SNTB1

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Syntrophin, beta 1 (dystrophin-associated protein A1, 59kDa, basic component 1)
Identifiers
Symbols SNTB1 ; A1B; 59-DAP; BSYN2; DAPA1B; FLJ22442; MGC111389; SNT2; SNT2B1; TIP-43
External IDs Template:OMIM5 Template:MGI HomoloGene9618
RNA expression pattern
File:PBB GE SNTB1 208608 s at tn.png
File:PBB GE SNTB1 214708 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

Syntrophin, beta 1 (dystrophin-associated protein A1, 59kDa, basic component 1), also known as SNTB1, is a human gene.[1]

Dystrophin is a large, rod-like cytoskeletal protein found at the inner surface of muscle fibers. Dystrophin is missing in Duchenne Muscular Dystrophy patients and is present in reduced amounts in Becker Muscular Dystrophy patients. The protein encoded by this gene is a peripheral membrane protein found associated with dystrophin and dystrophin-related proteins. This gene is a member of the syntrophin gene family, which contains at least two other structurally-related genes.[1]

References

  1. 1.0 1.1 "Entrez Gene: SNTB1 syntrophin, beta 1 (dystrophin-associated protein A1, 59kDa, basic component 1)".

Further reading

  • Ahn AH, Kunkel LM (1995). "Syntrophin binds to an alternatively spliced exon of dystrophin". J. Cell Biol. 128 (3): 363–71. PMID 7844150.
  • Yang B, Ibraghimov-Beskrovnaya O, Moomaw CR; et al. (1994). "Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression". J. Biol. Chem. 269 (8): 6040–4. PMID 8119949.
  • Ahn AH, Yoshida M, Anderson MS; et al. (1994). "Cloning of human basic A1, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8q23-24". Proc. Natl. Acad. Sci. U.S.A. 91 (10): 4446–50. PMID 8183929.
  • Ahn AH, Freener CA, Gussoni E; et al. (1996). "The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives". J. Biol. Chem. 271 (5): 2724–30. PMID 8576247.
  • Gee SH, Madhavan R, Levinson SR; et al. (1998). "Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins". J. Neurosci. 18 (1): 128–37. PMID 9412493.
  • Rousset R, Fabre S, Desbois C; et al. (1998). "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins". Oncogene. 16 (5): 643–54. doi:10.1038/sj.onc.1201567. PMID 9482110.
  • Hasegawa M, Cuenda A, Spillantini MG; et al. (1999). "Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition". J. Biol. Chem. 274 (18): 12626–31. PMID 10212242.
  • Blake DJ, Hawkes R, Benson MA, Beesley PW (1999). "Different dystrophin-like complexes are expressed in neurons and glia". J. Cell Biol. 147 (3): 645–58. PMID 10545507.
  • Newey SE, Benson MA, Ponting CP; et al. (2001). "Alternative splicing of dystrobrevin regulates the stoichiometry of syntrophin binding to the dystrophin protein complex". Curr. Biol. 10 (20): 1295–8. PMID 11069112.
  • Marchand S, Stetzkowski-Marden F, Cartaud J (2001). "Differential targeting of components of the dystrophin complex to the postsynaptic membrane". Eur. J. Neurosci. 13 (2): 221–9. PMID 11168526.
  • Hogan A, Shepherd L, Chabot J; et al. (2001). "Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions". J. Biol. Chem. 276 (28): 26526–33. doi:10.1074/jbc.M104156200. PMID 11352924.
  • Kutsenko AS, Gizatullin RZ, Al-Amin AN; et al. (2002). "NotI flanking sequences: a tool for gene discovery and verification of the human genome". Nucleic Acids Res. 30 (14): 3163–70. PMID 12136098.
  • 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.
  • Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
  • Leonoudakis D, Conti LR, Anderson S; et al. (2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. doi:10.1074/jbc.M400285200. PMID 15024025.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Okuhira K, Fitzgerald ML, Sarracino DA; et al. (2006). "Purification of ATP-binding cassette transporter A1 and associated binding proteins reveals the importance of beta1-syntrophin in cholesterol efflux". J. Biol. Chem. 280 (47): 39653–64. doi:10.1074/jbc.M510187200. PMID 16192269.
  • Kawai-Yamada M, Saito Y, Jin L; et al. (2006). "A novel Arabidopsis gene causes Bax-like lethality in Saccharomyces cerevisiae". J. Biol. Chem. 280 (47): 39468–73. doi:10.1074/jbc.M509632200. PMID 16192270.
  • Ejtehadi HD, Freimanis GL, Ali HA; et al. (2006). "The potential role of human endogenous retrovirus K10 in the pathogenesis of rheumatoid arthritis: a preliminary study". Ann. Rheum. Dis. 65 (5): 612–6. doi:10.1136/ard.2004.031146. PMID 16192292.
  • Chen Z, Hague C, Hall RA, Minneman KP (2006). "Syntrophins regulate alpha1D-adrenergic receptors through a PDZ domain-mediated interaction". J. Biol. Chem. 281 (18): 12414–20. doi:10.1074/jbc.M508651200. PMID 16533813.

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