RNPEP

RNPEP
Identifiers
Aliases	RNPEP, AP-B, arginyl aminopeptidase, APB
External IDs	OMIM: 602675; MGI: 2384902; HomoloGene: 10628; GeneCards: RNPEP; OMA:RNPEP - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	202,006,147 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	135,211,822 bp
RNA expression pattern
	Top expressed in
	mucosa of transverse colon; ; duodenum; ; granulocyte; ; rectum; ; monocyte; ; gonad; ; right uterine tube; ; mucosa of esophagus; ; olfactory zone of nasal mucosa; ; stromal cell of endometrium;
	Top expressed in
	granulocyte; ; seminal vesicula; ; crypt of lieberkuhn of small intestine; ; epithelium of stomach; ; jejunum; ; duodenum; ; pyloric antrum; ; molar; ; right kidney; ; genital tubercle;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	peptide binding; zinc ion binding; peptidase activity; aminopeptidase activity; metalloexopeptidase activity; metalloaminopeptidase activity; metallopeptidase activity; hydrolase activity; metal ion binding; epoxide hydrolase activity;
Cellular component	plasma membrane; extracellular exosome; secretory granule; extracellular space; extracellular region;
Biological process	proteolysis; negative regulation of blood pressure; peptide catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	6051
	215615
	ENSG00000176393
	ENSMUSG00000041926
	Q9H4A4
	Q8VCT3
	NM_020216; NM_001319182; NM_001319183; NM_001319184
	NM_001159624; NM_145417
	NP_001306111; NP_001306112; NP_001306113; NP_064601
	NP_001153096; NP_663392
	Wikidata
View/Edit Human	View/Edit Mouse

Aminopeptidase B is an enzyme that in humans is encoded by the RNPEP gene.^[5]^[6]^[7]

References

Belhacene N, Mari B, Rossi B, Auberger P (1993). "Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation". Eur. J. Immunol. 23 (8): 1948–55. doi:10.1002/eji.1830230833. PMID 8344358. S2CID 855382.
Gress TM, Müller-Pillasch F, Geng M, et al. (1996). "A pancreatic cancer-specific expression profile". Oncogene. 13 (8): 1819–30. PMID 8895530.
Balogh A, Cadel S, Foulon T, et al. (1998). "Aminopeptidase B: a processing enzyme secreted and associated with the plasma membrane of rat pheochromocytoma (PC12) cells". J. Cell Sci. 111 (2): 161–9. doi:10.1242/jcs.111.2.161. PMID 9405297.
Piesse C, Tymms M, Garrafa E, et al. (2002). "Human aminopeptidase B (rnpep) on chromosome 1q32.2: complementary DNA, genomic structure and expression". Gene. 292 (1–2): 129–40. doi:10.1016/S0378-1119(02)00650-9. PMID 12119107.
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.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Fukasawa KM, Hirose J, Hata T, Ono Y (2006). "Aspartic acid 405 contributes to the substrate specificity of aminopeptidase B". Biochemistry. 45 (38): 11425–31. doi:10.1021/bi0604577. PMID 16981702.

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

RNPEP

References

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