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P21281

- VATB2_HUMAN

UniProt

P21281 - VATB2_HUMAN

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Protein

V-type proton ATPase subunit B, brain isoform

Gene

ATP6V1B2

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: ProtInc
  3. proton-transporting ATPase activity, rotational mechanism Source: ProtInc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular iron ion homeostasis Source: Reactome
  3. insulin receptor signaling pathway Source: Reactome
  4. interaction with host Source: Reactome
  5. phagosome maturation Source: Reactome
  6. proton transport Source: ProtInc
  7. transferrin transport Source: Reactome
  8. 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. extracellular vesicular exosome Source: UniProtKB
  3. integral component of membrane Source: Ensembl
  4. intracellular membrane-bounded organelle Source: HPA
  5. lysosomal membrane Source: UniProtKB
  6. microvillus Source: Ensembl
  7. plasma membrane Source: UniProtKB
  8. proton-transporting V-type ATPase, V1 domain Source: InterPro
  9. ruffle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

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. 66 interactions.
IntActiP21281. 4 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.
OMAiTVCEFTG.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6014.1.
PIRi B44138.
I39208.
RefSeqi NP_001684.2. NM_001693.3.
UniGenei Hs.295917.

3D structure databases

ProteinModelPortali P21281.
SMRi P21281. Positions 55-505.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107009. 66 interactions.
IntActi P21281. 4 interactions.
MINTi MINT-5004128.
STRINGi 9606.ENSP00000276390.

Chemistry

BindingDBi P21281.
ChEMBLi CHEMBL5641.
DrugBanki DB05260. Gallium nitrate.

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 P21281.

Polymorphism databases

DMDMi 12643271.

2D gel databases

REPRODUCTION-2DPAGE IPI00007812.

Proteomic databases

MaxQBi P21281.
PaxDbi P21281.
PeptideAtlasi P21281.
PRIDEi P21281.

Protocols and materials databases

DNASUi 526.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000276390 ; ENSP00000276390 ; ENSG00000147416 .
GeneIDi 526.
KEGGi hsa:526.
UCSCi uc003wzp.3. human.

Organism-specific databases

CTDi 526.
GeneCardsi GC08P020054.
HGNCi HGNC:854. ATP6V1B2.
HPAi HPA008147.
MIMi 606939. gene.
neXtProti NX_P21281.
PharmGKBi PA25155.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1156.
GeneTreei ENSGT00550000074724.
HOGENOMi HOG000165320.
HOVERGENi HBG002176.
InParanoidi P21281.
KOi K02147.
OMAi TVCEFTG.
OrthoDBi EOG7NW68Q.
PhylomeDBi P21281.
TreeFami TF300313.

Enzyme and pathway databases

BioCyci MetaCyc:HS07429-MONOMER.
Reactomei REACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

GeneWikii ATP6V1B2.
GenomeRNAii 526.
NextBioi 2183.
PROi P21281.
SOURCEi Search...

Gene expression databases

Bgeei P21281.
CleanExi HS_ATP6V1B2.
ExpressionAtlasi P21281. baseline and differential.
Genevestigatori P21281.

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. "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: October 29, 2014
This is version 156 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