骨骼肌肌动蛋白α1

2023-03-08 11:45| 来源: 网络整理| 查看: 265

ACTA1已知的結構PDB直系同源搜索: PDBe RCSB PDBID列表

1T44

識別號别名ACTA1；, ACTA, ASMA, CFTD, CFTD1, CFTDM, MPFD, NEM1, NEM2, NEM3, Actin, alpha 1, SHPM, actin, alpha 1, skeletal muscle, actin alpha 1, skeletal muscle外部IDOMIM：102610 MGI：87902 HomoloGene：121702 GeneCards：ACTA1 基因位置（人类）染色体1號染色體[1]基因座1q42.13起始229,430,365 bp[1]终止229,434,104 bp[1]基因位置（小鼠）染色体小鼠8号染色体[2]基因座8 E2|8 72.26 cM起始124,618,508 bp[2]终止124,621,490 bp[2]RNA表达模式查阅更多表达数据基因本體分子功能• 核苷酸結合• myosin binding• ADP binding• structural constituent of cytoskeleton• 血浆蛋白结合• ATP結合細胞組分• 細胞質• cell body• 细胞质基质• blood microparticle• 絲狀偽足• 肌节• striated muscle thin filament• 应力纤维• 细胞外液• 微丝• actin cytoskeleton• 外排體• 细胞骨架• 板状伪足生物學過程• 肌肉收缩• response to steroid hormone• skeletal muscle fiber adaptation• response to mechanical stimulus• skeletal muscle thin filament assembly• response to lithium ion• 增殖• positive regulation of gene expression• muscle filament sliding• mesenchyme migration• response to extracellular stimulus• skeletal muscle fiber developmentSources:Amigo / QuickGO直系同源物種人類小鼠Entrez

11459

Ensembl

ENSG00000143632

ENSMUSG00000031972

UniProt

P68133

P68134

mRNA序列

NM_001100

NM_001272041NM_009606

蛋白序列

NP_001091

NP_001258970NP_033736

基因位置（UCSC）Chr 1: 229.43 – 229.43 MbChr 8: 124.62 – 124.62 MbPubMed查找[3][4]維基數據檢視/編輯人類檢視/編輯小鼠

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。[5][6]

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。[7]

目录 1 骨骼肌肌动蛋白基因表达 2 相互作用 3 参见 4 参考资料 5 延申阅读 6 外部链接骨骼肌肌动蛋白基因表达[编辑]

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。[8]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。[9]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。[10]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。[11]

相互作用[编辑]

肌动蛋白α1已被证明与TMSB4X、[12][13]MIB2[14]和PRKCE产生相互作用。[15]

