| Predicate | Object |
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| rdf:type | |
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Proteasome component PRE5
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| http://www.biopax.org/relea... |
PSA1_YEAST
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
3.4.25.1,
Macropain subunit PRE5,
Multicatalytic endopeptidase complex subunit PRE5,
Proteinase YSCE subunit PRE5
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| http://www.biopax.org/relea... |
FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad specificity. SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. MISCELLANEOUS: Present with 7210 molecules/cell in log phase SD medium. SIMILARITY: Belongs to the peptidase T1A family. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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