ID:PSA3_HUMAN DESCRIPTION: RecName: Full=Proteasome subunit alpha type-3; EC=3.4.25.1; AltName: Full=Macropain subunit C8; AltName: Full=Multicatalytic endopeptidase complex subunit C8; AltName: Full=Proteasome component C8; FUNCTION: The proteasome is a multicatalytic proteinase complex which 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. The proteasome has an ATP-dependent proteolytic activity. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2. 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. Interacts with AURKB. Interacts with CDKN1A. Interacts with HIV-1 TAT protein. Interacts with hepatitis C virus (HCV) F protein. Interacts with Epstein-Barr virus EBNA3 proteins. Interacts with MDM2 and RB1. Interacts with the C-terminus of TBXA2R isoform 2. INTERACTION: P29590:PML; NbExp=2; IntAct=EBI-348380, EBI-295890; P25786:PSMA1; NbExp=3; IntAct=EBI-348380, EBI-359352; P25789:PSMA4; NbExp=4; IntAct=EBI-348380, EBI-359310; P60900:PSMA6; NbExp=2; IntAct=EBI-348380, EBI-357793; O14818:PSMA7; NbExp=4; IntAct=EBI-348380, EBI-603272; SUBCELLULAR LOCATION: Cytoplasm. Nucleus. INDUCTION: Down-regulated by antioxidants BO-653 and probucol. Up- regulated by bacterial lipopolysaccharides (LPS) and TNF. SIMILARITY: Belongs to the peptidase T1A family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P25788
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006508 proteolysis GO:0006511 ubiquitin-dependent protein catabolic process GO:0016032 viral process GO:0016579 protein deubiquitination GO:0043687 post-translational protein modification GO:0051603 proteolysis involved in cellular protein catabolic process GO:0052548 regulation of endopeptidase activity