| + |
LNX1 | down-regulates quantity by destabilization 
ubiquitination
|
GRIN1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272901 |
|
|
in vitro |
|
| pmid |
sentence |
| 22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LNX1 | down-regulates quantity by destabilization
ubiquitination
|
KCNA4 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272899 |
|
|
in vitro |
|
| pmid |
sentence |
| 22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo.The C-terminal LNX1 PDZ1-binding motifs of the ATP-binding cassette, subfamily A member 1 (ABC-1), PBK, glutamate receptor, ionotropic, N-methyl d-aspartate 1 (GRIN1), and Claudin-17 significantly promoted the ubiquitination of the corresponding artificial degrons by LNX1ΔPDZ234. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LNX1 | down-regulates quantity by destabilization
polyubiquitination
|
ZBTB8A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272777 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19668196 |
LNX (ligand of Numb protein-X) is a RING finger and four PDZ domain-containing E3 ubiquitin ligase. Lnx-l induced K48-linked polyubiquitylation of Boz, leading to its proteasomal degradation in human 293T cells and in zebrafish embryos. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LNX1 | down-regulates quantity by destabilization
ubiquitination
|
BCR |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272903 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LNX1 | down-regulates quantity by destabilization
ubiquitination
|
PBK |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272898 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity 
ubiquitination
|
LNX1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271094 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LNX1 | down-regulates
ubiquitination
|
NUMB |
0.73 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112201 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11782429 |
Lnx functions as a ring type e3 ubiquitin ligase that targets the cell fate determinant numb for ubiquitin-dependent degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LNX1 | down-regulates quantity by destabilization
ubiquitination
|
CLDN17 |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272900 |
|
|
in vitro |
|
| pmid |
sentence |
| 22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LNX1 | down-regulates quantity by destabilization
ubiquitination
|
ABCA1 |
0.243 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272902 |
|
|
in vitro |
|
| pmid |
sentence |
| 22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
LNX1
- 
- 