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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Acylphosphatase-2''' is an [[enzyme]] that in [[human]]s is encoded by the ''ACYP2'' [[gene]].<ref name="pmid8268218">{{cite journal | vauthors = Modesti A, Raugei G, Taddei N, Marzocchini R, Vecchi M, Camici G, Manao G, Ramponi G | title = Chemical synthesis and expression of a gene coding for human muscle acylphosphatase | journal = Biochimica et Biophysica Acta | volume = 1216 | issue = 3 | pages = 369–74 | date = Dec 1993 | pmid = 8268218 | pmc =  | doi = 10.1016/0167-4781(93)90003-v }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACYP2 acylphosphatase 2, muscle type| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=98| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_ACYP2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aps.
| PDB = {{PDB2|1aps}}
| Name = Acylphosphatase 2, muscle type
| HGNCid = 180
| Symbol = ACYP2
| AltSymbols =; ACYM; ACYP
| OMIM = 102595
| ECnumber = 
| Homologene = 41776
| MGIid = 1922822
| GeneAtlas_image1 = PBB_GE_ACYP2_gnf1h09944_at_tn.png
| Function = {{GNF_GO|id=GO:0003998 |text = acylphosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006796 |text = phosphate metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 98
    | Hs_Ensembl = ENSG00000170634
    | Hs_RefseqProtein = NP_612457
    | Hs_RefseqmRNA = NM_138448
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 54195914
    | Hs_GenLoc_end = 54385777
    | Hs_Uniprot = P14621
    | Mm_EntrezGene = 75572
    | Mm_Ensembl = ENSMUSG00000060923
    | Mm_RefseqmRNA = NM_029344
    | Mm_RefseqProtein = NP_083620
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 30405992
    | Mm_GenLoc_end = 30549396
    | Mm_Uniprot = Q5SPV7
  }}
}}
'''Acylphosphatase 2, muscle type''', also known as '''ACYP2''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Acylphosphatase]] can [[hydrolyze]] the phosphoenzyme intermediate of different [[Biological membrane|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 (biology)|tissue]] localization. This gene encodes the muscle-type [[isoform]] (MT). An increase of the MT isoform is associated with muscle differentiation.<ref name="entrez"/>
{{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.<ref name="entrez">{{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 = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|ACYP2}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Parrini C, Taddei N, Ramazzotti M, Degl'Innocenti D, Ramponi G, Dobson CM, Chiti F | title = Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation | journal = Structure | volume = 13 | issue = 8 | pages = 1143–1151 | date = Aug 2005 | pmid = 16084386 | doi = 10.1016/j.str.2005.04.022 }}
| citations =
* {{cite journal | vauthors = Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM | title = Reversal of protein aggregation provides evidence for multiple aggregated States | journal = Journal of Molecular Biology | volume = 346 | issue = 2 | pages = 603–616 | date = Feb 2005 | pmid = 15670608 | doi = 10.1016/j.jmb.2004.11.067 }}
*{{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 | vauthors = Paoli P, Pazzagli L, Giannoni E, Caselli A, Manao G, Camici G, Ramponi G | title = A nucleophilic catalysis step is involved in the hydrolysis of aryl phosphate monoesters by human CT acylphosphatase | journal = The Journal of Biological Chemistry | volume = 278 | issue = 1 | pages = 194–199 | date = Jan 2003 | pmid = 12409302 | doi = 10.1074/jbc.M206918200 }}
*{{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 | vauthors = Chiti F, Taddei N, Baroni F, Capanni C, Stefani M, Ramponi G, Dobson CM | title = Kinetic partitioning of protein folding and aggregation | journal = Nature Structural Biology | volume = 9 | issue = 2 | pages = 137–143 | date = Feb 2002 | pmid = 11799398 | doi = 10.1038/nsb752 }}
*{{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 | vauthors = Chiti F, Taddei N, White PM, Bucciantini M, Magherini F, Stefani M, Dobson CM | title = Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding | journal = Nature Structural Biology | volume = 6 | issue = 11 | pages = 1005–1009 | date = Nov 1999 | pmid = 10542090 | doi = 10.1038/14890 }}
*{{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 | vauthors = Fiaschi T, Marzocchini R, Raugei G, Veggi D, Chiarugi P, Ramponi G | title = The 5'-untranslated region of the human muscle acylphosphatase mRNA has an inhibitory effect on protein expression | journal = FEBS Letters | volume = 417 | issue = 1 | pages = 130–134 | date = Nov 1997 | pmid = 9395090 | doi = 10.1016/S0014-5793(97)01270-2 }}
*{{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 | vauthors = Chiarugi P, Degl'Innocenti D, Raugei G, Fiaschi T, Ramponi G | title = Differential migration of acylphosphatase isoenzymes from cytoplasm to nucleus during apoptotic cell death | journal = Biochemical and Biophysical Research Communications | volume = 231 | issue = 3 | pages = 717–721 | date = Feb 1997 | pmid = 9070879 | doi = 10.1006/bbrc.1997.6176 }}
*{{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 | vauthors = Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G | title = Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase | journal = FEBS Letters | volume = 367 | issue = 2 | pages = 145–148 | date = Jun 1995 | pmid = 7796909 | doi = 10.1016/0014-5793(95)00553-L }}
*{{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 | vauthors = Chiarugi P, Raugei G, Marzocchini R, Fiaschi T, Ciccarelli C, Berti A, Ramponi G | title = Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone | journal = The Biochemical Journal | volume = 311 | issue = 2 | pages = 567–73 | date = Oct 1995 | pmid = 7487897 | pmc = 1136037 | doi =  10.1042/bj3110567}}
*{{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 | vauthors = Manao G, Camici G, Modesti A, Liguri G, Berti A, Stefani M, Cappugi G, Ramponi G | title = Human skeletal muscle acylphosphatase: the primary structure | journal = Molecular Biology & Medicine | volume = 2 | issue = 6 | pages = 369–78 | date = Dec 1984 | pmid = 6100723 | 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 | vauthors = Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G | title = A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure | journal = Biochemistry | volume = 25 | issue = 24 | pages = 8089–8094 | date = Dec 1986 | pmid = 3026468 | doi = 10.1021/bi00372a044 }}
*{{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= }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=98}}
[[Category:Human proteins]]


{{protein-stub}}
{{gene-2-stub}}
{{WikiDoc Sources}}

Latest revision as of 17:47, 29 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Acylphosphatase-2 is an enzyme that in humans is encoded by the ACYP2 gene.[1][2]

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.[2]

References

  1. ↑ Modesti A, Raugei G, Taddei N, Marzocchini R, Vecchi M, Camici G, Manao G, Ramponi G (Dec 1993). "Chemical synthesis and expression of a gene coding for human muscle acylphosphatase". Biochimica et Biophysica Acta. 1216 (3): 369–74. doi:10.1016/0167-4781(93)90003-v. PMID 8268218.
  2. ↑ 2.0 2.1 "Entrez Gene: ACYP2 acylphosphatase 2, muscle type".

External links

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.


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