UVRAG

UniProt ID: Q9P2Y5
Organism: Homo sapiens
Review Status: COMPLETE
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Gene Description

UVRAG is a regulatory/adaptor subunit of the UVRAG-containing class III PI3K complex II (PI3KC3-C2) and a late autophagy/endolysosomal trafficking factor. It binds Beclin 1/PIK3C3 complex machinery, supports PI3P-dependent autophagosome maturation, and coordinates HOPS/class C VPS and SNARE-dependent fusion events at autophagosomes and endosomes. UVRAG also has supported but non-core roles in Golgi-ER retrograde trafficking, degradative endocytic traffic, cytokinesis, and autophagy-independent DNA repair/centrosome stability.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000323 lytic vacuole
IBA
GO_REF:0000033 		MODIFY
Summary: Lytic vacuole is a non-human/generalized ancestor for UVRAG lysosome/endolysosomal localization.
Reason: For human UVRAG, lysosome, late endosome, and autophagosome/autophagosome membrane are more precise locations for the late autophagy and endosomal trafficking role.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Late endosome {ECO:0000269|PubMed:18843052}
file:human/UVRAG/UVRAG-uniprot.txt
Cytoplasmic vesicle, autophagosome
file:human/UVRAG/UVRAG-uniprot.txt
Early endosome {ECO:0000269|PubMed:18552835
GO:0000149 SNARE binding
IBA
GO_REF:0000033 		ACCEPT
Summary: SNARE binding is supported for UVRAG in late endosomal/autophagosome fusion contexts.
Reason: UVRAG interacts with endosomal SNARE machinery and promotes fusogenic SNARE complex formation with class C VPS/HOPS-associated trafficking machinery.
Supporting Evidence:
PMID:24550300
interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and endosomal
PMID:24550300
by assembling a specific fusogenic SNARE complex
file:human/UVRAG/UVRAG-uniprot.txt
SNARE complex and promotes fusogenic SNARE complex formation during
GO:0035493 SNARE complex assembly
IBA
GO_REF:0000033 		ACCEPT
Summary: SNARE complex assembly captures a specific UVRAG role in late endosomal/autophagosome fusion machinery.
Reason: UVRAG promotes fusogenic SNARE complex formation in class C VPS/HOPS-dependent membrane fusion, making this more informative than generic protein binding.
Supporting Evidence:
PMID:24550300
interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and endosomal
PMID:24550300
by assembling a specific fusogenic SNARE complex
file:human/UVRAG/UVRAG-uniprot.txt
SNARE complex and promotes fusogenic SNARE complex formation during
GO:0000775 chromosome, centromeric region
IEA
GO_REF:0000044 		KEEP AS NON CORE
Summary: Centromeric/chromosome localization is experimentally tied to UVRAG genome-stability biology but is not PN core.
Reason: UVRAG has an autophagy-independent DNA repair and chromosome/centrosome stability branch. Retain as non-core relative to class III PI3K/autophagosome maturation biology.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0005764 lysosome
IEA
GO_REF:0000044 		ACCEPT
Summary: Lysosome localization is compatible with UVRAG late autophagy/endolysosomal trafficking.
Reason: UVRAG functions in autophagosome fusion with late endosomes/lysosomes and endocytic cargo delivery to degradative compartments.
Supporting Evidence:
PMID:18552835
autophagosome fusion with late endosomes/lysosomes
file:human/UVRAG/UVRAG-uniprot.txt
Lysosome {ECO:0000269|PubMed:18843052}
GO:0005769 early endosome
IEA
GO_REF:0000044 		ACCEPT
Summary: Early endosome localization is supported for UVRAG endosomal trafficking biology.
Reason: UVRAG is found on endosomal compartments and contributes to endosome/endosome fusion and degradative endocytic trafficking.
Supporting Evidence:
PMID:18552835
endosome-endosome fusion, resulting in rapid degradation of endocytic cargo
file:human/UVRAG/UVRAG-uniprot.txt
Early endosome {ECO:0000269|PubMed:18552835
GO:0005770 late endosome
IEA
GO_REF:0000044 		ACCEPT
Summary: Late endosome localization is supported and relevant to UVRAG autophagosome/endosome maturation.
Reason: The UVRAG-class C VPS/HOPS axis promotes autophagosome fusion with late endosomes/lysosomes and late endocytic fusion.
Supporting Evidence:
PMID:18552835
autophagosome fusion with late endosomes/lysosomes
file:human/UVRAG/UVRAG-uniprot.txt
Late endosome {ECO:0000269|PubMed:18843052}
GO:0005776 autophagosome
IEA
GO_REF:0000044 		ACCEPT
Summary: Autophagosome localization is directly relevant to UVRAG/PACER-mediated autophagosome maturation.
Reason: UVRAG is recruited to autophagosome-associated structures and participates in PI3KC3/HOPS activation during autophagosome maturation.
Supporting Evidence:
PMID:28306502
Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
file:human/UVRAG/UVRAG-uniprot.txt
Cytoplasmic vesicle, autophagosome
GO:0005783 endoplasmic reticulum
IEA
GO_REF:0000044 		KEEP AS NON CORE
Summary: Endoplasmic reticulum localization is supported for the RINT1/NRZ retrograde trafficking branch.
Reason: UVRAG has a PtdIns(3)P-dependent ER tethering and Golgi-ER retrograde transport role. This is supported but secondary to the PN class III PI3K/autophagosome maturation focus.
Supporting Evidence:
PMID:24056303
PtdIns(3)P)-binding protein
PMID:24056303
acts as an integral component of the RINT-1-containing ER tethering complex
PMID:24056303
Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
GO:0006914 autophagy
IEA
GO_REF:0000117 		MODIFY
Summary: Broad autophagy is directionally correct but should be narrowed to UVRAG autophagosome maturation/positive autophagy regulation.
Reason: UVRAG regulates class III PI3K/HOPS-dependent autophagosome maturation and Beclin1-PI3KC3 autophagy signaling; the parent autophagy term loses that specificity.
Supporting Evidence:
PMID:16799551
positive regulator of the Beclin1-PI(3)KC3 complex
PMID:18843052
Atg14, and UVRAG are not present in the same complex
file:human/UVRAG/UVRAG-uniprot.txt
acts as a regulatory subunit of the alternative PI3K complex II
file:human/UVRAG/UVRAG-uniprot.txt
mediates formation of phosphatidylinositol 3-phosphate
PMID:18552835
interacts with the class C Vps complex
PMID:18552835
autophagosome fusion with late endosomes/lysosomes
GO:0016192 vesicle-mediated transport
IEA
GO_REF:0000117 		MODIFY
Summary: Vesicle-mediated transport is too broad for UVRAG; the supported processes are Golgi-ER retrograde transport and endolysosomal/autophagic trafficking.
Reason: UVRAG couples PtdIns(3)P-dependent ER tethering, ATG9 transport, endosome fusion, and autophagosome maturation. More specific transport terms should be used instead of the broad parent.
Supporting Evidence:
PMID:18552835
interacts with the class C Vps complex
PMID:18552835
autophagosome fusion with late endosomes/lysosomes
PMID:24056303
PtdIns(3)P)-binding protein
PMID:24056303
acts as an integral component of the RINT-1-containing ER tethering complex
PMID:24056303
Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
GO:0030496 midbody
IEA
GO_REF:0000044 		KEEP AS NON CORE
Summary: Midbody localization is supported for UVRAG cytokinesis biology but is not PN core.
Reason: The PI3KC3-C2/BIF-1-containing subcomplex has a supported cytokinesis/midbody branch; retain it as non-core relative to autophagosome maturation.
Supporting Evidence:
PMID:20643123
strong localisation of these proteins to the midbody
file:human/UVRAG/UVRAG-uniprot.txt
Midbody
GO:0031410 cytoplasmic vesicle
IEA
GO_REF:0000117 		MODIFY
Summary: Cytoplasmic vesicle is true but too broad for UVRAG localization.
Reason: UVRAG is better localized to autophagosome/autophagosome membrane and early/late endosome compartments relevant to PI3KC3-C2 and HOPS/SNARE trafficking.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Late endosome {ECO:0000269|PubMed:18843052}
file:human/UVRAG/UVRAG-uniprot.txt
Cytoplasmic vesicle, autophagosome
file:human/UVRAG/UVRAG-uniprot.txt
Early endosome {ECO:0000269|PubMed:18552835
GO:0036092 phosphatidylinositol-3-phosphate biosynthetic process
IEA
GO_REF:0000117 		ACCEPT
Summary: UVRAG is involved in PI3P biosynthesis as a PI3KC3-C2 regulatory subunit rather than as the lipid kinase itself.
Reason: UVRAG activates/regulates PIK3C3/VPS34 within PI3KC3-C2, which mediates formation of phosphatidylinositol 3-phosphate during autophagy/endosomal trafficking.
Supporting Evidence:
PMID:16799551
positive regulator of the Beclin1-PI(3)KC3 complex
PMID:18843052
Atg14, and UVRAG are not present in the same complex
file:human/UVRAG/UVRAG-uniprot.txt
acts as a regulatory subunit of the alternative PI3K complex II
file:human/UVRAG/UVRAG-uniprot.txt
mediates formation of phosphatidylinositol 3-phosphate
GO:0043933 protein-containing complex organization
IEA
GO_REF:0000117 		MODIFY
Summary: Protein-containing complex organization is too broad for UVRAG; SNARE/HOPS and PI3KC3-C2 complex roles are more specific.
Reason: UVRAG participates in specific PI3KC3-C2, HOPS/class C VPS, and SNARE assembly contexts. Generic complex organization should be replaced by the specific supported complex/process annotations.
Supporting Evidence:
PMID:24550300
interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and endosomal
PMID:24550300
by assembling a specific fusogenic SNARE complex
file:human/UVRAG/UVRAG-uniprot.txt
SNARE complex and promotes fusogenic SNARE complex formation during
PMID:16799551
positive regulator of the Beclin1-PI(3)KC3 complex
PMID:18843052
Atg14, and UVRAG are not present in the same complex
GO:0005515 protein binding
IPI
PMID:17891140
Bif-1 interacts with Beclin 1 through UVRAG and regulates au... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:19050071
Identification of Barkor as a mammalian autophagy-specific f... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:20562859
Network organization of the human autophagy system. 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:21062745
The RUN domain of rubicon is important for hVps34 binding, l... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:21597469
UV irradiation resistance-associated gene suppresses apoptos... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:22081109
Inhibition of autophagy by TAB2 and TAB3. 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:22493499
Receptor signaling lymphocyte-activation molecule family 1 (... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:23954414
Beclin 2 functions in autophagy, degradation of G protein-co... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:24034250
EGFR-mediated Beclin 1 phosphorylation in autophagy suppress... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:24056303
PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and A... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:24554770
The HOPS complex mediates autophagosome-lysosome fusion thro... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:24785657
NRBF2 regulates macroautophagy as a component of Vps34 Compl... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:24849286
NRBF2 regulates autophagy and prevents liver injury by modul... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:25490155
Architecture and dynamics of the autophagic phosphatidylinos... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:26496610
A human interactome in three quantitative dimensions organiz... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:32296183
A reference map of the human binary protein interactome. 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:33961781
Dual proteome-scale networks reveal cell-specific remodeling... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:34386498
ORF3a-Mediated Incomplete Autophagy Facilitates Severe Acute... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:35044719
Proteome-scale mapping of binding sites in the unstructured ... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:35271311
OpenCell: Endogenous tagging for the cartography of human ce... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:37219487
Large-scale phosphomimetic screening identifies phospho-modu... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0000149 SNARE binding
IEA
GO_REF:0000107 		ACCEPT
Summary: SNARE binding is supported for UVRAG in late endosomal/autophagosome fusion contexts.
Reason: UVRAG interacts with endosomal SNARE machinery and promotes fusogenic SNARE complex formation with class C VPS/HOPS-associated trafficking machinery.
Supporting Evidence:
PMID:24550300
interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and endosomal
PMID:24550300
by assembling a specific fusogenic SNARE complex
file:human/UVRAG/UVRAG-uniprot.txt
SNARE complex and promotes fusogenic SNARE complex formation during
GO:0006281 DNA repair
IEA
GO_REF:0000120 		KEEP AS NON CORE
Summary: DNA repair is supported for UVRAG but is an autophagy-independent non-core branch in this PN review.
Reason: The strongest evidence supports UVRAG activation of DNA-PK in NHEJ and chromosomal stability, but this should not be treated as the proteostasis/autophagy core function.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0007051 spindle organization
IEA
GO_REF:0000107 		KEEP AS NON CORE
Summary: Spindle organization is a non-core inference from UVRAG centrosome/chromosome stability biology.
Reason: The paper supports proper chromosome segregation and centrosome stability, but this is outside the class III PI3K/autophagosome maturation core.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0007059 chromosome segregation
IEA
GO_REF:0000107 		KEEP AS NON CORE
Summary: Chromosome segregation is supported by UVRAG centrosome/chromosome stability evidence but is non-core.
Reason: UVRAG disruption causes centrosome instability and aneuploidy; retain as non-core genome-stability biology.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0007098 centrosome cycle
IEA
GO_REF:0000120 		KEEP AS NON CORE
Summary: Centrosome cycle is supported as a non-core centrosome stability/chromosome segregation branch.
Reason: UVRAG interacts with CEP63 and is required for centrosome stability, but this is separate from the PN autophagy/endolysosomal core.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0017124 SH3 domain binding
IEA
GO_REF:0000107 		KEEP AS NON CORE
Summary: SH3 domain binding is compatible with the SH3GLB1/Bif-1 interaction but is not the core UVRAG function.
Reason: The SH3GLB1 interaction helps connect UVRAG to BECN1/PI3KC3-C2, but the more informative annotations are PI3KC3-C2 membership and autophagosome/endosomal trafficking roles.
Supporting Evidence:
PMID:17891140
Bif-1 interacts with Beclin 1 through UVRAG
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with SH3GLB1
GO:0032991 protein-containing complex
IEA
GO_REF:0000120 		MODIFY
Summary: Protein-containing complex is correct but too generic for UVRAG.
Reason: UVRAG is a component/regulatory subunit of the UVRAG-containing PI3KC3-C2 complex; the generic complex term should be narrowed to the type II class III PI3K complex.
Supporting Evidence:
PMID:16799551
positive regulator of the Beclin1-PI(3)KC3 complex
PMID:18843052
Atg14, and UVRAG are not present in the same complex
file:human/UVRAG/UVRAG-uniprot.txt
acts as a regulatory subunit of the alternative PI3K complex II
file:human/UVRAG/UVRAG-uniprot.txt
mediates formation of phosphatidylinositol 3-phosphate
GO:0045335 phagocytic vesicle
IEA
GO_REF:0000107 		KEEP AS NON CORE
Summary: Phagocytic vesicle context is supported through SLAMF1/Vps34/Beclin1/UVRAG phagosome signaling but is non-core.
Reason: This is a macrophage/phagosome-specific branch of UVRAG-containing class III PI3K signaling rather than the central autophagosome maturation role.
Supporting Evidence:
PMID:22493499
Slamf1 interacts with the class III PI3K Vps34 in a complex with Beclin-1 and UVRAG
PMID:22493499
Slamf1 recruits a subset of Vps34-associated proteins
GO:0010506 regulation of autophagy
IDA
PMID:16799551
Autophagic and tumour suppressor activity of a novel Beclin1... 		MODIFY
Summary: UVRAG positively regulates Beclin1-PI3KC3 autophagy activity, so the undirected regulation term should be narrowed.
Reason: The cited evidence presents UVRAG as a positive regulator/activator of the Beclin1-PI3KC3 complex and autophagy, not merely an unspecified regulator.
Supporting Evidence:
PMID:16799551
positive regulator of the Beclin1-PI(3)KC3 complex
PMID:16799551
UVRAG-mediated activation of the Beclin1-PI(3)KC3 complex promotes autophagy
GO:0035032 phosphatidylinositol 3-kinase complex, class III
IPI
PMID:25490155
Architecture and dynamics of the autophagic phosphatidylinos... 		MODIFY
Summary: Generic class III PI3K complex membership is correct but underspecified for UVRAG.
Reason: UVRAG defines the type II/PI3KC3-C2 branch rather than the ATG14-containing type I complex. The GO term should be narrowed to class III PI3K complex type II.
Supporting Evidence:
PMID:16799551
positive regulator of the Beclin1-PI(3)KC3 complex
PMID:18843052
Atg14, and UVRAG are not present in the same complex
file:human/UVRAG/UVRAG-uniprot.txt
acts as a regulatory subunit of the alternative PI3K complex II
file:human/UVRAG/UVRAG-uniprot.txt
mediates formation of phosphatidylinositol 3-phosphate
GO:0036092 phosphatidylinositol-3-phosphate biosynthetic process
IDA
PMID:8999962
Characterization of p150, an adaptor protein for the human p... 		ACCEPT
Summary: UVRAG is involved in PI3P biosynthesis as a PI3KC3-C2 regulatory subunit rather than as the lipid kinase itself.
Reason: UVRAG activates/regulates PIK3C3/VPS34 within PI3KC3-C2, which mediates formation of phosphatidylinositol 3-phosphate during autophagy/endosomal trafficking.
Supporting Evidence:
PMID:16799551
positive regulator of the Beclin1-PI(3)KC3 complex
PMID:18843052
Atg14, and UVRAG are not present in the same complex
file:human/UVRAG/UVRAG-uniprot.txt
acts as a regulatory subunit of the alternative PI3K complex II
file:human/UVRAG/UVRAG-uniprot.txt
mediates formation of phosphatidylinositol 3-phosphate
GO:0005769 early endosome
EXP
PMID:18552835
Beclin1-binding UVRAG targets the class C Vps complex to coo... 		ACCEPT
Summary: Early endosome localization is supported for UVRAG endosomal trafficking biology.
Reason: UVRAG is found on endosomal compartments and contributes to endosome/endosome fusion and degradative endocytic trafficking.
Supporting Evidence:
PMID:18552835
endosome-endosome fusion, resulting in rapid degradation of endocytic cargo
file:human/UVRAG/UVRAG-uniprot.txt
Early endosome {ECO:0000269|PubMed:18552835
GO:0033116 endoplasmic reticulum-Golgi intermediate compartment membrane
TAS
Reactome:R-HSA-9730505 		MARK AS OVER ANNOTATED
Summary: ERGIC membrane is a virus-event-specific Reactome localization and is too specific for general UVRAG biology.
Reason: The Reactome event records SARS-CoV-2 3a binding to UVRAG and disruption of a Beclin1:VPS34:UVRAG complex; it does not establish ERGIC membrane as a stable UVRAG cellular component. ER and autophagosome/endosome locations are better supported.
Supporting Evidence:
Reactome:R-HSA-9730505
SARS-CoV-2 3a binds to UVRAG
file:human/UVRAG/UVRAG-uniprot.txt
Endoplasmic reticulum {ECO:0000269|PubMed:24056303}
GO:0000421 autophagosome membrane
IDA
PMID:28306502
Pacer Mediates the Function of Class III PI3K and HOPS Compl... 		ACCEPT
Summary: Autophagosome membrane localization is directly supported for UVRAG/PACER-mediated maturation.
Reason: UVRAG is recruited to autophagosomes through RUBCNL/PACER and supports local PI3KC3/HOPS activity for autophagosome maturation.
Supporting Evidence:
PMID:28306502
Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
file:human/UVRAG/UVRAG-uniprot.txt
Recruited to autophagosome following interaction with RUBCNL/PACER
GO:0005515 protein binding
IPI
PMID:28306502
Pacer Mediates the Function of Class III PI3K and HOPS Compl... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0097352 autophagosome maturation
IDA
PMID:28306502
Pacer Mediates the Function of Class III PI3K and HOPS Compl... 		ACCEPT
Summary: Autophagosome maturation is a core UVRAG process.
Reason: UVRAG coordinates PI3KC3/HOPS/class C VPS machinery and autophagosome-lysosome/endosome fusion during late autophagy.
Supporting Evidence:
PMID:18552835
interacts with the class C Vps complex
PMID:18552835
autophagosome fusion with late endosomes/lysosomes
PMID:28306502
Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
file:human/UVRAG/UVRAG-uniprot.txt
Involved in maturation of autophagosomes and degradative endocytic trafficking
PMID:25533187
UVRAG is released from RUBICON to interact with the HOPS complex
GO:0005515 protein binding
IPI
PMID:28479384
Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in ... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:1901098 positive regulation of autophagosome maturation
TAS
PMID:21118109
The role of ESCRT proteins in fusion events involving lysoso... 		ACCEPT
Summary: Positive regulation of autophagosome maturation is core and well supported.
Reason: UVRAG enhances autophagosome/endosome maturation via HOPS/class C VPS engagement and is released from inhibitory RUBICON interaction upon dephosphorylation.
Supporting Evidence:
PMID:18552835
interacts with the class C Vps complex
PMID:18552835
autophagosome fusion with late endosomes/lysosomes
PMID:28306502
Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
file:human/UVRAG/UVRAG-uniprot.txt
Involved in maturation of autophagosomes and degradative endocytic trafficking
PMID:25533187
enhances autophagosome and endosome maturation
GO:0071985 multivesicular body sorting pathway
TAS
PMID:21118109
The role of ESCRT proteins in fusion events involving lysoso... 		KEEP AS NON CORE
Summary: Multivesicular body/endosomal sorting is supported but non-core in the PN autophagy review.
Reason: UVRAG contributes to degradative endocytic trafficking and endosome fusion, but the PN core is PI3KC3-C2/autophagosome maturation.
Supporting Evidence:
PMID:18552835
endosome-endosome fusion, resulting in rapid degradation of endocytic cargo
PMID:20643123
regulates both receptor degradation and cytokinesis
GO:0005813 centrosome
IDA
PMID:22542840
A dual role for UVRAG in maintaining chromosomal stability i... 		KEEP AS NON CORE
Summary: Centrosome localization is supported but non-core.
Reason: UVRAG localizes to centrosomes and interacts with CEP63 in an autophagy-independent chromosome-stability branch.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0006281 DNA repair
IMP
PMID:22542840
A dual role for UVRAG in maintaining chromosomal stability i... 		KEEP AS NON CORE
Summary: DNA repair is supported for UVRAG but is an autophagy-independent non-core branch in this PN review.
Reason: The strongest evidence supports UVRAG activation of DNA-PK in NHEJ and chromosomal stability, but this should not be treated as the proteostasis/autophagy core function.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0007098 centrosome cycle
IMP
PMID:22542840
A dual role for UVRAG in maintaining chromosomal stability i... 		KEEP AS NON CORE
Summary: Centrosome cycle is supported as a non-core centrosome stability/chromosome segregation branch.
Reason: UVRAG interacts with CEP63 and is required for centrosome stability, but this is separate from the PN autophagy/endolysosomal core.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0070418 DNA-dependent protein kinase complex
IDA
PMID:22542840
A dual role for UVRAG in maintaining chromosomal stability i... 		KEEP AS NON CORE
Summary: DNA-PK complex colocalization/association is supported but non-core.
Reason: UVRAG binds/activates DNA-PK for NHEJ, but this genome-stability function is outside the PN autophagosome maturation core.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0071900 regulation of protein serine/threonine kinase activity
IDA
PMID:22542840
A dual role for UVRAG in maintaining chromosomal stability i... 		KEEP AS NON CORE
Summary: Regulation of serine/threonine kinase activity is supported through DNA-PK activation but is broad and non-core.
Reason: The specific supported kinase is DNA-PK in NHEJ; this should not be interpreted as a core proteostasis/autophagy function.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0097680 double-strand break repair via classical nonhomologous end joining
IDA
PMID:22542840
A dual role for UVRAG in maintaining chromosomal stability i... 		KEEP AS NON CORE
Summary: Classical NHEJ is supported for UVRAG but non-core.
Reason: UVRAG promotes DNA-PK-dependent NHEJ and chromosome stability, but this is a separate autophagy-independent branch.
Supporting Evidence:
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
PMID:22542840
centrosome instability and aneuploidy
file:human/UVRAG/UVRAG-uniprot.txt
Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
GO:0030496 midbody
IDA
PMID:20643123
A phosphatidylinositol 3-kinase class III sub-complex contai... 		KEEP AS NON CORE
Summary: Midbody localization is supported for UVRAG cytokinesis biology but is not PN core.
Reason: The PI3KC3-C2/BIF-1-containing subcomplex has a supported cytokinesis/midbody branch; retain it as non-core relative to autophagosome maturation.
Supporting Evidence:
PMID:20643123
strong localisation of these proteins to the midbody
file:human/UVRAG/UVRAG-uniprot.txt
Midbody
GO:0032465 regulation of cytokinesis
IMP
PMID:20643123
A phosphatidylinositol 3-kinase class III sub-complex contai... 		KEEP AS NON CORE
Summary: Regulation of cytokinesis is supported through the UVRAG/BIF-1 PI3KC3 subcomplex but non-core.
Reason: The cytokinesis/midbody role is experimentally supported, but it is distinct from the PN autophagosome maturation function.
Supporting Evidence:
PMID:20643123
regulates both receptor degradation and cytokinesis
PMID:20643123
strong localisation of these proteins to the midbody
GO:0032801 receptor catabolic process
IMP
PMID:20643123
A phosphatidylinositol 3-kinase class III sub-complex contai... 		KEEP AS NON CORE
Summary: Receptor catabolic process is supported but non-core.
Reason: UVRAG-containing PI3KC3-C2/BIF-1 machinery regulates degradative endocytic traffic and receptor degradation, but this is secondary to the PN autophagy review.
Supporting Evidence:
PMID:20643123
regulates both receptor degradation and cytokinesis
PMID:25533187
facilitates the lysosomal degradation of epidermal growth factor receptor
GO:0005783 endoplasmic reticulum
IDA
PMID:24056303
PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and A... 		KEEP AS NON CORE
Summary: Endoplasmic reticulum localization is supported for the RINT1/NRZ retrograde trafficking branch.
Reason: UVRAG has a PtdIns(3)P-dependent ER tethering and Golgi-ER retrograde transport role. This is supported but secondary to the PN class III PI3K/autophagosome maturation focus.
Supporting Evidence:
PMID:24056303
PtdIns(3)P)-binding protein
PMID:24056303
acts as an integral component of the RINT-1-containing ER tethering complex
PMID:24056303
Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
IMP
PMID:24056303
PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and A... 		KEEP AS NON CORE
Summary: Golgi-to-ER retrograde transport is supported for UVRAG and retained as non-core trafficking biology.
Reason: UVRAG binds PtdIns(3)P, associates with the RINT1/NRZ ER tethering complex, and coordinates COPI cargo transfer; this is a real trafficking branch outside the core PN autophagosome maturation term.
Supporting Evidence:
PMID:24056303
PtdIns(3)P)-binding protein
PMID:24056303
acts as an integral component of the RINT-1-containing ER tethering complex
PMID:24056303
Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
GO:0006914 autophagy
IMP
PMID:24056303
PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and A... 		MODIFY
Summary: The PMID:24056303 evidence is better captured as ATG9/autophagy-related trafficking rather than broad autophagy.
Reason: This paper supports UVRAG movement between ER tethering and Beclin/Bif-1/PI3KC3 machinery to mobilize ATG9 transport; autophagy is too broad for the specific mechanism.
Supporting Evidence:
PMID:24056303
PtdIns(3)P)-binding protein
PMID:24056303
acts as an integral component of the RINT-1-containing ER tethering complex
PMID:24056303
Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
GO:0051684 maintenance of Golgi location
IMP
PMID:24056303
PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and A... 		KEEP AS NON CORE
Summary: Maintenance of Golgi location is supported through the UVRAG/RINT1 retrograde trafficking branch but non-core.
Reason: Knockdown/displacement of UVRAG disrupts COPI cargo transfer and Golgi integrity, but this is secondary to PI3KC3-C2/autophagy maturation in the PN context.
Supporting Evidence:
PMID:24056303
PtdIns(3)P)-binding protein
PMID:24056303
acts as an integral component of the RINT-1-containing ER tethering complex
PMID:24056303
Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
GO:0005515 protein binding
IPI
PMID:22354037
Genome-wide siRNA screen reveals amino acid starvation-induc... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005515 protein binding
IPI
PMID:19270696
Two Beclin 1-binding proteins, Atg14L and Rubicon, reciproca... 		MARK AS OVER ANNOTATED
Summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG function.
Reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other assemblies. Retaining protein binding obscures the biological function and should be replaced by specific complex membership or binding terms where curatable.
Supporting Evidence:
file:human/UVRAG/UVRAG-uniprot.txt
Component of the PI3K (PI3KC3/PI3K-III/class III
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with VPS16; VPS11; VPS18; VPS33
file:human/UVRAG/UVRAG-uniprot.txt
Interacts with PRKDC, XRCC6 and XRCC5
GO:0005764 lysosome
IDA
PMID:19270696
Two Beclin 1-binding proteins, Atg14L and Rubicon, reciproca... 		ACCEPT
Summary: Lysosome localization is compatible with UVRAG late autophagy/endolysosomal trafficking.
Reason: UVRAG functions in autophagosome fusion with late endosomes/lysosomes and endocytic cargo delivery to degradative compartments.
Supporting Evidence:
PMID:18552835
autophagosome fusion with late endosomes/lysosomes
file:human/UVRAG/UVRAG-uniprot.txt
Lysosome {ECO:0000269|PubMed:18843052}
GO:0005769 early endosome
IDA
PMID:19270696
Two Beclin 1-binding proteins, Atg14L and Rubicon, reciproca... 		ACCEPT
Summary: Early endosome localization is supported for UVRAG endosomal trafficking biology.
Reason: UVRAG is found on endosomal compartments and contributes to endosome/endosome fusion and degradative endocytic trafficking.
Supporting Evidence:
PMID:18552835
endosome-endosome fusion, resulting in rapid degradation of endocytic cargo
file:human/UVRAG/UVRAG-uniprot.txt
Early endosome {ECO:0000269|PubMed:18552835
GO:0005770 late endosome
IDA
PMID:19270696
Two Beclin 1-binding proteins, Atg14L and Rubicon, reciproca... 		ACCEPT
Summary: Late endosome localization is supported and relevant to UVRAG autophagosome/endosome maturation.
Reason: The UVRAG-class C VPS/HOPS axis promotes autophagosome fusion with late endosomes/lysosomes and late endocytic fusion.
Supporting Evidence:
PMID:18552835
autophagosome fusion with late endosomes/lysosomes
file:human/UVRAG/UVRAG-uniprot.txt
Late endosome {ECO:0000269|PubMed:18843052}
GO:0005737 cytoplasm
TAS
PMID:9169138
Molecular cloning of a novel human gene encoding a 63-kDa pr... 		KEEP AS NON CORE
Summary: Cytoplasm is a broad legacy localization for UVRAG.
Reason: The original cloning paper supports a cytoplasmic protein, but current evidence localizes UVRAG more specifically to endosomes, autophagosomes, ER, midbody, and chromosome/centrosome contexts.
Supporting Evidence:
PMID:9169138
novel 63-kDa cytoplasmic protein
file:human/UVRAG/UVRAG-uniprot.txt
Cytoplasmic vesicle, autophagosome
GO:0006281 DNA repair
TAS
PMID:9169138
Molecular cloning of a novel human gene encoding a 63-kDa pr... 		KEEP AS NON CORE
Summary: DNA repair is supported for UVRAG but is an autophagy-independent non-core branch in this PN review.
Reason: The strongest evidence supports UVRAG activation of DNA-PK in NHEJ and chromosomal stability, but this should not be treated as the proteostasis/autophagy core function.
Supporting Evidence:
PMID:9169138
novel 63-kDa cytoplasmic protein
PMID:22542840
UVRAG promotes DNA double-strand-break repair by directly binding and activating
GO:0030674 protein-macromolecule adaptor activity
IDA
PMID:16799551
Autophagic and tumour suppressor activity of a novel Beclin1... 		NEW
Summary: UVRAG has a supported adaptor/regulatory subunit role in PI3KC3-C2 and late fusion machinery.
Reason: Add this as a more informative molecular-function annotation than generic protein binding. UVRAG links BECN1/PIK3C3 complex machinery with class C VPS/HOPS and SNARE-dependent trafficking during autophagosome/endosome maturation.
Supporting Evidence:
PMID:16799551
positive regulator of the Beclin1-PI(3)KC3 complex
PMID:18843052
Atg14, and UVRAG are not present in the same complex
PMID:18552835
interacts with the class C Vps complex
PMID:24550300
by assembling a specific fusogenic SNARE complex
file:human/UVRAG/UVRAG-uniprot.txt
acts as a regulatory subunit of the alternative PI3K complex II

