ACTA1 actin alpha 1, skeletal muscle [Homo sapiens (human)] - Gene

Summary

Official Symbol: ACTA1provided by HGNC
Official Full Name: actin alpha 1, skeletal muscleprovided by HGNC
Primary source: HGNC:HGNC:129
See related: Ensembl:ENSG00000143632 MIM:102610; AllianceGenome:HGNC:129
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: ACTA; ASMA; CFTD; MPFD; NEM1; NEM2; NEM3; SHPM; CFTD1; CFTDM; CMYO2A; CMYO2B; CMYO2C; CMYP2A; CMYP2B; CMYP2C
Summary: The product encoded by this gene belongs to the actin family of proteins, which are highly conserved proteins that play a role in cell motility, structure and integrity. Alpha, beta and gamma actin isoforms have been identified, with alpha actins being a major constituent of the contractile apparatus, while beta and gamma actins are involved in the regulation of cell motility. This actin is an alpha actin that is found in skeletal muscle. Mutations in this gene cause a variety of myopathies, including nemaline myopathy, congenital myopathy with excess of thin myofilaments, congenital myopathy with cores, and congenital myopathy with fiber-type disproportion, diseases that lead to muscle fiber defects with manifestations such as hypotonia. [provided by RefSeq, Sep 2019]
Expression: Biased expression in heart (RPKM 1670.9), esophagus (RPKM 297.6) and 1 other tissue See more
Orthologs: mouse all
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Genomic context

Location:: 1q42.13

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (229431245..229434094, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (228809946..228812800, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (229566992..229569841, complement)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A recurrent ACTA1 amino acid change in mosaic form causes milder asymmetric myopathy.
Title: A recurrent ACTA1 amino acid change in mosaic form causes milder asymmetric myopathy.
Different Mouse Models of Nemaline Myopathy Harboring Acta1 Mutations Display Differing Abnormalities Related to Mitochondrial Biology.
Title: Different Mouse Models of Nemaline Myopathy Harboring Acta1 Mutations Display Differing Abnormalities Related to Mitochondrial Biology.
Novel p.Asp27Glu ACTA1 variant features congenital myopathy with finger flexor weakness, cardiomyopathy, and cardiac conduction defects.
Title: Novel p.Asp27Glu ACTA1 variant features congenital myopathy with finger flexor weakness, cardiomyopathy, and cardiac conduction defects.
alpha-SMA positive vascular mural cells suppress cyst formation in hemangioblastoma.
Title: α-SMA positive vascular mural cells suppress cyst formation in hemangioblastoma.
Severe ACTA1-related nemaline myopathy: intranuclear rods, cytoplasmic bodies, and enlarged perinuclear space as characteristic pathological features on muscle biopsies.
Title: Severe ACTA1-related nemaline myopathy: intranuclear rods, cytoplasmic bodies, and enlarged perinuclear space as characteristic pathological features on muscle biopsies.
Activin A Causes Muscle Atrophy through MEF2C-Dependent Impaired Myogenesis.
Title: Activin A Causes Muscle Atrophy through MEF2C-Dependent Impaired Myogenesis.
Mutational and clinical spectrum in a cohort of Chinese patients with hereditary nemaline myopathy.
Title: Mutational and clinical spectrum in a cohort of Chinese patients with hereditary nemaline myopathy.
Osteosarcoma-Derived Extracellular Vesicles Induce Lung Fibroblast Reprogramming.
Title: Osteosarcoma-Derived Extracellular Vesicles Induce Lung Fibroblast Reprogramming.
Metabolic Alterations in Spheroid-Cultured Hepatic Stellate Cells.
Title: Metabolic Alterations in Spheroid-Cultured Hepatic Stellate Cells.
carrying a similar clinical phenotype of some members of the original family and the same ACTA1 mutation, revealed the presence of numerous nemaline rods, suggesting that there must be other factors that explain the absence of nemaline rods
Title: Autosomal dominant distal myopathy with nemaline rods due to p.Glu197Asp mutation in ACTA1.

