UniProt functional annotation for Q8R5C8



	UniProt functional annotation for Q8R5C8

UniProt code: Q8R5C8.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Chromatin reader that specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 or H3.2). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage (PubMed:24590075). Binds non-specifically to dsDNA (By similarity). Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth (PubMed:24590075). {ECO:0000250|UniProtKB:Q15326, ECO:0000269|PubMed:24590075}.

Subunit: Homooligomer; forms homooligomers via its C-terminus. Interacts with histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3). Interacts (via MYND-type zinc finger) with NCOR1. Interacts (via MYND- type zinc finger) with MGA protein (via PXLXP motif). Interacts (via MYND-type zinc finger) with EZH2. Interacts with EMSY and E2F6. Interacts with PIAS1 and UBE2I (By similarity). {ECO:0000250|UniProtKB:Q15326}.

Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15326}. Chromosome {ECO:0000250|UniProtKB:Q15326}. Note=Associates with chromatin and mitotic chromosomes. {ECO:0000250|UniProtKB:Q15326}.

Domain: The PWWP domain specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and adopts a five-bladed beta- barrel fold with an extended C-terminal alpha-helix, with a conserved H3.3K36me3-binding aromatic cage formed by Phe-291 and Trp-294 of the beta1-beta2 loop and Phe-310 of the beta3-beta4 loop. Specific recognition of H3.3 histone is mediated by the encapsulation of the H3.3-specific 'Ser 31' residue in a composite pocket formed by the tandem bromo-PWWP domains (PubMed:24590075). {ECO:0000269|PubMed:24590075}.

Ptm: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q15326}.

Ptm: Sumoylated following its interaction with PIAS1 and UBE2I. {ECO:0000250|UniProtKB:Q15326}.

Sequence caution: Sequence=AAH22945.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Chromatin reader that specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 or H3.2). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage (PubMed:24590075). Binds non-specifically to dsDNA (By similarity). Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth (PubMed:24590075). {ECO:0000250\|UniProtKB:Q15326, ECO:0000269\|PubMed:24590075}.


Subunit:		Homooligomer; forms homooligomers via its C-terminus. Interacts with histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3). Interacts (via MYND-type zinc finger) with NCOR1. Interacts (via MYND- type zinc finger) with MGA protein (via PXLXP motif). Interacts (via MYND-type zinc finger) with EZH2. Interacts with EMSY and E2F6. Interacts with PIAS1 and UBE2I (By similarity). {ECO:0000250\|UniProtKB:Q15326}.
Subcellular location:		Nucleus {ECO:0000250\|UniProtKB:Q15326}. Chromosome {ECO:0000250\|UniProtKB:Q15326}. Note=Associates with chromatin and mitotic chromosomes. {ECO:0000250\|UniProtKB:Q15326}.
Domain:		The PWWP domain specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and adopts a five-bladed beta- barrel fold with an extended C-terminal alpha-helix, with a conserved H3.3K36me3-binding aromatic cage formed by Phe-291 and Trp-294 of the beta1-beta2 loop and Phe-310 of the beta3-beta4 loop. Specific recognition of H3.3 histone is mediated by the encapsulation of the H3.3-specific 'Ser 31' residue in a composite pocket formed by the tandem bromo-PWWP domains (PubMed:24590075). {ECO:0000269\|PubMed:24590075}.
Ptm:		Ubiquitinated, leading to proteasomal degradation. {ECO:0000250\|UniProtKB:Q15326}.
Ptm:		Sumoylated following its interaction with PIAS1 and UBE2I. {ECO:0000250\|UniProtKB:Q15326}.
Sequence caution:		Sequence=AAH22945.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};