Version 5.4
Homo sapiens Protein: ATP5L2
Summary
InnateDB Protein IDBP-473777.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ATP5L2
Protein Name ATP synthase, H+ transporting, mitochondrial Fo complex, subunit G2
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000421076
InnateDB Gene IDBG-408803 (ATP5L2)
Protein Structure
UniProt Annotation
Function Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). {ECO:0000250}.
Subcellular Localization Mitochondrion membrane {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0015078 hydrogen ion transmembrane transporter activity
Biological Process
GO:0015986 ATP synthesis coupled proton transport
Cellular Component
GO:0000276 mitochondrial proton-transporting ATP synthase complex, coupling factor F(o)
Protein Structure and Domains
PDB ID
InterPro IPR006808 ATPase, F0 complex, subunit G, mitochondrial
IPR016702 Mitochondrial ATP synthase subunit g, animal
PFAM PF04718
PRINTS
PIRSF PIRSF017835
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q7Z4Y8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 267020
UniGene
RefSeq NP_001159349
HUGO HGNC:13213
OMIM
CCDS CCDS54534
HPRD
IMGT
EMBL AF092923 BC093719 BC093721
GenPept AAP97217

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca