ACYP2

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Acylphosphatase 2, muscle type
PDB rendering based on 1aps.
Available structures: 1aps
Identifiers
Symbol(s) ACYP2; ACYM; ACYP
External IDs OMIM: 102595 MGI: 1922822 HomoloGene: 41776
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 98 75572
Ensembl ENSG00000170634 ENSMUSG00000060923
Uniprot P14621 Q5SPV7
Refseq NM_138448 (mRNA)
NP_612457 (protein)		 NM_029344 (mRNA)
NP_083620 (protein)
Location Chr 2: 54.2 - 54.39 Mb Chr 11: 30.41 - 30.55 Mb
Pubmed search [1] [2]

Acylphosphatase 2, muscle type, also known as ACYP2, is a human gene.[1]

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.[1]

[edit] References

  1. ^ a b Entrez Gene: ACYP2 acylphosphatase 2, muscle type.

[edit] 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
  • 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. 
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