Actinin, alpha 1

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Actinin, alpha 1
Protein ACTN1 PDB 1sjj.png
PDB rendering based on 1sjj.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols ACTN1 ; BDPLT15
External IDs OMIM102575 MGI2137706 HomoloGene55553 GeneCards: ACTN1 Gene
RNA expression pattern
PBB GE ACTN1 208636 at tn.png
PBB GE ACTN1 208637 x at tn.png
PBB GE ACTN1 211160 x at tn.png
More reference expression data
Species Human Mouse
Entrez 87 109711
Ensembl ENSG00000072110 ENSMUSG00000015143
UniProt P12814 Q7TPR4
RefSeq (mRNA) NM_001102 NM_134156
RefSeq (protein) NP_001093 NP_598917
Location (UCSC) Chr 14:
68.87 – 68.98 Mb
Chr 12:
80.17 – 80.26 Mb
PubMed search [1] [2]

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.[1]


Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene.[2]


Actinin, alpha 1 has been shown to interact with:

See also[edit]


  1. ^ Youssoufian H, McAfee M, Kwiatkowski DJ (Jul 1990). "Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene". Am J Hum Genet 47 (1): 62–72. PMC 1683765. PMID 2349951. 
  2. ^ "Entrez Gene: ACTN1 actinin, alpha 1". 
  3. ^ a b Dhavan R, Greer PL, Morabito MA, Orlando LR, Tsai LH (September 2002). "The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner". J. Neurosci. 22 (18): 7879–91. PMID 12223541. 
  4. ^ Gonzalez AM, Otey C, Edlund M, Jones JC (December 2001). "Interactions of a hemidesmosome component and actinin family members". J. Cell. Sci. 114 (Pt 23): 4197–206. PMID 11739652. 
  5. ^ Bunn RC, Jensen MA, Reed BC (April 1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell 10 (4): 819–32. doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040. 
  6. ^ Vallenius T, Luukko K, Mäkelä TP (April 2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. PMID 10753915. 
  7. ^ Bauer K, Kratzer M, Otte M, de Quintana KL, Hagmann J, Arnold GJ, Eckerskorn C, Lottspeich F, Siess W (December 2000). "Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells". Blood 96 (13): 4236–45. PMID 11110697. 
  8. ^ Feng S, Reséndiz JC, Christodoulides N, Lu X, Arboleda D, Berndt MC, Kroll MH (January 2002). "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry 41 (4): 1100–8. doi:10.1021/bi0156005. PMID 11802708. 
  9. ^ Asada M, Irie K, Morimoto K, Yamada A, Ikeda W, Takeuchi M, Takai Y (February 2003). "ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions". J. Biol. Chem. 278 (6): 4103–11. doi:10.1074/jbc.M209832200. PMID 12446711. 
  10. ^ Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (May 1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. PMID 10224105. 
  11. ^ Li B, Trueb B (September 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. doi:10.1074/jbc.M100789200. PMID 11423549. 
  12. ^ Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A (2006). "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).". Brain Res 1116 (1): 50–7. doi:10.1016/j.brainres.2006.07.122. PMID 16973135. 

Further reading[edit]

External links[edit]