ATP14/YLR295C Summary Help

Standard Name ATP14
Systematic Name YLR295C
Feature Type ORF, Verified
Description Subunit h of the F0 sector of mitochondrial F1F0 ATP synthase; F1F0 ATP synthase is a large, evolutionarily conserved enzyme complex required for ATP synthesis; protein abundance increases in response to DNA replication stress (1, 2 and see Summary Paragraph)
Name Description ATP synthase
Chromosomal Location
ChrXII:722373 to 721999 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All ATP14 GO evidence and references
  View Computational GO annotations for ATP14
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 5 genes
Resources
Classical genetics
null
repressible
Large-scale survey
null
Resources
78 total interaction(s) for 70 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 6
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 1
  • Biochemical Activity: 2
  • Co-purification: 5
  • Protein-RNA: 1
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 30
  • Positive Genetic: 22
  • Synthetic Growth Defect: 3
  • Synthetic Haploinsufficiency: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 124
Molecular Weight (Da) 14,128
Isoelectric Point (pI) 4.45
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXII:722373 to 721999 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..375 722373..721999 2011-02-03 1996-07-31
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 SGDIDS000004286
SUMMARY PARAGRAPH for ATP14

ATP14 encodes subunit h of yeast mitochondrial ATP synthase (1). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (3). The structure of this enzyme complex is highly conserved among diverse organisms and consists of two major components, soluble F1 and membrane-bound F0, each of which contains many subunits. Subunit h is one of only a few known ATP synthase subunits that are unique to yeast mitochondria; no subunit h homologs have been identified in either mammalian mitochondria or bacteria. Although the specific function of this protein is not yet known, it is essential for F0 assembly and ATP synthase activity (4 and references therein). Its N-terminal 32 amino acids are removed during import into mitochondria (5). Deletion of ATP14, like deletions in many genes necessary for the function or maintenance of mitochondria, leads to a "petite" phenotyepe that is slow-growing and unable to survive on nonfermentable carbon sources (1).

General ATP synthase structure and function are reviewed in references 3 and 6. For a review that is specific to yeast, see reference 4.

Last updated: 2007-10-23 Contact SGD

References cited on this page View Complete Literature Guide for ATP14
1) Arselin G, et al.  (1996) ATP synthase of yeast mitochondria. Isolation of the subunit h and disruption of the ATP14 gene. J Biol Chem 271(34):20284-90
2) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
3) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
4) 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
5) Du Y, et al.  (2006) Top-down approaches for measuring expression ratios of intact yeast proteins using Fourier transform mass spectrometry. Anal Chem 78(3):686-94
6) Nakamoto RK, et al.  (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28():205-34