ATP6V1B1: Difference between revisions

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Revision as of 18:27, 29 August 2017

V-type proton ATPase subunit B, kidney isoform is an enzyme that in humans is encoded by the ATP6V1B1 gene.^[1]^[2]^[3]

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c, and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness.^[3]

References

↑ Karet FE, Finberg KE, Nelson RD, Nayir A, Mocan H, Sanjad SA, Rodriguez-Soriano J, Santos F, Cremers CW, Di Pietro A, Hoffbrand BI, Winiarski J, Bakkaloglu A, Ozen S, Dusunsel R, Goodyer P, Hulton SA, Wu DK, Skvorak AB, Morton CC, Cunningham MJ, Jha V, Lifton RP (Feb 1999). "Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness". Nat Genet. 21 (1): 84–90. doi:10.1038/5022. PMID 9916796.
↑ Sudhof TC, Fried VA, Stone DK, Johnston PA, Xie XS (Sep 1989). "Human endomembrane H+ pump strongly resembles the ATP-synthetase of Archaebacteria". Proc Natl Acad Sci U S A. 86 (16): 6067–71. doi:10.1073/pnas.86.16.6067. PMC 297776. PMID 2527371.
↑ ^3.0 ^3.1 "Entrez Gene: ATP6V1B1 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)".

External links

Human ATP6V1B1 genome location and ATP6V1B1 gene details page in the UCSC Genome Browser.

Schuler GD, Boguski MS, Stewart EA, et al. (1996). "A gene map of the human genome". Science. 274 (5287): 540–6. doi:10.1126/science.274.5287.540. PMID 8849440.
Finbow ME, Harrison MA (1997). "The vacuolar H+-ATPase: a universal proton pump of eukaryotes". Biochem. J. 324 (Pt 3): 697–712. doi:10.1042/bj3240697. PMC 1218484. PMID 9210392.
Stevens TH, Forgac M (1998). "Structure, function and regulation of the vacuolar (H+)-ATPase". Annu. Rev. Cell Dev. Biol. 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
Nelson N, Harvey WR (1999). "Vacuolar and plasma membrane proton-adenosinetriphosphatases". Physiol. Rev. 79 (2): 361–85. PMID 10221984.
Forgac M (1999). "Structure and properties of the vacuolar (H+)-ATPases". J. Biol. Chem. 274 (19): 12951–4. doi:10.1074/jbc.274.19.12951. PMID 10224039.
Kane PM (1999). "Introduction: V-ATPases 1992-1998". J. Bioenerg. Biomembr. 31 (1): 3–5. doi:10.1023/A:1001884227654. PMID 10340843.
Wieczorek H, Brown D, Grinstein S, et al. (1999). "Animal plasma membrane energization by proton-motive V-ATPases". BioEssays. 21 (8): 637–48. doi:10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W. PMID 10440860.
Nishi T, Forgac M (2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps". Nat. Rev. Mol. Cell Biol. 3 (2): 94–103. doi:10.1038/nrm729. PMID 11836511.
Kawasaki-Nishi S, Nishi T, Forgac M (2003). "Proton translocation driven by ATP hydrolysis in V-ATPases". FEBS Lett. 545 (1): 76–85. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495.
Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase". Biol. Cell. 95 (7): 453–7. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
van Hille B, Richener H, Schmid P, et al. (1994). "Heterogeneity of vacuolar H(+)-ATPase: differential expression of two human subunit B isoforms". Biochem. J. 303 (Pt 1): 191–8. doi:10.1042/bj3030191. PMC 1137575. PMID 7945239.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Breton S, Smith PJ, Lui B, Brown D (1996). "Acidification of the male reproductive tract by a proton pumping (H+)-ATPase". Nat. Med. 2 (4): 470–2. doi:10.1038/nm0496-470. PMID 8597961.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

[pmid9916796-1] Karet FE, Finberg KE, Nelson RD, Nayir A, Mocan H, Sanjad SA, Rodriguez-Soriano J, Santos F, Cremers CW, Di Pietro A, Hoffbrand BI, Winiarski J, Bakkaloglu A, Ozen S, Dusunsel R, Goodyer P, Hulton SA, Wu DK, Skvorak AB, Morton CC, Cunningham MJ, Jha V, Lifton RP (Feb 1999). "Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness". Nat Genet. 21 (1): 84–90. doi:10.1038/5022. PMID 9916796.

