Aliases for PSMD14 Gene
- Proteasome 26S Subunit, Non-ATPase 14 2 3 5
- POH1 2 3 4
- Proteasome (Prosome, Macropain) 26S Subunit, Non-ATPase, 14 2 3
- 26S Proteasome Non-ATPase Regulatory Subunit 14 3 4
- 26S Proteasome-Associated PAD1 Homolog 1 3 4
- Testis Tissue Sperm-Binding Protein Li 69n 3
- 26S Proteasome Regulatory Subunit Rpn11 3
External Ids for PSMD14 Gene
Previous GeneCards Identifiers for PSMD14 Gene
This gene encodes a component of the 26S proteasome. The 26S proteasome is a large multiprotein complex that catalyzes the degradation of ubiquitinated intracellular proteins. The encoded protein is a component of the 19S regulatory cap complex of the 26S proteasome and mediates substrate deubiquitination. A pseudogene of this gene is also located on the long arm of chromosome 2. [provided by RefSeq, Feb 2012]
GeneCards Summary for PSMD14 Gene
PSMD14 (Proteasome 26S Subunit, Non-ATPase 14) is a Protein Coding gene. Diseases associated with PSMD14 include Cystic Fibrosis and Angelman Syndrome. Among its related pathways are Downstream signaling events of B Cell Receptor (BCR) and CDK-mediated phosphorylation and removal of Cdc6. Gene Ontology (GO) annotations related to this gene include metallopeptidase activity and proteasome binding. An important paralog of this gene is COPS5.
UniProtKB/Swiss-Prot Summary for PSMD14 Gene
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading.