BAIT

SEC61

translocon subunit SEC61, L000001852, YLR378C
Conserved ER protein translocation channel; essential subunit of Sec61 complex (Sec61p, Sbh1p, and Sss1p); forms channel for SRP-dependent protein import; with Sec63 complex allows SRP-independent protein import into ER; involved in posttranslational soluble protein import into the ER, ERAD of soluble substrates, and misfolded soluble protein export from the ER
Saccharomyces cerevisiae (S288c)
PREY

SEC66

HSS1, SEC71, Sec63 complex subunit SEC66, L000001856, YBR171W
Non-essential subunit of Sec63 complex; with Sec61 complex, Kar2p/BiP and Lhs1p forms a channel competent for SRP-dependent and post-translational SRP-independent protein targeting and import into the ER; other members are Sec63p, Sec62p, and Sec72p
GO Process (2)
GO Function (1)
GO Component (3)
Saccharomyces cerevisiae (S288c)

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Preferential targeting of an SRP-dependent precursor to the Ssh1p translocon in yeast.

Spiller MP, Stirling CJ

Protein translocation across the endoplasmic reticulum (ER) membrane occurs via a "translocon" channel formed by the Sec61p complex. A homologue of Sec61p, called Ssh1p, has been identified in yeast and here we use trapped translocation intermediates to demonstrate that a specific SRP-dependent substrate, Sec71p, is targeted exclusively to Ssh1p. Strikingly, we found that, in the absence of Ssh1p, precursor could ... [more]

Unknown Mar. 28, 2011; 0(0); [Pubmed: 21454595]

Throughput

  • Low Throughput

Additional Notes

  • cross-linked

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SEC66 SEC61
Affinity Capture-MS
Affinity Capture-MS

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 is identified by mass spectrometric methods.

High9BioGRID
3603980
SEC61 SEC66
Affinity Capture-MS
Affinity Capture-MS

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 is identified by mass spectrometric methods.

High-BioGRID
2935202
SEC61 SEC66
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.1279BioGRID
2003263
SEC66 SEC61
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.2552BioGRID
2029519
SEC66 SEC61
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-12.9353BioGRID
896665
SEC66 SEC61
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

High-BioGRID
433249

Curated By

  • BioGRID