| + |
UBE2D1 | up-regulates activity 
binding
|
KPC |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271514 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15531880 |
We now describe a previously unidentified E3 complex: KPC (Kip1 ubiquitination-promoting complex), consisting of KPC1 and KPC2. KPC1 contains a RING-finger domain, and KPC2 contains a ubiquitin-like domain and two ubiquitin-associated domains. KPC interacts with and ubiquitinates p27(Kip1) and is localized to the cytoplasm. Overexpression of KPC promoted the degradation of p27(Kip1), whereas a dominant-negative mutant of KPC1 delayed p27(Kip1) degradation. Polyubiquitination activity of KPC was apparent with only Ubc4 or UbcH5A. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
UBAC1 | form complex 
binding
|
KPC |
0.881 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271512 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15531880 |
We now describe a previously unidentified E3 complex: KPC (Kip1 ubiquitination-promoting complex), consisting of KPC1 and KPC2. KPC1 contains a RING-finger domain, and KPC2 contains a ubiquitin-like domain and two ubiquitin-associated domains. KPC interacts with and ubiquitinates p27(Kip1) and is localized to the cytoplasm. Overexpression of KPC promoted the degradation of p27(Kip1), whereas a dominant-negative mutant of KPC1 delayed p27(Kip1) degradation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
KPC | down-regulates quantity by destabilization 
polyubiquitination
|
CDKN1B |
0.442 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271513 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15531880 |
We now describe a previously unidentified E3 complex: KPC (Kip1 ubiquitination-promoting complex), consisting of KPC1 and KPC2. KPC1 contains a RING-finger domain, and KPC2 contains a ubiquitin-like domain and two ubiquitin-associated domains. KPC interacts with and ubiquitinates p27(Kip1) and is localized to the cytoplasm. Overexpression of KPC promoted the degradation of p27(Kip1), whereas a dominant-negative mutant of KPC1 delayed p27(Kip1) degradation. Polyubiquitination activity of KPC was apparent with only Ubc4 or UbcH5A. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
UBE2D2 | up-regulates activity
binding
|
KPC |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271515 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15531880 |
We now describe a previously unidentified E3 complex: KPC (Kip1 ubiquitination-promoting complex), consisting of KPC1 and KPC2. KPC1 contains a RING-finger domain, and KPC2 contains a ubiquitin-like domain and two ubiquitin-associated domains. KPC interacts with and ubiquitinates p27(Kip1) and is localized to the cytoplasm. Overexpression of KPC promoted the degradation of p27(Kip1), whereas a dominant-negative mutant of KPC1 delayed p27(Kip1) degradation. Polyubiquitination activity of KPC was apparent with only Ubc4 or UbcH5A. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RNF123 | form complex
binding
|
KPC |
0.881 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271511 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 15531880 |
We now describe a previously unidentified E3 complex: KPC (Kip1 ubiquitination-promoting complex), consisting of KPC1 and KPC2. KPC1 contains a RING-finger domain, and KPC2 contains a ubiquitin-like domain and two ubiquitin-associated domains. KPC interacts with and ubiquitinates p27(Kip1) and is localized to the cytoplasm. Overexpression of KPC promoted the degradation of p27(Kip1), whereas a dominant-negative mutant of KPC1 delayed p27(Kip1) degradation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
KPC