+ |
UBE2L3 | up-regulates activity
binding
|
RNF19B |
0.494 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271591 |
|
|
Homo sapiens |
Natural Killer Cell |
pmid |
sentence |
16709802 |
We demonstrated that both UbcH7 and UbcH8 bind to full-length NKLAM. We demonstrated decreased protein expression and enhanced ubiquitination of URKL-1 in the presence of NKLAM. These data indicate that NKLAM is a RING finger protein that binds Ubcs and |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF19B | down-regulates quantity by destabilization
ubiquitination
|
UCKL1 |
0.603 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271590 |
|
|
Homo sapiens |
Natural Killer Cell |
pmid |
sentence |
16709802 |
We demonstrated that both UbcH7 and UbcH8 bind to full-length NKLAM. We demonstrated decreased protein expression and enhanced ubiquitination of URKL-1 in the presence of NKLAM. These data indicate that NKLAM is a RING finger protein that binds Ubcs and has as one of its substrates, URKL-1, thus defining this cytolytic protein as an E3 ubiquitin ligase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBE2E2 | up-regulates activity
binding
|
RNF19B |
0.484 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271592 |
|
|
Homo sapiens |
Natural Killer Cell |
pmid |
sentence |
16709802 |
We demonstrated that both UbcH7 and UbcH8 bind to full-length NKLAM. We demonstrated decreased protein expression and enhanced ubiquitination of URKL-1 in the presence of NKLAM. These data indicate that NKLAM is a RING finger protein that binds Ubcs and |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF19B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271173 |
|
|
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 |