ACYP2

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
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
Wikidata
View/Edit Human

Acylphosphatase-2 is an enzyme that in humans is encoded by the ACYP2 gene.

Function

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.

External links

• Human ACYP2 genome location and ACYP2 gene details page in the UCSC Genome Browser.

Further reading

• Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F (Aug 2005). "Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation". Structure. 13 (8): 1143–1151. doi:10.1016/j.str.2005.04.022. PMID 16084386.
• Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM (Feb 2005). "Reversal of protein aggregation provides evidence for multiple aggregated States". Journal of Molecular Biology. 346 (2): 603–616. doi:10.1016/j.jmb.2004.11.067. PMID 15670608.
• Paoli P, Pazzagli L, Giannoni E, Caselli A, Manao G, Camici G, Ramponi G (Jan 2003). "A nucleophilic catalysis step is involved in the hydrolysis of aryl phosphate monoesters by human CT acylphosphatase". The Journal of Biological Chemistry. 278 (1): 194–199. doi:10.1074/jbc.M206918200. PMID 12409302.
• Chiti F, Taddei N, Baroni F, Capanni C, Stefani M, Ramponi G, Dobson CM (Feb 2002). "Kinetic partitioning of protein folding and aggregation". Nature Structural Biology. 9 (2): 137–143. doi:10.1038/nsb752. PMID 11799398.
• Chiti F, Taddei N, White PM, Bucciantini M, Magherini F, Stefani M, Dobson CM (Nov 1999). "Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding". Nature Structural Biology. 6 (11): 1005–1009. doi:10.1038/14890. PMID 10542090.
• Fiaschi T, Marzocchini R, Raugei G, Veggi D, Chiarugi P, Ramponi G (Nov 1997). "The 5'-untranslated region of the human muscle acylphosphatase mRNA has an inhibitory effect on protein expression". FEBS Letters. 417 (1): 130–134. doi:10.1016/S0014-5793(97)01270-2. PMID 9395090.
• Chiarugi P, Degl'Innocenti D, Raugei G, Fiaschi T, Ramponi G (Feb 1997). "Differential migration of acylphosphatase isoenzymes from cytoplasm to nucleus during apoptotic cell death". Biochemical and Biophysical Research Communications. 231 (3): 717–721. doi:10.1006/bbrc.1997.6176. PMID 9070879.
• Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G (Jun 1995). "Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase". FEBS Letters. 367 (2): 145–148. doi:10.1016/0014-5793(95)00553-L. PMID 7796909.
• Chiarugi P, Raugei G, Marzocchini R, Fiaschi T, Ciccarelli C, Berti A, Ramponi G (Oct 1995). "Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone". The Biochemical Journal. 311 (2): 567–73. doi:10.1042/bj3110567. PMC 1136037. PMID 7487897.
• Manao G, Camici G, Modesti A, Liguri G, Berti A, Stefani M, Cappugi G, Ramponi G (Dec 1984). "Human skeletal muscle acylphosphatase: the primary structure". Molecular Biology & Medicine. 2 (6): 369–78. PMID 6100723.
• Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G (Dec 1986). "A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure". Biochemistry. 25 (24): 8089–8094. doi:10.1021/bi00372a044. PMID 3026468.