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    ACTB actin, beta [ Homo sapiens ]

    Gene ID: 60, updated on 19-May-2012
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    Summary

    Official Symbol
    ACTBprovided by HGNC
    Official Full Name
    actin, betaprovided by HGNC
    Primary source
    HGNC:132
    See related
    Ensembl:ENSG00000075624; HPRD:00032; MIM:102630; Vega:OTTHUMG00000023268
    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
    BRWS1; PS1TP5BP1
    Summary
    This gene encodes one of six different actin proteins. Actins are highly conserved proteins that are involved in cell motility, structure, and integrity. This actin is a major constituent of the contractile apparatus and one of the two nonmuscle cytoskeletal actins. [provided by RefSeq, Jul 2008]
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    Genomic context

    Location :
    7p22
    Sequence :
    Chromosome: 7; NC_000007.13 (5566779..5570232, complement)
    See ACTB in Epigenomics, MapViewer

    Chromosome 7 - NC_000007.13Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC100129484 Neighboring gene F-box and leucine-rich repeat protein 18 Neighboring gene microRNA 589 Neighboring gene uncharacterized LOC100505829 Neighboring gene S100 calcium binding protein A11 pseudogene Neighboring gene fascin homolog 1, actin-bundling protein (Strongylocentrotus purpuratus)

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    Genomic regions, transcripts, and products

    Go to nucleotideGraphics FASTA GenBank

    Go to reference sequence details
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    Bibliography

    Related articles in PubMed

    1. Active maintenance of nuclear actin by importin 9 supports transcription. Dopie J, et al. Proc Natl Acad Sci U S A, 2012 Feb 28. PMID 22323606.
    2. Effects of antioxidant supplementation on mRNA expression of glucose-6-phosphate dehydrogenase, β-actin and 18S rRNA in the anterior capsule of the lens in cataract patients. Hayashi R, et al. Exp Eye Res, 2012 Mar. PMID 22285204.
    3. Integrative analysis of the ubiquitin proteome isolated using Tandem Ubiquitin Binding Entities (TUBEs). Lopitz-Otsoa F, et al. J Proteomics, 2012 Jun 6. PMID 22178446.
    4. Proteomic analysis of the 20S proteasome (PSMA3)-interacting proteins reveals a functional link between the proteasome and mRNA metabolism. Fedorova OA, et al. Biochem Biophys Res Commun, 2011 Dec 16. PMID 22079093.
    5. Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels. Lee KA, et al. J Biol Chem, 2011 Dec 2. PMID 21987572.

    See all (264) citations in PubMed

    GeneRIFs: Gene References Into Functions What's a GeneRIF?

    1. Recombinant human actin is constantly shuttled into the murine nucleus by importin 9 and out by exportin 6. Nuclear actin is required for maximal transcription.
      Title: Active maintenance of nuclear actin by importin 9 supports transcription.
    2. Antioxidant supplementation was noted to increase G6PDH in the pentose phosphate cycle and 18S rRNA in the ribosome. There were no significant changes in the gene expression levels of beta-ACT
      Title: Effects of antioxidant supplementation on mRNA expression of glucose-6-phosphate dehydrogenase, β-actin and 18S rRNA in the anterior capsule of the lens in cataract patients.
    3. non-muscle alpha-ACTN4, HSPA5 and cytoplasmic ACTB, should be targeted in idiopathic premature ovarian failure cases
      Title: Identification and validation of candidate biomarkers involved in human ovarian autoimmunity.
    4. Data indicate taht candidate genes ACTB, BZW, OCM, MACC1, NXPH1, PRPS1L1, RAC1 and RPA3, which lie within the DFNB90 region, were sequenced and no potentially causal variants were identified.
      Title: Novel autosomal recessive nonsyndromic hearing impairment locus DFNB90 maps to 7p22.1-p15.3.
    5. ACTB showed high expression in forensic skin and body-fluid samples, providing a suitable marker for skin identification
      Title: mRNA-based skin identification for forensic applications.
    6. Nuclear beta-actin controls growth arrest of epithelial cells.
      Title: Depletion of nuclear actin is a key mediator of quiescence in epithelial cells.
    7. Data suggest that the existence of a common epitope on the molecules of phosducin and beta-actin may reflect a topological similarity of a small region of their surfaces.
      Title: Phosducin and monomeric β-actin have common epitope recognized by anti-phosducin antibodies.
    8. Findings indicate that activation of the cofilin-F-actin pathway contributes to tumor cell migration and metastasis enhanced by Aur-A, revealing a novel function for mitotic Aur-A kinase in tumor progression.
      Title: The mitotic kinase Aurora-A induces mammary cell migration and breast cancer metastasis by activating the Cofilin-F-actin pathway.
    9. The actin network plays a role in nuclear ERalpha actions in breast cancer cells.
      Title: Identification of a hormone-regulated dynamic nuclear actin network associated with estrogen receptor alpha in human breast cancer cell nuclei.
    10. Immunoblot analysis revealed profoundly decreased beta-actin levels during Ectromelia virus infection replicative cycle in the infected cells 24 hrs post infection.
      Title: Contribution of rearranged actin structures to the spread of Ectromelia virus infection in vitro.
    Submit: New GeneRIF Correction See all (34)
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    Phenotypes

