SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0VATB1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameATP6V1B1
DescriptionVacuolar atp synthase subunit b, kidney isoform (ec 3.6.3.14) (v- atpase b1 subunit) (vacuolar proton pump b isoform 1) (endomembrane proton pump 58 kda subunit).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0007588 excretion (TAS)
0007605 perception of sound (TAS)
0015992 proton transport (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/1261184464.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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
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.V-ATPases (also known as V1V0-ATPase or vacuolar ATPase) () are found in the eukaryotic endomembrane system.nd in the plasma membrane of prokaryotes and certain specialised eukaryotic cells. V-ATPases hydrolyse ATP to drive a proton pump.nd are involved in a variety of vital intra- and inter-cellular processes such as receptor mediated endocytosis.rotein trafficking.ctive transport of metabolites.omeostasis and neurotransmitter release . V-ATPases are composed of two linked complexes: the V1 complex (subunits A-H) contains the catalytic core that hydrolyses ATP.hile the V0 complex (subunits a... d) forms the membrane-spanning pore. V-ATPases may have an additional role in membrane fusion through binding to t-SNARE proteins .This entry represents subunit B from the V1 complex of V-ATPases. There are three copies each of subunits A () and B.oth of which participate in nucleotide binding. However.nly subunit A is catalytic for ATP hydrolysis.ubunit B being noncatalytic . More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR005723:ATPase, V1 complex, subunit B
IPR000194:ATP-synt_ab 
Evalue:-91.5528411865234 
Location:166-393IPR000793:ATP-synt_ab_C 
Evalue:-25.0362129211426 
Location:410-500IPR004100:ATP-synt_ab_N 
Evalue:-10.958607673645 
Location:44-110
SequencesProtein: VATB1_HUMAN (513 aa)
mRNA: M25809 NM_001692
Local Annotation
Synapse Ontology
The directed movement of substances, either within a vesicle or in the vesicle membrane, into, out of or within a cell.
sdb:0057 axon transport  (Evidence:keywords)
KO assignmentK02147
  Level 3 annotation:
    V-type H+-transporting ATPase subunit B
  Level 2 annotation:
    ATP synthesis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 69 residues, 71016505-71016710Exon2: 20 residues, 71024295-71024351Exon3: 35 residues, 71038683-71038782Exon4: 33 residues, 71038970-71039064Exon5: 28 residues, 71039655-71039733Exon6: 48 residues, 71040576-71040716Exon7: 36 residues, 71041558-71041660Exon8: 34 residues, 71042233-71042331Exon9: 43 residues, 71043414-71043538Exon10: 52 residues, 71043799-71043950Exon11: 29 residues, 71044209-71044292Exon12: 37 residues, 71045075-71045180Exon13: 45 residues, 71045373-71045503Exon14: 159 residues, 71045595-71046068Exon15: 2 residues, -Jump to VATB1_HUMANExon1: 52 residues, 71016556-71016710Exon2: 20 residues, 71024295-71024351Exon3: 35 residues, 71038683-71038782Exon4: 33 residues, 71038970-71039064Exon5: 28 residues, 71039655-71039733Exon6: 48 residues, 71040576-71040716Exon7: 36 residues, 71041558-71041660Exon8: 34 residues, 71042233-71042331Exon9: 43 residues, 71043414-71043538Exon10: 52 residues, 71043799-71043950Exon11: 29 residues, 71044209-71044292Exon12: 37 residues, 71045075-71045180Exon13: 45 residues, 71045373-71045503Exon14: 131 residues, 71045595-71045984Exon15: 24 residues, 71045993-71046060Exon16: 2 residues, -Jump to VATB1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3169 71412396-71515695 ~-103K 20632(ZNF638)(+)Loci: 3168 71016505-71046068 ~-30K 20619(ATP6V1B1)(+)Link out to UCSC