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P56381

- ATP5E_HUMAN

UniProt

P56381 - ATP5E_HUMAN

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
  1. 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

    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

    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.
    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

    MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAEKTSG SNVKIVKVKK   50
    E 51
    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.
    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

    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 1, 2014
    This is version 128 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