PREY

BYSL

BYSTIN, RP5-973N23.2
bystin-like
GO Process (2)
GO Function (2)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens

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.

Publication

The BioPlex Network of Human Protein Interactions: Additional Unpublished AP-MS Results (Pre-Publication)

Huttlin EL, Pontano-Vaites L, Navarrete-Perea J, Bruckner RJ, Gebreab F, Gygi MP, Thornock A, Fu S, Maenpaa E, Golbazi A, Stricker K, Guha Thakurta S, Zhang T, Rad R, Paulo JA, Harper JW, Gygi SP

As part of an ongoing effort led by Steve Gygi, Wade Harper, and Ed Huttlin in the Department of Cell Biology at Harvard Medical School, we are systematically profiling the interactions among human proteins using affinity purification mass spectrometry. In this effort, HA-tagged bait proteins obtained from the human ORFeome collection (version 8.1; Marc Vidal) are expressed individually in human ... [more]

Status: Pre-Publication Dataset

Quantitative Score

  • 0.601996543 [compPASS Score]

Throughput

  • High Throughput

Additional Notes

  • BioPlex HCT (unpublished interaction)
  • BioPlex HCT HCT116 cells CompPASS score = 0.60199654315085, threshold = 0.362. Quantitative scores are calculated by CompPASS-Plus (Huttlin et al. Cell 2015, PMID: 26186194). The 0.362 threshold represents the top 2% of scores in HCT116.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BYSL RPS8
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
3348941
BYSL RPS8
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
3644874
BYSL RPS8
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High0.1182BioGRID
1271376

Curated By

  • BioGRID