Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00829

- ATPB_BOVIN

UniProt

P00829 - ATPB_BOVIN

Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP5B

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Jan 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

    Catalytic activityi

    ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi206 – 2138ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. proton-transporting ATPase activity, rotational mechanism Source: Ensembl
    4. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. ATP catabolic process Source: UniProtKB
    3. ATP hydrolysis coupled proton transport Source: InterPro
    4. ATP synthesis coupled proton transport Source: InterPro
    5. lipid metabolic process Source: Ensembl
    6. negative regulation of cell adhesion involved in substrate-bound cell migration Source: Ensembl
    7. regulation of intracellular pH Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_212639. Formation of ATP by chemiosmotic coupling.
    REACT_214581. Transcriptional activation of mitochondrial biogenesis.
    REACT_215731. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
    Gene namesi
    Name:ATP5B
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 5

    Subcellular locationi

    Mitochondrion. Mitochondrion inner membrane
    Note: Peripheral membrane protein.

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. mitochondrial nucleoid Source: Ensembl
    3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    4. plasma membrane Source: Ensembl
    5. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW

    Keywords - Cellular componenti

    CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4848Mitochondrion2 PublicationsAdd
    BLAST
    Chaini49 – 528480ATP synthase subunit beta, mitochondrialPRO_0000002442Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi106 – 1061O-linked (GlcNAc)By similarity
    Modified residuei124 – 1241N6-acetyllysine; alternateBy similarity
    Modified residuei124 – 1241N6-succinyllysine; alternateBy similarity
    Modified residuei161 – 1611N6-acetyllysine; alternateBy similarity
    Modified residuei161 – 1611N6-succinyllysine; alternateBy similarity
    Modified residuei198 – 1981N6-acetyllysineBy similarity
    Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
    Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
    Modified residuei264 – 2641N6-acetyllysine; alternateBy similarity
    Modified residuei264 – 2641N6-succinyllysine; alternateBy similarity
    Modified residuei426 – 4261N6-acetyllysineBy similarity
    Modified residuei480 – 4801N6-acetyllysineBy similarity
    Modified residuei485 – 4851N6-acetyllysineBy similarity
    Modified residuei522 – 5221N6-acetyllysine; alternateBy similarity
    Modified residuei522 – 5221N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    PaxDbiP00829.
    PRIDEiP00829.

    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. Interacts with PPIF. Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficency.4 Publications

    Protein-protein interaction databases

    DIPiDIP-35476N.
    IntActiP00829. 5 interactions.
    MINTiMINT-5006882.

