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Identification
HMDB Protein ID HMDBP09207
Secondary Accession Numbers
  • 14989
Name ATP synthase subunit epsilon-like protein, mitochondrial
Synonyms Not Available
Gene Name ATP5EP2
Protein Type Enzyme
Biological Properties
General Function Involved in hydrogen ion transporting ATP synthase activity, rotational mechanism
Specific Function Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
membrane part
mitochondrial proton-transporting atp synthase complex, catalytic core f(1)
mitochondrial membrane part
Function
proton-transporting atpase activity, rotational mechanism
hydrogen ion transporting atp synthase activity, rotational mechanism
transmembrane transporter activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
hydrogen ion transmembrane transporter activity
transporter activity
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
atp synthesis coupled proton transport
atp biosynthetic process
Cellular Location
  1. Mitochondrion
  2. Mitochondrion inner membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 13q12
SNPs ATP5EP2
Gene Sequence
>156 bp
ATGGTGGCCTACTGGAGACAGGCTGGACTCAGCTACATCCGATACTCCCAGATCTGTGCA
AAAGTAGTGAGAGATGCACTGAAGACAGAATTCAAAGCAAATGCCAAAAAGACTTCTGGC
AACAGCGTAAAAATTGTGAAAGTAAAGAAGGAATAA
Protein Properties
Number of Residues 51
Molecular Weight 5806.8
Theoretical pI 10.79
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>ATP synthase subunit epsilon-like protein, mitochondrial
MVAYWRQAGLSYIRYSQICAKVVRDALKTEFKANAKKTSGNSVKIVKVKKE
GenBank ID Protein 55665865
UniProtKB/Swiss-Prot ID Q5VTU8
UniProtKB/Swiss-Prot Entry Name AT5EL_HUMAN
PDB IDs
GenBank Gene ID AL591024
GeneCard ID ATP5EP2
GenAtlas ID ATP5EP2
HGNC ID HGNC:34026
References
General References
  1. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  2. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed:15057823 ]