RBBP7: Difference between revisions

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[[Model organism]]s have been used in the study of RBBP7 function. A conditional [[knockout mouse]] line, called ''Rbbp7<sup>tm1a(EUCOMM)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Rbbp7 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4455962 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–342 | year = 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | year = 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A Mouse for All Reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | year = 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref>
[[Model organism]]s have been used in the study of RBBP7 function. A conditional [[knockout mouse]] line, called ''Rbbp7<sup>tm1a(EUCOMM)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Rbbp7 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4455962 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–342 | year = 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | year = 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A Mouse for All Reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | year = 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref>


Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism. | journal = Genome Biol | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty one tests were carried out on [[mutant]] mice and one significant abnormality was observed: [[hemizygous]] mutant males had decreased CD4-positive and CD8-positive [[T cell]] numbers.<ref name="mgp_reference" />
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism | journal = Genome Biol | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty one tests were carried out on [[mutant]] mice and one significant abnormality was observed: [[hemizygous]] mutant males had decreased CD4-positive and CD8-positive [[T cell]] numbers.<ref name="mgp_reference" />


== Interactions ==
== Interactions ==
Line 65: Line 65:
RBBP7 has been shown to [[Protein-protein interaction|interact]] with:
RBBP7 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
{{div col|colwidth=20em}}
* [[BRCA1]],<ref name = pmid10220405/><ref name = pmid11394910>{{cite journal | vauthors = Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY | title = Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1 | journal = Biochem. Biophys. Res. Commun. | volume = 284 | issue = 2 | pages = 507–14 | date = June 2001 | pmid = 11394910 | doi = 10.1006/bbrc.2001.5003 }}</ref><ref name = "pmid11746496">{{cite journal | vauthors = Yarden RI, Brody LC | title = Identification of proteins that interact with BRCA1 by Far-Western library screening | journal = J. Cell. Biochem. | volume = 83 | issue = 4 | pages = 521–31 | pmid = 11746496 | doi =  10.1002/jcb.1257}}</ref>
* [[BRCA1]],<ref name = pmid10220405/><ref name = pmid11394910>{{cite journal | vauthors = Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY | title = Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1 | journal = Biochem. Biophys. Res. Commun. | volume = 284 | issue = 2 | pages = 507–14 | date = June 2001 | pmid = 11394910 | doi = 10.1006/bbrc.2001.5003 }}</ref><ref name = "pmid11746496">{{cite journal | vauthors = Yarden RI, Brody LC | title = Identification of proteins that interact with BRCA1 by Far-Western library screening | journal = J. Cell. Biochem. | volume = 83 | issue = 4 | pages = 521–31 | pmid = 11746496 | doi =  10.1002/jcb.1257| year = 2001 | url = https://zenodo.org/record/1229223 | format = Submitted manuscript }}</ref>
* [[GATAD2B]],<ref name = pmid11756549>{{cite journal | vauthors = Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y | title = Identification and functional characterization of the p66/p68 components of the MeCP1 complex | journal = Mol. Cell. Biol. | volume = 22 | issue = 2 | pages = 536–46 | date = January 2002 | pmid = 11756549 | pmc = 139742 | doi =  10.1128/mcb.22.2.536-546.2002}}</ref>  
* [[GATAD2B]],<ref name = pmid11756549>{{cite journal | vauthors = Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y | title = Identification and functional characterization of the p66/p68 components of the MeCP1 complex | journal = Mol. Cell. Biol. | volume = 22 | issue = 2 | pages = 536–46 | date = January 2002 | pmid = 11756549 | pmc = 139742 | doi =  10.1128/mcb.22.2.536-546.2002}}</ref>  
