ATP6V0E1:V-type proton ATPase subunit e 1

Gene Name
V-type proton ATPase subunit e 1
Protein ID
O15342
Chromosome ID
5
HPP Status
2
Protein Name
V-type proton ATPase subunit e 1
Synonyms

V-ATPase subunit e 1

H(+)-transporting two-sector ATPase, subunit H

V-type proton ATPase subunit e 1

ATP6H

vacuolar proton-ATPase subunit M9.2

V-ATPase M9.2 subunit

vacuolar ATP synthase subunit H

Vma21p

V-ATPase 9.2 kDa membrane accessory protein

vacuolar proton pump subunit e 1

Vacuolar proton pump subunit e 1

ATPase, H+ transporting, lysosomal (vacuolar proton pump) 9kD

V-ATPase H subunit

M9.2

ATP6V0E

Vma21

ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e

ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e1

vacuolar proton pump H subunit


[Reference: http://www.genecards.org/cgi-bin/carddisp.pl?gene=ATP6V0E1 ]
Chromosomal Position
5q35.1 | Start:172983757 End:172983757
Sequence
O15342.fasta
Description

Entrez Gene Summary for ATP6V0E1
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is possibly part of the V0 subunit. Since two nontranscribed pseudogenes have been found in dog, it is possible that the localization to chromosome 2 for this gene by radiation hybrid mapping is representing a pseudogene. Genomic mapping puts the chromosomal location on 5q35.3. (provided by RefSeq, Jul 2008)

UniProtKB Summary for ATP6V0E1
Function: Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells

Tocris Summary for ATP6V0E1
H+-ATPase (also known as vacuolar ATPase, V-ATPase) is a enzyme transporter that functions to acidify intracellular compartments in eukaryotic cells. It is ubiquitously expressed and is present in endomembrane organelles such as vacuoles, lysosomes, endosomes, the Golgi apparatus, chromaffin granules and coated vesicles, as well as in the plasma membrane. H+-ATPase is a multisubunit complex composed of two domains. The V1 domain is responsible for ATP hydrolysis and the V0 domain is responsible for protein translocation. There are two main mechanisms of regulating H+-ATPase activity; recycling of H+-ATPase-containing vesicles to and from the plasma membrane and glucose-sensitive assembly/disassembly of the holoenzyme complex. These transporters play an important role in processes such as receptor-mediated endocytosis, protein degradation and coupled transport. They have a function in bone reabsorption and mutations in the A3 gene cause recessive osteopetrosis. Furthermore, H+-ATPases have been implicated in tumor metastasis and regulation of sperm motility and maturation.

[Reference: http://www.genecards.org/cgi-bin/carddisp.pl?gene=ATP6V0E1 ]
External IDs
Hgnc ID: 863 EntrezGene ID: 8992 Ensembl ID: ENSG00000113732
[Reference: http://www.genecards.org/cgi-bin/carddisp.pl?gene=ATP6V0E1 ]
Reference Source
http://www.nextprot.org

Gene Reference Into Function (GeneRIF)


PubMed IDGeneRIF TextLast Update
12163484Data demonstrate the physiological significance of the interaction between the E and H subunits of V-ATPase and extend previous studies on the arrangement of subunits on the peripheral stalk of V-ATPase.2010-01-21
17576770there is an important role for physical association between aldolase and the A, B and E subunits of V-ATPase in the regulation of the proton pump2010-01-21
Reference
http://www.ncbi.nlm.nih.gov/gene/about-generif
ftp://ftp.ncbi.nih.gov/gene/GeneRIF/

OMICSDI Browser



Relevant citations within the PubMed literature

         

Putative/known Functions



Localisation



Homologues, Orthologues, Paralogues and Family



Sequence Similarity and Functional Annotation


Sequence Similarity

Db NameQuery UniSubject UniSequence LengthAlignment LengthIdentityCoverageMismatchesGap OpeningsQuery StartQuery EndSubject StartSubject EndEvalueBit Score
Reviewed non-human mammalian with experimental evidenceVA0E1_HUMANVA0E1_BOVIN818197.53100201811811E-40159
Reference
Islam MT, Garg G, Hancock WS, Risk BA, Baker MS, Ranganathan S (2014) Protannotator: A Semiautomated Pipeline for Chromosome-Wise Functional Annotation of the "Missing" Human Proteome. J Proteome Res. 13, 76-83.

