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V-type proton ATPase subunit B, kidney isoform (V-ATPase subunit B 1) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 1)

 VATB1_HUMAN             Reviewed;         513 AA.
P15313; Q53FY0; Q6P4H6;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
27-SEP-2017, entry version 189.
RecName: Full=V-type proton ATPase subunit B, kidney isoform;
Short=V-ATPase subunit B 1;
AltName: Full=Endomembrane proton pump 58 kDa subunit;
AltName: Full=Vacuolar proton pump subunit B 1;
Name=ATP6V1B1; Synonyms=ATP6B1, VATB, VPP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=2527371; DOI=10.1073/pnas.86.16.6067;
Suedhof T.C., Fried V.A., Stone D.K., Johnston P.A., Xie X.-S.;
"Human endomembrane H+ pump strongly resembles the ATP-synthetase of
Archaebacteria.";
Proc. Natl. Acad. Sci. U.S.A. 86:6067-6071(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-30.
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.,
Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A.,
Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S.,
Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH SLC9A3R1 AND SLC4A7, DOMAIN, AND MUTAGENESIS OF
LEU-513.
PubMed=12444018; DOI=10.1152/ajpcell.00225.2002;
Pushkin A., Abuladze N., Newman D., Muronets V., Sassani P.,
Tatishchev S., Kurtz I.;
"The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ
motifs involved in their interaction.";
Am. J. Physiol. 284:C667-C673(2003).
[7]
VARIANTS DRTA-D PRO-81; TRP-124; ARG-174; PRO-275; GLU-316; ARG-346
AND SER-364, AND TISSUE SPECIFICITY.
PubMed=9916796; DOI=10.1038/5022;
Karet F.E., Finberg K.E., Nelson R.D., Nayir A., Mocan H.,
Sanjad S.A., Rodriguez-Soriano J., Santos F., Cremers C.W.R.J.,
Di Pietro A., Hoffbrand B.I., Winiarski J., Bakkaloglu A., Ozen S.,
Dusunsel R., Goodyer P., Hulton S.A., Wu D.K., Skvorak A.B.,
Morton C.C., Cunningham M.J., Jha V., Lifton R.P.;
"Mutations in the gene encoding B1 subunit of H+-ATPase cause renal
tubular acidosis with sensorineural deafness.";
Nat. Genet. 21:84-90(1999).
[8]
VARIANTS DRTA-D PRO-81; VAL-123; CYS-157; PRO-275 AND ARG-346, AND
VARIANTS ILE-30 AND LYS-161.
PubMed=12414817; DOI=10.1136/jmg.39.11.796;
Stover E.H., Borthwick K.J., Bavalia C., Eady N., Fritz D.M.,
Rungroj N., Giersch A.B.S., Morton C.C., Axon P.R., Akil I.,
Al-Sabban E.A., Baguley D.M., Bianca S., Bakkaloglu A., Bircan Z.,
Chauveau D., Clermont M.-J., Guala A., Hulton S.A., Kroes H.,
Li Volti G., Mir S., Mocan H., Nayir A., Ozen S.,
Rodriguez Soriano J., Sanjad S.A., Tasic V., Taylor C.M.,
Topaloglu R., Smith A.N., Karet F.E.;
"Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal
renal tubular acidosis with new evidence for hearing loss.";
J. Med. Genet. 39:796-803(2002).
[9]
VARIANT HIS-465, AND VARIANTS DRTA-D PRO-81 AND ARG-346.
PubMed=12579397; DOI=10.1007/s00467-002-1018-8;
Ruf R., Rensing C., Topaloglu R., Guay-Woodford L., Klein C.,
Vollmer M., Otto E., Beekmann F., Haller M., Wiedensohler A.,
Leumann E., Antignac C., Rizzoni G., Filler G., Brandis M.,
Weber J.L., Hildebrandt F.;
"Confirmation of the ATP6B1 gene as responsible for distal renal
tubular acidosis.";
Pediatr. Nephrol. 18:105-109(2003).
[10]
VARIANT HIS-465.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- 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.
