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{{Infobox_gene}}
'''Beta-actin''' (human gene and protein symbol '''''ACTB'''''/'''ACTB''') is one of six different [[actin]] isoforms which have been identified in humans.  This is one of the two nonmuscle [[cytoskeletal]] actins.  Actins are highly conserved proteins<ref name=gunning>{{cite journal | vauthors = Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC | title = The evolution of compositionally and functionally distinct actin filaments | journal = Journal of Cell Science | volume = 128 | issue = 11 | pages = 2009–2019 | date = Jun 2015 | pmid = 25788699 | doi = 10.1242/jcs.165563 }}</ref><ref name="pmid6842590">{{cite journal | vauthors = Hanukoglu I, Tanese N, Fuchs E | title = Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions | journal = Journal of Molecular Biology | volume = 163 | issue = 4 | pages = 673–8 | date = Feb 1983 | pmid = 6842590 | doi = 10.1016/0022-2836(83)90117-1 }}</ref> that are involved in cell motility, structure and integrity.  Alpha actins are a major constituent of the contractile apparatus.<ref>{{cite web | title = Entrez Gene: ACTB actin, beta| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=60| accessdate = }}</ref>


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Beta-actin has been shown to [[Protein-protein interaction|interact]] with [[SPTBN2]].<ref name="pmid11357136">{{cite journal | vauthors = Mao B, Wu W, Li Y, Hoppe D, Stannek P, Glinka A, Niehrs C | title = LDL-receptor-related protein 6 is a receptor for Dickkopf proteins | journal = Nature | volume = 411 | issue = 6835 | pages = 321–5 | date = May 2001 | pmid = 11357136 | doi = 10.1038/35077108 }}</ref><ref name="pmid11461920">{{cite journal | vauthors = Holleran EA, Ligon LA, Tokito M, Stankewich MC, Morrow JS, Holzbaur EL | title = beta III spectrin binds to the Arp1 subunit of dynactin | journal = The Journal of Biological Chemistry | volume = 276 | issue = 39 | pages = 36598–605 | date = Sep 2001 | pmid = 11461920 | doi = 10.1074/jbc.M104838200 }}</ref> In addition, [[RNA-binding protein]] Sam68 was found to interact with the mRNA encoding β-actin, which regulates the synaptic formation of the dendritic spines with its cytoskeletal components.
{{GNF_Protein_box
| image = PBB_Protein_ACTB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1atn.
| PDB = {{PDB2|1atn}}, {{PDB2|1c0f}}, {{PDB2|1c0g}}, {{PDB2|1d4x}}, {{PDB2|1dej}}, {{PDB2|1eqy}}, {{PDB2|1esv}}, {{PDB2|1h1v}}, {{PDB2|1hlu}}, {{PDB2|1ijj}}, {{PDB2|1j6z}}, {{PDB2|1kxp}}, {{PDB2|1lcu}}, {{PDB2|1lot}}, {{PDB2|1m8q}}, {{PDB2|1ma9}}, {{PDB2|1mdu}}, {{PDB2|1mvw}}, {{PDB2|1nlv}}, {{PDB2|1nm1}}, {{PDB2|1nmd}}, {{PDB2|1nwk}}, {{PDB2|1o18}}, {{PDB2|1o19}}, {{PDB2|1o1a}}, {{PDB2|1o1b}}, {{PDB2|1o1c}}, {{PDB2|1o1d}}, {{PDB2|1o1e}}, {{PDB2|1o1f}}, {{PDB2|1o1g}}, {{PDB2|1p8z}}, {{PDB2|1qz5}}, {{PDB2|1qz6}}, {{PDB2|1rdw}}, {{PDB2|1rfq}}, {{PDB2|1rgi}}, {{PDB2|1s22}}, {{PDB2|1sqk}}, {{PDB2|1t44}}, {{PDB2|1wua}}, {{PDB2|1y64}}, {{PDB2|1yxq}}, {{PDB2|2a3z}}, {{PDB2|2a40}}, {{PDB2|2a41}}, {{PDB2|2a42}}, {{PDB2|2a5x}}, {{PDB2|2asm}}, {{PDB2|2aso}}, {{PDB2|2asp}}, {{PDB2|2btf}}, {{PDB2|2d1k}}, {{PDB2|2ff3}}, {{PDB2|2ff6}}, {{PDB2|2fxu}}, {{PDB2|2gwj}}, {{PDB2|2gwk}}, {{PDB2|2hf3}}, {{PDB2|2hf4}}, {{PDB2|2hmp}}, {{PDB2|2oan}}, {{PDB2|2q1n}}, {{PDB2|2q31}}, {{PDB2|2q36}}
| Name = Actin, beta
| HGNCid = 132
| Symbol = ACTB
| AltSymbols =; PS1TP5BP1
| OMIM = 102630
| ECnumber =
| Homologene = 74383
| MGIid = 87904
| GeneAtlas_image1 = PBB_GE_ACTB_200801_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACTB_213867_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0035267 |text = NuA4 histone acetyltransferase complex}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 60
    | Hs_Ensembl = ENSG00000075624
    | Hs_RefseqProtein = NP_001092
    | Hs_RefseqmRNA = NM_001101
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 5533313
    | Hs_GenLoc_end = 5535814
    | Hs_Uniprot = P60709
    | Mm_EntrezGene = 11461
    | Mm_Ensembl = ENSMUSG00000029580
    | Mm_RefseqmRNA = NM_007393
    | Mm_RefseqProtein = NP_031419
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 143168256
    | Mm_GenLoc_end = 143171864
    | Mm_Uniprot = A1E281
  }}
}}
'''Beta-actin (gene name ACTB)''' is one of six different [[actin]] isoforms which have been identified in humans.  This is one of the two nonmuscle [[cytoskeletal]] actins. Actins are highly conserved proteins that are involved in cell motility, structure and integrity.  Alpha actins are a major constituent of the contractile apparatus.<ref>{{cite web | title = Entrez Gene: ACTB actin, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=60| accessdate = }}</ref>


