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Protein

ATP synthase subunit epsilon-like protein, mitochondrial

Gene

ATP5EP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit epsilon-like protein, mitochondrial
Gene namesi
Name:ATP5EP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:34026. ATP5EP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi74746994.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5151ATP synthase subunit epsilon-like protein, mitochondrialPRO_0000347182Add
BLAST

Proteomic databases

PaxDbiQ5VTU8.
PRIDEiQ5VTU8.

Expressioni

Gene expression databases

BgeeiQ5VTU8.

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) (By similarity).By similarity

Protein-protein interaction databases

IntActiQ5VTU8. 3 interactions.
STRINGi9606.ENSP00000370414.

Structurei

3D structure databases

ProteinModelPortaliQ5VTU8.
SMRiQ5VTU8. Positions 2-48.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic ATPase epsilon family.Curated

Phylogenomic databases

eggNOGiNOG318665.
GeneTreeiENSGT00390000015470.
HOGENOMiHOG000214506.
HOVERGENiHBG050611.
InParanoidiQ5VTU8.
OMAiQICAKVV.
OrthoDBiEOG7GQXZP.
PhylomeDBiQ5VTU8.
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.

Q5VTU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAYWRQAGL SYIRYSQICA KVVRDALKTE FKANAKKTSG NSVKIVKVKK

E
Length:51
Mass (Da):5,807
Last modified:December 7, 2004 - v1
Checksum:i3352CE8EC90F6DCE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591024 Genomic DNA. Translation: CAH70632.1.
UniGeneiHs.574118.

Genome annotation databases

EnsembliENST00000381026; ENSP00000370414; ENSG00000180389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591024 Genomic DNA. Translation: CAH70632.1.
UniGeneiHs.574118.

3D structure databases

ProteinModelPortaliQ5VTU8.
SMRiQ5VTU8. Positions 2-48.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5VTU8. 3 interactions.
STRINGi9606.ENSP00000370414.

Polymorphism and mutation databases

DMDMi74746994.

Proteomic databases

PaxDbiQ5VTU8.
PRIDEiQ5VTU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381026; ENSP00000370414; ENSG00000180389.

Organism-specific databases

GeneCardsiGC13P028519.
HGNCiHGNC:34026. ATP5EP2.
HPAiHPA042142.
neXtProtiNX_Q5VTU8.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG318665.
GeneTreeiENSGT00390000015470.
HOGENOMiHOG000214506.
HOVERGENiHBG050611.
InParanoidiQ5VTU8.
OMAiQICAKVV.
OrthoDBiEOG7GQXZP.
PhylomeDBiQ5VTU8.
TreeFamiTF300278.

Miscellaneous databases

ChiTaRSiATP5EP2. human.
PROiQ5VTU8.

Gene expression databases

BgeeiQ5VTU8.

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.
ProtoNetiSearch...

Publicationsi

  1. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiAT5EL_HUMAN
AccessioniPrimary (citable) accession number: Q5VTU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: December 7, 2004
Last modified: June 24, 2015
This is version 84 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

Caution

Defined as a pseudogene by HGNC. However, proteomic data on a specific peptide from PubMed:17924679 suggest the existence of this protein.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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.