| + |
GABARAP | up-regulates activity 
binding
|
GPHN |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264971 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25882190 |
The GABA(A)R-associated protein GABARAP was found to bind to the gamma2 subunit of GABA(A)Rs. Here we show that GABARAP interacts with gephyrin in both biochemical assays and transfected cells. Our data indicate that GABARAP-gephyrin interactions are not important for postsynaptic GABA(A)R anchoring but may be implicated in receptor sorting and/or targeting mechanisms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | GABAergic synapse |
| + |
O-phosphoethanolamine | up-regulates
chemical activation
|
GABARAP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142011 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16303767 |
Three human atg8 (hatg8) homologs, lc3, gabarap, and gate-16, have been characterized as modifiers in reactions mediated by hatg7 (an e1-like enzyme) and hatg3 (an e2-like enzyme) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATG4B | up-regulates activity
cleavage
|
GABARAP |
0.856 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141929 |
|
|
in vitro |
|
| pmid |
sentence |
| 16303767 |
In vivo and in vitro biochemical analyses have shown that human atg4b is an authentic cysteine protease essential for cleavage of the c terminus of each atg8 homolog to expose the c-terminal gly |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Autophagy |
| + |
WDFY3 | down-regulates quantity by destabilization 
binding
|
GABARAP |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266796 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 24668264 |
Here, we show that ALFY binds selectively to LC3C and the GABARAPs through a LIR in its WD40 domain. Binding of ALFY to GABARAP is indispensable for its recruitment to LC3B-positive structures and, thus, for the clearance of certain p62 structures by autophagy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATG3 | up-regulates activity
binding
|
GABARAP |
0.842 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141868 |
|
|
in vitro |
|
| pmid |
sentence |
| 16303767 |
Three human atg8 (hatg8) homologs, lc3, gabarap, and gate-16, have been characterized as modifiers in reactions mediated by hatg7 (an e1-like enzyme) and hatg3 (an e2-like enzyme) |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Autophagy |
| + |
ULK1 | up-regulates
binding
|
GABARAP |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85614 |
|
|
Homo sapiens |
HeLa Cell, Neuron |
| pmid |
sentence |
| 11146101 |
N-terminal proline/serine rich (ps) domain of ulk1 (amino acid 287-416) is required for ulk1-gate-16 and ulk1-gabarap protein interactions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NBR1 | up-regulates
binding
|
GABARAP |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184261 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19250911 |
We performed glutathione s-transferase (gst) pull-down assays using extracts from hek293 cells overexpressing an ha-tagged nbr1(d50r) mutant, which lacks the ability to bind p62 (lamark et al., 2003) (figures s1a and s1b, available online), and gst fusions of six human atg8 homologs: gabarap, gabarapl1, gabarapl2, lc3a, lc3b, and lc3c. Indeed, nbr1 interacted with all these members of the mammalian atg8 protein family |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ANK3 | up-regulates activity
binding
|
GABARAP |
0.454 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266709 |
|
|
Mus musculus |
Pyramidal Neuron |
| pmid |
sentence |
| 30504823 |
Importantly, the 480 kDa ankyrin-G isoform has also been shown to stabilize GABAergic synapses on the soma and AIS of excitatory pyramidal neurons by interacting with the GABAA receptor-associated protein (GABARAP) to inhibit GABAA receptor endocytosis |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
GABARAP | up-regulates activity
binding
|
mTORC1 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219391 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11146101 |
N-terminal proline/serine rich (ps) domain of ulk1 (amino acid 287-416) is required for ulk1-gate-16 and ulk1-gabarap protein interactions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Autophagy |
| + |
GABARAP | up-regulates activity
binding
|
GABA-A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264972 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25882190 |
GABARAP was originally isolated as a binding partner of the GABAA receptor γ2-subunit in a yeast two-hybrid screen, and was suggested to have a role in the targeting and clustering of GABAA receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | GABAergic synapse |
| + |
GABARAP | up-regulates
binding
|
TBC1D25 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172536 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21383079 |
In this study, we report evidence demonstrating that oatl1, a putative rab guanosine triphosphatase-activating protein (gap), is a novel binding partner of atg8 homologues in mammalian cells. Oatl1 is recruited to isolation membranes and autophagosomes through direct interaction with atg8 homologues and is involved in the fusion between autophagosomes and lysosomes through its gap activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TP53INP1 | up-regulates
binding
|
GABARAP |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196664 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22421968 |
Tp53inp1 is also able to interact with atg8-family proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
GABARAP
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