UFD1
UFD1 (ubiquitin recognition factor in ER-associated degradation 1, also known as UFD1L) is an essential component of the ubiquitin-dependent proteolytic pathway. It partners with VCP and NPLOC4 to bind ubiquitinated proteins and direct them towards degradation. Browse Assay Genie's current range of UFD1 research reagents below, or read on for the biology behind the target.
UFD1 is an essential component of the ubiquitin-dependent proteolytic pathway, which degrades ubiquitin fusion proteins. It acts as part of a ternary complex with VCP (valosin-containing protein) and NPLOC4 (nuclear protein localization-4). This complex binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the endoplasmic reticulum to the cytoplasm, where they are degraded by the proteasome.
Beyond protein quality control, the NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. UFD1 has also been described as a negative regulator of type I interferon production: with VCP and NPLOC4 it binds RIGI and recruits RNF125, promoting RIGI ubiquitination and degradation. UniProt notes that it may be involved in the development of some ectoderm-derived structures.
The UFD1 protein belongs to the UFD1 family and is found in the nucleus and the cytosol. HGNC classifies the gene within the VCP-Ufd1-Npl4 complex subunits group. Orthologous genes are named Ufd1 in mouse and rat. Alternative splicing produces multiple transcript variants that encode different isoforms, and a related pseudogene has been identified on chromosome 18.
The gene was formerly named ubiquitin fusion degradation 1-like (UFD1L), with the symbol reflecting its relationship to the yeast Ufd1 gene. Mutations in the UFD1 gene have been associated with Catch 22 syndrome, as well as cardiac and craniofacial defects, making it a point of interest in developmental and congenital disease research.
UFD1 works with VCP and NPLOC4 to export misfolded proteins from the ER to the cytoplasm for proteasomal degradation.
The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is needed to form a closed nuclear envelope.
UFD1 acts with VCP and NPLOC4 to recruit RNF125 to RIGI, promoting its degradation and limiting type I interferon production.
UFD1 mutations have been associated with Catch 22 syndrome and with cardiac and craniofacial defects.
UFD1 is an essential component of the ubiquitin-dependent proteolytic pathway. With VCP and NPLOC4 it binds ubiquitinated proteins and supports export of misfolded proteins from the ER for proteasomal degradation. The same complex regulates spindle disassembly after mitosis and nuclear envelope closure.
UFD1 was previously known as UFD1L, and earlier names include ubiquitin fusion degradation 1-like. UniProt calls it ubiquitin recognition factor in ER-associated degradation protein 1. Alternative splicing gives multiple transcript variants encoding different isoforms.
Mutations in the UFD1 gene have been associated with Catch 22 syndrome, along with cardiac and craniofacial defects. Orthologues named Ufd1 exist in mouse and rat, and the yeast gene is the origin of the older name; check the datasheet of any product for its validated reactivity.
Partners in the VCP-Ufd1-Npl4 complex and related ubiquitin and innate immune signalling targets.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q92890; product specifications from Assay Genie datasheets.