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    ACTG1 actin gamma 1 [ Homo sapiens (human) ]

    Gene ID: 71, updated on 9-Dec-2024

    Summary

    Official Symbol
    ACTG1provided by HGNC
    Official Full Name
    actin gamma 1provided by HGNC
    Primary source
    HGNC:HGNC:144
    See related
    Ensembl:ENSG00000184009 MIM:102560; AllianceGenome:HGNC:144
    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
    ACT; ACTG; DFNA20; DFNA26; HEL-176
    Summary
    Actins are highly conserved proteins that are involved in various types of cell motility and in maintenance of the cytoskeleton. Three main groups of actin isoforms have been identified in vertebrate animals: alpha, beta, and gamma. 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 all cell types. Mutations in this gene are associated with DFNA20/26, a subtype of autosomal dominant non-syndromic sensorineural progressive hearing loss and also with Baraitser-Winter syndrome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2017]
    Expression
    Ubiquitous expression in ovary (RPKM 1227.2), esophagus (RPKM 970.4) and 25 other tissues See more
    Orthologs
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    See ACTG1 in Genome Data Viewer
    Location:
    17q25.3
    Exon count:
    7
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 17 NC_000017.11 (81509971..81512799, complement)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 17 NC_060941.1 (82427089..82429917, complement)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 17 NC_000017.10 (79476997..79479825, complement)

    Chromosome 17 - NC_000017.11Genomic Context describing neighboring genes Neighboring gene BAH domain and coiled-coil containing 1 Neighboring gene uncharacterized LOC124904084 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79422900-79423848 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79423849-79424797 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79438477-79438978 Neighboring gene CRISPRi-validated cis-regulatory element chr17.6006 Neighboring gene long intergenic non-protein coding RNA 1971 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9127 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79455547-79456267 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79456989-79457708 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79460397-79460898 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79466919-79467642 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12964 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9128 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9129 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12965 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12966 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9130 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79482073-79482696 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79482697-79483322 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12967 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:79483947-79484572 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79484573-79485196 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9133 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9134 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12969 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12970 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79495325-79495851 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79495852-79496377 Neighboring gene fascin actin-bundling protein 2, retinal Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79504525-79505496 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79507853-79508353 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:79516844-79517639 Neighboring gene FA core complex associated protein 100 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9135 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9136 Neighboring gene uncharacterized LOC124904085 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 9137 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 12971

    Genomic regions, transcripts, and products

    Expression

    • 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

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?

    HIV-1 interactions

    Protein interactions

    Protein Gene Interaction Pubs
    Envelope surface glycoprotein gp120 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 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 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 Inducible T-cell kinase (ITK) affects viral entry and gp120-induced actin reorganization 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 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 induces loss of F-actin assembly and inhibits retinoid receptor-mediated transcription 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 induces rearrangement of actin microfilaments in dendritic cells, leading to uropod and ruffle formation, as well as the recruitment of T cells with a pronounced focal polarization of F-actin toward the DC/T cell contact sites PubMed
    nef N-terminal myristoylated, but not unmyristoylated, HIV-1 Nef associates with actin in human B and T lymphocytes forming a high-molecular-mass complex of 150-300 kDa that influences the subcellular localization of Nef PubMed
    Pr55(Gag) 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
    gag HIV-1 Gag assembly and budding occur through an actin-driven mechanism 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
    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 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 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
    Vpr vpr A stable-isotope labeling by amino acids in cell culture coupled with mass spectrometry-based proteomics identifies downregulation of actin, gamma 1 (ACTG1) expression by HIV-1 Vpr in Vpr transduced macrophages PubMed
    vpr HIV-1 Vpr-expressing Jurkat T cell clones showed a significant increase in G-actin polymerization to filamentous actin (F-actin), indicating a role of Vpr in microfilament system assembly. Vpr also causes disruption of the actin cytoskeleton in yeast. PubMed
    matrix 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

    Go to the HIV-1, Human Interaction Database

    Pathways from PubChem

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    enables profilin binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    enables protein kinase binding IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables structural constituent of cytoskeleton IC
    Inferred by Curator
    more info
    PubMed 
    enables structural constituent of postsynaptic actin cytoskeleton IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables ubiquitin protein ligase binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within_positive_effect angiogenesis IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in axonogenesis IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in cell motility IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in cellular response to type II interferon IEA
    Inferred from Electronic Annotation
    more info
     
