The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. This particular subunit has been shown to interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. In addition, this subunit is involved in regulating hepatitis virus C internal ribosome entry site (IRES) activity, an activity essential for viral replication. This core alpha subunit is also involved in regulating the hypoxia-inducible factor-1alpha, a transcription factor important for cellular responses to oxygen tension. Multiple isoforms of this subunit arising from alternative splicing may exist but alternative transcripts for only two isoforms have been defined. A pseudogene has been identified on chromosome 9.
Related Pathway
Cell cycle
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HEK293T cells were transfected with the pCMV6-ENTRY control (Left lane) or pCMV6-ENTRY PSMA7 (RC201169, Right lane) cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-PSMA7.
Flow cytometric analysis of Jurkat cells, using anti-PSMA7 antibody(TA500694),(Red) compared to a nonspecific negative control antibody(TA50011)(Blue).
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