Core Functions

UVRAG acts as the UVRAG-defining regulatory/adaptor subunit of PI3KC3-C2, linking PIK3C3/PIK3R4/BECN1 complex activity to PI3P-dependent endosomal and late autophagy trafficking.

Molecular Function:
protein-macromolecule adaptor activity
Directly Involved In:
phosphatidylinositol-3-phosphate biosynthetic process autophagosome maturation positive regulation of autophagosome maturation multivesicular body sorting pathway
Cellular Locations:
autophagosome autophagosome membrane early endosome late endosome lysosome
In Complex:
phosphatidylinositol 3-kinase complex, class III, type II
Supporting Evidence:
  • PMID:16799551
    positive regulator of the Beclin1-PI(3)KC3 complex
  • PMID:18843052
    Atg14, and UVRAG are not present in the same complex
  • file:human/UVRAG/UVRAG-uniprot.txt
    acts as a regulatory subunit of the alternative PI3K complex II
  • file:human/UVRAG/UVRAG-uniprot.txt
    mediates formation of phosphatidylinositol 3-phosphate
  • PMID:18552835
    interacts with the class C Vps complex
  • PMID:18552835
    autophagosome fusion with late endosomes/lysosomes
  • PMID:28306502
    Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
  • file:human/UVRAG/UVRAG-uniprot.txt
    Involved in maturation of autophagosomes and degradative endocytic trafficking

UVRAG engages class C VPS/HOPS and endosomal/autophagosomal SNARE machinery to promote fusogenic SNARE complex assembly during late endosomal and autophagosome maturation events.

Molecular Function:
SNARE binding
Directly Involved In:
SNARE complex assembly autophagosome maturation
Cellular Locations:
late endosome lysosome autophagosome membrane
Supporting Evidence:
  • PMID:24550300
    interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and endosomal
  • PMID:24550300
    by assembling a specific fusogenic SNARE complex
  • file:human/UVRAG/UVRAG-uniprot.txt
    SNARE complex and promotes fusogenic SNARE complex formation during
  • PMID:18552835
    interacts with the class C Vps complex
  • PMID:18552835
    autophagosome fusion with late endosomes/lysosomes

References

GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000044
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
GO_REF:0000107
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
GO_REF:0000117
Electronic Gene Ontology annotations created by ARBA machine learning models
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
PMID:16799551
Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG.
PMID:17891140
Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis.
PMID:18552835
Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking.
PMID:19050071
Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase.
PMID:19270696
Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages.
PMID:20562859
Network organization of the human autophagy system.
PMID:20643123
A phosphatidylinositol 3-kinase class III sub-complex containing VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic.
PMID:21062745
The RUN domain of rubicon is important for hVps34 binding, lipid kinase inhibition, and autophagy suppression.
PMID:21118109
The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes.
PMID:21597469
UV irradiation resistance-associated gene suppresses apoptosis by interfering with BAX activation.
PMID:22081109
Inhibition of autophagy by TAB2 and TAB3.
PMID:22354037
Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC.
PMID:22493499
Receptor signaling lymphocyte-activation molecule family 1 (Slamf1) regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-associated gene (UVRAG) complex.
PMID:22542840
A dual role for UVRAG in maintaining chromosomal stability independent of autophagy.
PMID:23954414
Beclin 2 functions in autophagy, degradation of G protein-coupled receptors, and metabolism.
PMID:24034250
EGFR-mediated Beclin 1 phosphorylation in autophagy suppression, tumor progression, and tumor chemoresistance.
PMID:24056303
PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex.
PMID:24554770
The HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17.
PMID:24785657
NRBF2 regulates macroautophagy as a component of Vps34 Complex I.
PMID:24849286
NRBF2 regulates autophagy and prevents liver injury by modulating Atg14L-linked phosphatidylinositol-3 kinase III activity.
PMID:25490155
Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex.
PMID:26496610
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
PMID:28306502
Pacer Mediates the Function of Class III PI3K and HOPS Complexes in Autophagosome Maturation by Engaging Stx17.
PMID:28479384
Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric cancer cells.
PMID:32296183
A reference map of the human binary protein interactome.
PMID:33961781
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
PMID:34386498
ORF3a-Mediated Incomplete Autophagy Facilitates Severe Acute Respiratory Syndrome Coronavirus-2 Replication.
PMID:35044719
Proteome-scale mapping of binding sites in the unstructured regions of the human proteome.
PMID:35271311
OpenCell: Endogenous tagging for the cartography of human cellular organization.
PMID:37219487
Large-scale phosphomimetic screening identifies phospho-modulated motif-based protein interactions.
PMID:8999962
Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase complex.
PMID:9169138
Molecular cloning of a novel human gene encoding a 63-kDa protein and its sublocalization within the 11q13 locus.
Reactome:R-HSA-9730505
SARS-CoV-2 3a binds to UVRAG
PMID:18843052
Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG.
PMID:24550300
UVRAG is required for virus entry through combinatorial interaction with the class C-Vps complex and SNAREs.
PMID:25533187
mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and endosome maturation.
file:human/UVRAG/UVRAG-uniprot.txt
UniProtKB record for human UVRAG
file:human/UVRAG/UVRAG-notes.md
UVRAG review notes

Suggested Questions for Experts

Q: Should UVRAG be curated directly to GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II rather than the parent class III PI3K complex term?

