PPP3CA

Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (PP2BA) is a protein that in humans is encoded by the PPP3CA gene.[5][6]

PPP3CA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1AUI, 1M63, 1MF8, 2JOG, 2JZI, 2P6B, 2R28, 2W73, 3LL8, 4F0Z, 4Q5U, 5C1V
Identifiers
Aliases	PPP3CA, CALN, CALNA, CALNA1, CCN1, CNA1, PPP2B, protein phosphatase 3 catalytic subunit alpha, IECEE, IECEE1, ACCIID
External IDs	OMIM: 114105 MGI: 107164 HomoloGene: 55497 GeneCards: PPP3CA
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q24 Start 101,023,409 bp[1] End 101,348,278 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 G3 Start 136,670,124 bp[2] End 136,937,727 bp[2]
RNA expression pattern 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 • GO:0001948 protein binding • drug binding • protein heterodimerization activity • enzyme binding • calcium-dependent protein serine/threonine phosphatase activity • hydrolase activity • cyclosporin A binding • calmodulin-dependent protein phosphatase activity Cellular component • membrane • cell membrane • calcineurin complex • nucleoplasm • Z disc • mitochondrion • sarcolemma • cell nucleus • cytosol • cytoplasm • cytoplasmic side of plasma membrane • dendritic spine • slit diaphragm • cell projection • synapse • Schaffer collateral - CA1 synapse • glutamatergic synapse Biological process • multicellular organismal response to stress • negative regulation of insulin secretion • protein import into nucleus • transition between fast and slow fiber • negative regulation of chromatin binding • response to amphetamine • modulation of chemical synaptic transmission • positive regulation of sequence-specific DNA binding transcription factor activity • response to calcium ion • Fc-epsilon receptor signaling pathway • cellular response to drug • cardiac muscle hypertrophy in response to stress • negative regulation of dendrite morphogenesis • skeletal muscle fiber development • positive regulation of cardiac muscle hypertrophy in response to stress • excitatory postsynaptic potential • T cell activation • cellular response to glucose stimulus • calcium ion transport • calcium-mediated signaling • dephosphorylation • positive regulation of transcription from RNA polymerase II promoter • Wnt signaling pathway, calcium modulating pathway • positive regulation of cardiac muscle hypertrophy • positive regulation of gene expression • negative regulation of gene expression • negative regulation of production of miRNAs involved in gene silencing by miRNA • positive regulation of connective tissue replacement • positive regulation of endocytosis • G1/S transition of mitotic cell cycle • protein dephosphorylation • calcineurin-NFAT signaling cascade • positive regulation of calcineurin-NFAT signaling cascade • brain development • positive regulation of cell migration • skeletal muscle tissue regeneration • positive regulation of cell adhesion • calcineurin-mediated signaling • postsynaptic modulation of chemical synaptic transmission • aging • peptidyl-serine dephosphorylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5530	19055
Ensembl	ENSG00000138814	ENSMUSG00000028161
UniProt	Q08209	P63328
RefSeq (mRNA)	NM_001130692 NM_000944 NM_001130691	NM_001293622 NM_008913
RefSeq (protein)	NP_000935 NP_001124163 NP_001124164	NP_001280551 NP_032939
Location (UCSC)	Chr 4: 101.02 – 101.35 Mb	Chr 3: 136.67 – 136.94 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000138814 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028161 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Universal protein resource accession number Q08209 for "Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform" at UniProt.
6. "Entrez Gene: Protein phosphatase 3, catalytic subunit, alpha isozyme". Retrieved 2011-12-18.

Further reading

• Crabtree GR (March 1999). "Generic signals and specific outcomes: signaling through Ca2+, calcineurin, and NF-AT". Cell. 96 (5): 611–4. doi:10.1016/S0092-8674(00)80571-1. PMID 10089876. S2CID 8817053.
• Wang HG, Pathan N, Ethell IM, Krajewski S, Yamaguchi Y, Shibasaki F, McKeon F, Bobo T, Franke TF, Reed JC (April 1999). "Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD". Science. 284 (5412): 339–43. doi:10.1126/science.284.5412.339. PMID 10195903.
• Fuentes JJ, Genescà L, Kingsbury TJ, Cunningham KW, Pérez-Riba M, Estivill X, de la Luna S (July 2000). "DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-mediated signaling pathways". Human Molecular Genetics. 9 (11): 1681–90. doi:10.1093/hmg/9.11.1681. PMID 10861295.
• Frey N, Richardson JA, Olson EN (December 2000). "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins". Proceedings of the National Academy of Sciences of the United States of America. 97 (26): 14632–7. doi:10.1073/pnas.260501097. PMC 18970. PMID 11114196.
• Siddiq A, Miyazaki T, Takagishi Y, Kanou Y, Hayasaka S, Inouye M, Seo H, Murata Y (May 2001). "Expression of ZAKI-4 messenger ribonucleic acid in the brain during rat development and the effect of hypothyroidism". Endocrinology. 142 (5): 1752–9. doi:10.1210/en.142.5.1752. PMID 11316738.
• Graef IA, Chen F, Chen L, Kuo A, Crabtree GR (June 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. S2CID 5278706.
• Mukerjee N, McGinnis KM, Gnegy ME, Wang KK (August 2001). "Caspase-mediated calcineurin activation contributes to IL-2 release during T cell activation". Biochemical and Biophysical Research Communications. 285 (5): 1192–9. CiteSeerX 10.1.1.414.4108. doi:10.1006/bbrc.2001.5278. PMID 11478781.
• Volkel H, Scholz M, Link J, Selzle M, Werner P, Tunnemann R, Jung G, Ludolph AC, Reuter A (August 2001). "Superoxide dismutase mutations of familial amyotrophic lateral sclerosis and the oxidative inactivation of calcineurin". FEBS Letters. 503 (2–3): 201–5. doi:10.1016/S0014-5793(01)02730-2. PMID 11513882. S2CID 44432580.
• Esau C, Boes M, Youn HD, Tatterson L, Liu JO, Chen J (November 2001). "Deletion of calcineurin and myocyte enhancer factor 2 (MEF2) binding domain of Cabin1 results in enhanced cytokine gene expression in T cells". The Journal of Experimental Medicine. 194 (10): 1449–59. doi:10.1084/jem.194.10.1449. PMC 2193671. PMID 11714752.
• Frey N, Olson EN (April 2002). "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins". The Journal of Biological Chemistry. 277 (16): 13998–4004. doi:10.1074/jbc.M200712200. PMID 11842093.