UBE2J1

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is located in the membrane of the endoplasmic reticulum (ER) and may contribute to quality control ER-associated degradation by the ubiquitin-proteasome system. [provided by RefSeq]

UBE2J1

Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) and is essential for cells to recover from ER stress (PubMed:28321712).
Plays a role in MAPKAPK2-dependent translational control of TNF-alpha synthesis (PubMed:24020373).
Acts also as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the E3 ubiquitin-protein ligase RNF26 (PubMed:33472082).
(Microbial infection) Promotes Dengue virus RNA replication by negatively regulating IFN-beta signaling and mediating 'Lys-48'-linked ubiquitination on IRF3 (PubMed:30157886).

Biological Process negative regulation of retrograde protein transport, ER to cytosol Source:ParkinsonsUK-UCL1 Publication
Biological Process protein N-linked glycosylation via asparagine Source:UniProtKB1 Publication
Biological Process protein polyubiquitination Source:GO_Central1 Publication
Biological Process regulation of macrophage cytokine production Source:Ensembl
Biological Process regulation of tumor necrosis factor production Source:Ensembl
Biological Process spermatid development Source:Ensembl
Biological Process ubiquitin-dependent ERAD pathway Source:UniProtKB1 Publication

Endoplasmic reticulum membrane

Cytoplasmic: 1-282
Helical: 283-303
Lumenal: 304-318

Phosphorylated at Ser-184 in a cytosolic stress-dependent manner by MAP kinase p38 MAPKAPK2.
Phosphorylated UBE2J1 is rapidly ubiquitinated and subsequently degraded by the proteasome.