==References==
Beta-actin has been shown to activate [[Endothelial NOS|eNOS]], thereby increasing NO production. An eight-amino acid residue (326-333) in actin has been shown to mediate the interaction between actin and eNOS<ref name=Actin_Enos>{{cite journal | vauthors = Kondrikov D, Fonseca FV, Elms S, Fulton D, Black SM, Block ER, Su Y | title = Beta-actin association with endothelial nitric-oxide synthase modulates nitric oxide and superoxide generation from the enzyme | journal = The Journal of Biological Chemistry | volume = 285 | issue = 7 | pages = 4319–27 | date = Feb 2010 | pmid = 19946124 | doi = 10.1074/jbc.M109.063172 | pmc=2836036}}</ref>
 
== Clinical relevance ==
 
Recurrent mutations in this gene have been associated to cases of [[diffuse large B-cell lymphoma]].<ref name="pmid22343534">{{cite journal | vauthors = Lohr JG, Stojanov P, Lawrence MS, Auclair D, Chapuy B, Sougnez C, Cruz-Gordillo P, Knoechel B, Asmann YW, Slager SL, Novak AJ, Dogan A, Ansell SM, Link BK, Zou L, Gould J, Saksena G, Stransky N, Rangel-Escareño C, Fernandez-Lopez JC, Hidalgo-Miranda A, Melendez-Zajgla J, Hernández-Lemus E, Schwarz-Cruz y Celis A, Imaz-Rosshandler I, Ojesina AI, Jung J, Pedamallu CS, Lander ES, Habermann TM, Cerhan JR, Shipp MA, Getz G, Golub TR | title = Discovery and prioritization of somatic mutations in diffuse large B-cell lymphoma (DLBCL) by whole-exome sequencing | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 109 | issue = 10 | pages = 3879–84 | date = Mar 2012 | pmid = 22343534 | pmc = 3309757 | doi = 10.1073/pnas.1121343109 }}</ref>
 
== Applications ==
 
Beta actin is usually used as a [[Western blot normalization|loading control]], for among others, the integrity of cells, [[protein degradation]], in [[PCR]] and [[Western blotting]]. Its molecular weight is approximately 42 kDa.
 
