tensin homolog, (PTEN), is simultaneously localized at the rear
GO:0006935 chemotaxis	IMP PMID:17623773 PTEN plays a role in the suppression of lateral pseudopod fo...	KEEP AS NON CORE	Summary: PTEN contributes to chemotaxis efficiency by suppressing lateral pseudopods; the more specific chemotaxis-to-cAMP term captures the core role. Reason: General chemotaxis parent term; the specific cAMP chemotaxis annotation is the informative core term. Supporting Evidence: PMID:17623773 the fundamental incapacity of pten(-) cells to suppress lateral pseudopod formation and turning
GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway	IDA PMID:17606871 Locally controlled inhibitory mechanisms are involved in euk...	KEEP AS NON CORE	Summary: PTEN participates in cAR1/GPCR chemosensing dynamics; its membrane distribution tracks receptor/G-protein activation and returns to baseline upon stimulus withdrawal. Reason: Involvement in the cAMP GPCR signaling response is genuine but a specialized signaling context, not the core molecular function. Supporting Evidence: PMID:17606871 the return of the PIP3 phosphatase PTEN and PHCrac-GFP to their pre-stimulus distribution
GO:0050919 negative chemotaxis	IMP PMID:17517960 Chemoattractants and chemorepellents act by inducing opposit...	KEEP AS NON CORE	Summary: During chemorepulsion the polarity of PI3K and PTEN is reversed relative to chemoattraction, with PTEN at the front, contributing to movement away from the source. Reason: Supported role in chemorepulsion/negative chemotaxis; a specialized directional context, non-core. Supporting Evidence: PMID:17517960 In 8CPT-cAMP gradients, the localization of PI3K and PTEN is reversed compared with cAMP gradients
GO:0031254 cell trailing edge	IDA PMID:16900100 Imaging of cell migration.	ACCEPT	Summary: PTEN is a rear/trailing-edge signaling component in migrating Dictyostelium cells. This review-derived localization is corroborated by primary imaging studies showing PTEN at the cell rear. Reason: Trailing-edge localization of PTEN is well established by direct imaging in primary studies; retained as a valid localization. Supporting Evidence: PMID:19011688 phosphatase and tensin homolog, (PTEN), is simultaneously localized at the rear

Gene Description

Existing Annotations Review

Core Functions

During cell division PTEN accumulates at the equatorial cortex and cleavage furrow, where by locally restricting PIP3 it contributes to cortical myosin II accumulation and successful cytokinesis; loss of PTEN causes multinucleation.

References

Deep Research

OpenScientist

📚 Additional Documentation

Notes

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