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Reviewed, UniProtKB/Swiss-Prot P36543 (VATE1_HUMAN)

Last modified December 15, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    V-type proton ATPase subunit E 1
      Short name=V-ATPase subunit E 1
Alternative name(s):
    Vacuolar proton pump subunit E 1
    V-ATPase 31 kDa subunit
      Short name=P31
Gene names
Name: ATP6V1E1
Synonyms: ATP6E, ATP6E2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

Subunit structure

V-ATPase is an heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). Interacts with ALDOC.

Tissue specificity

Ubiquitous. Ref.8

Sequence similarities

Belongs to the V-ATPase E subunit family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATP6V1G2O956701EBI-348639,EBI-348290

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 226225V-type proton ATPase subunit E 1
PRO_0000117295

Amino acid modifications

Modified residue21N-acetylalanine
Modified residue561Phosphotyrosine Ref.9

Natural variations

Natural variant501R → G in a colorectal cancer sample; somatic mutation. Ref.12
VAR_036565

Experimental info

Sequence conflict321A → R in CAA50592. Ref.3
Sequence conflict861A → G Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36543-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: DFD0D44E6D9AEA17

FASTA22626,145
        10         20         30         40         50         60 
MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK 

        70         80         90        100        110        120 
EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ RLSKVVKDTT RYQVLLDGLV 

       130        140        150        160        170        180 
LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK AIPMYKIATK NDVDVQIDQE SYLPEDIAGG 

       190        200        210        220 
VEIYNGDRKI KVSNTLESRL DLIAQQMMPE VRGALFGANA NRKFLD 

« Hide

References

« Hide 'large scale' references
[1]"Immunologic evidence that vacuolar H+ ATPases with heterogeneous forms of Mr = 31,000 subunit have different membrane distributions in mammalian kidney."
Hemken P., Guo X.-L., Wang Z.-Q., Zhang K., Gluck S.
J. Biol. Chem. 267:9948-9957(1992) [PubMed: 1533641] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The E subunit of vacuolar H(+)-ATPase localizes close to the centromere on human chromosome 22."
Baud V., Mears A., Lamour V., Scamps C., McDermid A., Lipinski M.
Hum. Mol. Genet. 3:335-339(1994) [PubMed: 8004105] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase."
van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.
Biochem. Biophys. Res. Commun. 197:15-21(1993) [PubMed: 8250920] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Osteoclastoma.
[4]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[6]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 112-131, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[7]"Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump."
Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.
J. Biol. Chem. 276:30407-30413(2001) [PubMed: 11399750] [Abstract]
Cited for: INTERACTION WITH ALDOC.
[8]"A human gene, ATP6E1, encoding a testis-specific isoform of H(+)-ATPase subunit E."
Imai-Senga Y., Sun-Wada G.H., Wada Y., Futai M.
Gene 289:7-12(2002) [PubMed: 12036578] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, MASS SPECTROMETRY.
Tissue: Lung.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-50.
+Additional computationally mapped references.

Cross-references

Sequence databases

X76228 mRNA. Translation: CAA53814.1.
X71491 mRNA. Translation: CAA50592.1.
CR456385 mRNA. Translation: CAG30271.1.
BC004443 mRNA. Translation: AAH04443.1.
IPIIPI00003856.
PIRS60562.
RefSeqNP_001687.1.
UniGeneHs.517338

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP36543. 3 interactions.
STRINGP36543.

Protein family/group databases

TCDB3.A.2.2.4. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

PTM databases

PhosphoSiteP36543.

Proteomic databases

PRIDEP36543.

Genome annotation databases

EnsemblENST00000253413; ENSP00000253413; ENSG00000131100; Homo sapiens. [Genome view]
GeneID529.
UCSCuc002zmr.1. human.

Organism-specific databases

CTD529.
GeneCardsGC22M016449.
H-InvDBHIX0016214.
HGNCHGNC:857. ATP6V1E1.
HPACAB009528.
CAB018699.
MIM108746. gene.
PharmGKBPA25158.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG525538.
HOVERGENP36543.
InParanoidP36543.
OMAQQRQKIM.
OrthoDBEOG9H48PB.

Enzyme and pathway databases

BRENDA3.6.3.14. 247.

Gene expression databases

ArrayExpressP36543.
BgeeP36543.
CleanExHS_ATP6V1E1.
GenevestigatorP36543.
GermOnlineENSG00000131100. Homo sapiens.

Family and domain databases

InterProIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamPF01991. vATP-synt_E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio2197.
SOURCESearch...

Entry information

Entry nameVATE1_HUMAN
AccessionPrimary (citable) accession number: P36543
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: December 15, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents