ATP6V1B2: Difference between revisions

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{{Infobox_gene}}
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'''V-type proton ATPase subunit B, brain isoform''' is an [[enzyme]] that in humans is encoded by the ''ATP6V1B2'' [[gene]].<ref name="pmid2145275">{{cite journal | vauthors = Bernasconi P, Rausch T, Struve I, Morgan L, Taiz L | title = An mRNA from human brain encodes an isoform of the B subunit of the vacuolar H(+)-ATPase | journal = J Biol Chem | volume = 265 | issue = 29 | pages = 17428–31 |date=Nov 1990 | pmid = 2145275 | pmc =  | doi =  }}</ref><ref name="pmid14580332">{{cite journal | vauthors = Smith AN, Lovering RC, Futai M, Takeda J, Brown D, Karet FE | title = Revised nomenclature for mammalian vacuolar-type H+ -ATPase subunit genes | journal = Mol Cell | volume = 12 | issue = 4 | pages = 801–3 |date=Oct 2003 | pmid = 14580332 | pmc =  | doi =10.1016/S1097-2765(03)00397-6 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1B2 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=526| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2
| HGNCid = 854
| Symbol = ATP6V1B2
| AltSymbols =; VATB; VPP3; ATP6B1B2; ATP6B2; HO57; Vma2
| OMIM = 606939
| ECnumber =
| Homologene = 1279
| MGIid = 109618
  | GeneAtlas_image1 = PBB_GE_ATP6V1B2_201089_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:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016469 |text = proton-transporting two-sector ATPase complex}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{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 = 526
    | Hs_Ensembl = ENSG00000147416
    | Hs_RefseqProtein = NP_001684
    | Hs_RefseqmRNA = NM_001693
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 20098984
    | Hs_GenLoc_end = 20123485
    | Hs_Uniprot = P21281
    | Mm_EntrezGene = 11966
    | Mm_Ensembl = ENSMUSG00000006273
    | Mm_RefseqmRNA = NM_007509
    | Mm_RefseqProtein = NP_031535
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 72017755
    | Mm_GenLoc_end = 72042699
    | Mm_Uniprot = Q3TG74
  }}
}}
'''ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2''', also known as '''ATP6V1B2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1B2 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=526| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of two V1 domain B subunit isoforms and is the only B isoform highly expressed in osteoclasts.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1B2 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=526| 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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of two V1 domain B subunit isoforms and is the only B isoform highly expressed in osteoclasts.<ref name="entrez"/>
 
In melanocytic cells ATP6V1B2 gene expression may be regulated by [[Microphthalmia-associated transcription factor|MITF]].<ref name="pmid19067971">{{cite journal | vauthors = Hoek KS, Schlegel NC, Eichhoff OM | title = Novel MITF targets identified using a two-step DNA microarray strategy | journal = Pigment Cell Melanoma Res. | volume = 21 | issue = 6 | pages = 665–76 | year = 2008 | pmid = 19067971 | doi = 10.1111/j.1755-148X.2008.00505.x |display-authors=etal}}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP6V1B2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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=  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=Nelson RD, Guo XL, Masood K, ''et al.'' |title=Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 8 |pages= 3541-5 |year= 1992 |pmid= 1373501 |doi= }}
*{{cite journal  | vauthors=Nelson RD, Guo XL, Masood K |title=Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 8 |pages= 3541–5 |year= 1992 |pmid= 1373501 |doi=10.1073/pnas.89.8.3541  | pmc=48904  |display-authors=etal}}
*{{cite journal  | author=Bernasconi P, Rausch T, Struve I, ''et al.'' |title=An mRNA from human brain encodes an isoform of the B subunit of the vacuolar H(+)-ATPase. |journal=J. Biol. Chem. |volume=265 |issue= 29 |pages= 17428-31 |year= 1990 |pmid= 2145275 |doi= }}
*{{cite journal  | vauthors=Lee BS, Underhill DM, Crane MK, Gluck SL |title=Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit gene in differentiating THP-1 cells. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7320–9 |year= 1995 |pmid= 7706273 |doi=10.1074/jbc.270.13.7320 }}
*{{cite journal  | author=Lee BS, Underhill DM, Crane MK, Gluck SL |title=Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit gene in differentiating THP-1 cells. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7320-9 |year= 1995 |pmid= 7706273 |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=  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=  }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:27, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

V-type proton ATPase subunit B, brain isoform is an enzyme that in humans is encoded by the ATP6V1B2 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, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of two V1 domain B subunit isoforms and is the only B isoform highly expressed in osteoclasts.[3]

In melanocytic cells ATP6V1B2 gene expression may be regulated by MITF.[4]

References

  1. ↑ Bernasconi P, Rausch T, Struve I, Morgan L, Taiz L (Nov 1990). "An mRNA from human brain encodes an isoform of the B subunit of the vacuolar H(+)-ATPase". J Biol Chem. 265 (29): 17428–31. PMID 2145275.
  2. ↑ Smith AN, Lovering RC, Futai M, Takeda J, Brown D, Karet FE (Oct 2003). "Revised nomenclature for mammalian vacuolar-type H+ -ATPase subunit genes". Mol Cell. 12 (4): 801–3. doi:10.1016/S1097-2765(03)00397-6. PMID 14580332.
  3. ↑ 3.0 3.1 "Entrez Gene: ATP6V1B2 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2".
  4. ↑ Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.

External links

Further reading



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