| Structural highlights
Function
DTX3L_HUMAN Ubiquitin ligase that mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1), in response to DNA damage. Protects cells exposed to DNA-damaging agents. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 'Lys-20' methylation (H4K20me). Involved in the recruitment of 53BP1/TP53BP1 to sites of DNA damage by mediating H4K91ub1 formation. In concert with PARP9, plays a role in PARP1-dependent DNA damage repair. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites.[1] [2] [3]
See Also
References
- ↑ Takeyama K, Aguiar RC, Gu L, He C, Freeman GJ, Kutok JL, Aster JC, Shipp MA. The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity. J Biol Chem. 2003 Jun 13;278(24):21930-7. Epub 2003 Apr 1. PMID:12670957 doi:https://dx.doi.org/10.1074/jbc.M301157200
- ↑ Yan Q, Dutt S, Xu R, Graves K, Juszczynski P, Manis JP, Shipp MA. BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response. Mol Cell. 2009 Oct 9;36(1):110-20. doi: 10.1016/j.molcel.2009.08.019. PMID:19818714 doi:https://dx.doi.org/10.1016/j.molcel.2009.08.019
- ↑ Yan Q, Xu R, Zhu L, Cheng X, Wang Z, Manis J, Shipp MA. BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8. Mol Cell Biol. 2013 Feb;33(4):845-57. doi: 10.1128/MCB.00990-12. Epub 2012 Dec, 10. PMID:23230272 doi:https://dx.doi.org/10.1128/MCB.00990-12
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