BAIT

SNTB2

D16S2531E, EST25263, SNT2B2, SNT3, SNTL
syntrophin, beta 2 (dystrophin-associated protein A1, 59kDa, basic component 2)
GO Process (0)
GO Function (2)
GO Component (6)
Homo sapiens
PREY

E6

HpV16gp1
transforming protein
GO Process (0)
GO Function (0)
GO Component (0)
Human papillomavirus (16)

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.

Publication

Quantifying domain-ligand affinities and specificities by high-throughput holdup assay.

Vincentelli R, Luck K, Poirson J, Polanowska J, Abdat J, Blemont M, Turchetto J, Iv F, Ricquier K, Straub ML, Forster A, Cassonnet P, Borg JP, Jacob Y, Masson M, Nomine Y, Reboul J, Wolff N, Charbonnier S, Trave G

Many protein interactions are mediated by small linear motifs interacting specifically with defined families of globular domains. Quantifying the specificity of a motif requires measuring and comparing its binding affinities to all its putative target domains. To this end, we developed the high-throughput holdup assay, a chromatographic approach that can measure up to 1,000 domain-motif equilibrium binding affinities per day. ... [more]

Nat Methods Aug. 01, 2015; 12(8);787-93 [Pubmed: 26053890]

Throughput

  • Low Throughput

Ontology Terms

  • uterine cervix (BTO:0001421)
  • hela cell (BTO:0000567) [cervical adenocarcinoma cell (BTO:0003165)]
  • epithelial cell of cervix (CL:0002535)

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
E6 SNTB2
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
3763263
E6 SNTB2
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
3786726
E6 SNTB2
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
3762938
E6 SNTB2
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
3776388
E6 SNTB2
Protein-peptide
Protein-peptide

An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.

High-BioGRID
-
E6 SNTB2
Reconstituted Complex
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.

Low/High-BioGRID
3768493

Curated By

  • BioGRID