Submit: New GeneRIF Correction See all GeneRIFs (90)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Actin accumulation myopathy MedGen: C3711389 OMIM: 161800 GeneReviews: Not available	Compare labs
Congenital myopathy 2b, severe infantile, autosomal recessive MedGen: C5830300 OMIM: 620265 GeneReviews: Not available	Compare labs
Congenital myopathy 2c, severe infantile, autosomal dominant MedGen: C5830333 OMIM: 620278 GeneReviews: Not available	Compare labs
Congenital myopathy with fiber type disproportion MedGen: C0546264 GeneReviews: Not available	Compare labs
Progressive scapulohumeroperoneal distal myopathy MedGen: C4225181 OMIM: 616852 GeneReviews: Not available	Compare labs

EBI GWAS Catalog

Description
A genome-wide association study identifies multiple susceptibility loci for chronic lymphocytic leukemia. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	CCR5 expression inhibits HIV-1 gp120-mediated early actin rearrangement in CD4/CXCR4 expressing 293T cells	PubMed
	env	SMS2 is involved in HIV-1 gp120-induced phosphorylation and activation of PYK2 and reorganization and polymerization of F-actin	PubMed
	env	HIV-1 gp120-CXCR4 signaling triggers cofilin activation and actin reorganization, which are important for a post entry process leading to viral nuclear localization	PubMed
	env	Gelsolin overexpression impairs HIV-1 gp120-induced cortical F-actin reorganization and capping and gp120-mediated CD4-CCR5 and CD4-CXCR4 redistribution in permissive lymphocytes	PubMed
	env	The N-terminal leucine-rich repeat fragment of Slit2 inhibits HIV-1 gp120-induced actin polymerization in T cells	PubMed
	env	Inducible T-cell kinase (ITK) affects viral entry and gp120-induced actin reorganization	PubMed
	env	NHERF1 is required for HIV-1 gp120-induced actin rearrangement	PubMed
	env	Syntenin-1 is recruited toward HIV-1 gp120/gp41-driven virus/cell and cell/cell contacts, associates with CD4, limits HIV-1-induced cell fusion and viral entry, and modulates gp120/gp41-triggered actin polymerization and PIP2 accumulation	PubMed
	env	Lck phosphorylates CD3zeta and the TCR-CD3 complex is recruited to a virological synapse (VS) when cells interact with gp120+ICAM-1 bilayers, leading to creation of an F-actin-depleted zone	PubMed
Envelope surface glycoprotein gp160, precursor	env	Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1	PubMed
Envelope transmembrane glycoprotein gp41	env	Syntenin-1 is recruited toward HIV-1 gp120/gp41-driven virus/cell and cell/cell contacts, associates with CD4, limits HIV-1-induced cell fusion and viral entry, and modulates gp120/gp41-triggered actin polymerization and PIP2 accumulation	PubMed
	env	The interaction of the long cytoplasmic tail of HIV-1 gp41 with the carboxy-terminal regulatory domain of p115-RhoGEF inhibits p115-mediated actin stress fiber formation and activation of serum response factor (SRF)	PubMed
Nef	nef	HIV-1 NA7 and SF2 Nef utilize their C-terminal aspartic acids to relocalize ACTA1 and ACTB (F-actin)	PubMed
	nef	HIV-1 Nef stabilizes podosomes and enhances the size of the F-actin core in human monocyte-derived macrophages	PubMed
	nef	HIV-1 Nef inhibits CXCL12 induced chemotaxis in Jurkat cells, monocytes, and PBMCs, which leads to marked downregulation of F-actin accumulation in cells	PubMed
	nef	HIV-1 Nef co-localizes with F-actin and reorganizes F-actin assembly in the cortical regions of human podocyte	PubMed
	nef	HIV-1 Nef induces loss of F-actin assembly and inhibits retinoid receptor-mediated transcription	PubMed
	nef	The HIV-1 Nef highly conserved valine-glycine-phenylalanine amino acid triplet (VGF) motif is essential for effects of Nef on actin dynamics and Lck localization	PubMed
	nef	HIV-1 Nef requires a PAK2 recruitment motif (F195/191I) for inhibition of actin remodeling and induction of cofilin hyperphosphorylation	PubMed
	nef	HIV-1 Nef disrupts F-actin at the cortical actin ring in both insulin-unstimulated and stimulated adipocytes	PubMed
Pr55(Gag)	gag	No major differences in relative actin incorporation between wild-type HIV-1 and Gag virus-like particles (VLPs) and between Gag and Gag(LZ) VLPs, indicating that the NC domain of Gag is not required for actin incorporation into HIV-1	PubMed
