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Actin, gamma 2, smooth muscle, enteric
PBB Protein ACTA1 image.jpg
PDB rendering based on 1atn.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs OMIM102545 HomoloGene123845 GeneCards: ACTG2 Gene
RNA expression pattern
PBB GE ACTG2 202274 at tn.png
More reference expression data
Species Human Mouse
Entrez 72 11468
Ensembl ENSG00000163017 ENSMUSG00000059430
UniProt P63267 P63268
RefSeq (mRNA) NM_001199893 NM_009610
RefSeq (protein) NP_001186822 NP_033740
Location (UCSC) Chr 2:
73.89 – 73.92 Mb
Chr 6:
83.51 – 83.54 Mb
PubMed search [1] [2]

Actin, gamma-enteric smooth muscle is a protein that in humans is encoded by the ACTG2 gene.[1][2][3]

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 2, encoded by this gene, is a smooth muscle actin found in enteric tissues.[3]


ACTG2 has been shown to interact with Emerin.[4]


  1. ^ Miwa T, Manabe Y, Kurokawa K, Kamada S, Kanda N, Bruns G, Ueyama H, Kakunaga T (July 1991). "Structure, chromosome location, and expression of the human smooth muscle (enteric type) gamma-actin gene: evolution of six human actin genes". Mol Cell Biol 11 (6): 3296–306. doi:10.1128/mcb.11.6.3296. PMC 360182. PMID 1710027. 
  2. ^ Ueyama H (May 1991). "A HindIII DNA polymorphism in the human enteric type smooth muscle actin gene (ACTSG)". Nucleic Acids Res 19 (2): 411. doi:10.1093/nar/19.2.411. PMC 333620. PMID 1673027. 
  3. ^ a b "Entrez Gene: ACTG2 actin, gamma 2, smooth muscle, enteric". 
  4. ^ Lattanzi, Giovanna; Cenni Vittoria; Marmiroli Sandra; Capanni Cristina; Mattioli Elisabetta; Merlini Luciano; Squarzoni Stefano; Maraldi Nadir Mario (April 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochem. Biophys. Res. Commun. (United States) 303 (3): 764–70. doi:10.1016/S0006-291X(03)00415-7. ISSN 0006-291X. PMID 12670476. 

Further reading[edit]