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Grindheim, A.K., Saraste, J. and Vedeler, A. (2017) Protein Phosphorylation and Its Role in the Regulation of Annexin A2 Function. Biochim Biophys Acta Gen Subj, 1861, 2515-2529. https://doi.org/10.1016/j.bbagen.2017.08.024

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• TITLE: Phosphorylation of AMMECR1 at Serine16 Is Not Essential for Its Nuclear Localization

  AUTHORS: Chengfeng Cai, Meng Xu, Yongquan Su, Huamin Zhou

  KEYWORDS: AMMECR1, Transcription, Phosphorylation, Nuclear Localization

  JOURNAL NAME: Journal of Biosciences and Medicines, Vol.7 No.11, November 27, 2019

  ABSTRACT: AMMECR1 is a critical gene in the pathogenesis of AMME syndrome. But, little is known about how AMMECR1 is regulated. Here, we showed that many human cell lines expressed AMMECR1. With Phos-tag SDS PAGE analysis, we demonstrated that AMMECR1 was constitutively phosphorylated at Ser16. AMMECR1 was localized in the nucleus. Mutation of Ser16 to alanine did not affect its nuclear localization. The homologs of AMMECR1, PAC688.03c and MTH857, were also nuclear proteins, but they were not phosphorylated when tested in HeLa cells. Therefore, AMMECR1 and its homologs might have atypical nuclear localization sequences.