	gag	HIV-1 Gag assembly proceeds with normal rates when actin filaments are either disrupted or stabilized in cells, indicating that the actin network is dispensable for HIV-1 assembly	PubMed
	gag	HIV-1 Gag assembly and budding occur through an actin-driven mechanism	PubMed
	gag	Tec kinase chemical inhibitors diminish the recruitment of ITK to the plasma membrane perturbing HIV-1 Gag-ITK co-localization, disrupting F-actin polymerization, and inhibiting HIV-1 release and replication	PubMed
	gag	HIV-1 Gag, ITK, and F-actin are located in overlapping and discrete regions of T cell-T cell contact sites	PubMed
	gag	Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1	PubMed
Tat	tat	Treatment with cannabinoids inhibits HIV-1 Tat-enhanced attachment of U937 cells to collagen IV, laminin, or ECM1 proteins, which is linked to the cannabinoid receptor type 2 and the modulation of beta1-integrin and actin distribution	PubMed
	tat	Treatment of primary hippocampal neurons with HIV-1 Tat produces a significant early reduction in F-actin labeled puncta. The cysteine rich domain (residues 22-37) of Tat is required for Tat-mediated reduction of F-actin labeled puncta	PubMed
	tat	Uptake of the HIV-1 Tat protein is regulated by arrangement of the actin cytoskeleton in epithelial cells	PubMed
	tat	Endothelial cell adherent to HIV-1 Tat induces rearrangement of actin cytoskeleton and is dependent on integrin alpha5beta3	PubMed
	tat	In Jurkat cells expressing HIV-1 Tat, decreased expression levels are found for basic cytoskeletal proteins such as actin, beta-tubulin, annexin, cofilin, gelsolin, and Rac/Rho-GDI complex	PubMed
	tat	Most of the components of the SWI2/SNF2 chromatin remodeling complex (BRG1/BRM, BAF250, BAF180, BAF170, BAF155, BAF60a, BAF53A, actin and InI) except BRM, BAF155 and BAF57, are identified to interact with HIV-1 Tat in Jurkat cell	PubMed
	tat	Signaling from multivalent TatP facilitates the frequent and constitutive recruitment of TatR to actin-associated membrane lipid-rafts	PubMed
	tat	HIV-1 Tat induces actin cytoskeletal rearrangements through p21-activated kinase 1 (PAK1) and downstream activation of the endothelial NADPH oxidase, an effect that is lost by introduction of mutations into the Tat cysteine-rich or basic domains	PubMed
matrix	gag	HIV-1 MA co-localizes with beta2 integrin, alphaM and alphaX integrins in the intracellular thick electron-dense membrane compartments, which contain talin, vinculin and paxillin that connect the integrin complexes to the actin cytoskeleton	PubMed
	gag	The localization of the HIV-1 reverse transcription complex to actin microfilaments is mediated by the interaction of a reverse transcription complex component (HIV-1 Matrix) with actin, but not vimentin (intermediate filaments) or tubulin (microtubules)	PubMed
nucleocapsid	gag	HIV-1 NC-like aggregates are associated with dsDNA synthesis by HIV-1 RT and appear to efficiently bind to F-actin filaments, a property that may be involved in targeting complexes to the nuclear envelope	PubMed
	gag	Mature HIV-1 Nucleocapsid, as well as the nucleocapsid domain of the HIV-1 Gag polyprotein, binds filamentous actin resulting in incorporation of actin into virus particles and enhancement of cell motility	PubMed
retropepsin	gag-pol	Actin, one of the most abundant proteins of the cell, is hydrolyzed by the human immunodeficiency virus type 1 (HIV-1) protease during acute infection of cultured human T lymphocytes	PubMed
	gag-pol	HIV-1 protease cleaves actin in vitro at amino acid residues 66-67, 94-95, and 126-127	PubMed
reverse transcriptase	gag-pol	HIV-1 NC-like aggregates are associated with dsDNA synthesis by HIV-1 RT and appear to efficiently bind to F-actin filaments, a property that may be involved in targeting complexes to the nuclear envelope	PubMed
	gag-pol	The localization of the HIV-1 reverse transcription complex to actin microfilaments is mediated by the interaction of a reverse transcription complex component (HIV-1 Matrix) with actin, but not vimentin (intermediate filaments) or tubulin (microtubules)	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

