P56385 (ATP5I_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit e, mitochondrial
Short name=ATPase subunit e

Gene names

Name:	ATP5I
Synonyms:	ATP5K

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	69 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay PubMed 12110673. Source: GOC mitochondrial ATP synthesis coupled proton transport Inferred by curator PubMed 12110673. Source: UniProtKB respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular_component	mitochondrial proton-transporting ATP synthase complex Inferred from direct assay PubMed 12110673. Source: UniProtKB mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: Compara
Molecular_function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro transmembrane transporter activity Inferred by curator PubMed 12110673. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 69	68	ATP synthase subunit e, mitochondrial		PRO_0000071684
Amino acid modifications
	Modified residue	32	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56385 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E4FF2B855F4535DC	FASTA	69	7,933
	10 20 30 40 50 60 MVPPVQVSPL IKLGRYSALF LGVAYGATRY NYLKPRAEEE RRIAAEEKKK QDELKRIARE LAEDDSILK

References

	« Hide 'large scale' referencesShow '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].
+	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.
IPI	IPI00218848.
RefSeq	NP_009031.1. NM_007100.3.
UniGene	Hs.85539.
3D structure databases
ProteinModelPortal	P56385.
ModBase	Search...
Protein-protein interaction databases
IntAct	P56385. 9 interactions.
STRING	9606.ENSP00000306003.
PTM databases
PhosphoSite	P56385.
Polymorphism databases
DMDM	3023369.
Proteomic databases
PaxDb	P56385.
PRIDE	P56385.
Protocols and materials databases
DNASU	521.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304312; ENSP00000306003; ENSG00000169020.
GeneID	521.
KEGG	hsa:521.
UCSC	uc003gas.3. human.
Organism-specific databases
CTD	521.
GeneCards	GC04M000667.
HGNC	HGNC:846. ATP5I.
HPA	HPA035010.
MIM	601519. gene.
neXtProt	NX_P56385.
PharmGKB	PA25136.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG81326.
HOGENOM	HOG000231826.
HOVERGEN	HBG050613.
InParanoid	P56385.
KO	K02129.
OMA	AEANEDT.
OrthoDB	EOG45758D.
PhylomeDB	P56385.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	P56385.
CleanEx	HS_ATP5I.
Genevestigator	P56385.
GermOnline	ENSG00000169020. Homo sapiens.
Family and domain databases
InterPro	IPR008386. ATPase_F0-cplx_esu_mt. [Graphical view]
Pfam	PF05680. ATP-synt_E. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5I. human.
GenomeRNAi	521.
NextBio	2159.
SOURCE	Search...

Entry information

Entry name

ATP5I_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.