InterPro domain: IPR045081

The ANP32 family members of phosphoproteins are composed of a N-terminal evolutionarily conserved leucine-rich repeat (LRR) domain and a C-terminal variable anionic region. They are multifunctional proteins involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription [ 1 , 2 , 3 , 4 ]. ANP32A is one of the components of the INHAT (INHibitor of AcetylTransferases) complex, which contains the histone chaperone TAF-I (template-activating factor-I), directly binds the core histones, and inhibits the acetylation of the core histones H3 and H4. ANP32B has been shown to interact with the core histones H3–H4 through its acidic concave domain [ 5 ]. ANP32E is an H2A.Z chaperone able specifically to remove H2A.Z from the nucleosome [ 6 ]. It has been shown that ANP32A is an essential host partner coopted to support influenza virus vRNP polymerase activity and contributes to the influenza virus host range. Moreover, ANP32A and ANP32B have been shown to cooperate with CRM1 to support HIV-1 RNA nuclear export [ 7 ].

1. Tumor suppressor pp32 represses cell growth through inhibition of transcription by blocking acetylation and phosphorylation of histone H3 and initiating its proapoptotic activity. Cell Death Differ 13, 1485-94
2. Tumor suppression and potentiation by manipulation of pp32 expression. Oncogene 20, 2153-60
3. PHAPI, CAS, and Hsp70 promote apoptosome formation by preventing Apaf-1 aggregation and enhancing nucleotide exchange on Apaf-1. Mol. Cell 30, 239-47
4. Identification of sequences required for inhibition of oncogene-mediated transformation by pp32. J Biol Chem 274, 20053-5
5. Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain. J Mol Biol 401, 97-114
6. ANP32E is a histone chaperone that removes H2A.Z from chromatin. Nature 505, 648-53
7. ANP32A and ANP32B are key factors in the Rev-dependent CRM1 pathway for nuclear export of HIV-1 unspliced mRNA. J Biol Chem 294, 15346-15357