PPP3CB

PPP3CB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4OR9, 4ORA, 4ORC
Identifiers
Aliases	PPP3CB, CALNA2, CALNB, CNA2, PP2Bbeta, protein phosphatase 3 catalytic subunit beta
External IDs	MGI: 107163 HomoloGene: 56429 GeneCards: PPP3CB
Gene ontology Molecular function • calcium ion binding • phosphoprotein phosphatase activity • protein dimerization activity • protein serine/threonine phosphatase activity • calmodulin-dependent protein phosphatase activity • metal ion binding • calmodulin binding • protein binding • drug binding • enzyme binding • protein phosphatase 2B binding • hydrolase activity Cellular component • cytosol • T-tubule • plasma membrane • calcineurin complex • nucleoplasm • Z disc Biological process • response to cytokine • lymphangiogenesis • regulation of insulin secretion • protein dephosphorylation • calcineurin-NFAT signaling cascade • memory • learning • regulation of synaptic plasticity • T cell homeostasis • positive regulation of transcription, DNA-templated • negative regulation of T cell mediated cytotoxicity • T cell proliferation • Fc-epsilon receptor signaling pathway • protein phosphorylation • heart development • T cell differentiation • cellular response to drug • positive regulation of NFAT protein import into nucleus • axon extension • regulation of gene expression • social behavior • positive regulation of insulin secretion involved in cellular response to glucose stimulus • locomotion involved in locomotory behavior • T cell activation • positive regulation of transcription from RNA polymerase II promoter • calcium ion regulated exocytosis • signal transduction • dephosphorylation • Wnt signaling pathway, calcium modulating pathway Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5532	19056
Ensembl	ENSG00000107758	ENSMUSG00000021816
UniProt	P16298	P48453
RefSeq (mRNA)	NM_001142353 NM_001142354 NM_001289968 NM_001289969 NM_021132	NM_008914 NM_001310426 NM_001310427
RefSeq (protein)	NP_001135825.1 NP_001135826.1 NP_001276897.1 NP_001276898.1 NP_066955.1	NP_001297355.1 NP_001297356.1 NP_032940.1
Location (UCSC)	Chr 10: 73.44 – 73.5 Mb	Chr 14: 20.5 – 20.55 Mb
PubMed search	[1]	[2]
Wikidata

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Serine/threonine-protein phosphatase 2C catalytic subunit beta isoform is an enzyme that in humans is encoded by the PPP3CB gene.^[3][4][5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Giri PR, Higuchi S, Kincaid RL (Jan 1992). "Chromosomal mapping of the human genes for the calmodulin-dependent protein phosphatase (calcineurin) catalytic subunit". Biochem Biophys Res Commun. 181 (1): 252–8. doi:10.1016/S0006-291X(05)81410-X. PMID 1659808.
4. 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. doi:10.1089/dna.1.1989.8.675. PMID 2558868.
5. "Entrez Gene: PPP3CB protein phosphatase 3 (formerly 2B), catalytic subunit, beta isoform".

Further reading

• Chen MX, Chen YH, Cohen PT (1992). "Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases.". FEBS Lett. 306 (1): 54–8. doi:10.1016/0014-5793(92)80836-6. PMID 1321058.
• McPartlin AE, Barker HM, Cohen PT (1991). "Identification of a third alternatively spliced cDNA encoding the catalytic subunit of protein phosphatase 2B beta.". Biochim. Biophys. Acta. 1088 (2): 308–10. doi:10.1016/0167-4781(91)90069-x. PMID 1848109.
• Guerini D, Klee CB (1990). "Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain.". Proc. Natl. Acad. Sci. U.S.A. 86 (23): 9183–7. doi:10.1073/pnas.86.23.9183. PMC 298458. PMID 2556704.
• Shibasaki F, McKeon F (1995). "Calcineurin functions in Ca(2+)-activated cell death in mammalian cells.". J. Cell Biol. 131 (3): 735–43. doi:10.1083/jcb.131.3.735. PMC 2120616. PMID 7593193.
• Muramatsu T, Kincaid RL (1993). "Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha).". Biochim. Biophys. Acta. 1178 (1): 117–20. doi:10.1016/0167-4889(93)90117-8. PMID 8392375.
• 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.
• Wang MG, Yi H, Guerini D, et al. (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.
• Sun L, Youn HD, Loh C, et al. (1998). "Cabin 1, a negative regulator for calcineurin signaling in T lymphocytes.". Immunity. 8 (6): 703–11. doi:10.1016/S1074-7613(00)80575-0. PMID 9655484.
• Aramburu J, Garcia-Cózar F, Raghavan A, et al. (1998). "Selective inhibition of NFAT activation by a peptide spanning the calcineurin targeting site of NFAT.". Mol. Cell. 1 (5): 627–37. doi:10.1016/S1097-2765(00)80063-5. PMID 9660947.
• Okamura H, Aramburu J, García-Rodríguez C, et al. (2000). "Concerted dephosphorylation of the transcription factor NFAT1 induces a conformational switch that regulates transcriptional activity.". Mol. Cell. 6 (3): 539–50. doi:10.1016/S1097-2765(00)00053-8. PMID 11030334.
• Frey N, Richardson JA, Olson EN (2001). "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins.". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14632–7. doi:10.1073/pnas.260501097. PMC 18970. PMID 11114196.
• Esau C, Boes M, Youn HD, et al. (2001). "Deletion of calcineurin and myocyte enhancer factor 2 (MEF2) binding domain of Cabin1 results in enhanced cytokine gene expression in T cells.". J. Exp. Med. 194 (10): 1449–59. doi:10.1084/jem.194.10.1449. PMC 2193671. PMID 11714752.
• Frey N, Olson EN (2002). "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins.". J. Biol. Chem. 277 (16): 13998–4004. doi:10.1074/jbc.M200712200. PMID 11842093.
• Banerjee A, Banks AS, Nawijn MC, et al. (2002). "Cutting edge: Suppressor of cytokine signaling 3 inhibits activation of NFATp.". J. Immunol. 168 (9): 4277–81. doi:10.4049/jimmunol.168.9.4277. PMID 11970967.
• 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.
• Genescà L, Aubareda A, Fuentes JJ, et al. (2003). "Phosphorylation of calcipressin 1 increases its ability to inhibit calcineurin and decreases calcipressin half-life.". Biochem. J. 374 (Pt 2): 567–75. doi:10.1042/BJ20030267. PMC 1223619. PMID 12809556.
• Bell O, Gaberman E, Kilav R, et al. (2005). "The protein phosphatase calcineurin determines basal parathyroid hormone gene expression.". Mol. Endocrinol. 19 (2): 516–26. doi:10.1210/me.2004-0108. PMID 15514034.