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| Syntrophin, beta 1 (dystrophin-associated protein A1, 59kDa, basic component 1) | ||||||||||||||
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| Identifiers | ||||||||||||||
| Symbols | SNTB1; A1B; 59-DAP; BSYN2; DAPA1B; FLJ22442; MGC111389; SNT2; SNT2B1; TIP-43 | |||||||||||||
| External IDs | OMIM: 600026 MGI: 101781 HomoloGene: 9618 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| More reference expression data | ||||||||||||||
| Orthologs | ||||||||||||||
| Species | Human | Mouse | ||||||||||||
| Entrez | 6641 | 20649 | ||||||||||||
| Ensembl | ENSG00000172164 | ENSMUSG00000060429 | ||||||||||||
| UniProt | Q13884 | Q99L88 | ||||||||||||
| RefSeq | NM_021021 (mRNA) | XM_001004146 (mRNA) | ||||||||||||
| NP_066301 (protein) | XP_001004146 (protein) | |||||||||||||
| Location | Chr 8: 121.62 - 121.89 Mb |
Chr 15: 55.47 - 55.74 Mb |
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| PubMed search | [1] | [2] | ||||||||||||
Beta-1-syntrophin is a protein that in humans is encoded by the SNTB1 gene.[1][2][3]
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.[3]
Interactions
SNTB1 has been shown to interact with Dystrophin.[4]
References
- ^ Ahn AH, Yoshida M, Anderson MS, Feener CA, Selig S, Hagiwara Y, Ozawa E, Kunkel LM (Jun 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.
- ^ Rousset R, Fabre S, Desbois C, Bantignies F, Jalinot P (Mar 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:. PMID 9482110.
- ^ a b "Entrez Gene: SNTB1 syntrophin, beta 1 (dystrophin-associated protein A1, 59kDa, basic component 1)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6641.
- ^ Ahn, A H; Kunkel L M (Feb. 1995). "Syntrophin binds to an alternatively spliced exon of dystrophin". J. Cell Biol. (UNITED STATES) 128 (3): 363-71. ISSN 0021-9525. PMID 7844150.
Further reading
- Ahn AH, Kunkel LM (1995). "Syntrophin binds to an alternatively spliced exon of dystrophin.". J. Cell Biol. 128 (3): 363–71. doi:. 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, 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. doi:. 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.
- 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. doi:. 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. doi:. 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. doi:. 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. doi:. 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:. 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. doi:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. PMID 16533813.
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