Relation Results

Summary

Name MPG
Full Name DNA-3-methyladenine glycosylase
Synonyms 3-alkyladenine DNA glycosylase, 3-methyladenine DNA glycosidase, ADPG, N-methylpurine-DNA glycosylase | AAG, ANPG, MID1
Primary ID P29372
Links - -
Type protein
Relations 6
Function Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesio ...
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Type: Score: Layout: SPV 
0.20.20.20.20.20.2UBE2D3MPGSTK36IGBP1UBE2D1PPP2CAUBE2E1

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Relations
Regulator
Mechanism
target
score ℹ
+ UBE2D3up-regulates activity img/direct-activation.png binding MPG 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271928 in vitro
pmid sentence
Here we report that MID1 catalyzes the in vitro ubiquitination of the catalytic subunit of PP2A (PP2Ac) in the absence of alpha4. In the presence of alpha4, the level of PP2Ac ubiquitination is reduced.The high molecular weight smear pattern was not as obvious, suggesting that domains within the C-terminal half of MID1 may contribute to the polyubiquitination of PP2Ac. We observed that PP2Ac was ubiquitinated in the presence of UbcH5a-c and UbcH6, similar to results obtained with MID1-catalyzed ubiquitination of alpha4 (Figure 2E)
Publications: 1 Organism: In Vitro
+ MPGdown-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination STK36 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272466 in vitro
pmid sentence
 Here, we show that MID1 catalyzes the ubiquitination and proteasomal cleavage of the GLI3 regulator Fu.
Publications: 1 Organism: In Vitro
+ MPGdown-regulates quantity by destabilization img/direct_inhibition.png monoubiquitination IGBP1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272040 Homo sapiens HEK-293 Cell
pmid sentence
 We show MID1-dependent monoubiquitination of α4 triggers calpain-mediated cleavage and switches α4's activity from protective to destructive, resulting in increased Tau phosphorylation. MID1 serves as the E3 ligase for α4 (2B), leading to a conformational change in α4 whereby the UIM of α4 binds in cis to the covalently attached ubiquitin (Ub; 3). This structural rearrangement then leads to calpain-mediated cleavage of the C terminus of α4 (4), allowing for polyubiquitination of PP2Ac by a currently unknown E3 ligase (5) and subsequent degradation by the proteasome.
Publications: 1 Organism: Homo Sapiens
+ UBE2D1up-regulates activity img/direct-activation.png binding MPG 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271927 in vitro
pmid sentence
Here we report that MID1 catalyzes the in vitro ubiquitination of the catalytic subunit of PP2A (PP2Ac) in the absence of alpha4. In the presence of alpha4, the level of PP2Ac ubiquitination is reduced.The high molecular weight smear pattern was not as obvious, suggesting that domains within the C-terminal half of MID1 may contribute to the polyubiquitination of PP2Ac. We observed that PP2Ac was ubiquitinated in the presence of UbcH5a-c and UbcH6, similar to results obtained with MID1-catalyzed ubiquitination of alpha4 (Figure 2E)
Publications: 1 Organism: In Vitro
+ MPGdown-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination PPP2CA 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271930 in vitro
pmid sentence
Here we report that MID1 catalyzes the in vitro ubiquitination of the catalytic subunit of PP2A (PP2Ac) in the absence of alpha4. In the presence of alpha4, the level of PP2Ac ubiquitination is reduced.The high molecular weight smear pattern was not as obvious, suggesting that domains within the C-terminal half of MID1 may contribute to the polyubiquitination of PP2Ac.
Publications: 1 Organism: In Vitro
+ UBE2E1up-regulates activity img/direct-activation.png binding MPG 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271929 in vitro
pmid sentence
Here we report that MID1 catalyzes the in vitro ubiquitination of the catalytic subunit of PP2A (PP2Ac) in the absence of alpha4. In the presence of alpha4, the level of PP2Ac ubiquitination is reduced.The high molecular weight smear pattern was not as obvious, suggesting that domains within the C-terminal half of MID1 may contribute to the polyubiquitination of PP2Ac. We observed that PP2Ac was ubiquitinated in the presence of UbcH5a-c and UbcH6, similar to results obtained with MID1-catalyzed ubiquitination of alpha4 (Figure 2E)
Publications: 1 Organism: In Vitro
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