    Structurei

    Secondary structure

    1
    528
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi60 – 678
    Beta strandi70 – 778
    Beta strandi85 – 906
    Beta strandi96 – 1049
    Beta strandi107 – 1148
    Beta strandi124 – 1274
    Beta strandi129 – 1313
    Beta strandi133 – 1353
    Helixi138 – 1403
    Beta strandi147 – 1493
    Beta strandi153 – 1553
    Beta strandi163 – 1664
    Helixi173 – 1753
    Helixi188 – 1936
    Beta strandi201 – 2066
    Beta strandi208 – 2114
    Helixi212 – 22312
    Turni224 – 2263
    Beta strandi228 – 23710
    Helixi240 – 25213
    Beta strandi254 – 2563
    Beta strandi258 – 2614
    Beta strandi265 – 2706
    Helixi276 – 29520
    Beta strandi297 – 2993
    Beta strandi301 – 3066
    Helixi309 – 31911
    Helixi320 – 3223
    Helixi328 – 3303
    Helixi335 – 3439
    Beta strandi346 – 3483
    Beta strandi349 – 3513
    Beta strandi354 – 3618
    Helixi363 – 3653
    Helixi370 – 3756
    Helixi376 – 3783
    Beta strandi380 – 3856
    Helixi387 – 3904
    Turni391 – 3933
    Turni400 – 4023
    Beta strandi404 – 4074
    Helixi410 – 4134
    Helixi415 – 44127
    Helixi443 – 4453
    Helixi448 – 46417
    Helixi469 – 4713
    Helixi472 – 4754
    Helixi484 – 49512
    Turni496 – 5016
    Helixi504 – 5074
    Helixi513 – 52412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BMFX-ray2.85D/E/F47-528[»]
    1COWX-ray3.10D/E/F47-528[»]
    1E1QX-ray2.61D/E/F47-528[»]
    1E1RX-ray2.50D/E/F47-528[»]
    1E79X-ray2.40D/E/F47-528[»]
    1EFRX-ray3.10D/E/F47-528[»]
    1H8EX-ray2.00D/E/F47-528[»]
    1H8HX-ray2.90D/E/F47-528[»]
    1NBMX-ray3.00D/E/F47-526[»]
    1OHHX-ray2.80D/E/F47-528[»]
    1QO1X-ray3.90D/E/F47-525[»]
    1W0JX-ray2.20D/E/F47-528[»]
    1W0KX-ray2.85D/E/F47-528[»]
    2CK3X-ray1.90D/E/F47-528[»]
    2JDIX-ray1.90D/E/F47-528[»]
    2JIZX-ray2.30D/E/F/K/L/M47-528[»]
    2JJ1X-ray2.70D/E/F/K/L/M47-528[»]
    2JJ2X-ray2.40D/E/F/K/L/M47-528[»]
    2V7QX-ray2.10D/E/F47-528[»]
    2W6EX-ray6.50D/E/F1-528[»]
    2W6FX-ray6.00D/E/F1-528[»]
    2W6GX-ray6.00D/E/F1-528[»]
    2W6HX-ray5.00D/E/F1-528[»]
    2W6IX-ray4.00D/E/F1-528[»]
    2W6JX-ray3.84D/E/F1-528[»]
    2WSSX-ray3.20D/E/F/M/N/O47-528[»]
    2XNDX-ray3.50D/E/F59-525[»]
    4ASUX-ray2.60D/E/F49-528[»]
    ProteinModelPortaliP00829.
    SMRiP00829. Positions 59-527.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00829.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0055.
    GeneTreeiENSGT00550000074800.
    HOGENOMiHOG000009605.
    HOVERGENiHBG004307.
    InParanoidiP00829.
    KOiK02133.
    OMAiNPAGQDV.
    OrthoDBiEOG73V6K6.
    TreeFamiTF105640.

    Family and domain databases

    Gene3Di1.10.1140.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01347. ATP_synth_beta_bact.
    InterProiIPR003593. AAA+_ATPase.
    IPR020003. ATPase_a/bsu_AS.
    IPR005722. ATPase_F1-cplx_bsu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR024034. ATPase_F1_bsu/V1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01039. atpD. 1 hit.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00829-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGLVGRVVA ASASGALRGL SPSAPLPQAQ LLLRAAPAAL QPARDYAAQA    50
    SPSPKAGATT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA 100
    QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIRIPVGPET LGRIMNVIGE 150
    PIDERGPIKT KQFAAIHAEA PEFVEMSVEQ EILVTGIKVV DLLAPYAKGG 200
    KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM 250
    IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 300
    VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK 350
    KGSITSVQAI YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP 400
    LDSTSRIMDP NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED 450
    KLTVSRARKI QRFLSQPFQV AEVFTGHLGK LVPLKETIKG FQQILAGEYD 500
    HLPEQAFYMV GPIEEAVAKA DKLAEEHS 528
    Length:528
    Mass (Da):56,284
    Last modified:January 1, 1990 - v2
    Checksum:i32218D14A5497F18
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti182 – 1821I → L AA sequence (PubMed:6298222)Curated
    Sequence conflicti182 – 1821I → L AA sequence (PubMed:2864455)Curated
    Sequence conflicti187 – 1871I → D AA sequence (PubMed:6298222)Curated
    Sequence conflicti187 – 1871I → D AA sequence (PubMed:2864455)Curated
    Sequence conflicti196 – 1961Y → I in CAA29094. (PubMed:2896550)Curated
    Sequence conflicti215 – 2151L → F AA sequence (PubMed:6298222)Curated
    Sequence conflicti215 – 2151L → F AA sequence (PubMed:2864455)Curated
    Sequence conflicti274 – 2741E → Q AA sequence (PubMed:6298222)Curated
    Sequence conflicti274 – 2741E → Q AA sequence (PubMed:2864455)Curated
    Sequence conflicti338 – 3381D → N AA sequence (PubMed:6298222)Curated
    Sequence conflicti338 – 3381D → N AA sequence (PubMed:2864455)Curated
    Sequence conflicti374 – 3741T → V AA sequence (PubMed:6298222)Curated
    Sequence conflicti374 – 3741T → V AA sequence (PubMed:2864455)Curated
    Sequence conflicti409 – 4091D → N AA sequence (PubMed:6298222)Curated
    Sequence conflicti409 – 4091D → N AA sequence (PubMed:2864455)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 502Missing in some mature chains.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20929 mRNA. Translation: AAA30395.1.
    BC116099 mRNA. Translation: AAI16100.1.
    X05605 mRNA. Translation: CAA29094.1.
    PIRiA28717. PWBOB.
    RefSeqiNP_786990.1. NM_175796.3.
    UniGeneiBt.4431.

