| + |
BECN1 | form complex 
binding
|
Vps34 Complex I |
0.935 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260315 |
|
|
in vitro |
|
| pmid |
sentence |
| 30397185 |
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 |
| + |
PAQR3 | up-regulates activity 
binding
|
Vps34 Complex I |
0.252 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273738 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26834238 |
Firstly, PAQR3 functions as a scaffold protein that facilitates the formation of ATG14L- but not UVRAG-linked VPS34 complex, leading to elevated capacity of PI(3)P generation ahead of starvation signals. Secondly, AMPK phosphorylates PAQR3 at threonine 32 and switches on PI(3)P production to initiate autophagosome formation swiftly after glucose starvation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Vps34 Complex I | up-regulates 
|
Autophagy |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260325 |
|
|
|
|
| pmid |
sentence |
| 30397185 |
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 |
| + |
PIK3R4 | form complex
binding
|
Vps34 Complex I |
0.917 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260317 |
|
|
in vitro |
|
| pmid |
sentence |
| 30397185 |
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 |
| + |
PIK3C3 | form complex
binding
|
Vps34 Complex I |
0.917 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260316 |
|
|
in vitro |
|
| pmid |
sentence |
| 30397185 |
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 |
| + |
ATG14 | form complex
binding
|
Vps34 Complex I |
0.908 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260318 |
|
|
in vitro |
|
| pmid |
sentence |
| 30397185 |
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 |
| + |
NRBF2 | down-regulates activity 
binding
|
Vps34 Complex I |
0.708 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265880 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 24785657 |
We have now identified NRBF2 (nuclear receptor-binding factor 2) as a new member of Vps34 Complex I. NRBF2 binds to complexes that include Vps34, Vps15, Beclin-1 and ATG-14L, but not the Vps34 Complex II component UVRAG (UV radiation resistance-associated gene). NRBF2 directly interacts with Vps15 via the Vps15 WD40 domain as well as other regions of Vps15. Thus NRBF2 plays a critical role in the induction of starvation-induced autophagy as a specific member of Vps34 Complex I. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Vps34 Complex I | up-regulates
|
Autophagosome_formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260323 |
|
|
|
|
| pmid |
sentence |
| 30397185 |
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 |
3.0
Vps34 Complex I
CPX-73