CAT80, COT2, SDC1, SSU2, SCF ubiquitin ligase complex subunit GRR1, L000000730, YJR090C
F-box protein component of an SCF ubiquitin-ligase complex; modular substrate specificity factor which associates with core SCF (Cdc53p, Skp1p and Hrt1p/Rbx1p) to form the SCF(Grr1) complex; SCF(Grr1) acts as a ubiquitin-protein ligase directing ubiquitination of substrates such as: Gic2p, Mks1p, Mth1p, Cln1p, Cln2p and Cln3p; involved in carbon catabolite repression, glucose-dependent divalent cation transport, glucose transport, morphogenesis, and sulfite detoxification
Saccharomyces cerevisiae (S288c)


BAP1, SSY2, L000002132, YDR463W
Transcription factor; contains a N-terminal regulatory motif (RI) that acts as a cytoplasmic retention determinant and as an Asi dependent degron in the nucleus; undergoes proteolytic processing by SPS (Ssy1p-Ptr3p-Ssy5p)-sensor component Ssy5p in response to extracellular amino acids; activates transcription of amino acid permease genes and may have a role in tRNA processing; STP1 has a paralog, STP2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.


Differential regulation of transcription factors Stp1 and Stp2 in the Ssy1-Ptr3-Ssy5 amino acid sensing pathway.

Tumusiime S, Zhang C, Overstreet MS, Liu Z

Stp1 and Stp2 are two homologous transcription factors activated in response to extracellular amino acid stimuli. Here we show that both ubiquitin-dependent degradation of Stp1 and Stp2 and their intracellular localization are differentially regulated. We have found that the E2 ubiquitin-conjugating enzyme Cdc34 is required for degradation of both full-length and processed Stp1, but not Stp2. We have also found ... [more]

J. Biol. Chem. Feb. 11, 2011; 286(6);4620-31 [Pubmed: 21127045]


  • Low Throughput

Curated By

  • BioGRID