ANP32E
Acidic (leucine-rich) nuclear phosphoprotein 32 family, member E | |||||||||||||
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Identifiers | |||||||||||||
Symbols | ANP32E ; LANP-L; LANPL | ||||||||||||
External IDs | OMIM: 609611 MGI: 1913721 HomoloGene: 137403 GeneCards: ANP32E Gene | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 81611 | 66471 | |||||||||||
Ensembl | ENSG00000143401 | ENSMUSG00000015749 | |||||||||||
UniProt | Q9BTT0 | P97822 | |||||||||||
RefSeq (mRNA) | NM_001136478 | NM_001253757 | |||||||||||
RefSeq (protein) | NP_001129950 | NP_001240686 | |||||||||||
Location (UCSC) | Chr 1: 150.19 – 150.21 Mb | Chr 3: 95.93 – 95.95 Mb | |||||||||||
PubMed search | |||||||||||||
Acidic leucine-rich nuclear phosphoprotein 32 family member E is a protein that in humans is encoded by the ANP32E gene.[1][2] The ANP32E gene is located on chromosome 1q22.[1] In mammalian cells, ANP32E has been shown to be an H2A.Z chaperone capable of promoting the removal of H2A.Z from chromatin.[3] In brain tissue, ANP32E together with Cpd1 regulate protein phosphatase 2A activity at synapses during synaptogenesis[4] and has been observed to form a complex with ANP32A and SET that stabilizes short-lived mRNAs containing AU-rich elements, as well as having acetyltransferase inhibitory activity (in a complex with SET) and having a role in chromatin remodeling and transcriptional regulation.[5]
See also
References
- ↑ 1.0 1.1 Jiang M, Ma Y, Ni X, Cao G, Ji C, Cheng H, Tang R, Xie Y, Mao Y (Nov 2002). "Molecular cloning and characterization of a novel human gene (ANP32E alias LANPL) from human fetal brain". Cytogenet Genome Res 97 (1–2): 68–71. doi:10.1159/000064058. PMID 12438741.
- ↑ "Entrez Gene: ANP32E acidic (leucine-rich) nuclear phosphoprotein 32 family, member E".
- ↑ Obri A, Ouararhni K, Papin C, Diebold ML, Padmanabhan K, Marek M, Stoll I, Roy L, Reilly PT, Mak TW, Dimitrov S, Romier C, Hamiche A (2014). "ANP32E is a histone chaperone that removes H2A.Z from chromatin". Nature 505 (7485): 648–53. doi:10.1038/nature12922. PMID 24463511.
- ↑ Costanzo RV, Vilá-Ortíz GJ, Perandones C, Carminatti H, Matilla A, Radrizzani M (2006). "Anp32e/Cpd1 regulates protein phosphatase 2A activity at synapses during synaptogenesis". Eur. J. Neurosci. 23 (2): 309–24. doi:10.1111/j.1460-9568.2005.04555.x. PMID 16420440.
- ↑ Santa-Coloma TA (2003). "Anp32e (Cpd1) and related protein phosphatase 2 inhibitors". Cerebellum 2 (4): 310–20. doi:10.1080/14734220310017212. PMID 14964690.
Further reading
- Matilla A, Radrizzani M (2005). "The Anp32 family of proteins containing leucine-rich repeats". Cerebellum 4 (1): 7–18. doi:10.1080/14734220410019020. PMID 15895553.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.