Acidic leucine-rich nuclear phosphoprotein 32
IPR045081
Definition
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 [[cite:PMID:16341127], [cite:PMID:11360199], [cite:PMID:18439902], [cite:PMID:10400610]]. 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 PMID:20538007. ANP32E is an H2A.Z chaperone able specifically to remove H2A.Z from the nucleosome PMID:24463511. 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 PMID:31444273.
5 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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