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Literature summary for 2.3.2.27 extracted from

  • Jung, Y.; Liu, G.; Chen, X.
    Pirh2 E3 ubiquitin ligase targets DNA polymerase eta for 20S proteasomal degradation (2010), Mol. Cell. Biol., 30, 1041-1048.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens Q96PM5 isoform PirH2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[PirH2-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [PolH]-L-lysine PolH, DNA polymerase eta, a Y family translesion polymerase and a target of the p53 tumor suppressor. PolH interacts with Pirh2 E3 ligase, via the polymerase-associated domain in PolH and the RING finger domain in Pirh2. PolH is recruited by Pirh2 and degraded by 20S proteasome in a ubiquitin-independent manner Homo sapiens [PirH2-ubiquitin-carrier protein]-L-cysteine + [PolH]-N6-ubiquitinyl-L-lysine
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Synonyms

Synonyms Comment Organism
Pirh2
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Homo sapiens

General Information

General Information Comment Organism
physiological function overexpression of E3 ligase Pirh2 decreases DNA polymerase PolH protein stability, whereas knockdown of Pirh2 increases it. Pirh2 knockdown leads to accumulation of PolH and, subsequently, enhances the survival of UV-irradiated cells Homo sapiens