BAIT

RPT2

YHS4, YTA5, proteasome regulatory particle base subunit RPT2, L000002559, YDL007W
ATPase of the 19S regulatory particle of the 26S proteasome; one of six ATPases of the regulatory particle; involved in the degradation of ubiquitinated substrates; required for normal peptide hydrolysis by the core 20S particle; N-myristoylation of Rpt2p at Gly2 is involved in regulating the proper intracellular distribution of proteasome activity by controlling the nuclear localization of the 26S proteasome
Saccharomyces cerevisiae (S288c)
PREY

RPT6

CIM3, CRL3, SCB68, SUG1, proteasome regulatory particle base subunit RPT6, L000002174, L000000406, L000002265, YGL048C
ATPase of the 19S regulatory particle of the 26S proteasome; one of six ATPases of the regulatory particle; involved in the degradation of ubiquitinated substrates; bound by ubiquitin-protein ligases Ubr1p and Ufd4p; localized mainly to the nucleus throughout the cell cycle; protein abundance increases in response to DNA replication stress
Saccharomyces cerevisiae (S288c)

Cross-Linking-MS (XL-MS)

An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).

Publication

High-density chemical cross-linking for modeling protein interactions.

Mintseris J, Gygi SP

Detailed mechanistic understanding of protein complex function is greatly enhanced by insights from its 3-dimensional structure. Traditional methods of protein structure elucidation remain expensive and labor-intensive and require highly purified starting material. Chemical cross-linking coupled with mass spectrometry offers an alternative that has seen increased use, especially in combination with other experimental approaches like cryo-electron microscopy. Here we report advances ... [more]

Proc Natl Acad Sci U S A Jan. 07, 2020; 117(1);93-102 [Pubmed: 31848235]

Throughput

  • Low Throughput

Additional Notes

  • High confidence interactions were identified using the PIXL (Protein Interactions from Cross-Linking) algorithm and stringently filtered to 1% FDR.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPT6 RPT2
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
-
RPT2 RPT6
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
-
RPT6 RPT2
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.

High6BioGRID
3614649
RPT6 RPT2
Affinity Capture-Western
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.

Low-BioGRID
-
RPT2 RPT6
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-0.01BioGRID
443000
RPT6 RPT2
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-0.01BioGRID
443002
RPT2 RPT6
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-0.3279BioGRID
1922688
RPT2 RPT6
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
-

Curated By

  • BioGRID