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P15313

- VATB1_HUMAN

UniProt

P15313 - VATB1_HUMAN

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Protein

V-type proton ATPase subunit B, kidney isoform

Gene

ATP6V1B1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. ATP binding Source: InterPro
  2. hydrogen ion transmembrane transporter activity Source: UniProtKB
  3. hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. ATP metabolic process Source: InterPro
  3. calcium ion homeostasis Source: UniProtKB
  4. cellular iron ion homeostasis Source: Reactome
  5. excretion Source: UniProtKB
  6. inner ear morphogenesis Source: UniProtKB
  7. insulin receptor signaling pathway Source: Reactome
  8. interaction with host Source: Reactome
  9. ossification Source: HGNC
  10. phagosome maturation Source: Reactome
  11. pH reduction Source: UniProtKB
  12. proton transport Source: HGNC
  13. regulation of pH Source: HGNC
  14. sensory perception of sound Source: UniProtKB
  15. transferrin transport Source: Reactome
  16. 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.

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: Chromosome 2

Organism-specific databases

HGNCiHGNC:853. ATP6V1B1.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. basolateral plasma membrane Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProtKB
  6. lateral plasma membrane Source: UniProtKB
  7. microvillus Source: UniProtKB
  8. proton-transporting V-type ATPase, V1 domain Source: InterPro
  9. 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) [MIM:267300]: An 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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

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.
GenevestigatoriP15313.

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.
OMAiGIDSQKT.
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]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15313 [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.

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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi215274116.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS1912.1.
PIRi A33281.
RefSeqi NP_001683.2. NM_001692.3.
UniGenei Hs.64173.

3D structure databases

ProteinModelPortali P15313.
SMRi P15313. Positions 41-497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107008. 93 interactions.
IntActi P15313. 3 interactions.
MINTi MINT-8417607.
STRINGi 9606.ENSP00000234396.

Chemistry

BindingDBi P15313.
ChEMBLi CHEMBL3217.

Protein family/group databases

TCDBi 3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSitei P15313.

Polymorphism databases

DMDMi 215274116.

Proteomic databases

MaxQBi P15313.
PaxDbi P15313.
PRIDEi P15313.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000234396 ; ENSP00000234396 ; ENSG00000116039 .
GeneIDi 525.
KEGGi hsa:525.
UCSCi uc002shi.1. human.

Organism-specific databases

CTDi 525.
GeneCardsi GC02P071162.
HGNCi HGNC:853. ATP6V1B1.
HPAi CAB009523.
HPA031847.
MIMi 192132. gene.
267300. phenotype.
neXtProti NX_P15313.
Orphaneti 402041. Autosomal recessive distal renal tubular acidosis.
PharmGKBi PA25154.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1156.
GeneTreei ENSGT00550000074724.
HOGENOMi HOG000165320.
HOVERGENi HBG002176.
InParanoidi P15313.
KOi K02147.
OMAi GIDSQKT.
OrthoDBi EOG7NW68Q.
PhylomeDBi P15313.
TreeFami TF300313.

Enzyme and pathway databases

BioCyci MetaCyc:HS03975-MONOMER.
Reactomei REACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

GeneWikii ATP6V1B1.
GenomeRNAii 525.
NextBioi 2179.
PROi P15313.
SOURCEi Search...

Gene expression databases

Bgeei P15313.
CleanExi HS_ATP6V1B1.
ExpressionAtlasi P15313. baseline and differential.
Genevestigatori P15313.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00310. ATP_synth_B_arch.
InterProi IPR020003. 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 ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 160 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