PROFILPELAJAR.COM

蛋白磷酸酶3，催化亚基，α同工酶
蛋白磷酸酶3，催化亚基，α同工酶
	PDB rendering based on 1aui.
有效结构
PDB	直系同源检索：PDBe, RCSB
PDB查询代码列表
	1AUI, 1M63, 1MF8, 2JOG, 2JZI, 2P6B, 2R28, 2W73
标识
代号	PPP3CA; CALN; CALNA; CALNA1; CCN1; CNA1; PPP2B
扩展标识	遗传学：114105 鼠基因：107164 同源基因：55497 GeneCards: PPP3CA Gene
EC編號	3.1.3.16
基因本体论描述
分子功能	· protein serine/threonine phosphatase activity; · calcium-dependent protein serine/threonine phosphatase activity; · calcium ion binding; · protein binding; · calmodulin binding; · hydrolase activity; · protein heterodimerization activity;
细胞成分	· soluble fraction; · insoluble fraction; · nucleus; · nucleolus; · cytoplasm; · mitochondrion; · microsome; · cytosol; · cytosol; · calcineurin complex; · membrane; · Z disc;
生物过程	· G1/S transition of mitotic cell cycle; · response to amphetamine; · protein dephosphorylation; · protein import into nucleus; · calcium ion transport; · response to stress; · positive regulation of transcription from RNA polymerase II promoter; · negative regulation of insulin secretion; · skeletal muscle fiber development; · regulation of synaptic transmission; · regulation of excitatory postsynaptic membrane potential; · cellular response to glucose stimulus;
	Sources: Amigo / QuickGO
RNA表达模式
	更多表达数据
直系同源体
物种	人类
Entrez	5530
Ensembl	ENSG00000138814
UniProt	Q08209
mRNA序列	NM_000944.4
蛋白序列	NP_000935.1
基因位置	Chr 4:; 101.94 – 102.27 Mb
PubMed查询	[1]
	查; 论; 编;

钙调磷酸酶^[1]（英語：Calcineurin，CaN）是钙和钙调蛋白依赖性的丝氨酸/苏氨酸蛋白磷酸酶；亦称为蛋白磷酸酶3（PPP3），旧称蛋白磷酸酶2B（PP2B）。其在体内的作用为启动T细胞并可以通过药物来阻断这一过程。

钙调磷酸酶为很多种免疫抑制药的作用对象如：环孢霉素，吡美莫司和他克莫司。

参考文献

^ 存档副本. [2021-12-09]. （原始内容存档于2021-12-09）.

深入阅读

Crabtree GR. Generic signals and specific outcomes: signaling through Ca2+, calcineurin, and NF-AT. Cell. 1999, 96 (5): 611–4. PMID 10089876. doi:10.1016/S0092-8674(00)80571-1.
Giri PR, Higuchi S, Kincaid RL. Chromosomal mapping of the human genes for the calmodulin-dependent protein phosphatase (calcineurin) catalytic subunit. Biochem. Biophys. Res. Commun. 1992, 181 (1): 252–8. PMID 1659808. doi:10.1016/S0006-291X(05)81410-X.
Kincaid RL, Giri PR, Higuchi S; et al. Cloning and characterization of molecular isoforms of the catalytic subunit of calcineurin using nonisotopic methods. J. Biol. Chem. 1990, 265 (19): 11312–9. PMID 2162844.
Guerini D, Klee CB. Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain. Proc. Natl. Acad. Sci. U.S.A. 1990, 86 (23): 9183–7. PMC 298458 . PMID 2556704. doi:10.1073/pnas.86.23.9183.
Kincaid RL, Nightingale MS, Martin BM. Characterization of a cDNA clone encoding the calmodulin-binding domain of mouse brain calcineurin. Proc. Natl. Acad. Sci. U.S.A. 1988, 85 (23): 8983–7. PMC 282646 . PMID 2848250. doi:10.1073/pnas.85.23.8983.
Coghlan VM, Perrino BA, Howard M; et al. Association of protein kinase A and protein phosphatase 2B with a common anchoring protein. Science. 1995, 267 (5194): 108–11. PMID 7528941. doi:10.1126/science.7528941.
Griffith JP, Kim JL, Kim EE; et al. X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell. 1995, 82 (3): 507–22. PMID 7543369. doi:10.1016/0092-8674(95)90439-5.
Shibasaki F, McKeon F. Calcineurin functions in Ca(2+)-activated cell death in mammalian cells. J. Cell Biol. 1995, 131 (3): 735–43. PMC 2120616 . PMID 7593193. doi:10.1083/jcb.131.3.735.
Muramatsu T, Kincaid RL. Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). Biochim. Biophys. Acta. 1993, 1178 (1): 117–20. PMID 8392375. doi:10.1016/0167-4889(93)90117-8.
Cameron AM, Steiner JP, Roskams AJ; et al. Calcineurin associated with the inositol 1,4,5-trisphosphate receptor-FKBP12 complex modulates Ca2+ flux. Cell. 1996, 83 (3): 463–72. PMID 8521476. doi:10.1016/0092-8674(95)90124-8.
Kissinger CR, Parge HE, Knighton DR; et al. Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature. 1996, 378 (6557): 641–4. PMID 8524402. doi:10.1038/378641a0.
Wang MG, Yi H, Guerini D; et al. 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. 1997, 72 (2-3): 236–41. PMID 8978785. doi:10.1159/000134198.
Shibasaki F, Kondo E, Akagi T, McKeon F. Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2. Nature. 1997, 386 (6626): 728–31. PMID 9109491. doi:10.1038/386728a0.
Kashishian A, Howard M, Loh C; et al. AKAP79 inhibits calcineurin through a site distinct from the immunophilin-binding region. J. Biol. Chem. 1998, 273 (42): 27412–9. PMID 9765270. doi:10.1074/jbc.273.42.27412.
Wang HG, Pathan N, Ethell IM; et al. Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD. Science. 1999, 284 (5412): 339–43. PMID 10195903. doi:10.1126/science.284.5412.339.
Fuentes JJ, Genescà L, Kingsbury TJ; et al. DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-mediated signaling pathways. Hum. Mol. Genet. 2000, 9 (11): 1681–90. PMID 10861295. doi:10.1093/hmg/9.11.1681.
Hartley JL, Temple GF, Brasch MA. DNA cloning using in vitro site-specific recombination. Genome Res. 2001, 10 (11): 1788–95. PMC 310948 . PMID 11076863. doi:10.1101/gr.143000.
Frey N, Richardson JA, Olson EN. Calsarcins, a novel family of sarcomeric calcineurin-binding proteins. Proc. Natl. Acad. Sci. U.S.A. 2001, 97 (26): 14632–7. PMC 18970 . PMID 11114196. doi:10.1073/pnas.260501097.
Siddiq A, Miyazaki T, Takagishi Y; et al. Expression of ZAKI-4 messenger ribonucleic acid in the brain during rat development and the effect of hypothyroidism. Endocrinology. 2001, 142 (5): 1752–9. PMID 11316738. doi:10.1210/en.142.5.1752.