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Beta-actin

 
Wikipedia: Beta-actin
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Actin, beta
PDB rendering based on 1atn.
Available structures: 1atn, 1c0f, 1c0g, 1d4x, 1dej, 1eqy, 1esv, 1h1v, 1hlu, 1ijj, 1j6z, 1kxp, 1lcu, 1lot, 1m8q, 1ma9, 1mdu, 1mvw, 1nlv, 1nm1, 1nmd, 1nwk, 1o18, 1o19, 1o1a, 1o1b, 1o1c, 1o1d, 1o1e, 1o1f, 1o1g, 1p8z, 1qz5, 1qz6, 1rdw, 1rfq, 1rgi, 1s22, 1sqk, 1t44, 1wua, 1y64, 1yxq, 2a3z, 2a40, 2a41, 2a42, 2a5x, 2asm, 2aso, 2asp, 2btf, 2d1k, 2ff3, 2ff6, 2fxu, 2gwj, 2gwk, 2hf3, 2hf4, 2hmp, 2oan, 2q1n, 2q31, 2q36
Identifiers
Symbols ACTB; PS1TP5BP1
External IDs OMIM: 102630 MGI87904 HomoloGene74383
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 60 11461
Ensembl ENSG00000075624 ENSMUSG00000029580
Uniprot P60709 A1E281
Refseq NM_001101 (mRNA)
NP_001092 (protein)
NM_007393 (mRNA)
NP_031419 (protein)
Location Chr 7: 5.53 - 5.54 Mb Chr 5: 143.17 - 143.17 Mb
Pubmed search [1] [2]

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.[1]

Contents

Interactions

Beta-actin has been shown to interact with SPTBN2.[2][3]

References

  1. ^ "Entrez Gene: ACTB actin, beta". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=60. 
  2. ^ 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 (England) 411 (6835): 321-5. doi:10.1038/35077108. ISSN 0028-0836. PMID 11357114. 
  3. ^ Holleran, E A; Ligon L A, Tokito M, Stankewich M C, Morrow J S, Holzbaur E L (Sep. 2001). "beta III spectrin binds to the Arp1 subunit of dynactin". J. Biol. Chem. (United States) 276 (39): 36598-605. doi:10.1074/jbc.M104838200. ISSN 0021-9258. PMID 11461920. 

Further reading

  • Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease.". Folia Biol. (Praha) 42 (5): 227–30. PMID 8997639. 
  • Gunning P, Weinberger R, Jeffrey P (1997). "Actin and tropomyosin isoforms in morphogenesis.". Anat. Embryol. 195 (4): 311–5. doi:10.1007/s004290050050. PMID 9108196. 
  • Kimura T, Hashimoto I, Nishikawa M, Fujisawa JI (1997). "A role for Rev in the association of HIV-1 gag mRNA with cytoskeletal beta-actin and viral protein expression.". Biochimie 78 (11-12): 1075–80. doi:10.1016/S0300-9084(97)86732-6. PMID 9150887. 
  • Szentirmay MN, Sawadogo M (2000). "Spatial organization of RNA polymerase II transcription in the nucleus.". Nucleic Acids Res. 28 (10): 2019–25. doi:10.1093/nar/28.10.2019. PMID 10773068. 
  • Anderson JL, Hope TJ (2005). "HIV accessory proteins and surviving the host cell.". Current HIV/AIDS reports 1 (1): 47–53. doi:10.1007/s11904-004-0007-x. PMID 16091223. 
  • Pederson T, Aebi U (2006). "Nuclear actin extends, with no contraction in sight.". Mol. Biol. Cell 16 (11): 5055–60. doi:10.1091/mbc.E05-07-0656. PMID 16148048. 

See also




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