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Protein

V-type proton ATPase subunit B, brain isoform

Gene

Atp6v1b2

Organism
Mus musculus (Mouse)
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. 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.
REACT_233181. Insulin receptor recycling.

Protein family/group databases

TCDBi3.A.2.2.6. 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
Vacuolar proton pump subunit B 2
Gene namesi
Name:Atp6v1b2
Synonyms:Atp6b2, Vat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:109618. Atp6v1b2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511V-type proton ATPase subunit B, brain isoformPRO_0000144627Add
BLAST

Proteomic databases

MaxQBiP62814.
PaxDbiP62814.
PRIDEiP62814.

2D gel databases

REPRODUCTION-2DPAGEP62814.
UCD-2DPAGEP62814.

PTM databases

PhosphoSiteiP62814.

Expressioni

Gene expression databases

BgeeiP62814.
CleanExiMM_ATP6V1B2.
ExpressionAtlasiP62814. baseline and differential.
GenevestigatoriP62814.

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

BioGridi198262. 1 interaction.
IntActiP62814. 7 interactions.
MINTiMINT-4139762.

Structurei

3D structure databases

ProteinModelPortaliP62814.
SMRiP62814. Positions 55-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Phylogenomic databases

eggNOGiCOG1156.
GeneTreeiENSGT00550000074724.
HOVERGENiHBG002176.
InParanoidiP62814.
KOiK02147.
OMAiWRERRYL.
OrthoDBiEOG7NW68Q.
PhylomeDBiP62814.
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.

P62814-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRAMRGIV NGAAPELPVP TGGPMAGARE 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
YLEFLQKFEK NFITQGPYEN RTVYETLDIG WQLLRIFPKE MLKRIPQSTL
510
SEFYPRDSAK H
Length:511
Mass (Da):56,551
Last modified:August 16, 2004 - v1
Checksum:iE116BF9A36EEF36B
GO

Sequence cautioni

The sequence BAE30303.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE30526.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE31441.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 232GG → RP in AAC52411 (PubMed:8741845).Curated
Sequence conflicti36 – 361S → G in AAC52411 (PubMed:8741845).Curated
Sequence conflicti80 – 801T → A in BAE35206 (PubMed:16141072).Curated
Sequence conflicti85 – 862QV → AS in AAC52411 (PubMed:8741845).Curated
Sequence conflicti262 – 2643NLA → ILP in AAC52411 (PubMed:8741845).Curated
Sequence conflicti270 – 2701E → K in BAE35536 (PubMed:16141072).Curated
Sequence conflicti270 – 2701E → K in BAE35612 (PubMed:16141072).Curated
Sequence conflicti276 – 2761R → C in AAC52411 (PubMed:8741845).Curated
Sequence conflicti300 – 3001M → T in AAC52411 (PubMed:8741845).Curated
Sequence conflicti304 – 3041A → P in AAC52411 (PubMed:8741845).Curated
Sequence conflicti318 – 3181P → H in BAE35536 (PubMed:16141072).Curated
Sequence conflicti318 – 3181P → H in BAE35612 (PubMed:16141072).Curated
Sequence conflicti365 – 3651I → M in BAE40674 (PubMed:16141072).Curated
Sequence conflicti371 – 3711Y → C in BAE35206 (PubMed:16141072).Curated
Sequence conflicti373 – 3731T → I in BAE30303 (PubMed:16141072).Curated
Sequence conflicti373 – 3731T → I in BAE30526 (PubMed:16141072).Curated
Sequence conflicti405 – 4051A → P in AAC52411 (PubMed:8741845).Curated
Sequence conflicti437 – 4371A → V in BAE30197 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13838 Genomic DNA. Translation: AAC52411.1.
Y12634 mRNA. Translation: CAA73182.1.
AK146499 mRNA. Translation: BAE27215.1.
AK151200 mRNA. Translation: BAE30197.1.
AK151322 mRNA. Translation: BAE30303.1. Different initiation.
AK151586 mRNA. Translation: BAE30526.1. Different initiation.
AK152718 mRNA. Translation: BAE31441.1. Different initiation.
AK152766 mRNA. Translation: BAE31479.1.
AK159133 mRNA. Translation: BAE34845.1.
AK159153 mRNA. Translation: BAE34860.1.
AK159586 mRNA. Translation: BAE35206.1.
AK159701 mRNA. Translation: BAE35300.1.
AK159986 mRNA. Translation: BAE35536.1.
AK160080 mRNA. Translation: BAE35612.1.
AK160854 mRNA. Translation: BAE36047.1.
AK166669 mRNA. Translation: BAE38930.1.
AK168852 mRNA. Translation: BAE40674.1.
AK169155 mRNA. Translation: BAE40934.1.
AK169270 mRNA. Translation: BAE41031.1.
BC012497 mRNA. Translation: AAH12497.1.
BC046302 mRNA. Translation: AAH46302.1.
BC085300 mRNA. Translation: AAH85300.1.
CCDSiCCDS40358.1.
RefSeqiNP_031535.2. NM_007509.3.
UniGeneiMm.249096.

