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Protein

V-type proton ATPase subunit B, kidney isoform

Gene

ATP6V1B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

GO - Molecular functioni

GO - Biological processi

  • ATP hydrolysis coupled proton transport Source: InterPro
  • ATP metabolic process Source: InterPro
  • calcium ion homeostasis Source: UniProtKB
  • cellular iron ion homeostasis Source: Reactome
  • excretion Source: UniProtKB
  • inner ear morphogenesis Source: UniProtKB
  • insulin receptor signaling pathway Source: Reactome
  • interaction with host Source: Reactome
  • ion transmembrane transport Source: Reactome
  • ossification Source: HGNC
  • phagosome maturation Source: Reactome
  • pH reduction Source: UniProtKB
  • proton transport Source: HGNC
  • regulation of pH Source: HGNC
  • sensory perception of sound Source: UniProtKB
  • transferrin transport Source: Reactome
  • transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS03975-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.
REACT_25300. Ion channel transport.

Protein family/group databases

TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit B, kidney isoform
Short name:
V-ATPase subunit B 1
Alternative name(s):
Endomembrane proton pump 58 kDa subunit
Vacuolar proton pump subunit B 1
Gene namesi
Name:ATP6V1B1
Synonyms:ATP6B1, VATB, VPP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:853. ATP6V1B1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • endomembrane system Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • lateral plasma membrane Source: UniProtKB
  • microvillus Source: UniProtKB
  • proton-transporting V-type ATPase, V1 domain Source: InterPro
  • vacuolar proton-transporting V-type ATPase complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Renal tubular acidosis, distal, with progressive nerve deafness (dRTA-D)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive disease characterized by the association of renal distal tubular acidosis with sensorineural hearing loss. Distal renal tubular acidosis is characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha-intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification.

See also OMIM:267300
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811L → P in dRTA-D. 3 Publications
VAR_007866
Natural varianti123 – 1231G → V in dRTA-D. 1 Publication
VAR_021012
Natural varianti124 – 1241R → W in dRTA-D. 1 Publication
VAR_007867
Natural varianti157 – 1571R → C in dRTA-D. 1 Publication
VAR_021013
Natural varianti174 – 1741M → R in dRTA-D. 1 Publication
VAR_007868
Natural varianti275 – 2751T → P in dRTA-D. 2 Publications
VAR_007869
Natural varianti316 – 3161G → E in dRTA-D. 1 Publication
VAR_007870
Natural varianti346 – 3461P → R in dRTA-D. 3 Publications
VAR_007871
Natural varianti364 – 3641G → S in dRTA-D. 1 Publication
VAR_007872
Natural varianti465 – 4651R → H in dRTA-D. 1 Publication
Corresponds to variant rs142905621 [ dbSNP | Ensembl ].
VAR_021015

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi513 – 5131L → G: Loss of interactions with SLC9A3R1 and SCL4A7. 1 Publication

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

MIMi267300. phenotype.
Orphaneti402041. Autosomal recessive distal renal tubular acidosis.
PharmGKBiPA25154.

Polymorphism and mutation databases

BioMutaiATP6V1B1.
DMDMi215274116.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513V-type proton ATPase subunit B, kidney isoformPRO_0000144624Add
BLAST

Proteomic databases

MaxQBiP15313.
PaxDbiP15313.
PRIDEiP15313.

PTM databases

PhosphoSiteiP15313.

Expressioni

Tissue specificityi

Expressed in the cochlea and endolymphatic sac.1 Publication

Gene expression databases

BgeeiP15313.
CleanExiHS_ATP6V1B1.
ExpressionAtlasiP15313. baseline and differential.
GenevisibleiP15313. HS.

Organism-specific databases

HPAiCAB009523.
HPA031847.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein). Forms a complex with SLC9A3R1 and SCL4A7.

Protein-protein interaction databases

BioGridi107008. 93 interactions.
IntActiP15313. 3 interactions.
MINTiMINT-8417607.
STRINGi9606.ENSP00000234396.

