APEH (gene)

APEH
Identifiers
Aliases	APEH, AARE, ACPH, APH, D3F15S2, D3S48E, DNF15S2, OPH, acylaminoacyl-peptide hydrolase
External IDs	MGI: 88041 HomoloGene: 1240 GeneCards: APEH
Gene ontology Molecular function • poly(A) RNA binding • omega peptidase activity • serine-type peptidase activity • protein binding • hydrolase activity • serine-type endopeptidase activity Cellular component • cytoplasm • cytosol • nuclear membrane • extracellular exosome Biological process • translational termination • beta-amyloid metabolic process • proteolysis Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	327	235606
Ensembl	ENSG00000164062	ENSMUSG00000032590
UniProt	P13798	Q8R146
RefSeq (mRNA)	NM_001640	NM_146226
RefSeq (protein)	NP_001631.3	NP_666338.2
Location (UCSC)	Chr 3: 49.67 – 49.68 Mb	Chr 9: 108.09 – 108.09 Mb
PubMed search	[1]	[2]
Wikidata

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Acylamino-acid-releasing enzyme is an enzyme that in humans is encoded by the APEH gene.^[3][4]

This gene encodes the enzyme acylpeptide hydrolase, which catalyzes the hydrolysis of the terminal acetylated amino acid preferentially from small acetylated peptides. The acetyl amino acid formed by this hydrolase is further processed to acetate and a free amino acid by an aminoacylase. This gene is located within the same region of chromosome 3 (3p21) as the aminoacylase gene, and deletions at this locus are also associated with a decrease in aminoacylase activity. The acylpeptide hydrolase is a homotetrameric protein of 300 kDa with each subunit consisting of 732 amino acid residues. It can play an important role in destroying oxidatively-damaged proteins in living cells. Deletions of this gene locus are found in various types of carcinomas, including small-cell lung carcinoma and renal cell carcinoma.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Erlandsson R, Bergerheim US, Boldog F, Marcsek Z, Kunimi K, Lin BY, Ingvarsson S, Castresana JS, Lee WH (Oct 1990). "A gene near the D3F15S2 site on 3p is expressed in normal human kidney but not or only at a severely reduced level in 11 of 15 primary renal cell carcinomas (RCC)". Oncogene. 5 (8): 1207–11. PMID 2392324.
4. "Entrez Gene: APEH N-acylaminoacyl-peptide hydrolase".

Further reading

• Sharma KK, Ortwerth BJ (1992). "Description of an acylpeptide hydrolase from lens". Exp. Eye Res. 54 (6): 1005–10. doi:10.1016/0014-4835(92)90165-O. PMID 1521574.
• Scaloni A, Jones WM, Barra D, et al. (1992). "Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme". J. Biol. Chem. 267 (6): 3811–8. PMID 1740429.
• Erlandsson R, Boldog F, Persson B, et al. (1991). "The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase". Oncogene. 6 (7): 1293–5. PMID 1861871.
• Jones WM, Scaloni A, Bossa F, et al. (1991). "Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities". Proc. Natl. Acad. Sci. U.S.A. 88 (6): 2194–8. doi:10.1073/pnas.88.6.2194. PMC 51196. PMID 2006156.
• Naylor SL, Marshall A, Hensel C, et al. (1989). "The DNF15S2 locus at 3p21 is transcribed in normal lung and small cell lung cancer". Genomics. 4 (3): 355–61. doi:10.1016/0888-7543(89)90342-X. PMID 2565880.
• Feese M, Scaloni A, Jones WM, et al. (1993). "Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase". J. Mol. Biol. 233 (3): 546–9. doi:10.1006/jmbi.1993.1531. PMID 8411161.
• Mitta M, Ohnogi H, Mizutani S, et al. (1996). "The nucleotide sequence of human acylamino acid-releasing enzyme". DNA Res. 3 (1): 31–5. doi:10.1093/dnares/3.1.31. PMID 8724851.
• Scaloni A, Ingallinella P, Andolfo A, et al. (1999). "Structural investigations on human erythrocyte acylpeptide hydrolase by mass spectrometric procedures". J. Protein Chem. 18 (3): 349–60. doi:10.1023/A:1021047730831. PMID 10395453.
• Raphel V, Giardina T, Guevel L, et al. (1999). "Cloning, sequencing and further characterization of acylpeptide hydrolase from porcine intestinal mucosa". Biochim. Biophys. Acta. 1432 (2): 371–81. doi:10.1016/S0167-4838(99)00087-4. PMID 10407158.
• Fujino T, Watanabe K, Beppu M, et al. (2000). "Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase". Biochim. Biophys. Acta. 1478 (1): 102–12. doi:10.1016/S0167-4838(00)00004-2. PMID 10719179.
• Richards P, Lees J (2002). "Functional proteomics using microchannel plate detectors". Proteomics. 2 (3): 256–61. doi:10.1002/1615-9861(200203)2:3<256::AID-PROT256>3.0.CO;2-K. PMID 11921441.
• Perrier J, Giardina T, Durand A, Puigserver A (2002). "Specific enhancement of acylase I and acylpeptide hydrolase activities by the corresponding N-acetylated substrates in primary rat hepatocyte cultures". Biol. Cell. 94 (1): 45–54. doi:10.1016/S0248-4900(01)01177-7. PMID 12000146.
• 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. PMC 139241. PMID 12477932.
• 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. PMC 528928. PMID 15489334.
• Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.