Version 5.4
Homo sapiens Protein: ATP6V0D2
Summary
InnateDB Protein IDBP-27529.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ATP6V0D2
Protein Name ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d2
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000285393
InnateDB Gene IDBG-27527 (ATP6V0D2)
Protein Structure
UniProt Annotation
Function Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis (By similarity). {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity Kidney, osteoclast and lung. {ECO:0000269PubMed:12384298}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 6 experimentally validated interaction(s) in this database.
They are also associated with 2 interaction(s) predicted by orthology.
Experimentally validated
Total 6 [view]
Protein-Protein 6 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0015078 hydrogen ion transmembrane transporter activity
Biological Process
GO:0006879 cellular iron ion homeostasis
GO:0008286 insulin receptor signaling pathway
GO:0015991 ATP hydrolysis coupled proton transport
GO:0033572 transferrin transport
GO:0051701 interaction with host
GO:0055085 transmembrane transport
GO:0090382 phagosome maturation
Cellular Component
GO:0005768 endosome
GO:0005769 early endosome
GO:0010008 endosome membrane
GO:0016020 membrane
GO:0016324 apical plasma membrane
GO:0016471 vacuolar proton-transporting V-type ATPase complex
GO:0030670 phagocytic vesicle membrane
GO:0033179 proton-transporting V-type ATPase, V0 domain
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR002843 ATPase, V0 complex, c/d subunit
IPR016727 ATPase, V0 complex, subunit d
PFAM PF01992
PRINTS
PIRSF PIRSF018497
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8N8Y2
PhosphoSite PhosphoSite-Q8N8Y2
TrEMBL E5RIR3
UniProt Splice Variant
Entrez Gene 245972
UniGene Hs.709047
RefSeq NP_689778
HUGO HGNC:18266
OMIM
CCDS CCDS6241
HPRD 16522
IMGT
EMBL AC023194 AC084128 AK096027 AY079172 BC065207 CH471060
GenPept AAH65207 AAL87000 BAC04679 EAW91631 EAW91632

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