== References ==
{{reflist}}
{{reflist}}


==Further reading==
==External links==
* {{UCSC gene info|ACTB}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Vandekerckhove J, Leavitt J, Kakunaga T, Weber K  | title = Coexpression of a mutant beta-actin and the two normal beta- and gamma-cytoplasmic actins in a stably transformed human cell line | journal = Cell | volume = 22 | issue = 3 | pages = 893–9 | year = 1980 | pmid = 6893954 | doi=10.1016/0092-8674(80)90566-8}}
| citations =  
* {{cite journal | vauthors = Leavitt J, Gunning P, Porreca P, Ng SY, Lin CS, Kedes L | title = Molecular cloning and characterization of mutant and wild-type human beta-actin genes | journal = Mol Cell Biology | volume = 4 | issue = 10 | pages = 1961–9 | date = 1984 | pmid = 6095033 | doi=10.1128/mcb.4.10.1961 | pmc=369012}}
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
* {{cite journal | vauthors = Ng SY, Gunning P, Eddy R, Ponte P, Leavitt J, Shows T, Kedes L | title = Evolution of the functional human beta-actin gene and its multi-pseudogene family: conservation of noncoding regions and chromosomal dispersion of pseudogenes | journal = Mol Cell Biology | volume = 5 | issue = 10 | pages = 2720–32 | year = 1985 | pmid = 3837182 | doi=10.1128/mcb.5.10.2720 | pmc=367010}}
*{{cite journal | author=Gunning P, Weinberger R, Jeffrey P |title=Actin and tropomyosin isoforms in morphogenesis. |journal=Anat. Embryol. |volume=195 |issue= 4 |pages= 311-5 |year= 1997 |pmid= 9108196 |doi= }}
* {{cite journal | vauthors = Snásel J, Pichová I | title = The cleavage of host cell proteins by HIV-1 protease | journal = Folia Biologica | volume = 42 | issue = 5 | pages = 227–30 | year = 1997 | pmid = 8997639 | doi = 10.1007/BF02818986 }}
*{{cite journal | author=Kimura T, Hashimoto I, Nishikawa M, Fujisawa JI |title=A role for Rev in the association of HIV-1 gag mRNA with cytoskeletal beta-actin and viral protein expression. |journal=Biochimie |volume=78 |issue= 11-12 |pages= 1075-80 |year= 1997 |pmid= 9150887 |doi= }}
* {{cite journal | vauthors = Gunning P, Weinberger R, Jeffrey P | title = Actin and tropomyosin isoforms in morphogenesis | journal = Anatomy and Embryology | volume = 195 | issue = 4 | pages = 311–5 | date = Apr 1997 | pmid = 9108196 | doi = 10.1007/s004290050050 }}
*{{cite journal | author=Szentirmay MN, Sawadogo M |title=Spatial organization of RNA polymerase II transcription in the nucleus. |journal=Nucleic Acids Res. |volume=28 |issue= 10 |pages= 2019-25 |year= 2000 |pmid= 10773068 |doi= }}
* {{cite journal | vauthors = Kimura T, Hashimoto I, Nishikawa M, Fujisawa JI | title = A role for Rev in the association of HIV-1 gag mRNA with cytoskeletal beta-actin and viral protein expression | journal = Biochimie | volume = 78 | issue = 11–12 | pages = 1075–80 | year = 1997 | pmid = 9150887 | doi = 10.1016/S0300-9084(97)86732-6 }}
*{{cite journal | author=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell. |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47-53 |year= 2005 |pmid= 16091223 |doi= }}
* {{cite journal | vauthors = Szentirmay MN, Sawadogo M | title = Spatial organization of RNA polymerase II transcription in the nucleus | journal = Nucleic Acids Research | volume = 28 | issue = 10 | pages = 2019–25 | date = May 2000 | pmid = 10773068 | pmc = 105382 | doi = 10.1093/nar/28.10.2019 }}
*{{cite journal | author=Pederson T, Aebi U |title=Nuclear actin extends, with no contraction in sight. |journal=Mol. Biol. Cell |volume=16 |issue= 11 |pages= 5055-60 |year= 2006 |pmid= 16148048 |doi= 10.1091/mbc.E05-07-0656 }}
* {{cite journal | vauthors = Anderson JL, Hope TJ | title = HIV accessory proteins and surviving the host cell | journal = Current HIV/AIDS Reports | volume = 1 | issue = 1 | pages = 47–53 | date = Apr 2004 | pmid = 16091223 | doi = 10.1007/s11904-004-0007-x }}
}}
* {{cite journal | vauthors = Pederson T, Aebi U | title = Nuclear actin extends, with no contraction in sight | journal = Molecular Biology of the Cell | volume = 16 | issue = 11 | pages = 5055–60 | date = Nov 2005 | pmid = 16148048 | pmc = 1266405 | doi = 10.1091/mbc.E05-07-0656 | url = http://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2383&context=oapubs }}
* {{cite journal | vauthors = Perrin BJ, Ervasti JM | title = The actin gene family: function follows isoform | journal = Cytoskeleton | volume = 67 | issue = 10 | pages = 630–4 | date = Oct 2010 | pmid = 20737541 | pmc = 2949686 | doi = 10.1002/cm.20475 }}
{{refend}}
{{refend}}


