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Actin, gamma 1

PDB rendering based on 1atn.
Available structures
1atn, 1c0f, 1c0g, 1d4x, 1dej, 1eqy, 1esv, 1h1v, 1hlu, 1ijj, 1j6z, 1kxp, 1lcu, 1lot, 1m8q, 1ma9, 1mdu, 1mvw, 1nlv, 1nm1, 1nmd, 1nwk, 1o18, 1o19, 1o1a, 1o1b, 1o1c, 1o1d, 1o1e, 1o1f, 1o1g, 1p8z, 1qz5, 1qz6, 1rdw, 1rfq, 1rgi, 1s22, 1sqk, 1t44, 1wua, 1y64, 1yxq, 2a3z, 2a40, 2a41, 2a42, 2a5x, 2asm, 2aso, 2asp, 2btf, 2d1k, 2ff3, 2ff6, 2fxu, 2gwj, 2gwk, 2hf3, 2hf4, 2hmp, 2oan, 2q1n, 2q31, 2q36
Identifiers
Symbols ACTG1; ACT; ACTG; DFNA20; DFNA26
External IDs OMIM102560 MGI87906 HomoloGene74402 GeneCards: ACTG1 Gene
RNA expression pattern
PBB GE ACTG1 211983 x at tn.png
PBB GE ACTG1 201550 x at tn.png
PBB GE ACTG1 211970 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 71 11465
Ensembl ENSG00000184009 n/a
UniProt P63261 n/a
RefSeq (mRNA) NM_001614 XM_001052054
RefSeq (protein) NP_001605 XP_001052054
Location (UCSC) Chr 17:
77.09 - 77.09 Mb
n/a
PubMed search [1] [2]

Actin, gamma 1, also known as ACTG1, is a gene.

Actins are highly conserved proteins that are involved in various types of cell motility, and maintenance of the cytoskeleton. In vertebrates, three main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. Actin, gamma 1, encoded by this gene, is a cytoplasmic actin found in nonmuscle cells.[1]

Contents

Interactions

ACTG1 has been shown to interact with TMSB4X[2][3] and CAP1.[4]

See also

References

  1. ^ "Entrez Gene: ACTG1 actin, gamma 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=71. 
  2. ^ Hertzog, Maud; van Heijenoort Carine, Didry Dominique, Gaudier Martin, Coutant Jérôme, Gigant Benoît, Didelot Gérard, Préat Thomas, Knossow Marcel, Guittet Eric, Carlier Marie-France (May. 2004). "The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly". Cell (United States) 117 (5): 611–23. ISSN 0092-8674. PMID 15163409. 
  3. ^ Van Troys, M; Dewitte D, Goethals M, Carlier M F, Vandekerckhove J, Ampe C (Jan. 1996). "The actin binding site of thymosin beta 4 mapped by mutational analysis". EMBO J. (ENGLAND) 15 (2): 201–10. ISSN 0261-4189. PMID 8617195. 
  4. ^ Hubberstey, A; Yu G, Loewith R, Lakusta C, Young D (Jun. 1996). "Mammalian CAP interacts with CAP, CAP2, and actin". J. Cell. Biochem. (UNITED STATES) 61 (3): 459–66. doi:10.1002/(SICI)1097-4644(19960601)61:3<459::AID-JCB13>3.0.CO;2-E. ISSN 0730-2312. PMID 8761950. 

