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P56135

- ATPK_MOUSE

UniProt

P56135 - ATPK_MOUSE

Protein

ATP synthase subunit f, mitochondrial

Gene

Atp5j2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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. ATPase activity Source: Ensembl

    GO - Biological processi

    1. ATP biosynthetic process Source: UniProtKB-KW
    2. proton transport Source: UniProtKB-KW

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit f, mitochondrial
    Gene namesi
    Name:Atp5j2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1927558. Atp5j2.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: MGI
    3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    4. mitochondrion Source: MGI
    5. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 8887ATP synthase subunit f, mitochondrialPRO_0000194825Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei16 – 161N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP56135.
    PRIDEiP56135.

    PTM databases

    PhosphoSiteiP56135.

    Expressioni

    Gene expression databases

    ArrayExpressiP56135.
    BgeeiP56135.
    GenevestigatoriP56135.

    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

    BioGridi208283. 1 interaction.
    IntActiP56135. 2 interactions.
    MINTiMINT-1843047.

    Structurei

    3D structure databases

    ProteinModelPortaliP56135.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei57 – 7620HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase F chain family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG292892.
    GeneTreeiENSGT00510000046986.
    HOGENOMiHOG000034215.
    HOVERGENiHBG002418.
    InParanoidiP56135.
    KOiK02130.
    OMAiYLWEYDH.
    OrthoDBiEOG73JKZ1.
    PhylomeDBiP56135.
    TreeFamiTF342865.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    P56135-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASLVPLKEK KLMEVKLGEL PSWIMMRDFT PSGIAGAFRR GYDRYYNKYI   50
    NVRKGSISGI SMVLAAYVVF SYCISYKELK HERRRKYH 88
    Length:88
    Mass (Da):10,344
    Last modified:January 23, 2007 - v3
    Checksum:i89526C72EC436E48
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB030192 mRNA. Translation: BAA92756.1.
    AK002519 mRNA. Translation: BAB22157.1.
    AK003235 mRNA. Translation: BAB22660.1.
    AK003817 mRNA. Translation: BAB23014.1.
    AK013130 mRNA. Translation: BAB28667.1.
    AK151737 mRNA. Translation: BAE30651.1.
    AK168095 mRNA. Translation: BAE40067.1.
    BC029226 mRNA. Translation: AAH29226.1.
    CCDSiCCDS39385.1.
    RefSeqiNP_065607.1. NM_020582.2.
    UniGeneiMm.133551.

    Genome annotation databases

    EnsembliENSMUST00000161741; ENSMUSP00000125504; ENSMUSG00000038690.
    GeneIDi57423.
    KEGGimmu:57423.
    UCSCiuc009amk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB030192 mRNA. Translation: BAA92756.1 .
    AK002519 mRNA. Translation: BAB22157.1 .
    AK003235 mRNA. Translation: BAB22660.1 .
    AK003817 mRNA. Translation: BAB23014.1 .
    AK013130 mRNA. Translation: BAB28667.1 .
    AK151737 mRNA. Translation: BAE30651.1 .
    AK168095 mRNA. Translation: BAE40067.1 .
    BC029226 mRNA. Translation: AAH29226.1 .
    CCDSi CCDS39385.1.
    RefSeqi NP_065607.1. NM_020582.2.
    UniGenei Mm.133551.

    3D structure databases

    ProteinModelPortali P56135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208283. 1 interaction.
    IntActi P56135. 2 interactions.
    MINTi MINT-1843047.

    PTM databases

    PhosphoSitei P56135.

    Proteomic databases

    PaxDbi P56135.
    PRIDEi P56135.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000161741 ; ENSMUSP00000125504 ; ENSMUSG00000038690 .
    GeneIDi 57423.
    KEGGi mmu:57423.
    UCSCi uc009amk.1. mouse.

    Organism-specific databases

    CTDi 9551.
    MGIi MGI:1927558. Atp5j2.

    Phylogenomic databases

    eggNOGi NOG292892.
    GeneTreei ENSGT00510000046986.
    HOGENOMi HOG000034215.
    HOVERGENi HBG002418.
    InParanoidi P56135.
    KOi K02130.
    OMAi YLWEYDH.
    OrthoDBi EOG73JKZ1.
    PhylomeDBi P56135.
    TreeFami TF342865.

    Miscellaneous databases

    ChiTaRSi ATP5J2. mouse.
    NextBioi 313776.
    PROi P56135.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56135.
    Bgeei P56135.
    Genevestigatori P56135.

    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. "Growth suppression of Escherichia coli by induction of expression of mammalian genes with transmembrane or ATPase domains."
      Inoue S., Sano H., Ohta M.
      Biochem. Biophys. Res. Commun. 268:553-561(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and DBA/2.
      Tissue: Bone marrow, Embryo and Kidney.
    3. "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].
      Strain: Czech II.
      Tissue: Mammary gland.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 17-39, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiATPK_MOUSE
    AccessioniPrimary (citable) accession number: P56135
    Secondary accession number(s): Q3THX9, Q9JMF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 98 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3