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ASF1A encodes a member of the H3/H4 family of histone chaperone proteins and is similar to the anti-silencing function-1 gene in yeast. Additionally we are shipping ASF1A Antibodies (123) and many more products for this protein.
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ASF1a promotes non-homologous end joining repair by facilitating phosphorylation of MDC1 by ATM (show ATM Proteins) at double-strand breaks.
These data suggest that CAF-1 (show CHAF1B Proteins)- and ASF1A-H3-H4-dependent deposition of the histone (H3 (show HIST3H3 Proteins)-H4)2 tetramers is compatible with MMR (show MRC1 Proteins) and protects the discontinuous daughter strand from unnecessary degradation by MMR (show MRC1 Proteins) machinery.
Data show that the ubiquitin-conjugating enzyme E2 RAD6A/B-MDM2 ubiquitin ligase machinery regulates anti-silencing function 1A protein (ASF1A) degradation.
quaternary complex of histone H3 (show HIST3H3 Proteins)-H4 heterodimer with chaperone ASF1 (show SRSF1 Proteins) and the replicative helicase subunit MCM2 (show MCM2 Proteins)
Thermodynamic analysis of the quaternary complex together with structural modeling support that ASF1 (show SRSF1 Proteins) and MCM2 (show MCM2 Proteins) could form a chaperoning module for histones H3 and H4 protecting them from promiscuous interactions.
Data indicate Tousled-like kinases (TLK1 (show TLK1 Proteins)) phosphorylation has an impact on cell cycle proteins Asf1a and Asf1b (show ASF1B Proteins) function.
findings show that ASF1A, a histone-remodeling chaperone specifically enriched in the metaphase II oocyte, is necessary for reprogramming of adult dermal fibroblasts into undifferentiated induced pluripotent stem cell
The ATR (show ANTXR1 Proteins) checkpoint pathway causes a histone chaperone normally associated with the replication fork, ASF1a, to degrade through a CRL1 (show IL27RA Proteins)(betaTRCP (show BTRC Proteins))-dependent ubiquitination/proteasome pathway, leading to the localized dechromatinization and gene repression.
Co-depletion of the histone chaperones ASF1a and ASF1b (show ASF1B Proteins) in human cells induces all hallmarks of alternative lengthening of telomeres in both primary and cancer cells.
Asf1a plays a role in regulating IE genes by assembling chromatin onto histone-free viral DNA by 3 h postinfection with herpes simplex virus 1
tousled-like kinases play important roles in DNA repair, not only by modulation of chromatin assembly via Asf1, but also by a more direct function in processing the ends of a tousled-like kinase via interaction with Rad9 (show RAD9A Proteins).
This gene encodes a member of the H3/H4 family of histone chaperone proteins and is similar to the anti-silencing function-1 gene in yeast. The protein is a key component of a histone donor complex that functions in nucleosome assembly. It interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair.
histone chaperone ASF1A
, histone chaperone ASF1A-like
, anti-silencing function 1
, anti-silencing function protein 1 homolog
, histone chaperone ASF1
, ASF1 anti-silencing function 1 homolog A
, ASF1 anti-silencing function 1-like protein A
, CCG1-interacting factor A
, anti-silencing function protein 1 homolog A