骨骼肌肌动蛋白α1(英语:Skeletal muscle, actin alpha 1)是一种在人类中由ACTA1基因编码的蛋白质。[6][7]
Quick Facts 骨骼肌肌动蛋白α1, 已知的结构 ...
骨骼肌肌动蛋白α1 |
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识别号 |
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别名 | ACTA1;, ACTA, ASMA, CFTD, CFTD1, CFTDM, MPFD, NEM1, NEM2, NEM3, Actin, alpha 1, SHPM, actin, alpha 1, skeletal muscle, actin alpha 1, skeletal muscle |
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外部ID | OMIM:102610 MGI:87909 HomoloGene:121702 GeneCards:ACTA1 |
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相关疾病 |
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congenital myopathy with excess of thin filaments[1] |
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RNA表达模式 |
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查阅更多表达数据 |
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直系同源 |
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物种 | 人类 | 小鼠 |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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mRNA序列 | | |
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蛋白序列 | | |
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基因位置(UCSC) | Chr 1: 229.43 – 229.43 Mb | Chr 19: 34.22 – 34.23 Mb |
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PubMed查找 | [4] | [5] |
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维基数据 |
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在骨骼肌中表达的肌动蛋白α1是已鉴定的六种不同肌动蛋白亚型之一。肌动蛋白是高度保守的蛋白质,它们参与细胞运动、结构和完整性。α肌动蛋白是收缩装置的主要成分。[8]
骨骼α肌动蛋白的表达是由已知会导致肌肉形成的刺激和条件诱导的。[9]这种情况导致定型细胞(卫星细胞)融合到肌管中,形成肌纤维。骨骼肌动蛋白本身在表达时会引起其他几种“生肌基因”的表达,这些基因对肌肉形成至关重要。[10]激活骨骼肌动蛋白基因表达的一个关键转录因子是血清反应因子,一种结合肌动蛋白基因启动子DNA上特定位点的蛋白质。[11]血清反应因子可以将许多其他蛋白质带到骨骼肌动蛋白的启动子,例如雄激素受体,从而有助于通过雄激素(通常称为合成代谢)类固醇诱导骨骼肌动蛋白基因表达。[12]
肌动蛋白α1已被证明与TMSB4X、[13][14]MIB2[15]和PRKCE产生相互作用。[16]
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- Ogawa H, Shiraki H, Matsuda Y, Nakagawa H. Interaction of adenylosuccinate synthetase with F-actin. European Journal of Biochemistry. April 1978, 85 (2): 331–7. PMID 648524. doi:10.1111/j.1432-1033.1978.tb12243.x.
- den Hartigh JC, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J. The EGF receptor is an actin-binding protein. The Journal of Cell Biology. October 1992, 119 (2): 349–55. PMC 2289650 . PMID 1383230. doi:10.1083/jcb.119.2.349.
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- Levine BA, Moir AJ, Patchell VB, Perry SV. Binding sites involved in the interaction of actin with the N-terminal region of dystrophin. FEBS Letters. February 1992, 298 (1): 44–8. PMID 1544421. doi:10.1016/0014-5793(92)80019-D .
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- Tomasselli AG, Hui JO, Adams L, Chosay J, Lowery D, Greenberg B, Yem A, Deibel MR, Zürcher-Neely H, Heinrikson RL. Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. The Journal of Biological Chemistry. August 1991, 266 (22): 14548–53. PMID 1907279. doi:10.1016/S0021-9258(18)98721-1 .
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- Takahashi K, Hiwada K, Kokubu T. Vascular smooth muscle calponin. A novel troponin T-like protein. Hypertension. June 1988, 11 (6 Pt 2): 620–6. PMID 2455687. doi:10.1161/01.hyp.11.6.620 .
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- Burgess DR, Broschat KO, Hayden JM. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. The Journal of Cell Biology. January 1987, 104 (1): 29–40. PMC 2117036 . PMID 3793760. doi:10.1083/jcb.104.1.29.
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- Hanauer A, Levin M, Heilig R, Daegelen D, Kahn A, Mandel JL. Isolation and characterization of cDNA clones for human skeletal muscle alpha actin. Nucleic Acids Research. June 1983, 11 (11): 3503–16. PMC 325982 . PMID 6190133. doi:10.1093/nar/11.11.3503.
- Bretscher A, Weber K. Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner. Cell. July 1980, 20 (3): 839–47. PMID 6893424. S2CID 568395. doi:10.1016/0092-8674(80)90330-X.