Gene Ontology annotation through association of InterPro records with GO terms.
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
Intestinal epithelial cells secrete exosome-like vesicles.
Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis.
Towards a proteome-scale map of the human protein-protein interaction network.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Dipeptide hydrolysis by the dinuclear zinc enzyme human renal dipeptidase: mechanistic insights from DFT calculations.
Novel associations of CPS1, MUT, NOX4, and DPEP1 with plasma homocysteine in a healthy population: a genome-wide evaluation of 13 974 participants in the Women's Genome Health Study.
DPEP1, expressed in the early stages of colon carcinogenesis, affects cancer cell invasiveness.
Primary structure of human microsomal dipeptidase deduced from molecular cloning.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
A proteome-scale map of the human interactome network.
Architecture of the human interactome defines protein communities and disease networks.
Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment reveals basis for lack of dipeptidase activity.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Beta-lactamase activity of purified and partially characterized human renal dipeptidase.
Comparative stability of carbapenem and penem antibiotics to human recombinant dehydropeptidase-I.
LTD4 is converted to LTE4 by DPEP1/2
DPEPs hydrolyse glycine from AFXBO-CG, AFNBO-CG
Deep research report on DPEP1
-
DPEP1 is a GPI-anchored binuclear-zinc membrane dipeptidase of the M19 family that hydrolyzes dipeptides, converts LTD4 to LTE4, hydrolyzes cysteinylglycine from glutathione catabolism, and hydrolyzes beta-lactam antibiotics.
"DPEP1 hydrolyzes dipeptides including glutathione catabolites (e.g., Cys-Gly), converts leukotriene D4 (LTD4) to LTE4, and hydrolyzes beta-lactam antibiotics such as thienamycin/imipenem; it is potently inhibited by cilastatin"
-
DPEP1 has a non-enzymatic function as an endothelial adhesion receptor for neutrophil recruitment, separable from its catalytic activity.
"A catalytically inert E141D DPEP1 mutant maintained neutrophil adhesion comparable to wild-type in cellular assays, while LSALT peptide binding to DPEP1 inhibited adhesion"