Peregrin: Difference between revisions

'''Peregrin''', also known as Bromodomain and PHD Finger-containing 1 ('''BRPF1''') is a 137 kDa protein that plays a versatile role in epigenetic signaling events. It contains three chromatin reader domains, including a <scene name='91/910741/Apo_bromodomain/1'>bromodomain</scene>, <scene name='91/910741/Apo_pzp/1'>PZP domain</scene> (two PHD fingers separated by a Zinc Knuckle), and '''proline-tryptophan-tryptophan-proline (<scene name='91/910741/Pwwp_unliganded/1'>PWWP</scene>) domain''' (from N to C terminus)<ref name="Yan">PMID:27939640</ref>. Through these three domains, it is capable of recognizing both modified and unmodified histones, as well as non-specifically binding DNA <ref name="Klein">PMID:31711755</ref>,<ref name="Glass1">PMID:24333487</ref>. BRPF1 carries out its function as a component of the MOZ (monocytic leukemic zinc-finger protein) histone acetyltransferase (HAT) complex <ref name="Obi">PMID:33554132</ref>. This complex is involved in the regulation of gene expression, particularly those involved with skeletal development, hematopoiesis, and neurodevelopmental processes <ref>PMID:19254709</ref>,<ref>PMID:27500495</ref>,<ref name="Klein" />. Accordingly, it has the greatest tissue distribution in the bone marrow and brain.