P18859 (ATP5J_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase-coupling factor 6, mitochondrial
Short name=ATPase subunit F6

Gene names

Name:	ATP5J
Synonyms:	ATP5A, ATPM

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	108 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 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 process	Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
PTM	Acetylation
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: InterPro
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...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 32	32	Mitochondrion Ref.8
	Chain	33 – 108	76	ATP synthase-coupling factor 6, mitochondrial		PRO_0000002527
Amino acid modifications
	Modified residue	41	1	N6-acetyllysine Ref.9
	Modified residue	46	1	N6-acetyllysine Ref.9
	Modified residue	99	1	N6-acetyllysine Ref.9
	Modified residue	105	1	N6-acetyllysine Ref.9
Natural variations
	Alternative sequence	1	1	M → MHCDGGISM in isoform 2.		VSP_046187
Experimental info
	Sequence conflict	68	1	Q → H in AAA58630. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: EDC1A14F01A10F17	FASTA	108	12,588
	10 20 30 40 50 60 MILQRLFRFS SVIRSAVSVH LRRNIGVTAV AFNKELDPIQ KLFVDKIREY KSKRQTSGGP 70 80 90 100 VDASSEYQQE LERELFKLKQ MFGNADMNTF PTFKFEDPKF EVIEKPQA
	Isoform 2 [UniParc]. Checksum: 2E376C23E0F75171	FASTA	116	13,388
	10 20 30 40 50 60 MHCDGGISMI LQRLFRFSSV IRSAVSVHLR RNIGVTAVAF NKELDPIQKL FVDKIREYKS 70 80 90 100 110 KRQTSGGPVD ASSEYQQELE RELFKLKQMF GNADMNTFPT FKFEDPKFEV IEKPQA

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY.
[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.
IPI	IPI00002521.
PIR	JT0563.
RefSeq	NP_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.
UniGene	Hs.246310.
3D structure databases
ProteinModelPortal	P18859.
ModBase	Search...
Protein-protein interaction databases
IntAct	P18859. 4 interactions.
STRING	9606.ENSP00000389649.
PTM databases
PhosphoSite	P18859.
Polymorphism databases
DMDM	114688.
2D gel databases
SWISS-2DPAGE	P18859.
Proteomic databases
PaxDb	P18859.
PRIDE	P18859.
Protocols and materials databases
DNASU	522.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000284971; ENSP00000284971; ENSG00000154723. ENST00000400087; ENSP00000382959; ENSG00000154723. ENST00000400090; ENSP00000382962; ENSG00000154723. ENST00000400093; ENSP00000382965; ENSG00000154723. ENST00000400094; ENSP00000382966; ENSG00000154723. ENST00000457143; ENSP00000389649; ENSG00000154723.
GeneID	522.
KEGG	hsa:522.
UCSC	uc002yls.3. human.
Organism-specific databases
CTD	522.
GeneCards	GC21M027088.
HGNC	HGNC:847. ATP5J.
HPA	HPA031069.
MIM	603152. gene.
neXtProt	NX_P18859.
PharmGKB	PA25137.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG265662.
HOGENOM	HOG000261672.
HOVERGEN	HBG062261.
KO	K02131.
PhylomeDB	P18859.
Enzyme and pathway databases
Pathway_Interaction_DB	hnf3apathway. FOXA1 transcription factor network.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P18859.
Bgee	P18859.
CleanEx	HS_ATP5J.
Genevestigator	P18859.
GermOnline	ENSG00000154723. Homo sapiens.
Family and domain databases
InterPro	IPR008387. ATPase_F0-cplx_f6su_mt. IPR016349. ATPase_F0-cplx_f6su_mt_subgr. [Graphical view]
PANTHER	PTHR12441. PTHR12441. 1 hit.
Pfam	PF05511. ATP-synt_F6. 1 hit. [Graphical view]
PIRSF	PIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
SUPFAM	SSF111357. ATPase_F0_F6_mt. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	522.
NextBio	2163.
SOURCE	Search...

Entry information

Entry name

ATP5J_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 135 of the entry and version 1 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.