Suggested experts: GO autophagy editors, ComplexPortal curators, Reactome autophagy curators

Q: Should UVRAG SNARE/HOPS activity be represented only by SNARE binding and SNARE complex assembly, or is a more specific autophagosome-lysosome fusion adaptor term needed?

Suggested experts: GO molecular function editors, autophagosome maturation experts

Q: Should UVRAG DNA repair and centrosome annotations remain non-core in autophagy-focused reviews even though they are experimentally supported?

Suggested experts: GO DNA repair editors, GO autophagy editors

Suggested Experiments

Experiment: Use UVRAG separation-of-function mutants that disrupt BECN1/PIK3C3 binding, HOPS/class C VPS binding, or SNARE binding, followed by PI3P imaging, STX17/HOPS recruitment, and autophagosome-lysosome fusion assays.

Hypothesis: PI3KC3-C2 complex engagement and HOPS/SNARE engagement define separable UVRAG contributions to PI3P production and autophagosome maturation.

Type: UVRAG autophagy maturation separation-of-function rescue

Experiment: Compare UVRAG wild type, DNA-PK-binding mutants, and CEP63/centrosome-interaction mutants in the same knockout-rescue background with autophagic flux, NHEJ reporter, and centrosome/chromosome segregation readouts.

Hypothesis: UVRAG autophagosome maturation and DNA repair/centrosome functions are genetically separable branches rather than one shared autophagy-dependent phenotype.

Type: parallel autophagy and genome-stability rescue assay

📚 Additional Documentation

Notes

(UVRAG-notes.md)

UVRAG review notes

Scope

UVRAG is reviewed here in the proteostasis-network neighborhood around class III PI3K complexes and late autophagy/endolysosomal trafficking. PN entries without PMIDs were used only as search/context cues, not as evidence.

Evidence synthesis

UVRAG is a Beclin 1/class III PI3K complex regulator. The original autophagy paper identifies UVRAG as a "positive regulator of the Beclin1-PI(3)KC3 complex" and states that "UVRAG-mediated activation of the Beclin1-PI(3)KC3 complex promotes autophagy" [PMID:16799551, "positive regulator of the Beclin1-PI(3)KC3 complex"; PMID:16799551, "UVRAG-mediated activation of the Beclin1-PI(3)KC3 complex promotes autophagy"]. The C1/C2 split is important: mammalian Atg14 and UVRAG both bind Beclin 1/Vps34 but "Atg14, and UVRAG are not present in the same complex", supporting UVRAG as the type II/PI3KC3-C2 subunit rather than the ATG14 C1 subunit [PMID:18843052, "Atg14, and UVRAG are not present in the same complex"].

The best-supported PN-relevant process is autophagosome maturation and late endolysosomal fusion. UVRAG "interacts with the class C Vps complex" and that interaction "stimulates Rab7 GTPase activity and autophagosome fusion with late endosomes/lysosomes" [PMID:18552835, "interacts with the class C Vps complex"; PMID:18552835, "stimulates Rab7 GTPase activity and autophagosome fusion with late endosomes/lysosomes"]. Pacer/RUBCNL further links UVRAG to autophagosome-specific PI3KC3/HOPS recruitment: "Pacer recruits PI3KC3 and HOPS complexes to the autophagosome" and the paper explicitly frames this in "autophagosome maturation" [PMID:28306502, "Pacer recruits PI3KC3 and HOPS complexes to the autophagosome"; PMID:28306502, "autophagosome maturation"]. UniProt also summarizes UVRAG as a PI3KC3-C2 subunit that "mediates formation of phosphatidylinositol 3-phosphate" and is "involved in maturation of autophagosomes and endocytosis" [file:human/UVRAG/UVRAG-uniprot.txt, "PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate"; file:human/UVRAG/UVRAG-uniprot.txt, "involved in maturation of autophagosomes and endocytosis"].

UVRAG also has a real endosomal/Golgi-ER trafficking role that should be retained but not mistaken for the PN class III PI3K component term. A PtdIns(3)P/ER tethering study identifies UVRAG as "a phosphatidylinositol-3-phosphate (PtdIns(3)P)-binding protein" and says it "acts as an integral component of the RINT-1-containing ER tethering complex" [PMID:24056303, "phosphatidylinositol-3-phosphate (PtdIns(3)P)-binding protein"; PMID:24056303, "acts as an integral component of the RINT-1-containing ER tethering complex"]. It also connects autophagy to ATG9 transport by reporting that UVRAG works with the "Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation" [PMID:24056303, "Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation"].

SNARE/HOPS binding is specific enough to preserve where GOA has SNARE binding or SNARE complex assembly. UVRAG "mediates viral endocytic transport and membrane penetration through interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and endosomal glutamine-containing SNAREs" and the authors conclude that UVRAG regulates viral entry "by assembling a specific fusogenic SNARE complex" [PMID:24550300, "interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and endosomal glutamine-containing SNAREs"; PMID:24550300, "by assembling a specific fusogenic SNARE complex"]. This virus-entry case is host-pathogen context, but it supports the biochemical SNARE/HOPS interaction axis summarized by UniProt.

The DNA repair and centrosome/chromosome annotations are experimentally supported but non-core for the proteostasis review. UVRAG "promotes DNA double-strand-break repair by directly binding and activating DNA-PK in nonhomologous end joining", and the same study reports that disrupting its centrosome association causes "centrosome instability and aneuploidy" [PMID:22542840, "promotes DNA double-strand-break repair by directly binding and activating DNA-PK in nonhomologous end joining"; PMID:22542840, "centrosome instability and aneuploidy"]. These should be retained as non-core rather than removed.

Curation calls

  • Treat UVRAG as the UVRAG-containing class III PI3K complex II regulatory/adaptor subunit. Replace generic GO:0035032 phosphatidylinositol 3-kinase complex, class III and GO:0032991 protein-containing complex rows with GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II.
  • Accept or keep core-relevant rows for GO:0097352 autophagosome maturation, GO:1901098 positive regulation of autophagosome maturation, GO:0036092 phosphatidylinositol-3-phosphate biosynthetic process, GO:0000149 SNARE binding, and GO:0035493 SNARE complex assembly.
  • Keep endosome/lysosome/autophagosome locations, but mark very broad cellular component rows as non-core or over-annotated where more specific locations exist.
  • Mark generic GO:0005515 protein binding rows as over-annotated. The underlying interactions are often real, but the term is not informative for gene function; the useful annotations are complex membership, SNARE binding, HOPS/class C VPS interaction context, and DNA-PK/centrosome non-core biology.
  • Keep DNA repair, NHEJ, DNA-PK colocalization, centrosome cycle, chromosome segregation, and related localization rows as non-core.

Falcon

Falcon deep research was started for UVRAG on 2026-06-02. The run timed out after the configured 600 seconds and did not produce UVRAG-deep-research-falcon.md; the review therefore relies on local UniProt, GOA, Reactome, and cached publication evidence.

Pn Notes

(UVRAG-pn-notes.md)

UVRAG PN Consistency Notes

  • Generated: 2026-06-18
  • Project: PROTEOSTASIS
  • Scope: PN consistency rereview against local AIGR review and available deep-research artifacts
  • UniProt: Q9P2Y5
  • AIGR review status: COMPLETE
  • Review batch: proteostasis-pr-1217 (PR 1217)
  • Batch change status: added

Source Files Checked

Deep Research Files

  • No *-deep-research*.md file found in this gene directory.

AIGR Review Snapshot

  • Description: UVRAG is a regulatory/adaptor subunit of the UVRAG-containing class III PI3K complex II (PI3KC3-C2) and a late autophagy/endolysosomal trafficking factor. It binds Beclin 1/PIK3C3 complex machinery, supports PI3P-dependent autophagosome maturation, and coordinates HOPS/class C VPS and SNARE-dependent fusion events at autophagosomes and endosomes. UVRAG also has supported but non-core roles in Golgi-ER retrograde trafficking, degradative endocytic traffic, cytokinesis, and autophagy-independent DNA repair/centrosome stability.
  • Existing/core annotation action counts: ACCEPT: 16; KEEP_AS_NON_CORE: 24; MARK_AS_OVER_ANNOTATED: 26; MODIFY: 9; NEW: 1

PN Consistency Summary

  • Consistency: Strong agreement. Deep research, review, and PN all place UVRAG as the regulatory/adaptor subunit defining the type II (UVRAG-containing) class III PI3K complex (PI3KC3-C2), driving autophagosome maturation and HOPS/SNARE-dependent late-endosome/lysosome fusion. The review's PN-core framing (autophagosome maturation, positive regulation of autophagy) matches the dossier Notes verbatim (mTOR-RUBCN regulation, HOPS recruitment).
  • PN story / NEW pressure: GO:0034272 (verified real, non-obsolete) is the projected complex term. GOA currently has only the generic parent GO:0035032; the review MODIFYs GO:0035032 → GO:0034272 (and also narrows GO:0032991/GO:0043933 to GO:0034272). So the PN's more_specific_than_existing_goa status is exactly right and the review already proposes the same upgrade. Verdict: already captured by the review's proposed MODIFY; no new NEW term needed.
  • Evidence alignment: PN cites PMID:18843052 (Atg14L/Rubicon reciprocal regulation), PMID:16799551-equivalent Beclin1-UVRAG work, plus the class-C VPS paper and review articles. Review uses the same anchors: PMID:18843052, PMID:16799551 (positive regulator of Beclin1-PI3KC3), PMID:24550300 (SNARE/C-Vps), PMID:28306502 (Pacer/HOPS), PMID:18552835. Excellent overlap.
  • Verdict: Consistent and well-supported; the review's GO:0034272 MODIFY is the correct, verified specific complex term and aligns with the PN projection. Best-aligned gene of the set.

Full Consistency Review

  • UniProt: Q9P2Y5 · batch: proteostasis-pr-1217 · review status: COMPLETE
  • PN placement: ALP …|Autophagosome closure maturation and lysosome fusion|Class 3 PI3K complex 2, direct|Class 3 PI3K complex 2 component ; PN-node mapping: type mapped/ok_for_propagation GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II (more_specific_than_existing_goa); group context_only GO:0035032 (class III PI3K complex); class context_only GO:0016236 macroautophagy.
  • Consistency: Strong agreement. Deep research, review, and PN all place UVRAG as the regulatory/adaptor subunit defining the type II (UVRAG-containing) class III PI3K complex (PI3KC3-C2), driving autophagosome maturation and HOPS/SNARE-dependent late-endosome/lysosome fusion. The review's PN-core framing (autophagosome maturation, positive regulation of autophagy) matches the dossier Notes verbatim (mTOR-RUBCN regulation, HOPS recruitment).
  • PN story / NEW pressure: GO:0034272 (verified real, non-obsolete) is the projected complex term. GOA currently has only the generic parent GO:0035032; the review MODIFYs GO:0035032 → GO:0034272 (and also narrows GO:0032991/GO:0043933 to GO:0034272). So the PN's more_specific_than_existing_goa status is exactly right and the review already proposes the same upgrade. Verdict: already captured by the review's proposed MODIFY; no new NEW term needed.
  • Mapping strategy: UVRAG genuinely sharpens the node — it is the defining type II component, so projecting the narrower GO:0034272 (vs the parent GO:0035032 the group keeps as context_only) is well justified, not over-reach. Scope ok_for_propagation at the leaf, context_only at the group, is the correct split (component leaves propagate complex membership; regulator/context group does not).
  • Evidence alignment: PN cites PMID:18843052 (Atg14L/Rubicon reciprocal regulation), PMID:16799551-equivalent Beclin1-UVRAG work, plus the class-C VPS paper and review articles. Review uses the same anchors: PMID:18843052, PMID:16799551 (positive regulator of Beclin1-PI3KC3), PMID:24550300 (SNARE/C-Vps), PMID:28306502 (Pacer/HOPS), PMID:18552835. Excellent overlap.
  • Verdict: Consistent and well-supported; the review's GO:0034272 MODIFY is the correct, verified specific complex term and aligns with the PN projection. Best-aligned gene of the set.

