Tissue Specificity | Ubiquitously expressed. |
Post Translational Modifications | Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation. Phosphorylation at Ser-192 by PRKDC in response to DNA damage promotes the histone chaperone activity and ability to replace histones at double-strand breaks (DSBs) at stalled or collapsed replication forks, leading to RAD51 recruitment. |
Function | Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51. Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. |
Protein Name | Histone Chaperone Asf1aAnti-Silencing Function Protein 1 Homolog AHasf1Hasf1aCcg1-Interacting Factor ACiaHcia |
Database Links | Reactome: R-HSA-2559584 |
Cellular Localisation | NucleusChromosome |
Alternative Antibody Names | Anti-Histone Chaperone Asf1a antibodyAnti-Anti-Silencing Function Protein 1 Homolog A antibodyAnti-Hasf1 antibodyAnti-Hasf1a antibodyAnti-Ccg1-Interacting Factor A antibodyAnti-Cia antibodyAnti-Hcia antibodyAnti-ASF1A antibodyAnti-CGI-98 antibodyAnti-HSPC146 antibody |
Information sourced from Uniprot.org