BAIT
MLP2
S000007510, YIL149C
Myosin-like protein associated with the nuclear envelope; nuclear basket protein that connects the nuclear pore complex with the nuclear interior; involved in the Tel1p pathway that controls telomere length; MLP2 has a paralog, MLP1, that arose from the whole genome duplication
GO Process (7)
GO Function (1)
GO Component (7)
Gene Ontology Biological Process
- negative regulation of protein import into nucleus during spindle assembly checkpoint [IGI]
- poly(A)+ mRNA export from nucleus [IMP]
- posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery [IMP]
- regulation of transcription, DNA-templated [IEP, IGI]
- spindle pole body organization [IMP]
- telomere tethering at nuclear periphery [IGI]
- transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
BPT1
ATP-binding cassette bilirubin transporter BPT1, YLL015W
ABC type transmembrane transporter of MRP/CFTR family; found in vacuolar membrane, involved in the transport of unconjugated bilirubin and in heavy metal detoxification via glutathione conjugates, along with Ycf1p
GO Process (3)
GO Function (2)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
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 nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly.
The two yeast proteins Mlp1p and Mlp2p (homologues of the vertebrate protein Tpr) are filamentous proteins attached to the nuclear face of nuclear pore complexes. Here we perform a proteomic analysis, which reveals that the two Mlps have strikingly different interacting partners, testifying to their different roles within the cell. We find that Mlp2p binds directly to Spc110p, Spc42p, and ... [more]
J. Cell Biol. Jul. 18, 2005; 170(2);225-35 [Pubmed: 16027220]
Throughput
- Low Throughput
Curated By
- BioGRID