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P56134 (ATPK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 subunit f, mitochondrial
Gene names
Name:ATP5J2
Synonyms:ATP5JL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length94 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. 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; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the ATPase F chain family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P56134-1)

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: P56134-2)

The sequence of this isoform differs from the canonical sequence as follows:
     5-10: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P56134-3)

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.
Isoform 4 (identifier: P56134-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 9493ATP synthase subunit f, mitochondrial
PRO_0000194824

Regions

Transmembrane63 – 8220Helical; Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.10
Modified residue221N6-acetyllysine By similarity

Natural variations

Alternative sequence5 – 106Missing in isoform 2 and isoform 4.
VSP_000437
Alternative sequence47 – 8640GYYRY…YKHLK → E in isoform 3 and isoform 4.
VSP_046746

Experimental info

Sequence conflict241G → L in AAH03678. Ref.8

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: D5F0D94273DEF880

FASTA9410,918
        10         20         30         40         50         60 
MASVGECPAP VPVKDKKLLE VKLGELPSWI LMRDFSPSGI FGAFQRGYYR YYNKYINVKK 

        70         80         90 
GSISGITMVL ACYVLFSYSF SYKHLKHERL RKYH 

« Hide

Isoform 2 [UniParc].

Checksum: 38072EB09CAC8D65
Show »

FASTA8810,363
Isoform 3 [UniParc].

Checksum: C19548A6E4E7BF11
Show »

FASTA556,295
Isoform 4 [UniParc].

Checksum: 3B1C513E7C1FA43F
Show »

FASTA495,741

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34692.1. [P56134-3]
CCDS47653.1. [P56134-4]
CCDS47654.1. [P56134-2]
CCDS5665.1. [P56134-1]
RefSeqNP_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]
UniGeneHs.521056.
Hs.656515.

3D structure databases

ProteinModelPortalP56134.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114923. 21 interactions.
IntActP56134. 17 interactions.
MINTMINT-1370314.
STRING9606.ENSP00000292475.

PTM databases

PhosphoSiteP56134.

Polymorphism databases

DMDM7404340.

Proteomic databases

MaxQBP56134.
PaxDbP56134.
PRIDEP56134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292475; ENSP00000292475; ENSG00000241468. [P56134-1]
ENST00000359832; ENSP00000352890; ENSG00000241468. [P56134-3]
ENST00000394186; ENSP00000377740; ENSG00000241468. [P56134-2]
ENST00000414062; ENSP00000412149; ENSG00000241468. [P56134-4]
ENST00000488775; ENSP00000418197; ENSG00000241468. [P56134-4]
GeneID9551.
KEGGhsa:9551.
UCSCuc003uql.3. human. [P56134-2]
uc003uqm.3. human. [P56134-1]

Organism-specific databases

CTD9551.
GeneCardsGC07M099046.
HGNCHGNC:848. ATP5J2.
neXtProtNX_P56134.
PharmGKBPA25138.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292892.
HOGENOMHOG000034215.
HOVERGENHBG002418.
InParanoidP56134.
KOK02130.
OrthoDBEOG73JKZ1.
PhylomeDBP56134.
TreeFamTF342865.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP56134.
BgeeP56134.
CleanExHS_ATP5J2.
GenevestigatorP56134.

Family and domain databases

InterProIPR019344. F1F0-ATPsyn_F_prd.
[Graphical view]
PANTHERPTHR13080. PTHR13080. 1 hit.
PfamPF10206. WRW. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP5J2.
GenomeRNAi9551.
NextBio35811.
PROP56134.

Entry information

Entry nameATPK_HUMAN
AccessionPrimary (citable) accession number: P56134
Secondary accession number(s): C9J8H9 expand/collapse secondary AC list , F8W7V3, O76079, Q6IBB3, Q96L83, Q9BTI8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 129 of the entry and version 3 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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM