| Post Translational Modifications | Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group. Directly cleaved by caspase-3/CASP3. |
| Function | Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription. Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative regulator of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in regulating tissue homeostasis. Exhibits histone chaperone properties, able to recruit histones to certain promoters, thus regulating the transcription of specific genes. Also plays an essential role in the nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1. Participates in the regulation of adequate adaptive immune responses by acting on mRNA expression and cell proliferation. (Microbial infection) Plays an essential role in influenza A and B viral genome replication. Also plays a role in foamy virus mRNA export from the nucleus to the cytoplasm. |
| Protein Name | Acidic Leucine-Rich Nuclear Phosphoprotein 32 Family Member BAcidic Protein Rich In LeucinesPutative Hla-Dr-Associated Protein I-2Phapi2Silver-Stainable Protein Ssp29 |
| Cellular Localisation | Isoform 1: NucleusCytoplasmAccumulates In The Nuclei At The S PhaseIsoform 2: CytoplasmLacks A Nuclear Localization Signal |
| Alternative Protein Names | Acidic Leucine-Rich Nuclear Phosphoprotein 32 Family Member B proteinAcidic Protein Rich In Leucines proteinPutative Hla-Dr-Associated Protein I-2 proteinPhapi2 proteinSilver-Stainable Protein Ssp29 proteinANP32B proteinAPRIL proteinPHAPI2 protein |
Information sourced from Uniprot.org
