Vps34 is the sole phosphatidylinositol 3-kinase of Saccharomyces cerevisiae (class III PI3K, ortholog of human PIK3C3). It phosphorylates phosphatidylinositol, but not PtdIns4P or PtdIns(4,5)P2, at the D-3 position to generate PtdIns3P (EC 2.7.1.137); it also autophosphorylates. Vps34 acts in a heterodimer with the regulatory protein kinase Vps15, which engages the Vps34 activation loop, and the Vps15-Vps34 arm assembles into two distinct heterotetrameric complexes: complex I (with Vps30/Atg6, Atg14 and Atg38), targeted by Atg14 to the phagophore assembly site where its PtdIns3P is essential for autophagosome formation, autophagy, the Cvt pathway and pexophagy; and complex II (with Vps30 and Vps38), targeted to endosomes and the vacuole membrane, where PtdIns3P recruits FYVE/PX effectors for carboxypeptidase Y sorting, endosome-to-vacuole traffic and retromer-mediated retrieval. Vps34-derived PtdIns3P is also the substrate for Fab1 production of PtdIns(3,5)P2.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000045 autophagosome assembly | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from the PIK3C3 clade. Complex I PtdIns3P at the PAS is essential for autophagosome formation in yeast; the inference is well supported. Supporting Evidence: PMID:24165940 Autophagy is characterized by the formation of an autophagosome, for which Vps34-dervied phosphatidylinositol 3-phosphate (PI3P) is essential. PMID:11157979 two distinct Vps34 PtdIns 3-kinase complexes exist: one, containing Vps15p, Vps30p, and Apg14p, functions in autophagy and the other containing Vps15p, Vps30p, and Vps38p functions in CPY sorting |
| GO:0000139 Golgi membrane | NAS PMID:11157979 Two distinct Vps34 phosphatidylinositol 3-kinase complexes f... | KEEP AS NON CORE | Summary: NAS citing Kihara et al. UniProt records peripheral association with TGN membranes, but direct evidence places Vps34 complexes on endosomes, the vacuole membrane and the PAS; Golgi association is a minor, non-core location. Supporting Evidence: file:yeast/VPS34/VPS34-uniprot.txt SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane |
| GO:0000329 fungal-type vacuole membrane | HDA PMID:19001347 The yeast vacuolar membrane proteome. | ACCEPT | Summary: Vacuolar membrane proteome (HTP). Consistent with the IDA localization of Vps34 to vacuolar membranes. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0000329 fungal-type vacuole membrane | IDA PMID:16421251 Assortment of phosphatidylinositol 3-kinase complexes--Atg14... | ACCEPT | Summary: Obara et al. localized Vps34 to the PAS, vacuolar membranes and endosomes. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0000407 phagophore assembly site | IBA GO_REF:0000033 | ACCEPT | Summary: IBA PAS localization from the PIK3C3 clade; supported by yeast data. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. PMID:16421251 The localization of these components to the PAS was Atg14p dependent but not dependent on Vps38p. |
| GO:0000407 phagophore assembly site | IDA PMID:16421251 Assortment of phosphatidylinositol 3-kinase complexes--Atg14... | ACCEPT | Summary: Obara et al.: Vps34 localizes to the PAS in an Atg14-dependent manner (complex I). Supporting Evidence: PMID:16421251 The localization of these components to the PAS was Atg14p dependent but not dependent on Vps38p. |
| GO:0000425 pexophagy | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA pexophagy. Vps34 complex I is required for pexophagy in S. cerevisiae; a specific selective-autophagy outcome of the core autophagy role, kept as non-core. Supporting Evidence: PMID:21121900 The function of Vps34p-containing complex I as well as a subset of PtdIns3P-binding proteins proved to be mandatory for the regulated degradation of peroxisomes. |
| GO:0000425 pexophagy | IMP PMID:21121900 The phosphoinositide 3-kinase Vps34p is required for pexopha... | KEEP AS NON CORE | Summary: Grunau et al. showed Vps34 complex I is required for pexophagy. Supporting Evidence: PMID:21121900 The function of Vps34p-containing complex I as well as a subset of PtdIns3P-binding proteins proved to be mandatory for the regulated degradation of peroxisomes. |
