UniProt functional annotation for Q68D10



	UniProt functional annotation for Q68D10

UniProt code: Q68D10.

Organism: Homo sapiens (Human).

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

Function: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin (PubMed:26109053). Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription (PubMed:26109053). Binds DNA and histones and promotes nucleosome assembly (in vitro) (PubMed:23378026, PubMed:26109053). Facilitates formation of tetrameric histone complexes containing histone H3 and H4 (PubMed:26109053). Modulates RNA polymerase 1-mediated transcription (By similarity). Binds DNA, with a preference for branched DNA species, such as Y-form DNA and Holliday junction DNA (PubMed:23378026). {ECO:0000250|UniProtKB:E1BUG7, ECO:0000269|PubMed:23378026}.

Subunit: Interacts with histones (PubMed:23378026). Interacts with a heterotetrameric complex formed by histone H3 and H4, especially when the histone tetramer is not bound to DNA (PubMed:26109053). {ECO:0000269|PubMed:23378026, ECO:0000269|PubMed:26109053}.

Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:E1BUG7}.

Domain: The acidic C-terminal domain mediates interaction with histone H3/H4 complexes. {ECO:0000269|PubMed:23378026, ECO:0000269|PubMed:26109053}.

Miscellaneous: The histone binding domain can functionally complement the yeast ortholog in regulating histone exchange and suppression of spurious transcription. {ECO:0000269|PubMed:26109053}.

Similarity: Belongs to the SPT2 family. {ECO:0000305}.

Sequence caution: Sequence=AAP13351.1; Type=Erroneous initiation; Note=Extended 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 chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin (PubMed:26109053). Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription (PubMed:26109053). Binds DNA and histones and promotes nucleosome assembly (in vitro) (PubMed:23378026, PubMed:26109053). Facilitates formation of tetrameric histone complexes containing histone H3 and H4 (PubMed:26109053). Modulates RNA polymerase 1-mediated transcription (By similarity). Binds DNA, with a preference for branched DNA species, such as Y-form DNA and Holliday junction DNA (PubMed:23378026). {ECO:0000250\|UniProtKB:E1BUG7, ECO:0000269\|PubMed:23378026}.


Subunit:		Interacts with histones (PubMed:23378026). Interacts with a heterotetrameric complex formed by histone H3 and H4, especially when the histone tetramer is not bound to DNA (PubMed:26109053). {ECO:0000269\|PubMed:23378026, ECO:0000269\|PubMed:26109053}.
Subcellular location:		Nucleus, nucleolus {ECO:0000250\|UniProtKB:E1BUG7}.
Domain:		The acidic C-terminal domain mediates interaction with histone H3/H4 complexes. {ECO:0000269\|PubMed:23378026, ECO:0000269\|PubMed:26109053}.
Miscellaneous:		The histone binding domain can functionally complement the yeast ortholog in regulating histone exchange and suppression of spurious transcription. {ECO:0000269\|PubMed:26109053}.
Similarity:		Belongs to the SPT2 family. {ECO:0000305}.
Sequence caution:		Sequence=AAP13351.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};