[pmid2527371-2] Sudhof TC, Fried VA, Stone DK, Johnston PA, Xie XS (Sep 1989). "Human endomembrane H+ pump strongly resembles the ATP-synthetase of Archaebacteria". Proc Natl Acad Sci U S A. 86 (16): 6067–71. doi:10.1073/pnas.86.16.6067. PMC 297776. PMID 2527371.

[entrez-3] 3.0 ^3.1 "Entrez Gene: ATP6V1B1 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)".

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
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+{{Underlinked|date=October 2016}}
-{{PBB_Controls
+{{Infobox_gene}}
-| update_page = yes
+'''V-type proton ATPase subunit B, kidney isoform''' is an [[enzyme]] that in humans is encoded by the ''ATP6V1B1'' [[gene]].<ref name="pmid9916796">{{cite journal | vauthors = Karet FE, Finberg KE, Nelson RD, Nayir A, Mocan H, Sanjad SA, Rodriguez-Soriano J, Santos F, Cremers CW, Di Pietro A, Hoffbrand BI, Winiarski J, Bakkaloglu A, Ozen S, Dusunsel R, Goodyer P, Hulton SA, Wu DK, Skvorak AB, Morton CC, Cunningham MJ, Jha V, Lifton RP | title = Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness | journal = Nat Genet | volume = 21 | issue = 1 | pages = 84–90 |date=Feb 1999 | pmid = 9916796 | pmc =  | doi = 10.1038/5022 }}</ref><ref name="pmid2527371">{{cite journal | vauthors = Sudhof TC, Fried VA, Stone DK, Johnston PA, Xie XS | title = Human endomembrane H+ pump strongly resembles the ATP-synthetase of Archaebacteria | journal = Proc Natl Acad Sci U S A | volume = 86 | issue = 16 | pages = 6067–71 |date=Sep 1989 | pmid = 2527371 | pmc = 297776 | doi =10.1073/pnas.86.16.6067  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1B1 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=525| accessdate = }}</ref>
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-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)
- | HGNCid = 853
- | Symbol = ATP6V1B1
- | AltSymbols =; ATP6B1; MGC32642; RTA1B; VATB; VMA2; VPP3
- | OMIM = 192132
- | ECnumber =
- | Homologene = 68198
- | MGIid = 103285
-  | GeneAtlas_image1 = PBB_GE_ATP6V1B1_205473_at_tn.png
- | Function = {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008553 |text = hydrogen-exporting ATPase activity, phosphorylative mechanism}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046933 |text = hydrogen ion transporting ATP synthase activity, rotational mechanism}} {{GNF_GO|id=GO:0046961 |text = hydrogen ion transporting ATPase activity, rotational mechanism}}
- | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0016324 |text = apical plasma membrane}} {{GNF_GO|id=GO:0016469 |text = proton-transporting two-sector ATPase complex}} {{GNF_GO|id=GO:0016471 |text = vacuolar proton-transporting V-type ATPase complex}}
- | Process = {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006885 |text = regulation of pH}} {{GNF_GO|id=GO:0007588 |text = excretion}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0015986 |text = ATP synthesis coupled proton transport}} {{GNF_GO|id=GO:0015988 |text = energy coupled proton transport, against electrochemical gradient}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 525
-    | Hs_Ensembl = ENSG00000116039
-    | Hs_RefseqProtein = NP_001683
-    | Hs_RefseqmRNA = NM_001692
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 2
-    | Hs_GenLoc_start = 71016529
-    | Hs_GenLoc_end = 71046063
-    | Hs_Uniprot = P15313
-    | Mm_EntrezGene = 110935
-    | Mm_Ensembl = ENSMUSG00000006269
-    | Mm_RefseqmRNA = NM_134157
-    | Mm_RefseqProtein = NP_598918
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 6
-    | Mm_GenLoc_start = 83708675
-    | Mm_GenLoc_end = 83724468
-    | Mm_Uniprot =
-  }}
-}}
