Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P56381

- ATP5E_HUMAN

UniProt

P56381 - ATP5E_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

ATP synthase subunit epsilon, mitochondrial

Gene

ATP5E

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

Functioni

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity).By similarity

GO - Molecular functioni

  1. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
  3. transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cellular metabolic process Source: Reactome
  3. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  4. respiratory electron transport chain Source: Reactome
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit epsilon, mitochondrial
Short name:
ATPase subunit epsilon
Gene namesi
Name:ATP5E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:838. ATP5E.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  3. mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Mitochondrial complex V deficiency, nuclear 3 (MC5DN3) [MIM:614053]: A mitochondrial disorder with heterogeneous clinical manifestations including dysmorphic features, psychomotor retardation, hypotonia, growth retardation, cardiomyopathy, enlarged liver, hypoplastic kidneys and elevated lactate levels in urine, plasma and cerebrospinal fluid.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121Y → C in MC5DN3. 1 Publication
VAR_066211

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614053. phenotype.
Orphaneti254913. Isolated ATP synthase deficiency.
PharmGKBiPA25128.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 5150ATP synthase subunit epsilon, mitochondrialPRO_0000071662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211N6-acetyllysine; alternate1 Publication
Modified residuei21 – 211N6-succinyllysine; alternateBy similarity
Modified residuei32 – 321N6-acetyllysine; alternateBy similarity
Modified residuei32 – 321N6-succinyllysine; alternateBy similarity
Modified residuei37 – 371N6-acetyllysine; alternateBy similarity
Modified residuei37 – 371N6-succinyllysine; alternateBy similarity
Modified residuei44 – 441N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP56381.
PaxDbiP56381.
PRIDEiP56381.

PTM databases

PhosphoSiteiP56381.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP56381.
CleanExiHS_ATP5E.
GenevestigatoriP56381.

Organism-specific databases

HPAiHPA042142.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 (By similarity).By similarity

Protein-protein interaction databases

BioGridi106999. 3 interactions.
IntActiP56381. 1 interaction.
MINTiMINT-3021407.
STRINGi9606.ENSP00000243997.

Structurei

3D structure databases

ProteinModelPortaliP56381.
SMRiP56381. Positions 2-48.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic ATPase epsilon family.Curated

Phylogenomic databases

eggNOGiNOG318665.
GeneTreeiENSGT00390000015470.
HOGENOMiHOG000214506.
HOVERGENiHBG050611.
InParanoidiP56381.
KOiK02135.
OMAiGIAWIMV.
OrthoDBiEOG7GQXZP.
PhylomeDBiP56381.
TreeFamiTF300278.

Family and domain databases

Gene3Di1.10.1620.20. 1 hit.
InterProiIPR006721. ATPase_F1-cplx_esu_mt.
[Graphical view]
PfamiPF04627. ATP-synt_Eps. 1 hit.
[Graphical view]
SUPFAMiSSF48690. SSF48690. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56381-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAEKTSG SNVKIVKVKK

E
Length:51
Mass (Da):5,780
Last modified:January 23, 2007 - v2
Checksum:iC3E8FDA7C9191CA4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121Y → C in MC5DN3. 1 Publication
VAR_066211

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF052955 mRNA. Translation: AAF72736.1.
AF077045 mRNA. Translation: AAD27778.1.
AK315493 mRNA. Translation: BAG37877.1.
BT007293 mRNA. Translation: AAP35957.1.
AL109840 Genomic DNA. Translation: CAC09372.1.
CH471077 Genomic DNA. Translation: EAW75445.1.
CH471077 Genomic DNA. Translation: EAW75446.1.
BC001690 mRNA. Translation: AAH01690.1.
BC003671 mRNA. Translation: AAH03671.1.
BC105811 mRNA. Translation: AAI05812.1.
CCDSiCCDS13476.1.
RefSeqiNP_008817.1. NM_006886.3.
UniGeneiHs.177530.

