Gene Ontology annotation through association of InterPro records with GO terms
Use of the ND evidence code for Gene Ontology (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
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments.
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Immunoisolated yeast Golgi subcompartments using the SNAREs Sed5 (early Golgi) and Tlg2 (late Golgi/endosome) and catalogued their membrane proteins; PTM1 (YKL039W) co-purified with the Tlg2 late-Golgi/endosome compartment, the experimental basis for its Golgi-membrane and early-endosome-membrane localization.
"we immunoisolated vesicles carrying either of the SNAREs Sed5 or Tlg2, the markers of the early and late Golgi compartments, respectively, and analyzed the membrane proteins"
A multidimensional chromatography technology for in-depth phosphoproteome analysis.
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Large-scale phosphoproteomic survey identifying PTM1 phosphorylation at Ser480, Thr483 and Thr498 in its cytoplasmic C-terminal tail.
"A multidimensional chromatography technology for in-depth phosphoproteome analysis"
Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A.
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Defines the GOST family (GOLD domain fused to a GPCR-like 7TM domain, the architecture shared by PTM1) and proposes a common membrane-trafficking role; shows the human paralog TMEM87A is neither a mechanosensitive channel nor a canonical G-protein-coupled receptor.
"structurally homologous GOST proteins could serve a common role in trafficking"
GPR180 is a new member of the Golgi-dynamics domain seven-transmembrane helix protein family.
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Reviews the GOST/GDD seven-transmembrane family: members localize to the Golgi/endosomal network and are speculated to act as trafficking chaperones for membrane-associated cargo, but their molecular function and ligands remain largely unknown.
"Little is known about ligands and the exact function of GOST proteins"