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http://purl.uniprot.org/citations/15200950http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15200950http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15200950http://www.w3.org/2000/01/rdf-schema#comment"The abundant chromatin-associated human factor HCF-1 is a heterodimeric complex of HCF-1N and HCF-1C subunits that are essential for two stages of the cell cycle. The HCF-1N subunit promotes G1 phase progression, whereas the HCF-1C subunit ensures proper cytokinesis at completion of M phase. How the HCF-1C subunit functions is unknown. Here, we show that HCF-1C subunit depletion causes extensive mitotic defects, including a switch from monomethyl to dimethyl lysine 20 of histone H4 (H4-K20) and defective chromosome alignment and segregation. Consistent with these activities, the HCF-1C subunit can associate with chromatin independently of the HCF-1N subunit and regulates the expression of the H4-K20 methyltransferase PR-Set7. Indeed, upregulation of PR-Set7 expression upon loss of HCF-1 leads to improper mitotic H4-K20 methylation and cytokinesis defects. These results establish the HCF-1C subunit as an important M phase regulator and suggest that H4-K20 methylation status contributes to chromosome behavior during mitosis and proper cytokinesis."xsd:string
http://purl.uniprot.org/citations/15200950http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2004.06.008"xsd:string
http://purl.uniprot.org/citations/15200950http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2004.06.008"xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/author"Herr W."xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/author"Herr W."xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/author"Julien E."xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/author"Julien E."xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/pages"713-725"xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/pages"713-725"xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/title"A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1."xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/title"A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1."xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/15200950http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/15200950http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15200950
http://purl.uniprot.org/citations/15200950http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15200950
http://purl.uniprot.org/citations/15200950http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15200950
http://purl.uniprot.org/citations/15200950http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15200950
http://purl.uniprot.org/uniprot/Q9NQR1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15200950
http://purl.uniprot.org/uniprot/Q9NQR1#attribution-D58DF8638FB23421A7D331DAEC8034E7http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15200950