Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae.
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry.
Subcellular localization of the yeast proteome.
Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA complex in Saccharomyces cerevisiae.
-
Hap2p, Hap3p and Hap5p assemble in a single step into the DNA-binding heterotrimer, and Hap4p joins only after DNA binding.
"Hap2p, Hap3p, and Hap5p assemble via a one-step pathway requiring all three subunits simultaneously"
Proteome survey reveals modularity of the yeast cell machinery.
Defining the budding yeast chromatin-associated interactome.
Effects of hap mutations on heme and cytochrome formation in yeast.
-
hap2 mutants have all cytochromes reduced to 40-50% of wild type and grow slowly on glycerol.
"In hap2 and hap3 strains all cytochromes were decreased proportionally to about 40-50% of wild type values."
Yeast HAP2 and HAP3: transcriptional activators in a heteromeric complex.
Cloning of yeast HAP5: a novel subunit of a heterotrimeric complex required for CCAAT binding.
-
Recombinant HAP2, HAP3 and HAP5 reconstitute CCAAT binding, and each subunit is required.
"purified recombinant HAP2, HAP3, and HAP5 are able to reconstitute CCAAT-binding activity in mobility shift analysis"
Mutations in yeast HAP2/HAP3 define a hybrid CCAAT box binding domain.
-
The HAP2 DNA-binding domain is a 21-residue region, and together with HAP3 it forms a hybrid CCAAT-binding domain.
"The DNA-binding domain of HAP2 is shown to be a 21 residue region containing three critical histidines and three critical arginines."
Sequence and nuclear localization of the Saccharomyces cerevisiae HAP2 protein, a transcriptional activator.
-
A HAP2-lacZ fusion is nuclear, and lexA-HAP2 activates transcription.
"a bifunctional HAP2-beta-galactosidase fusion gene was localized to the yeast nucleus"
Identification, mutational analysis, and coactivator requirements of two distinct transcriptional activation domains of the Saccharomyces cerevisiae Hap4 protein.
A multiprotein complex that interacts with RNA polymerase II elongator.
UniProt entry P06774 (HAP2_YEAST)
HAP2 PANTHER subfamily placement analysis