| GO:0004672 protein kinase activity | IDA PMID:7989323 Vps34p required for yeast vacuolar protein sorting is a mult... | KEEP AS NON CORE | Summary: Stack and Emr showed Vps34 autophosphorylates (Ser in vivo; Ser/Thr/Tyr in vitro). The protein kinase activity is real but its physiological significance is unclear compared with the lipid kinase activity. Supporting Evidence: PMID:7989323 the Vps34 phosphatidylinositol 3-kinase undergoes an autophosphorylation event both in vivo and in vitro |
| GO:0005515 protein binding | IPI PMID:16839886 Activation of the phosphatidylinositol 3-kinase Vps34 by a G... | REMOVE | Summary: Gpa1 (P08539) directly binds Vps34 and Vps15 at endosomes and stimulates PtdIns3P production in pheromone signalling. The interaction is genuine, but bare 'protein binding' is uninformative; removal does not dispute it. Supporting Evidence: PMID:16839886 We demonstrate that Gpa1 is present at endosomes, where it interacts directly with both Vps34 and Vps15 and stimulates increased production of phosphatidylinositol 3-phosphate. |
| GO:0005515 protein binding | IPI PMID:20489023 A global protein kinase and phosphatase interaction network ... | REMOVE | Summary: Vps15 (P22219) interaction from a high-throughput kinase/phosphatase AP-MS network. Vps15 is the obligate regulatory subunit, captured by the complex I/II annotations; bare 'protein binding' adds no information. Supporting Evidence: PMID:26450213 Vps34 and Vps15 intertwine in one arm, where the Vps15 kinase domain engages the Vps34 activation loop to regulate its activity. |
| GO:0005515 protein binding | IPI PMID:24165940 Atg38 is required for autophagy-specific phosphatidylinosito... | REMOVE | Summary: Vps15 interaction (Araki et al.). Captured more informatively by PI3K complex I/II membership; bare protein binding is uninformative. Supporting Evidence: PMID:24165940 In atg38Ξ cells, autophagic activity was significantly reduced and PI3-kinase complex I dissociated into the Vps15-Vps34 and Atg14-Vps30 subcomplexes. |
| GO:0005515 protein binding | IPI PMID:24165940 Atg38 is required for autophagy-specific phosphatidylinosito... | REMOVE | Summary: Atg38 (Q05789) directly binds Vps34 and holds complex I together. Genuine, but captured better by complex I membership; bare protein binding is uninformative. Supporting Evidence: PMID:24165940 In atg38Ξ cells, autophagic activity was significantly reduced and PI3-kinase complex I dissociated into the Vps15-Vps34 and Atg14-Vps30 subcomplexes. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: Vps15 interaction from a proteome-wide interactome; redundant with complex membership and uninformative. Supporting Evidence: PMID:26450213 Vps34 and Vps15 intertwine in one arm, where the Vps15 kinase domain engages the Vps34 activation loop to regulate its activity. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Broad IBA 'cytoplasm' from the PI3K/PI4K family node; uninformative. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0005768 endosome | IBA GO_REF:0000033 | ACCEPT | Summary: IBA endosome localization from the PIK3C3 clade; Vps34 complex II localizes to endosomes. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0005768 endosome | IDA PMID:16421251 Assortment of phosphatidylinositol 3-kinase complexes--Atg14... | ACCEPT | Summary: Obara et al.: Vps34 punctate structures include endosomes, dependent on Vps38. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0005777 peroxisome | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA peroxisome. Vps34 associates with peroxisomes in yeast, but this is a specialised location related to pexophagy. Supporting Evidence: PMID:21121900 have demonstrated that the lipid kinase Vps34p is already associated with peroxisomes during biogenesis |
| GO:0005777 peroxisome | IDA PMID:21121900 The phosphoinositide 3-kinase Vps34p is required for pexopha... | KEEP AS NON CORE | Summary: Grunau et al. found PtdIns3P-synthesising activity and Vps34 associated with peroxisomes. Supporting Evidence: PMID:21121900 have demonstrated that the lipid kinase Vps34p is already associated with peroxisomes during biogenesis |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt SubCell mapping (Golgi apparatus) from the TGN membrane statement; minor location. Supporting Evidence: file:yeast/VPS34/VPS34-uniprot.txt SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane |
| GO:0005829 cytosol | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | KEEP AS NON CORE | Summary: HTP GFP library localization to cytosol. Vps34 is a peripheral membrane protein with a soluble pool; the active enzyme is membrane-associated. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | MODIFY | Summary: YeastPathways RCA default 'cytosol'. Vps34 phosphorylates PI on endosomal, vacuolar and PAS membranes; the location of activity is better given as endosome membrane (complex II) and PAS (complex I). Proposed replacements: endosome membrane Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0006897 endocytosis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA 'endocytosis' from the PIK3C3 clade. In yeast Vps34 PtdIns3P governs endosomal sorting and delivery to the vacuole rather than endocytic internalisation; retained as non-core. Supporting Evidence: PMID:11157979 two distinct Vps34 PtdIns 3-kinase complexes exist: one, containing Vps15p, Vps30p, and Apg14p, functions in autophagy and the other containing Vps15p, Vps30p, and Vps38p functions in CPY sorting |
| GO:0006914 autophagy | IDA PMID:24165940 Atg38 is required for autophagy-specific phosphatidylinosito... | ACCEPT | Summary: Araki et al.: Vps34-derived PtdIns3P is essential for autophagy and complex I integrity (via Atg38) is needed for full autophagic activity. Supporting Evidence: PMID:24165940 Autophagy is characterized by the formation of an autophagosome, for which Vps34-dervied phosphatidylinositol 3-phosphate (PI3P) is essential. PMID:24165940 In atg38Ξ cells, autophagic activity was significantly reduced and PI3-kinase complex I dissociated into the Vps15-Vps34 and Atg14-Vps30 subcomplexes. |
| GO:0010008 endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt SubCell mapping to endosome membrane; consistent with experimental data. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0010008 endosome membrane | NAS PMID:11157979 Two distinct Vps34 phosphatidylinositol 3-kinase complexes f... | ACCEPT | Summary: NAS (Kihara et al.) for endosome membrane; consistent with complex II localization. Supporting Evidence: PMID:11157979 two distinct Vps34 PtdIns 3-kinase complexes exist: one, containing Vps15p, Vps30p, and Apg14p, functions in autophagy and the other containing Vps15p, Vps30p, and Vps38p functions in CPY sorting PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0016020 membrane | IBA GO_REF:0000033 | TOO GENERAL | Summary: Generic 'membrane' IBA; true but uninformative. Supporting Evidence: PMID:16421251 Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes. |
| GO:0016236 macroautophagy | IMP PMID:32788210 Potassium starvation induces autophagy in yeast. | ACCEPT | Summary: Rangarajan et al.: potassium-starvation-induced autophagy requires Vps34 and the PI3K complex. Consistent with Vps34's core role in macroautophagy. Supporting Evidence: PMID:32788210 We found that potassium-dependent autophagy requires the core pathway kinases Atg1, Atg5, and Vps34, and other components of the phosphatidylinositol 3-kinase complex. |
| GO:0016301 kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro PI3/4-kinase domain mapping to generic kinase activity; the specific activity is PI 3-kinase. Proposed replacements: 1-phosphatidylinositol-3-kinase activity Supporting Evidence: PMID:7989323 Vps34p is a phosphatidylinositol-specific 3-kinase, as it is able to utilize phosphatidylinositol (PtdIns) but not PtdIns(4)P or PtdIns(4,5)P2 as substrates |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA PI 3-kinase activity from the PIK3C3 clade; Vps34 is the founding member with direct biochemical evidence. Supporting Evidence: PMID:7989323 Vps34p is a phosphatidylinositol-specific 3-kinase, as it is able to utilize phosphatidylinositol (PtdIns) but not PtdIns(4)P or PtdIns(4,5)P2 as substrates |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IDA PMID:7989323 Vps34p required for yeast vacuolar protein