BAIT

C1GALT1

C1GALT, T-synthase
core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
Homo sapiens
PREY

C1GALT1C1

C1GALT2, C38H2-L1, COSMC, MST143, TNPS, HSPC067
C1GALT1-specific chaperone 1
Homo sapiens

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Regulation of protein O-glycosylation by the endoplasmic reticulum-localized molecular chaperone Cosmc.

Ju T, Aryal RP, Stowell CJ, Cummings RD

Regulatory pathways for protein glycosylation are poorly understood, but expression of branchpoint enzymes is critical. A key branchpoint enzyme is the T-synthase, which directs synthesis of the common core 1 O-glycan structure (T-antigen), the precursor structure for most mucin-type O-glycans in a wide variety of glycoproteins. Formation of active T-synthase, which resides in the Golgi apparatus, requires a unique molecular ... [more]

J. Cell Biol. Aug. 11, 2008; 182(3);531-42 [Pubmed: 18695044]

Throughput

  • Low Throughput

Curated By

  • BioGRID