Actinin alpha 1

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ACTN1
Protein ACTN1 PDB 1sjj.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACTN1, BDPLT15, actinin alpha 1
External IDsOMIM: 102575 MGI: 2137706 HomoloGene: 55553 GeneCards: ACTN1
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for ACTN1
Genomic location for ACTN1
Band14q24.1|14q22-q24Start68,874,143 bp[1]
End68,979,440 bp[1]
RNA expression pattern
PBB GE ACTN1 211160 x at fs.png

PBB GE ACTN1 208636 at fs.png

PBB GE ACTN1 208637 x at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001102
NM_001130004
NM_001130005

NM_134156
NM_001346669

RefSeq (protein)

NP_001093
NP_001123476
NP_001123477
NP_001093.1

NP_001333598
NP_598917

Location (UCSC)Chr 14: 68.87 – 68.98 MbChr 12: 80.17 – 80.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.[5]

Function[edit]

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.[6]

Interactions[edit]

Actinin, alpha 1 has been shown to interact with:

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000072110 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000015143 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ "Entrez Gene: ACTN1 actinin, alpha 1".
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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.
  13. ^ 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.
  14. ^ 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.
  15. ^ 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.
  16. ^ 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]