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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1993-8-12
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pubmed:databankReference | |
pubmed:abstractText |
The mouse Lmp-2 gene is located within the major histocompatibility complex (MHC) class II region and encodes a subunit of the 20S cytosolic proteasome. Previous studies indicated that the 20S proteasome is a catalytic core of the 26S proteolytic complex that possesses a latent multicatalytic proteinase activity and catalyzes an ATP-dependent, selective breakdown of proteins ligated to ubiquitin. This complex has recently been postulated to be involved in the processing of endogenous antigenic peptides for the MHC class I pathway. Here, we report the genomic organization and tissue expression of the mouse Lmp-2 gene. We have cloned and sequenced the entire mouse Lmp-2 gene, including 5'- and 3'-flanking regions. The gene consists of six exons, and its genomic organization is very similar to that of the recently described human LMP2 gene. Putative promoter and enhancer elements were identified in the 5'-flanking region by sequence comparison with known consensus sequences. The Lmp-2 gene is expressed in most tissues of unstimulated mice, except for brain tissue. The comparison of the 5'-flanking region of human and mouse sequences is discussed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/LMP-2 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0888-7543
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:geneSymbol |
Lmp-2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
664-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8325639-3T3 Cells,
pubmed-meshheading:8325639-Amino Acid Sequence,
pubmed-meshheading:8325639-Animals,
pubmed-meshheading:8325639-Base Sequence,
pubmed-meshheading:8325639-Blotting, Northern,
pubmed-meshheading:8325639-Cysteine Endopeptidases,
pubmed-meshheading:8325639-DNA,
pubmed-meshheading:8325639-Gene Expression,
pubmed-meshheading:8325639-Humans,
pubmed-meshheading:8325639-Major Histocompatibility Complex,
pubmed-meshheading:8325639-Mice,
pubmed-meshheading:8325639-Molecular Sequence Data,
pubmed-meshheading:8325639-Multienzyme Complexes,
pubmed-meshheading:8325639-Organ Specificity,
pubmed-meshheading:8325639-Proteasome Endopeptidase Complex,
pubmed-meshheading:8325639-Proteins,
pubmed-meshheading:8325639-Restriction Mapping,
pubmed-meshheading:8325639-Sequence Homology, Nucleic Acid
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pubmed:year |
1993
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pubmed:articleTitle |
Genomic organization and tissue expression of mouse proteasome gene Lmp-2.
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pubmed:affiliation |
Department of Immunology, Mayo Graduate School of Medicine, Rochester, Minnesota 55905.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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