-!- SUBUNIT: 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). Forms a complex
with SLC9A3R1 and SCL4A7.
-!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
protein. Note=Endomembrane.
-!- TISSUE SPECIFICITY: Expressed in the cochlea and endolymphatic
sac. {ECO:0000269|PubMed:9916796}.
-!- DOMAIN: The PDZ-binding motif mediates interactions with SLC9A3R1
and SCL4A7. {ECO:0000269|PubMed:12444018}.
-!- DISEASE: Renal tubular acidosis, distal, with progressive nerve
deafness (dRTA-D) [MIM:267300]: An autosomal recessive disease
characterized by the association of renal distal tubular acidosis
with sensorineural hearing loss. Distal renal tubular acidosis is
characterized by reduced ability to acidify urine, variable
hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis,
and nephrolithiasis. It is due to functional failure of alpha-
intercalated cells of the cortical collecting duct of the distal
nephron, where vectorial proton transport is required for urinary
acidification. {ECO:0000269|PubMed:12414817,
ECO:0000269|PubMed:12579397, ECO:0000269|PubMed:9916796}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA36498.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M25809; AAA36498.1; ALT_INIT; mRNA.
EMBL; AK291121; BAF83810.1; -; mRNA.
EMBL; AK313194; BAG36011.1; -; mRNA.
EMBL; AK223151; BAD96871.1; -; mRNA.
EMBL; CH471053; EAW99790.1; -; Genomic_DNA.
EMBL; BC063411; AAH63411.1; -; mRNA.
CCDS; CCDS1912.1; -.
PIR; A33281; A33281.
RefSeq; NP_001683.2; NM_001692.3.
UniGene; Hs.64173; -.
ProteinModelPortal; P15313; -.
SMR; P15313; -.
BioGrid; 107008; 94.
IntAct; P15313; 5.
MINT; MINT-8417607; -.
STRING; 9606.ENSP00000234396; -.
BindingDB; P15313; -.
ChEMBL; CHEMBL3217; -.
TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
iPTMnet; P15313; -.
PhosphoSitePlus; P15313; -.
BioMuta; ATP6V1B1; -.
DMDM; 215274116; -.
EPD; P15313; -.
MaxQB; P15313; -.
PaxDb; P15313; -.
PeptideAtlas; P15313; -.
PRIDE; P15313; -.
Ensembl; ENST00000234396; ENSP00000234396; ENSG00000116039.
GeneID; 525; -.
KEGG; hsa:525; -.
UCSC; uc002shj.4; human.
CTD; 525; -.
DisGeNET; 525; -.
EuPathDB; HostDB:ENSG00000116039.11; -.
GeneCards; ATP6V1B1; -.
HGNC; HGNC:853; ATP6V1B1.
HPA; CAB009523; -.
HPA; HPA031847; -.
MalaCards; ATP6V1B1; -.
MIM; 192132; gene.
MIM; 267300; phenotype.
neXtProt; NX_P15313; -.
OpenTargets; ENSG00000116039; -.
Orphanet; 402041; Autosomal recessive distal renal tubular acidosis.
PharmGKB; PA25154; -.
eggNOG; KOG1351; Eukaryota.
eggNOG; COG1156; LUCA.
GeneTree; ENSGT00550000074724; -.
HOGENOM; HOG000165320; -.
HOVERGEN; HBG002176; -.
InParanoid; P15313; -.
KO; K02147; -.
OMA; EHMQAVT; -.
OrthoDB; EOG091G04TR; -.
PhylomeDB; P15313; -.
TreeFam; TF300313; -.
BioCyc; MetaCyc:HS03975-MONOMER; -.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-77387; Insulin receptor recycling.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
Reactome; R-HSA-983712; Ion channel transport.
GeneWiki; ATP6V1B1; -.
GenomeRNAi; 525; -.
PRO; PR:P15313; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000116039; -.
CleanEx; HS_ATP6V1B1; -.
ExpressionAtlas; P15313; baseline and differential.
Genevisible; P15313; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
GO; GO:0005902; C:microvillus; ISS:UniProtKB.
GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IMP:HGNC.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0016820; F:hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances; IEA:InterPro.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0007588; P:excretion; IMP:UniProtKB.
GO; GO:0042472; P:inner ear morphogenesis; IMP:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0001503; P:ossification; IMP:HGNC.
GO; GO:0045851; P:pH reduction; IMP:UniProtKB.
GO; GO:0090383; P:phagosome acidification; TAS:Reactome.
GO; GO:0015992; P:proton transport; IMP:HGNC.
GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0006885; P:regulation of pH; IMP:HGNC.
GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
Gene3D; 1.10.1140.10; -; 1.
HAMAP; MF_00310; ATP_synth_B_arch; 1.
InterPro; IPR020003; ATPase_a/bsu_AS.
InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
InterPro; IPR024034; ATPase_F1/V1_b/a_C.
InterPro; IPR005723; ATPase_V1-cplx_bsu.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR022879; V-ATPase_su_B/beta.
PANTHER; PTHR43389; PTHR43389; 1.
Pfam; PF00006; ATP-synt_ab; 1.
Pfam; PF02874; ATP-synt_ab_N; 1.
PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
1: Evidence at protein level;
Complete proteome; Deafness; Disease mutation; Hydrogen ion transport;
Hydrolase; Ion transport; Membrane; Polymorphism; Reference proteome;
Transport.
CHAIN 1 513 V-type proton ATPase subunit B, kidney
isoform.
/FTId=PRO_0000144624.
MOTIF 510 513 PDZ-binding.
VARIANT 30 30 T -> I (in dbSNP:rs17720303).
{ECO:0000269|PubMed:12414817,
ECO:0000269|Ref.3}.
/FTId=VAR_021011.
VARIANT 81 81 L -> P (in dRTA-D; dbSNP:rs121964880).
{ECO:0000269|PubMed:12414817,
ECO:0000269|PubMed:12579397,
ECO:0000269|PubMed:9916796}.
/FTId=VAR_007866.
VARIANT 123 123 G -> V (in dRTA-D).
{ECO:0000269|PubMed:12414817}.
/FTId=VAR_021012.
VARIANT 124 124 R -> W (in dRTA-D; dbSNP:rs727505222).
{ECO:0000269|PubMed:9916796}.
/FTId=VAR_007867.
VARIANT 157 157 R -> C (in dRTA-D; dbSNP:rs782500780).
{ECO:0000269|PubMed:12414817}.
/FTId=VAR_021013.
VARIANT 161 161 E -> K (in dbSNP:rs114234874).
{ECO:0000269|PubMed:12414817}.
/FTId=VAR_021014.
VARIANT 174 174 M -> R (in dRTA-D).
{ECO:0000269|PubMed:9916796}.
/FTId=VAR_007868.
VARIANT 275 275 T -> P (in dRTA-D).
{ECO:0000269|PubMed:12414817,
ECO:0000269|PubMed:9916796}.
/FTId=VAR_007869.
VARIANT 316 316 G -> E (in dRTA-D).
{ECO:0000269|PubMed:9916796}.
/FTId=VAR_007870.
VARIANT 346 346 P -> R (in dRTA-D; dbSNP:rs781838938).
{ECO:0000269|PubMed:12414817,
ECO:0000269|PubMed:12579397,
ECO:0000269|PubMed:9916796}.
/FTId=VAR_007871.
VARIANT 364 364 G -> S (in dRTA-D).
{ECO:0000269|PubMed:9916796}.
/FTId=VAR_007872.
VARIANT 465 465 R -> H (in dbSNP:rs142905621).
{ECO:0000269|PubMed:12579397,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_021015.
MUTAGEN 513 513 L->G: Loss of interactions with SLC9A3R1
and SCL4A7.
{ECO:0000269|PubMed:12444018}.
CONFLICT 467 467 V -> M (in Ref. 1; AAA36498).
{ECO:0000305}.
CONFLICT 474 474 G -> S (in Ref. 1; AAA36498).
{ECO:0000305}.
