RNPEP

Identifiers

RNPEP, AP-B, arginyl aminopeptidase

External IDs

MGI: 2384902 HomoloGene: 10628 GeneCards: RNPEP

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	• extracellular fluid • extracellular region • plasma membrane • extracellular exosome • secretory granule
Biological process	• proteolysis • negative regulation of blood pressure • peptide catabolic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


6051


215615

Ensembl


ENSG00000176393


ENSMUSG00000041926

UniProt


Q9H4A4


Q8VCT3

RefSeq (mRNA)


NM_020216 NM_001319182 NM_001319183 NM_001319184


NM_001159624 NM_145417

RefSeq (protein)


NP_064601.3 NP_001306111.1 NP_001306112.1 NP_001306113.1


NP_001153096.1 NP_663392.2

Location (UCSC)

Chr 1: 201.98 – 202.01 Mb

Chr 1: 135.26 – 135.28 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Aminopeptidase B is an enzyme that in humans is encoded by the RNPEP gene.^[3]^[4]^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Aurich-Costa J, Cadel S, Gouzy C, Foulon T, Cherif D, Cohen P (Apr 1998). "Assignment of the aminopeptidase B gene (RNPEP) to human chromosome 1 band q32 by in situ hybridization". Cytogenet Cell Genet. 79 (1–2): 143–4. doi:10.1159/000134703. PMID 9533033.
↑ Foulon T, Cadel S, Cohen P (Oct 1999). "Aminopeptidase B (EC 3.4.11.6)". Int J Biochem Cell Biol. 31 (7): 747–50. doi:10.1016/S1357-2725(99)00021-7. PMID 10467730.
↑ "Entrez Gene: RNPEP arginyl aminopeptidase (aminopeptidase B)".

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.
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. 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. 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.

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O

3.4.13	Dipeptidase 1 2 3

3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II

3.4.15	Angiotensin-converting enzyme

3.4.16	Serine type carboxypeptidases: Cathepsin A DD-transpeptidase

3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II

Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

External links

The MEROPS online database for peptidases and their inhibitors: M01.014

This article is issued from Wikipedia - version of the 5/23/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

RNPEP

References

Further reading

External links