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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
43
|
| pubmed:dateCreated |
1995-12-14
|
| pubmed:databankReference | |
| pubmed:abstractText |
The syntrophin family of dystrophin-associated proteins consists of three isoforms, alpha 1, beta 1, and beta 2, each encoded by a distinct gene. We have cloned and characterized the mouse alpha 1- and beta 2-syntrophin genes. The mouse alpha 1-syntrophin gene ( > 24 kilobases) is comprised of eight exons. The mouse beta 2-syntrophin gene ( > 33 kilobases) contains seven exons, all of which have homologues at the corresponding position in the alpha 1-syntrophin gene. Primer extension analysis reveals two transcription initiation sites in the alpha 1-syntrophin gene and a single site in the beta 2-syntrophin gene. The sequence immediately 5' of the transcription start sites of both genes lacks a TATA box but is GC-rich and has multiple putative SP1 binding sites. The alpha 1-syntrophin gene is located on human chromosome 20 and mouse chromosome 2, while the beta 2-syntrophin gene is on human chromosome 16 and mouse chromosome 8. Analysis of the amino acid sequence of the syntrophins reveals the presence of four conserved domains. The carboxyl-terminal 56 amino acids are highly conserved and constitute a syntrophin unique domain. Two pleckstrin homology domains are located at the amino-terminal end of the protein. The first pleckstrin homology domain is interrupted by a domain homologous to repeated sequences originally found in the Drosophila discs-large protein.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/syntrophin,
http://linkedlifedata.com/resource/pubmed/chemical/syntrophin alpha1
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
27
|
| pubmed:volume |
270
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
25859-65
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:7592771-Amino Acid Sequence,
pubmed-meshheading:7592771-Animals,
pubmed-meshheading:7592771-Base Sequence,
pubmed-meshheading:7592771-Binding Sites,
pubmed-meshheading:7592771-Calcium-Binding Proteins,
pubmed-meshheading:7592771-Chromosome Mapping,
pubmed-meshheading:7592771-Chromosomes, Human, Pair 20,
pubmed-meshheading:7592771-Conserved Sequence,
pubmed-meshheading:7592771-Crosses, Genetic,
pubmed-meshheading:7592771-Dystrophin-Associated Proteins,
pubmed-meshheading:7592771-Exons,
pubmed-meshheading:7592771-Humans,
pubmed-meshheading:7592771-Introns,
pubmed-meshheading:7592771-Membrane Proteins,
pubmed-meshheading:7592771-Mice,
pubmed-meshheading:7592771-Molecular Sequence Data,
pubmed-meshheading:7592771-Muridae,
pubmed-meshheading:7592771-Muscle Proteins,
pubmed-meshheading:7592771-Promoter Regions, Genetic,
pubmed-meshheading:7592771-Sequence Analysis, DNA,
pubmed-meshheading:7592771-Sequence Homology, Amino Acid,
pubmed-meshheading:7592771-Transcription, Genetic
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Mouse alpha 1- and beta 2-syntrophin gene structure, chromosome localization, and homology with a discs large domain.
|
| pubmed:affiliation |
Department of Physiology, University of North Carolina, Chapel Hill 27599-7545, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|