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Protein

ATP synthase subunit f, mitochondrial

Gene

ATP5J2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Minor subunit located with subunit a in the membrane.

GO - Molecular functioni

  • transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  • cellular metabolic process Source: Reactome
  • mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  • proton transport Source: UniProtKB
  • respiratory electron transport chain Source: Reactome
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, 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 subunit f, mitochondrial
Gene namesi
Name:ATP5J2
Synonyms:ATP5JL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:848. ATP5J2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei63 – 8220HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: Reactome
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25138.

Polymorphism and mutation databases

BioMutaiATP5J2.
DMDMi7404340.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 9493ATP synthase subunit f, mitochondrialPRO_0000194824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei22 – 221N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP56134.
PaxDbiP56134.
PRIDEiP56134.

PTM databases

PhosphoSiteiP56134.

Expressioni

Gene expression databases

BgeeiP56134.
CleanExiHS_ATP5J2.
ExpressionAtlasiP56134. baseline and differential.
GenevisibleiP56134. HS.

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).By similarity

Protein-protein interaction databases

BioGridi114923. 21 interactions.
IntActiP56134. 18 interactions.
MINTiMINT-1370314.
STRINGi9606.ENSP00000292475.

Structurei

3D structure databases

ProteinModelPortaliP56134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase F chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292892.
GeneTreeiENSGT00510000046986.
HOGENOMiHOG000293164.
HOVERGENiHBG002418.
InParanoidiP56134.
KOiK02130.
OrthoDBiEOG73JKZ1.
PhylomeDBiP56134.
TreeFamiTF342865.

Family and domain databases

InterProiIPR019344. F1F0-ATPsyn_F_prd.
[Graphical view]
PANTHERiPTHR13080. PTHR13080. 1 hit.
PfamiPF10206. WRW. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P56134-1) [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

        10         20         30         40         50
MASVGECPAP VPVKDKKLLE VKLGELPSWI LMRDFSPSGI FGAFQRGYYR
60 70 80 90
YYNKYINVKK GSISGITMVL ACYVLFSYSF SYKHLKHERL RKYH
Length:94
Mass (Da):10,918
Last modified:January 23, 2007 - v3
Checksum:iD5F0D94273DEF880
GO
Isoform 2 (identifier: P56134-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     5-10: Missing.

Note: No experimental confirmation available.
Show »
Length:88
Mass (Da):10,363
Checksum:i38072EB09CAC8D65
GO
Isoform 3 (identifier: P56134-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     47-86: GYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLK → E

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:55
Mass (Da):6,295
Checksum:iC19548A6E4E7BF11
GO
Isoform 4 (identifier: P56134-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     5-10: Missing.
     47-86: GYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLK → E

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:49
Mass (Da):5,741
Checksum:i3B1C513E7C1FA43F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241G → L in AAH03678 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei5 – 106Missing in isoform 2 and isoform 4. 1 PublicationVSP_000437
Alternative sequencei47 – 8640GYYRY…YKHLK → E in isoform 3 and isoform 4. CuratedVSP_046746Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088918 mRNA. Translation: AAC34895.1.
AF047436 mRNA. Translation: AAC39887.1.
AY046911 mRNA. Translation: AAL06647.1.
CR456891 mRNA. Translation: CAG33172.1.
CR542155 mRNA. Translation: CAG46952.1.
AC073063 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23877.1.
CH471091 Genomic DNA. Translation: EAW76661.1.
BC003678 mRNA. Translation: AAH03678.1.
CCDSiCCDS34692.1. [P56134-3]
CCDS47653.1. [P56134-4]
CCDS47654.1. [P56134-2]
CCDS5665.1. [P56134-1]
RefSeqiNP_001003713.1. NM_001003713.2. [P56134-2]
NP_001003714.1. NM_001003714.2. [P56134-3]
NP_001034267.1. NM_001039178.2. [P56134-4]
NP_004880.1. NM_004889.3. [P56134-1]
UniGeneiHs.521056.
Hs.656515.

