rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
2
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pubmed:dateCreated |
1991-12-2
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D10293,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D90502,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64053,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64054,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64055,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64056,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64057,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64058,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64059,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64060,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S61910
|
pubmed:abstractText |
We have isolated a cDNA clone encoding a homolog of mammalian calcineurin B (the regulatory subunit of calmodulin-dependent protein phosphatase) by screening a cDNA expression library of Saccharomyces cerevisiae with antiserum against bovine calcineurin B. The yeast calcineurin B homolog (YCNB) is composed of 175 amino acids with a calculated molecular mass of 19,639 daltons and contains four putative Ca(2+)-binding domains. The amino-acid alignment of YCNB with human calcineurin B demonstrates 53% sequence identity and 82% homology. Southern blot analysis indicates that the gene for YCNB is a single-copy gene. Thus, yeast calmodulin-dependent protein phosphatase apparently has a heterodimeric structure similar to that of the enzyme in mammalians.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
31
|
pubmed:volume |
180
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
1159-63
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1659397-Amino Acid Sequence,
pubmed-meshheading:1659397-Animals,
pubmed-meshheading:1659397-Base Sequence,
pubmed-meshheading:1659397-Blotting, Southern,
pubmed-meshheading:1659397-Blotting, Western,
pubmed-meshheading:1659397-Calcineurin,
pubmed-meshheading:1659397-Calmodulin-Binding Proteins,
pubmed-meshheading:1659397-Cattle,
pubmed-meshheading:1659397-Cloning, Molecular,
pubmed-meshheading:1659397-DNA, Fungal,
pubmed-meshheading:1659397-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1659397-Genes, Fungal,
pubmed-meshheading:1659397-Humans,
pubmed-meshheading:1659397-Molecular Sequence Data,
pubmed-meshheading:1659397-Phosphoprotein Phosphatases,
pubmed-meshheading:1659397-Saccharomyces cerevisiae,
pubmed-meshheading:1659397-Sequence Homology, Nucleic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
cDNA cloning of a calcineurin B homolog in Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Pharmacology, Kobe University School of Medicine, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|