PN Dossier Context

  • review_batch: proteostasis-pr-1217
  • review_yaml: genes/human/UVRAG/UVRAG-ai-review.yaml
  • PN workbook rows: 1

PN row 1: Autophagy-Lysosome Pathway | Autophagosome closure maturation and lysosome fusion | Class 3 PI3K complex 2, direct | Class 3 PI3K complex 2 component

  • UniProt: Q9P2Y5
  • In branches: ALP
  • Notes: Member of class III PI3K complex 2 that is involved in endosome and autophagosome matureration and recruits the HOPS complex for lysosome fusion. Phosphorylation by mTOR promotes binding of UVRAG to RUBCN, preventing binding to HOPS and inhibiting autophagosome maturation.
  • PN references (titles):
    • Mammalian Autophagy: How Does It Work? | Annual Review of Biochemistry (annualreviews.org)
    • role of autophagy in cardiovascular pathology | Cardiovascular Research | Oxford Academic (oup.com)
    • Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking | Nature Cell Biology
    • Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages | Nature Cell Biology
  • PN-node mapping records (path + ancestors):
    • [type] Autophagy-Lysosome Pathway|Autophagosome closure maturation and lysosome fusion|Class 3 PI3K complex 2, direct|Class 3 PI3K complex 2 component
      status=mapped scope=ok_for_propagation_to_go GO=[GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II]
      rationale: This PN type denotes component membership in the direct class III PI3K complex 2 module used during autophagosome maturation and lysosome fusion. The corresponding GO complex term is the right propagation target.
    • [group] Autophagy-Lysosome Pathway|Autophagosome closure maturation and lysosome fusion|Class 3 PI3K complex 2, direct
      status=context_only scope=too_broad_to_propagate GO=[GO:0035032 phosphatidylinositol 3-kinase complex, class III]
      rationale: Reviewed as a class-III PI3K complex context or regulator bucket. This node is useful for curator interpretation, but it should not project cellular-component membership; only explicit complex-component leaves propagate to GO complex terms.
    • [class] Autophagy-Lysosome Pathway|Autophagosome closure maturation and lysosome fusion
      status=context_only scope=too_broad_to_propagate GO=[GO:0016236 macroautophagy]
      rationale: This class is a late macroautophagy context, but the subtree mixes docking, fusion, localization, membrane-composition, and unknown late-stage roles. The class-level relation is useful for display while propagation is restricted to narrower mechanism nodes.
    • [branch] Autophagy-Lysosome Pathway
      status=no_mapping scope= GO=[]
      rationale: Reviewed as the top-level PN branch. It is a project taxonomy umbrella rather than a direct GO assertion; all propagation must come from manually curated child nodes.

Projected GO annotations (1)

  • GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | scope=ok_for_propagation_to_go | goa_status=more_specific_than_existing_goa | from=Autophagy-Lysosome Pathway|Autophagosome closure maturation and lysosome fusion|Class 3 PI3K complex 2, direct|Class 3 PI3K complex 2 component

Note

This file is generated from the current PROTEOSTASIS phase-1 dossier and local gene-review artifacts. Edit the source review, PN mapping, or dossier rather than this generated note when correcting the underlying curation.

