BAIT
BMH1
APR6, 14-3-3 family protein BMH1, L000000185, YER177W
14-3-3 protein, major isoform; controls proteome at post-transcriptional level, binds proteins and DNA, involved in regulation of exocytosis, vesicle transport, Ras/MAPK and rapamycin-sensitive signaling, aggresome formation, spindle position checkpoint; protein increases in abundance and relative distribution to the nucleus increases upon DNA replication stress; antiapoptotic gene similar to human 14-3-3; BMH1 has a paralog, BMH2, that arose from whole genome duplication
GO Process (12)
GO Function (3)
GO Component (3)
Gene Ontology Biological Process
- DNA damage checkpoint [IMP]
- Ras protein signal transduction [IGI]
- aggresome assembly [IMP]
- ascospore formation [IGI]
- fungal-type cell wall chitin biosynthetic process [IGI]
- glycogen metabolic process [IGI]
- mitotic spindle orientation checkpoint [IGI]
- negative regulation of apoptotic process [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IMP]
- negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [IPI]
- pseudohyphal growth [IGI]
- signal transduction involved in filamentous growth [IGI]
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
ACO1
ACONS, HEL60, IREB1, IREBP, IREBP1, IRP1, RP11-334P12.1
aconitase 1, soluble
GO Process (2)
GO Function (5)
GO Component (6)
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking.
14-3-3-interacting proteins were isolated from extracts of proliferating HeLa cells using 14-3-3 affinity chromatography, eluting with a phosphopeptide that competes with targets for 14-3-3 binding. The isolated proteins did not bind to 14-3-3 proteins (14-3-3s) after dephosphorylation with protein phosphatase 2A (PP2A), indicating that binding to 14-3-3s requires their phosphorylation. The binding proteins identified by tryptic mass fingerprinting and Western ... [more]
Biochem. J. Apr. 15, 2004; 379(Pt 2);395-408 [Pubmed: 14744259]
Throughput
- Low Throughput
Curated By
- BioGRID