RBBP7

RBBP7
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3CFS, 3CFV
Identifiers
Aliases	RBBP7, RbAp46, retinoblastoma binding protein 7, RB binding protein 7, chromatin remodeling factor
External IDs	OMIM: 300825; MGI: 1194910; HomoloGene: 55702; GeneCards: RBBP7; OMA:RBBP7 - orthologs
Gene location (Human)
Chr.	X chromosome (human)
End	16,870,362 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	161,562,088 bp
RNA expression pattern
	Top expressed in
	oocyte; ; secondary oocyte; ; right adrenal gland; ; right adrenal cortex; ; left adrenal cortex; ; corpus epididymis; ; seminal vesicula; ; endothelial cell; ; right testis; ; left ovary;
	Top expressed in
	primitive streak; ; migratory enteric neural crest cell; ; medullary collecting duct; ; condyle; ; ureter; ; Paneth cell; ; internal carotid artery; ; fossa; ; external carotid artery; ; vas deferens;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein binding; RNA binding; histone deacetylase activity;
Cellular component	NuRD complex; ESC/E(Z) complex; nucleus; nucleoplasm; cytosol;
Biological process	regulation of transcription, DNA-templated; response to steroid hormone; cellular heat acclimation; negative regulation of transcription by RNA polymerase II; CENP-A containing chromatin assembly; transcription, DNA-templated; multicellular organism development; DNA replication; negative regulation of gene expression, epigenetic; negative regulation of cell growth; cell population proliferation; negative regulation of transcription, DNA-templated; regulation of signal transduction by p53 class mediator; histone deacetylation; post-translational protein modification; negative regulation of G0 to G1 transition; chromatin organization;
	Sources:Amigo / QuickGO
Orthologs
	5931
	245688
	ENSG00000102054
	ENSMUSG00000031353
	Q16576
	Q60973
	NM_001198719; NM_002893
	NM_009031
	NP_001185648; NP_002884
	NP_033057
	Wikidata
View/Edit Human	View/Edit Mouse

Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 gene.^[5]

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.^[6]

Interactions

RBBP7 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000102054 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031353 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b 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.
^ "Entrez Gene: RBBP7 retinoblastoma binding protein 7".
^ ^a ^b 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. Bibcode:1999PNAS...96.4983Y. doi:10.1073/pnas.96.9.4983. PMC 21803. PMID 10220405.
^ 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.
^ Yarden RI, Brody LC (2001). "Identification of proteins that interact with BRCA1 by Far-Western library screening". J. Cell. Biochem. 83 (4): 521–31. doi:10.1002/jcb.1257. PMID 11746496. S2CID 29703139.
^ 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.
^ ^a ^b 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.
^ 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. hdl:1842/684. PMID 10471499. S2CID 6147725.
^ ^a ^b ^c 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.
^ 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.
^ ^a ^b 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.
^ ^a ^b 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.