参见[编辑] 肌动蛋白 β-肌动蛋白参考资料[编辑] ^ 1.0 1.1 1.2 GRCh38: Ensembl release 89: ENSG00000143632 - Ensembl, May 2017 ^ 2.0 2.1 2.2 GRCm38: Ensembl release 89: ENSMUSG00000031972 - Ensembl, May 2017 ^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine. ^ Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine. ^ Mogensen J, Kruse TA, Børglum AD. Assignment of the human skeletal muscle [FC12]a-actin gene (ACTA1) to chromosome 1q42.13-->q42.2 by radiation hybrid mapping. Cytogenetics and Cell Genetics. March 1999, 83 (3–4): 224–5. PMID 10072583. S2CID 84202330. doi:10.1159/000015184. ^ Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L. Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed. Molecular and Cellular Biology. May 1983, 3 (5): 787–95. PMC 368601 . PMID 6865942. doi:10.1128/mcb.3.5.787. ^ Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle. ^ Bandman E. Contractile protein isoforms in muscle development. Developmental Biology. December 1992, 154 (2): 273–83. PMID 1358730. doi:10.1016/0012-1606(92)90067-Q. ^ Gunning PW, Ferguson V, Brennan KJ, Hardeman EC. Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle. Journal of Cell Science. February 2001, 114 (Pt 3): 513–24. PMID 11171321. doi:10.1242/jcs.114.3.513. ^ Belaguli NS, Zhou W, Trinh TH, Majesky MW, Schwartz RJ. Dominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targets. Molecular and Cellular Biology. July 1999, 19 (7): 4582–91. PMC 84256 . PMID 10373507. doi:10.1128/mcb.19.7.4582. ^ Vlahopoulos S, Zimmer WE, Jenster G, Belaguli NS, Balk SP, Brinkmann AO, Lanz RB, Zoumpourlis VC, Schwartz RJ. Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene. The Journal of Biological Chemistry. March 2005, 280 (9): 7786–92. PMID 15623502. doi:10.1074/jbc.M413992200 . ^ Ballweber E, Hannappel E, Huff T, Stephan H, Haener M, Taschner N, Stoffler D, Aebi U, Mannherz HG. Polymerisation of chemically cross-linked actin:thymosin beta(4) complex to filamentous actin: alteration in helical parameters and visualisation of thymosin beta(4) binding on F-actin. Journal of Molecular Biology. January 2002, 315 (4): 613–25. PMID 11812134. doi:10.1006/jmbi.2001.5281. ^ Safer D, Sosnick TR, Elzinga M. Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. Biochemistry. May 1997, 36 (19): 5806–16. PMID 9153421. doi:10.1021/bi970185v. ^ Takeuchi T, Heng HH, Ye CJ, Liang SB, Iwata J, Sonobe H, Ohtsuki Y. Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma. The American Journal of Pathology. October 2003, 163 (4): 1395–404. PMC 1868282 . PMID 14507647. doi:10.1016/S0002-9440(10)63497-9. ^ England K, Ashford D, Kidd D, Rumsby M. PKC epsilon is associated with myosin IIA and actin in fibroblasts. Cellular Signalling. June 2002, 14 (6): 529–36. PMID 11897493. doi:10.1016/S0898-6568(01)00277-7. 延申阅读[编辑] Snásel J, Pichová I. The cleavage of host cell proteins by HIV-1 protease. Folia Biologica. 1997, 42 (5): 227–30. PMID 8997639. S2CID 7617882. doi:10.1007/BF02818986. Di Fiore PP, Scita G. Eps8 in the midst of GTPases. The International Journal of Biochemistry & Cell Biology. October 2002, 34 (10): 1178–83. PMID 12127568. doi:10.1016/S1357-2725(02)00064-X. 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. Adams LD, Tomasselli AG, Robbins P, Moss B, Heinrikson RL. HIV-1 protease cleaves actin during acute infection of human T-lymphocytes. AIDS Research and Human Retroviruses. February 1992, 8 (2): 291–5. PMID 1540415. doi:10.1089/aid.1992.8.291. 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 . Rijken PJ, Hage WJ, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J. Epidermal growth factor induces rapid reorganization of the actin microfilament system in human A431 cells. Journal of Cell Science. November 1991,. 