Full text data of ATP6V1B2
ATP6V1B2
(ATP6B2, VPP3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
V-type proton ATPase subunit B, brain isoform; V-ATPase subunit B 2 (Endomembrane proton pump 58 kDa subunit; HO57; Vacuolar proton pump subunit B 2)
V-type proton ATPase subunit B, brain isoform; V-ATPase subunit B 2 (Endomembrane proton pump 58 kDa subunit; HO57; Vacuolar proton pump subunit B 2)
UniProt
P21281
ID VATB2_HUMAN Reviewed; 511 AA.
AC P21281; B2R5Z3; D3DSQ5; Q14544; Q15859; Q96IR0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 3.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=V-type proton ATPase subunit B, brain isoform;
DE Short=V-ATPase subunit B 2;
DE AltName: Full=Endomembrane proton pump 58 kDa subunit;
DE AltName: Full=HO57;
DE AltName: Full=Vacuolar proton pump subunit B 2;
GN Name=ATP6V1B2; Synonyms=ATP6B2, VPP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=1373501; DOI=10.1073/pnas.89.8.3541;
RA Nelson R.D., Guo X.-L., Masood K., Brown D., Kalkbrenner M., Gluck S.;
RT "Selectively amplified expression of an isoform of the vacuolar H(+)-
RT ATPase 56-kilodalton subunit in renal intercalated cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3541-3545(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7945239;
RA van Hille B., Richener H., Schmid P., Puettner I., Green J.R.,
RA Bilbe G.;
RT "Heterogeneity of vacuolar H(+)-ATPase: differential expression of two
RT human subunit B isoforms.";
RL Biochem. J. 303:191-198(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX PubMed=7706273; DOI=10.1074/jbc.270.13.7320;
RA Lee B.S., Underhill D.M., Crane M.K., Gluck S.L.;
RT "Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit
RT gene in differentiating THP-1 cells.";
RL J. Biol. Chem. 270:7320-7329(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-511.
RC TISSUE=Brain;
RX PubMed=2145275;
RA Bernasconi P., Rausch T., Struve I., Morgan L., Taiz L.;
RT "An mRNA from human brain encodes an isoform of the B subunit of the
RT vacuolar H(+)-ATPase.";
RL J. Biol. Chem. 265:17428-17431(1990).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Non-catalytic subunit of the peripheral V1 complex of
CC vacuolar ATPase. V-ATPase is responsible for acidifying a variety
CC of intracellular compartments in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (main components: subunits A, B,
CC C, D, E, and F) attached to an integral membrane V0 proton pore
CC complex (main component: the proteolipid protein).
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC protein. Melanosome. Note=Endomembrane. Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
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DR EMBL; M60346; AAA35610.1; -; mRNA.
DR EMBL; L35249; AAA58661.1; -; mRNA.
DR EMBL; AK312372; BAG35290.1; -; mRNA.
DR EMBL; CH471080; EAW63758.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63759.1; -; Genomic_DNA.
DR EMBL; BC003100; AAH03100.1; -; mRNA.
DR EMBL; BC007309; AAH07309.1; -; mRNA.
DR EMBL; BC030640; AAH30640.1; -; mRNA.
DR EMBL; Z37165; CAA85522.1; -; Genomic_DNA.
DR EMBL; X62949; CAA44721.1; -; mRNA.
DR PIR; B44138; B44138.
DR PIR; I39208; I39208.
DR RefSeq; NP_001684.2; NM_001693.3.
DR UniGene; Hs.295917; -.
DR ProteinModelPortal; P21281; -.
DR SMR; P21281; 55-505.
DR IntAct; P21281; 4.
DR MINT; MINT-5004128; -.
DR STRING; 9606.ENSP00000276390; -.
DR BindingDB; P21281; -.
DR ChEMBL; CHEMBL5641; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; P21281; -.
DR DMDM; 12643271; -.
DR REPRODUCTION-2DPAGE; IPI00007812; -.
DR PaxDb; P21281; -.
DR PeptideAtlas; P21281; -.
DR PRIDE; P21281; -.
DR DNASU; 526; -.
DR Ensembl; ENST00000276390; ENSP00000276390; ENSG00000147416.
DR GeneID; 526; -.
DR KEGG; hsa:526; -.
DR UCSC; uc003wzp.3; human.
DR CTD; 526; -.
DR GeneCards; GC08P020054; -.
DR HGNC; HGNC:854; ATP6V1B2.
DR HPA; HPA008147; -.
DR MIM; 606939; gene.
DR neXtProt; NX_P21281; -.
DR PharmGKB; PA25155; -.
DR eggNOG; COG1156; -.
DR HOGENOM; HOG000165320; -.
DR HOVERGEN; HBG002176; -.
DR InParanoid; P21281; -.
DR KO; K02147; -.
DR OMA; ETMKMPV; -.
DR OrthoDB; EOG7NW68Q; -.
DR PhylomeDB; P21281; -.
DR BioCyc; MetaCyc:HS07429-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V1B2; -.
DR GenomeRNAi; 526; -.
DR NextBio; 2183; -.
DR PRO; PR:P21281; -.
DR ArrayExpress; P21281; -.
DR Bgee; P21281; -.
DR CleanEx; HS_ATP6V1B2; -.
DR Genevestigator; P21281; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral to membrane; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:ProtInc.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR004100; ATPase_F1_a/bsu_N.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport;
KW Membrane; Reference proteome; Transport.
FT CHAIN 1 511 V-type proton ATPase subunit B, brain
FT isoform.
FT /FTId=PRO_0000144626.
FT CONFLICT 28 28 A -> S (in Ref. 1; CAA44721).
FT CONFLICT 29 29 R -> Q (in Ref. 5; AAH30640).
FT CONFLICT 171 171 Q -> R (in Ref. 5; AAH30640).
FT CONFLICT 342 342 E -> G (in Ref. 5; AAH30640).
FT CONFLICT 376 376 Q -> L (in Ref. 2; AAA58661).
FT CONFLICT 424 425 AC -> RA (in Ref. 7; AAA35610).
FT CONFLICT 435 435 M -> V (in Ref. 7; AAA35610).
FT CONFLICT 510 511 KH -> ND (in Ref. 7; AAA35610).
SQ SEQUENCE 511 AA; 56501 MW; E01E85BBA36E5DED CRC64;
MALRAMRGIV NGAAPELPVP TGGPAVGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL
DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR
TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM
NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET
ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM
SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD
ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN
QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFER NFIAQGPYEN RTVFETLDIG
WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H
//
ID VATB2_HUMAN Reviewed; 511 AA.
AC P21281; B2R5Z3; D3DSQ5; Q14544; Q15859; Q96IR0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 3.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=V-type proton ATPase subunit B, brain isoform;
DE Short=V-ATPase subunit B 2;
DE AltName: Full=Endomembrane proton pump 58 kDa subunit;
DE AltName: Full=HO57;
DE AltName: Full=Vacuolar proton pump subunit B 2;
GN Name=ATP6V1B2; Synonyms=ATP6B2, VPP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=1373501; DOI=10.1073/pnas.89.8.3541;
RA Nelson R.D., Guo X.-L., Masood K., Brown D., Kalkbrenner M., Gluck S.;
RT "Selectively amplified expression of an isoform of the vacuolar H(+)-
RT ATPase 56-kilodalton subunit in renal intercalated cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3541-3545(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7945239;
RA van Hille B., Richener H., Schmid P., Puettner I., Green J.R.,
RA Bilbe G.;
RT "Heterogeneity of vacuolar H(+)-ATPase: differential expression of two
RT human subunit B isoforms.";
RL Biochem. J. 303:191-198(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX PubMed=7706273; DOI=10.1074/jbc.270.13.7320;
RA Lee B.S., Underhill D.M., Crane M.K., Gluck S.L.;
RT "Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit
RT gene in differentiating THP-1 cells.";
RL J. Biol. Chem. 270:7320-7329(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-511.
