PPP3CB

PPP3CB
Identifiers
Aliases	PPP3CB, CALNA2, CALNB, CNA2, PP2Bbeta, protein phosphatase 3 catalytic subunit beta
External IDs	OMIM: 114106; MGI: 107163; HomoloGene: 56429; GeneCards: PPP3CB; OMA:PPP3CB - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4OR9, 4ORA, 4ORC
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.1.3.16 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 10 (human) Band 10q22.2 Start 73,436,433 bp End 73,496,024 bp
Gene location (Mouse) Chr. Chromosome 14 (mouse) Band 14|14 A3 Start 20,549,432 bp End 20,596,641 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell Skeletal muscle tissue of rectus abdominis biceps brachii Skeletal muscle tissue of biceps brachii middle temporal gyrus vastus lateralis muscle lateral nuclear group of thalamus superior frontal gyrus orbitofrontal cortex glutes Top expressed in subiculum dorsal striatum triceps brachii muscle olfactory tubercle lateral septal nucleus anterior amygdaloid area medial dorsal nucleus temporal muscle nucleus accumbens sternocleidomastoid muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding phosphoprotein phosphatase activity protein dimerization activity protein serine/threonine phosphatase activity metal ion binding calmodulin binding protein binding enzyme binding protein phosphatase 2B binding hydrolase activity calmodulin-dependent protein phosphatase activity Cellular component cytosol T-tubule plasma membrane calcineurin complex nucleoplasm Z discdkac cytoplasm glutamatergic synapse Biological process response to cytokine lymphangiogenesis regulation of insulin secretion 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 development of the heart T cell differentiation 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 by RNA polymerase II calcium-ion regulated exocytosis signal transduction dephosphorylation Wnt signaling pathway, calcium modulating pathway protein dephosphorylation regulation of synaptic vesicle endocytosis calcineurin-mediated signaling Sources:Amigo / QuickGO
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 NP_001135826 NP_001276897 NP_001276898 NP_066955 NP_001297355 NP_001297356 NP_032940 Location (UCSC) Chr 10: 73.44 – 73.5 Mb Chr 14: 20.55 – 20.6 Mb PubMed search
Wikidata
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Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (PP2BB) is an enzyme that in humans is encoded by the PPP3CB gene.

Function and Location

Enables different functions, including calmodulin dependent protein phosphatase: calmodulin binding; and binding protein phosphatase 2B.

Calcinuerin-NFAT signaling; lysosome organization; protein regulation to nucleaus.

Location

Found in the cytoplasm, and is a part of the calcinuerin complex.

Can be related with biomarkers of focal segments of schizophrenia.

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. S2CID 31397906.
• 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. Bibcode:1995Natur.378..641K. doi:10.1038/378641a0. PMID 8524402. S2CID 4337105.
• 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. Bibcode:2000PNAS...9714632F. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 27672093.