Further reading

  • Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease.". Folia Biol. (Praha) 42 (5): 227–30. PMID 8997639. 
  • Rodríguez Del Castillo A, Vitale ML, Trifaró JM (1992). "Ca2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5,-biphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation.". J. Cell Biol. 119 (4): 797–810. doi:10.1083/jcb.119.4.797. PMID 1331119. 
  • Adams LD, Tomasselli AG, Robbins P, et al. (1992). "HIV-1 protease cleaves actin during acute infection of human T-lymphocytes.". AIDS Res. Hum. Retroviruses 8 (2): 291–5. doi:10.1089/aid.1992.8.291. PMID 1540415. 
  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151. 
  • Tomasselli AG, Hui JO, Adams L, et al. (1991). "Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus.". J. Biol. Chem. 266 (22): 14548–53. PMID 1907279. 
  • Shoeman RL, Kesselmier C, Mothes E, et al. (1991). "Non-viral cellular substrates for human immunodeficiency virus type 1 protease.". FEBS Lett. 278 (2): 199–203. doi:10.1016/0014-5793(91)80116-K. PMID 1991513. 
  • Erba HP, Eddy R, Shows T, et al. (1988). "Structure, chromosome location, and expression of the human gamma-actin gene: differential evolution, location, and expression of the cytoskeletal beta- and gamma-actin genes.". Mol. Cell. Biol. 8 (4): 1775–89. PMID 2837653. 
  • Vandekerckhove J, Schering B, Bärmann M, Aktories K (1988). "Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in arginine 177.". J. Biol. Chem. 263 (2): 696–700. PMID 3335520. 
  • Chou CC, Davis RC, Fuller ML, et al. (1987). "Gamma-actin: unusual mRNA 3'-untranslated sequence conservation and amino acid substitutions that may be cancer related.". Proc. Natl. Acad. Sci. U.S.A. 84 (9): 2575–9. doi:10.1073/pnas.84.9.2575. PMID 3472224. 
  • Hesterberg LK, Weber K (1986). "Isolation of a domain of villin retaining calcium-dependent interaction with G-actin, but devoid of F-actin fragmenting activity.". Eur. J. Biochem. 154 (1): 135–40. doi:10.1111/j.1432-1033.1986.tb09368.x. PMID 3510866. 
  • Erba HP, Gunning P, Kedes L (1986). "Nucleotide sequence of the human gamma cytoskeletal actin mRNA: anomalous evolution of vertebrate non-muscle actin genes.". Nucleic Acids Res. 14 (13): 5275–94. doi:10.1093/nar/14.13.5275. PMID 3737401. 
  • Fuchs E, Kim KH, Hanukoglu I, Tanese N (1984). "The evolution and complexity of the genes encoding the cytoskeletal proteins of human epidermal cells.". Curr. Probl. Dermatol. 11: 27–44. PMID 6686106. 
  • Gunning P, Ponte P, Okayama H, et al. (1983). "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.". Mol. Cell. Biol. 3 (5): 787–95. PMID 6865942. 
  • Bretscher A, Weber K (1980). "Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner.". Cell 20 (3): 839–47. doi:10.1016/0092-8674(80)90330-X. PMID 6893424. 
  • Pedrotti B, Colombo R, Islam K (1995). "Microtubule associated protein MAP1A is an actin-binding and crosslinking protein.". Cell Motil. Cytoskeleton 29 (2): 110–6. doi:10.1002/cm.970290203. PMID 7820861. 
  • Pope B, Maciver S, Weeds A (1995). "Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites.". Biochemistry 34 (5): 1583–8. doi:10.1021/bi00005a014. PMID 7849017. 
  • Jesaitis AJ, Erickson RW, Klotz KN, et al. (1993). "Functional molecular complexes of human N-formyl chemoattractant receptors and actin.". J. Immunol. 151 (10): 5653–65. PMID 8228254. 
  • Hawkins M, Pope B, Maciver SK, Weeds AG (1993). "Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments.". Biochemistry 32 (38): 9985–93. doi:10.1021/bi00089a014. PMID 8399167. 
  • Yu FX, Lin SC, Morrison-Bogorad M, et al. (1993). "Thymosin beta 10 and thymosin beta 4 are both actin monomer sequestering proteins.". J. Biol. Chem. 268 (1): 502–9. PMID 8416954. 
  • Jalaguier S, Mornet D, Mesnier D, et al. (1996). "Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation.". FEBS Lett. 384 (2): 112–6. doi:10.1016/0014-5793(96)00295-5. PMID 8612804. 
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