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Protein

V-type proton ATPase subunit E 2

Gene

ATP6V1E2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. This isoform is essential for energy coupling involved in acidification of acrosome (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS10256-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.
REACT_25300. Ion channel transport.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit E 2
Short name:
V-ATPase subunit E 2
Alternative name(s):
Vacuolar proton pump subunit E 2
Gene namesi
Name:ATP6V1E2
Synonyms:ATP6E1, ATP6EL2, ATP6V1EL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18125. ATP6V1E2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25159.

Polymorphism and mutation databases

BioMutaiATP6V1E2.
DMDMi74731076.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226V-type proton ATPase subunit E 2PRO_0000282344Add
BLAST

Proteomic databases

MaxQBiQ96A05.
PaxDbiQ96A05.
PRIDEiQ96A05.

PTM databases

PhosphoSiteiQ96A05.

Expressioni

Tissue specificityi

Testis specific.1 Publication

Gene expression databases

BgeeiQ96A05.
CleanExiHS_ATP6V1E2.
GenevestigatoriQ96A05.

Organism-specific databases

HPAiHPA052784.

Interactioni

Subunit structurei

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
ATP6V1G1O753486EBI-8650380,EBI-711802
C9orf16Q9BUW73EBI-8650380,EBI-752084

Protein-protein interaction databases

BioGridi124715. 5 interactions.
IntActiQ96A05. 2 interactions.
STRINGi9606.ENSP00000304891.

Structurei

3D structure databases

ProteinModelPortaliQ96A05.
SMRiQ96A05. Positions 2-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase E subunit family.Curated

Phylogenomic databases

eggNOGiCOG1390.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
HOVERGENiHBG002309.
InParanoidiQ96A05.
KOiK02150.
OMAiSGNQRIK.
OrthoDBiEOG70PC01.
PhylomeDBiQ96A05.
TreeFamiTF313479.

Family and domain databases

HAMAPiMF_00311. ATP_synth_E_arch.
InterProiIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamiPF01991. vATP-synt_E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96A05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSDVDVKK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR
60 70 80 90 100
LKIMEYYEKK EKQIEQQKKI LMSTMRNQAR LKVLRARNDL ISDLLSEAKL
110 120 130 140 150
RLSRIVEDPE VYQGLLDKLV LQGLLRLLEP VMIVRCRPQD LLLVEAAVQK
160 170 180 190 200
AIPEYMTISQ KHVEVQIDKE AYLAVNAAGG VEVYSGNQRI KVSNTLESRL
210 220
DLSAKQKMPE IRMALFGANT NRKFFI
Length:226
Mass (Da):26,074
Last modified:December 1, 2001 - v1
Checksum:i40546707D944ED20
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB074759 mRNA. Translation: BAC00847.1.
AK058055 mRNA. Translation: BAB71643.1.
AC018682 Genomic DNA. Translation: AAY14833.1.
BC008981 mRNA. Translation: AAH08981.1.
BC034808 mRNA. Translation: AAH34808.1.
CCDSiCCDS1826.1.
RefSeqiNP_542384.1. NM_080653.3.
XP_005264690.1. XM_005264633.1.
XP_005264691.1. XM_005264634.1.
UniGeneiHs.659656.

Genome annotation databases

EnsembliENST00000306448; ENSP00000304891; ENSG00000250565.
ENST00000522587; ENSP00000428141; ENSG00000250565.
GeneIDi90423.
KEGGihsa:90423.
UCSCiuc002ruy.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB074759 mRNA. Translation: BAC00847.1.
AK058055 mRNA. Translation: BAB71643.1.
AC018682 Genomic DNA. Translation: AAY14833.1.
BC008981 mRNA. Translation: AAH08981.1.
BC034808 mRNA. Translation: AAH34808.1.
CCDSiCCDS1826.1.
RefSeqiNP_542384.1. NM_080653.3.
XP_005264690.1. XM_005264633.1.
XP_005264691.1. XM_005264634.1.
UniGeneiHs.659656.

3D structure databases

ProteinModelPortaliQ96A05.
SMRiQ96A05. Positions 2-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124715. 5 interactions.
IntActiQ96A05. 2 interactions.
STRINGi9606.ENSP00000304891.

PTM databases

PhosphoSiteiQ96A05.

Polymorphism and mutation databases

BioMutaiATP6V1E2.
DMDMi74731076.

Proteomic databases

MaxQBiQ96A05.
PaxDbiQ96A05.
PRIDEiQ96A05.

Protocols and materials databases

DNASUi90423.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306448; ENSP00000304891; ENSG00000250565.
ENST00000522587; ENSP00000428141; ENSG00000250565.
GeneIDi90423.
KEGGihsa:90423.
UCSCiuc002ruy.3. human.

Organism-specific databases

CTDi90423.
GeneCardsiGC02M046717.
HGNCiHGNC:18125. ATP6V1E2.
HPAiHPA052784.
neXtProtiNX_Q96A05.
PharmGKBiPA25159.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1390.
GeneTreeiENSGT00390000002730.
HOGENOMiHOG000202506.
HOVERGENiHBG002309.
InParanoidiQ96A05.
KOiK02150.
OMAiSGNQRIK.
OrthoDBiEOG70PC01.
PhylomeDBiQ96A05.
TreeFamiTF313479.

Enzyme and pathway databases

BioCyciMetaCyc:HS10256-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.
REACT_25300. Ion channel transport.

Miscellaneous databases

GeneWikiiATP6V1E2.
GenomeRNAii90423.
NextBioi76752.
PROiQ96A05.

Gene expression databases

BgeeiQ96A05.
CleanExiHS_ATP6V1E2.
GenevestigatoriQ96A05.

Family and domain databases

HAMAPiMF_00311. ATP_synth_E_arch.
InterProiIPR002842. ATPase_V1/A1-cplx_esu.
[Graphical view]
PfamiPF01991. vATP-synt_E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "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.
    , 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].
    Tissue: Testis.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain and Cervix.

Entry informationi

Entry nameiVATE2_HUMAN
AccessioniPrimary (citable) accession number: Q96A05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 1, 2001
Last modified: May 27, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.