ACYP2

Acylphosphatase 2, muscle type
PDB rendering based on 1aps.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1aps​
Identifiers
Symbols	ACYP2 ; ACYM; ACYP
External IDs	Template:OMIM5 Template:MGI HomoloGene: 41776
Gene ontology Molecular function Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Acylphosphatase 2, muscle type, also known as ACYP2, is a human gene.

Acylphosphatase can hydrolyze the phosphoenzyme intermediate of different membrane pumps, particularly the Ca2+/Mg2+-ATPase from sarcoplasmic reticulum of skeletal muscle. Two isoenzymes have been isolated, called muscle acylphosphatase and erythrocyte acylphosphatase on the basis of their tissue localization. This gene encodes the muscle-type isoform (MT). An increase of the MT isoform is associated with muscle differentiation.

Further reading

• Parrini C, Taddei N, Ramazzotti M; et al. (2007). "Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation". Structure. 13 (8): 1143–51. doi:10.1016/j.str.2005.04.022. PMID 16084386.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Calamai M, Canale C, Relini A; et al. (2005). "Reversal of protein aggregation provides evidence for multiple aggregated States". J. Mol. Biol. 346 (2): 603–16. doi:10.1016/j.jmb.2004.11.067. PMID 15670608.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Paoli P, Pazzagli L, Giannoni E; et al. (2003). "A nucleophilic catalysis step is involved in the hydrolysis of aryl phosphate monoesters by human CT acylphosphatase". J. Biol. Chem. 278 (1): 194–9. doi:10.1074/jbc.M206918200. PMID 12409302.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chiti F, Taddei N, Baroni F; et al. (2002). "Kinetic partitioning of protein folding and aggregation". Nat. Struct. Biol. 9 (2): 137–43. doi:10.1038/nsb752. PMID 11799398.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chiti F, Taddei N, White PM; et al. (2002). "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding". Nat. Struct. Biol. 6 (11): 1005–9. doi:10.1038/14890. PMID 10542090.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fiaschi T, Marzocchini R, Raugei G; et al. (1998). "The 5'-untranslated region of the human muscle acylphosphatase mRNA has an inhibitory effect on protein expression". FEBS Lett. 417 (1): 130–4. PMID 9395090.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chiarugi P, Degl'Innocenti D, Raugei G; et al. (1997). "Differential migration of acylphosphatase isoenzymes from cytoplasm to nucleus during apoptotic cell death". Biochem. Biophys. Res. Commun. 231 (3): 717–21. doi:10.1006/bbrc.1997.6176. PMID 9070879.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Modesti A, Raugei G, Taddei N; et al. (1994). "Chemical synthesis and expression of a gene coding for human muscle acylphosphatase". Biochim. Biophys. Acta. 1216 (3): 369–74. PMID 8268218.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fiaschi T, Raugei G, Marzocchini R; et al. (1995). "Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase". FEBS Lett. 367 (2): 145–8. PMID 7796909.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chiarugi P, Raugei G, Marzocchini R; et al. (1995). "Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone". Biochem. J. 311 ( Pt 2): 567–73. PMID 7487897.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Manao G, Camici G, Modesti A; et al. (1986). "Human skeletal muscle acylphosphatase: the primary structure". Mol. Biol. Med. 2 (6): 369–78. PMID 6100723.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Liguri G, Camici G, Manao G; et al. (1987). "A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure". Biochemistry. 25 (24): 8089–94. PMID 3026468.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)