    Review eQTL and phenotype association data in this region using PheGenI

    Baraitser-Winter syndrome 2

    Dystonia, juvenile-onset

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    HIV-1 protein interactions

    Protein Gene Interaction Pubs
    Envelope transmembrane glycoprotein gp41 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 Assays with phage-displayed Nef from HIV-1 NL4-3 have been used to identify a series of guanidine alkaloid-based inhibitors of Nef interactions with p53, actin, and p56(lck) PubMed
    nef Disruption of the actin cytoskeleton by treatment with CytD and LatB complements the infectivity defect of HIV-1 virions lacking Nef, suggesting Nef interacts with actin to enhance virion infectivity 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
    Rev rev Rev plays an important role in the compartmentation of translation by directing RRE-containing mRNAs to the beta-actin to form the perinuclear clusters at which the synthesis of viral structural proteins begins PubMed
    rev during Rev-mediated nuclear export of HIV-1 mRNA, actin binds to eukaryotic initiation factor 5A (eIF-5A), a protein that interacts directly with Rev and facilitates the nuclear export process PubMed
    rev beta actin is involved in the Rev-dependent nuclear export of unspliced and incompletely spliced HIV-1 mRNA PubMed
    Tat 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 Upregulation of actin, heat shock protein 90 and mitochondrial single-stranded DNA binding protein, and downregulation of lactate dehydrogenase are identified in human astrocytes expressing Tat 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 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 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 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
    gag-pol Eukaryotic beta-actin binds to either the large subunit (p66) of HIV-1 reverse transcriptase or to the HIV-1 Pol precursor polyprotein in vitro; this interaction is believed to be important for the secretion of HIV-1 virions PubMed

