ACP2

ACP2

Identifiers

ACP2, acid phosphatase 2, lysosomal, LAP

External IDs

MGI: 87882 HomoloGene: 1217 GeneCards: ACP2

Gene ontology
Molecular function	• hydrolase activity • acid phosphatase activity
Cellular component	• integral component of membrane • lysosomal membrane • lysosome • lysosomal lumen • extracellular exosome • membrane
Biological process	• skeletal system development • lysosome organization • dephosphorylation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse


53


11432


ENSG00000134575


ENSMUSG00000002103


P11117


P24638

RefSeq (mRNA)

NM_001131064 NM_001302489 NM_001302490 NM_001302491 NM_001302492
NM_001610


NM_007387

RefSeq (protein)


NP_001289418 NP_001289419 NP_001289420 NP_001289421 NP_001601


NP_031413

Location (UCSC)

Chr 11: 47.24 – 47.25 Mb

Chr 2: 91.2 – 91.21 Mb

PubMed search

^[1]

^[2]

View/Edit Human

View/Edit Mouse

Lysosomal acid phosphatase is an enzyme that in humans is encoded by the ACP2 gene.^[3]^[4]

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.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. PMID 975882. doi:10.1159/000130598.
1 2 "Entrez Gene: ACP2 acid phosphatase 2, lysosomal".

External links

Human ACP2 genome location and ACP2 gene details page in the UCSC Genome Browser.

Further reading

Moss DW, Raymond FD, Wile DB (1995). "Clinical and biological aspects of acid phosphatase.". Critical reviews in clinical laboratory sciences. 32 (4): 431–67. PMID 7576159. doi:10.3109/10408369509084690.
Gierek T, Lisiewicz T, Pilch J (1977). "Intracellular enzymatic response of lymphocytes and neutrophils in patients with cancer of the larynx.". Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch. 104 (2): 208–15. PMID 69583.
Jones C, Kao FT (1979). "Regional mapping of the gene for human lysosomal acid phosphatase (ACP2) using a hybrid clone panel containing segments of human chromosome 11.". Hum. Genet. 45 (1): 1–10. PMID 730175. doi:10.1007/BF00277567.
Geier C, von Figura K, Pohlmann R (1989). "Structure of the human lysosomal acid phosphatase gene.". Eur. J. Biochem. 183 (3): 611–6. PMID 2776754. doi:10.1111/j.1432-1033.1989.tb21090.x.
Lemansky P, Gieselmann V, Hasilik A, von Figura K (1985). "Synthesis and transport of lysosomal acid phosphatase in normal and I-cell fibroblasts.". J. Biol. Chem. 260 (15): 9023–30. PMID 3160696.
Pohlmann R, Krentler C, Schmidt B, et al. (1989). "Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment.". EMBO J. 7 (8): 2343–50. PMC 457099 . PMID 3191910.
Waheed A, Van Etten RL (1985). "Biosynthesis and processing of lysosomal acid phosphatase in cultured human cells.". Arch. Biochem. Biophys. 243 (1): 274–83. PMID 3904632. doi:10.1016/0003-9861(85)90796-9.
Nadler HL, Egan TJ (1970). "Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder.". N. Engl. J. Med. 282 (6): 302–7. PMID 5410815. doi:10.1056/NEJM197002052820604.
Bass DA, Lewis JC, Szejda P, et al. (1981). "Activation of lysosomal acid phosphatase of eosinophil leukocytes.". Lab. Invest. 44 (5): 403–9. PMID 6164873.
Chappard D, Alexandre C, Riffat G (1983). "Histochemical identification of osteoclasts. Review of current methods and reappraisal of a simple procedure for routine diagnosis on undecalcified human iliac bone biopsies.". Basic and Applied Histochemistry. 27 (2): 75–85. PMID 6193776.
Moszczyński P, Lisiewicz J (1984). "Beta-glucuronidase of lymphocytes in ontogenetic development of man.". Arch. Immunol. Ther. Exp. (Warsz.). 31 (2): 171–6. PMID 6651479.
Radzun HJ, Parwaresch MR (1981). "Isoelectric focusing pattern of acid phosphatase and acid esterase in human blood cells, including thymocytes, T lymphocytes, and B lymphocytes.". Exp. Hematol. 8 (6): 737–41. PMID 6970673.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. PMID 8619474. doi:10.1006/abio.1996.0138.
Whitelock RB, Fukuchi T, Zhou L, et al. (1997). "Cathepsin G, acid phosphatase, and alpha 1-proteinase inhibitor messenger RNA levels in keratoconus corneas.". Invest. Ophthalmol. Vis. Sci. 38 (2): 529–34. PMID 9040486.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMC 139146 . PMID 9110174. doi:10.1101/gr.7.4.353.
Obermüller S, Kiecke C, von Figura K, Höning S (2002). "The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targeting to lysosomes.". J. Cell. Sci. 115 (Pt 1): 185–94. PMID 11801736.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.

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