| + |
PKA | down-regulates quantity by destabilization 
phosphorylation
|
ATG16L1 (isoform 2) |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277489 |
Ser268 |
SRAATRRsVSSFPVP |
in vitro |
|
| pmid |
sentence |
| 31580256 |
PKA phosphorylates ATG16L1α at Ser268 and ATG16L1β at Ser269, driving phosphorylation-dependent degradation of ATG16L1 protein. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PKA | down-regulates quantity by destabilization
phosphorylation
|
ATG16L1 (isoform 1) |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277488 |
Ser269 |
RAATKRLsQPAGGLL |
in vitro |
|
| pmid |
sentence |
| 31580256 |
PKA phosphorylates ATG16L1α at Ser268 and ATG16L1β at Ser269, driving phosphorylation-dependent degradation of ATG16L1 protein. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
WIPI2 | up-regulates quantity 
binding
|
ATG16L1 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268478 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 28561066 |
WIPI1 assists WIPI2 in recruiting ATG16L for LC3 lipidation. WIPI1-WIPI2 heterodimer may function more efficiently in ATG16L complex recruitment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFE3 | up-regulates quantity by expression 
transcriptional regulation
|
ATG16L1 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276807 |
|
|
|
|
| pmid |
sentence |
| 24448649 |
The most significantly up-regulated genes encode proteins that play an essential role in formation of autophagosomes (ATG16L1, ATG9B, GABARAPL1, and WIPI1), as well as their degradation (UVRAG). Analysis of the LC3II/LC3I ratio upon TFE3, TFEB, or MITF1 overexpression confirmed autophagy induction (Fig. 4, B and C). Accordingly, we observed an accumulation of autophagosomes in TFE3-expressing cells |
|
| Publications: |
1 |
| + |
NOD2 | up-regulates activity
binding
|
ATG16L1 |
0.75 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252405 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19898471 |
By a mechanism independent of the adaptor RIP2 and transcription factor NF-kappaB, Nod1 and Nod2 recruited the autophagy protein ATG16L1 to the plasma membrane at the bacterial entry site. Our results link bacterial sensing by Nod proteins to the induction of autophagy and provide a functional link between Nod2 and ATG16L1, which are encoded by two of the most important genes associated with Crohn's disease. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GAN | down-regulates quantity
ubiquitination
|
ATG16L1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268948 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 30770803 |
Here we identify Gigaxonin24, an E3 ligase mutated in a fatal neurodegenerative disease called giant axonal neuropathy (GAN)25, as the first regulator of ATG16L1. Gigaxonin poly-ubiquitinates and controls the degradation of ATG16L1, and is essential to activate autophagy. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
NOD1 | up-regulates activity
binding
|
ATG16L1 |
0.672 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252406 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19898471 |
By a mechanism independent of the adaptor RIP2 and transcription factor NF-kappaB, Nod1 and Nod2 recruited the autophagy protein ATG16L1 to the plasma membrane at the bacterial entry site. Our results link bacterial sensing by Nod proteins to the induction of autophagy and provide a functional link between Nod2 and ATG16L1, which are encoded by two of the most important genes associated with Crohn's disease. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATG16L1 | form complex 
binding
|
ATG12/5/16L1 |
0.882 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226696 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18321988 |
Atg12 is conjugated to atg5 and forms an approximately 800-kda protein complex with atg16l (referred to as atg16l complex). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
HEK-293 Cell |
| + |
WIPI1 | up-regulates quantity
binding
|
ATG16L1 |
0.594 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268477 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 28561066 |
WIPI1 assists WIPI2 in recruiting ATG16L for LC3 lipidation. WIPI1-WIPI2 heterodimer may function more efficiently in ATG16L complex recruitment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAB33B | up-regulates
binding
|
ATG16L1 |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178542 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18448665 |
Olgi-resident small gtpase rab33b interacts with atg16l and modulates autophagosome formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATG16L1 | up-regulates
binding
|
CLTCL1 |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166705 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20639872 |
Clathrin heavy-chain interacts with atg16l1, and is involved in the formation of atg16l1-positive early autophagosome precursors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATG16L1 | up-regulates
binding
|
CLTC |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166702 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20639872 |
Clathrin heavy-chain interacts with atg16l1, and is involved in the formation of atg16l1-positive early autophagosome precursors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ATG16L1
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