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P15313

- VATB1_HUMAN

UniProt

P15313 - VATB1_HUMAN

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
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    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

    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. endomembrane system Source: UniProtKB-SubCell
    6. extracellular vesicular exosome Source: UniProt
    7. lateral plasma membrane Source: UniProtKB
    8. microvillus Source: UniProtKB
    9. proton-transporting V-type ATPase, V1 domain Source: InterPro
    10. vacuolar proton-transporting V-type ATPase complex Source: HGNC

    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.
    Orphaneti93611. Autosomal recessive distal renal tubular acidosis with deafness.
    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

    ArrayExpressiP15313.
    BgeeiP15313.
    CleanExiHS_ATP6V1B1.
    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. 81 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.
    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.

    P15313-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMEIDSRPG GLPGSSCNLG AAREHMQAVT RNYITHPRVT YRTVCSVNGP    50
    LVVLDRVKFA QYAEIVHFTL PDGTQRSGQV LEVAGTKAIV QVFEGTSGID 100
    ARKTTCEFTG DILRTPVSED MLGRVFNGSG KPIDKGPVVM AEDFLDINGQ 150
    PINPHSRIYP EEMIQTGISP IDVMNSIARG QKIPIFSAAG LPHNEIAAQI 200
    CRQAGLVKKS KAVLDYHDDN FAIVFAAMGV NMETARFFKS DFEQNGTMGN 250
    VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA 300
    LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM 350
    PNDDITHPIP DLTGFITEGQ IYVDRQLHNR QIYPPINVLP SLSRLMKSAI 400
    GEGMTRKDHG DVSNQLYACY AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ 450
    KFEKNFINQG PYENRSVFES LDLGWKLLRI FPKEMLKRIP QAVIDEFYSR 500
    EGALQDLAPD TAL 513
    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. 81 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 93611. Autosomal recessive distal renal tubular acidosis with deafness.
    PharmGKBi PA25154.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1156.
    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

    ArrayExpressi P15313.
    Bgeei P15313.
    CleanExi HS_ATP6V1B1.
    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

    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 1, 2014
    This is version 159 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