sorting is a mult... | ACCEPT | Summary: Stack and Emr: Vps34 is a PtdIns-specific 3-kinase in vitro. Supporting Evidence: PMID:7989323 Vps34p is a phosphatidylinositol-specific 3-kinase, as it is able to utilize phosphatidylinositol (PtdIns) but not PtdIns(4)P or PtdIns(4,5)P2 as substrates |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IDA PMID:8385367 Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene es... | ACCEPT | Summary: Schu et al.: overexpressed Vps34 increases PI 3-kinase activity that is immunoprecipitated with anti-Vps34. Supporting Evidence: PMID:8385367 Overexpression of Vps34p resulted in an increase in PI 3-kinase activity, and this activity was specifically precipitated with antisera to Vps34p. |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EC 2.7.1.137/RHEA:12709 and InterPro/ARBA mapping; correct. Supporting Evidence: file:yeast/VPS34/VPS34-uniprot.txt EC=2.7.1.137; Evidence={ECO:0000269|PubMed:7989323, |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IMP PMID:8385367 Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene es... | ACCEPT | Summary: Schu et al.: vps34 deletion or point mutants lack detectable PI 3-kinase activity. Supporting Evidence: PMID:8385367 Yeast strains deleted for the VPS34 gene or carrying vps34 point mutations lacked detectable PI 3-kinase activity and exhibited severe defects in vacuolar protein sorting. |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways PWY3O-242 places Vps34 on PI + ATP -> PI3P (EC 2.7.1.137); correct step. Supporting Evidence: PMID:7989323 Vps34p is a phosphatidylinositol-specific 3-kinase, as it is able to utilize phosphatidylinositol (PtdIns) but not PtdIns(4)P or PtdIns(4,5)P2 as substrates file:yeast/VPS34/VPS34-uniprot.txt EC=2.7.1.137; Evidence={ECO:0000269|PubMed:7989323, |
| GO:0032968 positive regulation of transcription elongation by RNA polymerase II | IMP PMID:23335340 Vps factors are required for efficient transcription elongat... | KEEP AS NON CORE | Summary: Gaur et al. found vps34 and vps15 mutants have transcription elongation phenotypes and that Vps factors crosslink to transcribed chromatin. Likely indirect, and mechanism unresolved; retained as non-core rather than overruling the experimental annotation. Supporting Evidence: PMID:23335340 yeast mutants lacking the phosphatidylinositol 3-phosphate [PI(3)P] kinase Vps34 or its associated protein kinase Vps15 display multiple phenotypes indicating impaired transcription elongation |
| GO:0033554 cellular response to stress | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ARBA mapping to 'cellular response to stress'; vague and not informative for Vps34. Supporting Evidence: PMID:32788210 We found that potassium-dependent autophagy requires the core pathway kinases Atg1, Atg5, and Vps34, and other components of the phosphatidylinositol 3-kinase complex. |
| GO:0034045 obsolete phagophore assembly site membrane | NAS PMID:24165940 Atg38 is required for autophagy-specific phosphatidylinosito... | MODIFY | Summary: Annotation to the obsolete term 'phagophore assembly site membrane'. GO obsoleted it because the PAS is not a membrane-bounded compartment; Vps34 complex I is recruited to the PAS (Atg14-dependent), so the appropriate replacement is phagophore assembly site. Proposed replacements: phagophore assembly site Supporting Evidence: PMID:16421251 The localization of these components to the PAS was Atg14p dependent but not dependent on Vps38p. |
| GO:0034271 phosphatidylinositol 3-kinase complex, class III, type I | IBA GO_REF:0000033 | ACCEPT | Summary: IBA complex I membership from the PIK3C3 clade. Supporting Evidence: PMID:11157979 two distinct Vps34 PtdIns 3-kinase complexes exist: one, containing Vps15p, Vps30p, and Apg14p, functions in autophagy and the other containing Vps15p, Vps30p, and Vps38p functions in CPY sorting |
| GO:0034271 phosphatidylinositol 3-kinase complex, class III, type I | IDA PMID:11157979 Two distinct Vps34 phosphatidylinositol 3-kinase complexes f... | ACCEPT | Summary: Kihara et al.: Vps34-Vps15-Vps30-Atg14 complex functions in autophagy (complex I). Supporting Evidence: PMID:11157979 two distinct Vps34 PtdIns 3-kinase complexes exist: one, containing Vps15p, Vps30p, and Apg14p, functions in autophagy and the other containing Vps15p, Vps30p, and Vps38p functions in CPY sorting |
