| Standard Name | BPL1 1 |
|---|---|
| Systematic Name | YDL141W |
| Alias | ACC2 2 |
| Feature Type | ORF, Verified |
| Description | Biotin:apoprotein ligase, covalently modifies proteins with the addition of biotin, required for acetyl-CoA carboxylase (Acc1p) holoenzyme formation (1, 3 and see Summary Paragraph) |
| Name Description | Biotin:apoProtein Ligase 1 |
| Chromosomal Location | |
|---|---|
Gene Ontology Annotations All BPL1 GO evidence and references
| View Computational GO annotations for BPL1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| High-throughput |
Mutant phenotypes All BPL1 Phenotype evidence and references
| Classical genetics | |
|---|---|
| null | |
| unspecified | |
| Large-scale survey | |
| conditional | |
| null | |
| overexpression | |
| Resources |
interactions All BPL1 Interaction evidence and references
| 21 total interaction(s) for 21 unique genes/features. | |
| Physical Interactions |
|
| Genetic Interactions |
|
| Resources |
|
Expression Summary
|
| |
| Resources |
Protein Information All BPL1 Protein evidence and references
| Localization | |
|---|---|
| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
|
| |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
| ||||||||||||
| Retrieve sequences | |||||||||||||
Analyze Sequence
| S288C only | |
|---|---|
| S288C vs. other species | |
| S288C vs. other strains |
Resources
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
|---|
| Primary SGDID | S000002300 |
|---|
SUMMARY PARAGRAPH for BPL1
BPL1 encodes biotin-apoprotein ligase (1), an enzyme that modifies proteins by covalently attaching biotin. Bpl1p is essential (3); among its substrates is Acc1p, acetyl-CoA carboxylase, which acts in fatty acid biosynthesis (3, 2). Bpl1p has strong sequence similarities to biotin--apoprotein ligases from E. coli and human; BPL1 can complement a deletion of E. coli birA (1). Mutations in the human biotin--apoprotein ligase are associated with ataxia and carboxylase deficiency (4).
References cited on this page View Complete Literature Guide for BPL1
| 1) | Cronan JE Jr and Wallace JC (1995) The gene encoding the biotin-apoprotein ligase of Saccharomyces cerevisiae. FEMS Microbiol Lett 130(2-3):221-9 |
| 2) | Mishina M, et al. (1980) Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin: apocarboxylase ligase. Eur J Biochem 111(1):79-87 |
| 3) | Hoja U, et al. (1998) Pleiotropic phenotype of acetyl-CoA-carboxylase-defective yeast cells--viability of a BPL1-amber mutation depending on its readthrough by normal tRNA(Gln)(CAG). Eur J Biochem 254(3):520-6 |
| 4) | Foury F (1997) Human genetic diseases: a cross-talk between man and yeast. Gene 195(1):1-10 |





