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P18859

- ATP5J_HUMAN

UniProt

P18859 - ATP5J_HUMAN

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Protein

ATP synthase-coupling factor 6, mitochondrial

Gene
ATP5J, ATP5A, ATPM
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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 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.

GO - Molecular functioni

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

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cellular metabolic process Source: Reactome
  3. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  4. respiratory electron transport chain Source: Reactome
  5. small molecule metabolic process Source: Reactome
  6. substantia nigra development Source: UniProt
Complete GO annotation...

Keywords - Biological processi

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-coupling factor 6, mitochondrial
Short name:
ATPase subunit F6
Gene namesi
Name:ATP5J
Synonyms:ATP5A, ATPM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:847. ATP5J.

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: UniProt
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25137.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232Mitochondrion1 PublicationAdd
BLAST
Chaini33 – 10876ATP synthase-coupling factor 6, mitochondrialPRO_0000002527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-acetyllysine1 Publication
Modified residuei46 – 461N6-acetyllysine1 Publication
Modified residuei79 – 791N6-acetyllysine By similarity
Modified residuei94 – 941N6-acetyllysine; alternate By similarity
Modified residuei94 – 941N6-succinyllysine; alternate By similarity
Modified residuei99 – 991N6-acetyllysine; alternate1 Publication
Modified residuei99 – 991N6-succinyllysine; alternate By similarity
Modified residuei105 – 1051N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP18859.
PaxDbiP18859.
PRIDEiP18859.

2D gel databases

SWISS-2DPAGEP18859.

PTM databases

PhosphoSiteiP18859.

Expressioni

Gene expression databases

ArrayExpressiP18859.
BgeeiP18859.
CleanExiHS_ATP5J.
GenevestigatoriP18859.

Organism-specific databases

HPAiHPA031069.

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.

Protein-protein interaction databases

BioGridi107006. 10 interactions.
IntActiP18859. 6 interactions.
MINTiMINT-3009016.
STRINGi9606.ENSP00000389649.

Structurei

3D structure databases

ProteinModelPortaliP18859.
SMRiP18859. Positions 36-101.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG265662.
HOGENOMiHOG000261672.
HOVERGENiHBG062261.
KOiK02131.
OMAiDMNTFPN.
PhylomeDBiP18859.
TreeFamiTF318998.

Family and domain databases

InterProiIPR008387. ATPase_F0-cplx_f6su_mt.
IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
[Graphical view]
PANTHERiPTHR12441. PTHR12441. 1 hit.
PfamiPF05511. ATP-synt_F6. 1 hit.
[Graphical view]
PIRSFiPIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
SUPFAMiSSF111357. SSF111357. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P18859-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MILQRLFRFS SVIRSAVSVH LRRNIGVTAV AFNKELDPIQ KLFVDKIREY    50
KSKRQTSGGP VDASSEYQQE LERELFKLKQ MFGNADMNTF PTFKFEDPKF 100
EVIEKPQA 108
Length:108
Mass (Da):12,588
Last modified:November 1, 1990 - v1
Checksum:iEDC1A14F01A10F17
GO
Isoform 2 (identifier: P18859-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:116
Mass (Da):13,388
Checksum:i2E376C23E0F75171
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MHCDGGISM in isoform 2. VSP_046187

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681Q → H in AAA58630. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13574.1. [P18859-1]
CCDS46637.1. [P18859-2]
PIRiJT0563.
RefSeqiNP_001003696.1. NM_001003696.1. [P18859-1]
NP_001003697.1. NM_001003697.1. [P18859-1]
NP_001003701.1. NM_001003701.1. [P18859-2]
NP_001003703.1. NM_001003703.1. [P18859-1]
NP_001676.2. NM_001685.4. [P18859-1]
XP_005261049.1. XM_005260992.2. [P18859-1]
UniGeneiHs.246310.

Genome annotation databases

EnsembliENST00000284971; 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]
GeneIDi522.
KEGGihsa:522.
UCSCiuc002yls.3. human. [P18859-1]

Polymorphism databases

DMDMi114688.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13574.1. [P18859-1 ]
CCDS46637.1. [P18859-2 ]
PIRi JT0563.
RefSeqi NP_001003696.1. NM_001003696.1. [P18859-1 ]
NP_001003697.1. NM_001003697.1. [P18859-1 ]
NP_001003701.1. NM_001003701.1. [P18859-2 ]
NP_001003703.1. NM_001003703.1. [P18859-1 ]
NP_001676.2. NM_001685.4. [P18859-1 ]
XP_005261049.1. XM_005260992.2. [P18859-1 ]
UniGenei Hs.246310.

3D structure databases

ProteinModelPortali P18859.
SMRi P18859. Positions 36-101.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107006. 10 interactions.
IntActi P18859. 6 interactions.
MINTi MINT-3009016.
STRINGi 9606.ENSP00000389649.

PTM databases

PhosphoSitei P18859.

Polymorphism databases

DMDMi 114688.

2D gel databases

SWISS-2DPAGE P18859.

Proteomic databases

MaxQBi P18859.
PaxDbi P18859.
PRIDEi P18859.

Protocols and materials databases

DNASUi 522.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000284971 ; 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 ]
GeneIDi 522.
KEGGi hsa:522.
UCSCi uc002yls.3. human. [P18859-1 ]

Organism-specific databases

CTDi 522.
GeneCardsi GC21M027088.
HGNCi HGNC:847. ATP5J.
HPAi HPA031069.
MIMi 603152. gene.
neXtProti NX_P18859.
PharmGKBi PA25137.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG265662.
HOGENOMi HOG000261672.
HOVERGENi HBG062261.
KOi K02131.
OMAi DMNTFPN.
PhylomeDBi P18859.
TreeFami TF318998.

Enzyme and pathway databases

Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

GeneWikii ATP5J.
GenomeRNAii 522.
NextBioi 2163.
PROi P18859.
SOURCEi Search...

Gene expression databases

ArrayExpressi P18859.
Bgeei P18859.
CleanExi HS_ATP5J.
Genevestigatori P18859.

Family and domain databases

InterProi IPR008387. ATPase_F0-cplx_f6su_mt.
IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
[Graphical view ]
PANTHERi PTHR12441. PTHR12441. 1 hit.
Pfami PF05511. ATP-synt_F6. 1 hit.
[Graphical view ]
PIRSFi PIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
SUPFAMi SSF111357. SSF111357. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATP5J_HUMAN
AccessioniPrimary (citable) accession number: P18859
Secondary accession number(s): J3KQ83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: September 3, 2014
This is version 147 of the entry and version 1 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 21
    Human chromosome 21: 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

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