+ |
UBE2J1 | down-regulates quantity by destabilization
ubiquitination
|
DIO2 |
0.387 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267481 |
Lys237 |
VCIVQRQkIAYLGGK |
Homo sapiens |
|
pmid |
sentence |
29892818 |
ER residency places D2 physically close to an array of proteins that interact and modify the D2 molecule via ubiquitination and targeting to the proteasomal system, explaining its relatively short half-life. Both ubiquitin conjugases UBC6 and or UBC7 interact with D2 and support D2 ubiquitination. Two Lys residues in D2 are involved in this process, K237 and K244. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267482 |
Lys244 |
KIAYLGGkGPFSYNL |
Homo sapiens |
|
pmid |
sentence |
29892818 |
ER residency places D2 physically close to an array of proteins that interact and modify the D2 molecule via ubiquitination and targeting to the proteasomal system, explaining its relatively short half-life. Both ubiquitin conjugases UBC6 and or UBC7 interact with D2 and support D2 ubiquitination. Two Lys residues in D2 are involved in this process, K237 and K244. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Thyroid Gland |
Pathways: | Thyroid Hormone Metabolism |
+ |
MAPKAPK2 | down-regulates quantity by destabilization
phosphorylation
|
UBE2J1 |
0.339 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263091 |
Ser184 |
KELARQIsFKAEVNS |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
24020373 |
Endoplasmic reticulum-associated ubiquitin-conjugating enzyme Ube2j1 is a novel substrate of MK2 (MAPKAP kinase-2) involved in MK2-mediated TNFα production. These findings strongly suggest that MK2 directly phosphorylates Ube2j1 at Ser(184) upon p38-activating stress in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBE2J1 | down-regulates quantity by destabilization
ubiquitination
|
DIO |
0.387 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270242 |
|
|
Homo sapiens |
|
pmid |
sentence |
29892818 |
ER residency places D2 physically close to an array of proteins that interact and modify the D2 molecule via ubiquitination and targeting to the proteasomal system, explaining its relatively short half-life. Both ubiquitin conjugases UBC6 and or UBC7 interact with D2 and support D2 ubiquitination. Two Lys residues in D2 are involved in this process, K237 and K244. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Thyroid Gland |
+ |
Ub:E1 (UBA6 substrate) | up-regulates activity
ubiquitination
|
UBE2J1 |
0.571 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271342 |
|
|
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 |
+ |
Ub:E1 (UBA1 substrate) | up-regulates activity
ubiquitination
|
UBE2J1 |
0.582 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271308 |
|
|
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 |
+ |
BIRC2 | down-regulates quantity by destabilization
ubiquitination
|
UBE2J1 |
0.377 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263092 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
28321712 |
We also found that ubiquitin-ligase (E3), c-IAP1 preferentially interacts with phosphorylated Ube2j1. Moreover, we noticed that phosphorylated Ube2j1 is rapidly degraded by the proteasome during ER stress cell recovery. Taken together, these data suggest that Ube2j1 and its phosphorylation is important for transient ER stress cell recovery and the phosphorylated Ube2j1 is degraded by the proteasome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |