| 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 PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein. Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes. |
| Protein Name | Proteasome Subunit Beta Type-8Low Molecular Mass Protein 7Macropain Subunit C13Multicatalytic Endopeptidase Complex Subunit C13Proteasome Component C13Proteasome Subunit Beta-5iReally Interesting New Gene 10 Protein |
| Database Links | Reactome: R-HSA-909733Reactome: R-HSA-9907900 |
| Cellular Localisation | CytoplasmNucleus |
| Alternative Protein Names | Proteasome Subunit Beta Type-8 proteinLow Molecular Mass Protein 7 proteinMacropain Subunit C13 proteinMulticatalytic Endopeptidase Complex Subunit C13 proteinProteasome Component C13 proteinProteasome Subunit Beta-5i proteinReally Interesting New Gene 10 Protein proteinPSMB8 proteinLMP7 proteinPSMB5i proteinRING10 proteinY2 protein |
Information sourced from Uniprot.org