| GO:0034271 phosphatidylinositol 3-kinase complex, class III, type I | IPI PMID:24165940 Atg38 is required for autophagy-specific phosphatidylinosito... | ACCEPT | Summary: Araki et al.: Atg38 is a stable complex I subunit linking Vps15-Vps34 and Atg14-Vps30. Supporting Evidence: PMID:24165940 In atg38Ξ cells, autophagic activity was significantly reduced and PI3-kinase complex I dissociated into the Vps15-Vps34 and Atg14-Vps30 subcomplexes. |
| GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | IBA GO_REF:0000033 | ACCEPT | Summary: IBA complex II membership from the PIK3C3 clade. Supporting Evidence: PMID:11157979 two distinct Vps34 PtdIns 3-kinase complexes exist: one, containing Vps15p, Vps30p, and Apg14p, functions in autophagy and the other containing Vps15p, Vps30p, and Vps38p functions in CPY sorting |
| GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | IDA PMID:11157979 Two distinct Vps34 phosphatidylinositol 3-kinase complexes f... | ACCEPT | Summary: Kihara et al.: Vps34-Vps15-Vps30-Vps38 complex functions in CPY sorting (complex II). Supporting Evidence: PMID:11157979 two distinct Vps34 PtdIns 3-kinase complexes exist: one, containing Vps15p, Vps30p, and Apg14p, functions in autophagy and the other containing Vps15p, Vps30p, and Vps38p functions in CPY sorting |
| GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | IPI PMID:26450213 Structure and flexibility of the endosomal Vps34 complex rev... | ACCEPT | Summary: Rostislavleva et al. solved the structure of yeast complex II (Vps34-Vps15-Vps30-Vps38). Supporting Evidence: PMID:26450213 We present the 4.4 angstrom crystal structure of the 385-kilodalton endosomal complex II PMID:26450213 Vps34 and Vps15 intertwine in one arm, where the Vps15 kinase domain engages the Vps34 activation loop to regulate its activity. |
| GO:0036092 phosphatidylinositol-3-phosphate biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: IBA PtdIns3P biosynthetic process; precise description of what Vps34 catalyses. Supporting Evidence: PMID:7989323 Vps34p is a phosphatidylinositol-specific 3-kinase, as it is able to utilize phosphatidylinositol (PtdIns) but not PtdIns(4)P or PtdIns(4,5)P2 as substrates |
| GO:0045324 late endosome to vacuole transport | NAS PMID:11157979 Two distinct Vps34 phosphatidylinositol 3-kinase complexes f... | ACCEPT | Summary: NAS (Kihara et al.). Vps34 complex II PtdIns3P is required for vacuolar protein sorting via endosomes; consistent with a role in endosome-to-vacuole transport. Supporting Evidence: PMID:11157979 two distinct Vps34 PtdIns 3-kinase complexes exist: one, containing Vps15p, Vps30p, and Apg14p, functions in autophagy and the other containing Vps15p, Vps30p, and Vps38p functions in CPY sorting PMID:8385367 Yeast strains deleted for the VPS34 gene or carrying vps34 point mutations lacked detectable PI 3-kinase activity and exhibited severe defects in vacuolar protein sorting. |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | IDA PMID:26450213 Structure and flexibility of the endosomal Vps34 complex rev... | ACCEPT | Summary: Complex II structure/activity study (Rostislavleva et al.). Vps34 synthesises PtdIns3P, so the parent 'phosphatidylinositol phosphate biosynthetic process' is correct; the more precise term phosphatidylinositol-3-phosphate biosynthetic process is also annotated. Supporting Evidence: PMID:26450213 We present the 4.4 angstrom crystal structure of the 385-kilodalton endosomal complex II |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | IDA PMID:7989323 Vps34p required for yeast vacuolar protein sorting is a mult... | ACCEPT | Summary: In vitro lipid kinase assays (Stack and Emr). Vps34 synthesises PtdIns3P, so the parent 'phosphatidylinositol phosphate biosynthetic process' is correct; the more precise term phosphatidylinositol-3-phosphate biosynthetic process is also annotated. Supporting Evidence: PMID:7989323 Vps34p is a phosphatidylinositol-specific 3-kinase, as it is able to utilize