InterProScan Annotation

Uniprot IDInterpro IDGo IDTypeNameCategoryDescription
VA0E1_HUMANIPR008389GO:0015078FamilyATPase, V0 complex, subunit e1/e2Molecular Functionhydrogen ion transmembrane transporter activity
VA0E1_HUMANIPR008389GO:0015991FamilyATPase, V0 complex, subunit e1/e2Biological ProcessATP hydrolysis coupled proton transport
VA0E1_HUMANIPR017385GO:0015078FamilyATPase, V0 complex, subunit e1/e2, metazoaMolecular Functionhydrogen ion transmembrane transporter activity
VA0E1_HUMANIPR017385GO:0015991FamilyATPase, V0 complex, subunit e1/e2, metazoaBiological ProcessATP hydrolysis coupled proton transport
Reference
Islam MT, Garg G, Hancock WS, Risk BA, Baker MS, Ranganathan S (2014) Protannotator: A Semiautomated Pipeline for Chromosome-Wise Functional Annotation of the "Missing" Human Proteome. J Proteome Res. 13, 76-83.

KEGG Pathways

Pathway IDDatabase NamePathway Name
hsa00190KEGG PATHWAYOxidative phosphorylation
hsa01100KEGG PATHWAYMetabolic pathways
hsa04145KEGG PATHWAYPhagosome
hsa04721KEGG PATHWAYSynaptic vesicle cycle
hsa04966KEGG PATHWAYCollecting duct acid secretion
hsa05110KEGG PATHWAYVibrio cholerae infection
hsa05120KEGG PATHWAYEpithelial cell signaling in Helicobacter pylori infection
hsa05323KEGG PATHWAYRheumatoid arthritis
Reference
Islam MT, Garg G, Hancock WS, Risk BA, Baker MS, Ranganathan S (2014) Protannotator: A Semiautomated Pipeline for Chromosome-Wise Functional Annotation of the "Missing" Human Proteome. J Proteome Res. 13, 76-83.

Post Translational Modifications



Protein Protein Interactions



Best Available Mass Spectra without FDR




Showing 1-18 of 18 items.

gpmDB

Peptide SequenceEvidence LevelLog ENumber Of ObservationSpectraAccession IDProteotypicityAnnotation
NETIWYLKgreen-7.81031ENSP00000265093Proteotypic
NETIWYLKgreen-7.81031ENSP00000265093Proteotypic
NETIWYLKgreen-7.51031ENSP00000265093Proteotypic
NETIWYLKgreen-7.51031ENSP00000265093Proteotypic
NETIWYLKgreen-7.01031ENSP00000265093Proteotypic
NETIWYLKgreen-7.01031ENSP00000265093Proteotypic
NETIWYLKgreen-6.91031ENSP00000265093Proteotypic
NETIWYLKgreen-6.91031ENSP00000265093Proteotypic
NETIWYLKgreen-6.41031ENSP00000265093Proteotypic
NETIWYLKgreen-6.41031ENSP00000265093Proteotypic
NETIWYLKgreen-6.41031ENSP00000265093Proteotypic
NETIWYLKgreen-6.41031ENSP00000265093Proteotypic
NETIWYLKgreen-6.21031ENSP00000265093Proteotypic
NETIWYLKgreen-6.21031ENSP00000265093Proteotypic
NETIWYLKgreen-6.11031ENSP00000265093Proteotypic
NETIWYLKgreen-6.11031ENSP00000265093Proteotypic
NETIWYLKgreen-6.11031ENSP00000265093Proteotypic
NETIWYLKgreen-6.11031ENSP00000265093Proteotypic
Evidence File
/mnt/mpp/ms_data/O15342_gpmdb.txt
Reference
Fenyö, David; Beavis, Ronald C. (2015). "The GPMDB REST interface". Bioinformatics 31 (12): 2056–2058. doi:10.1093/bioinformatics/btv107. ISSN 1367-4803.
http://gpmdb.thegpm.org/ ">Global Proteome Machine Database - THE GPM