    Go to the HIV-1, Human Protein Interaction Database

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    Interactions

    Products Interactant Other Gene Complex Source Pubs Description
    NP_001092.1 NP_001092.1 ACTB    BIND  PubMed Actin interacts with itself to form an F-actin. 
    NP_001092.1 AC133065.3 CIITA    BIND  PubMed Beta-actin interacts with p-MHC2TA. 
    NP_001092.1 NP_005214.2 DNASE1    BIND  PubMed DNASE1 (DNase I) interacts with ACTB (beta-actin). 
    NP_001092.1 NP_114032.1 HNRNPU    BIND  PubMed ACTB (beta-actin) interacts with HNRPU (hnRNP U). 
    NP_001092.1 U22970.1 IFI6    BIND  PubMed Beta-actin interacts with p-G1P3. 
    NP_001092.1 NP_036515.3 OSTF1    BIND  PubMed SH3P2 interacts with beta-actin. 
    NP_001092.1 NP_061887.2 POLR1B    BIND  PubMed Pol I interacts with actin. 
    NP_001092.1 U13369.1 RIBIN    BIND  PubMed Actin interacts with rDNA. 
    NP_001092.1 NP_060897.2 RRN3    BIND  PubMed TIF-IA interacts with actin. 
    P60709 Q8N0Z2 ABRA    HPRD  PubMed  
    P60709 P60709 ACTB    HPRD  PubMed  
    P60709 P68032 ACTC1    HPRD  PubMed  
    P60709 P63261 ACTG1    HPRD  PubMed  
    P60709 P09917 ALOX5    HPRD  PubMed  
    P60709 O15143 ARPC1B    HPRD  PubMed  
    P60709 Activating transcription factor 7 interacting protein ATF7IP    HPRD  PubMed  
    P60709 Q9NV56 C20orf20    HPRD  PubMed  
    P60709 Q01518 CAP1    HPRD  PubMed  
    P60709 P52907 CAPZA1    HPRD  PubMed  
    P60709 P78371 CCT2    HPRD  PubMed  
    P60709 P50991 CCT4    HPRD  PubMed  
    P60709 P48643 CCT5    HPRD  PubMed  
    P60709 P50990 CCT8    HPRD  PubMed  
    P60709 Q13319 CDK5R2    HPRD  PubMed  
    P60709 P23528 CFL1    HPRD  PubMed  
    P60709 Q9Y281 CFL2    HPRD  PubMed  
    P60709 Q9Y696 CLIC4    HPRD  PubMed  
    P60709 P54105 CLNS1A    HPRD  PubMed  
    P60709 Q99439 CNN2    HPRD  PubMed  
    P60709 P31146 CORO1A    HPRD  PubMed  
    P60709 Q99829 CPNE1    HPRD  PubMed  
    P60709 Q96FN4 CPNE2    HPRD  PubMed  
    P60709 Q96A23 CPNE4    HPRD  PubMed  
    P60709 P48729 CSNK1A1    HPRD  PubMed  
    P60709 P24855 DNASE1    HPRD  PubMed  
    P60709 P60981 DSTN    HPRD  PubMed  
    P60709 P63167 DYNLL1    HPRD  PubMed  
    P60709 P68104 EEF1A1    HPRD  PubMed  
    P60709 P50402 EMD    HPRD  PubMed  
    P60709 Q08495 EPB49    HPRD  PubMed  
    P60709 P15311 EZR    HPRD  PubMed  
    P60709 Q13643 FHL3    HPRD  PubMed  
    P60709 Q13045 FLII    HPRD  PubMed  
    P60709 P04406 GAPDH    HPRD  PubMed  
    P60709 Q03113 GNA12    HPRD  PubMed  
    P60709 P06396 GSN    HPRD  PubMed  
    P60709 P08631 HCK    HPRD  PubMed  
    P60709 Q99729 HNRNPAB    HPRD  PubMed  
    P60709 Q00839 HNRNPU    HPRD  PubMed  
    P60709 P51659 HSD17B4    HPRD  PubMed  
    P60709 Q14847 LASP1    HPRD  PubMed  
    P60709 Q9UHV8 LGALS13    HPRD  PubMed  
    P60709 P02545 LMNA    HPRD  PubMed  
    P60709 P29536 LMOD1    HPRD  PubMed  
    P60709 P07948 LYN    HPRD  PubMed  
    P60709 P46821 MAP1B    HPRD  PubMed  
    P60709 P11137 MAP2    HPRD  PubMed  
    P60709 P10636 MAPT    HPRD  PubMed  
    P60709 P20591 MX1    HPRD  PubMed  
    P60709 Q8IUG5 MYO18B    HPRD  PubMed  
    P60709 Q12965 MYO1E    HPRD  PubMed  
    P60709 Q99972 MYOC    HPRD  PubMed  
    P60709 P61601 NCALD    HPRD  PubMed  
    P60709 P14598 NCF1    HPRD  PubMed  
    P60709 O76041 NEBL    HPRD  PubMed  
    P60709 P35228 NOS2    HPRD  PubMed  
    P60709 Q86VF7 NRAP    HPRD  PubMed  
    P60709 P21589 NT5E    HPRD  PubMed  
    P60709 Q99572 P2RX7    HPRD  PubMed  
    P60709 P49585 PCYT1A    HPRD  PubMed  
    P60709 Q96HC4 PDLIM5    HPRD  PubMed  
    P60709 O60925 PFDN1    HPRD  PubMed  
    P60709 Q9NQP4 PFDN4    HPRD  PubMed  
    P60709 P07737 PFN1    HPRD  PubMed  
    P60709 P35080 PFN2    HPRD  PubMed  
    P60709 Phosphatase and actin regulator 4 PHACTR4    HPRD  PubMed  
    P60709 Q13393 PLD1    HPRD  PubMed  
    P60709 O14939 PLD2    HPRD  PubMed  
    P60709 P24928 POLR2A    HPRD  PubMed  
    P60709 Q05655 PRKCD    HPRD  PubMed  
    P60709 P21246 PTN    HPRD  PubMed  
    P60709 P20338 RAB4A    HPRD  PubMed  
    P60709 P63000 RAC1    HPRD  PubMed  
    P60709 P15153 RAC2    HPRD  PubMed  
    P60709 P31949 S100A11    HPRD  PubMed  
    P60709 Q9Y5Y9 SCN10A    HPRD  PubMed  
    P60709 P04278 SHBG    HPRD  PubMed  
    P60709 P84022 SMAD3    HPRD  PubMed  
    P60709 O15198 SMAD9    HPRD  PubMed  
    P60709 P51532 SMARCA4    HPRD  PubMed  
    P60709 Q13813 SPTAN1    HPRD  PubMed  
    P60709 Slingshot 1 SSH1    HPRD  PubMed  
    P60709 Q76I76 SSH2    HPRD  PubMed  
    P60709 Q8TE77 SSH3    HPRD  PubMed  
    P60709 Q12846 STX4    HPRD  PubMed  
    P60709 P57105 SYNJ2BP    HPRD  PubMed  
    P60709 TANC TANC1    HPRD  PubMed  
    P60709 P21980 TGM2    HPRD  PubMed  
    P60709 P62328 TMSB4X    HPRD  PubMed  
    P60709 P48788 TNNI2    HPRD  PubMed  
    P60709 P09493 TPM1    HPRD  PubMed  
    P60709 P07951 TPM2    HPRD  PubMed  
    P60709 P06753 TPM3    HPRD  PubMed  
    P60709 P62760 VSNL1    HPRD  PubMed  
    P60709 Q92558 WASF1    HPRD  PubMed  
    P60709 Q8IV90 WASF2    HPRD  PubMed  
    P60709 Q9UPY6 WASF3    HPRD  PubMed  
    P60709 Q96QU8 XPO6    HPRD  PubMed  
    P60709 TMSL1     HPRD  PubMed  
    P60709 TMSL4     HPRD  PubMed  
    BioGRID:106575 BioGRID:106575 ACTB    BioGRID  PubMed Affinity Capture-Western; Reconstituted Complex; Two-hybrid 
    BioGRID:106575 BioGRID:106586 ACTG1    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:115404 ACTR2    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:115403 ACTR3    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:113684 AIMP2    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:106807 ANXA7    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:106957 ATF3    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:107070 BCL2L1    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:114691 BCL7C    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:120548 C20orf20    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:115760 CARM1    BioGRID  PubMed Affinity Capture-Western; Co-purification 
    BioGRID:106575 BioGRID:107315 CBL    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:115827 CCT2    BioGRID  PubMed Co-crystal Structure 
    BioGRID:106575 BioGRID:116603 CCT5    BioGRID  PubMed Co-crystal Structure 
    BioGRID:106575 BioGRID:107460 CDKN1A    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:107463 CDKN2A    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:107487 CENPA    BioGRID  PubMed Co-purification 
    BioGRID:106575 BioGRID:107499 CFL1    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:107500 CFL2    BioGRID  PubMed Affinity Capture-Western; Two-hybrid 
    BioGRID:106575 BioGRID:107872 CTGF    BioGRID  PubMed Affinity Capture-Western; Co-purification; Reconstituted Complex 
    BioGRID:106575 BioGRID:198565 Cct3    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:198567 Cct4    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:198568 Cct5    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:198569 Cct6a    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:198571 Cct7    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:198572 Cct8    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:223714 Cdk9    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:121004 DMAP1    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:116223 DSTN    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:971788 EBNA-LP    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:128178 EIF2C4    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:108325 EMD    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:108403 ESR1    BioGRID  PubMed Affinity Capture-MS; Affinity Capture-Western 
    BioGRID:106575 BioGRID:236625 Ep300    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:108465 FABP4    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:199841 Gata4    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:109268 H2AFX    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:109404 HMMR    BioGRID  PubMed Protein-peptide 
    BioGRID:106575 BioGRID:200452 Hspa1b    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:120076 INO80    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:115779 KAT5    BioGRID  PubMed Affinity Capture-MS; Co-purification 
    BioGRID:106575 BioGRID:121122 MEPCE    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:110411 MGMT    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:116134 MORF4L1    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:115001 MORF4L2    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:110694 MYC    BioGRID  PubMed Co-purification 
    BioGRID:106575 BioGRID:123839 NCALD    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:575724 NCF1    BioGRID  PubMed Far Western 
    BioGRID:106575 BioGRID:110768 NCF2    BioGRID  PubMed Far Western 
    BioGRID:106575 BioGRID:248286 P2rx7    BioGRID  PubMed Affinity Capture-MS; Affinity Capture-Western 
    BioGRID:106575 BioGRID:111136 PCK1    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:114854 PCYT1B    BioGRID  PubMed Co-crystal Structure 
    BioGRID:106575 BioGRID:111237 PFN1    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:170522 PFN1    BioGRID  PubMed Co-crystal Structure 
    BioGRID:106575 BioGRID:111426 POLR2A    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:114369 PROM1    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:111657 PSMA3    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:114513 PSTPIP1    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:198967 Pcyt1a    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:231814 Pcyt1b    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:119719 RAB8B    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:111817 RAC1    BioGRID  PubMed Far Western 
    BioGRID:106575 BioGRID:111818 RAC2    BioGRID  PubMed Far Western 
    BioGRID:106575 BioGRID:107529 RCC1    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:114166 RUVBL1    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:116067 RUVBL2    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:110263 SMAD3    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:112481 SMARCA4    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:112485 SMARCC2    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:112489 SMARCE1    BioGRID  PubMed Affinity Capture-MS; Affinity Capture-Western 
    BioGRID:106575 BioGRID:112490 SMN1    BioGRID  PubMed Affinity Capture-MS; Two-hybrid 
    BioGRID:106575 BioGRID:112590 SPTBN2    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:119950 SSH1    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:124548 SSH2    BioGRID  PubMed Reconstituted Complex 
    BioGRID:106575 BioGRID:112745 TAF11    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:106575 BioGRID:112937 TJP1    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:112938 TK1    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:113127 TTR    BioGRID  PubMed Two-hybrid 
    BioGRID:106575 BioGRID:113164 UBC    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:119509 UCHL5    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:113269 VHL    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:116168 YWHAQ    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:106575 BioGRID:1205537 gag    BioGRID  PubMed Affinity Capture-Western; FRET 
    BioGRID:106575 BioGRID:1205541 tat    BioGRID  PubMed Affinity Capture-Western 
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    General gene information

