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Protein

ATP synthase subunit e, mitochondrial

Gene

ATP5I

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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 F0 domain. Minor subunit located with subunit a in the membrane.

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro
  2. transmembrane transporter activity Source: UniProtKB

GO - Biological processi

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

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 e, mitochondrial
Short name:
ATPase subunit e
Gene namesi
Name:ATP5I
Synonyms:ATP5K
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:846. ATP5I.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  3. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: InterPro
  4. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25136.

Polymorphism and mutation databases

BioMutaiATP5I.
DMDMi3023369.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 6968ATP synthase subunit e, mitochondrialPRO_0000071684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP56385.
PaxDbiP56385.
PRIDEiP56385.

PTM databases

PhosphoSiteiP56385.

Expressioni

Gene expression databases

BgeeiP56385.
CleanExiHS_ATP5I.
GenevestigatoriP56385.

Organism-specific databases

HPAiHPA035010.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. 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

BioGridi107005. 13 interactions.
IntActiP56385. 10 interactions.
STRINGi9606.ENSP00000306003.

Structurei

3D structure databases

ProteinModelPortaliP56385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase e subunit family.Curated

Phylogenomic databases

eggNOGiNOG81326.
GeneTreeiENSGT00390000005102.
HOGENOMiHOG000231826.
HOVERGENiHBG050613.
InParanoidiP56385.
KOiK02129.
OMAiMVPPVEV.
OrthoDBiEOG7MD4T1.
PhylomeDBiP56385.
TreeFamiTF314719.

Family and domain databases

InterProiIPR008386. ATPase_F0-cplx_esu_mt.
[Graphical view]
PfamiPF05680. ATP-synt_E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P56385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPPVQVSPL IKLGRYSALF LGVAYGATRY NYLKPRAEEE RRIAAEEKKK
60
QDELKRIARE LAEDDSILK
Length:69
Mass (Da):7,933
Last modified:January 23, 2007 - v2
Checksum:iE4FF2B855F4535DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50371 mRNA. Translation: BAA23322.1.
BT006922 mRNA. Translation: AAP35568.1.
BC003679 mRNA. Translation: AAH03679.1.
BC105610 mRNA. Translation: AAI05611.1.
CCDSiCCDS3337.1.
RefSeqiNP_009031.1. NM_007100.3.
UniGeneiHs.85539.

Genome annotation databases

EnsembliENST00000304312; ENSP00000306003; ENSG00000169020.
GeneIDi521.
KEGGihsa:521.
UCSCiuc003gas.3. human.

Polymorphism and mutation databases

BioMutaiATP5I.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50371 mRNA. Translation: BAA23322.1.
BT006922 mRNA. Translation: AAP35568.1.
BC003679 mRNA. Translation: AAH03679.1.
BC105610 mRNA. Translation: AAI05611.1.
CCDSiCCDS3337.1.
RefSeqiNP_009031.1. NM_007100.3.
UniGeneiHs.85539.

3D structure databases

ProteinModelPortaliP56385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107005. 13 interactions.
IntActiP56385. 10 interactions.
STRINGi9606.ENSP00000306003.

PTM databases

PhosphoSiteiP56385.

Polymorphism and mutation databases

BioMutaiATP5I.
DMDMi3023369.

Proteomic databases

MaxQBiP56385.
PaxDbiP56385.
PRIDEiP56385.

Protocols and materials databases

DNASUi521.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304312; ENSP00000306003; ENSG00000169020.
GeneIDi521.
KEGGihsa:521.
UCSCiuc003gas.3. human.

Organism-specific databases

CTDi521.
GeneCardsiGC04M000667.
HGNCiHGNC:846. ATP5I.
HPAiHPA035010.
MIMi601519. gene.
neXtProtiNX_P56385.
PharmGKBiPA25136.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG81326.
GeneTreeiENSGT00390000005102.
HOGENOMiHOG000231826.
HOVERGENiHBG050613.
InParanoidiP56385.
KOiK02129.
OMAiMVPPVEV.
OrthoDBiEOG7MD4T1.
PhylomeDBiP56385.
TreeFamiTF314719.

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiATP5I. human.
GeneWikiiATP5I.
GenomeRNAii521.
NextBioi2159.
PROiP56385.
SOURCEiSearch...

Gene expression databases

BgeeiP56385.
CleanExiHS_ATP5I.
GenevestigatoriP56385.

Family and domain databases

InterProiIPR008386. ATPase_F0-cplx_esu_mt.
[Graphical view]
PfamiPF05680. ATP-synt_E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a human homolog of rat ATP synthase subunit e from human fetal brain."
    Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S., Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M., Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  2. "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].
  3. "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.
  4. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
    Xu G., Shin S.B., Jaffrey S.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-16.
    Tissue: Leukemic T-cell.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATP5I_HUMAN
AccessioniPrimary (citable) accession number: P56385
Secondary accession number(s): Q0D2L9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 126 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.