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ATP5F1B ATP synthase F1 subunit beta [ Bos taurus (domestic cattle) ]

Gene ID: 327675, updated on 10-May-2025
Official Symbol
ATP5F1Bprovided by VGNC
Official Full Name
ATP synthase F1 subunit betaprovided by VGNC
Primary source
VGNC:VGNC:26300
See related
BGD:BT12445; EnsemblRapid:ENSBTAG00070011990
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bos taurus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as
ATP5B
Orthologs
human mouse all
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See ATP5F1B in Genome Data Viewer
Location:
chromosome: 5
Exon count:
10
Annotation release Status Assembly Chr Location
RS_2024_12 current ARS-UCD2.0 (GCF_002263795.3) 5 NC_037332.1 (56789641..56795014)

Chromosome 5 - NC_037332.1Genomic Context describing neighboring genes Neighboring gene cytohesin-2-like Neighboring gene prostaglandin E synthase 3 Neighboring gene small nucleolar RNA SNORD59 Neighboring gene uncharacterized LOC112446708 Neighboring gene microRNA mir-677 Neighboring gene bromodomain adjacent to zinc finger domain 2A Neighboring gene RNA binding motif single stranded interacting protein 2

Genomic Sequence:
NC_037332.1 Chromosome 5 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

  • Project title: Dominette sequence data
  • BioProject: PRJNA294306
  • Analysis date: Tue Dec 17 08:57:05 2024

Related articles in PubMed

  1. The amino acid sequence of the beta-subunit of ATP synthase from bovine heart mitochondria. Runswick MJ, et al. J Biol Chem, 1983 Mar 10. PMID 6298222
  2. Effects of an ATP analogue, adenosine 5'-[α-thio]-triphosphate, on F1-ATPase rotary catalysis, torque generation, and inhibited intermediated formation. Yukawa A, et al. Biochem Biophys Res Commun, 2015 Mar 13. PMID 25681765
  3. Rotation triggers nucleotide-independent conformational transition of the empty β subunit of F₁-ATPase. Czub J, et al. J Am Chem Soc, 2014 May 14. PMID 24798048
  4. Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria. Rees DM, et al. Proc Natl Acad Sci U S A, 2012 Jul 10. PMID 22733764, Free PMC Article
  5. When beef-heart mitochondrial F1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites. Milgrom YM. Eur J Biochem, 1991 Sep 15. PMID 1833193

See all (27) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Combining cryoelectron microscopy data with bioinformatic analysis allowed the authors to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits.
    Title: Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.
  2. These data indicate that interaction with the alpha-phosphate is not crucial for efficient catalysis, but likely contributes to avoid formation of ADP-inhibited intermediates.
    Title: Effects of an ATP analogue, adenosine 5'-[α-thio]-triphosphate, on F1-ATPase rotary catalysis, torque generation, and inhibited intermediated formation.
  3. Molecular dynamics simulations show that the nucleotide-free beta subunit, initially in the open, low-affinity state, undergoes a spontaneous closing transition to the half-open state in response to the gamma rotation in the synthesis direction.
    Title: Rotation triggers nucleotide-independent conformational transition of the empty β subunit of F₁-ATPase.
  4. analysis of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria
    Title: Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria.
  5. Molecular dynamics simulations of F1-ATPase suggest that the equilibrium conformation of a nucleotide-free beta-subunit is the open conformation and that the transition from the closed to the open conformation can occur in a few tens of nanoseconds.
    Title: Domain motion of individual F1-ATPase β-subunits during unbiased molecular dynamics simulations.
  6. molecular dynamic analysis of interaction between the gamma-subunit and a C-terminal fragment of the beta-subunit of F1-ATPase
    Title: A molecular dynamic analysis of interaction between the gamma-subunit and a C-terminal fragment of the beta-subunit of F1-ATPase.
  7. The catalytic sites of beef heart mitochondrial F1-ATPase were studied by electron spin echo envelope modulation (ESEEM) spectroscopy, using Mn(II) as a paramagnetic probe
    Title: Conformational role of the divalent metal in bovine heart mitochondrial F1-ATPase: an electron spin echo envelope modulation study.
  8. Inhibition arises by IF(1) imposing the structure and properties of the beta(TP)-alpha(TP) interface on the beta(DP)-alpha(DP) interface, thereby preventing it from hydrolyzing the bound ATP.
    Title: How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria.
  9. The beneficial effects of dietary resveratrol may derive in part by preventing mitochondrial ATP synthesis in tumor cells, thereby inducing apoptosis
    Title: Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols.
Submit: New GeneRIF Correction

Markers

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables proton-transporting ATP synthase activity, rotational mechanism IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in proton motive force-driven mitochondrial ATP synthesis IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in proton transmembrane transport IEA
Inferred from Electronic Annotation
more info
 PubMed 
Preferred Names
ATP synthase F(1) complex catalytic subunit beta, mitochondrial
Names
ATP synthase subunit beta, mitochondrial
ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide
F1-ATPase beta-subunit
mitochondrial ATP synthase beta subunit
NP_786990.1

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_175796.3 → NP_786990.1  ATP synthase F(1) complex catalytic subunit beta, mitochondrial precursor

    See identical proteins and their annotated locations for NP_786990.1

    Status: PROVISIONAL

    Source sequence(s)
    M20929
    UniProtKB/Swiss-Prot
    P00829, Q1JQA9, Q9T2U4, Q9T2U5
    UniProtKB/TrEMBL
    A0A452DII8
    Related
    ENSBTAP00070016108.1, ENSBTAT00070027026.1
    Conserved Domains (1) summary
    PRK09280
    Location:58 → 524
    PRK09280; F0F1 ATP synthase subunit beta; Validated

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2024_12

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

  1. NC_037332.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    56789641..56795014
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00829.2 GenPept UniProtKB/Swiss-Prot:P00829

Gene LinkOut

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Molecular Biology Databases
Research Materials