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0ATPB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameATP5B
DescriptionAtp synthase beta chain, mitochondrial precursor (ec 3.6.3.14).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005753 proton-transporting ATP synthase complex (s... (TAS)
0005754 proton-transporting ATP synthase, catalytic... (TAS)
0005215 transporter activity (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient.sing the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse.sing the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases.hich can differ in function (ATP synthesis and/or hydrolysis).tructure (F-.- and A-ATPases contain rotary motors) and in the type of ions they transport . F-ATPases (F1F0-ATPases) in mitochondria.hloroplasts and bacterial plasma membranes are the prime producers of ATP.sing the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles.atalysing ATP hydrolysis to transport solutes and lower pH in organelles.A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles.nd function to transport a variety of different ions across membranes.E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs.ncluding extracellular ATP.This entry represents the alpha and beta subunits found in the F1.1.nd A1 complexes of F-.- and A-ATPases.espectively (sometimes called the A and B subunits in V- and A-ATPases).s well as flagellar ATPase and the termination factor Rho. The F-ATPases (or F1F0-ATPases).-ATPases (or V1V0-ATPases) and A-ATPases (or A1A0-ATPases) are composed of two linked complexes: the F1.1 or A1 complex contains the catalytic core that synthesizes/hydrolyses ATP.nd the F0.0 or A0 complex that forms the membrane-spanning pore. The F-.- and A-ATPases all contain rotary motors.ne that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis .In F-ATPases.here are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex.hile the remaining F1 subunits (gamma.elta.psilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits.hose on the beta subunits being catalytic.hile those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP.hich are induced by the rotation of the gamma subunit.tself is driven by the movement of protons through the F0 complex C subunit .In V- and A-ATPases.he alpha/A and beta/B subunits of the V1 or A1 complex are homologous to the alpha and beta subunits in the F1 complex of F-ATPases.xcept that the alpha subunit is catalytic and the beta subunit is regulatory.The alpha/A and beta/B subunits can each be divided into three regions.r domains.entred around the ATP-binding pocket.nd based on structure and function. The central domain contains the nucleotide-binding residues that make direct contact with the ADP/ATP molecule .More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR000194:ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient.sing the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse.sing the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases.hich can differ in function (ATP synthesis and/or hydrolysis).tructure (F-.- and A-ATPases contain rotary motors) and in the type of ions they transport . F-ATPases (F1F0-ATPases) in mitochondria.hloroplasts and bacterial plasma membranes are the prime producers of ATP.sing the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles.atalysing ATP hydrolysis to transport solutes and lower pH in organelles.A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles.nd function to transport a variety of different ions across membranes.E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs.ncluding extracellular ATP.This entry represents the alpha and beta subunits found in the F1.1.nd A1 complexes of F-.- and A-ATPases.espectively (sometimes called the A and B subunits in V- and A-ATPases). The F-ATPases (or F1F0-ATPases).-ATPases (or V1V0-ATPases) and A-ATPases (or A1A0-ATPases) are composed of two linked complexes: the F1.1 or A1 complex contains the catalytic core that synthesizes/hydrolyses ATP.nd the F0.0 or A0 complex that forms the membrane-spanning pore. The F-.- and A-ATPases all contain rotary motors.ne that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis .In F-ATPases.here are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex.hile the remaining F1 subunits (gamma.elta.psilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits.hose on the beta subunits being catalytic.hile those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP.hich are induced by the rotation of the gamma subunit.tself is driven by the movement of protons through the F0 complex C subunit .In V- and A-ATPases.he alpha/A and beta/B subunits of the V1 or A1 complex are homologous to the alpha and beta subunits in the F1 complex of F-ATPases.xcept that the alpha subunit is catalytic and the beta subunit is regulatory.The alpha/A and beta/B subunits can each be divided into three regions.r domains.entred around the ATP-binding pocket.nd based on structure and function.here the central region is the nucleotide-binding domain () . This entry represents the C-terminal domain of the alpha/A/beta/B subunits.hich forms a left-handed superhelix composed of 4-5 individual helices. The C-terminal domain can vary between the alpha and beta subunits.nd between different ATPases . More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR000793:ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient.sing the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse.sing the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases.hich can differ in function (ATP synthesis and/or hydrolysis).tructure (F-.- and A-ATPases contain rotary motors) and in the type of ions they transport . F-ATPases (F1F0-ATPases) in mitochondria.hloroplasts and bacterial plasma membranes are the prime producers of ATP.sing the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles.atalysing ATP hydrolysis to transport solutes and lower pH in organelles.A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles.nd function to transport a variety of different ions across membranes.E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs.ncluding extracellular ATP.This entry represents the alpha and beta subunits found in the F1.1.nd A1 complexes of F-.- and A-ATPases.espectively (sometimes called the A and B subunits in V- and A-ATPases). The F-ATPases (or F1F0-ATPases).