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P56134

- ATPK_HUMAN

UniProt

P56134 - ATPK_HUMAN

Protein

ATP synthase subunit f, mitochondrial

Gene

ATP5J2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    1. transmembrane transporter activity Source: UniProtKB

    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. proton transport Source: UniProtKB
    5. respiratory electron transport chain Source: Reactome
    6. small molecule metabolic process Source: Reactome

    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: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:848. ATP5J2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of membrane Source: UniProtKB-KW
    3. mitochondrial inner membrane Source: Reactome
    4. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    5. nucleus Source: UniProt
    6. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25138.

    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

    ArrayExpressiP56134.
    BgeeiP56134.
    CleanExiHS_ATP5J2.
    GenevestigatoriP56134.

    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. 23 interactions.
    IntActiP56134. 17 interactions.
    MINTiMINT-1370314.
    STRINGi9606.ENSP00000292475.

    Structurei

    3D structure databases

    ProteinModelPortaliP56134.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

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

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase F chain family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG292892.
    HOGENOMiHOG000034215.
    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. Align

    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

    MASVGECPAP VPVKDKKLLE VKLGELPSWI LMRDFSPSGI FGAFQRGYYR   50
    YYNKYINVKK GSISGITMVL ACYVLFSYSF SYKHLKHERL RKYH 94
    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:
    EMBL
    GenBank
    DDBJ
    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. [P56134-1]
    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]

    Polymorphism databases

    DMDMi7404340.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS34692.1. [P56134-3 ]
    CCDS47653.1. [P56134-4 ]
    CCDS47654.1. [P56134-2 ]
    CCDS5665.1. [P56134-1 ]
    RefSeqi NP_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 ]
    UniGenei Hs.521056.
    Hs.656515.

    3D structure databases

    ProteinModelPortali P56134.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114923. 23 interactions.
    IntActi P56134. 17 interactions.
    MINTi MINT-1370314.
    STRINGi 9606.ENSP00000292475.

    PTM databases

    PhosphoSitei P56134.

    Polymorphism databases

    DMDMi 7404340.

    Proteomic databases

    MaxQBi P56134.
    PaxDbi P56134.
    PRIDEi P56134.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292475 ; ENSP00000292475 ; ENSG00000241468 . [P56134-1 ]
    ENST00000359832 ; ENSP00000352890 ; ENSG00000241468 . [P56134-3 ]
    ENST00000394186 ; ENSP00000377740 ; ENSG00000241468 . [P56134-2 ]
    ENST00000414062 ; ENSP00000412149 ; ENSG00000241468 . [P56134-4 ]
    ENST00000488775 ; ENSP00000418197 ; ENSG00000241468 . [P56134-4 ]
    GeneIDi 9551.
    KEGGi hsa:9551.
    UCSCi uc003uql.3. human. [P56134-2 ]
    uc003uqm.3. human. [P56134-1 ]

    Organism-specific databases

    CTDi 9551.
    GeneCardsi GC07M099046.
    HGNCi HGNC:848. ATP5J2.
    neXtProti NX_P56134.
    PharmGKBi PA25138.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292892.
    HOGENOMi HOG000034215.
    HOVERGENi HBG002418.
    InParanoidi P56134.
    KOi K02130.
    OrthoDBi EOG73JKZ1.
    PhylomeDBi P56134.
    TreeFami TF342865.

    Enzyme and pathway databases

    Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    GeneWikii ATP5J2.
    GenomeRNAii 9551.
    NextBioi 35811.
    PROi P56134.

    Gene expression databases

    ArrayExpressi P56134.
    Bgeei P56134.
    CleanExi HS_ATP5J2.
    Genevestigatori P56134.

    Family and domain databases

    InterProi IPR019344. F1F0-ATPsyn_F_prd.
    [Graphical view ]
    PANTHERi PTHR13080. PTHR13080. 1 hit.
    Pfami PF10206. WRW. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 131 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