RC TISSUE=Brain;
RX PubMed=2145275;
RA Bernasconi P., Rausch T., Struve I., Morgan L., Taiz L.;
RT "An mRNA from human brain encodes an isoform of the B subunit of the
RT vacuolar H(+)-ATPase.";
RL J. Biol. Chem. 265:17428-17431(1990).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Non-catalytic subunit of the peripheral V1 complex of
CC vacuolar ATPase. V-ATPase is responsible for acidifying a variety
CC of intracellular compartments in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (main components: subunits A, B,
CC C, D, E, and F) attached to an integral membrane V0 proton pore
CC complex (main component: the proteolipid protein).
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC protein. Melanosome. Note=Endomembrane. Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
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DR EMBL; M60346; AAA35610.1; -; mRNA.
DR EMBL; L35249; AAA58661.1; -; mRNA.
DR EMBL; AK312372; BAG35290.1; -; mRNA.
DR EMBL; CH471080; EAW63758.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63759.1; -; Genomic_DNA.
DR EMBL; BC003100; AAH03100.1; -; mRNA.
DR EMBL; BC007309; AAH07309.1; -; mRNA.
DR EMBL; BC030640; AAH30640.1; -; mRNA.
DR EMBL; Z37165; CAA85522.1; -; Genomic_DNA.
DR EMBL; X62949; CAA44721.1; -; mRNA.
DR PIR; B44138; B44138.
DR PIR; I39208; I39208.
DR RefSeq; NP_001684.2; NM_001693.3.
DR UniGene; Hs.295917; -.
DR ProteinModelPortal; P21281; -.
DR SMR; P21281; 55-505.
DR IntAct; P21281; 4.
DR MINT; MINT-5004128; -.
DR STRING; 9606.ENSP00000276390; -.
DR BindingDB; P21281; -.
DR ChEMBL; CHEMBL5641; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; P21281; -.
DR DMDM; 12643271; -.
DR REPRODUCTION-2DPAGE; IPI00007812; -.
DR PaxDb; P21281; -.
DR PeptideAtlas; P21281; -.
DR PRIDE; P21281; -.
DR DNASU; 526; -.
DR Ensembl; ENST00000276390; ENSP00000276390; ENSG00000147416.
DR GeneID; 526; -.
DR KEGG; hsa:526; -.
DR UCSC; uc003wzp.3; human.
DR CTD; 526; -.
DR GeneCards; GC08P020054; -.
DR HGNC; HGNC:854; ATP6V1B2.
DR HPA; HPA008147; -.
DR MIM; 606939; gene.
DR neXtProt; NX_P21281; -.
DR PharmGKB; PA25155; -.
DR eggNOG; COG1156; -.
DR HOGENOM; HOG000165320; -.
DR HOVERGEN; HBG002176; -.
DR InParanoid; P21281; -.
DR KO; K02147; -.
DR OMA; ETMKMPV; -.
DR OrthoDB; EOG7NW68Q; -.
DR PhylomeDB; P21281; -.
DR BioCyc; MetaCyc:HS07429-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V1B2; -.
DR GenomeRNAi; 526; -.
DR NextBio; 2183; -.
DR PRO; PR:P21281; -.
DR ArrayExpress; P21281; -.
DR Bgee; P21281; -.
DR CleanEx; HS_ATP6V1B2; -.
DR Genevestigator; P21281; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral to membrane; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:ProtInc.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR004100; ATPase_F1_a/bsu_N.
DR InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport;
KW Membrane; Reference proteome; Transport.
FT CHAIN 1 511 V-type proton ATPase subunit B, brain
FT isoform.
FT /FTId=PRO_0000144626.
FT CONFLICT 28 28 A -> S (in Ref. 1; CAA44721).
FT CONFLICT 29 29 R -> Q (in Ref. 5; AAH30640).
FT CONFLICT 171 171 Q -> R (in Ref. 5; AAH30640).
FT CONFLICT 342 342 E -> G (in Ref. 5; AAH30640).
FT CONFLICT 376 376 Q -> L (in Ref. 2; AAA58661).
FT CONFLICT 424 425 AC -> RA (in Ref. 7; AAA35610).
FT CONFLICT 435 435 M -> V (in Ref. 7; AAA35610).
FT CONFLICT 510 511 KH -> ND (in Ref. 7; AAA35610).