Structurei

3D structure databases

ProteinModelPortaliP15313.
SMRiP15313. Positions 41-497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi510 – 5134PDZ-binding

Domaini

The PDZ-binding motif mediates interactions with SLC9A3R1 and SCL4A7.1 Publication

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiCOG1156.
GeneTreeiENSGT00550000074724.
HOGENOMiHOG000165320.
HOVERGENiHBG002176.
InParanoidiP15313.
KOiK02147.
OMAiNEGDITH.
OrthoDBiEOG7NW68Q.
PhylomeDBiP15313.
TreeFamiTF300313.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMEIDSRPG GLPGSSCNLG AAREHMQAVT RNYITHPRVT YRTVCSVNGP
60 70 80 90 100
LVVLDRVKFA QYAEIVHFTL PDGTQRSGQV LEVAGTKAIV QVFEGTSGID
110 120 130 140 150
ARKTTCEFTG DILRTPVSED MLGRVFNGSG KPIDKGPVVM AEDFLDINGQ
160 170 180 190 200
PINPHSRIYP EEMIQTGISP IDVMNSIARG QKIPIFSAAG LPHNEIAAQI
210 220 230 240 250
CRQAGLVKKS KAVLDYHDDN FAIVFAAMGV NMETARFFKS DFEQNGTMGN
260 270 280 290 300
VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA
310 320 330 340 350
LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM
360 370 380 390 400
PNDDITHPIP DLTGFITEGQ IYVDRQLHNR QIYPPINVLP SLSRLMKSAI
410 420 430 440 450
GEGMTRKDHG DVSNQLYACY AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ
460 470 480 490 500
KFEKNFINQG PYENRSVFES LDLGWKLLRI FPKEMLKRIP QAVIDEFYSR
510
EGALQDLAPD TAL
Length:513
Mass (Da):56,833
Last modified:November 25, 2008 - v3
Checksum:i5399E2849F3B99AA
GO

Sequence cautioni

The sequence AAA36498.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti467 – 4671V → M in AAA36498 (PubMed:2527371).Curated
Sequence conflicti474 – 4741G → S in AAA36498 (PubMed:2527371).Curated
Sequence conflicti503 – 5031A → R in AAA36498 (PubMed:2527371).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti30 – 301T → I.2 Publications
Corresponds to variant rs17720303 [ dbSNP | Ensembl ].
VAR_021011
Natural varianti81 – 811L → P in dRTA-D. 3 Publications
VAR_007866
Natural varianti123 – 1231G → V in dRTA-D. 1 Publication
VAR_021012
Natural varianti124 – 1241R → W in dRTA-D. 1 Publication
VAR_007867
Natural varianti157 – 1571R → C in dRTA-D. 1 Publication
VAR_021013
Natural varianti161 – 1611E → K.1 Publication
Corresponds to variant rs114234874 [ dbSNP | Ensembl ].
VAR_021014
Natural varianti174 – 1741M → R in dRTA-D. 1 Publication
VAR_007868
Natural varianti275 – 2751T → P in dRTA-D. 2 Publications
VAR_007869
Natural varianti316 – 3161G → E in dRTA-D. 1 Publication
VAR_007870
Natural varianti346 – 3461P → R in dRTA-D. 3 Publications
VAR_007871
Natural varianti364 – 3641G → S in dRTA-D. 1 Publication
VAR_007872
Natural varianti465 – 4651R → H in dRTA-D. 1 Publication
Corresponds to variant rs142905621 [ dbSNP | Ensembl ].
VAR_021015

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25809 mRNA. Translation: AAA36498.1. Different initiation.
AK291121 mRNA. Translation: BAF83810.1.
AK313194 mRNA. Translation: BAG36011.1.
AK223151 mRNA. Translation: BAD96871.1.
CH471053 Genomic DNA. Translation: EAW99790.1.
BC063411 mRNA. Translation: AAH63411.1.
CCDSiCCDS1912.1.
PIRiA33281.
RefSeqiNP_001683.2. NM_001692.3.
UniGeneiHs.64173.