    acts_upstream_of_or_within maintenance of blood-brain barrier NAS
    Non-traceable Author Statement
    more info
    PubMed 
    involved_in morphogenesis of a polarized epithelium IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in platelet aggregation HMP PubMed 
    involved_in positive regulation of cell migration IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in positive regulation of gene expression IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in positive regulation of wound healing IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in postsynaptic actin cytoskeleton organization IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in protein localization to bicellular tight junction IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in regulation of focal adhesion assembly IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in regulation of stress fiber assembly IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in regulation of synaptic vesicle endocytosis IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in regulation of transepithelial transport IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in sarcomere organization IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in tight junction assembly IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    Component Evidence Code Pubs
    part_of NuA4 histone acetyltransferase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in Schaffer collateral - CA1 synapse IEA
    Inferred from Electronic Annotation
    more info
     
    is_active_in actin cytoskeleton IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    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 apical junction complex IDA
    Inferred from Direct Assay
    more info
    PubMed 
    is_active_in axon IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in basal body patch IEA
    Inferred from Electronic Annotation
    more info
     
    located_in blood microparticle HDA PubMed 
    located_in calyx of Held IEA
    Inferred from Electronic Annotation
    more info
     
    located_in cell-cell junction IDA
    Inferred from Direct Assay
    more info
    PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in cytoskeleton ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    located_in cytoskeleton TAS
    Traceable Author Statement
    more info
    PubMed 
    located_in cytosol TAS
    Traceable Author Statement
    more info
     
    located_in dense body ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    located_in extracellular exosome HDA PubMed 
    located_in extracellular exosome IDA
    Inferred from Direct Assay
    more info
    PubMed 
    located_in extracellular space HDA PubMed 
    part_of filamentous actin IEA
    Inferred from Electronic Annotation
    more info
     
    located_in focal adhesion ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    located_in membrane HDA PubMed 
    is_active_in membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in myofibril IEA
    Inferred from Electronic Annotation
    more info
     
    located_in nucleus HDA PubMed 
    located_in phagocytic vesicle IEA
    Inferred from Electronic Annotation
    more info
     
    located_in plasma membrane ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    located_in plasma membrane TAS
    Traceable Author Statement
    more info
     
    is_active_in synapse IBA
    Inferred from Biological aspect of Ancestor
    more info
     

    General protein information

    Preferred Names
    actin, cytoplasmic 2
    Names
    cytoskeletal gamma-actin
    epididymis luminal protein 176

    NCBI Reference Sequences (RefSeq)

    NEW Try the new Transcript table

    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.

    Genomic

    1. NG_011433.1 RefSeqGene

      Range
      5003..7831
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001199954.3 → NP_001186883.1  actin, cytoplasmic 2

      See identical proteins and their annotated locations for NP_001186883.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the longest transcript. Variants 1 and 2 encode the same protein.
      Source sequence(s)
      AC139149, BC063495
      Consensus CDS
      CCDS11782.1
      UniProtKB/Swiss-Prot
      A8K7C2, P02571, P14104, P63261, P99022, Q5U032, Q96E67
      UniProtKB/TrEMBL
      Q53G76, Q53G99, Q53GK6
      Related
      ENSP00000466346.2, ENST00000570382.2
      Conserved Domains (1) summary
      PTZ00281
      Location:1 → 375
      PTZ00281; actin; Provisional
    2. NM_001614.5 → NP_001605.1  actin, cytoplasmic 2

      See identical proteins and their annotated locations for NP_001605.1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR, compared to variant 1. Variants 1 and 2 encode the same protein.
      Source sequence(s)
      BC063495, X04098
      Consensus CDS
      CCDS11782.1
      UniProtKB/Swiss-Prot
      A8K7C2, P02571, P14104, P63261, P99022, Q5U032, Q96E67
      UniProtKB/TrEMBL
      Q53G76, Q53G99, Q53GK6
      Related
      ENSP00000458435.1, ENST00000573283.7
      Conserved Domains (1) summary
      PTZ00281
      Location:1 → 375
      PTZ00281; actin; Provisional

    RNA

    1. NR_037688.3 RNA Sequence

      Status: REVIEWED

      Description
      Transcript Variant: This variant (3) includes an alternate splice site in the 3' UTR, compared to variant 1, which makes the transcript a candidate for nonsense-mediated mRNA decay (NMD). Transcripts subjected to NMD are degraded prior to protein translation. The transcript is sufficiently abundant to represent as a RefSeq record though a predicted protein is not represented.
      Source sequence(s)
      AC139149, BC063495
      Related
      ENST00000681092.1

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000017.11 Reference GRCh38.p14 Primary Assembly

      Range
      81509971..81512799 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Reference GRCh38.p14 PATCHES

    Genomic

    1. NW_025791805.1 Reference GRCh38.p14 PATCHES

      Range
      166176..169004 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060941.1 Alternate T2T-CHM13v2.0

      Range
      82427089..82429917 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)