Aliases for HERPUD1 Gene
- Homocysteine Inducible ER Protein With Ubiquitin Like Domain 1 2 3 5
- Homocysteine-Inducible, Endoplasmic Reticulum Stress-Inducible, Ubiquitin-Like Domain Member 1 2 3
- Methyl Methanesulfonate (MMF)-Inducible Fragment Protein 1 3 4
- Mif1 3 4
- HERP 3 4
- Homocysteine-Inducible Endoplasmic Reticulum Stress-Inducible Ubiquitin-Like Domain Member 1 Protein 3
External Ids for HERPUD1 Gene
Previous GeneCards Identifiers for HERPUD1 Gene
The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the ER stress response. This response includes the inhibition of translation to prevent further accumulation of unfolded proteins, the increased expression of proteins involved in polypeptide folding, known as the unfolded protein response (UPR), and the destruction of misfolded proteins by the ER-associated protein degradation (ERAD) system. This gene may play a role in both UPR and ERAD. Its expression is induced by UPR and it has an ER stress response element in its promoter region while the encoded protein has an N-terminal ubiquitin-like domain which may interact with the ERAD system. This protein has been shown to interact with presenilin proteins and to increase the level of amyloid-beta protein following its overexpression. Alternative splicing of this gene produces multiple transcript variants encoding different isoforms. The full-length nature of all transcript variants has not been determined. [provided by RefSeq, Jan 2013]
GeneCards Summary for HERPUD1 Gene
HERPUD1 (Homocysteine Inducible ER Protein With Ubiquitin Like Domain 1) is a Protein Coding gene. Among its related pathways are Protein processing in endoplasmic reticulum and Unfolded Protein Response (UPR). Gene Ontology (GO) annotations related to this gene include ion channel binding. An important paralog of this gene is HERPUD2.
UniProtKB/Swiss-Prot for HERPUD1 Gene
Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Could enhance presenilin-mediated amyloid-beta protein 40 generation. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway (PubMed:18307982).