The PWWP domain is found in the BR140 family, which includes peregrine (also known as protein BR140 or Brpf1) and BR140-like proteins 1 and 2 (Bromodomain and PHD finger-containing proteins 2 and 3). BR140 is the only family to contain the PWWP domain at the C terminus, with PHD and bromo domains in the N-terminal region. Brpf1 is part of the MOZ/MORF complex which has a histone H3 acetyltransferase activity [, ]. The PWWP domain of Brpf1 has been shown to bind H3K36me3 [].The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids. The PWWP domain is found in numerous proteins that are involved in cell division, growth and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding proteins, that function as transcription factors regulating a variety of developmental processes [].
This entry represents the ePHD finger of Peregrin (also known as BRPF1), which is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ) -dependent histone acetylation, and is required for Hox gene expression and segmental identity []. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development [, ]. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia. It contains a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. This PHD finger binds to methylated lysine 4 of histone H3 (H3K4me), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His [, ].
This entry represents the PHD finger of BRPF1. BRPF1, also termed peregrin, or protein Br140, is a multi-domain protein that binds histones, mediates monocytic leukemic zinc-finger protein (MOZ) -dependent histone acetylation, and is required for Hox gene expression and segmental identity []. It is a close partner of the MOZ histone acetyltransferase (HAT) complex and a novel Trithorax group (TrxG) member with a central role during development [, ]. BRPF1 is primarily a nuclear protein that has a broad tissue distribution and is abundant in testes and spermatogonia []. It contains a plant homeodomain (PHD) zinc finger followed by a non-canonical ePHD finger, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. PHD and ePHD fingers both bind to lysine 4 of histone H3 (K4H3), bromodomains interact with acetylated lysines on N-terminal tails of histones and other proteins, and PWWP domains show histone-binding and chromatin association properties. BRPF1 may be involved in chromatin remodeling [, ].
This entry represents the ePHD finger of BRPF3. BRF3 is a homologue of BRPF1 and BRPF2. The extended plant homeodomain (ePHD) zinc finger is characterized as Cys2HisCys5HisCys2His. BRPF3 is a scaffold protein that forms a novel monocytic leukemic zinc finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complex with other regulatory subunits []. BRPF3 contains a plant homeodomain (PHD) finger followed by this non-canonical ePHD finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain [].
