ACTA1

From Wikipedia, the free encyclopedia

Actin, alpha 1, skeletal muscle

PDB rendering based on 1atn.

Available structures: 1atn, 1c0g, 1d4x, 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

Symbol(s)

ACTA1; ACTA; ASMA; CFTD; CFTD1; CFTDM; MPFD; NEM1; NEM2; NEM3

External IDs

OMIM: 102610 MGI: 87902 HomoloGene: 88645

Gene ontology
Molecular Function:	• nucleotide binding • structural molecule activity • structural constituent of cytoskeleton • protein binding • ATP binding • myosin binding • ADP binding
Cellular Component:	• stress fiber • cytoskeleton • striated muscle thin filament • actin filament
Biological Process:	• muscle contraction • muscle thin filament assembly • skeletal muscle fiber development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001100 (mRNA)
NP_001091 (protein)

NM_009606 (mRNA)
NP_033736 (protein)

Location

Chr 1: 227.63 - 227.64 Mb

Chr 8: 126.78 - 126.78 Mb

Pubmed search

[1]

[2]

Actin, alpha 1, skeletal muscle, also known as ACTA1, is a human gene.

Actin alpha 1 which is expressed in skeletal muscle is one of six different actin isoforms which have been identified. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.^[1]

[edit] See also

Actin
ACTB

[edit] References

^ Entrez Gene: ACTA1 actin, alpha 1, skeletal muscle.

[edit] 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.
Di Fiore PP, Scita G (2002). "Eps8 in the midst of GTPases.". Int. J. Biochem. Cell Biol. 34 (10): 1178–83. PMID 12127568.
Ogawa H, Shiraki H, Matsuda Y, Nakagawa H (1978). "Interaction of adenylosuccinate synthetase with F-actin.". Eur. J. Biochem. 85 (2): 331–7. PMID 648524.
Caccamise DA (1978). "My franchise was a teen-age lion's den.". Dental economics - oral hygiene 66 (11): 36–43. PMID 1074709.
den Hartigh JC, van Bergen en Henegouwen PM, Verkleij AJ, Boonstra J (1992). "The EGF receptor is an actin-binding protein.". J. Cell Biol. 119 (2): 349–55. PMID 1383230.
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. PMID 1540415.
Levine BA, Moir AJ, Patchell VB, Perry SV (1992). "Binding sites involved in the interaction of actin with the N-terminal region of dystrophin.". FEBS Lett. 298 (1): 44–8. PMID 1544421.
Rijken PJ, Hage WJ, van Bergen en Henegouwen PM, et al. (1992). "Epidermal growth factor induces rapid reorganization of the actin microfilament system in human A431 cells.". J. Cell. Sci. 100 ( Pt 3): 491–9. PMID 1808202.
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. PMID 1991513.
Winder SJ, Walsh MP (1990). "Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation.". J. Biol. Chem. 265 (17): 10148–55. PMID 2161834.
Kabsch W, Mannherz HG, Suck D, et al. (1990). "Atomic structure of the actin:DNase I complex.". Nature 347 (6288): 37–44. doi:10.1038/347037a0. PMID 2395459.
Takahashi K, Hiwada K, Kokubu T (1988). "Vascular smooth muscle calponin. A novel troponin T-like protein.". Hypertension 11 (6 Pt 2): 620–6. PMID 2455687.
Taylor A, Erba HP, Muscat GE, Kedes L (1989). "Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains.". Genomics 3 (4): 323–36. PMID 2907503.
Shen BW, Josephs R, Steck TL (1986). "Ultrastructure of the intact skeleton of the human erythrocyte membrane.". J. Cell Biol. 102 (3): 997–1006. PMID 2936753.
Burgess DR, Broschat KO, Hayden JM (1987). "Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins.". J. Cell Biol. 104 (1): 29–40. PMID 3793760.
Kedes L, Ng SY, Lin CS, et al. (1986). "The human beta-actin multigene family.". Trans. Assoc. Am. Physicians 98: 42–6. PMID 3842206.
Hanauer A, Levin M, Heilig R, et al. (1983). "Isolation and characterization of cDNA clones for human skeletal muscle alpha actin.". Nucleic Acids Res. 11 (11): 3503–16. PMID 6190133.
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. PMID 6893424.