    Markers

    Genotypes

    Homology

    Pathways from BioSystems

    • Adherens junction, organism-specific biosystem (from KEGG)
      Adherens junction, organism-specific biosystemCell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation....
    • Adherens junction, conserved biosystem (from KEGG)
      Adherens junction, conserved biosystemCell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation....
    • Arrhythmogenic right ventricular cardiomyopathy (ARVC), organism-specific biosystem (from KEGG)
      Arrhythmogenic right ventricular cardiomyopathy (ARVC), organism-specific biosystemArrhythmogenic right ventricular cardiomyopathy (ARVC) is an inherited heart muscle disease that may result in arrhythmia, heart failure, and sudden death. The hallmark pathological findings are prog...
    • Arrhythmogenic right ventricular cardiomyopathy (ARVC), conserved biosystem (from KEGG)
      Arrhythmogenic right ventricular cardiomyopathy (ARVC), conserved biosystemArrhythmogenic right ventricular cardiomyopathy (ARVC) is an inherited heart muscle disease that may result in arrhythmia, heart failure, and sudden death. The hallmark pathological findings are prog...
    • Bacterial invasion of epithelial cells, organism-specific biosystem (from KEGG)
      Bacterial invasion of epithelial cells, organism-specific biosystemMany pathogenic bacteria can invade phagocytic and non-phagocytic cells and colonize them intracellularly, then become disseminated to other cells. Invasive bacteria induce their own uptake by non-ph...
    • Bacterial invasion of epithelial cells, conserved biosystem (from KEGG)
      Bacterial invasion of epithelial cells, conserved biosystemMany pathogenic bacteria can invade phagocytic and non-phagocytic cells and colonize them intracellularly, then become disseminated to other cells. Invasive bacteria induce their own uptake by non-ph...
    • Chaperonin-mediated protein folding, organism-specific biosystem (from REACTOME)
      Chaperonin-mediated protein folding, organism-specific biosystemThe eukaryotic chaperonin TCP-1 ring complex (TRiC/ CCT) plays an essential role in the folding of a subset of proteins prominent among which are the actins and tubulins (reviewed in Altschuler and...
    • Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystem (from REACTOME)
      Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystemIn the case of actin and tubulin folding, and perhaps other substrates, the emerging polypeptide chain is transferred from the ribosome to TRiC via Prefoldin (Vainberg et al., 1998).
    • Dilated cardiomyopathy, organism-specific biosystem (from KEGG)
      Dilated cardiomyopathy, organism-specific biosystemDilated cardiomyopathy (DCM) is a heart muscle disease characterised by dilation and impaired contraction of the left or both ventricles that results in progressive heart failure and sudden cardiac d...
    • Dilated cardiomyopathy, conserved biosystem (from KEGG)
      Dilated cardiomyopathy, conserved biosystemDilated cardiomyopathy (DCM) is a heart muscle disease characterised by dilation and impaired contraction of the left or both ventricles that results in progressive heart failure and sudden cardiac d...
    • Focal Adhesion, organism-specific biosystem (from WikiPathways)
      Focal Adhesion, organism-specific biosystemCell-matrix adhesions play essential roles in important biological processes including cell motility, cell proliferation, cell differentiation, regulation of gene expression and cell survival. At the...
    • Focal adhesion, organism-specific biosystem (from KEGG)
      Focal adhesion, organism-specific biosystemCell-matrix adhesions play essential roles in important biological processes including cell motility, cell proliferation, cell differentiation, regulation of gene expression and cell survival. At the...
    • Focal adhesion, conserved biosystem (from KEGG)
      Focal adhesion, conserved biosystemCell-matrix adhesions play essential roles in important biological processes including cell motility, cell proliferation, cell differentiation, regulation of gene expression and cell survival. At the...
    • Folding of actin by CCT/TriC, organism-specific biosystem (from REACTOME)
      Folding of actin by CCT/TriC, organism-specific biosystemNucleotide-independent transfer of beta-actin from prefoldin to CCT occurs when prefoldin binds to CCT (Vainberg et al., 1998). Following ATP- dependent folding within CCT (Gao et al., 1992), beta-a...
    • Gastric acid secretion, organism-specific biosystem (from KEGG)
      Gastric acid secretion, organism-specific biosystemGastric acid is a key factor in normal upper gastrointestinal functions, including protein digestion and calcium and iron absorption, as well as providing some protection against bacterial infections...
    • Gastric acid secretion, conserved biosystem (from KEGG)
      Gastric acid secretion, conserved biosystemGastric acid is a key factor in normal upper gastrointestinal functions, including protein digestion and calcium and iron absorption, as well as providing some protection against bacterial infections...
    • Hypertrophic cardiomyopathy (HCM), organism-specific biosystem (from KEGG)
      Hypertrophic cardiomyopathy (HCM), organism-specific biosystemHypertrophic cardiomyopathy (HCM) is a primary myocardial disorder with an autosomal dominant pattern of inheritance that is characterized by hypertrophy of the left ventricles with histological feat...
    • Hypertrophic cardiomyopathy (HCM), conserved biosystem (from KEGG)
      Hypertrophic cardiomyopathy (HCM), conserved biosystemHypertrophic cardiomyopathy (HCM) is a primary myocardial disorder with an autosomal dominant pattern of inheritance that is characterized by hypertrophy of the left ventricles with histological feat...
    • Influenza A, organism-specific biosystem (from KEGG)
