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.[3]
↑ 4.04.1Silljé HH, Nigg EA (Jul 2001). "Identification of human Asf1 chromatin assembly factors as substrates of Tousled-like kinases". Current Biology. 11 (13): 1068–73. doi:10.1016/S0960-9822(01)00298-6. PMID11470414.
↑Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.
Munakata T, Adachi N, Yokoyama N, Kuzuhara T, Horikoshi M (Mar 2000). "A human homologue of yeast anti-silencing factor has histone chaperone activity". Genes to Cells. 5 (3): 221–33. doi:10.1046/j.1365-2443.2000.00319.x. PMID10759893.
Silljé HH, Nigg EA (Jul 2001). "Identification of human Asf1 chromatin assembly factors as substrates of Tousled-like kinases". Current Biology. 11 (13): 1068–73. doi:10.1016/S0960-9822(01)00298-6. PMID11470414.
Agez M, Chen J, Guerois R, van Heijenoort C, Thuret JY, Mann C, Ochsenbein F (Feb 2007). "Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights". Structure. 15 (2): 191–9. doi:10.1016/j.str.2007.01.002. PMID17292837.
Natsume R, Eitoku M, Akai Y, Sano N, Horikoshi M, Senda T (Mar 2007). "Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4". Nature. 446 (7133): 338–41. doi:10.1038/nature05613. PMID17293877.