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, DEE91
External IDs	OMIM: 114105; MGI: 107164; HomoloGene: 55497; GeneCards: PPP3CA; OMA:PPP3CA - orthologs
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 136,375,885 bp[2] End 136,643,488 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 23 endothelial cell middle temporal gyrus Region I of hippocampus proper postcentral gyrus Brodmann area 46 entorhinal cortex orbitofrontal cortex external globus pallidus pons Top expressed in olfactory tubercle hippocampus proper lateral septal nucleus globus pallidus nucleus accumbens anterior amygdaloid area lobe of cerebellum subiculum Region I of hippocampus proper prefrontal cortex 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 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 plasma membrane calcineurin complex nucleoplasm Z discdkac mitochondrion sarcolemma 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 DNA-binding transcription factor activity response to calcium ion Fc-epsilon receptor signaling pathway 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 by RNA polymerase II 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 human ageing 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: 136.38 – 136.64 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. Bibcode:1999Sci...284..339W. 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. Bibcode:2000PNAS...9714632F. 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/endo.142.5.8156. 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.