AKR1/YDR264C Summary

AKR1 BASIC INFORMATION

Standard Name	AKR1
Systematic Name	YDR264C
Feature Type	ORF, Verified
Description	Palmitoyl transferase involved in protein palmitoylation; acts as a negative regulator of pheromone response pathway; required for endocytosis of pheromone receptors; involved in cell shape control; contains ankyrin repeats (1)
Name Description	AnKyrin Repeat-containing protein

GO Annotations	All AKR1 GO evidence and references
	View Computational GO annotations for AKR1
Molecular Function
Manually curated	protein-cysteine S-palmitoleyltransferase activity (IDA)
Biological Process
Manually curated	endocytosis (IMP) pheromone-dependent signal transduction involved in conjugation with cellular fusion (IGI) protein amino acid palmitoylation (IDA, IMP) protein targeting to membrane (IMP)
Cellular Component
Manually curated	membrane (IDA)

Mutant Phenotype	All AKR1 Phenotype details and references
Classical genetics
null	metal resistance: decreased palmitoylated protein modification: decreased carboxypeptidase Y (Prc1p) modification: decreased resistance to hydroxyurea: decreased resistance to Calcofluor White: decreased
Large-scale survey
null	acid pH resistance: decreased bud morphology: abnormal cell size: increased polyphosphate accumulation: abnormal competitive fitness: decreased fermentative growth: decreased rate freeze-thaw resistance: decreased heat sensitivity: increased hyperosmotic stress resistance: decreased metal resistance: decreased resistance to L-1,4-dithiothreitol: decreased resistance to calcium dichloride: decreased resistance to caffeine: decreased resistance to cycloheximide: decreased resistance to ethanol: decreased resistance to hydroxyurea: decreased resistance to hygromycin B: decreased resistance to rapamycin: decreased resistance to oleate: decreased resistance to 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid: decreased resistance to monensin: decreased resistance to 5-fluorouracil: decreased resistance to doxorubicin: decreased resistance to propan-1-ol: decreased sporulation: decreased toxin resistance: decreased utilization of carbon source: decreased utilization of phosphorus source: decreased viable
overexpression	vegetative growth: decreased

Interactions	AKR1 All interactions details and references
	61 total interaction(s) for 54 unique genes/features.
Physical Interactions	Affinity Capture-MS: 8 Affinity Capture-RNA: 1 Biochemical Activity: 6 Co-localization: 1 Co-purification: 2 PCA: 22 Two-hybrid: 8
Genetic Interactions	Synthetic Growth Defect: 4 Synthetic Lethality: 2 Synthetic Rescue: 7

Sequence Information

ChrIV:998320 to 996026 | |

Note: this feature is encoded on the Crick strand.

Last Update

Coordinates: 2008-06-05 | Sequence: 1996-07-31

Subfeature details

	Relative Coordinates	Chromosomal Coordinates	Most Recent Updates
	Relative Coordinates	Chromosomal Coordinates	Coordinates	Sequence
CDS	1..2295	998320..996026	2008-06-05	1996-07-31

External Links	All Associated Seq \| E.C. \| Entrez Gene \| Entrez RefSeq Protein \| MIPS \| UniProtKB

Primary SGDID	S000002672

AKR1 RESOURCES

Click on map for expanded view

SGD ORF map	GBrowse

Click on histogram for expression summary
Expression Summary

ADDITIONAL INFORMATION for AKR1

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for AKR1]

1)	Roth AF, et al. (2002) The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. J Cell Biol 159(1):23-8

SGD^tm pages Database Copyright © 1997-2010 The Board of Trustees of Leland Stanford Junior University. Permission to use the information contained in this database was given by the researchers/institutes who contributed or published the information. Users of the database are solely responsible for compliance with any copyright restrictions, including those applying to the author abstracts. Documents from this server are provided "AS-IS" without any warranty, expressed or implied. The SGD project at Stanford University is supported by a Genome Research Resource Grant from the US National Human Genome Research Institute, part of the US National Institutes of Health.