BPL1/YDL141W Summary Help

BPL1 BASIC INFORMATION

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
GO Annotations All BPL1 GO evidence and references
    View Computational GO annotations for BPL1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Pathways
Mutant Phenotype All BPL1 Phenotype details and references
Classical genetics
null
unspecified
Large-scale survey
conditional
null
overexpression
Interactions BPL1 All interactions details and references
7 total interaction(s) for 7 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 5
  • Reconstituted Complex: 1
Genetic Interactions
  • Phenotypic Suppression: 1
Sequence Information
ChrIV:203040 to 205112 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..2073 203040..205112 1996-07-31 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000002300

BPL1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Protein Info & Structure
  • Localization Resources
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  • Phenotype Resources
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  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for BPL1

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).

Last updated: 1999-11-02

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