Relation Results

Summary

Name Vps34 Complex II
Primary ID SIGNOR-C241
Links CPX-74
Type complex
Formed by BECN1, PIK3C3, PIK3R4, UVRAG
Relations 6
Pathways Autophagy

Viewer

Type: Score: Layout: SPV 
0.8140.70.8810.70.9030.891UVRAGVps34 Complex IIAutophagosome_formationPIK3R4AutophagyBECN1PIK3C3

Relations

Regulator
Mechanism
target
score
+ form complex img/form-complex.png binding Vps34 Complex II 0.814
Identifier Residue Sequence Organism Cell Line
SIGNOR-260322 in vitro
pmid sentence
PtdIns3P recruits specific recognition modules that are common in protein-sorting pathways, such as autophagy and endocytic sorting. It is best characterized in two heterotetramers, complexes I and II. Complex I is composed of VPS34, VPS15, Beclin 1, and autophagy-related gene (ATG)14L, whereas complex II replaces ATG14L with UVRAG. |Complexes I and II are critical for early events in autophagy and endocytic sorting, respectively.
Publications: 1 Organism: In Vitro
Pathways:Autophagy
+ up-regulates img/indirect-activation.png Autophagosome_formation 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-260324
pmid sentence
PtdIns3P recruits specific recognition modules that are common in protein-sorting pathways, such as autophagy and endocytic sorting. It is best characterized in two heterotetramers, complexes I and II. Complex I is composed of VPS34, VPS15, Beclin 1, and autophagy-related gene (ATG)14L, whereas complex II replaces ATG14L with UVRAG. |Complexes I and II are critical for early events in autophagy and endocytic sorting, respectively.
Publications: 1
Pathways:Autophagy
+ form complex img/form-complex.png binding Vps34 Complex II 0.881
Identifier Residue Sequence Organism Cell Line
SIGNOR-260321 in vitro
pmid sentence
PtdIns3P recruits specific recognition modules that are common in protein-sorting pathways, such as autophagy and endocytic sorting. It is best characterized in two heterotetramers, complexes I and II. Complex I is composed of VPS34, VPS15, Beclin 1, and autophagy-related gene (ATG)14L, whereas complex II replaces ATG14L with UVRAG. |Complexes I and II are critical for early events in autophagy and endocytic sorting, respectively.
Publications: 1 Organism: In Vitro
+ up-regulates img/indirect-activation.png Autophagy 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-260326
pmid sentence
PtdIns3P recruits specific recognition modules that are common in protein-sorting pathways, such as autophagy and endocytic sorting. It is best characterized in two heterotetramers, complexes I and II. Complex I is composed of VPS34, VPS15, Beclin 1, and autophagy-related gene (ATG)14L, whereas complex II replaces ATG14L with UVRAG. |Complexes I and II are critical for early events in autophagy and endocytic sorting, respectively.
Publications: 1
Pathways:Autophagy
+ form complex img/form-complex.png binding Vps34 Complex II 0.903
Identifier Residue Sequence Organism Cell Line
SIGNOR-260319 in vitro
pmid sentence
PtdIns3P recruits specific recognition modules that are common in protein-sorting pathways, such as autophagy and endocytic sorting. It is best characterized in two heterotetramers, complexes I and II. Complex I is composed of VPS34, VPS15, Beclin 1, and autophagy-related gene (ATG)14L, whereas complex II replaces ATG14L with UVRAG. |Complexes I and II are critical for early events in autophagy and endocytic sorting, respectively.
Publications: 1 Organism: In Vitro
Pathways:Autophagy
+ form complex img/form-complex.png binding Vps34 Complex II 0.891
Identifier Residue Sequence Organism Cell Line
SIGNOR-260320 in vitro
pmid sentence
PtdIns3P recruits specific recognition modules that are common in protein-sorting pathways, such as autophagy and endocytic sorting. It is best characterized in two heterotetramers, complexes I and II. Complex I is composed of VPS34, VPS15, Beclin 1, and autophagy-related gene (ATG)14L, whereas complex II replaces ATG14L with UVRAG. |Complexes I and II are critical for early events in autophagy and endocytic sorting, respectively.
Publications: 1 Organism: In Vitro
Pathways:Autophagy
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