Version 5.4
Mus musculus Protein: Atp6v0e
Summary
InnateDB Protein IDBP-155344.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Atp6v0e
Protein Name ATPase, H+ transporting, lysosomal V0 subunit E
Synonyms Atp6k; Atp6v0e1; M9.2;
Species Mus musculus
Ensembl Protein ENSMUSP00000015719
InnateDB Gene IDBG-155342 (Atp6v0e)
Protein Structure
UniProt Annotation
Function Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. {ECO:0000250}.
Subcellular Localization Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0015078 hydrogen ion transmembrane transporter activity
GO:0016787 hydrolase activity
Biological Process
GO:0008152 metabolic process
GO:0015991 ATP hydrolysis coupled proton transport
GO:0016049 cell growth
GO:0043200 response to amino acid
Cellular Component
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0033179 proton-transporting V-type ATPase, V0 domain
Protein Structure and Domains
PDB ID MGI:1328318
InterPro IPR008389 ATPase, V0 complex, subunit e1/e2
IPR017385 ATPase, V0 complex, subunit e1/e2, metazoa
PFAM PF05493
PRINTS
PIRSF PIRSF038097
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9CQD8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 11974
UniGene Mm.443141
RefSeq NP_079548
MGI ID
MGI Symbol Atp6v0e
OMIM
CCDS CCDS28554
HPRD
IMGT
EMBL AK007610 AK013229 AK017760 AK030335 AK134836 AK159669 AK168015 BC024733
GenPept AAH24733 BAB25133 BAB28727 BAB30911 BAC26909 BAE22305 BAE35273 BAE40002

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