-'''ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)''', also known as '''ATP6V1B1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1B1 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=525| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1B1 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1 (Renal tubular acidosis with deafness)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=525| accessdate = }}</ref>
+| summary_text = This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness.<ref name="entrez" />
 }}
 ==References==
-{{reflist|2}}
+{{reflist}}
+==External links==
+* {{UCSC gene info|ATP6V1B1}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Schuler GD, Boguski MS, Stewart EA, ''et al.'' |title=A gene map of the human genome. |journal=Science |volume=274 |issue= 5287 |pages= 540-6 |year= 1996 |pmid= 8849440 |doi=  }}
+*{{cite journal  | vauthors=Schuler GD, Boguski MS, Stewart EA |title=A gene map of the human genome |journal=Science |volume=274 |issue= 5287 |pages= 540–6 |year= 1996 |pmid= 8849440 |doi=10.1126/science.274.5287.540  |display-authors=etal}}
-*{{cite journal  | author=Finbow ME, Harrison MA |title=The vacuolar H+-ATPase: a universal proton pump of eukaryotes. |journal=Biochem. J. |volume=324 ( Pt 3) |issue=  |pages= 697-712 |year= 1997 |pmid= 9210392 |doi=  }}
+*{{cite journal  | vauthors=Finbow ME, Harrison MA |title=The vacuolar H+-ATPase: a universal proton pump of eukaryotes |journal=Biochem. J. |volume=324 |issue=  Pt 3|pages= 697–712 |year= 1997 |pmid= 9210392 |doi=  10.1042/bj3240697| pmc=1218484  }}
-*{{cite journal  | author=Stevens TH, Forgac M |title=Structure, function and regulation of the vacuolar (H+)-ATPase. |journal=Annu. Rev. Cell Dev. Biol. |volume=13 |issue=  |pages= 779-808 |year= 1998 |pmid= 9442887 |doi= 10.1146/annurev.cellbio.13.1.779 }}
+*{{cite journal  | vauthors=Stevens TH, Forgac M |title=Structure, function and regulation of the vacuolar (H+)-ATPase |journal=Annu. Rev. Cell Dev. Biol. |volume=13 |issue=  |pages= 779–808 |year= 1998 |pmid= 9442887 |doi= 10.1146/annurev.cellbio.13.1.779 }}
-*{{cite journal  | author=Nelson N, Harvey WR |title=Vacuolar and plasma membrane proton-adenosinetriphosphatases. |journal=Physiol. Rev. |volume=79 |issue= 2 |pages= 361-85 |year= 1999 |pmid= 10221984 |doi=  }}
+*{{cite journal  | vauthors=Nelson N, Harvey WR |title=Vacuolar and plasma membrane proton-adenosinetriphosphatases |journal=Physiol. Rev. |volume=79 |issue= 2 |pages= 361–85 |year= 1999 |pmid= 10221984 |doi=  }}
-*{{cite journal  | author=Forgac M |title=Structure and properties of the vacuolar (H+)-ATPases. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 12951-4 |year= 1999 |pmid= 10224039 |doi=  }}
+*{{cite journal  | author=Forgac M |title=Structure and properties of the vacuolar (H+)-ATPases |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 12951–4 |year= 1999 |pmid= 10224039 |doi=10.1074/jbc.274.19.12951  }}
-*{{cite journal  | author=Kane PM |title=Introduction: V-ATPases 1992-1998. |journal=J. Bioenerg. Biomembr. |volume=31 |issue= 1 |pages= 3-5 |year= 1999 |pmid= 10340843 |doi=  }}
+*{{cite journal  | author=Kane PM |title=Introduction: V-ATPases 1992-1998 |journal=J. Bioenerg. Biomembr. |volume=31 |issue= 1 |pages= 3–5 |year= 1999 |pmid= 10340843 |doi=10.1023/A:1001884227654  }}
-*{{cite journal  | author=Wieczorek H, Brown D, Grinstein S, ''et al.'' |title=Animal plasma membrane energization by proton-motive V-ATPases. |journal=Bioessays |volume=21 |issue= 8 |pages= 637-48 |year= 1999 |pmid= 10440860 |doi= 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W }}
+*{{cite journal  | vauthors=Wieczorek H, Brown D, Grinstein S |title=Animal plasma membrane energization by proton-motive V-ATPases |journal=BioEssays |volume=21 |issue= 8 |pages= 637–48 |year= 1999 |pmid= 10440860 |doi= 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W |display-authors=etal}}
