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APEH
Identifiers
Aliases	APEH, AARE, ACPH, APH, D3F15S2, D3S48E, DNF15S2, OPH, acylaminoacyl-peptide hydrolase
External IDs	OMIM: 102645; MGI: 88041; HomoloGene: 1240; GeneCards: APEH; OMA:APEH - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p21.31 Start 49,674,014 bp End 49,683,971 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9 F1|9 59.07 cM Start 107,962,612 bp End 107,971,805 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon anterior pituitary muscle of thigh right lobe of thyroid gland left lobe of thyroid gland right adrenal gland right adrenal cortex apex of heart left adrenal gland left adrenal cortex Top expressed in fetal liver hematopoietic progenitor cell right kidney human kidney epithelium of small intestine interventricular septum duodenum jejunum left lobe of liver spleen intestinal villus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function omega peptidase activity serine-type peptidase activity protein binding hydrolase activity serine-type endopeptidase activity identical protein binding RNA binding Cellular component nuclear membrane extracellular exosome extracellular region cytoplasm cytosol ficolin-1-rich granule lumen Biological process translational termination amyloid-beta metabolic process proteolysis neutrophil degranulation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 327 235606 Ensembl ENSG00000164062 ENSMUSG00000032590 UniProt P13798 Q8R146 RefSeq (mRNA) NM_001640 NM_146226 RefSeq (protein) NP_001631 NP_666338 Location (UCSC) Chr 3: 49.67 – 49.68 Mb Chr 9: 107.96 – 107.97 Mb PubMed search
Wikidata
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Acylamino-acid-releasing enzyme is an enzyme that in humans is encoded by the APEH gene.

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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000164062 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000032590 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. ^ "Entrez Gene: APEH N-acylaminoacyl-peptide hydrolase".

External links

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

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. doi:10.1016/S0021-9258(19)50598-1. 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. Bibcode:1991PNAS...88.2194J. 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. S2CID 35403281.
• 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. S2CID 44466566.
• 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. S2CID 10936126.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID 9746088.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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