      Influenza A, organism-specific biosystemInfluenza is a contagious respiratory disease caused by influenza virus infection. Influenza A virus is responsible for both annual seasonal epidemics and periodic worldwide pandemics. Novel strains ...
    • Influenza A, conserved biosystem (from KEGG)
      Influenza A, conserved biosystemInfluenza is a contagious respiratory disease caused by influenza virus infection. Influenza A virus is responsible for both annual seasonal epidemics and periodic worldwide pandemics. Novel strains ...
    • Leukocyte transendothelial migration, organism-specific biosystem (from KEGG)
      Leukocyte transendothelial migration, organism-specific biosystemLeukocyte migaration from the blood into tissues is vital for immune surveillance and inflammation. During this diapedesis of leukocytes, the leukocytes bind to endothelial cell adhesion molecules (C...
    • Leukocyte transendothelial migration, conserved biosystem (from KEGG)
      Leukocyte transendothelial migration, conserved biosystemLeukocyte migaration from the blood into tissues is vital for immune surveillance and inflammation. During this diapedesis of leukocytes, the leukocytes bind to endothelial cell adhesion molecules (C...
    • Metabolism of proteins, organism-specific biosystem (from REACTOME)
      Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
    • Myometrial Relaxation and Contraction Pathways, organism-specific biosystem (from WikiPathways)
      Myometrial Relaxation and Contraction Pathways, organism-specific biosystemThis pathway illustrates signaling networks implicated in uterine muscle contraction at labor and quiescence throughout gestation (pregnancy). The muscle of the uterus, responsible for contractile ac...
    • Pathogenic Escherichia coli infection, organism-specific biosystem (from KEGG)
      Pathogenic Escherichia coli infection, organism-specific biosystemEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction o...
    • Pathogenic Escherichia coli infection, conserved biosystem (from KEGG)
      Pathogenic Escherichia coli infection, conserved biosystemEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction o...
    • Phagosome, organism-specific biosystem (from KEGG)
      Phagosome, organism-specific biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
    • Phagosome, conserved biosystem (from KEGG)
      Phagosome, conserved biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
    • Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystem (from REACTOME)
      Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystemUnfolded actins and tubulins bound to prefoldin are transferred to CCT via a docking mechanism (McCormack and Willison, 2001).
    • Protein folding, organism-specific biosystem (from REACTOME)
      Protein folding, organism-specific biosystemDue to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and...
    • Regulation of Actin Cytoskeleton, organism-specific biosystem (from WikiPathways)
      Regulation of Actin Cytoskeleton, organism-specific biosystem
      Regulation of Actin Cytoskeleton
    • Regulation of actin cytoskeleton, organism-specific biosystem (from KEGG)
      Regulation of actin cytoskeleton, organism-specific biosystem
      Regulation of actin cytoskeleton
    • Regulation of actin cytoskeleton, conserved biosystem (from KEGG)
      Regulation of actin cytoskeleton, conserved biosystem
      Regulation of actin cytoskeleton
    • Salmonella infection, organism-specific biosystem (from KEGG)
      Salmonella infection, organism-specific biosystemSalmonella infection usually presents as a self-limiting gastroenteritis or the more severe typhoid fever and bacteremia. The common disease-causing Salmonella species in human is a single species, S...
    • Salmonella infection, conserved biosystem (from KEGG)
      Salmonella infection, conserved biosystemSalmonella infection usually presents as a self-limiting gastroenteritis or the more severe typhoid fever and bacteremia. The common disease-causing Salmonella species in human is a single species, S...
    • Shigellosis, organism-specific biosystem (from KEGG)
      Shigellosis, organism-specific biosystemShigellosis, or bacillary dysentery, is an intestinal infection caused by Shigella, a genus of enterobacteria. Shigella are potential food-borne pathogens that are capable of colonizing the intestina...
    • Tight junction, organism-specific biosystem (from KEGG)
      Tight junction, organism-specific biosystemEpithelial tight junctions (TJs) are composed of at least three types of transmembrane protein -occludin, claudin and junctional adhesion molecules (JAMs)- and a cytoplasmic 'plaque' consisting of ma...
    • Tight junction, conserved biosystem (from KEGG)
      Tight junction, conserved biosystemEpithelial tight junctions (TJs) are composed of at least three types of transmembrane protein -occludin, claudin and junctional adhesion molecules (JAMs)- and a cytoplasmic 'plaque' consisting of ma...
    • Vibrio cholerae infection, organism-specific biosystem (from KEGG)
      Vibrio cholerae infection, organism-specific biosystemCholera toxin (CTX) is one of the main virulence factors of Vibrio cholerae. Once secreted, CTX B-chain (CTXB) binds to ganglioside GM1 on the surface of the host's cells. After binding takes place, ...
    • Vibrio cholerae infection, conserved biosystem (from KEGG)
      Vibrio cholerae infection, conserved biosystemCholera toxin (CTX) is one of the main virulence factors of Vibrio cholerae. Once secreted, CTX B-chain (CTXB) binds to ganglioside GM1 on the surface of the host's cells. After binding takes place, ...
    • Viral myocarditis, organism-specific biosystem (from KEGG)
      Viral myocarditis, organism-specific biosystemMyocarditis is a cardiac disease associated with inflammation and injury of the myocardium. It results from various etiologies, both noninfectious and infectious, but coxsackievirus B3 (CVB3) is stil...