-*{{cite journal  | author=Nishi T, Forgac M |title=The vacuolar (H+)-ATPases--nature's most versatile proton pumps. |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 2 |pages= 94-103 |year= 2002 |pmid= 11836511 |doi= 10.1038/nrm729 }}
+*{{cite journal  | vauthors=Nishi T, Forgac M |title=The vacuolar (H+)-ATPases--nature's most versatile proton pumps |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 2 |pages= 94–103 |year= 2002 |pmid= 11836511 |doi= 10.1038/nrm729 }}
-*{{cite journal  | author=Kawasaki-Nishi S, Nishi T, Forgac M |title=Proton translocation driven by ATP hydrolysis in V-ATPases. |journal=FEBS Lett. |volume=545 |issue= 1 |pages= 76-85 |year= 2003 |pmid= 12788495 |doi=  }}
+*{{cite journal  | vauthors=Kawasaki-Nishi S, Nishi T, Forgac M |title=Proton translocation driven by ATP hydrolysis in V-ATPases |journal=FEBS Lett. |volume=545 |issue= 1 |pages= 76–85 |year= 2003 |pmid= 12788495 |doi=10.1016/S0014-5793(03)00396-X  }}
-*{{cite journal  | author=Morel N |title=Neurotransmitter release: the dark side of the vacuolar-H+ATPase. |journal=Biol. Cell |volume=95 |issue= 7 |pages= 453-7 |year= 2004 |pmid= 14597263 |doi=  }}
+*{{cite journal  | author=Morel N |title=Neurotransmitter release: the dark side of the vacuolar-H+ATPase |journal=Biol. Cell |volume=95 |issue= 7 |pages= 453–7 |year= 2004 |pmid= 14597263 |doi=10.1016/S0248-4900(03)00075-3  }}
-*{{cite journal  | author=Südhof TC, Fried VA, Stone DK, ''et al.'' |title=Human endomembrane H+ pump strongly resembles the ATP-synthetase of Archaebacteria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 16 |pages= 6067-71 |year= 1989 |pmid= 2527371 |doi=  }}
+*{{cite journal  | vauthors=van Hille B, Richener H, Schmid P |title=Heterogeneity of vacuolar H(+)-ATPase: differential expression of two human subunit B isoforms |journal=Biochem. J. |volume=303 |issue=  Pt 1|pages= 191–8 |year= 1994 |pmid= 7945239 |doi=  10.1042/bj3030191| pmc=1137575  |display-authors=etal}}
-*{{cite journal  | author=van Hille B, Richener H, Schmid P, ''et al.'' |title=Heterogeneity of vacuolar H(+)-ATPase: differential expression of two human subunit B isoforms. |journal=Biochem. J. |volume=303 ( Pt 1) |issue=  |pages= 191-8 |year= 1994 |pmid= 7945239 |doi=  }}
+*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
-*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
+*{{cite journal  | vauthors=Breton S, Smith PJ, Lui B, Brown D |title=Acidification of the male reproductive tract by a proton pumping (H+)-ATPase |journal=Nat. Med. |volume=2 |issue= 4 |pages= 470–2 |year= 1996 |pmid= 8597961 |doi=10.1038/nm0496-470  }}
-*{{cite journal  | author=Breton S, Smith PJ, Lui B, Brown D |title=Acidification of the male reproductive tract by a proton pumping (H+)-ATPase. |journal=Nat. Med. |volume=2 |issue= 4 |pages= 470-2 |year= 1996 |pmid= 8597961 |doi=  }}
+*{{cite journal  | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791  }}
-*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
+*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
-*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
-*{{cite journal  | author=Karet FE, Finberg KE, Nelson RD, ''et al.'' |title=Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness. |journal=Nat. Genet. |volume=21 |issue= 1 |pages= 84-90 |year= 1999 |pmid= 9916796 |doi= 10.1038/5022 }}
 }}
 {{refend}}
-{{protein-stub}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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+{{PBB_Controls
+| update_page = yes
+| require_manual_inspection = no
+| update_protein_box = yes
+| update_summary = yes
+| update_citations = yes
+}}
+{{gene-2-stub}}

ATP6V1B1: Difference between revisions

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