Genome annotation databases

EnsembliENST00000234396; ENSP00000234396; ENSG00000116039.
GeneIDi525.
KEGGihsa:525.
UCSCiuc002shi.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25809 mRNA. Translation: AAA36498.1. Different initiation.
AK291121 mRNA. Translation: BAF83810.1.
AK313194 mRNA. Translation: BAG36011.1.
AK223151 mRNA. Translation: BAD96871.1.
CH471053 Genomic DNA. Translation: EAW99790.1.
BC063411 mRNA. Translation: AAH63411.1.
CCDSiCCDS1912.1.
PIRiA33281.
RefSeqiNP_001683.2. NM_001692.3.
UniGeneiHs.64173.

3D structure databases

ProteinModelPortaliP15313.
SMRiP15313. Positions 41-497.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107008. 93 interactions.
IntActiP15313. 3 interactions.
MINTiMINT-8417607.
STRINGi9606.ENSP00000234396.

Chemistry

BindingDBiP15313.
ChEMBLiCHEMBL3217.

Protein family/group databases

TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteiP15313.

Polymorphism and mutation databases

BioMutaiATP6V1B1.
DMDMi215274116.

Proteomic databases

MaxQBiP15313.
PaxDbiP15313.
PRIDEiP15313.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234396; ENSP00000234396; ENSG00000116039.
GeneIDi525.
KEGGihsa:525.
UCSCiuc002shi.1. human.

Organism-specific databases

CTDi525.
GeneCardsiGC02P071162.
HGNCiHGNC:853. ATP6V1B1.
HPAiCAB009523.
HPA031847.
MIMi192132. gene.
267300. phenotype.
neXtProtiNX_P15313.
Orphaneti402041. Autosomal recessive distal renal tubular acidosis.
PharmGKBiPA25154.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1156.
GeneTreeiENSGT00550000074724.
HOGENOMiHOG000165320.
HOVERGENiHBG002176.
InParanoidiP15313.
KOiK02147.
OMAiNEGDITH.
OrthoDBiEOG7NW68Q.
PhylomeDBiP15313.
TreeFamiTF300313.

Enzyme and pathway databases

BioCyciMetaCyc:HS03975-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.
REACT_25300. Ion channel transport.

Miscellaneous databases

GeneWikiiATP6V1B1.
GenomeRNAii525.
NextBioi2179.
PROiP15313.
SOURCEiSearch...

Gene expression databases

BgeeiP15313.
CleanExiHS_ATP6V1B1.
ExpressionAtlasiP15313. baseline and differential.
GenevisibleiP15313. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00310. ATP_synth_B_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR005723. ATPase_V1-cplx_bsu.
IPR027417. P-loop_NTPase.
IPR022879. V-ATPase_su_B/beta.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
PIRSFiPIRSF039114. V-ATPsynth_beta/V-ATPase_B. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human endomembrane H+ pump strongly resembles the ATP-synthetase of Archaebacteria."
    Suedhof T.C., Fried V.A., Stone D.K., Johnston P.A., Xie X.-S.
    Proc. Natl. Acad. Sci. U.S.A. 86:6067-6071(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-30.
    Tissue: Kidney.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  6. "The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ motifs involved in their interaction."
    Pushkin A., Abuladze N., Newman D., Muronets V., Sassani P., Tatishchev S., Kurtz I.
    Am. J. Physiol. 284:C667-C673(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A3R1 AND SLC4A7, DOMAIN, MUTAGENESIS OF LEU-513.
  7. Cited for: VARIANTS DRTA-D PRO-81; TRP-124; ARG-174; PRO-275; GLU-316; ARG-346 AND SER-364, TISSUE SPECIFICITY.
  8. Cited for: VARIANTS DRTA-D PRO-81; VAL-123; CYS-157; PRO-275 AND ARG-346, VARIANTS ILE-30 AND LYS-161.
  9. Cited for: VARIANTS DRTA-D PRO-81; ARG-346 AND HIS-465.

Entry informationi

Entry nameiVATB1_HUMAN
AccessioniPrimary (citable) accession number: P15313
Secondary accession number(s): Q53FY0, Q6P4H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: July 22, 2015
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.