Genome annotation databases

EnsembliENST00000243997; ENSP00000243997; ENSG00000124172.
ENST00000395659; ENSP00000379019; ENSG00000124172.
ENST00000395663; ENSP00000379023; ENSG00000124172.
GeneIDi514.
KEGGihsa:514.
UCSCiuc002yal.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF052955 mRNA. Translation: AAF72736.1 .
AF077045 mRNA. Translation: AAD27778.1 .
AK315493 mRNA. Translation: BAG37877.1 .
BT007293 mRNA. Translation: AAP35957.1 .
AL109840 Genomic DNA. Translation: CAC09372.1 .
CH471077 Genomic DNA. Translation: EAW75445.1 .
CH471077 Genomic DNA. Translation: EAW75446.1 .
BC001690 mRNA. Translation: AAH01690.1 .
BC003671 mRNA. Translation: AAH03671.1 .
BC105811 mRNA. Translation: AAI05812.1 .
CCDSi CCDS13476.1.
RefSeqi NP_008817.1. NM_006886.3.
UniGenei Hs.177530.

3D structure databases

ProteinModelPortali P56381.
SMRi P56381. Positions 2-48.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106999. 3 interactions.
IntActi P56381. 1 interaction.
MINTi MINT-3021407.
STRINGi 9606.ENSP00000243997.

PTM databases

PhosphoSitei P56381.

Proteomic databases

MaxQBi P56381.
PaxDbi P56381.
PRIDEi P56381.

Protocols and materials databases

DNASUi 514.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000243997 ; ENSP00000243997 ; ENSG00000124172 .
ENST00000395659 ; ENSP00000379019 ; ENSG00000124172 .
ENST00000395663 ; ENSP00000379023 ; ENSG00000124172 .
GeneIDi 514.
KEGGi hsa:514.
UCSCi uc002yal.3. human.

Organism-specific databases

CTDi 514.
GeneCardsi GC20M057600.
HGNCi HGNC:838. ATP5E.
HPAi HPA042142.
MIMi 606153. gene.
614053. phenotype.
neXtProti NX_P56381.
Orphaneti 254913. Isolated ATP synthase deficiency.
PharmGKBi PA25128.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG318665.
GeneTreei ENSGT00390000015470.
HOGENOMi HOG000214506.
HOVERGENi HBG050611.
InParanoidi P56381.
KOi K02135.
OMAi GIAWIMV.
OrthoDBi EOG7GQXZP.
PhylomeDBi P56381.
TreeFami TF300278.

Enzyme and pathway databases

Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSi ATP5E. human.
GeneWikii ATP5E.
GenomeRNAii 514.
NextBioi 2129.
PROi P56381.
SOURCEi Search...

Gene expression databases

Bgeei P56381.
CleanExi HS_ATP5E.
Genevestigatori P56381.

Family and domain databases

Gene3Di 1.10.1620.20. 1 hit.
InterProi IPR006721. ATPase_F1-cplx_esu_mt.
[Graphical view ]
Pfami PF04627. ATP-synt_Eps. 1 hit.
[Graphical view ]
SUPFAMi SSF48690. SSF48690. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization and mapping of the human ATP5E gene, identification of pseudogene ATP5EP1, and definition of the ATP5E motif."
    Tu Q., Yu L., Zhang P., Zhang M., Zhang H., Jiang J., Chen C., Zhao S.
    Biochem. J. 347:17-21(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  3. "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].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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].
    Tissue: Kidney and Skin.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Mitochondrial ATP synthase deficiency due to a mutation in the ATP5E gene for the F1 epsilon subunit."
    Mayr J.A., Havlickova V., Zimmermann F., Magler I., Kaplanova V., Jesina P., Pecinova A., Nuskova H., Koch J., Sperl W., Houstek J.
    Hum. Mol. Genet. 19:3430-3439(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MC5DN3 CYS-12.

Entry informationi

Entry nameiATP5E_HUMAN
AccessioniPrimary (citable) accession number: P56381
Secondary accession number(s): B2RDD0, E1P5H6, Q53XU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 129 of the entry and version 2 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 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3