IndraLab

Statements


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"USP16 interacts with HERC2 and modulates the ubiquitination in DNA repair machinery components."

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"Here we report that the histone H2A deubiquitinase USP16 interacts with HERC2, fine-tunes the ubiquitin signal during repair, and importantly, is required for terminating the ubiquitination signal after repair."

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"Here we report that the histone H2A deubiquitinase USP16 interacts with HERC2, fine-tunes the ubiquitin signal during repair, and importantly, is required for terminating the ubiquitination signal after repair."

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"This mechanism may explain the evolution of the USP16-HERC2 interaction ( xref , xref , xref online): the USP16 coil-coiled interaction domain at ∼200 a."

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"HERC2 interacts with the coiled-coil domain of USP16 through its C-terminal HECT domain."

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"Furthermore, HERC2 interacts with the disordered region of USP16 (residues 136–185) through its C-terminal HECT domain (residues 4421–4834), increasing the intracellular expression of USP16 [ xref ]."

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"The histone H2A deubiquitinase USP16 interacts with HERC2 and fine-tunes cellular response to DNA damage."

sparser
"USP16 interacts with HERC2 and modulates the ubiquitination in DNA repair machinery components ( xref )."