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Actin, beta
Protein ACTB PDB 1atn.png
PDB rendering based on 1atn.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols ACTB ; BRWS1; PS1TP5BP1
External IDs OMIM102630 MGI87904 HomoloGene110648 GeneCards: ACTB Gene
RNA expression pattern
PBB GE ACTB 200801 x at tn.png
PBB GE ACTB 213867 x at tn.png
More reference expression data
Species Human Mouse
Entrez 60 11461
Ensembl ENSG00000075624 ENSMUSG00000029580
UniProt P60709 P60710
RefSeq (mRNA) NM_001101 NM_007393
RefSeq (protein) NP_001092 NP_031419
Location (UCSC) Chr 7:
5.53 – 5.56 Mb
Chr 5:
142.9 – 142.91 Mb
PubMed search [1] [2]

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]


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[edit]

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


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.


  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. 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. 

Further reading[edit]

See also[edit]