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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1998-7-1
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pubmed:databankReference |
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pubmed:abstractText |
The U2 snRNP component SAP 155 contacts pre-mRNA on both sides of the branch site early in spliceosome assembly and is therefore positioned near or at the spliceosome catalytic center. We have isolated a cDNA encoding human SAP 155 and identified its highly related Saccharomyces cerevisiae homolog (50% identity). The carboxy-terminal two-thirds of SAP 155 shows the highest conservation and is remarkably similar to the regulatory subunit A of the phosphatase PP2A. Significantly, SAP 155 is phosphorylated concomitant with or just after catalytic step one, making this the first example of a protein modification tightly regulated with splicing catalysis.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-1331983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-1589782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-1717489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-2146679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-2188729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-7526381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-7926772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-7988565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8045264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8211113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8254721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8332490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8387646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8566756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8617202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8668147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8722179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-8811184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-9030686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-9085842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-9159080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9585501-9303319
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoprotein, U2 Small Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0890-9369
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1409-14
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9585501-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9585501-Amino Acid Sequence,
pubmed-meshheading:9585501-Animals,
pubmed-meshheading:9585501-Binding Sites,
pubmed-meshheading:9585501-Caenorhabditis elegans,
pubmed-meshheading:9585501-Catalysis,
pubmed-meshheading:9585501-Consensus Sequence,
pubmed-meshheading:9585501-DNA, Complementary,
pubmed-meshheading:9585501-Genes, Fungal,
pubmed-meshheading:9585501-Helminth Proteins,
pubmed-meshheading:9585501-Humans,
pubmed-meshheading:9585501-Macromolecular Substances,
pubmed-meshheading:9585501-Molecular Sequence Data,
pubmed-meshheading:9585501-Phosphoprotein Phosphatases,
pubmed-meshheading:9585501-Phosphoproteins,
pubmed-meshheading:9585501-Phosphorylation,
pubmed-meshheading:9585501-Protein Binding,
pubmed-meshheading:9585501-Protein Processing, Post-Translational,
pubmed-meshheading:9585501-RNA Precursors,
pubmed-meshheading:9585501-RNA Splicing,
pubmed-meshheading:9585501-Ribonucleoprotein, U2 Small Nuclear,
pubmed-meshheading:9585501-Saccharomyces cerevisiae,
pubmed-meshheading:9585501-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9585501-Schizosaccharomyces,
pubmed-meshheading:9585501-Sequence Alignment,
pubmed-meshheading:9585501-Sequence Homology, Amino Acid,
pubmed-meshheading:9585501-Spliceosomes
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pubmed:year |
1998
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pubmed:articleTitle |
Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis.
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pubmed:affiliation |
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.pende014@mc.duke.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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