ATP11/YNL315C Summary Help

Standard Name ATP11
Systematic Name YNL315C
Feature Type ORF, Verified
Description Molecular chaperone; required for the assembly of alpha and beta subunits into the F1 sector of mitochondrial F1F0 ATP synthase; N-terminally propionylated in vivo (1, 2, 3 and see Summary Paragraph)
Name Description ATP synthase
Chromosomal Location
ChrXIV:44280 to 43324 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All ATP11 GO evidence and references
  View Computational GO annotations for ATP11
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 6 genes
Classical genetics
Large-scale survey
210 total interaction(s) for 205 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 4
  • Affinity Capture-RNA: 5
  • Co-fractionation: 2
  • Two-hybrid: 7

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 139
  • Phenotypic Suppression: 4
  • Positive Genetic: 38
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 2
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 318
Molecular Weight (Da) 36,851
Isoelectric Point (pI) 9.79
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIV:44280 to 43324 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..957 44280..43324 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005259

ATP11 encodes a protein required for the assembly of mitochondrial ATP synthase 4. The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (5) and consists of two major components, soluble F1 and membrane-bound F0, each of which contains many subunits (6). The catalytic core of the enzyme resides in the F1 component and consists of a hexamer of alternating alpha (Atp1p) and beta (Atp2p) subunits (7, 8). Although Atp11p binds selectively to the beta subunit, it is not a part of the ATP synthase complex. Instead, Atp11p binds to isolated beta subunits in order to prevent beta subunit aggregation prior to F1 assembly. It is likely that Atp11p is displaced by the alpha subunit during complex assembly (9). A second protein, Atp12p, functions in a similar manner to prevent aggregation of the alpha subunit prior to F1 assembly (4, 10).

Deletion of ATP11 leads to aggregation of beta subunits and loss of F1 assembly. Although ATP11 is required for the production of functional ATP synthase, it is not essential for life in yeast. Like deletions in many genes necessary for the function or maintenance of mitochondria, loss of ATP11 leads to a "petite" phenotype that is slow-growing and unable to survive on nonfermentable carbon sources (4).

Last updated: 2001-02-27 Contact SGD

References cited on this page View Complete Literature Guide for ATP11
1) Ackerman S  (2002) Atp11p and Atp12p are chaperones for F(1)-ATPase biogenesis in mitochondria. Biochim Biophys Acta 1555(1-3):101
2) Hinton A, et al.  (2003) A purified subfragment of yeast Atp11p retains full molecular chaperone activity. J Biol Chem 278(36):34110-3
3) Foyn H, et al.  (2013) Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo. Mol Cell Proteomics 12(1):42-54
4) Ackerman SH and Tzagoloff A  (1990) Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase. Proc Natl Acad Sci U S A 87(13):4986-90
5) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
6) Devenish RJ, et al.  (2000) Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex. Biochim Biophys Acta 1458(2-3):428-42
7) Abrahams JP, et al.  (1993) Inherent asymmetry of the structure of F1-ATPase from bovine heart mitochondria at 6.5 A resolution. EMBO J 12(5):1775-80
8) Abrahams JP, et al.  (1994) Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370(6491):621-8
9) Wang ZG and Ackerman SH  (2000) The assembly factor Atp11p binds to the beta-subunit of the mitochondrial F(1)-ATPase. J Biol Chem 275(8):5767-72
10) Wang ZG, et al.  (2000) The alpha-subunit of the mitochondrial F(1) ATPase interacts directly with the assembly factor Atp12p. EMBO J 19(7):1486-93