📄 View Raw YAML

 
id: Q9P2Y5
gene_symbol: UVRAG
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: 'UVRAG is a regulatory/adaptor subunit of the UVRAG-containing class III PI3K complex II (PI3KC3-C2)
  and a late autophagy/endolysosomal trafficking factor. It binds Beclin 1/PIK3C3 complex machinery, supports PI3P-dependent
  autophagosome maturation, and coordinates HOPS/class C VPS and SNARE-dependent fusion events at autophagosomes
  and endosomes. UVRAG also has supported but non-core roles in Golgi-ER retrograde trafficking, degradative endocytic
  traffic, cytokinesis, and autophagy-independent DNA repair/centrosome stability.'
alternative_products:
- name: '1'
  id: Q9P2Y5-1
- name: '2'
  id: Q9P2Y5-2
  sequence_note: VSP_056176
existing_annotations:
- term:
    id: GO:0000323
    label: lytic vacuole
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Lytic vacuole is a non-human/generalized ancestor for UVRAG lysosome/endolysosomal localization.
    action: MODIFY
    reason: For human UVRAG, lysosome, late endosome, and autophagosome/autophagosome membrane are more 
      precise locations for the late autophagy and endosomal trafficking role.
    proposed_replacement_terms:
    - id: GO:0005764
      label: lysosome
    - id: GO:0005770
      label: late endosome
    - id: GO:0005776
      label: autophagosome
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - PMID:18552835
    - PMID:18843052
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Late endosome {ECO:0000269|PubMed:18843052}
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Cytoplasmic vesicle, autophagosome
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Early endosome {ECO:0000269|PubMed:18552835
- term:
    id: GO:0000149
    label: SNARE binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: SNARE binding is supported for UVRAG in late endosomal/autophagosome fusion contexts.
    action: ACCEPT
    reason: UVRAG interacts with endosomal SNARE machinery and promotes fusogenic SNARE complex formation with
      class C VPS/HOPS-associated trafficking machinery.
    additional_reference_ids:
    - PMID:24550300
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24550300
      supporting_text: interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and 
        endosomal
    - reference_id: PMID:24550300
      supporting_text: by assembling a specific fusogenic SNARE complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: SNARE complex and promotes fusogenic SNARE complex formation during
- term:
    id: GO:0035493
    label: SNARE complex assembly
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: SNARE complex assembly captures a specific UVRAG role in late endosomal/autophagosome fusion 
      machinery.
    action: ACCEPT
    reason: UVRAG promotes fusogenic SNARE complex formation in class C VPS/HOPS-dependent membrane fusion, 
      making this more informative than generic protein binding.
    additional_reference_ids:
    - PMID:24550300
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24550300
      supporting_text: interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and 
        endosomal
    - reference_id: PMID:24550300
      supporting_text: by assembling a specific fusogenic SNARE complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: SNARE complex and promotes fusogenic SNARE complex formation during
- term:
    id: GO:0000775
    label: chromosome, centromeric region
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Centromeric/chromosome localization is experimentally tied to UVRAG genome-stability biology but 
      is not PN core.
    action: KEEP_AS_NON_CORE
    reason: UVRAG has an autophagy-independent DNA repair and chromosome/centrosome stability branch. Retain 
      as non-core relative to class III PI3K/autophagosome maturation biology.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0005764
    label: lysosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Lysosome localization is compatible with UVRAG late autophagy/endolysosomal trafficking.
    action: ACCEPT
    reason: UVRAG functions in autophagosome fusion with late endosomes/lysosomes and endocytic cargo delivery
      to degradative compartments.
    additional_reference_ids:
    - PMID:18552835
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: autophagosome fusion with late endosomes/lysosomes
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Lysosome {ECO:0000269|PubMed:18843052}
- term:
    id: GO:0005769
    label: early endosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Early endosome localization is supported for UVRAG endosomal trafficking biology.
    action: ACCEPT
    reason: UVRAG is found on endosomal compartments and contributes to endosome/endosome fusion and 
      degradative endocytic trafficking.
    additional_reference_ids:
    - PMID:18552835
    - PMID:18843052
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: endosome-endosome fusion, resulting in rapid degradation of endocytic cargo
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Early endosome {ECO:0000269|PubMed:18552835
- term:
    id: GO:0005770
    label: late endosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Late endosome localization is supported and relevant to UVRAG autophagosome/endosome maturation.
    action: ACCEPT
    reason: The UVRAG-class C VPS/HOPS axis promotes autophagosome fusion with late endosomes/lysosomes and 
      late endocytic fusion.
    additional_reference_ids:
    - PMID:18552835
    - PMID:18843052
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: autophagosome fusion with late endosomes/lysosomes
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Late endosome {ECO:0000269|PubMed:18843052}
- term:
    id: GO:0005776
    label: autophagosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Autophagosome localization is directly relevant to UVRAG/PACER-mediated autophagosome maturation.
    action: ACCEPT
    reason: UVRAG is recruited to autophagosome-associated structures and participates in PI3KC3/HOPS 
      activation during autophagosome maturation.
    additional_reference_ids:
    - PMID:28306502
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:28306502
      supporting_text: Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Cytoplasmic vesicle, autophagosome
- term:
    id: GO:0005783
    label: endoplasmic reticulum
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Endoplasmic reticulum localization is supported for the RINT1/NRZ retrograde trafficking branch.
    action: KEEP_AS_NON_CORE
    reason: UVRAG has a PtdIns(3)P-dependent ER tethering and Golgi-ER retrograde transport role. This is 
      supported but secondary to the PN class III PI3K/autophagosome maturation focus.
    additional_reference_ids:
    - PMID:24056303
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24056303
      supporting_text: PtdIns(3)P)-binding protein
    - reference_id: PMID:24056303
      supporting_text: acts as an integral component of the RINT-1-containing ER tethering complex
    - reference_id: PMID:24056303
      supporting_text: Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
- term:
    id: GO:0006914
    label: autophagy
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: involved_in
  review:
    summary: Broad autophagy is directionally correct but should be narrowed to UVRAG autophagosome 
      maturation/positive autophagy regulation.
    action: MODIFY
    reason: UVRAG regulates class III PI3K/HOPS-dependent autophagosome maturation and Beclin1-PI3KC3 
      autophagy signaling; the parent autophagy term loses that specificity.
    proposed_replacement_terms:
    - id: GO:0097352
      label: autophagosome maturation
    - id: GO:0010508
      label: positive regulation of autophagy
    additional_reference_ids:
    - PMID:16799551
    - PMID:18552835
    - PMID:28306502
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:16799551
      supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
    - reference_id: PMID:18843052
      supporting_text: Atg14, and UVRAG are not present in the same complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: acts as a regulatory subunit of the alternative PI3K complex II
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: mediates formation of phosphatidylinositol 3-phosphate
    - reference_id: PMID:18552835
      supporting_text: interacts with the class C Vps complex
    - reference_id: PMID:18552835
      supporting_text: autophagosome fusion with late endosomes/lysosomes
- term:
    id: GO:0016192
    label: vesicle-mediated transport
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: involved_in
  review:
    summary: Vesicle-mediated transport is too broad for UVRAG; the supported processes are Golgi-ER 
      retrograde transport and endolysosomal/autophagic trafficking.
    action: MODIFY
    reason: UVRAG couples PtdIns(3)P-dependent ER tethering, ATG9 transport, endosome fusion, and 
      autophagosome maturation. More specific transport terms should be used instead of the broad parent.
    proposed_replacement_terms:
    - id: GO:0006890
      label: retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
    - id: GO:0071985
      label: multivesicular body sorting pathway
    - id: GO:0097352
      label: autophagosome maturation
    additional_reference_ids:
    - PMID:18552835
    - PMID:24056303
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: interacts with the class C Vps complex
    - reference_id: PMID:18552835
      supporting_text: autophagosome fusion with late endosomes/lysosomes
    - reference_id: PMID:24056303
      supporting_text: PtdIns(3)P)-binding protein
    - reference_id: PMID:24056303
      supporting_text: acts as an integral component of the RINT-1-containing ER tethering complex
    - reference_id: PMID:24056303
      supporting_text: Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
- term:
    id: GO:0030496
    label: midbody
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Midbody localization is supported for UVRAG cytokinesis biology but is not PN core.
    action: KEEP_AS_NON_CORE
    reason: The PI3KC3-C2/BIF-1-containing subcomplex has a supported cytokinesis/midbody branch; retain it as
      non-core relative to autophagosome maturation.
    additional_reference_ids:
    - PMID:20643123
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:20643123
      supporting_text: strong localisation of these proteins to the midbody
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Midbody
- term:
    id: GO:0031410
    label: cytoplasmic vesicle
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: located_in
  review:
    summary: Cytoplasmic vesicle is true but too broad for UVRAG localization.
    action: MODIFY
    reason: UVRAG is better localized to autophagosome/autophagosome membrane and early/late endosome 
      compartments relevant to PI3KC3-C2 and HOPS/SNARE trafficking.
    proposed_replacement_terms:
    - id: GO:0005776
      label: autophagosome
    - id: GO:0000421
      label: autophagosome membrane
    - id: GO:0005769
      label: early endosome
    - id: GO:0005770
      label: late endosome
    additional_reference_ids:
    - PMID:18552835
    - PMID:28306502
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Late endosome {ECO:0000269|PubMed:18843052}
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Cytoplasmic vesicle, autophagosome
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Early endosome {ECO:0000269|PubMed:18552835
- term:
    id: GO:0036092
    label: phosphatidylinositol-3-phosphate biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: involved_in
  review:
    summary: UVRAG is involved in PI3P biosynthesis as a PI3KC3-C2 regulatory subunit rather than as the lipid
      kinase itself.
    action: ACCEPT
    reason: UVRAG activates/regulates PIK3C3/VPS34 within PI3KC3-C2, which mediates formation of 
      phosphatidylinositol 3-phosphate during autophagy/endosomal trafficking.
    additional_reference_ids:
    - PMID:16799551
    - PMID:20643123
    - PMID:24056303
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:16799551
      supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
    - reference_id: PMID:18843052
      supporting_text: Atg14, and UVRAG are not present in the same complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: acts as a regulatory subunit of the alternative PI3K complex II
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: mediates formation of phosphatidylinositol 3-phosphate
- term:
    id: GO:0043933
    label: protein-containing complex organization
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: involved_in
  review:
    summary: Protein-containing complex organization is too broad for UVRAG; SNARE/HOPS and PI3KC3-C2 complex 
      roles are more specific.
    action: MODIFY
    reason: UVRAG participates in specific PI3KC3-C2, HOPS/class C VPS, and SNARE assembly contexts. Generic 
      complex organization should be replaced by the specific supported complex/process annotations.
    proposed_replacement_terms:
    - id: GO:0035493
      label: SNARE complex assembly
    - id: GO:0034272
      label: phosphatidylinositol 3-kinase complex, class III, type II
    additional_reference_ids:
    - PMID:24550300
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24550300
      supporting_text: interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and 
        endosomal
    - reference_id: PMID:24550300
      supporting_text: by assembling a specific fusogenic SNARE complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: SNARE complex and promotes fusogenic SNARE complex formation during
    - reference_id: PMID:16799551
      supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
    - reference_id: PMID:18843052
      supporting_text: Atg14, and UVRAG are not present in the same complex
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17891140
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19050071
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20562859
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21062745
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21597469
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22081109
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22493499
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23954414
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24034250
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24056303
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24554770
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24785657
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24849286
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25490155
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:26496610
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33961781
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:34386498
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:35044719
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:35271311
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:37219487
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0000149
    label: SNARE binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: enables
  review:
    summary: SNARE binding is supported for UVRAG in late endosomal/autophagosome fusion contexts.
    action: ACCEPT
    reason: UVRAG interacts with endosomal SNARE machinery and promotes fusogenic SNARE complex formation with
      class C VPS/HOPS-associated trafficking machinery.
    additional_reference_ids:
    - PMID:24550300
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24550300
      supporting_text: interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and 
        endosomal
    - reference_id: PMID:24550300
      supporting_text: by assembling a specific fusogenic SNARE complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: SNARE complex and promotes fusogenic SNARE complex formation during
- term:
    id: GO:0006281
    label: DNA repair
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: DNA repair is supported for UVRAG but is an autophagy-independent non-core branch in this PN 
      review.
    action: KEEP_AS_NON_CORE
    reason: The strongest evidence supports UVRAG activation of DNA-PK in NHEJ and chromosomal stability, but 
      this should not be treated as the proteostasis/autophagy core function.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0007051
    label: spindle organization
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Spindle organization is a non-core inference from UVRAG centrosome/chromosome stability biology.
    action: KEEP_AS_NON_CORE
    reason: The paper supports proper chromosome segregation and centrosome stability, but this is outside the
      class III PI3K/autophagosome maturation core.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0007059
    label: chromosome segregation
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Chromosome segregation is supported by UVRAG centrosome/chromosome stability evidence but is 
      non-core.
    action: KEEP_AS_NON_CORE
    reason: UVRAG disruption causes centrosome instability and aneuploidy; retain as non-core genome-stability
      biology.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0007098
    label: centrosome cycle
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: Centrosome cycle is supported as a non-core centrosome stability/chromosome segregation branch.
    action: KEEP_AS_NON_CORE
    reason: UVRAG interacts with CEP63 and is required for centrosome stability, but this is separate from the
      PN autophagy/endolysosomal core.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0017124
    label: SH3 domain binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: enables
  review:
    summary: SH3 domain binding is compatible with the SH3GLB1/Bif-1 interaction but is not the core UVRAG 
