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{{Infobox_gene}}
'''Lysosomal acid phosphatase''' is an [[enzyme]] that in humans is encoded by the ''ACP2'' [[gene]].<ref name="pmid975882">{{cite journal | vauthors = Shows TB, Brown JA, Lalley PA | title = Assignment and linear order of human acid phosphatase-2, esterase A4, and lactate dehydrogenase A genes on chromosome 11 | journal = Cytogenet Cell Genet | volume = 16 | issue = 1-5 | pages = 231–4 |date=Dec 1976 | pmid = 975882 | pmc =  | doi =10.1159/000130598  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACP2 acid phosphatase 2, lysosomal| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53| accessdate = }}</ref>
'''Lysosomal [[acid phosphatase]]''' is composed of two subunits, alpha and beta, and is chemically and genetically distinct from [[red cell acid phosphatase]]. Lysosomal acid phosphatase 2 is a member of a family of distinct isoenzymes which hydrolyze [[orthophosphoric monoester]]s to [[alcohol]] and [[phosphate]]. [[Acid phosphatase deficiency]] is caused by [[mutation]]s in the ACP2 (beta subunit) and [[ACP3]] (alpha subunit) genes.<ref name="entrez"/>
==References==
{{reflist}}
==External links==
* {{UCSC gene info|ACP2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | vauthors=Moss DW, Raymond FD, Wile DB |title=Clinical and biological aspects of acid phosphatase. |journal=Critical reviews in clinical laboratory sciences |volume=32 |issue= 4 |pages= 431–67 |year= 1995 |pmid= 7576159 |doi=10.3109/10408369509084690  }}
*{{cite journal  | vauthors=Gierek T, Lisiewicz T, Pilch J |title=Intracellular enzymatic response of lymphocytes and neutrophils in patients with cancer of the larynx. |journal=Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch. |volume=104 |issue= 2 |pages= 208–15 |year= 1977 |pmid= 69583 |doi=  }}
*{{cite journal  | vauthors=Jones C, Kao FT |title=Regional mapping of the gene for human lysosomal acid phosphatase (ACP2) using a hybrid clone panel containing segments of human chromosome 11. |journal=Hum. Genet. |volume=45 |issue= 1 |pages= 1–10 |year= 1979 |pmid= 730175 |doi=10.1007/BF00277567  }}
*{{cite journal  | vauthors=Geier C, von Figura K, Pohlmann R |title=Structure of the human lysosomal acid phosphatase gene. |journal=Eur. J. Biochem. |volume=183 |issue= 3 |pages= 611–6 |year= 1989 |pmid= 2776754 |doi=10.1111/j.1432-1033.1989.tb21090.x  }}
*{{cite journal  | vauthors=Lemansky P, Gieselmann V, Hasilik A, von Figura K |title=Synthesis and transport of lysosomal acid phosphatase in normal and I-cell fibroblasts. |journal=J. Biol. Chem. |volume=260 |issue= 15 |pages= 9023–30 |year= 1985 |pmid= 3160696 |doi=  }}
*{{cite journal  | vauthors=Pohlmann R, Krentler C, Schmidt B |title=Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. |journal=EMBO J. |volume=7 |issue= 8 |pages= 2343–50 |year= 1989 |pmid= 3191910 |doi=  | pmc=457099  |display-authors=etal}}
*{{cite journal  | vauthors=Waheed A, Van Etten RL |title=Biosynthesis and processing of lysosomal acid phosphatase in cultured human cells. |journal=Arch. Biochem. Biophys. |volume=243 |issue= 1 |pages= 274–83 |year= 1985 |pmid= 3904632 |doi=10.1016/0003-9861(85)90796-9  }}
*{{cite journal  | vauthors=Nadler HL, Egan TJ |title=Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder. |journal=N. Engl. J. Med. |volume=282 |issue= 6 |pages= 302–7 |year= 1970 |pmid= 5410815 |doi=10.1056/NEJM197002052820604  }}
*{{cite journal  | vauthors=Bass DA, Lewis JC, Szejda P |title=Activation of lysosomal acid phosphatase of eosinophil leukocytes. |journal=Lab. Invest. |volume=44 |issue= 5 |pages= 403–9 |year= 1981 |pmid= 6164873 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Chappard D, Alexandre C, Riffat G |title=Histochemical identification of osteoclasts. Review of current methods and reappraisal of a simple procedure for routine diagnosis on undecalcified human iliac bone biopsies. |journal=Basic and Applied Histochemistry |volume=27 |issue= 2 |pages= 75–85 |year= 1983 |pmid= 6193776 |doi=  }}
*{{cite journal  | vauthors=Moszczyński P, Lisiewicz J |title=Beta-glucuronidase of lymphocytes in ontogenetic development of man. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=31 |issue= 2 |pages= 171–6 |year= 1984 |pmid= 6651479 |doi=  }}
