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ATP5PB ATP synthase peripheral stalk-membrane subunit b [ Homo sapiens (human) ]

Gene ID: 515, updated on 14-Nov-2024

Summary

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Official Symbol
ATP5PBprovided by HGNC
Official Full Name
ATP synthase peripheral stalk-membrane subunit bprovided by HGNC
Primary source
HGNC:HGNC:840
See related
Ensembl:ENSG00000116459 MIM:603270; AllianceGenome:HGNC:840
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
PIG47; ATP5F1
Summary
This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the b subunit of the proton channel. [provided by RefSeq, Jul 2008]
Expression
Ubiquitous expression in heart (RPKM 107.3), colon (RPKM 76.0) and 25 other tissues See more
Orthologs
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Genomic context

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See ATP5PB in Genome Data Viewer
Location:
1p13.2
Exon count:
7
Annotation release Status Assembly Chr Location
RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 1 NC_000001.11 (111449464..111462773)
RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 1 NC_060925.1 (111464148..111477456)
RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 1 NC_000001.10 (111992086..112005395)

Chromosome 1 - NC_000001.11Genomic Context describing neighboring genes Neighboring gene UBE2F pseudogene 3 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 1495 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 1496 Neighboring gene WD repeat domain 77 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 1497 Neighboring gene chromosome 1 open reading frame 162 Neighboring gene transmembrane and immunoglobulin domain containing 3 Neighboring gene RNA, U6 small nuclear 792, pseudogene

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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Related articles in PubMed

  1. Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria. Higuti T, et al. Biochem Biophys Res Commun, 1991 Aug 15. PMID 1831354
  2. Down-regulation of mitochondrial ATPase by hypermethylation mechanism in chronic myeloid leukemia is associated with multidrug resistance. Li RJ, et al. Ann Oncol, 2010 Jul. PMID 20038517
  3. Nitration of tyrosine residues 368 and 345 in the beta-subunit elicits FoF1-ATPase activity loss. Fujisawa Y, et al. Biochem J, 2009 Sep 25. PMID 19650768
  4. The expression of subunit c correlates with and thus may limit the biosynthesis of the mitochondrial F0F1-ATPase in brown adipose tissue. Houstĕk J, et al. J Biol Chem, 1995 Mar 31. PMID 7706317
  5. Two genes encoding the bovine mitochondrial ATP synthase proteolipid specify precursors with different import sequences and are expressed in a tissue-specific manner. Gay NJ, et al. EMBO J, 1985 Dec 16. PMID 2868890, Free PMC Article

See all (127) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Down-regulation of mitochondrial ATPase by hypermethylation mechanism in chronic myeloid leukemia is associated with multidrug resistance.
    Title: Down-regulation of mitochondrial ATPase by hypermethylation mechanism in chronic myeloid leukemia is associated with multidrug resistance.
  2. Nitration of tyrosine residues 368 and 345 in the beta-subunit elicits FoF1-ATPase activity loss.
    Title: Nitration of tyrosine residues 368 and 345 in the beta-subunit elicits FoF1-ATPase activity loss.
  3. Observational study of gene-disease association. (HuGE Navigator)
    Title: Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
Submit: New GeneRIF Correction

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See Variation Viewer (GRCh37.p13)

HIV-1 interactions

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Protein interactions

Protein Gene Interaction Pubs
Vpr vpr A stable-isotope labeling by amino acids in cell culture coupled with mass spectrometry-based proteomics identifies downregulation of ATP synthase, mitochondrial Fo complex, subunit B1 (ATP5F1) expression by HIV-1 Vpr in Vpr transduced macrophages PubMed
Vpu vpu HIV-1 Vpu is identified to have a physical interaction with ATP synthase, H+ transporting, mitochondrial Fo complex, subunit B1 (ATP5F1) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses PubMed

Go to the HIV-1, Human Interaction Database

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Clone Names

  • MGC24431

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
contributes_to proton-transporting ATP synthase activity, rotational mechanism IBA
Inferred from Biological aspect of Ancestor
more info
  
contributes_to proton-transporting ATP synthase activity, rotational mechanism IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in proton motive force-driven ATP synthesis IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in proton motive force-driven ATP synthesis NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in proton motive force-driven mitochondrial ATP synthesis IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proton transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
involved_in substantia nigra development HEP PubMed 
Component Evidence Code Pubs
located_in membrane HDA PubMed 
located_in mitochondrial inner membrane NAS
Non-traceable Author Statement
more info
 PubMed 
located_in mitochondrial inner membrane TAS
Traceable Author Statement
more info
  
located_in mitochondrial matrix NAS
Non-traceable Author Statement
more info
 PubMed 
located_in mitochondrion HDA PubMed 
located_in mitochondrion HTP PubMed 
located_in mitochondrion IC
Inferred by Curator
more info
 PubMed 
located_in mitochondrion IDA
Inferred from Direct Assay
more info
  
located_in nucleus HDA PubMed 
part_of proton-transporting ATP synthase complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of proton-transporting ATP synthase complex, coupling factor F(o) IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
ATP synthase F(0) complex subunit B1, mitochondrial
Names
ATP synthase B chain, mitochondrial
ATP synthase proton-transporting mitochondrial F(0) complex subunit B1
ATP synthase subunit b, mitochondrial
ATP synthase, H+ transporting, mitochondrial F0 complex, subunit B1
ATP synthase, H+ transporting, mitochondrial F0 complex, subunit b
ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1
ATPase subunit b
H+-ATP synthase subunit b
cell proliferation-inducing protein 47

NCBI Reference Sequences (RefSeq)

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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_001688.5 → NP_001679.2  ATP synthase F(0) complex subunit B1, mitochondrial precursor

    See identical proteins and their annotated locations for NP_001679.2

    Status: REVIEWED

    Source sequence(s)
    AI754631, AL390195, AW778751, BF237506
    Consensus CDS
    CCDS836.1
    UniProtKB/Swiss-Prot
    P24539, Q9BQ68, Q9BRU8
    UniProtKB/TrEMBL
    A0A024R0E1, A8K4W2, Q08ET0, Q53GB3
    Related
    ENSP00000358737.3, ENST00000369722.8
    Conserved Domains (1) summary
    pfam05405
    Location:83 → 244
    Mt_ATP-synt_B; Mitochondrial ATP synthase B chain precursor (ATP-synt_B)

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

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

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000001.11 Reference GRCh38.p14 Primary Assembly

    Range
    111449464..111462773
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060925.1 Alternate T2T-CHM13v2.0

    Range
    111464148..111477456
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. NM_001002014.1: Suppressed sequence

    Description
    NM_001002014.1: This RefSeq record was removed by NCBI staff. Contact info@ncbi.nlm.nih.gov for further information.

  2. NM_001002015.1: Suppressed sequence

    Description
    NM_001002015.1: This RefSeq record was removed by NCBI staff. Contact info@ncbi.nlm.nih.gov for further information.
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P24539.2 GenPept UniProtKB/Swiss-Prot:P24539

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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