Aliases for DTL Gene
- Denticleless E3 Ubiquitin Protein Ligase Homolog 2 3
- Denticleless E3 Ubiquitin Protein Ligase Homolog (Drosophila) 2 5
- Retinoic Acid-Regulated Nuclear Matrix-Associated Protein 3 4
- RA Regulated Nuclear Matrix Associated Protein 2 3
- Lethal(2) Denticleless Protein Homolog 3 4
- DDB1- And CUL4-Associated Factor 2 3 4
- DDB1 And CUL4 Associated Factor 2 2 3
- DCAF2 3 4
External Ids for DTL Gene
Previous GeneCards Identifiers for DTL Gene
GeneCards Summary for DTL Gene
DTL (Denticleless E3 Ubiquitin Protein Ligase Homolog) is a Protein Coding gene. Among its related pathways are DNA Double-Strand Break Repair and Translesion synthesis by Y family DNA polymerases bypasses lesions on DNA template. GO annotations related to this gene include ubiquitin-protein transferase activity.
UniProtKB/Swiss-Prot for DTL Gene
Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBXO18/FBH1 and KMT5A (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the K+4 motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the Lys-164 monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613).