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P36543 (VATE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V-type proton ATPase subunit E 1

Short name=V-ATPase subunit E 1
Alternative name(s):
V-ATPase 31 kDa subunit
Short name=p31
Vacuolar proton pump subunit E 1
Gene names
Name:ATP6V1E1
Synonyms:ATP6E, ATP6E2
OrganismHomo sapiens (Human) [Reference 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. HAMAP-Rule MF_00311

Subunit structure

V-ATPase is a 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 RABL2/RABL2A; binds preferentially to GTP-bound RABL2 By similarity. Interacts with ALDOC. Interacts with RAB11B. Ref.9 Ref.13

Tissue specificity

Ubiquitous. Ref.10

Sequence similarities

Belongs to the V-ATPase E subunit family.

Ontologies

Keywords
   Biological processHydrogen ion transport
Ion transport
Transport
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: Ensembl

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

interaction with host

Traceable author statement. Source: Reactome

phagosome maturation

Traceable author statement. Source: Reactome

proton transport

Traceable author statement Ref.3. Source: ProtInc

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

microvillus

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

proton-transporting two-sector ATPase complex

Traceable author statement Ref.3. Source: ProtInc

proton-transporting two-sector ATPase complex, catalytic domain

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATPase binding

Inferred from physical interaction Ref.13. Source: UniProtKB

hydrogen-exporting ATPase activity, phosphorylative mechanism

Inferred from electronic annotation. Source: Ensembl

proton-transporting ATPase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P36543-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P36543-2)

The sequence of this isoform differs from the canonical sequence as follows:
     12-33: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P36543-3)

The sequence of this isoform differs from the canonical sequence as follows:
     93-122: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 226225V-type proton ATPase subunit E 1 HAMAP-Rule MF_00311
PRO_0000117295

Amino acid modifications

Modified residue21N-acetylalanine Ref.11
Modified residue561Phosphotyrosine By similarity

Natural variations

Alternative sequence12 – 3322Missing in isoform 2.
VSP_042925
Alternative sequence93 – 12230Missing in isoform 3.
VSP_044589
Natural variant501R → G in a colorectal cancer sample; somatic mutation. Ref.14
VAR_036565

Experimental info

Sequence conflict321A → R in CAA50592. Ref.3
Sequence conflict861A → G no nucleotide entry Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 [UniParc].

Checksum: 25B2BADC0BE9B22B
Show »

FASTA20423,587
Isoform 3 [UniParc].

Checksum: 32EEBB32390D88A2
Show »

FASTA19622,706

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Brain and Cerebellum.
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[8]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 112-131, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALDOC.
[10]"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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Rab11b and its effector Rip11 regulate the acidosis-induced traffic of V-ATPase in salivary ducts."
Oehlke O., Martin H.W., Osterberg N., Roussa E.
J. Cell. Physiol. 226:638-651(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11B.
[14]"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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-50.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76228 mRNA. Translation: CAA53814.1.
X71491 mRNA. Translation: CAA50592.1.
CR456385 mRNA. Translation: CAG30271.1.
AK294623 mRNA. Translation: BAG57804.1.
AK315941 mRNA. Translation: BAH14312.1.
AC004019 Genomic DNA. No translation available.
AC006285 Genomic DNA. No translation available.
AC007666 Genomic DNA. No translation available.
BC004443 mRNA. Translation: AAH04443.1.
PIRS60562.
RefSeqNP_001034455.1. NM_001039366.1.
NP_001034456.1. NM_001039367.1.
NP_001687.1. NM_001696.3.
UniGeneHs.517338.

3D structure databases

ProteinModelPortalP36543.
SMRP36543. Positions 2-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107012. 41 interactions.
IntActP36543. 7 interactions.
MINTMINT-5002575.
STRING9606.ENSP00000253413.

Protein family/group databases

TCDB3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteP36543.

Polymorphism databases

DMDM549207.

2D gel databases

UCD-2DPAGEP36543.

Proteomic databases

PaxDbP36543.
PRIDEP36543.

Protocols and materials databases

DNASU529.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253413; ENSP00000253413; ENSG00000131100. [P36543-1]
ENST00000399796; ENSP00000382694; ENSG00000131100. [P36543-3]
ENST00000399798; ENSP00000382696; ENSG00000131100. [P36543-2]
GeneID529.
KEGGhsa:529.
UCSCuc002zmr.1. human. [P36543-1]
uc002zms.1. human.
uc002zmt.1. human. [P36543-2]

Organism-specific databases

CTD529.
GeneCardsGC22M018074.
HGNCHGNC:857. ATP6V1E1.
HPACAB009528.
CAB018699.
HPA029196.
MIM108746. gene.
neXtProtNX_P36543.
PharmGKBPA25158.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1390.
HOGENOMHOG000202506.
HOVERGENHBG002309.
InParanoidP36543.
KOK02150.
OMATIRCRKQ.
OrthoDBEOG70PC01.
PhylomeDBP36543.
TreeFamTF313479.

Enzyme and pathway databases

BioCycMetaCyc:HS05489-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP36543.
BgeeP36543.
CleanExHS_ATP6V1E1.
GenevestigatorP36543.

Family and domain databases

HAMAPMF_00311. ATP_synth_E_arch.
InterProIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamPF01991. vATP-synt_E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP6V1E1.
GenomeRNAi529.
NextBio2197.
PROP36543.
SOURCESearch...

Entry information

Entry nameVATE1_HUMAN
AccessionPrimary (citable) accession number: P36543
Secondary accession number(s): A8MUE4, A8MUN4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

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