| + |
MKRN1 | up-regulates activity 
ubiquitination
|
RPS10 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272216 |
Lys107 |
ETGRPRPkGLEGERP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31640799 |
We show that MKRN1 directly binds to the cytoplasmic poly(A)-binding protein (PABPC1) and associates with polysomes. MKRN1 is positioned upstream of poly(A) tails in mRNAs in a PABPC1-dependent manner. Ubiquitin remnant profiling and in vitro ubiquitylation assays uncover PABPC1 and ribosomal protein RPS10 as direct ubiquitylation substrates of MKRN1.Our data show that MKRN1 associates with polysomes and ubiquitylates RPS10, indicating a role in translational control. We hypothesize that ribosomes encountering the MKRN1-PABPC1 complex are stalled, possibly via ubiquitylation of RPS10 on K107 and other MKRN1 substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MKRN1 | down-regulates quantity by destabilization 
polyubiquitination
|
TP53 |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271846 |
Lys291 |
TEEENLRkKGEPHHE |
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 19536131 |
Makorin Ring Finger Protein 1 (MKRN1) is a transcriptional co-regulator and an E3 ligase. Here, we show that MKRN1 simultaneously functions as a differentially negative regulator of p53 and p21. In normal conditions, MKRN1 could destabilize both p53 and p21 through ubiquitination and proteasome-dependent degradation. As a result, depletion of MKRN1 induced growth arrest through activation of p53 and p21. K291 and K292 of p53 are required for MKRN1-mediated degradation and ubiquitination of p53 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271847 |
Lys292 |
EEENLRKkGEPHHEL |
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 19536131 |
Makorin Ring Finger Protein 1 (MKRN1) is a transcriptional co-regulator and an E3 ligase. Here, we show that MKRN1 simultaneously functions as a differentially negative regulator of p53 and p21. In normal conditions, MKRN1 could destabilize both p53 and p21 through ubiquitination and proteasome-dependent degradation. As a result, depletion of MKRN1 induced growth arrest through activation of p53 and p21. K291 and K292 of p53 are required for MKRN1-mediated degradation and ubiquitination of p53 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MKRN1 | down-regulates quantity by destabilization
polyubiquitination
|
CDKN1A |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271845 |
|
|
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 19536131 |
Makorin Ring Finger Protein 1 (MKRN1) is a transcriptional co-regulator and an E3 ligase. Here, we show that MKRN1 simultaneously functions as a differentially negative regulator of p53 and p21. In normal conditions, MKRN1 could destabilize both p53 and p21 through ubiquitination and proteasome-dependent degradation. As a result, depletion of MKRN1 induced growth arrest through activation of p53 and p21. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MKRN1 | down-regulates quantity by destabilization
polyubiquitination
|
TERT |
0.488 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271529 |
|
|
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 15805468 |
MKRN1 functions as an E3 ubiquitin-ligase for hTERT in vitro and in vivo. Furthermore, we have used the yeast two-hybrid method to identify a novel RING finger gene (MKRN1) encoding an E3 ligase that mediates ubiquitination of hTERT. Overexpression of MKRN1 in telomerase-positive cells promotes the degradation of hTERT and decreases telomerase activity and subsequently telomere length. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MKRN1 | up-regulates activity
ubiquitination
|
PABPC1 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272215 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31640799 |
We show that MKRN1 directly binds to the cytoplasmic poly(A)-binding protein (PABPC1) and associates with polysomes. MKRN1 is positioned upstream of poly(A) tails in mRNAs in a PABPC1-dependent manner. Ubiquitin remnant profiling and in vitro ubiquitylation assays uncover PABPC1 and ribosomal protein RPS10 as direct ubiquitylation substrates of MKRN1.Our data show that MKRN1 associates with polysomes and ubiquitylates RPS10, indicating a role in translational control. We hypothesize that ribosomes encountering the MKRN1-PABPC1 complex are stalled, possibly via ubiquitylation of RPS10 on K107 and other MKRN1 substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
MKRN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271234 |
|
|
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 |
| + |
MKRN1 | down-regulates quantity by destabilization
polyubiquitination
|
CDKN2A |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272036 |
|
|
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 23104211 |
Biochemical analyses confirmed that MKRN1 targets p14ARF for ubiquitination and subsequent proteasome-dependent degradation.The Skp1-Cul1-F-box-protein44 (SCF(FBXO44)) complex ubiquitinates full-length BRCA1 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MKRN1
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