      function.
    action: KEEP_AS_NON_CORE
    reason: The SH3GLB1 interaction helps connect UVRAG to BECN1/PI3KC3-C2, but the more informative 
      annotations are PI3KC3-C2 membership and autophagosome/endosomal trafficking roles.
    additional_reference_ids:
    - PMID:17891140
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:17891140
      supporting_text: Bif-1 interacts with Beclin 1 through UVRAG
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with SH3GLB1
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: part_of
  review:
    summary: Protein-containing complex is correct but too generic for UVRAG.
    action: MODIFY
    reason: UVRAG is a component/regulatory subunit of the UVRAG-containing PI3KC3-C2 complex; the generic 
      complex term should be narrowed to the type II class III PI3K complex.
    proposed_replacement_terms:
    - id: GO:0034272
      label: phosphatidylinositol 3-kinase complex, class III, type II
    additional_reference_ids:
    - PMID:18843052
    - PMID:20643123
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:16799551
      supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
    - reference_id: PMID:18843052
      supporting_text: Atg14, and UVRAG are not present in the same complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: acts as a regulatory subunit of the alternative PI3K complex II
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: mediates formation of phosphatidylinositol 3-phosphate
- term:
    id: GO:0045335
    label: phagocytic vesicle
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: located_in
  review:
    summary: Phagocytic vesicle context is supported through SLAMF1/Vps34/Beclin1/UVRAG phagosome signaling 
      but is non-core.
    action: KEEP_AS_NON_CORE
    reason: This is a macrophage/phagosome-specific branch of UVRAG-containing class III PI3K signaling rather
      than the central autophagosome maturation role.
    additional_reference_ids:
    - PMID:22493499
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22493499
      supporting_text: Slamf1 interacts with the class III PI3K Vps34 in a complex with Beclin-1 and UVRAG
    - reference_id: PMID:22493499
      supporting_text: Slamf1 recruits a subset of Vps34-associated proteins
- term:
    id: GO:0010506
    label: regulation of autophagy
  evidence_type: IDA
  original_reference_id: PMID:16799551
  qualifier: involved_in
  review:
    summary: UVRAG positively regulates Beclin1-PI3KC3 autophagy activity, so the undirected regulation term 
      should be narrowed.
    action: MODIFY
    reason: The cited evidence presents UVRAG as a positive regulator/activator of the Beclin1-PI3KC3 complex 
      and autophagy, not merely an unspecified regulator.
    proposed_replacement_terms:
    - id: GO:0010508
      label: positive regulation of autophagy
    - id: GO:0097352
      label: autophagosome maturation
    additional_reference_ids:
    - PMID:16799551
    - PMID:18552835
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:16799551
      supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
    - reference_id: PMID:16799551
      supporting_text: UVRAG-mediated activation of the Beclin1-PI(3)KC3 complex promotes autophagy
- term:
    id: GO:0035032
    label: phosphatidylinositol 3-kinase complex, class III
  evidence_type: IPI
  original_reference_id: PMID:25490155
  qualifier: part_of
  review:
    summary: Generic class III PI3K complex membership is correct but underspecified for UVRAG.
    action: MODIFY
    reason: UVRAG defines the type II/PI3KC3-C2 branch rather than the ATG14-containing type I complex. The GO
      term should be narrowed to class III PI3K complex type II.
    proposed_replacement_terms:
    - id: GO:0034272
      label: phosphatidylinositol 3-kinase complex, class III, type II
    additional_reference_ids:
    - PMID:18843052
    - PMID:20643123
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:16799551
      supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
    - reference_id: PMID:18843052
      supporting_text: Atg14, and UVRAG are not present in the same complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: acts as a regulatory subunit of the alternative PI3K complex II
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: mediates formation of phosphatidylinositol 3-phosphate
- term:
    id: GO:0036092
    label: phosphatidylinositol-3-phosphate biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:8999962
  qualifier: involved_in
  review:
    summary: UVRAG is involved in PI3P biosynthesis as a PI3KC3-C2 regulatory subunit rather than as the lipid
      kinase itself.
    action: ACCEPT
    reason: UVRAG activates/regulates PIK3C3/VPS34 within PI3KC3-C2, which mediates formation of 
      phosphatidylinositol 3-phosphate during autophagy/endosomal trafficking.
    additional_reference_ids:
    - PMID:16799551
    - PMID:20643123
    - PMID:24056303
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:16799551
      supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
    - reference_id: PMID:18843052
      supporting_text: Atg14, and UVRAG are not present in the same complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: acts as a regulatory subunit of the alternative PI3K complex II
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: mediates formation of phosphatidylinositol 3-phosphate
- term:
    id: GO:0005769
    label: early endosome
  evidence_type: EXP
  original_reference_id: PMID:18552835
  qualifier: located_in
  review:
    summary: Early endosome localization is supported for UVRAG endosomal trafficking biology.
    action: ACCEPT
    reason: UVRAG is found on endosomal compartments and contributes to endosome/endosome fusion and 
      degradative endocytic trafficking.
    additional_reference_ids:
    - PMID:18552835
    - PMID:18843052
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: endosome-endosome fusion, resulting in rapid degradation of endocytic cargo
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Early endosome {ECO:0000269|PubMed:18552835
- term:
    id: GO:0033116
    label: endoplasmic reticulum-Golgi intermediate compartment membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9730505
  qualifier: located_in
  review:
    summary: ERGIC membrane is a virus-event-specific Reactome localization and is too specific for general 
      UVRAG biology.
    action: MARK_AS_OVER_ANNOTATED
    reason: The Reactome event records SARS-CoV-2 3a binding to UVRAG and disruption of a Beclin1:VPS34:UVRAG 
      complex; it does not establish ERGIC membrane as a stable UVRAG cellular component. ER and 
      autophagosome/endosome locations are better supported.
    proposed_replacement_terms:
    - id: GO:0005783
      label: endoplasmic reticulum
    - id: GO:0005776
      label: autophagosome
    - id: GO:0005769
      label: early endosome
    additional_reference_ids:
    - Reactome:R-HSA-9730505
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: Reactome:R-HSA-9730505
      supporting_text: SARS-CoV-2 3a binds to UVRAG
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Endoplasmic reticulum {ECO:0000269|PubMed:24056303}
- term:
    id: GO:0000421
    label: autophagosome membrane
  evidence_type: IDA
  original_reference_id: PMID:28306502
  qualifier: located_in
  review:
    summary: Autophagosome membrane localization is directly supported for UVRAG/PACER-mediated maturation.
    action: ACCEPT
    reason: UVRAG is recruited to autophagosomes through RUBCNL/PACER and supports local PI3KC3/HOPS activity 
      for autophagosome maturation.
    additional_reference_ids:
    - PMID:28306502
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:28306502
      supporting_text: Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Recruited to autophagosome following interaction with RUBCNL/PACER
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28306502
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0097352
    label: autophagosome maturation
  evidence_type: IDA
  original_reference_id: PMID:28306502
  qualifier: involved_in
  review:
    summary: Autophagosome maturation is a core UVRAG process.
    action: ACCEPT
    reason: UVRAG coordinates PI3KC3/HOPS/class C VPS machinery and autophagosome-lysosome/endosome fusion 
      during late autophagy.
    additional_reference_ids:
    - PMID:18552835
    - PMID:28306502
    - PMID:25533187
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: interacts with the class C Vps complex
    - reference_id: PMID:18552835
      supporting_text: autophagosome fusion with late endosomes/lysosomes
    - reference_id: PMID:28306502
      supporting_text: Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Involved in maturation of autophagosomes and degradative endocytic trafficking
    - reference_id: PMID:25533187
      supporting_text: UVRAG is released from RUBICON to interact with the HOPS complex
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28479384
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:1901098
    label: positive regulation of autophagosome maturation
  evidence_type: TAS
  original_reference_id: PMID:21118109
  qualifier: involved_in
  review:
    summary: Positive regulation of autophagosome maturation is core and well supported.
    action: ACCEPT
    reason: UVRAG enhances autophagosome/endosome maturation via HOPS/class C VPS engagement and is released 
      from inhibitory RUBICON interaction upon dephosphorylation.
    additional_reference_ids:
    - PMID:18552835
    - PMID:25533187
    - PMID:28306502
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: interacts with the class C Vps complex
    - reference_id: PMID:18552835
      supporting_text: autophagosome fusion with late endosomes/lysosomes
    - reference_id: PMID:28306502
      supporting_text: Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Involved in maturation of autophagosomes and degradative endocytic trafficking
    - reference_id: PMID:25533187
      supporting_text: enhances autophagosome and endosome maturation
- term:
    id: GO:0071985
    label: multivesicular body sorting pathway
  evidence_type: TAS
  original_reference_id: PMID:21118109
  qualifier: involved_in
  review:
    summary: Multivesicular body/endosomal sorting is supported but non-core in the PN autophagy review.
    action: KEEP_AS_NON_CORE
    reason: UVRAG contributes to degradative endocytic trafficking and endosome fusion, but the PN core is 
      PI3KC3-C2/autophagosome maturation.
    additional_reference_ids:
    - PMID:18552835
    - PMID:20643123
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: endosome-endosome fusion, resulting in rapid degradation of endocytic cargo
    - reference_id: PMID:20643123
      supporting_text: regulates both receptor degradation and cytokinesis
- term:
    id: GO:0005813
    label: centrosome
  evidence_type: IDA
  original_reference_id: PMID:22542840
  qualifier: located_in
  review:
    summary: Centrosome localization is supported but non-core.
    action: KEEP_AS_NON_CORE
    reason: UVRAG localizes to centrosomes and interacts with CEP63 in an autophagy-independent 
      chromosome-stability branch.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0006281
    label: DNA repair
  evidence_type: IMP
  original_reference_id: PMID:22542840
  qualifier: involved_in
  review:
    summary: DNA repair is supported for UVRAG but is an autophagy-independent non-core branch in this PN 
      review.
    action: KEEP_AS_NON_CORE
    reason: The strongest evidence supports UVRAG activation of DNA-PK in NHEJ and chromosomal stability, but 
      this should not be treated as the proteostasis/autophagy core function.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0007098
    label: centrosome cycle
  evidence_type: IMP
  original_reference_id: PMID:22542840
  qualifier: involved_in
  review:
    summary: Centrosome cycle is supported as a non-core centrosome stability/chromosome segregation branch.
    action: KEEP_AS_NON_CORE
    reason: UVRAG interacts with CEP63 and is required for centrosome stability, but this is separate from the
      PN autophagy/endolysosomal core.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0070418
    label: DNA-dependent protein kinase complex
  evidence_type: IDA
  original_reference_id: PMID:22542840
  qualifier: colocalizes_with
  review:
    summary: DNA-PK complex colocalization/association is supported but non-core.
    action: KEEP_AS_NON_CORE
    reason: UVRAG binds/activates DNA-PK for NHEJ, but this genome-stability function is outside the PN 
      autophagosome maturation core.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0071900
    label: regulation of protein serine/threonine kinase activity
  evidence_type: IDA
  original_reference_id: PMID:22542840
  qualifier: involved_in
  review:
    summary: Regulation of serine/threonine kinase activity is supported through DNA-PK activation but is 
      broad and non-core.
    action: KEEP_AS_NON_CORE
    reason: The specific supported kinase is DNA-PK in NHEJ; this should not be interpreted as a core 
      proteostasis/autophagy function.
    proposed_replacement_terms:
    - id: GO:0097680
      label: double-strand break repair via classical nonhomologous end joining
    - id: GO:0006281
      label: DNA repair
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0097680
    label: double-strand break repair via classical nonhomologous end joining
  evidence_type: IDA
  original_reference_id: PMID:22542840
  qualifier: involved_in
  review:
    summary: Classical NHEJ is supported for UVRAG but non-core.
    action: KEEP_AS_NON_CORE
    reason: UVRAG promotes DNA-PK-dependent NHEJ and chromosome stability, but this is a separate 
      autophagy-independent branch.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
    - reference_id: PMID:22542840
      supporting_text: centrosome instability and aneuploidy
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Promotes DNA double-strand break (DSB) repair by association with DNA-dependent
- term:
    id: GO:0030496
    label: midbody
  evidence_type: IDA
  original_reference_id: PMID:20643123
  qualifier: located_in
  review:
    summary: Midbody localization is supported for UVRAG cytokinesis biology but is not PN core.
    action: KEEP_AS_NON_CORE
    reason: The PI3KC3-C2/BIF-1-containing subcomplex has a supported cytokinesis/midbody branch; retain it as
      non-core relative to autophagosome maturation.
    additional_reference_ids:
    - PMID:20643123
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:20643123
      supporting_text: strong localisation of these proteins to the midbody
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Midbody
- term:
    id: GO:0032465
    label: regulation of cytokinesis
  evidence_type: IMP
  original_reference_id: PMID:20643123
  qualifier: involved_in
  review:
    summary: Regulation of cytokinesis is supported through the UVRAG/BIF-1 PI3KC3 subcomplex but non-core.
    action: KEEP_AS_NON_CORE
    reason: The cytokinesis/midbody role is experimentally supported, but it is distinct from the PN 
      autophagosome maturation function.
    additional_reference_ids:
    - PMID:20643123
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:20643123
      supporting_text: regulates both receptor degradation and cytokinesis
    - reference_id: PMID:20643123
      supporting_text: strong localisation of these proteins to the midbody
- term:
    id: GO:0032801
    label: receptor catabolic process
  evidence_type: IMP
  original_reference_id: PMID:20643123
  qualifier: involved_in
  review:
    summary: Receptor catabolic process is supported but non-core.
    action: KEEP_AS_NON_CORE
    reason: UVRAG-containing PI3KC3-C2/BIF-1 machinery regulates degradative endocytic traffic and receptor 
      degradation, but this is secondary to the PN autophagy review.
    additional_reference_ids:
    - PMID:20643123
    - PMID:25533187
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:20643123
      supporting_text: regulates both receptor degradation and cytokinesis
    - reference_id: PMID:25533187
      supporting_text: facilitates the lysosomal degradation of epidermal growth factor receptor
- term:
    id: GO:0005783
    label: endoplasmic reticulum
  evidence_type: IDA
  original_reference_id: PMID:24056303
  qualifier: part_of
  review:
    summary: Endoplasmic reticulum localization is supported for the RINT1/NRZ retrograde trafficking branch.
    action: KEEP_AS_NON_CORE
    reason: UVRAG has a PtdIns(3)P-dependent ER tethering and Golgi-ER retrograde transport role. This is 
      supported but secondary to the PN class III PI3K/autophagosome maturation focus.
    additional_reference_ids:
    - PMID:24056303
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24056303
      supporting_text: PtdIns(3)P)-binding protein
    - reference_id: PMID:24056303
      supporting_text: acts as an integral component of the RINT-1-containing ER tethering complex
    - reference_id: PMID:24056303
      supporting_text: Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
- term:
    id: GO:0006890
    label: retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
  evidence_type: IMP
  original_reference_id: PMID:24056303
  qualifier: involved_in
  review:
    summary: Golgi-to-ER retrograde transport is supported for UVRAG and retained as non-core trafficking 
      biology.
    action: KEEP_AS_NON_CORE
    reason: UVRAG binds PtdIns(3)P, associates with the RINT1/NRZ ER tethering complex, and coordinates COPI 
      cargo transfer; this is a real trafficking branch outside the core PN autophagosome maturation term.
    additional_reference_ids:
    - PMID:24056303
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24056303
      supporting_text: PtdIns(3)P)-binding protein
    - reference_id: PMID:24056303