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Tat protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    kinesin binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    nitric-oxide synthase binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    protein binding IPI
    Inferred from Physical Interaction
    more info
    		  
    protein kinase binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    structural constituent of cytoskeleton TAS
    Traceable Author Statement
    more info
    		 PubMed 
    Process Evidence Code Pubs
    'de novo' posttranslational protein folding TAS
    Traceable Author Statement
    more info
    		  
    adherens junction organization TAS
    Traceable Author Statement
    more info
    		  
    axon guidance TAS
    Traceable Author Statement
    more info
    		  
    blood coagulation TAS
    Traceable Author Statement
    more info
    		  
    cell junction assembly TAS
    Traceable Author Statement
    more info
    		  
    cell-cell junction organization TAS
    Traceable Author Statement
    more info
    		  
    cellular component movement TAS
    Traceable Author Statement
    more info
    		 PubMed 
    cellular protein metabolic process TAS
    Traceable Author Statement
    more info
    		  
    protein folding TAS
    Traceable Author Statement
    more info
    		  
    response to calcium ion IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    MLL5-L complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    NuA4 histone acetyltransferase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    axon IEA
    Inferred from Electronic Annotation
    more info
    		  
    cortical cytoskeleton IEA
    Inferred from Electronic Annotation
    more info
    		  
    cytoplasm TAS
    Traceable Author Statement
    more info
    		 PubMed 
    cytoskeleton TAS
    Traceable Author Statement
    more info
    		 PubMed 
    cytosol TAS
    Traceable Author Statement
    more info
    		  
    protein complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    ribonucleoprotein complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    soluble fraction IEA
    Inferred from Electronic Annotation
    more info
    		  
    Help top of page

    General protein information

    Preferred Names
    actin, cytoplasmic 1
    Names
    actin, cytoplasmic 1
    beta cytoskeletal actin
    PS1TP5-binding protein 1
    Help top of page

    NCBI Reference Sequences (RefSeq)

    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_007992.1 RefSeqGene

      Range
      5001..8454
      Download
      GenBank, FASTA, Sequence Viewer (Graphics), LRG_132

    mRNA and Protein(s)

