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P00829

- ATPB_BOVIN

UniProt

P00829 - ATPB_BOVIN

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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

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. proton-transporting ATPase activity, rotational mechanism Source: Ensembl
  3. 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. osteoblast differentiation Source: Ensembl
  8. regulation of intracellular pH Source: Ensembl
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  3. mitochondrial nucleoid Source: Ensembl
  4. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  5. nucleus Source: Ensembl
  6. plasma membrane Source: Ensembl
  7. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4TSFX-ray3.20D/E/F49-528[»]
4TT3X-ray3.21D/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

        10         20         30         40         50
MLGLVGRVVA ASASGALRGL SPSAPLPQAQ LLLRAAPAAL QPARDYAAQA
60 70 80 90 100
SPSPKAGATT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA
110 120 130 140 150
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIRIPVGPET LGRIMNVIGE
160 170 180 190 200
PIDERGPIKT KQFAAIHAEA PEFVEMSVEQ EILVTGIKVV DLLAPYAKGG
210 220 230 240 250
KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM
260 270 280 290 300
IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
310 320 330 340 350
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK
360 370 380 390 400
KGSITSVQAI YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP
410 420 430 440 450
LDSTSRIMDP NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED
460 470 480 490 500
KLTVSRARKI QRFLSQPFQV AEVFTGHLGK LVPLKETIKG FQQILAGEYD
510 520
HLPEQAFYMV GPIEEAVAKA DKLAEEHS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4TSF X-ray 3.20 D/E/F 49-528 [» ]
4TT3 X-ray 3.21 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

BindingDBi P00829.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 153 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