    Genome annotation databases

    EnsembliENSBTAT00000017710; ENSBTAP00000017710; ENSBTAG00000013315.
    GeneIDi327675.
    KEGGibta:327675.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20929 mRNA. Translation: AAA30395.1 .
    BC116099 mRNA. Translation: AAI16100.1 .
    X05605 mRNA. Translation: CAA29094.1 .
    PIRi A28717. PWBOB.
    RefSeqi NP_786990.1. NM_175796.3.
    UniGenei Bt.4431.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BMF X-ray 2.85 D/E/F 47-528 [» ]
    1COW X-ray 3.10 D/E/F 47-528 [» ]
    1E1Q X-ray 2.61 D/E/F 47-528 [» ]
    1E1R X-ray 2.50 D/E/F 47-528 [» ]
    1E79 X-ray 2.40 D/E/F 47-528 [» ]
    1EFR X-ray 3.10 D/E/F 47-528 [» ]
    1H8E X-ray 2.00 D/E/F 47-528 [» ]
    1H8H X-ray 2.90 D/E/F 47-528 [» ]
    1NBM X-ray 3.00 D/E/F 47-526 [» ]
    1OHH X-ray 2.80 D/E/F 47-528 [» ]
    1QO1 X-ray 3.90 D/E/F 47-525 [» ]
    1W0J X-ray 2.20 D/E/F 47-528 [» ]
    1W0K X-ray 2.85 D/E/F 47-528 [» ]
    2CK3 X-ray 1.90 D/E/F 47-528 [» ]
    2JDI X-ray 1.90 D/E/F 47-528 [» ]
    2JIZ X-ray 2.30 D/E/F/K/L/M 47-528 [» ]
    2JJ1 X-ray 2.70 D/E/F/K/L/M 47-528 [» ]
    2JJ2 X-ray 2.40 D/E/F/K/L/M 47-528 [» ]
    2V7Q X-ray 2.10 D/E/F 47-528 [» ]
    2W6E X-ray 6.50 D/E/F 1-528 [» ]
    2W6F X-ray 6.00 D/E/F 1-528 [» ]
    2W6G X-ray 6.00 D/E/F 1-528 [» ]
    2W6H X-ray 5.00 D/E/F 1-528 [» ]
    2W6I X-ray 4.00 D/E/F 1-528 [» ]
    2W6J X-ray 3.84 D/E/F 1-528 [» ]
    2WSS X-ray 3.20 D/E/F/M/N/O 47-528 [» ]
    2XND X-ray 3.50 D/E/F 59-525 [» ]
    4ASU X-ray 2.60 D/E/F 49-528 [» ]
    ProteinModelPortali P00829.
    SMRi P00829. Positions 59-527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35476N.
    IntActi P00829. 5 interactions.
    MINTi MINT-5006882.

    Chemistry

    ChEMBLi CHEMBL612444.

    Proteomic databases

    PaxDbi P00829.
    PRIDEi P00829.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000017710 ; ENSBTAP00000017710 ; ENSBTAG00000013315 .
    GeneIDi 327675.
    KEGGi bta:327675.

    Organism-specific databases

    CTDi 506.

