+ |
UBE2G2 | down-regulates quantity by destabilization
ubiquitination
|
DIO2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267483 |
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-267484 |
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 |
+ |
UBE2G2 | down-regulates quantity by destabilization
ubiquitination
|
DIO |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270244 |
|
|
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 |
+ |
UBE2G2 | up-regulates activity
ubiquitination
|
SYVN1 |
0.681 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272593 |
|
|
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
14593114 |
We show that human HRD1 is a non-glycosylated, stable ER protein with a cytosolic RING-H2 finger domain. In the presence of the ubiquitin-conjugating enzyme UBC7, the RING-H2 finger has in vitro ubiquitination activity for Lys(48)-specific polyubiquitin linkage, suggesting that human HRD1 is an E3 ubiquitin ligase involved in protein degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
Ub:E1 (UBA6 substrate) | up-regulates activity
ubiquitination
|
UBE2G2 |
0.655 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271344 |
|
|
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
|
UBE2G2 |
0.71 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271310 |
|
|
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 |