| Tissue Specificity | |
| Post Translational Modifications | Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. |
| 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. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. |
| Protein Name | Proteasome Subunit Beta Type-9Low Molecular Mass Protein 2Macropain Chain 7Multicatalytic Endopeptidase Complex Chain 7Proteasome Chain 7Proteasome Subunit Beta-1iReally Interesting New Gene 12 Protein |
| Database Links | Reactome: R-HSA-9907900 |
| Cellular Localisation | CytoplasmNucleus |
| Alternative ELISA Names | Proteasome Subunit Beta Type-9 ELISA kitLow Molecular Mass Protein 2 ELISA kitMacropain Chain 7 ELISA kitMulticatalytic Endopeptidase Complex Chain 7 ELISA kitProteasome Chain 7 ELISA kitProteasome Subunit Beta-1i ELISA kitReally Interesting New Gene 12 Protein ELISA kitPSMB9 ELISA kitLMP2 ELISA kitPSMB6i ELISA kitRING12 ELISA kit |
| output | |
Information sourced from Uniprot.org