BAIT
SF3A2
PRP11, PRPF11, SAP62, SF3a66
splicing factor 3a, subunit 2, 66kDa
GO Process (5)
GO Function (2)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
HNRNPK
CSBP, HNRPK, TUNP, RP11-575L7.1
heterogeneous nuclear ribonucleoprotein K
GO Process (10)
GO Function (6)
GO Component (7)
Gene Ontology Biological Process
- RNA processing [TAS]
- RNA splicing [TAS]
- gene expression [TAS]
- mRNA splicing, via spliceosome [IC, TAS]
- positive regulation of low-density lipoprotein particle receptor biosynthetic process [IMP]
- positive regulation of receptor-mediated endocytosis [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of low-density lipoprotein particle clearance [IMP]
- signal transduction [TAS]
Gene Ontology Molecular Function- RNA binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IMP]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IMP]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- single-stranded DNA binding [TAS]
- RNA binding [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IMP]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IMP]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- single-stranded DNA binding [TAS]
Gene Ontology Cellular Component
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
Composition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexes.
Little is known about the higher-order structure of prespliceosomal A complexes, in which pairing of the pre-mRNA's splice sites occurs. Here, human A complexes were isolated under physiological conditions by double-affinity selection. Purified complexes contained stoichiometric amounts of U1, U2 and pre-mRNA, and crosslinking studies indicated that these form concomitant base pairing interactions with one another. A complexes contained nearly ... [more]
EMBO J. Mar. 21, 2007; 26(6);1737-48 [Pubmed: 17332742]
Throughput
- Low Throughput
Curated By
- BioGRID