      supporting_text: acts as an integral component of the RINT-1-containing ER tethering complex
    - reference_id: PMID:24056303
      supporting_text: Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
- term:
    id: GO:0006914
    label: autophagy
  evidence_type: IMP
  original_reference_id: PMID:24056303
  qualifier: involved_in
  review:
    summary: The PMID:24056303 evidence is better captured as ATG9/autophagy-related trafficking rather than 
      broad autophagy.
    action: MODIFY
    reason: This paper supports UVRAG movement between ER tethering and Beclin/Bif-1/PI3KC3 machinery to 
      mobilize ATG9 transport; autophagy is too broad for the specific mechanism.
    proposed_replacement_terms:
    - id: GO:0006890
      label: retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
    - id: GO:0000045
      label: autophagosome assembly
    additional_reference_ids:
    - PMID:24056303
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24056303
      supporting_text: PtdIns(3)P)-binding protein
    - reference_id: PMID:24056303
      supporting_text: acts as an integral component of the RINT-1-containing ER tethering complex
    - reference_id: PMID:24056303
      supporting_text: Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
- term:
    id: GO:0051684
    label: maintenance of Golgi location
  evidence_type: IMP
  original_reference_id: PMID:24056303
  qualifier: involved_in
  review:
    summary: Maintenance of Golgi location is supported through the UVRAG/RINT1 retrograde trafficking branch 
      but non-core.
    action: KEEP_AS_NON_CORE
    reason: Knockdown/displacement of UVRAG disrupts COPI cargo transfer and Golgi integrity, but this is 
      secondary to PI3KC3-C2/autophagy maturation in the PN context.
    additional_reference_ids:
    - PMID:24056303
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:24056303
      supporting_text: PtdIns(3)P)-binding protein
    - reference_id: PMID:24056303
      supporting_text: acts as an integral component of the RINT-1-containing ER tethering complex
    - reference_id: PMID:24056303
      supporting_text: Bif-1-beclin-1-PI(3)KC3 complex to mobilize Atg9 translocation
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22354037
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19270696
  qualifier: enables
  review:
    summary: The interaction evidence may be real, but generic protein binding is not an informative UVRAG 
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: UVRAG has specific complex/adaptor roles in PI3KC3-C2, HOPS/class C VPS, SNARE, DNA-PK, and other 
      assemblies. Retaining protein binding obscures the biological function and should be replaced by 
      specific complex membership or binding terms where curatable.
    additional_reference_ids:
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Component of the PI3K (PI3KC3/PI3K-III/class III
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with VPS16; VPS11; VPS18; VPS33
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Interacts with PRKDC, XRCC6 and XRCC5
- term:
    id: GO:0005764
    label: lysosome
  evidence_type: IDA
  original_reference_id: PMID:19270696
  qualifier: located_in
  review:
    summary: Lysosome localization is compatible with UVRAG late autophagy/endolysosomal trafficking.
    action: ACCEPT
    reason: UVRAG functions in autophagosome fusion with late endosomes/lysosomes and endocytic cargo delivery
      to degradative compartments.
    additional_reference_ids:
    - PMID:18552835
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: autophagosome fusion with late endosomes/lysosomes
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Lysosome {ECO:0000269|PubMed:18843052}
- term:
    id: GO:0005769
    label: early endosome
  evidence_type: IDA
  original_reference_id: PMID:19270696
  qualifier: located_in
  review:
    summary: Early endosome localization is supported for UVRAG endosomal trafficking biology.
    action: ACCEPT
    reason: UVRAG is found on endosomal compartments and contributes to endosome/endosome fusion and 
      degradative endocytic trafficking.
    additional_reference_ids:
    - PMID:18552835
    - PMID:18843052
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: endosome-endosome fusion, resulting in rapid degradation of endocytic cargo
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Early endosome {ECO:0000269|PubMed:18552835
- term:
    id: GO:0005770
    label: late endosome
  evidence_type: IDA
  original_reference_id: PMID:19270696
  qualifier: located_in
  review:
    summary: Late endosome localization is supported and relevant to UVRAG autophagosome/endosome maturation.
    action: ACCEPT
    reason: The UVRAG-class C VPS/HOPS axis promotes autophagosome fusion with late endosomes/lysosomes and 
      late endocytic fusion.
    additional_reference_ids:
    - PMID:18552835
    - PMID:18843052
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:18552835
      supporting_text: autophagosome fusion with late endosomes/lysosomes
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Late endosome {ECO:0000269|PubMed:18843052}
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: TAS
  original_reference_id: PMID:9169138
  qualifier: located_in
  review:
    summary: Cytoplasm is a broad legacy localization for UVRAG.
    action: KEEP_AS_NON_CORE
    reason: The original cloning paper supports a cytoplasmic protein, but current evidence localizes UVRAG 
      more specifically to endosomes, autophagosomes, ER, midbody, and chromosome/centrosome contexts.
    proposed_replacement_terms:
    - id: GO:0005776
      label: autophagosome
    - id: GO:0005769
      label: early endosome
    - id: GO:0005770
      label: late endosome
    additional_reference_ids:
    - PMID:9169138
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:9169138
      supporting_text: novel 63-kDa cytoplasmic protein
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: Cytoplasmic vesicle, autophagosome
- term:
    id: GO:0006281
    label: DNA repair
  evidence_type: TAS
  original_reference_id: PMID:9169138
  qualifier: involved_in
  review:
    summary: DNA repair is supported for UVRAG but is an autophagy-independent non-core branch in this PN 
      review.
    action: KEEP_AS_NON_CORE
    reason: The strongest evidence supports UVRAG activation of DNA-PK in NHEJ and chromosomal stability, but 
      this should not be treated as the proteostasis/autophagy core function.
    additional_reference_ids:
    - PMID:22542840
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:9169138
      supporting_text: novel 63-kDa cytoplasmic protein
    - reference_id: PMID:22542840
      supporting_text: UVRAG promotes DNA double-strand-break repair by directly binding and activating
- term:
    id: GO:0030674
    label: protein-macromolecule adaptor activity
  evidence_type: IDA
  original_reference_id: PMID:16799551
  qualifier: enables
  review:
    summary: UVRAG has a supported adaptor/regulatory subunit role in PI3KC3-C2 and late fusion machinery.
    action: NEW
    reason: Add this as a more informative molecular-function annotation than generic protein binding. UVRAG 
      links BECN1/PIK3C3 complex machinery with class C VPS/HOPS and SNARE-dependent trafficking during 
      autophagosome/endosome maturation.
    additional_reference_ids:
    - PMID:18552835
    - PMID:18843052
    - PMID:24550300
    - PMID:28306502
    - file:human/UVRAG/UVRAG-uniprot.txt
    - file:human/UVRAG/UVRAG-notes.md
    supported_by:
    - reference_id: PMID:16799551
      supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
    - reference_id: PMID:18843052
      supporting_text: Atg14, and UVRAG are not present in the same complex
    - reference_id: PMID:18552835
      supporting_text: interacts with the class C Vps complex
    - reference_id: PMID:24550300
      supporting_text: by assembling a specific fusogenic SNARE complex
    - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
      supporting_text: acts as a regulatory subunit of the alternative PI3K complex II
references:
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, 
    accompanied by conservative changes to GO terms applied by UniProt
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl 
    Compara
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:16799551
  title: Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG.
  findings: []
- id: PMID:17891140
  title: Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis.
  findings: []
- id: PMID:18552835
  title: Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and 
    endocytic trafficking.
  findings: []
- id: PMID:19050071
  title: Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III 
    phosphatidylinositol 3-kinase.
  findings: []
- id: PMID:19270696
  title: Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different 
    stages.
  findings: []
- id: PMID:20562859
  title: Network organization of the human autophagy system.
  findings: []
- id: PMID:20643123
  title: A phosphatidylinositol 3-kinase class III sub-complex containing VPS15, VPS34, Beclin 1, UVRAG and 
    BIF-1 regulates cytokinesis and degradative endocytic traffic.
  findings: []
- id: PMID:21062745
  title: The RUN domain of rubicon is important for hVps34 binding, lipid kinase inhibition, and autophagy 
    suppression.
  findings: []
- id: PMID:21118109
  title: The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes.
  findings: []
- id: PMID:21597469
  title: UV irradiation resistance-associated gene suppresses apoptosis by interfering with BAX activation.
  findings: []
- id: PMID:22081109
  title: Inhibition of autophagy by TAB2 and TAB3.
  findings: []
- id: PMID:22354037
  title: Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC.
  findings: []
- id: PMID:22493499
  title: Receptor signaling lymphocyte-activation molecule family 1 (Slamf1) regulates membrane fusion and 
    NADPH oxidase 2 (NOX2) activity by recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-associated
    gene (UVRAG) complex.
  findings: []
- id: PMID:22542840
  title: A dual role for UVRAG in maintaining chromosomal stability independent of autophagy.
  findings: []
- id: PMID:23954414
  title: Beclin 2 functions in autophagy, degradation of G protein-coupled receptors, and metabolism.
  findings: []
- id: PMID:24034250
  title: EGFR-mediated Beclin 1 phosphorylation in autophagy suppression, tumor progression, and tumor 
    chemoresistance.
  findings: []
- id: PMID:24056303
  title: PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential 
    interactions with the ER tether and the beclin 1 complex.
  findings: []
- id: PMID:24554770
  title: The HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17.
  findings: []
- id: PMID:24785657
  title: NRBF2 regulates macroautophagy as a component of Vps34 Complex I.
  findings: []
- id: PMID:24849286
  title: NRBF2 regulates autophagy and prevents liver injury by modulating Atg14L-linked 
    phosphatidylinositol-3 kinase III activity.
  findings: []
- id: PMID:25490155
  title: Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex.
  findings: []
- id: PMID:26496610
  title: A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
  findings: []
- id: PMID:28306502
  title: Pacer Mediates the Function of Class III PI3K and HOPS Complexes in Autophagosome Maturation by 
    Engaging Stx17.
  findings: []
- id: PMID:28479384
  title: Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric cancer cells.
  findings: []
- id: PMID:32296183
  title: A reference map of the human binary protein interactome.
  findings: []
- id: PMID:33961781
  title: Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
  findings: []
- id: PMID:34386498
  title: ORF3a-Mediated Incomplete Autophagy Facilitates Severe Acute Respiratory Syndrome Coronavirus-2 
    Replication.
  findings: []
- id: PMID:35044719
  title: Proteome-scale mapping of binding sites in the unstructured regions of the human proteome.
  findings: []
- id: PMID:35271311
  title: 'OpenCell: Endogenous tagging for the cartography of human cellular organization.'
  findings: []
- id: PMID:37219487
  title: Large-scale phosphomimetic screening identifies phospho-modulated motif-based protein interactions.
  findings: []
- id: PMID:8999962
  title: Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. 
    Substrate presentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase complex.
  findings: []
- id: PMID:9169138
  title: Molecular cloning of a novel human gene encoding a 63-kDa protein and its sublocalization within the 
    11q13 locus.
  findings: []
- id: Reactome:R-HSA-9730505
  title: SARS-CoV-2 3a binds to UVRAG
  findings: []
- id: PMID:18843052
  title: Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG.
  findings: []
- id: PMID:24550300
  title: UVRAG is required for virus entry through combinatorial interaction with the class C-Vps complex and 
    SNAREs.
  findings: []
- id: PMID:25533187
  title: mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and endosome maturation.
  findings: []
- id: file:human/UVRAG/UVRAG-uniprot.txt
  title: UniProtKB record for human UVRAG
  findings: []
- id: file:human/UVRAG/UVRAG-notes.md
  title: UVRAG review notes
  findings: []
core_functions:
- molecular_function:
    id: GO:0030674
    label: protein-macromolecule adaptor activity
  description: UVRAG acts as the UVRAG-defining regulatory/adaptor subunit of PI3KC3-C2, linking 
    PIK3C3/PIK3R4/BECN1 complex activity to PI3P-dependent endosomal and late autophagy trafficking.
  directly_involved_in:
  - id: GO:0036092
    label: phosphatidylinositol-3-phosphate biosynthetic process
  - id: GO:0097352
    label: autophagosome maturation
  - id: GO:1901098
    label: positive regulation of autophagosome maturation
  - id: GO:0071985
    label: multivesicular body sorting pathway
  locations:
  - id: GO:0005776
    label: autophagosome
  - id: GO:0000421
    label: autophagosome membrane
  - id: GO:0005769
    label: early endosome
  - id: GO:0005770
    label: late endosome
  - id: GO:0005764
    label: lysosome
  in_complex:
    id: GO:0034272
    label: phosphatidylinositol 3-kinase complex, class III, type II
  supported_by:
  - reference_id: PMID:16799551
    supporting_text: positive regulator of the Beclin1-PI(3)KC3 complex
  - reference_id: PMID:18843052
    supporting_text: Atg14, and UVRAG are not present in the same complex
  - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
    supporting_text: acts as a regulatory subunit of the alternative PI3K complex II
  - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
    supporting_text: mediates formation of phosphatidylinositol 3-phosphate
  - &id001
    reference_id: PMID:18552835
    supporting_text: interacts with the class C Vps complex
  - &id002
    reference_id: PMID:18552835
    supporting_text: autophagosome fusion with late endosomes/lysosomes
  - reference_id: PMID:28306502
    supporting_text: Pacer recruits PI3KC3 and HOPS complexes to the autophagosome
  - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
    supporting_text: Involved in maturation of autophagosomes and degradative endocytic trafficking
- molecular_function:
    id: GO:0000149
    label: SNARE binding
  description: UVRAG engages class C VPS/HOPS and endosomal/autophagosomal SNARE machinery to promote 
    fusogenic SNARE complex assembly during late endosomal and autophagosome maturation events.
  directly_involved_in:
  - id: GO:0035493
    label: SNARE complex assembly
  - id: GO:0097352
    label: autophagosome maturation
  locations:
  - id: GO:0005770
    label: late endosome
  - id: GO:0005764
    label: lysosome
  - id: GO:0000421
    label: autophagosome membrane
  supported_by:
  - reference_id: PMID:24550300
    supporting_text: interactions with the class C vacuolar protein sorting (C-Vps) tethering complex and 
      endosomal
  - reference_id: PMID:24550300
    supporting_text: by assembling a specific fusogenic SNARE complex
  - reference_id: file:human/UVRAG/UVRAG-uniprot.txt
    supporting_text: SNARE complex and promotes fusogenic SNARE complex formation during
  - *id001
  - *id002
proposed_new_terms: []
suggested_questions:
- question: Should UVRAG be curated directly to GO:0034272 phosphatidylinositol 3-kinase complex, class III, 
    type II rather than the parent class III PI3K complex term?
  experts:
  - GO autophagy editors
  - ComplexPortal curators
  - Reactome autophagy curators
- question: Should UVRAG SNARE/HOPS activity be represented only by SNARE binding and SNARE complex assembly, 
    or is a more specific autophagosome-lysosome fusion adaptor term needed?
  experts:
  - GO molecular function editors
  - autophagosome maturation experts
- question: Should UVRAG DNA repair and centrosome annotations remain non-core in autophagy-focused reviews 
    even though they are experimentally supported?
  experts:
  - GO DNA repair editors
  - GO autophagy editors
suggested_experiments:
- description: Use UVRAG separation-of-function mutants that disrupt BECN1/PIK3C3 binding, HOPS/class C VPS 
    binding, or SNARE binding, followed by PI3P imaging, STX17/HOPS recruitment, and autophagosome-lysosome 
    fusion assays.
  experiment_type: UVRAG autophagy maturation separation-of-function rescue
  hypothesis: PI3KC3-C2 complex engagement and HOPS/SNARE engagement define separable UVRAG contributions to 
    PI3P production and autophagosome maturation.
- description: Compare UVRAG wild type, DNA-PK-binding mutants, and CEP63/centrosome-interaction mutants in 
    the same knockout-rescue background with autophagic flux, NHEJ reporter, and centrosome/chromosome 
    segregation readouts.
  experiment_type: parallel autophagy and genome-stability rescue assay
  hypothesis: UVRAG autophagosome maturation and DNA repair/centrosome functions are genetically separable 
    branches rather than one shared autophagy-dependent phenotype.