Gene: MSL3
Alternate names for this Gene: MRSXBA|MRXS36|MRXSBA|MSL3L1
Gene Summary: This gene encodes a nuclear protein that is similar to the product of the Drosophila male-specific lethal-3 gene. The Drosophila protein plays a critical role in a dosage-compensation pathway, which equalizes X-linked gene expression in males and females. Thus, the human protein is thought to play a similar function in chromatin remodeling and transcriptional regulation, and it has been found as part of a complex that is responsible for histone H4 lysine-16 acetylation. This gene can undergo X inactivation. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 2, 7 and 8.
Gene is located in Chromosome: X
Location in Chromosome : Xp22.2
Description of this Gene: MSL complex subunit 3
Type of Gene: protein-coding
rs1555907215 in
MSL3 gene and
Dysmorphic features
PMID 25900149 2015 The MSL complex: juggling RNA-protein interactions for dosage compensation and beyond.
PMID 15988010 2005 The MRG domain mediates the functional integration of MSL3 into the dosage compensation complex.
PMID 24898753 2014 Mof-associated complexes have overlapping and unique roles in regulating pluripotency in embryonic stem cells and during differentiation.
PMID 28135719 2017 Prevalence and architecture of de novo mutations in developmental disorders.
PMID 20657587 2010 Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.
PMID 20943666 2010 Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4.
PMID 16227571 2005 A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16.
rs1555907215 in
MSL3 gene and
Muscle hypotonia
PMID 16227571 2005 A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16.
PMID 20943666 2010 Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4.
PMID 25900149 2015 The MSL complex: juggling RNA-protein interactions for dosage compensation and beyond.
PMID 24898753 2014 Mof-associated complexes have overlapping and unique roles in regulating pluripotency in embryonic stem cells and during differentiation.
PMID 28135719 2017 Prevalence and architecture of de novo mutations in developmental disorders.
PMID 20657587 2010 Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.
PMID 15988010 2005 The MRG domain mediates the functional integration of MSL3 into the dosage compensation complex.