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

DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation.

Close P, East P, Dirac-Svejstrup AB, Hartmann H, Heron M, Maslen S, Chariot A, Soeding J, Skehel M, Svejstrup JQ

Alternative messenger RNA splicing is the main reason that vast mammalian proteomic complexity can be achieved with a limited number of genes. Splicing is physically and functionally coupled to transcription, and is greatly affected by the rate of transcript elongation. As the nascent pre-mRNA emerges from transcribing RNA polymerase II (RNAPII), it is assembled into a messenger ribonucleoprotein (mRNP) particle; ... [more]

Nature Apr. 19, 2012; 484(7394);386-9 [Pubmed: 22446626]

Throughput

High Throughput

Additional Notes

figure 1, S2.

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
HNRNPA1 GADD45GIP1	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.	Huttlin EL (2015)	High	0.7908	BioGRID	1184559

Curated By

BioGRID

Interaction Summary

HNRNPA1

Gene Ontology Biological Process

Gene Ontology Molecular Function

RNA binding [TAS]poly(A) RNA binding [IDA]protein binding [IPI]single-stranded DNA binding [IDA]single-stranded RNA binding [IC]

Gene Ontology Cellular Component

GADD45GIP1