PMC350549P3 (e-PCR)
- UniSTS:273239

PMC23952P1 (e-PCR)
- UniSTS:272216

PMC110143P1 (e-PCR)
- UniSTS:270184

LOC345651 (e-PCR)
- UniSTS:265879

Acta1 (e-PCR), detects polymorphism
- UniSTS:478947

RH36158 (e-PCR)
- UniSTS:78325

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables ADP binding	TAS Traceable Author Statement more info	PubMed
enables ATP binding	TAS Traceable Author Statement more info	PubMed
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables myosin binding	TAS Traceable Author Statement more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables structural constituent of cytoskeleton	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to potassium ion	IEA Inferred from Electronic Annotation more info
involved_in mesenchyme migration	ISS Inferred from Sequence or Structural Similarity more info
involved_in muscle contraction	TAS Traceable Author Statement more info	PubMed
involved_in positive regulation of gene expression	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to mechanical stimulus	IEA Inferred from Electronic Annotation more info
involved_in response to steroid hormone	IEA Inferred from Electronic Annotation more info
involved_in skeletal muscle fiber adaptation	IEA Inferred from Electronic Annotation more info
involved_in skeletal muscle fiber development	ISS Inferred from Sequence or Structural Similarity more info
involved_in skeletal muscle thin filament assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in skeletal muscle thin filament assembly	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in actin cytoskeleton	IBA Inferred from Biological aspect of Ancestor more info
located_in actin cytoskeleton	IMP Inferred from Mutant Phenotype more info	PubMed
is_active_in actin filament	IBA Inferred from Biological aspect of Ancestor more info
located_in actin filament	IDA Inferred from Direct Assay more info	PubMed
located_in blood microparticle	HDA more info	PubMed
located_in cell body	ISS Inferred from Sequence or Structural Similarity more info
located_in cytosol	TAS Traceable Author Statement more info
located_in extracellular exosome	HDA more info	PubMed
located_in extracellular space	HDA more info	PubMed
located_in filopodium	ISS Inferred from Sequence or Structural Similarity more info
located_in lamellipodium	ISS Inferred from Sequence or Structural Similarity more info
located_in sarcomere	IDA Inferred from Direct Assay more info	PubMed
is_active_in stress fiber	IBA Inferred from Biological aspect of Ancestor more info
located_in stress fiber	IDA Inferred from Direct Assay more info	PubMed
is_active_in striated muscle thin filament	IBA Inferred from Biological aspect of Ancestor more info
located_in striated muscle thin filament	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: actin, alpha skeletal muscle

Names: nemaline myopathy type 3

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.