Genome annotation databases

EnsembliENST00000292475; ENSP00000292475; ENSG00000241468.
ENST00000359832; ENSP00000352890; ENSG00000241468. [P56134-3]
ENST00000394186; ENSP00000377740; ENSG00000241468. [P56134-2]
ENST00000414062; ENSP00000412149; ENSG00000241468. [P56134-4]
ENST00000488775; ENSP00000418197; ENSG00000241468. [P56134-4]
GeneIDi9551.
KEGGihsa:9551.
UCSCiuc003uql.3. human. [P56134-2]
uc003uqm.3. human. [P56134-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088918 mRNA. Translation: AAC34895.1.
AF047436 mRNA. Translation: AAC39887.1.
AY046911 mRNA. Translation: AAL06647.1.
CR456891 mRNA. Translation: CAG33172.1.
CR542155 mRNA. Translation: CAG46952.1.
AC073063 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23877.1.
CH471091 Genomic DNA. Translation: EAW76661.1.
BC003678 mRNA. Translation: AAH03678.1.
CCDSiCCDS34692.1. [P56134-3]
CCDS47653.1. [P56134-4]
CCDS47654.1. [P56134-2]
CCDS5665.1. [P56134-1]
RefSeqiNP_001003713.1. NM_001003713.2. [P56134-2]
NP_001003714.1. NM_001003714.2. [P56134-3]
NP_001034267.1. NM_001039178.2. [P56134-4]
NP_004880.1. NM_004889.3. [P56134-1]
UniGeneiHs.521056.
Hs.656515.

3D structure databases

ProteinModelPortaliP56134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114923. 21 interactions.
IntActiP56134. 18 interactions.
MINTiMINT-1370314.
STRINGi9606.ENSP00000292475.

PTM databases

PhosphoSiteiP56134.

Polymorphism and mutation databases

BioMutaiATP5J2.
DMDMi7404340.

Proteomic databases

MaxQBiP56134.
PaxDbiP56134.
PRIDEiP56134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000292475; ENSP00000292475; ENSG00000241468.
ENST00000359832; ENSP00000352890; ENSG00000241468. [P56134-3]
ENST00000394186; ENSP00000377740; ENSG00000241468. [P56134-2]
ENST00000414062; ENSP00000412149; ENSG00000241468. [P56134-4]
ENST00000488775; ENSP00000418197; ENSG00000241468. [P56134-4]
GeneIDi9551.
KEGGihsa:9551.
UCSCiuc003uql.3. human. [P56134-2]
uc003uqm.3. human. [P56134-1]

Organism-specific databases

CTDi9551.
GeneCardsiGC07M099046.
HGNCiHGNC:848. ATP5J2.
neXtProtiNX_P56134.
PharmGKBiPA25138.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG292892.
GeneTreeiENSGT00510000046986.
HOGENOMiHOG000293164.
HOVERGENiHBG002418.
InParanoidiP56134.
KOiK02130.
OrthoDBiEOG73JKZ1.
PhylomeDBiP56134.
TreeFamiTF342865.

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

GeneWikiiATP5J2.
GenomeRNAii9551.
NextBioi35811.
PROiP56134.

Gene expression databases

BgeeiP56134.
CleanExiHS_ATP5J2.
ExpressionAtlasiP56134. baseline and differential.
GenevisibleiP56134. HS.

Family and domain databases

InterProiIPR019344. F1F0-ATPsyn_F_prd.
[Graphical view]
PANTHERiPTHR13080. PTHR13080. 1 hit.
PfamiPF10206. WRW. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, and chromosomal localization of a human F1F0-type ATPase subunit f."
    Lee H.C., Kang Y.J., Park D.S., Lee C.M., Cho W.K., Ahn H.J., Lee M.Y., Hwang M.Y., Jin S.W., Sohn U.I.K.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Thymus.
  2. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
    Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
    Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  3. "F1Fo-ATP synthase complex Fo membrane domain f subunit of Homo sapiens."
    Guo J.H., Yu L., Dai F.Y., She X.Y.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Kidney.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATPK_HUMAN
AccessioniPrimary (citable) accession number: P56134
Secondary accession number(s): C9J8H9
, F8W7V3, O76079, Q6IBB3, Q96L83, Q9BTI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 139 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.