*{{cite journal  | vauthors=Radzun HJ, Parwaresch MR |title=Isoelectric focusing pattern of acid phosphatase and acid esterase in human blood cells, including thymocytes, T lymphocytes, and B lymphocytes. |journal=Exp. Hematol. |volume=8 |issue= 6 |pages= 737–41 |year= 1981 |pmid= 6970673 |doi=  }}
*{{cite journal  | vauthors=Andersson B, Wentland MA, Ricafrente JY |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 |display-authors=etal}}
*{{cite journal  | vauthors=Whitelock RB, Fukuchi T, Zhou L |title=Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas. |journal=Invest. Ophthalmol. Vis. Sci. |volume=38 |issue= 2 |pages= 529–34 |year= 1997 |pmid= 9040486 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Yu W, Andersson B, Worley KC |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=  10.1101/gr.7.4.353| pmc=139146  |display-authors=etal}}
*{{cite journal  | vauthors=Obermüller S, Kiecke C, von Figura K, Höning S |title=The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targeting to lysosomes. |journal=J. Cell Sci. |volume=115 |issue= Pt 1 |pages= 185–94 |year= 2002 |pmid= 11801736 |doi=  }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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  | pmc=139241 |display-authors=etal}}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |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  | pmc=528928 |display-authors=etal}}
}}
{{refend}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Category:Human proteins]]
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Acid phosphatase 2, lysosomal
| HGNCid = 123
| Symbol = ACP2
| AltSymbols =;
| OMIM = 171650
| ECnumber = 
| Homologene = 1217
| MGIid = 87882
| GeneAtlas_image1 = PBB_GE_ACP2_202767_at_tn.png
| Function = {{GNF_GO|id=GO:0003993 |text = acid phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005765 |text = lysosomal membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0007040 |text = lysosome organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 53
    | Hs_Ensembl = ENSG00000134575
    | Hs_RefseqProtein = NP_001601
    | Hs_RefseqmRNA = NM_001610
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 47217429
    | Hs_GenLoc_end = 47226939
    | Hs_Uniprot = P11117
    | Mm_EntrezGene = 11432
    | Mm_Ensembl = ENSMUSG00000002103
    | Mm_RefseqmRNA = NM_007387
    | Mm_RefseqProtein = NP_031413
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 91003758
    | Mm_GenLoc_end = 91013613
    | Mm_Uniprot = Q3U4F3
  }}
}}
'''Acid phosphatase 2, lysosomal''', also known as '''ACP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACP2 acid phosphatase 2, lysosomal| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Lysosomal acid phosphatase is comprised of two subunits, alpha and beta, and is chemically and genetically distinct from red cell acid phosphatase. Lysosomal acid phosphatase 2 is a member of a family of distinct isoenzymes which hydrolyze orthophosphoric monoesters to alcohol and phosphate. Acid phosphatase deficiency is caused by mutations in the ACP2 (beta subunit) and ACP3 (alpha subunit) genes.<ref name="entrez">{{cite web | title = Entrez Gene: ACP2 acid phosphatase 2, lysosomal| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=53| accessdate = }}</ref>
}}
==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Moss DW, Raymond FD, Wile DB |title=Clinical and biological aspects of acid phosphatase. |journal=Critical reviews in clinical laboratory sciences |volume=32 |issue= 4 |pages= 431-67 |year= 1995 |pmid= 7576159 |doi=  }}
*{{cite journal  | author=Gierek T, Lisiewicz T, Pilch J |title=Intracellular enzymatic response of lymphocytes and neutrophils in patients with cancer of the larynx. |journal=Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch. |volume=104 |issue= 2 |pages= 208-15 |year= 1977 |pmid= 69583 |doi=  }}
*{{cite journal  | author=Jones C, Kao FT |title=Regional mapping of the gene for human lysosomal acid phosphatase (ACP2) using a hybrid clone panel containing segments of human chromosome 11. |journal=Hum. Genet. |volume=45 |issue= 1 |pages= 1-10 |year= 1979 |pmid= 730175 |doi=  }}
