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P56385 (ATP5I_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit e, mitochondrial

Short name=ATPase subunit e
Gene names
Name:ATP5I
Synonyms:ATP5K
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length69 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Sequence similarities

Belongs to the ATPase e subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 6968ATP synthase subunit e, mitochondrial
PRO_0000071684

Amino acid modifications

Modified residue341N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P56385 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E4FF2B855F4535DC

FASTA697,933
        10         20         30         40         50         60 
MVPPVQVSPL IKLGRYSALF LGVAYGATRY NYLKPRAEEE RRIAAEEKKK QDELKRIARE 


LAEDDSILK 

« Hide

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50371 mRNA. Translation: BAA23322.1.
BT006922 mRNA. Translation: AAP35568.1.
BC003679 mRNA. Translation: AAH03679.1.
BC105610 mRNA. Translation: AAI05611.1.
RefSeqNP_009031.1. NM_007100.3.
UniGeneHs.85539.

3D structure databases

ProteinModelPortalP56385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107005. 9 interactions.
IntActP56385. 9 interactions.
STRING9606.ENSP00000306003.

PTM databases

PhosphoSiteP56385.

Polymorphism databases

DMDM3023369.

Proteomic databases

PaxDbP56385.
PRIDEP56385.

Protocols and materials databases

DNASU521.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304312; ENSP00000306003; ENSG00000169020.
GeneID521.
KEGGhsa:521.
UCSCuc003gas.3. human.

Organism-specific databases

CTD521.
GeneCardsGC04M000667.
HGNCHGNC:846. ATP5I.
HPAHPA035010.
MIM601519. gene.
neXtProtNX_P56385.
PharmGKBPA25136.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81326.
HOGENOMHOG000231826.
HOVERGENHBG050613.
InParanoidP56385.
KOK02129.
OMAAEANEDT.
OrthoDBEOG7MD4T1.
PhylomeDBP56385.
TreeFamTF314719.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP56385.
CleanExHS_ATP5I.
GenevestigatorP56385.

Family and domain databases

InterProIPR008386. ATPase_F0-cplx_esu_mt.
[Graphical view]
PfamPF05680. ATP-synt_E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5I. human.
GeneWikiATP5I.
GenomeRNAi521.
NextBio2159.
PROP56385.
SOURCESearch...

Entry information

Entry nameATP5I_HUMAN
AccessionPrimary (citable) accession number: P56385
Secondary accession number(s): Q0D2L9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM