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Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure.. Additionally we are shipping and many more products for this protein.
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Studies identi fi ed a novel signal of nuclear localization (NLS) in all MSL1 protein isoforms and found that the combination of both NLS allows for its intra-nuclear focal accumulation and nuclear transport of TTC4 while all MSL1 isoforms affect H4K16Ac.
The MSL1 bound to Nupr1, with a moderate affinity (2.8 microM) in an entropically-driven process. MSL1 did not bind to non-damaged DNA, but it bound to chemically-damaged-DNA with a moderate affinity (1.2 microM) also in an entropically-driven process.
MSL1 (show SNRPB2 Antibodies) plays an important role in mediating irradiation-induced DNA repair through formation of HAT (show MGEA5 Antibodies) complexes and interaction with 53BP1 (show TP53BP1 Antibodies). P8 acts as a negative regulator of this process by interacting with MSL1 (show SNRPB2 Antibodies) and preventing its role on HAT (show MGEA5 Antibodies) activity.
A multisubunit human histone acetylase complex that contains homologs of the Drosophila MSL proteins MOF (show KAT8 Antibodies), MSL1 (hampin A), MSL2 (show MSL2 Antibodies), and MSL3 (show MSL3 Antibodies) was described. This complex is responsible for histone H4 lysine-16 acetylation of all cellular chromosomes.
Msl1 interacts with Msl3 as an extended chain forming an extensive hydrophobic interface, whereas the Msl1-MOF interface involves electrostatic interactions between the HAT domain and a long helix of Msl1.
hampin may be linked to diverse regulatory processes in the nucleus
Describes the primary structure of the protein hampin, which shares about 26% sequence identity with the Drosophila MSL1 protein. In mouse, at least five splice isoforms exist, two of which have restricted tissue specificity (testes).
Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure.
, male-specific lethal 1 homolog
, male-specific lethal 1-like 1
, male-specific lethal-1 homolog 1