==See also==
== See also ==
* [[Actin]]
* [[Actin]]
* [[ACTA1]]
* [[ACTA1]]
{{PDB Gallery|geneid=60}}
{{Cytoskeletal Proteins}}




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Latest revision as of 14:10, 4 November 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Beta-actin (human gene and protein symbol ACTB/ACTB) is one of six different actin isoforms which have been identified in humans. This is one of the two nonmuscle cytoskeletal actins. Actins are highly conserved proteins[1][2] that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.[3]

Interactions

Beta-actin has been shown to interact with SPTBN2.[4][5] In addition, RNA-binding protein Sam68 was found to interact with the mRNA encoding β-actin, which regulates the synaptic formation of the dendritic spines with its cytoskeletal components.

Beta-actin has been shown to activate eNOS, thereby increasing NO production. An eight-amino acid residue (326-333) in actin has been shown to mediate the interaction between actin and eNOS[6]

Clinical relevance

Recurrent mutations in this gene have been associated to cases of diffuse large B-cell lymphoma.[7]

Applications

Beta actin is usually used as a loading control, for among others, the integrity of cells, protein degradation, in PCR and Western blotting. Its molecular weight is approximately 42 kDa.

References

  1. ↑ Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC (Jun 2015). "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009–2019. doi:10.1242/jcs.165563. PMID 25788699.
  2. ↑ Hanukoglu I, Tanese N, Fuchs E (Feb 1983). "Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions". Journal of Molecular Biology. 163 (4): 673–8. doi:10.1016/0022-2836(83)90117-1. PMID 6842590.
  3. ↑ "Entrez Gene: ACTB actin, beta".
  4. ↑ Mao B, Wu W, Li Y, Hoppe D, Stannek P, Glinka A, Niehrs C (May 2001). "LDL-receptor-related protein 6 is a receptor for Dickkopf proteins". Nature. 411 (6835): 321–5. doi:10.1038/35077108. PMID 11357136.
  5. ↑ Holleran EA, Ligon LA, Tokito M, Stankewich MC, Morrow JS, Holzbaur EL (Sep 2001). "beta III spectrin binds to the Arp1 subunit of dynactin". The Journal of Biological Chemistry. 276 (39): 36598–605. doi:10.1074/jbc.M104838200. PMID 11461920.
  6. ↑ Kondrikov D, Fonseca FV, Elms S, Fulton D, Black SM, Block ER, Su Y (Feb 2010). "Beta-actin association with endothelial nitric-oxide synthase modulates nitric oxide and superoxide generation from the enzyme". The Journal of Biological Chemistry. 285 (7): 4319–27. doi:10.1074/jbc.M109.063172. PMC 2836036. PMID 19946124.
  7. ↑ Lohr JG, Stojanov P, Lawrence MS, Auclair D, Chapuy B, Sougnez C, Cruz-Gordillo P, Knoechel B, Asmann YW, Slager SL, Novak AJ, Dogan A, Ansell SM, Link BK, Zou L, Gould J, Saksena G, Stransky N, Rangel-Escareño C, Fernandez-Lopez JC, Hidalgo-Miranda A, Melendez-Zajgla J, Hernández-Lemus E, Schwarz-Cruz y Celis A, Imaz-Rosshandler I, Ojesina AI, Jung J, Pedamallu CS, Lander ES, Habermann TM, Cerhan JR, Shipp MA, Getz G, Golub TR (Mar 2012). "Discovery and prioritization of somatic mutations in diffuse large B-cell lymphoma (DLBCL) by whole-exome sequencing". Proceedings of the National Academy of Sciences of the United States of America. 109 (10): 3879–84. doi:10.1073/pnas.1121343109. PMC 3309757. PMID 22343534.

External links

Further reading

See also


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