CONFLICT 503 503 A -> R (in Ref. 1; AAA36498).
{ECO:0000305}.
SEQUENCE 513 AA; 56833 MW; 5399E2849F3B99AA CRC64;
MAMEIDSRPG GLPGSSCNLG AAREHMQAVT RNYITHPRVT YRTVCSVNGP LVVLDRVKFA
QYAEIVHFTL PDGTQRSGQV LEVAGTKAIV QVFEGTSGID ARKTTCEFTG DILRTPVSED
MLGRVFNGSG KPIDKGPVVM AEDFLDINGQ PINPHSRIYP EEMIQTGISP IDVMNSIARG
QKIPIFSAAG LPHNEIAAQI CRQAGLVKKS KAVLDYHDDN FAIVFAAMGV NMETARFFKS
DFEQNGTMGN VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA
LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM PNDDITHPIP
DLTGFITEGQ IYVDRQLHNR QIYPPINVLP SLSRLMKSAI GEGMTRKDHG DVSNQLYACY
AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ KFEKNFINQG PYENRSVFES LDLGWKLLRI
FPKEMLKRIP QAVIDEFYSR EGALQDLAPD TAL


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EIAAB45693 ATP6V1H,Pig,Sus scrofa,Vacuolar proton pump subunit H,Vacuolar proton pump subunit SFD,V-ATPase 50_57 kDa subunits,V-ATPase subunit H,V-type proton ATPase subunit H
EIAAB45573 ATP6H,ATP6V0E,ATP6V0E1,Homo sapiens,Human,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45629 ATP6AP1,ATP6IP1,ATP6S1,Bos taurus,Bovine,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45570 ATP6H,ATP6V0E,ATP6V0E1,Bos taurus,Bovine,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45562 Atp6d,Atp6v0d1,Mouse,Mus musculus,P39,Physophilin,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,V-type proton ATPase subunit d 1
EIAAB45652 Atp6a1,Atp6a2,Atp6v1a,Atp6v1a1,Mouse,Mus musculus,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45577 ATP6V0E2,ATP6V0E2L,C7orf32,Homo sapiens,Human,Lysosomal 9 kDa H(+)-transporting ATPase V0 subunit e2,Vacuolar proton pump subunit e 2,V-ATPase subunit e 2,V-type proton ATPase subunit e 2
EIAAB45686 ATP6G,ATP6G2,ATP6V1G2,Homo sapiens,Human,NG38,Vacuolar proton pump subunit G 2,V-ATPase 13 kDa subunit 2,V-ATPase subunit G 2,V-type proton ATPase subunit G 2
EIAAB45651 ATP6A1,ATP6V1A,ATP6V1A1,Bos taurus,Bovine,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45650 ATP6A1,ATP6V1A,ATP6V1A1,Pig,Sus scrofa,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45678 ATP6S14,ATP6V1F,Homo sapiens,Human,Vacuolar proton pump subunit F,VATF,V-ATPase 14 kDa subunit,V-ATPase subunit F,V-type proton ATPase subunit F
EIAAB45673 ATP6E,ATP6E2,ATP6V1E1,Homo sapiens,Human,p31,Vacuolar proton pump subunit E 1,V-ATPase 31 kDa subunit,V-ATPase subunit E 1,V-type proton ATPase subunit E 1
EIAAB45679 Atp6s14,Atp6v1f,Mouse,Mus musculus,Vacuolar proton pump subunit F,Vatf,V-ATPase 14 kDa subunit,V-ATPase subunit F,V-type proton ATPase subunit F
EIAAB45681 ATP6S14,ATP6V1F,Bos taurus,Bovine,Vacuolar proton pump subunit F,VATF,V-ATPase 14 kDa subunit,V-ATPase subunit F,V-type proton ATPase subunit F
EIAAB45688 Atp6g2,Atp6v1g2,Mouse,Mus musculus,Ng38,Vacuolar proton pump subunit G 2,V-ATPase 13 kDa subunit 2,V-ATPase subunit G 2,V-type proton ATPase subunit G 2


 

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