    Phylogenomic databases

    eggNOGi COG0055.
    GeneTreei ENSGT00550000074800.
    HOGENOMi HOG000009605.
    HOVERGENi HBG004307.
    InParanoidi P00829.
    KOi K02133.
    OMAi NPAGQDV.
    OrthoDBi EOG73V6K6.
    TreeFami TF105640.

    Enzyme and pathway databases

    Reactomei REACT_212639. Formation of ATP by chemiosmotic coupling.
    REACT_214581. Transcriptional activation of mitochondrial biogenesis.
    REACT_215731. Mitochondrial protein import.

    Miscellaneous databases

    EvolutionaryTracei P00829.
    NextBioi 20810140.

    Family and domain databases

    Gene3Di 1.10.1140.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_01347. ATP_synth_beta_bact.
    InterProi IPR003593. AAA+_ATPase.
    IPR020003. ATPase_a/bsu_AS.
    IPR005722. ATPase_F1-cplx_bsu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR024034. ATPase_F1_bsu/V1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01039. atpD. 1 hit.
    PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a complementary DNA for the nuclear-coded precursor of the beta-subunit of bovine mitochondrial F1-ATPase."
      Breen G.A.M., Holmans P.L., Garnett K.E.
      Biochemistry 27:3955-3961(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Ascending colon.
    3. "The amino acid sequence of the beta-subunit of ATP synthase from bovine heart mitochondria."
      Runswick M.J., Walker J.E.
      J. Biol. Chem. 258:3081-3089(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-528.
    4. "Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria."
      Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D., Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.
      J. Mol. Biol. 184:677-701(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 49-528.
    5. "Sequence analysis of cDNAs for the human and bovine ATP synthase beta subunit: mitochondrial DNA genes sustain seventeen times more mutations."
      Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A., Greenberg B.D.
      Curr. Genet. 12:81-90(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-528.
      Tissue: Heart.
    6. "Identification of the subunits of F1F0-ATPase from bovine heart mitochondria."
      Walker J.E., Lutter R., Dupuis A., Runswick M.J.
      Biochemistry 30:5369-5378(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 47-55.
      Tissue: Heart.
    7. "When beef-heart mitochondrial F1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites."
      Milgrom Y.M.
      Eur. J. Biochem. 200:789-795(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 388-422.
      Tissue: Heart.
    8. "The sites of labeling of the beta-subunit of bovine mitochondrial F1-ATPase with 8-azido-ATP."
      Hollemans M., Runswick M.J., Fearnley I.M., Walker J.E.
      J. Biol. Chem. 258:9307-9313(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: ATP-BINDING SITE.
    9. "Structural elucidation of N-terminal post-translational modifications by mass spectrometry: application to chicken enolase and the alpha- and beta-subunits of bovine mitochondrial F1-ATPase."
      Gibson B.W., Daley D.J., Williams D.H.
      Anal. Biochem. 169:217-226(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS.
    10. "Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria."
      Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.
      FEBS Lett. 581:3145-3148(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
    11. "Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex."
      Giorgio V., Bisetto E., Soriano M.E., Dabbeni-Sala F., Basso E., Petronilli V., Forte M.A., Bernardi P., Lippe G.
      J. Biol. Chem. 284:33982-33988(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPIF.
    12. "Structure at 2.8-A resolution of F1-ATPase from bovine heart mitochondria."
      Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.
      Nature 370:621-628(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 48-528.
    13. "The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin."
      Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G., Walker J.E.
      Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 48-528.
    14. "Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism."
      Orriss G.L., Leslie A.G., Braig K., Walker J.E.
      Structure 6:831-837(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 48-528.
    15. "The structure of bovine F1-ATPase in complex with its regulatory protein IF1."
      Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.
      Nat. Struct. Biol. 10:744-750(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 47-528 IN COMPLEX WITH ATPIF1; ATP5A1 AND ATP5C1.
    16. "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria."
      Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.
      Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 47-528 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5C1; ATP5D AND ATP5E.

    Entry informationi

    Entry nameiATPB_BOVIN
    AccessioniPrimary (citable) accession number: P00829
    Secondary accession number(s): Q1JQA9, Q9T2U4, Q9T2U5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3