KES1 oxysterol-binding protein KES1 [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Official Symbol: KES1
Official Full Name: oxysterol-binding protein KES1
Primary source: SGD:S000006066
Locus tag: YPL145C
See related: AllianceGenome:SGD:S000006066; FungiDB:YPL145C; VEuPathDB:YPL145C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: BSR3; LPI3; OSH4
Summary: Enables oxysterol binding activity; phospholipid binding activity; and sterol transfer activity. Involved in several processes, including ER to Golgi ceramide transport; piecemeal microautophagy of the nucleus; and post-Golgi vesicle-mediated transport. Located in Golgi membrane. Orthologous to human OSBPL10 (oxysterol binding protein like 10) and OSBPL11 (oxysterol binding protein like 11). [provided by Alliance of Genome Resources, Nov 2024]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

See KES1 in Genome Data Viewer

Location:: chromosome: XVI

Exon count:: 1

Sequence:: Chromosome: XVI; NC_001148.4 (278395..279699, complement)

Chromosome XVI - NC_001148.4 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Proposed dual membrane contact with full-length Osh4.
Title: Proposed dual membrane contact with full-length Osh4.
Coordinated regulation of phosphatidylinositol 4-phosphate and phosphatidylserine levels by Osh4p and Osh5p is an essential regulatory mechanism in autophagy.
Title: Coordinated regulation of phosphatidylinositol 4-phosphate and phosphatidylserine levels by Osh4p and Osh5p is an essential regulatory mechanism in autophagy.
This study developed an image processing technique for identifying packing defects to quantify the relationship between the amphipathic lipid packing sensor (ALPS) motif peptide of the Osh4 protein in yeast and packing defects on a membrane model using molecular dynamics simulations. The probability of the ALPS peptide moving toward the membrane increases when it is near a large packing defect.
Title: Effect of Membrane Lipid Packing on Stable Binding of the ALPS Peptide.
the sterol content in the mitochondrial fraction was significantly decreased in vivo after Osh4 inactivation in a genetic background in which all the other OSH genes were deleted.
Title: Oxysterol-binding protein homologs mediate sterol transport from the endoplasmic reticulum to mitochondria in yeast.
Osh4-mediated exocytosis depends upon lipid binding and exchange without a strict requirement for sterol.
Title: Lipid-dependent regulation of exocytosis in S. cerevisiae by OSBP homolog (Osh) 4.
Deletion of KES1 suppresses plasma membrane-missorting defects and the accumulation of intracellular ergosterol in drs2 mutants.
Title: Phosphatidylserine translocation at the yeast trans-Golgi network regulates protein sorting into exocytic vesicles.
Osh4p transports sterol against its gradient between two membranes by dissipating the energy of a phosphatidylinositol-4-phosphate gradient.
Title: A phosphatidylinositol-4-phosphate powered exchange mechanism to create a lipid gradient between membranes.
Osh4p is needed to reduce the level of phosphatidylinositol-4-phosphate on secretory vesicles as they mature.
Title: Osh4p is needed to reduce the level of phosphatidylinositol-4-phosphate on secretory vesicles as they mature.
The results point to the stress-related proteins Ahp1, Yhb1 and Oye2, as well as Gln1 and Kes1 as putative candidates for being evaluated as biomarkers for diagnostic assays of S. cerevisiae infections.
Title: Immunoproteomic profiling of Saccharomyces cerevisiae systemic infection in a murine model.
X-ray crystallographic determination of the conformational changes Osh4 undergoes during ligand binding.
Title: Synthesis and structure of 16,22-diketocholesterol bound to oxysterol-binding protein Osh4.

Submit: New GeneRIF Correction See all GeneRIFs (20)

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables lipid binding	IDA Inferred from Direct Assay more info	PubMed
enables lipid binding	IEA Inferred from Electronic Annotation more info
enables lipid binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables oxysterol binding	IBA Inferred from Biological aspect of Ancestor more info
enables oxysterol binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables oxysterol binding	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables phosphatidic acid binding	IDA Inferred from Direct Assay more info	PubMed
enables phosphatidylinositol-4,5-bisphosphate binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables phosphatidylinositol-4-phosphate binding	IDA Inferred from Direct Assay more info	PubMed
enables sterol transfer activity	IDA Inferred from Direct Assay more info	PubMed
enables sterol transfer activity	IEA Inferred from Electronic Annotation more info
enables sterol transfer activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in ER to Golgi ceramide transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in endocytosis	IEA Inferred from Electronic Annotation more info
involved_in endocytosis	IGI Inferred from Genetic Interaction more info	PubMed
involved_in exocytosis	IEA Inferred from Electronic Annotation more info
involved_in exocytosis	IGI Inferred from Genetic Interaction more info	PubMed
involved_in lipid transport	IEA Inferred from Electronic Annotation more info
involved_in maintenance of cell polarity	IEA Inferred from Electronic Annotation more info
involved_in maintenance of cell polarity	IGI Inferred from Genetic Interaction more info	PubMed
involved_in piecemeal microautophagy of the nucleus	IEA Inferred from Electronic Annotation more info
involved_in piecemeal microautophagy of the nucleus	IGI Inferred from Genetic Interaction more info	PubMed
involved_in post-Golgi vesicle-mediated transport	IGI Inferred from Genetic Interaction more info	PubMed
involved_in sphingolipid metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in sterol transport	IDA Inferred from Direct Assay more info	PubMed
involved_in sterol transport	IGI Inferred from Genetic Interaction more info	PubMed
involved_in sterol transport	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
located_in Golgi membrane	IDA Inferred from Direct Assay more info	PubMed
located_in Golgi membrane	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
is_active_in membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in membrane	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: oxysterol-binding protein KES1

NP_015180.1

Sterol/phosphatidylinositol-4-phosphate (PI(4)P) exchanger; one of seven members of the yeast oxysterol binding protein family; involved in negative regulation of Sec14p-dependent Golgi complex secretory functions, peripheral membrane protein that localizes to the Golgi complex; KES1 has a paralog, HES1, that arose from the whole genome duplication