+ |
ATG7 | up-regulates activity
binding
|
GABARAPL2 |
0.903 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-142002 |
|
|
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 |
+ |
NBR1 | up-regulates
binding
|
GABARAPL2 |
0.735 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184267 |
|
|
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 |
+ |
TP53INP2 | up-regulates
binding
|
GABARAPL2 |
0.589 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182611 |
|
|
Homo sapiens |
|
pmid |
sentence |
19056683 |
Tp53inp2 binds to lc3 as well as to lc3-related proteins gabarap and gabarap-like2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ATG3 | up-regulates activity
binding
|
GABARAPL2 |
0.869 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-141926 |
|
|
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 |
+ |
GABARAPL2 | up-regulates activity
binding
|
SQSTM1 |
0.861 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-156307 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17580304 |
P62 binds both to lc3a and -b and the related gabarap family proteins/this interaction is necessary for autophagic degradation of p62-positive cytoplasmic inclusion bodies containing ubiquitinated proteins. We also demonstrate that alis are indistinguisha |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Autophagy |
+ |
ATG4B | up-regulates activity
cleavage
|
GABARAPL2 |
0.838 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-141932 |
|
|
in vitro |
|
pmid |
sentence |
16303767 |
In mammals, at least three atg8 homologs, lc3, gabarap, and gate-16, have been identified (fig. 1a), all of which have structural ubiquitin folds (1416). 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 |
+ |
TP53INP1 | up-regulates
binding
|
GABARAPL2 |
0.388 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-196667 |
|
|
Homo sapiens |
|
pmid |
sentence |
22421968 |
In this work, we show that tp53inp1 is also able to interact with atg8-family proteins and to induce autophagy-dependent cell death. mammalian cells contain multiple atg8 orthologs belonging to three subfamilies: microtubule-associated protein 1 light chain 3, -aminobutyric acid receptor-associated protein (gabarap) and -aminobutyric acid receptor-associated protein like 2 (gabarapl2). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |