SPTBN2

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Spectrin, beta, non-erythrocytic 2
File:PBB Protein SPTBN2 image.jpg
PDB rendering based on 1wjm.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SPTBN2 ; SCA5
External IDs Template:OMIM5 Template:MGI HomoloGene48482
RNA expression pattern
File:PBB GE SPTBN2 205155 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Spectrin, beta, non-erythrocytic 2, also known as SPTBN2, is a human gene.[1]


References

  1. "Entrez Gene: SPTBN2 spectrin, beta, non-erythrocytic 2".

Further reading

  • De Matteis MA, Morrow JS (2000). "Spectrin tethers and mesh in the biosynthetic pathway". J. Cell. Sci. 113 ( Pt 13): 2331–43. PMID 10852813.
  • Ranum LP, Schut LJ, Lundgren JK; et al. (1995). "Spinocerebellar ataxia type 5 in a family descended from the grandparents of President Lincoln maps to chromosome 11". Nat. Genet. 8 (3): 280–4. doi:10.1038/ng1194-280. PMID 7874171.
  • Nagase T, Ishikawa K, Nakajima D; et al. (1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 4 (2): 141–50. PMID 9205841.
  • Ohara O, Ohara R, Yamakawa H; et al. (1998). "Characterization of a new beta-spectrin gene which is predominantly expressed in brain". Brain Res. Mol. Brain Res. 57 (2): 181–92. PMID 9675416.
  • Sakaguchi G, Orita S, Naito A; et al. (1998). "A novel brain-specific isoform of beta spectrin: isolation and its interaction with Munc13". Biochem. Biophys. Res. Commun. 248 (3): 846–51. doi:10.1006/bbrc.1998.9067. PMID 9704016.
  • Stankewich MC, Tse WT, Peters LL; et al. (1998). "A widely expressed betaIII spectrin associated with Golgi and cytoplasmic vesicles". Proc. Natl. Acad. Sci. U.S.A. 95 (24): 14158–63. PMID 9826670.
  • Holleran EA, Ligon LA, Tokito M; et al. (2001). "beta III spectrin binds to the Arp1 subunit of dynactin". J. Biol. Chem. 276 (39): 36598–605. doi:10.1074/jbc.M104838200. PMID 11461920.
  • Shoeman RL, Hartig R, Hauses C, Traub P (2003). "Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease". Cell Biol. Int. 26 (6): 529–39. PMID 12119179.
  • Nakayama M, Kikuno R, Ohara O (2003). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs". Genome Res. 12 (11): 1773–84. doi:10.1101/gr.406902. PMID 12421765.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Bignone PA, Baines AJ (2003). "Spectrin alpha II and beta II isoforms interact with high affinity at the tetramerization site". Biochem. J. 374 (Pt 3): 613–24. doi:10.1042/BJ20030507. PMID 12820899.
  • Ikeda Y, Dick KA, Weatherspoon MR; et al. (2006). "Spectrin mutations cause spinocerebellar ataxia type 5". Nat. Genet. 38 (2): 184–90. doi:10.1038/ng1728. PMID 16429157.
  • Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.

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