Genome annotation databases

EnsembliENSMUST00000006435; ENSMUSP00000006435; ENSMUSG00000006273.
GeneIDi11966.
KEGGimmu:11966.
UCSCiuc009lww.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13838 Genomic DNA. Translation: AAC52411.1.
Y12634 mRNA. Translation: CAA73182.1.
AK146499 mRNA. Translation: BAE27215.1.
AK151200 mRNA. Translation: BAE30197.1.
AK151322 mRNA. Translation: BAE30303.1. Different initiation.
AK151586 mRNA. Translation: BAE30526.1. Different initiation.
AK152718 mRNA. Translation: BAE31441.1. Different initiation.
AK152766 mRNA. Translation: BAE31479.1.
AK159133 mRNA. Translation: BAE34845.1.
AK159153 mRNA. Translation: BAE34860.1.
AK159586 mRNA. Translation: BAE35206.1.
AK159701 mRNA. Translation: BAE35300.1.
AK159986 mRNA. Translation: BAE35536.1.
AK160080 mRNA. Translation: BAE35612.1.
AK160854 mRNA. Translation: BAE36047.1.
AK166669 mRNA. Translation: BAE38930.1.
AK168852 mRNA. Translation: BAE40674.1.
AK169155 mRNA. Translation: BAE40934.1.
AK169270 mRNA. Translation: BAE41031.1.
BC012497 mRNA. Translation: AAH12497.1.
BC046302 mRNA. Translation: AAH46302.1.
BC085300 mRNA. Translation: AAH85300.1.
CCDSiCCDS40358.1.
RefSeqiNP_031535.2. NM_007509.3.
UniGeneiMm.249096.

3D structure databases

ProteinModelPortaliP62814.
SMRiP62814. Positions 55-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198262. 1 interaction.
IntActiP62814. 7 interactions.
MINTiMINT-4139762.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteiP62814.

2D gel databases

REPRODUCTION-2DPAGEP62814.
UCD-2DPAGEP62814.

Proteomic databases

MaxQBiP62814.
PaxDbiP62814.
PRIDEiP62814.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006435; ENSMUSP00000006435; ENSMUSG00000006273.
GeneIDi11966.
KEGGimmu:11966.
UCSCiuc009lww.2. mouse.

Organism-specific databases

CTDi526.
MGIiMGI:109618. Atp6v1b2.

Phylogenomic databases

eggNOGiCOG1156.
GeneTreeiENSGT00550000074724.
HOVERGENiHBG002176.
InParanoidiP62814.
KOiK02147.
OMAiWRERRYL.
OrthoDBiEOG7NW68Q.
PhylomeDBiP62814.
TreeFamiTF300313.

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.
REACT_233181. Insulin receptor recycling.

Miscellaneous databases

ChiTaRSiAtp6v1b2. mouse.
NextBioi280091.
PROiP62814.
SOURCEiSearch...

Gene expression databases

BgeeiP62814.
CleanExiMM_ATP6V1B2.
ExpressionAtlasiP62814. baseline and differential.
GenevestigatoriP62814.

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. "Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts."
    Laitala T., Howell M.L., Dean G.E., Vaananen H.K.
    Mol. Biol. Cell 7:129-142(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Antisense technology and bone resorption."
    Westberg M.S., Lundberg L.G.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Bone marrow, Brain and Heart.
  4. "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: Eye and Olfactory epithelium.
  5. Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 49-64; 68-130; 164-185; 189-208; 277-308; 322-337; 387-400; 404-430; 437-457; 461-485 AND 495-506, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.

Entry informationi

Entry nameiVATB2_MOUSE
AccessioniPrimary (citable) accession number: P62814
Secondary accession number(s): O09045
, P50517, Q3TG74, Q3TL62, Q3TVK6, Q3TWR0, Q3U791, Q3U7C8, Q3U9Z0, Q3UAW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: February 4, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.