Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis.
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The H3.1 deposition machinery is the CAF-1 histone chaperone, which mediates DNA-synthesis-dependent (replication-coupled) nucleosome assembly.
"The H3.1 and H3.3 complexes contain distinct histone chaperones, CAF-1 and HIRA, that we show are necessary to mediate DNA-synthesis-dependent and -independent nucleosome assembly, respectively."
Cell array-based intracellular localization screening reveals novel functional features of human chromosome 21 proteins.
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CHAF1B is nuclear at interphase (chromatin assembly / DNA replication) and translocates to the cytoplasm during cell division.
"The chromatin assembly factor I p60 subunit (CHAF1B) protein translocated from the nucleus into the cytoplasm during cell division."
Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly.
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CAF-1 p60 (CHAF1B) uses B-domain-like motifs to bind ASF1a, competing with HIRA for the same surface.
"CAF-1 p60 also uses B domain-like motifs for binding to ASF1a, thereby competing with HIRA."
Human-chromatin-related protein interactions identify a demethylase complex required for chromosome segregation.
A High-Density Map for Navigating the Human Polycomb Complexome.
Architecture of the human interactome defines protein communities and disease networks.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Multimodal cell maps as a foundation for structural and functional genomics.
The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication.
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p150 and p60 directly interact and are both required for replication-dependent nucleosome assembly; they form complexes with newly synthesized H3 and acetylated H4.
"p150 and p60 directly interact and are both required for DNA replication-dependent assembly of nucleosomes."
Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4.
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The chromatin assembly complex contains the three CAF-1 subunits (p150, p60, p48) plus H3 and H4 and promotes DNA replication-dependent chromatin assembly.
"a chromatin assembly complex (CAC), which contains the three subunits of CAF-1 (p150, p60, p48) and H3 and H4, and promotes DNA replication-dependent chromatin assembly."
Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle.
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All three CAF-1 subunits (p150, p60, p48) are present through the cell cycle; p150/p60 are nuclear and concentrate at replication sites in S phase, and p60 is hyperphosphorylated and inactive in mitosis.
"In interphase, p150 and p60 are bound to the nucleus, but they predominantly dissociate from chromatin during mitosis. During S phase, p150 and p60 are concentrated at sites of intranuclear DNA replication."
UniProt entry Q13112 (CAF1B_HUMAN)
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CHAF1B is a component of the CAF-1 histone chaperone complex (RBBP4, CHAF1B, CHAF1A); CHAF1A binds directly to CHAF1B; interacts with histones H3.1, H3.2, H3.1t.
"Subunit of the CAF-1 complex that contains RBBP4, CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B."
Falcon deep research report for CHAF1B