Post Translational Modifications | Within the major histocompatibility complex class I (MHC I) peptide loading complex forms reversible disulfide-linked heterodimers with TAPBP as part of its protein folding chaperone activity. This is essential to assist the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Phosphorylated. |
Function | Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone. Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity. |
Protein Name | Protein Disulfide-Isomerase A358 Kda Glucose-Regulated Protein58 Kda Microsomal ProteinP58Disulfide Isomerase Er-60Endoplasmic Reticulum Resident Protein 57Er Protein 57Erp57Endoplasmic Reticulum Resident Protein 60Er Protein 60Erp60 |
Database Links | Reactome: R-HSA-1236974Reactome: R-HSA-901042Reactome: R-HSA-983170 |
Cellular Localisation | Endoplasmic ReticulumEndoplasmic Reticulum LumenMelanosomeIdentified By Mass Spectrometry In Melanosome Fractions From Stage I To Stage Iv |
Alternative Protein Names | Protein Disulfide-Isomerase A3 protein58 Kda Glucose-Regulated Protein protein58 Kda Microsomal Protein proteinP58 proteinDisulfide Isomerase Er-60 proteinEndoplasmic Reticulum Resident Protein 57 proteinEr Protein 57 proteinErp57 proteinEndoplasmic Reticulum Resident Protein 60 proteinEr Protein 60 proteinErp60 proteinPDIA3 proteinERP57 proteinERP60 proteinGRP58 protein |
Information sourced from Uniprot.org