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The study reports the crystal structure of the H2A.Z-binding domain of Drosophila melanogaster YL1 (dYL1-Z) in complex with an H2A.Z-H2B dimer at 1.9-A resolution.
The 2.7-A-resolution crystal structure of the human YL1-H2A.Z (show H2AFZ ELISA Kits)-H2B complex shows that YL1 binding, similarly to ANP32E (show ANP32E ELISA Kits) binding, triggers an extension of the H2A.Z (show H2AFZ ELISA Kits) alphaC helix.
Results identify YL1 as a subunit of the TRRAP/TIP60 HAT complex, and also as a component of a novel mammalian multiprotein complex that includes the SNF2-related helicase SRCAP.
The protein encoded by this gene is a shared subunit of two multi-component complexes, the histone acetyltransferase complex TRRAP/TIP60 as well as the chromatin remodeling SRCAP-containing complex. The TRRAP/TIP60 complex acetylates nucleosomal histones important for transcriptional regulation, double strand DNA break repair and apoptosis. The SRCAP-containing complex catalyzes the exchange of histone H2A with the histone variant Htz1 (H2AFZ) into nucleosomes. This protein may be responsible for binding H2AFZ, which has a role in chromosome segregation. This protein may also have a role in regulating long-term hematopoietic stem cell activity. Alternative splicing results in multiple transcript variants that encode different protein isoforms.
, vacuolar protein sorting-associated protein 72 homolog
, transcription factor-like 1
, potential vacuolar protein sorting protein
, vacuolar protein sorting 72 homolog (S. cerevisiae)
, protein YL-1
, transformation suppressor gene YL-1