UniProt functional annotation for Q9H8M2



	UniProt functional annotation for Q9H8M2

UniProt code: Q9H8M2.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Plays a role in chromatin remodeling and regulation of transcription (PubMed:22464331, PubMed:26365797). Acts as a chromatin reader that recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated (PubMed:26365797). Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA- histone contacts within a nucleosome in an ATP-dependent manner (PubMed:29374058). Orchestrates also the RAD51-RAD54 complex formation and thereby plays a role in homologous recombination (HR) (PubMed:32457312). {ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:26365797, ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:32457312}.

Subunit: Binds acetylated histones H3 and H4 (PubMed:22464331, PubMed:26365797). Binds butyrylated histone H4 (PubMed:26365797). Component of the multiprotein chromatin-remodeling subcomplex SWI/SNF called GBAF, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). Interacts (via N-terminal bromodomain) with acteylated RAD54 (PubMed:32457312). Interacts (via C-terminus) with RAD51 (PubMed:32457312). {ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:26365797, ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:32457312}.

Domain: The Bromo domain mediates interaction with histones that have acetylated lysine residues at specific positions (PubMed:22464331). Also recognizes and binds histones that are butyrylated (PubMed:26365797). {ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:26365797}.

Miscellaneous: [Isoform 5]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}.

Sequence caution: Sequence=BAB15565.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Plays a role in chromatin remodeling and regulation of transcription (PubMed:22464331, PubMed:26365797). Acts as a chromatin reader that recognizes and binds acylated histones: binds histones that are acetylated and/or butyrylated (PubMed:26365797). Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA- histone contacts within a nucleosome in an ATP-dependent manner (PubMed:29374058). Orchestrates also the RAD51-RAD54 complex formation and thereby plays a role in homologous recombination (HR) (PubMed:32457312). {ECO:0000269\|PubMed:22464331, ECO:0000269\|PubMed:26365797, ECO:0000269\|PubMed:29374058, ECO:0000269\|PubMed:32457312}.


Subunit:		Binds acetylated histones H3 and H4 (PubMed:22464331, PubMed:26365797). Binds butyrylated histone H4 (PubMed:26365797). Component of the multiprotein chromatin-remodeling subcomplex SWI/SNF called GBAF, which includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). Interacts (via N-terminal bromodomain) with acteylated RAD54 (PubMed:32457312). Interacts (via C-terminus) with RAD51 (PubMed:32457312). {ECO:0000269\|PubMed:22464331, ECO:0000269\|PubMed:26365797, ECO:0000269\|PubMed:29374058, ECO:0000269\|PubMed:32457312}.
Domain:		The Bromo domain mediates interaction with histones that have acetylated lysine residues at specific positions (PubMed:22464331). Also recognizes and binds histones that are butyrylated (PubMed:26365797). {ECO:0000269\|PubMed:22464331, ECO:0000269\|PubMed:26365797}.
Miscellaneous:		[Isoform 5]: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}.
Sequence caution:		Sequence=BAB15565.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};