* [[HDAC1]],<ref name = pmid12920132>{{cite journal | vauthors = Yao YL, Yang WM | title = The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity | journal = J. Biol. Chem. | volume = 278 | issue = 43 | pages = 42560–8 | date = October 2003 | pmid = 12920132 | doi = 10.1074/jbc.M302955200 }}</ref><ref name = pmid10471499>{{cite journal | vauthors = Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A | title = MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex | journal = Nat. Genet. | volume = 23 | issue = 1 | pages = 58–61 | date = September 1999 | pmid = 10471499 | doi = 10.1038/12659 }}</ref><ref name = pmid10444591>{{cite journal | vauthors = Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D | title = Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation | journal = Genes Dev. | volume = 13 | issue = 15 | pages = 1924–35 | date = August 1999 | pmid = 10444591 | pmc = 316920 | doi =  10.1101/gad.13.15.1924}}</ref><ref name = pmid9150135>{{cite journal | vauthors = Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D | title = Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex | journal = Cell | volume = 89 | issue = 3 | pages = 357–64 | date = May 1997 | pmid = 9150135 | doi =  10.1016/s0092-8674(00)80216-0}}</ref>  
* [[HDAC1]],<ref name = pmid12920132>{{cite journal | vauthors = Yao YL, Yang WM | title = The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity | journal = J. Biol. Chem. | volume = 278 | issue = 43 | pages = 42560–8 | date = October 2003 | pmid = 12920132 | doi = 10.1074/jbc.M302955200 }}</ref><ref name = pmid10471499>{{cite journal | vauthors = Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A | title = MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex | journal = Nat. Genet. | volume = 23 | issue = 1 | pages = 58–61 | date = September 1999 | pmid = 10471499 | doi = 10.1038/12659 }}</ref><ref name = pmid10444591>{{cite journal | vauthors = Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D | title = Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation | journal = Genes Dev. | volume = 13 | issue = 15 | pages = 1924–35 | date = August 1999 | pmid = 10444591 | pmc = 316920 | doi =  10.1101/gad.13.15.1924}}</ref><ref name = pmid9150135>{{cite journal | vauthors = Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D | title = Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex | journal = Cell | volume = 89 | issue = 3 | pages = 357–64 | date = May 1997 | pmid = 9150135 | doi =  10.1016/s0092-8674(00)80216-0}}</ref>  
Line 94: Line 94:
* {{cite journal | vauthors = Skowyra D, Zeremski M, Neznanov N, Li M, Choi Y, Uesugi M, Hauser CA, Gu W, Gudkov AV, Qin J | title = Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex | journal = J. Biol. Chem. | volume = 276 | issue = 12 | pages = 8734–8739 | year = 2001 | pmid = 11118440 | doi = 10.1074/jbc.M007664200 }}
* {{cite journal | vauthors = Skowyra D, Zeremski M, Neznanov N, Li M, Choi Y, Uesugi M, Hauser CA, Gu W, Gudkov AV, Qin J | title = Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex | journal = J. Biol. Chem. | volume = 276 | issue = 12 | pages = 8734–8739 | year = 2001 | pmid = 11118440 | doi = 10.1074/jbc.M007664200 }}
* {{cite journal | vauthors = Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY | title = Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1 | journal = Biochem. Biophys. Res. Commun. | volume = 284 | issue = 2 | pages = 507–514 | year = 2001 | pmid = 11394910 | doi = 10.1006/bbrc.2001.5003 }}
* {{cite journal | vauthors = Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY | title = Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1 | journal = Biochem. Biophys. Res. Commun. | volume = 284 | issue = 2 | pages = 507–514 | year = 2001 | pmid = 11394910 | doi = 10.1006/bbrc.2001.5003 }}
* {{cite journal | vauthors = Yarden RI, Brody LC | title = Identification of proteins that interact with BRCA1 by Far-Western library screening | journal = J. Cell. Biochem. | volume = 83 | issue = 4 | pages = 521–531 | year = 2002 | pmid = 11746496 | doi = 10.1002/jcb.1257 }}
* {{cite journal | vauthors = Yarden RI, Brody LC | title = Identification of proteins that interact with BRCA1 by Far-Western library screening | journal = J. Cell. Biochem. | volume = 83 | issue = 4 | pages = 521–531 | year = 2002 | pmid = 11746496 | doi = 10.1002/jcb.1257 | url = https://zenodo.org/record/1229223 | format = Submitted manuscript }}
* {{cite journal | vauthors = Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D | title = Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1) | journal = Mol. Cell. Biol. | volume = 22 | issue = 3 | pages = 835–848 | year = 2002 | pmid = 11784859 | pmc = 133546 | doi = 10.1128/MCB.22.3.835-848.2002 }}
* {{cite journal | vauthors = Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D | title = Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1) | journal = Mol. Cell. Biol. | volume = 22 | issue = 3 | pages = 835–848 | year = 2002 | pmid = 11784859 | pmc = 133546 | doi = 10.1128/MCB.22.3.835-848.2002 }}
* {{cite journal | vauthors = Vaute O, Nicolas E, Vandel L, Trouche D | title = Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases | journal = Nucleic Acids Res. | volume = 30 | issue = 2 | pages = 475–481 | year = 2002 | pmid = 11788710 | pmc = 99834 | doi = 10.1093/nar/30.2.475 }}
* {{cite journal | vauthors = Vaute O, Nicolas E, Vandel L, Trouche D | title = Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases | journal = Nucleic Acids Res. | volume = 30 | issue = 2 | pages = 475–481 | year = 2002 | pmid = 11788710 | pmc = 99834 | doi = 10.1093/nar/30.2.475 }}

