PPP3CA

Protein phosphatase 3, catalytic subunit, alpha isozyme
PDB rendering based on 1aui.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1AUI​, 1M63​, 1MF8​, 2JOG​, 2JZI​, 2P6B​, 2R28​, 2W73​, 3LL8​, 4F0Z​, 4Q5U​
Identifiers
Symbols	PPP3CA ; CALN; CALNA; CALNA1; CCN1; CNA1; PPP2B
External IDs	OMIM: 114105 MGI: 107164 HomoloGene: 55497 ChEMBL: 4445 GeneCards: PPP3CA Gene
EC number	3.1.3.16
Gene ontology Molecular function • protein serine/threonine phosphatase activity • calcium ion binding • protein binding • calmodulin binding • drug binding • enzyme binding • calmodulin-dependent protein phosphatase activity • protein heterodimerization activity • protein dimerization activity Cellular component • nucleoplasm • cytoplasm • mitochondrion • cytosol • calcineurin complex • Z disc • sarcolemma Biological process • G1/S transition of mitotic cell cycle • response to amphetamine • stimulatory C-type lectin receptor signaling pathway • protein dephosphorylation • protein import into nucleus • calcium ion transport • transition between fast and slow fiber • cardiac muscle hypertrophy in response to stress • dephosphorylation • calcineurin-NFAT signaling cascade • multicellular organismal response to stress • negative regulation of chromatin binding • cellular response to drug • Fc-epsilon receptor signaling pathway • T cell activation • innate immune response • positive regulation of transcription from RNA polymerase II promoter • negative regulation of insulin secretion • skeletal muscle fiber development • negative regulation of dendrite morphogenesis • regulation of synaptic transmission • positive regulation of sequence-specific DNA binding transcription factor activity • positive regulation of NFAT protein import into nucleus • response to calcium ion • regulation of excitatory postsynaptic membrane potential • cellular response to glucose stimulus • positive regulation of cardiac muscle hypertrophy in response to stress Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5530	19055
Ensembl	ENSG00000138814	ENSMUSG00000028161
UniProt	Q08209	P63328
RefSeq (mRNA)	NM_000944	NM_001293622
RefSeq (protein)	NP_000935	NP_001280551
Location (UCSC)	Chr 4: 101.02 – 101.35 Mb	Chr 3: 136.67 – 136.94 Mb
PubMed search

Protein phosphatase 3, catalytic subunit, alpha isozyme is a protein that in humans is encoded by the PPP3CA gene.^[1]

References

1. "Entrez Gene: Protein phosphatase 3, catalytic subunit, alpha isozyme". Retrieved 2011-12-18.

Further reading

• Crabtree, G. R. (1999). "Generic signals and specific outcomes: Signaling through Ca2+, calcineurin, and NF-AT". Cell 96 (5): 611–614. doi:10.1016/S0092-8674(00)80571-1. PMID 10089876.
• Wang, H. G.; Pathan, N.; Ethell, I. M.; Krajewski, S.; Yamaguchi, Y.; Shibasaki, F.; McKeon, F.; Bobo, T.; Franke, T. F.; Reed, J. C. (1999). "Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD". Science 284 (5412): 339–343. doi:10.1126/science.284.5412.339. PMID 10195903.
• Fuentes, J. J.; Genescà, L.; Kingsbury, T. J.; Cunningham, K. W.; Pérez-Riba, M.; Estivill, X.; De La Luna, S. (2000). "DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-mediated signaling pathways". Human Molecular Genetics 9 (11): 1681–1690. doi:10.1093/hmg/9.11.1681. PMID 10861295.
• Frey, N.; Richardson, J. A.; Olson, E. N. (2000). "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins". Proceedings of the National Academy of Sciences 97 (26): 14632–14637. 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. (2001). "Expression of ZAKI-4 messenger ribonucleic acid in the brain during rat development and the effect of hypothyroidism". Endocrinology 142 (5): 1752–1759. doi:10.1210/en.142.5.1752. PMID 11316738.
• Graef, I. A.; Chen, F.; Chen, L.; Kuo, A.; Crabtree, G. R. (2001). "Signals transduced by Ca(2+)/calcineurin and NFATc3/c4 pattern the developing vasculature". Cell 105 (7): 863–875. doi:10.1016/S0092-8674(01)00396-8. PMID 11439183.
• Mukerjee, N.; McGinnis, K. M.; Gnegy, M. E.; Wang, K. K. W. (2001). "Caspase-Mediated Calcineurin Activation Contributes to IL-2 Release during T Cell Activation". Biochemical and Biophysical Research Communications 285 (5): 1192–1199. doi:10.1006/bbrc.2001.5278. PMID 11478781.
• Volkel, H.; Scholz, M.; Link, J.; Selzle, M.; Werner, P.; Tunnemann, R.; Jung, G.; Ludolph, A. C.; Reuter, A. (2001). "Superoxide dismutase mutations of familial amyotrophic lateral sclerosis and the oxidative inactivation of calcineurin". FEBS Letters 503 (2–3): 201–205. doi:10.1016/S0014-5793(01)02730-2. PMID 11513882.
• Esau, C.; Boes, M.; Youn, H. D.; Tatterson, L.; Liu, J. O.; Chen, J. (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): 1449–1459. doi:10.1084/jem.194.10.1449. PMC 2193671. PMID 11714752.
• Frey, N.; Olson, E. N. (2002). "Calsarcin-3, a Novel Skeletal Muscle-specific Member of the Calsarcin Family, Interacts with Multiple Z-disc Proteins". Journal of Biological Chemistry 277 (16): 13998–14004. doi:10.1074/jbc.M200712200. PMID 11842093.