NLRP2

From Wikipedia, the free encyclopedia

NLR family, pyrin domain containing 2

Identifiers

NLRP2; NBS1; CLR19.9; FLJ20510; NALP2; PAN1; PYPAF2

External IDs

OMIM: 609364 MGI: 3041206 HomoloGene: 56789

Gene ontology
Molecular Function:	• nucleotide binding • protein binding • ATP binding • Pyrin domain binding
Cellular Component:	• cytoplasm
Biological Process:	• apoptosis • defense response • positive regulation of caspase activity • positive regulation of interleukin-1 beta secretion

Orthologs

Human

Mouse

n/a

Refseq

NM_017852 (mRNA)
NP_060322 (protein)

NM_177690 (mRNA)
NP_808358 (protein)

Location

Chr 19: 60.17 - 60.2 Mb

Chr 7: 4.9 - 4.95 Mb

Pubmed search

[1]

[2]

NLR family, pyrin domain containing 2, also known as NLRP2, is a human gene.^[1]

NALP proteins, such as NALP2, are characterized by an N-terminal pyrin (MIM 608107) domain (PYD) and are involved in the activation of caspase-1 (CASP1; MIM 147678) by Toll-like receptors (see TLR4; MIM 603030). They may also be involved in protein complexes that activate proinflammatory caspases (Tschopp et al., 2003).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: NLRP2 NLR family, pyrin domain containing 2.

[edit] Further reading

Bertin J, DiStefano PS (2001). "The PYRIN domain: a novel motif found in apoptosis and inflammation proteins.". Cell Death Differ. 7 (12): 1273–4. doi:10.1038/sj.cdd.4400774. PMID 11270363.
Tschopp J, Martinon F, Burns K (2003). "NALPs: a novel protein family involved in inflammation.". Nat. Rev. Mol. Cell Biol. 4 (2): 95–104. doi:10.1038/nrm1019. PMID 12563287.
Teng SC, Wu KJ, Tseng SF, et al. (2007). "Importin KPNA2, NBS1, DNA repair and tumorigenesis.". J. Mol. Histol. 37 (5-7): 293–9. doi:10.1007/s10735-006-9032-y. PMID 16752129.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Martinon F, Hofmann K, Tschopp J (2001). "The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation.". Curr. Biol. 11 (4): R118–20. PMID 11250163.
Wang L, Manji GA, Grenier JM, et al. (2002). "PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-kappa B and caspase-1-dependent cytokine processing.". J. Biol. Chem. 277 (33): 29874–80. doi:10.1074/jbc.M203915200. PMID 12019269.
Grenier JM, Wang L, Manji GA, et al. (2002). "Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-kappaB and caspase-1.". FEBS Lett. 530 (1-3): 73–8. PMID 12387869.
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.
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.
Agostini L, Martinon F, Burns K, et al. (2004). "NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder.". Immunity 20 (3): 319–25. PMID 15030775.
Bruey JM, Bruey-Sedano N, Newman R, et al. (2005). "PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages.". J. Biol. Chem. 279 (50): 51897–907. doi:10.1074/jbc.M406741200. PMID 15456791.
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.
Kinoshita T, Wang Y, Hasegawa M, et al. (2005). "PYPAF3, a PYRIN-containing APAF-1-like protein, is a feedback regulator of caspase-1-dependent interleukin-1beta secretion.". J. Biol. Chem. 280 (23): 21720–5. doi:10.1074/jbc.M410057200. PMID 15817483.
Rink L, Slupianek A, Stoklosa T, et al. (2007). "Enhanced phosphorylation of Nbs1, a member of DNA repair/checkpoint complex Mre11-RAD50-Nbs1, can be targeted to increase the efficacy of imatinib mesylate against BCR/ABL-positive leukemia cells.". Blood 110 (2): 651–60. doi:10.1182/blood-2006-08-042630. PMID 17431132.