UniProt functional annotation for Q9UKL0



	UniProt functional annotation for Q9UKL0

UniProt code: Q9UKL0.

Organism: Homo sapiens (Human).

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

Function: Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. {ECO:0000269|PubMed:11171972, ECO:0000269|PubMed:11516394, ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:12399542, ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16140033}.

Subunit: Interacts directly with GFI1 and GFI1B in a RCOR/GFI/KDM1A/HDAC complex. Interacts with INMS1 (By similarity). Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with REST. Interacts with the SMARCE1/BAF57, suggesting that the BHC complex may recruit the ATP-dependent chromatin-remodeling SWI- SNF complex. {ECO:0000250, ECO:0000269|PubMed:10449787, ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:11171972, ECO:0000269|PubMed:11516394, ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:12192000, ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16140033, ECO:0000269|PubMed:16885027}.

Subunit: (Microbial infection) Interacts with herpes virus HSV-1 ICP0 protein; the interaction leads to the disruption of the BHC complex, thereby preventing the BHC complex from repressing transcription of viral genes. {ECO:0000269|PubMed:15897453}.

Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:15897453}. Note=Upon infection by HSV-1, it is partially translocated into the cytoplasm in an HSV-1-dependent manner.

Tissue specificity: Ubiquitously expressed. {ECO:0000269|PubMed:10449787}.

Domain: The SANT domains may bridge the nucleosomal substrates and the demethylase KDM1A. {ECO:0000269|PubMed:16140033}.

Ptm: Phosphorylated by HSV-1 protein kinases in case of infection. {ECO:0000269|PubMed:15897453}.

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

Sequence caution: Sequence=AAH51003.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAH64495.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAH64495.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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:		Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. {ECO:0000269\|PubMed:11171972, ECO:0000269\|PubMed:11516394, ECO:0000269\|PubMed:12032298, ECO:0000269\|PubMed:12399542, ECO:0000269\|PubMed:12493763, ECO:0000269\|PubMed:16079794, ECO:0000269\|PubMed:16140033}.


Subunit:		Interacts directly with GFI1 and GFI1B in a RCOR/GFI/KDM1A/HDAC complex. Interacts with INMS1 (By similarity). Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with REST. Interacts with the SMARCE1/BAF57, suggesting that the BHC complex may recruit the ATP-dependent chromatin-remodeling SWI- SNF complex. {ECO:0000250, ECO:0000269\|PubMed:10449787, ECO:0000269\|PubMed:10734093, ECO:0000269\|PubMed:11102443, ECO:0000269\|PubMed:11171972, ECO:0000269\|PubMed:11516394, ECO:0000269\|PubMed:12032298, ECO:0000269\|PubMed:12192000, ECO:0000269\|PubMed:12493763, ECO:0000269\|PubMed:16079794, ECO:0000269\|PubMed:16140033, ECO:0000269\|PubMed:16885027}.
Subunit:		(Microbial infection) Interacts with herpes virus HSV-1 ICP0 protein; the interaction leads to the disruption of the BHC complex, thereby preventing the BHC complex from repressing transcription of viral genes. {ECO:0000269\|PubMed:15897453}.
Subcellular location:		Nucleus {ECO:0000255\|PROSITE-ProRule:PRU00512, ECO:0000255\|PROSITE-ProRule:PRU00624, ECO:0000269\|PubMed:10734093, ECO:0000269\|PubMed:15897453}. Note=Upon infection by HSV-1, it is partially translocated into the cytoplasm in an HSV-1-dependent manner.
Tissue specificity:		Ubiquitously expressed. {ECO:0000269\|PubMed:10449787}.
Domain:		The SANT domains may bridge the nucleosomal substrates and the demethylase KDM1A. {ECO:0000269\|PubMed:16140033}.
Ptm:		Phosphorylated by HSV-1 protein kinases in case of infection. {ECO:0000269\|PubMed:15897453}.
Similarity:		Belongs to the CoREST family. {ECO:0000305}.
Sequence caution:		Sequence=AAH51003.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAH64495.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAH64495.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};