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P24539

- AT5F1_HUMAN

UniProt

P24539 - AT5F1_HUMAN

Protein

ATP synthase F(0) complex subunit B1, mitochondrial

Gene

ATP5F1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    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.

    GO - Molecular functioni

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

    GO - Biological processi

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

    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 F(0) complex subunit B1, mitochondrial
    Alternative name(s):
    ATP synthase proton-transporting mitochondrial F(0) complex subunit B1
    ATP synthase subunit b
    Short name:
    ATPase subunit b
    Gene namesi
    Name:ATP5F1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:840. ATP5F1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. membrane Source: UniProtKB
    3. mitochondrial inner membrane Source: Reactome
    4. mitochondrial matrix Source: UniProtKB
    5. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    6. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: RefGenome
    7. mitochondrion Source: UniProt
    8. nucleus Source: UniProt

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25130.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4242MitochondrionAdd
    BLAST
    Chaini43 – 256214ATP synthase F(0) complex subunit B1, mitochondrialPRO_0000002513Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311N6-succinyllysineBy similarity
    Modified residuei139 – 1391N6-acetyllysineBy similarity
    Modified residuei154 – 1541N6-acetyllysineBy similarity
    Modified residuei162 – 1621N6-acetyllysineBy similarity
    Modified residuei221 – 2211N6-acetyllysine1 Publication
    Modified residuei233 – 2331N6-acetyllysine1 Publication
    Modified residuei244 – 2441N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP24539.
    PaxDbiP24539.
    PeptideAtlasiP24539.
    PRIDEiP24539.

    PTM databases

    PhosphoSiteiP24539.

    Expressioni

    Gene expression databases

    ArrayExpressiP24539.
    BgeeiP24539.
    CleanExiHS_ATP5F1.
    GenevestigatoriP24539.

    Organism-specific databases

    HPAiHPA046067.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. 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

    BioGridi107000. 20 interactions.
    IntActiP24539. 17 interactions.
    MINTiMINT-3010280.
    STRINGi9606.ENSP00000358737.

    Structurei

    3D structure databases

    ProteinModelPortaliP24539.
    SMRiP24539. Positions 121-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic ATPase B chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG245616.
    HOGENOMiHOG000007163.
    HOVERGENiHBG050604.
    InParanoidiP24539.
    KOiK02127.
    OMAiVINHETF.
    OrthoDBiEOG7V4B02.
    PhylomeDBiP24539.
    TreeFamiTF313250.

    Family and domain databases

    InterProiIPR008688. ATPase_B_chain/sub_B/MI25.
    IPR013837. ATPase_F0_sub_B/B_chain.
    [Graphical view]
    PANTHERiPTHR12733. PTHR12733. 1 hit.
    PfamiPF05405. Mt_ATP-synt_B. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24539-1 [UniParc]FASTAAdd to Basket

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    MLSRVVLSAA ATAAPSLKNA AFLGPGVLQA TRTFHTGQPH LVPVPPLPEY    50
    GGKVRYGLIP EEFFQFLYPK TGVTGPYVLG TGLILYALSK EIYVISAETF 100
    TALSVLGVMV YGIKKYGPFV ADFADKLNEQ KLAQLEEAKQ ASIQHIQNAI 150
    DTEKSQQALV QKRHYLFDVQ RNNIAMALEV TYRERLYRVY KEVKNRLDYH 200
    ISVQNMMRRK EQEHMINWVE KHVVQSISTQ QEKETIAKCI ADLKLLAKKA 250
    QAQPVM 256
    Length:256
    Mass (Da):28,909
    Last modified:May 2, 2002 - v2
    Checksum:i743B1C54BFFEBBBD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841I → V in CAA42782. (PubMed:1831354)Curated
    Sequence conflicti91 – 911E → G in AAH05960. (PubMed:15489334)Curated
    Sequence conflicti194 – 1941K → R in AAH05960. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti152 – 1521T → M.
    Corresponds to variant rs1264895 [ dbSNP | Ensembl ].
    VAR_033534
    Natural varianti152 – 1521T → N.
    Corresponds to variant rs1264895 [ dbSNP | Ensembl ].
    VAR_013176

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60221 mRNA. Translation: CAA42782.1.
    AL390195 Genomic DNA. Translation: CAC36042.1.
    BC005366 mRNA. Translation: AAH05366.1.
    BC005960 mRNA. Translation: AAH05960.1.
    BC016350 mRNA. Translation: AAH16350.1.
    CCDSiCCDS836.1.
    PIRiJQ1144.
    RefSeqiNP_001679.2. NM_001688.4.
    UniGeneiHs.514870.

    Genome annotation databases

    EnsembliENST00000369722; ENSP00000358737; ENSG00000116459.
    GeneIDi515.
    KEGGihsa:515.
    UCSCiuc001ebc.3. human.

    Polymorphism databases

    DMDMi20455474.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60221 mRNA. Translation: CAA42782.1 .
    AL390195 Genomic DNA. Translation: CAC36042.1 .
    BC005366 mRNA. Translation: AAH05366.1 .
    BC005960 mRNA. Translation: AAH05960.1 .
    BC016350 mRNA. Translation: AAH16350.1 .
    CCDSi CCDS836.1.
    PIRi JQ1144.
    RefSeqi NP_001679.2. NM_001688.4.
    UniGenei Hs.514870.

    3D structure databases

    ProteinModelPortali P24539.
    SMRi P24539. Positions 121-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107000. 20 interactions.
    IntActi P24539. 17 interactions.
    MINTi MINT-3010280.
    STRINGi 9606.ENSP00000358737.

    PTM databases

    PhosphoSitei P24539.

    Polymorphism databases

    DMDMi 20455474.

    Proteomic databases

    MaxQBi P24539.
    PaxDbi P24539.
    PeptideAtlasi P24539.
    PRIDEi P24539.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369722 ; ENSP00000358737 ; ENSG00000116459 .
    GeneIDi 515.
    KEGGi hsa:515.
    UCSCi uc001ebc.3. human.

    Organism-specific databases

    CTDi 515.
    GeneCardsi GC01P111991.
    HGNCi HGNC:840. ATP5F1.
    HPAi HPA046067.
    MIMi 603270. gene.
    neXtProti NX_P24539.
    PharmGKBi PA25130.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245616.
    HOGENOMi HOG000007163.
    HOVERGENi HBG050604.
    InParanoidi P24539.
    KOi K02127.
    OMAi VINHETF.
    OrthoDBi EOG7V4B02.
    PhylomeDBi P24539.
    TreeFami TF313250.

    Enzyme and pathway databases

    Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    GeneWikii ATP5F1.
    GenomeRNAii 515.
    NextBioi 2135.
    PROi P24539.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24539.
    Bgeei P24539.
    CleanExi HS_ATP5F1.
    Genevestigatori P24539.

    Family and domain databases

    InterProi IPR008688. ATPase_B_chain/sub_B/MI25.
    IPR013837. ATPase_F0_sub_B/B_chain.
    [Graphical view ]
    PANTHERi PTHR12733. PTHR12733. 1 hit.
    Pfami PF05405. Mt_ATP-synt_B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria."
      Higuti T., Tsurumi C., Osaka F., Kawamura Y., Tsujita H., Yoshihara Y., Tani I., Tanaka K., Ichirara A.
      Biochem. Biophys. Res. Commun. 178:1014-1020(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Brain.
    4. "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-221 AND LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAT5F1_HUMAN
    AccessioniPrimary (citable) accession number: P24539
    Secondary accession number(s): Q9BQ68, Q9BRU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: May 2, 2002
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3