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P62814 (VATB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Atp6v1b2
Synonyms:Atp6b2, Vat2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00310

Subunit structure

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).

Subcellular location

Endomembrane system; Peripheral membrane protein. Melanosome By similarity. Note: Endomembrane. HAMAP-Rule MF_00310

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence caution

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

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511V-type proton ATPase subunit B, brain isoform HAMAP-Rule MF_00310
PRO_0000144627

Experimental info

Sequence conflict22 – 232GG → RP in AAC52411. Ref.1
Sequence conflict361S → G in AAC52411. Ref.1
Sequence conflict801T → A in BAE35206. Ref.3
Sequence conflict85 – 862QV → AS in AAC52411. Ref.1
Sequence conflict262 – 2643NLA → ILP in AAC52411. Ref.1
Sequence conflict2701E → K in BAE35536. Ref.3
Sequence conflict2701E → K in BAE35612. Ref.3
Sequence conflict2761R → C in AAC52411. Ref.1
Sequence conflict3001M → T in AAC52411. Ref.1
Sequence conflict3041A → P in AAC52411. Ref.1
Sequence conflict3181P → H in BAE35536. Ref.3
Sequence conflict3181P → H in BAE35612. Ref.3
Sequence conflict3651I → M in BAE40674. Ref.3
Sequence conflict3711Y → C in BAE35206. Ref.3
Sequence conflict3731T → I in BAE30303. Ref.3
Sequence conflict3731T → I in BAE30526. Ref.3
Sequence conflict4051A → P in AAC52411. Ref.1
Sequence conflict4371A → V in BAE30197. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P62814 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: E116BF9A36EEF36B

FASTA51156,551
        10         20         30         40         50         60 
MALRAMRGIV NGAAPELPVP TGGPMAGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL 

        70         80         90        100        110        120 
DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR 

       130        140        150        160        170        180 
TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM 

       190        200        210        220        230        240 
NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET 

       250        260        270        280        290        300 
ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM 

       310        320        330        340        350        360 
SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD 

       370        380        390        400        410        420 
ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN 

       430        440        450        460        470        480 
QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFEK NFITQGPYEN RTVYETLDIG 

       490        500        510 
WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS40358.1.
RefSeqNP_031535.2. NM_007509.3.
UniGeneMm.249096.

3D structure databases

ProteinModelPortalP62814.
SMRP62814. Positions 55-505.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198262. 1 interaction.
IntActP62814. 7 interactions.
MINTMINT-4139762.

Protein family/group databases

TCDB3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteP62814.

2D gel databases

REPRODUCTION-2DPAGEP62814.
UCD-2DPAGEP62814.

Proteomic databases

MaxQBP62814.
PaxDbP62814.
PRIDEP62814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006435; ENSMUSP00000006435; ENSMUSG00000006273.
GeneID11966.
KEGGmmu:11966.
UCSCuc009lww.2. mouse.

Organism-specific databases

CTD526.
MGIMGI:109618. Atp6v1b2.

Phylogenomic databases

eggNOGCOG1156.
GeneTreeENSGT00550000074724.
HOVERGENHBG002176.
InParanoidP62814.
KOK02147.
OMATVCEFTG.
OrthoDBEOG7NW68Q.
PhylomeDBP62814.
TreeFamTF300313.

Gene expression databases

ArrayExpressP62814.
BgeeP62814.
CleanExMM_ATP6V1B2.
GenevestigatorP62814.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00310. ATP_synth_B_arch.
InterProIPR020003. 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]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01040. V-ATPase_V1_B. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP6V1B2. mouse.
NextBio280091.
PROP62814.
SOURCESearch...

Entry information

Entry nameVATB2_MOUSE
AccessionPrimary (citable) accession number: P62814
Secondary accession number(s): O09045 expand/collapse secondary AC list , P50517, Q3TG74, Q3TL62, Q3TVK6, Q3TWR0, Q3U791, Q3U7C8, Q3U9Z0, Q3UAW7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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