ATP synthase subunit e, mitochondrial

NameATP synthase subunit e, mitochondrial
Synonyms
  • ATP5K
  • ATPase subunit e
Gene NameATP5I
OrganismHuman
Amino acid sequence
>lcl|BSEQ0049755|ATP synthase subunit e, mitochondrial
MVPPVQVSPLIKLGRYSALFLGVAYGATRYNYLKPRAEEERRIAAEEKKKQDELKRIARE
LAEDDSILK
Number of residuesNone
Molecular Weight7933.11
Theoretical pINone
GO Classification
Functions
  • hydrogen ion transmembrane transporter activity
  • transmembrane transporter activity
Processes
  • ATP biosynthetic process
  • mitochondrial ATP synthesis coupled proton transport
Components
  • mitochondrion
  • mitochondrial inner membrane
  • mitochondrial proton-transporting ATP synthase complex
  • mitochondrial proton-transporting ATP synthase complex, coupling factor F(o)
General FunctionMitochondrial 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(0) domain. Minor subunit located with subunit a in the membrane.
Specific FunctionHydrogen ion transmembrane transporter activity
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP56385
UniProtKB Entry Name
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0049756|ATP synthase subunit e, mitochondrial (ATP5I)
ATGGTGCCACCGGTGCAGGTCTCTCCGCTCATCAAGCTCGGCCGCTACTCCGCCCTGTTC
CTCGGTGTGGCCTACGGAGCCACGCGCTACAATTACCTAAAACCTCGGGCAGAAGAGGAG
AGGAGGATAGCAGCAGAAGAGAAGAAGAAGCAGGATGAACTGAAACGGATTGCCAGAGAA
TTGGCAGAAGATGACAGCATATTAAAGTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome Location4
Locus4p16.3
References
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  3. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [21269460 ]
  4. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [22814378 ]
  5. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [24275569 ]
  6. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [25944712 ]

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