| Tissue Specificity | Ubiquitous. |
| Post Translational Modifications | Auto-AMPylated in vitro.it is unclear whether auto-AMPylation is relevant in vivo. N-glycosylated.predominantly glycosylated at Asn-275. |
| Function | Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context. The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place. Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity. Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates. |
| Peptide Name | Protein Adenylyltransferase FicdAmpylator FicdDe-Ampylase FicdFic Domain-Containing ProteinHuntingtin Yeast Partner EHuntingtin-Interacting Protein 13Hip-13Huntingtin-Interacting Protein E |
| Cellular Localisation | Endoplasmic Reticulum MembraneSingle-Pass Type Ii Membrane Protein |
| Alternative Peptide Names | Protein Adenylyltransferase Ficd proteinAmpylator Ficd proteinDe-Ampylase Ficd proteinFic Domain-Containing Protein proteinHuntingtin Yeast Partner E proteinHuntingtin-Interacting Protein 13 proteinHip-13 proteinHuntingtin-Interacting Protein E proteinFICD proteinHIP13 proteinHYPE proteinUNQ3041 proteinPRO9857 protein |
Information sourced from Uniprot.org
