CPN2

Carboxypeptidase N subunit 2 is an enzyme that in humans is encoded by the CPN2 gene.[5][6][7]

For the Canadian airport with the TC LID, CPN2, see Pontiac Airpark.

CPN2
Identifiers
Aliases	CPN2, ACBP, carboxypeptidase N subunit 2
External IDs	OMIM: 603104 MGI: 1919006 HomoloGene: 19487 GeneCards: CPN2
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q29 Start 194,339,768 bp[1] End 194,351,328 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16|16 B2 Start 30,256,378 bp[2] End 30,267,499 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0010576 enzyme regulator activity • metallocarboxypeptidase activity Cellular component • blood microparticle • extracellular exosome • extracellular region • extracellular • extracellular matrix Biological process • protein stabilization • GO:0048552 regulation of catalytic activity • proteolysis • regulation of complement activation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1370	71756
Ensembl	ENSG00000178772	ENSMUSG00000023176
UniProt	P22792	Q9DBB9
RefSeq (mRNA)	NM_001080513 NM_001291988 NM_001309	NM_027904
RefSeq (protein)	NP_001073982 NP_001278917	NP_082180
Location (UCSC)	Chr 3: 194.34 – 194.35 Mb	Chr 16: 30.26 – 30.27 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000178772 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000023176 - 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. Tan F, Weerasinghe DK, Skidgel RA, Tamei H, Kaul RK, Roninson IB, Schilling JW, Erdos EG (Feb 1990). "The deduced protein sequence of the human carboxypeptidase N high molecular weight subunit reveals the presence of leucine-rich tandem repeats". J Biol Chem. 265 (1): 13–9. PMID 2378615.
6. Riley DA, Tan F, Miletich DJ, Skidgel RA (Apr 1999). "Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1)". Genomics. 50 (1): 105–8. doi:10.1006/geno.1998.5295. PMID 9628828.
7. "Entrez Gene: CPN2 carboxypeptidase N, polypeptide 2".

External links

• Human CPN2 genome location and CPN2 gene details page in the UCSC Genome Browser.

Further reading

• Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
• 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.
• Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wiśniewski JR (2004). "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry". Proteomics. 4 (2): 454–65. doi:10.1002/pmic.200300556. PMID 14760718.
• 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.
• Skidgel RA, Bennett CD, Schilling JW, et al. (1988). "Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: comparison with other carboxypeptidases". Biochem. Biophys. Res. Commun. 154 (3): 1323–9. doi:10.1016/0006-291X(88)90284-7. PMID 3408501.