Latest revision as of 00:03, 6 September 2018

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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

Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 gene.[1]

Function

This protein is a ubiquitously expressed nuclear protein and belongs to a highly conserved subfamily of WD-repeat proteins. It is found among several proteins that binds directly to retinoblastoma protein, which regulates cell proliferation. The encoded protein is found in many histone deacetylase complexes, including mSin3 co-repressor complex. It is also present in protein complexes involved in chromatin assembly. This protein can interact with BRCA1 tumor-suppressor gene and may have a role in the regulation of cell proliferation and differentiation.[2]

Model organisms

Model organisms have been used in the study of RBBP7 function. A conditional knockout mouse line, called Rbbp7tm1a(EUCOMM)Wtsi[6][7] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[8][9][10]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[4][11] Twenty one tests were carried out on mutant mice and one significant abnormality was observed: hemizygous mutant males had decreased CD4-positive and CD8-positive T cell numbers.[4]

Interactions

RBBP7 has been shown to interact with:

References

  1. ↑ 1.0 1.1 Qian YW, Lee EY (Dec 1995). "Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast". J Biol Chem. 270 (43): 25507–25513. doi:10.1074/jbc.270.43.25507. PMID 7503932.
  2. ↑ "Entrez Gene: RBBP7 retinoblastoma binding protein 7".
  3. ↑ "Peripheral blood lymphocytes data for Rbbp7". Wellcome Trust Sanger Institute.[dead link]
  4. ↑ 4.0 4.1 4.2 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  5. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  6. ↑ "International Knockout Mouse Consortium".
  7. ↑ "Mouse Genome Informatics".
  8. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  9. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  10. ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  11. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  12. ↑ 12.0 12.1 Yarden RI, Brody LC (April 1999). "BRCA1 interacts with components of the histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4983–8. doi:10.1073/pnas.96.9.4983. PMC 21803. PMID 10220405.
  13. ↑ Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY (June 2001). "Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1". Biochem. Biophys. Res. Commun. 284 (2): 507–14. doi:10.1006/bbrc.2001.5003. PMID 11394910.
  14. ↑ Yarden RI, Brody LC (2001). "Identification of proteins that interact with BRCA1 by Far-Western library screening" (Submitted manuscript). J. Cell. Biochem. 83 (4): 521–31. doi:10.1002/jcb.1257. PMID 11746496.
  15. ↑ Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y (January 2002). "Identification and functional characterization of the p66/p68 components of the MeCP1 complex". Mol. Cell. Biol. 22 (2): 536–46. doi:10.1128/mcb.22.2.536-546.2002. PMC 139742. PMID 11756549.
  16. ↑ 16.0 16.1 Yao YL, Yang WM (October 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". J. Biol. Chem. 278 (43): 42560–8. doi:10.1074/jbc.M302955200. PMID 12920132.
  17. ↑ Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (September 1999). "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex". Nat. Genet. 23 (1): 58–61. doi:10.1038/12659. PMID 10471499.
  18. ↑ 18.0 18.1 18.2 Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (August 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
  19. ↑ Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/s0092-8674(00)80216-0. PMID 9150135.
  20. ↑ 20.0 20.1 Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (June 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell. 1 (7): 1021–31. doi:10.1016/s1097-2765(00)80102-1. PMID 9651585.
  21. ↑ 21.0 21.1 Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (February 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Mol. Cell. Biol. 22 (3): 835–48. doi:10.1128/mcb.22.3.835-848.2002. PMC 133546. PMID 11784859.

Further reading

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