-ATPases (or V1V0-ATPases) and A-ATPases (or A1A0-ATPases) are composed of two linked complexes: the F1.1 or A1 complex contains the catalytic core that synthesizes/hydrolyses ATP.nd the F0.0 or A0 complex that forms the membrane-spanning pore. The F-.- and A-ATPases all contain rotary motors.ne that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis .In F-ATPases.here are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex.hile the remaining F1 subunits (gamma.elta.psilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits.hose on the beta subunits being catalytic.hile those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP.hich are induced by the rotation of the gamma subunit.tself is driven by the movement of protons through the F0 complex C subunit .In V- and A-ATPases.he alpha/A and beta/B subunits of the V1 or A1 complex are homologous to the alpha and beta subunits in the F1 complex of F-ATPases.xcept that the alpha subunit is catalytic and the beta subunit is regulatory.The alpha/A and beta/B subunits can each be divided into three regions.r domains.entred around the ATP-binding pocket.nd based on structure and function.here the central region is the nucleotide-binding domain () . This entry represents the N-terminal domain of the alpha/A/beta/B subunits.hich forms a closed beta-barrel with Greek-key topology. More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR004100:ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal
AAA ATPases form a large.unctionally diverse protein family belonging to the AAA+ superfamily of ring-shaped P-loop NTPases.hich exert their activity through the energy-dependent unfolding of macromolecules. AAA ATPases contain a P-loop NTPase domain.hich is the most abundant class of NTP-binding protein fold.nd is found throughout all kingdoms of life . P-loop NTPase domains act to hydrolyse the beta-gamma phosphate bond of bound nucleoside triphosphate. There are two classes of P-loop domains: the KG (kinase-GTPase) division.nd the ASCE division.he latter including the AAA+ group as well as several other ATPases.There are at least six major clades of AAA domains (metalloproteases.eiotic proteins.1 and D2 domains of ATPases with two AAA domains.roteasome subunits.nd BSC1).s well as several minor clades.ome of which consist of hypothetical proteins . The domain organisation of AAA ATPases consists of a non-ATPase N-terminal domain that acts in substrate recognition.ollowed by one or two AAA domains (D1 and D2).ne of which may be degenerate.
  IPR003593:AAA ATPase
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient.sing the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse.sing the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases.hich can differ in function (ATP synthesis and/or hydrolysis).tructure (F-.- and A-ATPases contain rotary motors) and in the type of ions they transport . F-ATPases (F1F0-ATPases) in mitochondria.hloroplasts and bacterial plasma membranes are the prime producers of ATP.sing the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles.atalysing ATP hydrolysis to transport solutes and lower pH in organelles.A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles.nd function to transport a variety of different ions across membranes.E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs.ncluding extracellular ATP.F-ATPases (also known as F1F0-ATPase.r H(+)-transporting two-sector ATPase) () are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha.eta.amma.elta.psilon).hile the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C).ine in mitochondria (A-G.6.8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex.he central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits.hile in the F0 complex.he ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions.ut the F0 rotor is usually stronger.sing the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis . These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient.This entry represents the beta subunit found in the F1 complex of F-ATPases. In F-ATPases.here are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex.hile the remaining F1 subunits (gamma.elta.psilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits.hose on the beta subunits being catalytic.hile those on the alpha subunits are regulatory. The alpha and beta subunits form a cylinder that is attached to the central stalk. The alpha/beta subunits undergo a sequence of conformational changes leading to the formation of ATP from ADP.hich are induced by the rotation of the gamma subunit.tself is driven by the movement of protons through the F0 complex C subunit .More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR005722:ATPase, F1 complex, beta subunit
IPR000194:ATP-synt_ab 
Evalue:-99.958610534668 
Location:185-405IPR000793:ATP-synt_ab_C 
Evalue:-51.7212448120117 
Location:418-525IPR004100:ATP-synt_ab_N 
Evalue:-26.1739253997803 
Location:63-129
SequencesProtein: ATPB_HUMAN (529 aa)
mRNA: NM_001686
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK02133
  Level 3 annotation:
    F-type H+-transporting ATPase beta chain
  Level 2 annotation:
    ATP synthesis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 84 residues, 55318225-55318474Exon2: 69 residues, 55319156-55319358Exon3: 73 residues, 55320030-55320243Exon4: 43 residues, 55322508-55322631Exon5: 55 residues, 55322723-55322882Exon6: 63 residues, 55323453-55323638Exon7: 42 residues, 55323887-55324009Exon8: 60 residues, 55324831-55325006Exon9: 63 residues, 55325221-55325404Exon10: 79 residues, 55325887-55326119Exon11: 2 residues, -Jump to ATPB_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2763 54396087-54399754 ~-4K 9024(BLOC1S1)(+)Loci: 2764 54423333-54430331 ~-7K 9030(GDF11)(+)Loci: 2765 54654128-54674745 ~-21K 9056(RAB5B)(+)Loci: 2766 54677309-54685574 ~-8K 9057(SUOX)(+)Loci: 2767 54798296-54802545 ~-4K 9067(+)Loci: 4051 54843395-54869544 ~-26K 9082(SMARCC2)(-)Loci: 4052 54951749-54980442 ~-29K 9095(CS)(-)Loci: 4053 55151003-55168448 ~-17K 9108(GLS2)(-)Loci: 4054 55275981-55316430 ~-40K 9114(BAZ2A)(-)Loci: 4055 55318225-55326119 ~-8K 9115(ATP5B)(-)Loci: 4056 55708568-55730160 ~-22K 9128(MYO1A)(-)Loci: 4050 54364622-54387894 ~-23K 9022(ITGA7)(-)Link out to UCSC