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edit Protein phosphatase 3 (formerly 2B), regulatory subunit B, alpha isoform PDB rendering based on 1aui. Available structures PDB 1aui, 1m63, 1mf8, 1tco, 2p6b Identifiers Symbols PPP3R1; CALNB1; CNB; CNB1 External IDs OMIM: 601302 MGI: 107172 HomoloGene: 68099 GeneCards: PPP3R1 Gene Gene Ontology Molecular function • calcium-dependent protein serine/threonine phosphatase activity • calcium ion binding • calmodulin inhibitor activity Cellular component • calcineurin complex Sources: Amigo / QuickGO Orthologs Species Human Mouse Entrez 5534 19058 Ensembl ENSG00000221823 ENSMUSG00000033953 UniProt P63098 Q63810 RefSeq (mRNA) NM_000945 NM_024459 RefSeq (protein) NP_000936 NP_077779 Location (UCSC) Chr 2: 68.36 - 68.49 Mb Chr 11: 17.06 - 17.1 Mb PubMed search [1] [2] Calcineurin subunit B type 1 also known as protein phosphatase 2B regulatory subunit 1 is a protein that in humans is encoded by the PPP3R1 gene.[1][2][3] Clinical significance The presence of a single nucleotide polymorphism rs1868402 in the PPP3R1 gene is strongly correlated with rapid progress of Alzheimer's disease.[4] References ^ Wang MG, Yi H, Guerini D, Klee CB, McBride OW (Jan 1997). "Calcineurin A alpha (PPP3CA), calcineurin A beta (PPP3CB) and calcineurin B (PPP3R1) are located on human chromosomes 4, 10q21→q22 and 2p16→p15 respectively". Cytogenet Cell Genet 72 (2-3): 236–41. doi:10.1159/000134198. PMID 8978785.  ^ Guerini D, Krinks MH, Sikela JM, Hahn WE, Klee CB (Mar 1990). "Isolation and sequence of a cDNA clone for human calcineurin B, the Ca2+-binding subunit of the Ca2+/calmodulin-stimulated protein phosphatase". DNA 8 (9): 675–82. PMID 2558868.  ^ "Entrez Gene: PPP3R1 protein phosphatase 3 (formerly 2B), regulatory subunit B, alpha isoform".  ^ Cruchaga C, Kauwe JSK, Mayo K, Spiegel N, Bertelsen S, et al. (2010). Myers, Amanda J.. ed. "SNPs Associated with Cerebrospinal Fluid Phospho-Tau Levels Influence Rate of Decline in Alzheimer's Disease". PLoS Genet 6 (9): e1001101. doi:10.1371/journal.pgen.1001101. PMC 2940763. PMID 20862329.  Further reading Kawamura A, Su MS (1995). "Interaction of FKBP12-FK506 with calcineurin A at the B subunit-binding domain.". J. Biol. Chem. 270 (26): 15463–6. doi:10.1074/jbc.270.26.15463. PMID 7541044.  Kissinger CR, Parge HE, Knighton DR, et al. (1996). "Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex.". Nature 378 (6557): 641–4. doi:10.1038/378641a0. PMID 8524402.  Feng B, Stemmer PM (1999). "Interactions of calcineurin A, calcineurin B, and Ca2+.". Biochemistry 38 (38): 12481–9. doi:10.1021/bi990492w. PMID 10493818.  Stratakis CA, Taymans SE (1999). "Structure of the gene coding for calcineurin B (PPP3R1) and mapping to D2S358-D2S1778 (chromosomal region 2p15).". DNA Seq. 9 (4): 227–30. doi:10.3109/10425179809105209. PMID 10520753.  Nishio H, Matsui K, Tsuji H, et al. (2000). "Immunolocalization of calcineurin and FKBP12, the FK506-binding protein, in Hassall's corpuscles of human thymus and epidermis.". Histochem. Cell Biol. 114 (1): 9–14. PMID 10959817.  Sokal I, Li N, Verlinde CL, et al. (2001). "Ca(2+)-binding proteins in the retina: from discovery to etiology of human disease(1).". Biochim. Biophys. Acta 1498 (2-3): 233–51. PMID 11108966.  Graef IA, Chen F, Chen L, et al. (2001). "Signals transduced by Ca(2+)/calcineurin and NFATc3/c4 pattern the developing vasculature.". Cell 105 (7): 863–75. doi:10.1016/S0092-8674(01)00396-8. PMID 11439183.  Al-Daraji WI, Grant KR, Ryan K, et al. (2002). "Localization of calcineurin/NFAT in human skin and psoriasis and inhibition of calcineurin/NFAT activation in human keratinocytes by cyclosporin A.". J. Invest. Dermatol. 118 (5): 779–88. doi:10.1046/j.1523-1747.2002.01709.x. PMID 11982754.  Huai Q, Kim HY, Liu Y, et al. (2002). "Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes.". Proc. Natl. Acad. Sci. U.S.A. 99 (19): 12037–42. doi:10.1073/pnas.192206699. PMC 129394. PMID 12218175.  Jin L, Harrison SC (2002). "Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin.". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13522–6. doi:10.1073/pnas.212504399. PMC 129706. PMID 12357034.  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.  Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (2003). "Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha.". Virology 303 (1): 174–80. doi:10.1006/viro.2002.1676. PMID 12482669.  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.  Bittinger MA, McWhinnie E, Meltzer J, et al. (2005). "Activation of cAMP response element-mediated gene expression by regulated nuclear transport of TORC proteins.". Curr. Biol. 14 (23): 2156–61. doi:10.1016/j.cub.2004.11.002. PMID 15589160.  Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.  Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.  Winslow MM, Gallo EM, Neilson JR, Crabtree GR (2006). "The calcineurin phosphatase complex modulates immunogenic B cell responses.". Immunity 24 (2): 141–52. doi:10.1016/j.immuni.2005.12.013. PMID 16473827.  Liu Q, Wilkins BJ, Lee YJ, et al. (2006). "Direct interaction and reciprocal regulation between ASK1 and calcineurin-NFAT control cardiomyocyte death and growth.". Mol. Cell. Biol. 26 (10): 3785–97. doi:10.1128/MCB.26.10.3785-3797.2006. PMC 1489013. PMID 16648474.  v · d · ePDB gallery 1aui: HUMAN CALCINEURIN HETERODIMER   1m63: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes   1mf8: Crystal Structure of human calcineurin complexed with cyclosporin A and human cyclophilin   1tco: TERNARY COMPLEX OF A CALCINEURIN A FRAGMENT, CALCINEURIN B, FKBP12 AND THE IMMUNOSUPPRESSANT DRUG FK506 (TACROLIMUS)   2p6b: Crystal Structure of Human Calcineurin in Complex with PVIVIT Peptide   This protein-related article is a stub. You can help Wikipedia by expanding it.v · d · e