SQ SEQUENCE 511 AA; 56501 MW; E01E85BBA36E5DED CRC64;
MALRAMRGIV NGAAPELPVP TGGPAVGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL
DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR
TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM
NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET
ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM
SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD
ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN
QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFER NFIAQGPYEN RTVFETLDIG
WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H
//
MIM
606939
*RECORD*
*FIELD* NO
606939
*FIELD* TI
*606939 ATPasE, H+ TRANSPORTING, LYSOSOMAL, 56/58-KD, V1 SUBUNIT B, ISOFORM
2; ATP6V1B2
read more;;ATP6B2;;
VACUOLAR PROTON PUMP B ISOFORM 2
*FIELD* TX
DESCRIPTION
ATP6B2 encodes a component of vacuolar ATPase (V-ATPase), a multisubunit
enzyme that mediates acidification of intracellular organelles. The
encoded protein is one of 2 B subunit isoforms contained within the
catalytic domain. See also ATP6B1 (192132).
CLONING
By using the consensus PCR primers to the V-ATPase B subunit, Bernasconi
et al. (1990) cloned a partial ATP6B2 cDNA from a human brain cDNA
library. The deduced 511-amino acid protein shares 90% sequence identity
with ATP6B1 and is expressed in human brain as a 3.2-kb transcript.
Nelson et al. (1992) cloned the full-length ATP6B2 cDNA from a human
kidney cDNA library. Sequence analysis of the B1 and B2 isoforms
indicated a high degree of conservation in the internal region of the
protein, but divergence at the N- and C-termini. Van Hille et al. (1994)
cloned isoform B2, which they called HO57, by RT-PCR with osteoclastoma
mRNA. They found ubiquitous expression of 3 mRNA species of 1.6, 2.6,
and 2.8 kb. High levels of expression were found in brain and kidney and
in the originating osteoclastoma, intermediate levels in pancreas, and
lower levels in liver, lung, placenta, heart, and muscle. By in situ
hybridization of osteoclastoma tumors, they found a high level of B2
transcript in osteoclast cells. In day 16 postcoitum mouse embryos, high
levels of subunit B mRNA were observed in the fifth cranial ganglia of
brain and in the developing tubule network of the kidney. High levels of
transcript were also detected in vertebrae, rib, and lower jaw bone
within large cells showing morphologic features characteristic of
osteoclasts.
GENE FUNCTION
Using antibodies to isoform B2, Lee et al. (1995) immunoprecipitated
several subunits of the V-ATPase complex and confirmed the presence of
isoform B2. They also found that the amount of V-ATPase recovered
increased with monocyte differentiation. By nuclear runoff analysis,
they determined that ATP6B2 mRNA is specifically transcriptionally
upregulated during differentiation of both native monocytes and cells of
a human monocytic leukemia cell line.
GENE STRUCTURE
Lee et al. (1995) found that the 5-prime flanking region contains a
TATA-less promoter with a high G+C content and multiple AP2 and SP1
binding sites in the 5-prime UTR and proximal coding region.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ATP6B2
gene to chromosome 8 (TMAP stSG1675).
*FIELD* RF
1. Bernasconi, P.; Rausch, T.; Struve, I.; Morgan, L.; Taiz, L.:
An mRNA from human brain encodes an isoform of the B subunit of the
vacuolar H(+)-ATPase. J. Biol. Chem. 265: 17428-17431, 1990.
2. Lee, B. S.; Underhill, D. M.; Crane, M. K.; Gluck, S. L.: Transcriptional
regulation of the vacuolar H(+)-ATPase B2 subunit gene in differentiating
THP-1 cells. J. Biol. Chem. 270: 7320-7329, 1995.
3. Nelson, R. D.; Guo, X.-L.; Masood, K.; Brown, D.; Kalkbrenner,
M.; Gluck, S.: Selectively amplified expression of an isoform of
the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated
cells. Proc. Nat. Acad. Sci. 89: 3541-3545, 1992.
4. van Hille, B.; Richener, H.; Schmid, P.; Puettner, I.; Green, J.
R.; Bilbe, G.: Heterogeneity of vacuolar H(+)-ATPase: differential
expression of two human subunit B isoforms. Biochem. J. 303: 191-198,
1994.
