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Protein

V-type proton ATPase subunit B, brain isoform

Gene

ATP6V1B2

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

  1. ATP binding Source: InterPro
  2. hydrogen ion transmembrane transporter activity Source: ProtInc
  3. proton-transporting ATPase activity, rotational mechanism Source: ProtInc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. ATP metabolic process Source: InterPro
  3. cellular iron ion homeostasis Source: Reactome
  4. insulin receptor signaling pathway Source: Reactome
  5. interaction with host Source: Reactome
  6. phagosome maturation Source: Reactome
  7. proton transport Source: ProtInc
  8. transferrin transport Source: Reactome
  9. 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:HS07429-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, brain isoform
Short name:
V-ATPase subunit B 2
Alternative name(s):
Endomembrane proton pump 58 kDa subunit
HO57
Vacuolar proton pump subunit B 2
Gene namesi
Name:ATP6V1B2
Synonyms:ATP6B2, VPP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:854. ATP6V1B2.

Subcellular locationi

Endomembrane system; Peripheral membrane protein. Melanosome
Note: Endomembrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. endomembrane system Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProtKB
  4. integral component of membrane Source: Ensembl
  5. intracellular membrane-bounded organelle Source: HPA
  6. lysosomal membrane Source: UniProtKB
  7. melanosome Source: UniProtKB-SubCell
  8. microvillus Source: Ensembl
  9. plasma membrane Source: UniProtKB
  10. proton-transporting V-type ATPase, V1 domain Source: InterPro
  11. ruffle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti79499. Autosomal dominant deafness-onychodystrophy syndrome.
PharmGKBiPA25155.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511V-type proton ATPase subunit B, brain isoformPRO_0000144626Add
BLAST

Proteomic databases

MaxQBiP21281.
PaxDbiP21281.
PeptideAtlasiP21281.
PRIDEiP21281.

2D gel databases

REPRODUCTION-2DPAGEIPI00007812.

PTM databases

PhosphoSiteiP21281.

Expressioni

Gene expression databases

BgeeiP21281.
CleanExiHS_ATP6V1B2.
ExpressionAtlasiP21281. baseline and differential.
GenevestigatoriP21281.

Organism-specific databases

HPAiHPA008147.

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).

Protein-protein interaction databases

BioGridi107009. 69 interactions.
IntActiP21281. 5 interactions.
MINTiMINT-5004128.
STRINGi9606.ENSP00000276390.

Structurei

3D structure databases

ProteinModelPortaliP21281.
SMRiP21281. Positions 55-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiCOG1156.
GeneTreeiENSGT00550000074724.
HOGENOMiHOG000165320.
HOVERGENiHBG002176.
InParanoidiP21281.
KOiK02147.
OMAiWRERRYL.
OrthoDBiEOG7NW68Q.
PhylomeDBiP21281.
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.

P21281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRAMRGIV NGAAPELPVP TGGPAVGARE QALAVSRNYL SQPRLTYKTV
60 70 80 90 100
SGVNGPLVIL DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE
110 120 130 140 150
GTSGIDAKKT SCEFTGDILR TPVSEDMLGR VFNGSGKPID RGPVVLAEDF
160 170 180 190 200
LDIMGQPINP QCRIYPEEMI QTGISAIDGM NSIARGQKIP IFSAAGLPHN
210 220 230 240 250
EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET ARFFKSDFEE
260 270 280 290 300
NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM
310 320 330 340 350
SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ
360 370 380 390 400
IPILTMPNDD ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR
410 420 430 440 450
LMKSAIGEGM TRKDHADVSN QLYACYAIGK DVQAMKAVVG EEALTSDDLL
460 470 480 490 500
YLEFLQKFER NFIAQGPYEN RTVFETLDIG WQLLRIFPKE MLKRIPQSTL
510
SEFYPRDSAK H
Length:511
Mass (Da):56,501
Last modified:December 1, 2000 - v3
Checksum:iE01E85BBA36E5DED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281A → S in CAA44721 (PubMed:1373501).Curated
Sequence conflicti29 – 291R → Q in AAH30640 (PubMed:15489334).Curated
Sequence conflicti171 – 1711Q → R in AAH30640 (PubMed:15489334).Curated
Sequence conflicti342 – 3421E → G in AAH30640 (PubMed:15489334).Curated
Sequence conflicti376 – 3761Q → L in AAA58661 (PubMed:7945239).Curated
Sequence conflicti424 – 4252AC → RA in AAA35610 (PubMed:2145275).Curated
Sequence conflicti435 – 4351M → V in AAA35610 (PubMed:2145275).Curated
Sequence conflicti510 – 5112KH → ND in AAA35610 (PubMed:2145275).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60346 mRNA. Translation: AAA35610.1.
L35249 mRNA. Translation: AAA58661.1.
AK312372 mRNA. Translation: BAG35290.1.
CH471080 Genomic DNA. Translation: EAW63758.1.
CH471080 Genomic DNA. Translation: EAW63759.1.
BC003100 mRNA. Translation: AAH03100.1.
BC007309 mRNA. Translation: AAH07309.1.
BC030640 mRNA. Translation: AAH30640.1.
Z37165 Genomic DNA. Translation: CAA85522.1.
X62949 mRNA. Translation: CAA44721.1.
CCDSiCCDS6014.1.
PIRiB44138.
I39208.
RefSeqiNP_001684.2. NM_001693.3.
UniGeneiHs.295917.

