Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features

Combined Automated Annotation using Multiple IEA Methods

Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans.

Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry.

Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs.

The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins.

A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis.

A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway.

Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier.

Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans.

The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.

Analysis of the Cellular Roles of MOCS3 Identifies a MOCS3-Independent Localization of NFS1 at the Tips of the Centrosome.

Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.

PXLP-K198-NFS1 transfers sulfur from cysteine onto MOCS3

Transfer of sulfur from MOCS3-S-S onto MOCS2A