ATP6V1B1

Protein identityUniProt · HPA

UniProt accession

P15313

Gene

ATP6V1B1

Ensembl

ENSG00000116039

Chromosome

2

Canonical length

513 aa

Protein class

Disease related genes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Transporters

Subcellular location

Nucleoplasm,Nuclear membrane

OverviewNCBI Gene

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

513 residues, UniProt reviewed canonical sequence.

>P15313|ATP6V1B1
     1  MAMEIDSRPG GLPGSSCNLG AAREHMQAVT RNYITHPRVT YRTVCSVNGP LVVLDRVKFA
    61  QYAEIVHFTL PDGTQRSGQV LEVAGTKAIV QVFEGTSGID ARKTTCEFTG DILRTPVSED
   121  MLGRVFNGSG KPIDKGPVVM AEDFLDINGQ PINPHSRIYP EEMIQTGISP IDVMNSIARG
   181  QKIPIFSAAG LPHNEIAAQI CRQAGLVKKS KAVLDYHDDN FAIVFAAMGV NMETARFFKS
   241  DFEQNGTMGN VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA
   301  LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM PNDDITHPIP
   361  DLTGFITEGQ IYVDRQLHNR QIYPPINVLP SLSRLMKSAI GEGMTRKDHG DVSNQLYACY
   421  AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ KFEKNFINQG PYENRSVFES LDLGWKLLRI
   481  FPKEMLKRIP QAVIDEFYSR EGALQDLAPD TAL

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ATP6V1B1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Cell surface

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.28

Highest tissue expression

132 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ATP6V1B1.

Disease | AllUniProt

Conditions ATP6V1B1 is implicated in, by any mechanism.

• Renal tubular acidosis, distal, 2, with progressive sensorineural hearing loss (DRTA2) MIM:267300

Disease | GeneticClinVar

127 pathogenic / likely-pathogenic of 874 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Renal tubular acidosis with progressive nerve deafness
• Inborn genetic diseases
• Distal renal tubular acidosis
• Renal tubulopathies
• ATP6V1B1-related disorder

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.95

gnomAD pLI

0

gnomAD missense Z

0.23

DepMap mean gene effect

-0.04

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• adult behavior
• ATP metabolic process
• calcium ion homeostasis
• chloride ion homeostasis
• inner ear morphogenesis
• olfactory behavior
• ossification
• pH reduction
• potassium ion homeostasis
• prostaglandin metabolic process
• proton transmembrane transport
• regulation of gene expression
• regulation of macroautophagy
• regulation of pH
• renal sodium excretion
• renal sodium ion transport
• renal tubular secretion
• renal water homeostasis
• sensory perception of sound
• synaptic vesicle lumen acidification
• vacuolar acidification
• vacuolar proton-transporting V-type ATPase complex assembly

Molecular functions

• ATP binding
• protein-containing complex binding
• proton transmembrane transporter activity
• proton-transporting ATPase activity, rotational mechanism

Cellular components

• apical plasma membrane
• basolateral plasma membrane
• cytoplasm
• cytosol
• extracellular exosome
• extrinsic component of synaptic vesicle membrane
• lateral plasma membrane
• microvillus
• vacuolar proton-transporting V-type ATPase complex
• vacuolar proton-transporting V-type ATPase, V1 domain

Protein domainsUniProt · Pfam · InterPro

• ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
• ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain
• ATPase, V1 complex, subunit B
• ATPase, alpha/beta subunit, nucleotide-binding domain, active site
• V-type ATP synthase regulatory subunit B/beta
• P-loop containing nucleoside triphosphate hydrolase
• ATP synthase A/B type, C-terminal domain
• ATP synthase alpha/beta family, nucleotide-binding domain
• ATP synthase alpha/beta family, beta-barrel domain
• C-terminal domain of V and A type ATP synthase

KeywordsUniProt

• ATP-binding
• Cell membrane
• Deafness
• Hydrogen ion transport
• Ion transport
• Membrane
• Nucleotide-binding
• Transport

InteractionsUniProt · HPA

Protein binding partners of ATP6V1B1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• ATP6V1A
• ATP6V1B2
• ATP6V1C1
• ATP6V1D
• ATP6V1E1
• ATP6V1G1