UniProt functional annotation for O14929



	UniProt functional annotation for O14929

UniProt code: O14929.

Organism: Homo sapiens (Human).

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

Function: Histone acetyltransferase that plays a role in different biological processes including cell cycle progression, glucose metabolism, histone production or DNA damage repair (PubMed:31278053, PubMed:20953179, PubMed:23653357, PubMed:32081014). Coordinates histone production and acetylation via H4 promoter binding (PubMed:31278053). Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac) (PubMed:22615379, PubMed:11585814). Drives H4 production by chromatin binding to support chromatin replication and acetylation. Since transcription of H4 genes is tightly coupled to S-phase, plays an important role in S-phase entry and progression (PubMed:31278053). Promotes homologous recombination in DNA repair by facilitating histone turnover and incorporation of acetylated H3.3 at sites of double-strand breaks (PubMed:23653357). In addition, acetylates other substrates such as chromatin-related proteins (PubMed:32081014). Acetylates also RSAD2 which mediates the interaction of ubiquitin ligase UBE4A with RSAD2 leading to RSAD2 ubiquitination and subsequent degradation (PubMed:31812350). {ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:20953179, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:23653357, ECO:0000269|PubMed:31278053, ECO:0000269|PubMed:31812350, ECO:0000269|PubMed:32081014}.

Function: (Microbial infection) Contributes to hepatitis B virus (HBV) replication by acetylating histone H4 at the sites of 'Lys-5' and 'Lys- 12' on the covalently closed circular DNA (cccDNA) minichromosome leading to its accumulation within the host cell. {ECO:0000269|PubMed:31695772}.

Catalytic activity: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:9427644};

Biophysicochemical properties: Kinetic parameters: KM=6.68 uM for acetyl-CoA {ECO:0000269|PubMed:22615379}; Note=kcat is 4.14 (sec-1) for acetyl-CoA. {ECO:0000269|PubMed:22615379};

Subunit: Catalytic subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4 and H2A. The interaction is dependent of the ability of RBBP7 to bind to the N-terminus of histones. Component of the histone H3.1 and H3.3 complexes. {ECO:0000269|PubMed:20953179, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:9427644}.

Subcellular location: [Isoform A]: Nucleus matrix {ECO:0000269|PubMed:20148353, ECO:0000269|PubMed:23653357}. Mitochondrion {ECO:0000269|PubMed:32081014}.

Subcellular location: [Isoform B]: Cytoplasm {ECO:0000269|PubMed:20148353}. Nucleus {ECO:0000269|PubMed:20148353}. Nucleus matrix {ECO:0000269|PubMed:20148353}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20148353}. Note=Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein. {ECO:0000269|PubMed:20148353}.

Developmental stage: Highly expressed in mitotic cells (at protein level). {ECO:0000269|PubMed:20148353}.

Induction: By viruses and interferons (PubMed:31812350). Up-regulated also by estrogen (PubMed:12841681). {ECO:0000269|PubMed:12841681, ECO:0000269|PubMed:31812350}.

Ptm: Phosphorylated by AMPK at Ser-190; phosphorylation increases HAT1 activity. {ECO:0000269|PubMed:28143904}.

Similarity: Belongs to the HAT1 family. {ECO:0000305}.

Sequence caution: Sequence=AAH18682.1; 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:		Histone acetyltransferase that plays a role in different biological processes including cell cycle progression, glucose metabolism, histone production or DNA damage repair (PubMed:31278053, PubMed:20953179, PubMed:23653357, PubMed:32081014). Coordinates histone production and acetylation via H4 promoter binding (PubMed:31278053). Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac) (PubMed:22615379, PubMed:11585814). Drives H4 production by chromatin binding to support chromatin replication and acetylation. Since transcription of H4 genes is tightly coupled to S-phase, plays an important role in S-phase entry and progression (PubMed:31278053). Promotes homologous recombination in DNA repair by facilitating histone turnover and incorporation of acetylated H3.3 at sites of double-strand breaks (PubMed:23653357). In addition, acetylates other substrates such as chromatin-related proteins (PubMed:32081014). Acetylates also RSAD2 which mediates the interaction of ubiquitin ligase UBE4A with RSAD2 leading to RSAD2 ubiquitination and subsequent degradation (PubMed:31812350). {ECO:0000269\|PubMed:11585814, ECO:0000269\|PubMed:20953179, ECO:0000269\|PubMed:22615379, ECO:0000269\|PubMed:23653357, ECO:0000269\|PubMed:31278053, ECO:0000269\|PubMed:31812350, ECO:0000269\|PubMed:32081014}.



Function:		(Microbial infection) Contributes to hepatitis B virus (HBV) replication by acetylating histone H4 at the sites of 'Lys-5' and 'Lys- 12' on the covalently closed circular DNA (cccDNA) minichromosome leading to its accumulation within the host cell. {ECO:0000269\|PubMed:31695772}.


Catalytic activity:		Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269\|PubMed:11585814, ECO:0000269\|PubMed:22615379, ECO:0000269\|PubMed:9427644};
Biophysicochemical properties:		Kinetic parameters: KM=6.68 uM for acetyl-CoA {ECO:0000269\|PubMed:22615379}; Note=kcat is 4.14 (sec-1) for acetyl-CoA. {ECO:0000269\|PubMed:22615379};
Subunit:		Catalytic subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4 and H2A. The interaction is dependent of the ability of RBBP7 to bind to the N-terminus of histones. Component of the histone H3.1 and H3.3 complexes. {ECO:0000269\|PubMed:20953179, ECO:0000269\|PubMed:22615379, ECO:0000269\|PubMed:9427644}.
Subcellular location:		[Isoform A]: Nucleus matrix {ECO:0000269\|PubMed:20148353, ECO:0000269\|PubMed:23653357}. Mitochondrion {ECO:0000269\|PubMed:32081014}.
Subcellular location:		[Isoform B]: Cytoplasm {ECO:0000269\|PubMed:20148353}. Nucleus {ECO:0000269\|PubMed:20148353}. Nucleus matrix {ECO:0000269\|PubMed:20148353}. Nucleus, nucleoplasm {ECO:0000269\|PubMed:20148353}. Note=Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein. {ECO:0000269\|PubMed:20148353}.
Developmental stage:		Highly expressed in mitotic cells (at protein level). {ECO:0000269\|PubMed:20148353}.
Induction:		By viruses and interferons (PubMed:31812350). Up-regulated also by estrogen (PubMed:12841681). {ECO:0000269\|PubMed:12841681, ECO:0000269\|PubMed:31812350}.
Ptm:		Phosphorylated by AMPK at Ser-190; phosphorylation increases HAT1 activity. {ECO:0000269\|PubMed:28143904}.
Similarity:		Belongs to the HAT1 family. {ECO:0000305}.
Sequence caution:		Sequence=AAH18682.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};