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Involved in both DNA replication and cell cycle control (PubMed:27906959). Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner (PubMed:27906959). Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression (PubMed:27906959). [UniProt]
C1orf55; dJ671D7.1; FLJ35382; protein SDE2 homolog; Replication stress response regulator SDE2; RGD1305572; SDE2; SDE2 telomere maintenance homolog; SDE2 telomere maintenance homolog (S. pombe); UPF0667 protein C1orf55; UPF0667 protein C1orf55 homolog
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