    1. NM_001101.3 → NP_001092.1  actin, cytoplasmic 1

      Status: REVIEWED

      Source sequence(s)
      AK130157, BC009636
      Consensus CDS
      CCDS5341.1
      UniProtKB/Swiss-Prot
      P60709
      UniProtKB/TrEMBL
      Q1KLZ0
      Related
      ENSP00000349960, OTTHUMP00000024886, ENST00000331789, OTTHUMT00000059589
      Conserved Domains (2) summary
      cd00012
      Location:7 – 373
      Blast Score: 1513
      ACTIN; Actin; An ubiquitous protein involved in the formation of filaments that are a major component of the cytoskeleton. Interaction with myosin provides the basis of muscular contraction and many aspects of cell motility. Each actin protomer binds one ...
      pfam00022
      Location:3 – 375
      Blast Score: 1706
      Actin; Actin

    RefSeqs of Annotated Genomes: Build 37.3

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

    Reference GRCh37.p5 Primary Assembly

    Genomic

    1. NC_000007.13 Reference GRCh37.p5 Primary Assembly

      Range
      5566779..5570232, complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate HuRef

    Genomic

    1. AC_000139.1 Alternate HuRef

      Range
      5479343..5482774, complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate CRA_TCAGchr7v2

    Genomic

    1. AC_000068.1 Alternate CRA_TCAGchr7v2

      Range
      5613124..5616577, complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Help top of page

    Related Sequences

    Nucleotide Protein
    Heading Accession and Version
    genomic AC006483.3 AAP22343.1
    genomic AY582799.1 AAS79319.1
    genomic AY970442.1 AAX82251.1
    genomic CH471144.1 EAW87341.1
      EAW87343.1
    genomic CS081475.1 CAI95947.1
    genomic FB571104.1 CAR95103.1
    genomic FB668235.1 CAS92761.1
    genomic GN346972.1 CAY56012.1
    genomic M10277.1 AAA51567.1
    mRNA AK025375.1 None
    mRNA AK058019.1 None
    mRNA AK098751.1 None
    mRNA AK130062.1 None
    mRNA AK130157.1 None
    mRNA AK222925.1 BAD96645.1
    mRNA AK223032.1 BAD96752.1
    mRNA AK223055.1 BAD96775.1
    mRNA AK225414.1 None
    mRNA AK301372.1 BAG62914.1
    mRNA AK304552.1 BAG65347.1
    mRNA AK308277.1 None
    mRNA AK309997.1 None
    mRNA AK316361.1 BAH14732.1
    mRNA BC001301.1 AAH01301.1
    mRNA BC002409.2 AAH02409.1
    mRNA BC004251.1 AAH04251.1
    mRNA BC008633.1 AAH08633.1
    mRNA BC009636.1 None
    mRNA BC012854.1 AAH12854.1
    mRNA BC013380.2 AAH13380.1
    mRNA BC013835.1 None
    mRNA BC014401.1 None
    mRNA BC014861.1 AAH14861.1
    mRNA BC016045.1 AAH16045.1
    mRNA BC023204.1 None
    mRNA BC113036.1 AAI13037.1
    mRNA D28354.1 BAA05720.1
    mRNA DQ407611.1 ABD66582.1
    mRNA DQ471327.1 ABF01018.1
    mRNA EF036500.1 ABO65086.1
    mRNA EF095209.1 ABL01513.1
    mRNA K00790.1 AAA51578.1
    mRNA M28424.1 AAB16906.1
    mRNA V00478.1 CAA23745.1
    mRNA X00351.1 CAA25099.1
    mRNA X63432.1 CAA45026.1
    other-genetic DQ890960.2 ABM81886.1
    other-genetic DQ894128.2 ABM85054.1
    Protein Accession Links
    GenPept Link UniProtKB Link
    A0AUL6 GenPept UniProtKB/TrEMBL:A0AUL6
    P60709.1 GenPept UniProtKB/Swiss-Prot:P60709
    Q1KLZ0 GenPept UniProtKB/TrEMBL:Q1KLZ0
    Q53G76 GenPept UniProtKB/TrEMBL:Q53G76
    Q53G99 GenPept UniProtKB/TrEMBL:Q53G99
    Q53GK6 GenPept UniProtKB/TrEMBL:Q53GK6
    Q562L3 GenPept UniProtKB/TrEMBL:Q562L3
    Q562S0 GenPept UniProtKB/TrEMBL:Q562S0
    Q9UE89 GenPept UniProtKB/TrEMBL:Q9UE89
    Q9UMN3 GenPept UniProtKB/TrEMBL:Q9UMN3
    Help top of page

    Additional Links

    Additional Links

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Chemical Information
    Medical
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