*{{cite journal  | author=Shows TB, Brown JA, Lalley PA |title=Assignment and linear order of human acid phosphatase-2, esterase A4, and lactate dehydrogenase A genes on chromosome 11. |journal=Cytogenet. Cell Genet. |volume=16 |issue= 1-5 |pages= 231-4 |year= 1976 |pmid= 975882 |doi=  }}
*{{cite journal  | author=Geier C, von Figura K, Pohlmann R |title=Structure of the human lysosomal acid phosphatase gene. |journal=Eur. J. Biochem. |volume=183 |issue= 3 |pages= 611-6 |year= 1989 |pmid= 2776754 |doi=  }}
*{{cite journal  | author=Lemansky P, Gieselmann V, Hasilik A, von Figura K |title=Synthesis and transport of lysosomal acid phosphatase in normal and I-cell fibroblasts. |journal=J. Biol. Chem. |volume=260 |issue= 15 |pages= 9023-30 |year= 1985 |pmid= 3160696 |doi=  }}
*{{cite journal  | author=Pohlmann R, Krentler C, Schmidt B, ''et al.'' |title=Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. |journal=EMBO J. |volume=7 |issue= 8 |pages= 2343-50 |year= 1989 |pmid= 3191910 |doi=  }}
*{{cite journal  | author=Waheed A, Van Etten RL |title=Biosynthesis and processing of lysosomal acid phosphatase in cultured human cells. |journal=Arch. Biochem. Biophys. |volume=243 |issue= 1 |pages= 274-83 |year= 1985 |pmid= 3904632 |doi=  }}
*{{cite journal  | author=Nadler HL, Egan TJ |title=Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder. |journal=N. Engl. J. Med. |volume=282 |issue= 6 |pages= 302-7 |year= 1970 |pmid= 5410815 |doi=  }}
*{{cite journal  | author=Bass DA, Lewis JC, Szejda P, ''et al.'' |title=Activation of lysosomal acid phosphatase of eosinophil leukocytes. |journal=Lab. Invest. |volume=44 |issue= 5 |pages= 403-9 |year= 1981 |pmid= 6164873 |doi=  }}
*{{cite journal  | author=Chappard D, Alexandre C, Riffat G |title=Histochemical identification of osteoclasts. Review of current methods and reappraisal of a simple procedure for routine diagnosis on undecalcified human iliac bone biopsies. |journal=Basic and applied histochemistry |volume=27 |issue= 2 |pages= 75-85 |year= 1983 |pmid= 6193776 |doi=  }}
*{{cite journal  | author=Moszczyński P, Lisiewicz J |title=Beta-glucuronidase of lymphocytes in ontogenetic development of man. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=31 |issue= 2 |pages= 171-6 |year= 1984 |pmid= 6651479 |doi=  }}
*{{cite journal  | author=Radzun HJ, Parwaresch MR |title=Isoelectric focusing pattern of acid phosphatase and acid esterase in human blood cells, including thymocytes, T lymphocytes, and B lymphocytes. |journal=Exp. Hematol. |volume=8 |issue= 6 |pages= 737-41 |year= 1981 |pmid= 6970673 |doi=  }}
*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal  | author=Whitelock RB, Fukuchi T, Zhou L, ''et al.'' |title=Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas. |journal=Invest. Ophthalmol. Vis. Sci. |volume=38 |issue= 2 |pages= 529-34 |year= 1997 |pmid= 9040486 |doi=  }}
*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
*{{cite journal  | author=Obermüller S, Kiecke C, von Figura K, Höning S |title=The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targetting to lysosomes. |journal=J. Cell. Sci. |volume=115 |issue= Pt 1 |pages= 185-94 |year= 2002 |pmid= 11801736 |doi=  }}
*{{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=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 }}
}}
{{refend}}


{{protein-stub}}
{{gene-11-stub}}
{{WikiDoc Sources}}

Latest revision as of 19:14, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Lysosomal acid phosphatase is an enzyme that in humans is encoded by the ACP2 gene.[1][2]

Lysosomal acid phosphatase is composed of two subunits, alpha and beta, and is chemically and genetically distinct from red cell acid phosphatase. Lysosomal acid phosphatase 2 is a member of a family of distinct isoenzymes which hydrolyze orthophosphoric monoesters to alcohol and phosphate. Acid phosphatase deficiency is caused by mutations in the ACP2 (beta subunit) and ACP3 (alpha subunit) genes.[2]

References

  1. ↑ Shows TB, Brown JA, Lalley PA (Dec 1976). "Assignment and linear order of human acid phosphatase-2, esterase A4, and lactate dehydrogenase A genes on chromosome 11". Cytogenet Cell Genet. 16 (1–5): 231–4. doi:10.1159/000130598. PMID 975882.
  2. ↑ 2.0 2.1 "Entrez Gene: ACP2 acid phosphatase 2, lysosomal".

External links

Further reading


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