*FIELD* CD
Patricia A. Hartz: 5/14/2002
*FIELD* ED
carol: 07/07/2006
carol: 9/9/2002
carol: 5/14/2002
*RECORD*
*FIELD* NO
606939
*FIELD* TI
*606939 ATPasE, H+ TRANSPORTING, LYSOSOMAL, 56/58-KD, V1 SUBUNIT B, ISOFORM
2; ATP6V1B2
read more;;ATP6B2;;
VACUOLAR PROTON PUMP B ISOFORM 2
*FIELD* TX
DESCRIPTION
ATP6B2 encodes a component of vacuolar ATPase (V-ATPase), a multisubunit
enzyme that mediates acidification of intracellular organelles. The
encoded protein is one of 2 B subunit isoforms contained within the
catalytic domain. See also ATP6B1 (192132).
CLONING
By using the consensus PCR primers to the V-ATPase B subunit, Bernasconi
et al. (1990) cloned a partial ATP6B2 cDNA from a human brain cDNA
library. The deduced 511-amino acid protein shares 90% sequence identity
with ATP6B1 and is expressed in human brain as a 3.2-kb transcript.
Nelson et al. (1992) cloned the full-length ATP6B2 cDNA from a human
kidney cDNA library. Sequence analysis of the B1 and B2 isoforms
indicated a high degree of conservation in the internal region of the
protein, but divergence at the N- and C-termini. Van Hille et al. (1994)
cloned isoform B2, which they called HO57, by RT-PCR with osteoclastoma
mRNA. They found ubiquitous expression of 3 mRNA species of 1.6, 2.6,
and 2.8 kb. High levels of expression were found in brain and kidney and
in the originating osteoclastoma, intermediate levels in pancreas, and
lower levels in liver, lung, placenta, heart, and muscle. By in situ
hybridization of osteoclastoma tumors, they found a high level of B2
transcript in osteoclast cells. In day 16 postcoitum mouse embryos, high
levels of subunit B mRNA were observed in the fifth cranial ganglia of
brain and in the developing tubule network of the kidney. High levels of
transcript were also detected in vertebrae, rib, and lower jaw bone
within large cells showing morphologic features characteristic of
osteoclasts.
GENE FUNCTION
Using antibodies to isoform B2, Lee et al. (1995) immunoprecipitated
several subunits of the V-ATPase complex and confirmed the presence of
isoform B2. They also found that the amount of V-ATPase recovered
increased with monocyte differentiation. By nuclear runoff analysis,
they determined that ATP6B2 mRNA is specifically transcriptionally
upregulated during differentiation of both native monocytes and cells of
a human monocytic leukemia cell line.
GENE STRUCTURE
Lee et al. (1995) found that the 5-prime flanking region contains a
TATA-less promoter with a high G+C content and multiple AP2 and SP1
binding sites in the 5-prime UTR and proximal coding region.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ATP6B2
gene to chromosome 8 (TMAP stSG1675).
*FIELD* RF
1. Bernasconi, P.; Rausch, T.; Struve, I.; Morgan, L.; Taiz, L.:
An mRNA from human brain encodes an isoform of the B subunit of the
vacuolar H(+)-ATPase. J. Biol. Chem. 265: 17428-17431, 1990.
2. Lee, B. S.; Underhill, D. M.; Crane, M. K.; Gluck, S. L.: Transcriptional
regulation of the vacuolar H(+)-ATPase B2 subunit gene in differentiating
THP-1 cells. J. Biol. Chem. 270: 7320-7329, 1995.
3. Nelson, R. D.; Guo, X.-L.; Masood, K.; Brown, D.; Kalkbrenner,
M.; Gluck, S.: Selectively amplified expression of an isoform of
the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated
cells. Proc. Nat. Acad. Sci. 89: 3541-3545, 1992.
4. van Hille, B.; Richener, H.; Schmid, P.; Puettner, I.; Green, J.
R.; Bilbe, G.: Heterogeneity of vacuolar H(+)-ATPase: differential
expression of two human subunit B isoforms. Biochem. J. 303: 191-198,
1994.
*FIELD* CD
Patricia A. Hartz: 5/14/2002
*FIELD* ED
carol: 07/07/2006
carol: 9/9/2002
carol: 5/14/2002