Actin, alpha skeletal muscle

ACTA1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1T44
Identifiers
Aliases	ACTA1, ACTA, ASMA, CFTD, CFTD1, CFTDM, MPFD, NEM1, NEM2, NEM3, Actin, alpha 1, SHPM, actin, alpha 1, skeletal muscle, actin alpha 1, skeletal muscle
External IDs	OMIM: 102610; MGI: 87902; HomoloGene: 121702; GeneCards: ACTA1; OMA:ACTA1 - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	229,434,104 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	124,621,490 bp
RNA expression pattern
	Top expressed in
	Skeletal muscle tissue of biceps brachii; ; glutes; ; triceps brachii muscle; ; Skeletal muscle tissue of rectus abdominis; ; thoracic diaphragm; ; tibialis anterior muscle; ; muscle of thigh; ; gastrocnemius muscle; ; body of tongue; ; deltoid muscle;
	Top expressed in
	ankle; ; soleus muscle; ; plantaris muscle; ; medial head of gastrocnemius muscle; ; intercostal muscle; ; muscle of thigh; ; body of femur; ; digastric muscle; ; temporal muscle; ; vastus lateralis muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; myosin binding; ADP binding; structural constituent of cytoskeleton; protein binding; ATP binding;
Cellular component	cytoplasm; cell body; cytosol; blood microparticle; filopodium; sarcomere; striated muscle thin filament; stress fiber; extracellular fluid; actin filament; actin cytoskeleton; extracellular exosome; cytoskeleton; lamellipodium;
Biological process	muscle contraction; response to steroid hormone; skeletal muscle fiber adaptation; response to mechanical stimulus; skeletal muscle thin filament assembly; response to lithium ion; cell growth; positive regulation of gene expression; muscle filament sliding; mesenchyme migration; response to extracellular stimulus; skeletal muscle fiber development;
	Sources:Amigo / QuickGO
Orthologs
	58
	11459
	ENSG00000143632
	ENSMUSG00000031972
	P68133
	P68134
	NM_001100
	NM_001272041; NM_009606
	NP_001091
	NP_001258970; NP_033736
	Wikidata
View/Edit Human	View/Edit Mouse

Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene.^[5]^[6]

Template:PBB Summary

Skeletal actin gene expression

Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation.^[7] Such conditions result in fusion of committed cells (satellite cells) into myotubes, to form muscle fibers. Skeletal actin itself, when expressed, causes expression of several other "myogenic genes", which are essential to muscle formation.^[8] One key transcription factor that activates skeletal actin gene expression is Serum Response Factor ("SRF"), a protein that binds to specific sites on the promoter DNA of the actin gene.^[9] SRF may bring a number of other proteins to the promoter of skeletal actin, such as andogen receptor, and thereby contribute to induction of skeletal actin gene expression by androgenic (often termed "anabolic") steroids.^[10]

Interactions

Actin, alpha 1 has been shown to interact with TMSB4X,^[11]^[12] MIB2^[13] and PRKCE.^[14]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000143632 – Ensembl, May 2017
^ ^a ^b ^c 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, Borglum AD (March 1999). "Assignment of the human skeletal muscle [FC12]a-actin gene (ACTA1) to chromosome 1q42.13-->q42.2 by radiation hybrid mapping". Cytogenet Cell Genet. 83 (3–4): 224–5. doi:10.1159/000015184. PMID 10072583.
^ Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L (August 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. doi:10.1128/mcb.3.5.787. PMC 368601. PMID 6865942.
^ Bandman, E (1992). "Contractile protein isoforms in muscle development". Developmental Biology. 154 (2): 273–83. doi:10.1016/0012-1606(92)90067-Q. PMID 1358730.
^ Gunning, PW; Ferguson, V; Brennan, KJ; Hardeman, EC (2001). "Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle". Journal of Cell Science. 114 (Pt 3): 513–24. PMID 11171321.
^ Belaguli, NS; Zhou, W; Trinh, TH; Majesky, MW; Schwartz, RJ (1999). "Dominant negative murine serum response factor: alternative splicing within the activation domain inhibits transactivation of serum response factor binding targets". Molecular and Cellular Biology. 19 (7): 4582–91. PMC 84256. PMID 10373507.
^ Vlahopoulos, S; Zimmer, WE; Jenster, G; Belaguli, NS; Balk, SP; Brinkmann, AO; Lanz, RB; Zoumpourlis, VC; Schwartz, RJ (2005). "Recruitment of the androgen receptor via serum response factor facilitates expression of a myogenic gene". The Journal of Biological Chemistry. 280 (9): 7786–92. doi:10.1074/jbc.M413992200. PMID 15623502.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ Ballweber, Edda; Hannappel Ewald; Huff Thomas; Stephan Harald; Haener Markus; Taschner Nicole; Stoffler Daniel; Aebi Ueli; Mannherz Hans Georg (January 2002). "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". J. Mol. Biol. 315 (4). England: 613–25. doi:10.1006/jmbi.2001.5281. ISSN 0022-2836. PMID 11812134. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
^ Safer, D; Sosnick T R; Elzinga M (May 1997). "Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends". Biochemistry. 36 (19). UNITED STATES: 5806–16. doi:10.1021/bi970185v. ISSN 0006-2960. PMID 9153421. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysummary=, and |laysource= (help)
^ Takeuchi, Tamotsu; Heng Henry H Q; Ye Christine J; Liang Sheng-Ben; Iwata Jun; Sonobe Hiroshi; Ohtsuki Yuji (October 2003). "Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma". Am. J. Pathol. 163 (4). United States: 1395–404. doi:10.1016/S0002-9440(10)63497-9. ISSN 0002-9440. PMC 1868282. PMID 14507647. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
^ England, Karen; Ashford David; Kidd Daniel; Rumsby Martin (June 2002). "PKC epsilon is associated with myosin IIA and actin in fibroblasts". Cell. Signal. 14 (6). England: 529–36. doi:10.1016/S0898-6568(01)00277-7. ISSN 0898-6568. PMID 11897493. {{cite journal}}: Cite has empty unknown parameters: |laysummary=, |laydate=, and |laysource= (help)