Huang S, Lee WH, Lee EY (1991). "A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product". Nature. 350 (6314): 160–162. Bibcode:1991Natur.350..160H. doi:10.1038/350160a0. PMID 2005966. S2CID 4345233.
Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–364. doi:10.1016/S0092-8674(00)80216-0. PMID 9150135.
Verreault A, Kaufman PD, Kobayashi R, Stillman B (1998). "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase". Curr. Biol. 8 (2): 96–108. Bibcode:1998CBio....8...96V. doi:10.1016/S0960-9822(98)70040-5. PMID 9427644. S2CID 201273.
Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell. 1 (7): 1021–1031. doi:10.1016/S1097-2765(00)80102-1. PMID 9651585.
Guan LS, Rauchman M, Wang ZY (1998). "Induction of Rb-associated protein (RbAp46) by Wilms' tumor suppressor WT1 mediates growth inhibition". J. Biol. Chem. 273 (42): 27047–27050. doi:10.1074/jbc.273.42.27047. PMID 9765217.
Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (1998). "The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities". Cell. 95 (2): 279–289. doi:10.1016/S0092-8674(00)81758-4. PMID 9790534. S2CID 18786866.
Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature. 395 (6705): 917–921. Bibcode:1998Natur.395..917T. doi:10.1038/27699. PMID 9804427. S2CID 4355885.
Yarden RI, Brody LC (1999). "BRCA1 interacts with components of the histone deacetylase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4983–4988. Bibcode:1999PNAS...96.4983Y. doi:10.1073/pnas.96.9.4983. PMC 21803. PMID 10220405.
Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15): 1924–1935. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
Wade PA, Gegonne A, Jones PL, Ballestar E, Aubry F, Wolffe AP (1999). "Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation". Nat. Genet. 23 (1): 62–66. doi:10.1038/12664. PMID 10471500. S2CID 52868103.
Zhang Q, Vo N, Goodman RH (2000). "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB". Mol. Cell. Biol. 20 (14): 4970–4978. doi:10.1128/MCB.20.14.4970-4978.2000. PMC 85947. PMID 10866654.
Humphrey GW, Wang Y, Russanova VR, Hirai T, Qin J, Nakatani Y, Howard BH (2001). "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1". J. Biol. Chem. 276 (9): 6817–6824. doi:10.1074/jbc.M007372200. PMID 11102443.
Skowyra D, Zeremski M, Neznanov N, Li M, Choi Y, Uesugi M, Hauser CA, Gu W, Gudkov AV, Qin J (2001). "Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex". J. Biol. Chem. 276 (12): 8734–8739. doi:10.1074/jbc.M007664200. PMID 11118440.
Chen GC, Guan LS, Yu JH, Li GC, Choi Kim HR, Wang ZY (2001). "Rb-associated protein 46 (RbAp46) inhibits transcriptional transactivation mediated by BRCA1". Biochem. Biophys. Res. Commun. 284 (2): 507–514. doi:10.1006/bbrc.2001.5003. PMID 11394910.
Yarden RI, Brody LC (2002). "Identification of proteins that interact with BRCA1 by Far-Western library screening". J. Cell. Biochem. 83 (4): 521–531. doi:10.1002/jcb.1257. PMID 11746496. S2CID 29703139.
Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Mol. Cell. Biol. 22 (3): 835–848. doi:10.1128/MCB.22.3.835-848.2002. PMC 133546. PMID 11784859.
Vaute O, Nicolas E, Vandel L, Trouche D (2002). "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases". Nucleic Acids Res. 30 (2): 475–481. doi:10.1093/nar/30.2.475. PMC 99834. PMID 11788710.
Saito M, Ishikawa F (2002). "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2". J. Biol. Chem. 277 (38): 35434–35439. doi:10.1074/jbc.M203455200. PMID 12124384.
Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D (2002). "Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein". Genes Dev. 16 (22): 2893–2905. doi:10.1101/gad.1035902. PMC 187479. PMID 12435631.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000102054 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000031353 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7503932-5] 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.

[entrez-6] "Entrez Gene: RBBP7 retinoblastoma binding protein 7".

[pmid10220405-7] 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. Bibcode:1999PNAS...96.4983Y. doi:10.1073/pnas.96.9.4983. PMC 21803. PMID 10220405.

[pmid11394910-8] 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.

[pmid11746496-9] Yarden RI, Brody LC (2001). "Identification of proteins that interact with BRCA1 by Far-Western library screening". J. Cell. Biochem. 83 (4): 521–31. doi:10.1002/jcb.1257. PMID 11746496. S2CID 29703139.

[pmid11756549-10] 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.

[pmid12920132-11] 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.

[pmid10471499-12] 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. hdl:1842/684. PMID 10471499. S2CID 6147725.

[pmid10444591-13] 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.

[pmid9150135-14] 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.

[pmid9651585-15] 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.

[pmid11784859-16] 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.

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Function

Interactions

References

Further reading