ACYP2

ACYP2

Acylphosphatase 2, muscle type, also known as ACYP2, is a human gene.cite web | title = Entrez Gene: ACYP2 acylphosphatase 2, muscle type| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=98| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: ACYP2 acylphosphatase 2, muscle type| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=98| accessdate = ]

References

Further reading

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

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  • Acylphosphatase — Pfam box Symbol = Acylphosphatase Name = Acylphosphatase width = 250 caption = PDB rendering based on PDB2|1APS. Pfam = PF00708 InterPro=IPR001792 SMART= PROSITE= PDOC00136 SCOP = 1aps TCDB = OPM family = OPM protein = PDB = PDB2|2GV1, PDB2|1APS …   Wikipedia

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