Aliases for PSMD2 Gene
- Proteasome 26S Subunit, Non-ATPase 2 2 3 5
- Proteasome (Prosome, Macropain) 26S Subunit, Non-ATPase, 2 2 3
- Tumor Necrosis Factor Type 1 Receptor-Associated Protein 2 3 4
- Protein 55.11 3 4
- TRAP2 3 4
- 26S Proteasome Non-ATPase Regulatory Subunit 2 3
- 26S Proteasome Regulatory Subunit RPN1 4
- 26S Proteasome Regulatory Subunit S2 4
External Ids for PSMD2 Gene
Previous GeneCards Identifiers for PSMD2 Gene
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core 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. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase 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 one of the non-ATPase subunits of the 19S regulator lid. In addition to participation in proteasome function, this subunit may also participate in the TNF signalling pathway since it interacts with the tumor necrosis factor type 1 receptor. A pseudogene has been identified on chromosome 1. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, Jul 2013]
GeneCards Summary for PSMD2 Gene
PSMD2 (Proteasome 26S Subunit, Non-ATPase 2) is a Protein Coding gene. Among its related pathways are Ubiquitin-Proteasome Dependent Proteolysis and Interleukin-3, 5 and GM-CSF signaling. GO annotations related to this gene include binding and enzyme regulator activity.
UniProtKB/Swiss-Prot for PSMD2 Gene
Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1.