Genome annotation databases

EnsembliENST00000276390; ENSP00000276390; ENSG00000147416.
GeneIDi526.
KEGGihsa:526.
UCSCiuc003wzp.3. human.

Polymorphism databases

DMDMi12643271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60346 mRNA. Translation: AAA35610.1.
L35249 mRNA. Translation: AAA58661.1.
AK312372 mRNA. Translation: BAG35290.1.
CH471080 Genomic DNA. Translation: EAW63758.1.
CH471080 Genomic DNA. Translation: EAW63759.1.
BC003100 mRNA. Translation: AAH03100.1.
BC007309 mRNA. Translation: AAH07309.1.
BC030640 mRNA. Translation: AAH30640.1.
Z37165 Genomic DNA. Translation: CAA85522.1.
X62949 mRNA. Translation: CAA44721.1.
CCDSiCCDS6014.1.
PIRiB44138.
I39208.
RefSeqiNP_001684.2. NM_001693.3.
UniGeneiHs.295917.

3D structure databases

ProteinModelPortaliP21281.
SMRiP21281. Positions 55-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107009. 69 interactions.
IntActiP21281. 5 interactions.
MINTiMINT-5004128.
STRINGi9606.ENSP00000276390.

Chemistry

BindingDBiP21281.
ChEMBLiCHEMBL5641.
DrugBankiDB05260. Gallium nitrate.

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

PhosphoSiteiP21281.

Polymorphism databases

DMDMi12643271.

2D gel databases

REPRODUCTION-2DPAGEIPI00007812.

Proteomic databases

MaxQBiP21281.
PaxDbiP21281.
PeptideAtlasiP21281.
PRIDEiP21281.

Protocols and materials databases

DNASUi526.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276390; ENSP00000276390; ENSG00000147416.
GeneIDi526.
KEGGihsa:526.
UCSCiuc003wzp.3. human.

Organism-specific databases

CTDi526.
GeneCardsiGC08P020054.
HGNCiHGNC:854. ATP6V1B2.
HPAiHPA008147.
MIMi606939. gene.
neXtProtiNX_P21281.
Orphaneti79499. Autosomal dominant deafness-onychodystrophy syndrome.
PharmGKBiPA25155.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1156.
GeneTreeiENSGT00550000074724.
HOGENOMiHOG000165320.
HOVERGENiHBG002176.
InParanoidiP21281.
KOiK02147.
OMAiWRERRYL.
OrthoDBiEOG7NW68Q.
PhylomeDBiP21281.
TreeFamiTF300313.

Enzyme and pathway databases

BioCyciMetaCyc:HS07429-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSiATP6V1B2. human.
GeneWikiiATP6V1B2.
GenomeRNAii526.
NextBioi2183.
PROiP21281.
SOURCEiSearch...

Gene expression databases

BgeeiP21281.
CleanExiHS_ATP6V1B2.
ExpressionAtlasiP21281. baseline and differential.
GenevestigatoriP21281.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells."
    Nelson R.D., Guo X.-L., Masood K., Brown D., Kalkbrenner M., Gluck S.
    Proc. Natl. Acad. Sci. U.S.A. 89:3541-3545(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Heterogeneity of vacuolar H(+)-ATPase: differential expression of two human subunit B isoforms."
    van Hille B., Richener H., Schmid P., Puettner I., Green J.R., Bilbe G.
    Biochem. J. 303:191-198(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Tissue: Amygdala.
  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: Brain and Eye.
  6. "Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit gene in differentiating THP-1 cells."
    Lee B.S., Underhill D.M., Crane M.K., Gluck S.L.
    J. Biol. Chem. 270:7320-7329(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
  7. "An mRNA from human brain encodes an isoform of the B subunit of the vacuolar H(+)-ATPase."
    Bernasconi P., Rausch T., Struve I., Morgan L., Taiz L.
    J. Biol. Chem. 265:17428-17431(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-511.
    Tissue: Brain.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVATB2_HUMAN
AccessioniPrimary (citable) accession number: P21281
Secondary accession number(s): B2R5Z3
, D3DSQ5, Q14544, Q15859, Q96IR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: December 1, 2000
Last modified: March 4, 2015
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 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.