100 ( Pt 3) (3): 491–9. PMID 1808202. doi:10.1242/jcs.100.3.491 . 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 . Shoeman RL, Kesselmier C, Mothes E, Höner B, Traub P. Non-viral cellular substrates for human immunodeficiency virus type 1 protease. FEBS Letters. January 1991, 278 (2): 199–203. PMID 1991513. doi:10.1016/0014-5793(91)80116-K . Winder SJ, Walsh MP. Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. The Journal of Biological Chemistry. June 1990, 265 (17): 10148–55. PMID 2161834. doi:10.1016/S0021-9258(19)38792-7 . Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC. Atomic structure of the actin:DNase I complex. Nature. September 1990, 347 (6288): 37–44. Bibcode:1990Natur.347...37K. PMID 2395459. S2CID 925337. doi:10.1038/347037a0. 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 . Taylor A, Erba HP, Muscat GE, Kedes L. Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains. Genomics. November 1988, 3 (4): 323–36. PMID 2907503. doi:10.1016/0888-7543(88)90123-1. Shen BW, Josephs R, Steck TL. Ultrastructure of the intact skeleton of the human erythrocyte membrane. The Journal of Cell Biology. March 1986, 102 (3): 997–1006. PMC 2114132 . PMID 2936753. doi:10.1083/jcb.102.3.997. 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. Kedes L, Ng SY, Lin CS, Gunning P, Eddy R, Shows T, Leavitt J. The human beta-actin multigene family. Transactions of the Association of American Physicians. 1986, 98: 42–6. PMID 3842206. 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. 外部链接[编辑] GeneReviews/NCBI/NIH/UW entry on Nemaline Myopathy Human ACTA1 genome location and ACTA1 gene details page in the UCSC Genome Browser（英语：UCSC Genome Browser）. 查论编蛋白质数据库图集 {{Template:PDB Gallery/{{{geneid}}}}} 查论编细胞骨架蛋白人类蛋白微丝（ABP）肌丝（英语：Myofilament）肌动蛋白 A1 A2 B C1 G1 G2 肌球蛋白 I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B 轻链 MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1 其它原肌球调节蛋白（英语：Tropomodulin） 1 2 3 4 肌钙蛋白 T 1 2 3 C 1 2 I 1 2 3 原肌球蛋白（英语：Tropomyosin） 1 2 3 4 辅肌动蛋白 1 2 3 4 Arp2/3複合體肌动蛋白解聚因子丝切蛋白（英语：Cofilin） 1 2 Destrin 凝溶胶蛋白前纤维蛋白 1 2 肌联蛋白其它 Wiskott-Aldrich syndrome protein 原纤蛋白（英语：Fibrillin）细丝蛋白（英语：Filamin） FLNA FLNB FLNC Espin TRIOBP 中间纤维Type 1/2（角蛋白细胞角蛋白（英语：Cytokeratin））上皮角蛋白（英语：Epithelial keratin）（软α-角蛋白） I型（英语：Type I keratin）/17号染色体 10 12 13 14 15 16 17 19 20 12号染色体 18 none 21 II型（英语：Type II keratin）/12号染色体 1 2A 3 4 5 6A 6B 7 8 9 毛发角蛋白（硬α-角蛋白） I型（英语：I型毛发角蛋白）/17号染色体 31 32 33A 33B 34 35 36 37 38 II型（英语：II型毛发角蛋白）/12号染色体 81 82 83 84 85 86 未分类α-角蛋白 17号染色体 23 24 25 26 27 28 39 40 12号染色体 71 72 73 74 75 76 77 78 79 80 非α-角蛋白 β-角蛋白（英语：Beta-keratin） Type 3 结蛋白（英语：Desmin）胶质纤维酸性蛋白（英语：Glial fibrillary acidic protein）外周蛋白（英语：Peripherin）波形蛋白 Type 4 介连蛋白（英语：Internexin）巢蛋白神经丝（英语：Neurofilament） NEFL NEFM NEFH Synemin Syncoilin Type 5 核纤层蛋白：A B 微管/MAPs微管蛋白 TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 驱动蛋白 KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3 动力蛋白鞭毛轴丝：DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 细胞质中：DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3 其它 tau蛋白动力蛋白激活蛋白（英语：Dynactin） DCTN1 微管去稳蛋白（英语：Stathmin）筑丝蛋白（英语：Tektin） TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 缢断蛋白 DNM1 DNM2 DNM3 连环蛋白（英语：Catenin） Alpha catenin β-连环蛋白 APC Plakoglobin (gamma catenin) Delta catenin GAN 膜蛋白 Dystrophin Dystroglycan Utrophin 锚蛋白 ANK1 ANK2 ANK3 血影蛋白 SPTA1 SPTAN1 SPTB SPTBN1 SPTBN2 SPTBN4 SPTBN5 其它 plakin 桥粒斑蛋白（英语：Desmoplakin）网蛋白（英语：Plectin]]]）踝蛋白（英语：Talin protein） TLN1 TLN2 粘着斑蛋白（英语：Vinculin）斑菲素蛋白（英语：Plakophilin） PKP1 PKP2 其它生物 Major sperm proteins 原核细胞骨架 Crescentin FtsZ MreB ParM 生化结构: 过氧化物酶体，骨架（中心体），上皮，纤毛，线粒体，细胞核（染色体）

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骨骼肌肌动蛋白α1

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