phosphatidylinositol (PtdIns) but not PtdIns(4)P or PtdIns(4,5)P2 as substrates |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | IDA PMID:8385367 Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene es... | ACCEPT | Summary: PI 3-kinase activity of Vps34 (Schu et al.). Vps34 synthesises PtdIns3P, so the parent 'phosphatidylinositol phosphate biosynthetic process' is correct; the more precise term phosphatidylinositol-3-phosphate biosynthetic process is also annotated. Supporting Evidence: PMID:8385367 Overexpression of Vps34p resulted in an increase in PI 3-kinase activity, and this activity was specifically precipitated with antisera to Vps34p. |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro mapping. Vps34 synthesises PtdIns3P, so the parent 'phosphatidylinositol phosphate biosynthetic process' is correct; the more precise term phosphatidylinositol-3-phosphate biosynthetic process is also annotated. Supporting Evidence: file:yeast/VPS34/VPS34-uniprot.txt EC=2.7.1.137; Evidence={ECO:0000269|PubMed:7989323, |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | IMP PMID:8385367 Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene es... | ACCEPT | Summary: vps34 mutants lack PI 3-kinase activity (Schu et al.). Vps34 synthesises PtdIns3P, so the parent 'phosphatidylinositol phosphate biosynthetic process' is correct; the more precise term phosphatidylinositol-3-phosphate biosynthetic process is also annotated. Supporting Evidence: PMID:8385367 Yeast strains deleted for the VPS34 gene or carrying vps34 point mutations lacked detectable PI 3-kinase activity and exhibited severe defects in vacuolar protein sorting. |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | NAS PMID:24165940 Atg38 is required for autophagy-specific phosphatidylinosito... | ACCEPT | Summary: NAS (Araki et al.). Vps34 synthesises PtdIns3P, so the parent 'phosphatidylinositol phosphate biosynthetic process' is correct; the more precise term phosphatidylinositol-3-phosphate biosynthetic process is also annotated. Supporting Evidence: PMID:24165940 Autophagy is characterized by the formation of an autophagosome, for which Vps34-dervied phosphatidylinositol 3-phosphate (PI3P) is essential. |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways PWY3O-242 RCA. Vps34 synthesises PtdIns3P, so the parent 'phosphatidylinositol phosphate biosynthetic process' is correct; the more precise term phosphatidylinositol-3-phosphate biosynthetic process is also annotated. Supporting Evidence: PMID:7989323 Vps34p is a phosphatidylinositol-specific 3-kinase, as it is able to utilize phosphatidylinositol (PtdIns) but not PtdIns(4)P or PtdIns(4,5)P2 as substrates file:yeast/VPS34/VPS34-uniprot.txt EC=2.7.1.137; Evidence={ECO:0000269|PubMed:7989323, |
| GO:0048015 phosphatidylinositol-mediated signaling | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA 'phosphatidylinositol-mediated signaling'; PtdIns3P recruits effectors, but the term is broad. Supporting Evidence: PMID:16839886 We demonstrate that Gpa1 is present at endosomes, where it interacts directly with both Vps34 and Vps15 and stimulates increased production of phosphatidylinositol 3-phosphate. |
| GO:0051365 cellular response to potassium ion starvation | IMP PMID:32788210 Potassium starvation induces autophagy in yeast. | KEEP AS NON CORE | Summary: Rangarajan et al.: Vps34 is required for autophagy induced by potassium starvation; a condition-specific readout of the core autophagy role. Supporting Evidence: PMID:32788210 We found that potassium-dependent autophagy requires the core pathway kinases Atg1, Atg5, and Vps34, and other components of the phosphatidylinositol 3-kinase complex. |
| GO:0071561 nucleus-vacuole junction | IDA PMID:23335340 Vps factors are required for efficient transcription elongat... | KEEP AS NON CORE | Summary: Gaur et al. observed a fraction of Vps34-GFP at nucleus-vacuole junctions; minor location, non-core. Supporting Evidence: PMID:23335340 We also observed colocalization of a fraction of Vps15-GFP and Vps34-GFP with nuclear pores at nucleus-vacuole (NV) junctions in live cells. |
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