CPN2

From Wikipedia, the free encyclopedia

Carboxypeptidase N, polypeptide 2

Identifiers

CPN2; ACBP

External IDs

OMIM: 603104 MGI: 1919006 HomoloGene: 19487

Gene ontology
Molecular Function:	• protein binding • enzyme regulator activity
Cellular Component:	• extracellular region
Biological Process:	• protein stabilization

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

XM_925798 (mRNA)
XP_930891 (protein)

NM_027904 (mRNA)
NP_082180 (protein)

Location

Chr 3: 195.54 - 195.55 Mb

Chr 16: 30.18 - 30.19 Mb

Pubmed search

[1]

[2]

Carboxypeptidase N, polypeptide 2, also known as CPN2, is a human gene.^[1]

[edit] References

^ Entrez Gene: CPN2 carboxypeptidase N, polypeptide 2.

[edit] 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. 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. 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. PMID 12477932.
Riley DA, Tan F, Miletich DJ, Skidgel RA (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.
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. PMID 3408501.
Tan F, Weerasinghe DK, Skidgel RA, et al. (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.