Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor.

Human lysosomal protective protein. Glycosylation, intracellular transport, and association with beta-galactosidase in the endoplasmic reticulum.

A mutation in a mild form of galactosialidosis impairs dimerization of the protective protein and renders it unstable.

Large-scale proteomics and phosphoproteomics of urinary exosomes.

Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function.

Defining the membrane proteome of NK cells.

Chaperone-mediated autophagy: molecular mechanisms and physiological relevance.

Galactosialidosis: simultaneous deficiency of esterase, carboxy-terminal deamidase and acid carboxypeptidase activities.

In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.

Galactosialidosis: a direct evidence that a 46-kilodalton protein restores deficient enzyme activities in fibroblasts.

Expression of cDNA encoding the human "protective protein" associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases.

Structure of the immunoregulatory sialidase NEU1.

NEU1,4 hydrolyze PSAP(195-273):GM3:PE

NEU1 hydrolyses Neu5Ac from glycoconjugates

Defective NEU1 does not hydrolyse Neu5Ac from glycoconjugates

Exocytosis of azurophil granule lumen proteins

NEU4 hydrolyses Neu5Ac from glycoconjugates

CTSA source and evidence summary

A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal "protective protein".

Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism.