プロテインホスファターゼ2B
- 関
- calcineurin、PP2B
WordNet
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
- any of a group of enzymes that act as a catalyst in the hydrolysis of organic phosphates
PrepTutorEJDIC
- 蛋白(たんばく)質
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/06/30 08:34:43」(JST)
[Wiki en表示]
PPP3CA |
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Available structures |
PDB |
Ortholog search: PDBe RCSB |
List of PDB id codes |
1AUI, 1M63, 1MF8, 2JOG, 2JZI, 2P6B, 2R28, 2W73, 3LL8, 4F0Z, 4Q5U, 5C1V
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Identifiers |
Aliases |
PPP3CA, CALN, CALNA, CALNA1, CCN1, CNA1, PPP2B, protein phosphatase 3 catalytic subunit alpha |
External IDs |
MGI: 107164 HomoloGene: 55497 GeneCards: 5530 |
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Genetically Related Diseases |
Disease Name |
References |
anorexia nervosa |
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Gene ontology |
Molecular function |
• calcium ion binding
• phosphoprotein phosphatase activity
• protein dimerization activity
• calmodulin-dependent protein phosphatase activity
• protein serine/threonine phosphatase activity
• metal ion binding
• calmodulin binding
• protein binding
• drug binding
• protein heterodimerization activity
• enzyme binding
• calcium-dependent protein serine/threonine phosphatase activity
• hydrolase activity
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Cellular component |
• postsynapse
• cytoplasm
• cytosol
• membrane
• plasma membrane
• calcineurin complex
• nucleoplasm
• Z disc
• mitochondrion
• sarcolemma
• nucleus
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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
• G1/S transition of mitotic cell cycle
• response to amphetamine
• protein dephosphorylation
• calcineurin-NFAT signaling cascade
• modulation of synaptic transmission
• positive regulation of sequence-specific DNA binding transcription factor activity
• stimulatory C-type lectin receptor signaling pathway
• 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
• positive regulation of NFAT protein import into nucleus
• innate immune response
• T cell activation
• cellular response to glucose stimulus
• calcium ion transport
• calcium-mediated signaling
• dephosphorylation
• positive regulation of transcription from RNA polymerase II promoter
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Sources:Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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NM_001130692
NM_000944
NM_001130691
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RefSeq (protein) |
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NP_000935.1
NP_001124163.1
NP_001124164.1
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NP_001280551.1
NP_032939.1
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Location (UCSC) |
Chr 4: 101.02 – 101.35 Mb |
Chr 3: 136.67 – 136.94 Mb |
PubMed search |
[2] |
[3] |
Wikidata |
View/Edit Human |
View/Edit Mouse |
Protein phosphatase 3, catalytic subunit, alpha isozyme is a protein that in humans is encoded by the PPP3CA gene.[1]
References
- ^ "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.
UpToDate Contents
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English Journal
- Targeting Transient Receptor Potential Channels by MicroRNAs Drives Tumor Development and Progression.
- Santoni G, Morelli MB, Santoni M, Nabissi M, Marinelli O, Amantini C.
- Advances in experimental medicine and biology. 2020 ;1131()605-623.
- Transient receptor potential (TRP) cation channel superfamily plays important roles in a variety of cellular processes such polymodal cellular sensing, adhesion, polarity, proliferation, differentiation and apoptosis. The expression of TRP channels is strictly regulated and their de-regulation can s
- PMID 31646527
- Canonical Transient Potential Receptor-3 Channels in Normal and Diseased Airway Smooth Muscle Cells.
- Wang YX, Wang L, Zheng YM.
- Advances in experimental medicine and biology. 2020 ;1131()471-487.
- All seven canonical transient potential receptor (TRPC1-7) channel members are expressed in mammalian airway smooth muscle cells (ASMCs). Among this family, TRPC3 channel plays an important role in the control of the resting [Ca] and agonist-induced increase in [Ca]. This channel is significantly up
- PMID 31646521
- An Update to Calcium Binding Proteins.
- Elíes J, Yáñez M, Pereira TMC, Gil-Longo J, MacDougall DA, Campos-Toimil M.
- Advances in experimental medicine and biology. 2020 ;1131()183-213.
- Ca binding proteins (CBP) are of key importance for calcium to play its role as a pivotal second messenger. CBP bind Ca in specific domains, contributing to the regulation of its concentration at the cytosol and intracellular stores. They also participate in numerous cellular functions by acting as
- PMID 31646511
Japanese Journal
- Regulation of the catalytic domain of protein phosphatase 1 by the terminal region of protein phosphatase 2B
- WANG Bai J.,TANG Wei,ZHANG Peng,WEI Qun
- The journal of biochemistry 151(3), 283-290, 2012-03-01
- NAID 10031166067
- Regulation of the catalytic domain of protein phosphatase 1 by the terminal region of protein phosphatase 2B
- Wang Bai J.,Tang Wei,Zhang Peng [他]
- Journal of Biochemistry 151(3), 283-290, 2012-03
- NAID 40019186005
- Interaction of Protein Phosphatase 1δ with Nucleophosmin in Human Osteoblastic Cells
- Haneji Tatsuji,Teramachi Jumpei,Hirashima Kanji,Kimura Koji,Morimoto Hiroyuki
- ACTA HISTOCHEMICA ET CYTOCHEMICA 45(1), 1-7, 2012
- … Protein phosphorylation and dephosphorylation has been recognized as an essential mechanism in the regulation of cellular metabolism and function in various tissues. … Serine and threonine protein phosphatases (PP) are divided into four categories: PP1, PP2A, PP2B, and PP2C. … Anti-PP1δ antibody recognized a protein present in the nucleolar regions in Saos-2 cells. …
- NAID 130001258485
Related Links
- Protein phosphatase 2 (PP2), also known as PP2A, is an enzyme that in humans is encoded by the PPP2CA gene. The PP2A heterotrimeric protein phosphatase, is a ubiquitous and conserved Serine/Threonine phosphatase with broad ...
★リンクテーブル★
[★]
- 英
- calcineurin, CN, CNR
- 同
- プロテインホスファターゼ2B protein phosphatase 2B、カルシニュリン、カルシノイリン
- 関
- IL-2、免疫抑制薬
[show details]
- Ca2+/カルモジュリン複合体依存性のセリン/スレオニン脱リン酸化酵素である。
- サブユニットAとサブユニットBからなるヘテロダイマー。
- 免疫抑制薬の標的分子となりえて、例えばシクロスポリンAやFK506などのカルシニューリン阻害薬によりT細胞中のカルシニューリンが阻害されることでIL-2の発現が低下し、結果としてT細胞の増殖が妨げられ免疫抑制が起こる。
[★]
- 関
- calcineurin、protein phosphatase 2B
[★]
- 英
- protein phosphatase 2B、PP2B
- 関
- カルシニューリン
[★]
ホスファターゼ、フォスファターゼ、脱リン酸化酵素、脱リン酸酵素
- 関
- phosphohydrolase、phosphoric monoester hydrolase
[★]
蛋白質ホスファターゼ