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RNPEP

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

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)^[1]

Band	1q32.1	Start	201,982,372bp^[1]
Band	1q32.1	End	202,006,147bp^[1]

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)^[2]

Band	1\|1 E4	Start	135,190,450bp^[2]
Band	1\|1 E4	End	135,211,822bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

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

BioGPS


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

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_001306111 NP_001306112 NP_001306113 NP_064601


NP_001153096 NP_663392

Location (UCSC)

Chr 1: 201.98 – 202.01 Mb

Chr 1: 135.19 – 135.21 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Aminopeptidase B is anenzyme that in humans is encoded by theRNPEPgene.^[5]^[6]^[7]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000176393 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000041926 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.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.

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

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	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)