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P18859 (ATP5J_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase-coupling factor 6, mitochondrial

Short name=ATPase subunit F6
Gene names
Name:ATP5J
Synonyms:ATP5A, ATPM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length108 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 and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.

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 eukaryotic ATPase subunit F6 family.

Ontologies

Keywords
   Biological processHydrogen ion transport
Ion transport
Transport
   Cellular componentCF(0)
Membrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 12110673. Source: GOC

cellular metabolic process

Traceable author statement. Source: Reactome

mitochondrial ATP synthesis coupled proton transport

Inferred by curator PubMed 12110673. Source: UniProtKB

respiratory electron transport chain

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentmitochondrial inner membrane

Traceable author statement. Source: Reactome

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: InterPro

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_functionhydrogen ion transmembrane transporter activity

Inferred from electronic annotation. Source: InterPro

transmembrane transporter activity

Inferred by curator PubMed 12110673. Source: UniProtKB

transporter activity

Non-traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P18859-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P18859-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHCDGGISM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion Ref.8
Chain33 – 10876ATP synthase-coupling factor 6, mitochondrial
PRO_0000002527

Amino acid modifications

Modified residue411N6-acetyllysine Ref.9
Modified residue461N6-acetyllysine Ref.9
Modified residue791N6-acetyllysine By similarity
Modified residue941N6-acetyllysine; alternate By similarity
Modified residue941N6-succinyllysine; alternate By similarity
Modified residue991N6-acetyllysine; alternate Ref.9
Modified residue991N6-succinyllysine; alternate By similarity
Modified residue1051N6-acetyllysine Ref.9

Natural variations

Alternative sequence11M → MHCDGGISM in isoform 2.
VSP_046187

Experimental info

Sequence conflict681Q → H in AAA58630. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: EDC1A14F01A10F17

FASTA10812,588
        10         20         30         40         50         60 
MILQRLFRFS SVIRSAVSVH LRRNIGVTAV AFNKELDPIQ KLFVDKIREY KSKRQTSGGP 

        70         80         90        100 
VDASSEYQQE LERELFKLKQ MFGNADMNTF PTFKFEDPKF EVIEKPQA 

« Hide

Isoform 2 [UniParc].

Checksum: 2E376C23E0F75171
Show »

FASTA11613,388

References

« Hide 'large scale' references
[1]"Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded precursor of coupling factor 6."
Javed A.A., Ogata K., Sanadi D.R.
Gene 97:307-310(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria."
Higuti T., Tsurumi C., Kawamura Y., Tsujita H., Osaka F., Yoshihara Y., Tani I., Tanaka K., Ichihara A.
Biochem. Biophys. Res. Commun. 178:793-799(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[4]"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] (ISOFORM 1).
[5]"Identification of genes related to Parkinson's disease using expressed sequence tags."
Kim J.M., Lee K.H., Jeon Y.J., Oh J.H., Jeong S.Y., Song I.S., Kim J.M., Lee D.S., Kim N.S.
DNA Res. 13:275-286(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
Tissue: Eye.
[8]"Human liver protein map: a reference database established by microsequencing and gel comparison."
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-43.
Tissue: Liver.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-46; LYS-99 AND LYS-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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
M37104 mRNA. Translation: AAA51807.1.
M73031 mRNA. Translation: AAA58630.1.
AL110183 mRNA. Translation: CAB53667.1.
BT007244 mRNA. Translation: AAP35908.1.
DT217787 mRNA. No translation available.
AP001694 Genomic DNA. No translation available.
BC001178 mRNA. Translation: AAH01178.1.
PIRJT0563.
RefSeqNP_001003696.1. NM_001003696.1.
NP_001003697.1. NM_001003697.1.
NP_001003701.1. NM_001003701.1.
NP_001003703.1. NM_001003703.1.
NP_001676.2. NM_001685.4.
XP_005261049.1. XM_005260992.2.
UniGeneHs.246310.

3D structure databases

ProteinModelPortalP18859.
SMRP18859. Positions 36-101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107006. 10 interactions.
IntActP18859. 6 interactions.
MINTMINT-3009016.
STRING9606.ENSP00000389649.

PTM databases

PhosphoSiteP18859.

Polymorphism databases

DMDM114688.

2D gel databases

SWISS-2DPAGEP18859.

Proteomic databases

PaxDbP18859.
PRIDEP18859.

Protocols and materials databases

DNASU522.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284971; ENSP00000284971; ENSG00000154723. [P18859-1]
ENST00000400087; ENSP00000382959; ENSG00000154723. [P18859-1]
ENST00000400090; ENSP00000382962; ENSG00000154723. [P18859-1]
ENST00000400093; ENSP00000382965; ENSG00000154723. [P18859-1]
ENST00000400094; ENSP00000382966; ENSG00000154723. [P18859-1]
ENST00000457143; ENSP00000389649; ENSG00000154723. [P18859-2]
GeneID522.
KEGGhsa:522.
UCSCuc002yls.3. human. [P18859-1]

Organism-specific databases

CTD522.
GeneCardsGC21M027088.
HGNCHGNC:847. ATP5J.
HPAHPA031069.
MIM603152. gene.
neXtProtNX_P18859.
PharmGKBPA25137.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265662.
HOGENOMHOG000261672.
HOVERGENHBG062261.
KOK02131.
OMADMNTFPN.
PhylomeDBP18859.
TreeFamTF318998.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP18859.
BgeeP18859.
CleanExHS_ATP5J.
GenevestigatorP18859.

Family and domain databases

InterProIPR008387. ATPase_F0-cplx_f6su_mt.
IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
[Graphical view]
PANTHERPTHR12441. PTHR12441. 1 hit.
PfamPF05511. ATP-synt_F6. 1 hit.
[Graphical view]
PIRSFPIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
SUPFAMSSF111357. SSF111357. 1 hit.
ProtoNetSearch...

Other

GeneWikiATP5J.
GenomeRNAi522.
NextBio2163.
PROP18859.
SOURCESearch...

Entry information

Entry nameATP5J_HUMAN
AccessionPrimary (citable) accession number: P18859
Secondary accession number(s): J3KQ83
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 144 of the entry and version 1 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 21

Human chromosome 21: entries, gene names and cross-references to MIM