Search results for RBBP7

Showing 12 results out of 12

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Protein (1 results from a total of 1)

Identifier: R-HSA-212227
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: RBBP7: Q16576

Reaction (6 results from a total of 6)

Identifier: R-HSA-5225649
Species: Homo sapiens
Compartment: nucleoplasm
RBBP7, a central component of the co-repressor complexes Sin3a, NURD and PRC2, can bind histone H3 arginine-3 (H3R2). Symmetrical dimethylation of this residue excludes RBBP7 binding but enhances binding of WDR5, a common component of the coactivator complexes MLL, SET1A, SET1B, NLS1 and ATAC (Migliori et al. 2012).
Identifier: R-HSA-3240957
Species: Homo sapiens
Compartment: nucleoplasm
The Polycomb repressor complex 2, PRC2-EZH2, consists of 5 proteins: EZH2, EED, RBBP4 (RBAP48), RBBP7 (RBAP46) and SUZ12, and is evolutionarily conserved. While RBBP4 and RBBP7 are proteins involved in various chromatin remodeling complexes, EZH2, EED and SUZ12 belong to the Polycomb group. EZH2 is also a member of the SET family of histone methyltransferases, and PRC2 trimethylates lysine residues K10 and K28 of HIST1H3A (histone H3), with K28 being the preferred site (Kuzmichev et al. 2002).
Identifier: R-HSA-5638332
Species: Homo sapiens
Compartment: nucleoplasm
EZH2 (KMT6, PRC2) is the catalytic subunit of the PRC2 (EZH2) Core complex, which additionally contains EED, SUZ12, AEBP2 and one of RBBP4 or RBBP7. It methylates lysine-28 (H3K27) of histone H3 (Cao et al. 2002, Czermin et al. 2002, Kuzmichev et al. 2002, Muller et al. 2002) leading to transcriptional repression of the affected target gene. It is able to mono-, di- and trimethylate lysine-28 (Cao & Zhang 2004).
Identifier: R-HSA-3662318
Species: Homo sapiens
Compartment: nucleoplasm
In humans, newly synthesized histone H4 is acetylated by the cytoplasmic Type B histone acetyltransferase (HAT) complex, which is composed of RBBP7 and HAT1. This interacts with histones H4 and H2A, acetylating soluble but not nucleosomal histone H4 at lysine-6 (H4K5) and lysine-13 (H4K12) and to a lesser extent lysine-6 of histone H2A (H2AK5) (Verreault et al. 1996). The HAT1:RBBP7 complex is part of the sNASP complex, a chaperone for H3-H4 (Campos et al. 2010). HAT1 also has a role in homologous recombination repair, probably as part of a larger complex, facilitating the enrichment of H4K5/K12-acetylated H3.3 to double-strand breaks thereby marking the damaged area for subsequent recruitment of key repair factors (Yang et al. 2013).

N.B. Coordinates of post-translational modifications described here follow UniProt standard practice whereby coordinates refer to the translated protein before any further processing. Histone literature typically refers to coordinates of the protein after the initiating methionine has been removed. Therefore the coordinates of post-translated residues in the Reactome database and described here are frequently +1 when compared with the literature.
Identifier: R-HSA-5218952
Species: Homo sapiens
Compartment: nucleoplasm
Histone H3 is symmetrically dimethylated on arginine-3 by PRMT5 and PRMT7 (Migliori et al. 2012, Tsai et al. 2013). This excludes binding of RBBP7, a central component of the co-repressor complexes Sin3a, NURD and PRC2. Conversely Me2sR3-histone H3 enhances binding of WDR5, a common component of the coactivator complexes MLL, SET1A, SET1B, NLS1 and ATAC. The interaction of histone H3 with WDR5 distinguishes symmetric dimethylation of arginine-3 from asymmetric dimethylation, which inhibits the recruitment of WDR5 to chromatin (Guccione et al. 2007, Hyllus et al. 2007, Migliori et al. 2012).
Identifier: R-HSA-3769447
Species: Homo sapiens
Compartment: nucleoplasm
HDAC1 and HDAC2 interact to form the catalytic core of several multisubunit complexes including the Sin3, nucleosome remodeling deacetylase (NuRD) and corepressor of REST (CoREST) complexes (Grozinger & Schreiber 2002). A 'core complex' of HDAC1/2 and the histone binding proteins RBBP7 (RbAp46) and RBBP4 (RbAp48), has been described in vivo and in vitro (Zhang et al. 1999). The Sin3 complex consists of this core complex plus SAP18 and SAP30, which appear to aid in stabilizing the protein associations and Sin3A, which serves as a scaffold for assembly of the complex and its interaction with various DNA binding proteins (Ayer 1999). Mammals express two Sin3 proteins, Sin3A and Sin3B. The recognized Sin3A core complex contains the HDAC1-2 catalytic core, SAP18 (Zhang et al. 1997), SAP30 (Zhang et al. 1998), RBBP7/4 (Ahringer 2000), SUDS3 (SAP45, SDS3) (Alland et al. 2002), ARID4B (SAP180) and SAP130 (Fleischer et al. 2003). Additional members are BRMS1 (breast cancer metastasis suppressor 1), ARID4A (Rb-binding protein 1) (Meehan et al. 2004) and SAP30L (Viiri et al. 2006). The Sin3A complex preferentially binds to hypoacetylated histones through the RBBP7/4 subunits (Vermeulen et al. 2004, Yoon et al. 2005). It can also be recruited to chromatin through the H3K4-di/trimethyl mark by ING1/2 (Shi et al. 2006, Pena et al. 2008).

The Sin3B complex shares some subunits in common with the Sin3A complex but may also contain distinct subunits (Le Guezennec et al. 2006a).

The NuRD complex contains a core histone deacetylase complex that consists of the HDAC1-2 catalytic core plus RBBP7 (RbAp46) and RBBP4 (RbAp48) (Ahringer 2000). The largest and key component is the Mi-2 remodelling subunit (dermatomyositis-specific autoantigen), which contains the ATPase/chromatin remodelling activity and physically associates with the other components. Mammals have two Mi-2 proteins: CHD3 (Mi-2alpha), and CHD4 (Mi-2 beta) (Seelig et al. 1996). CHD4 (Mi-2 beta) is the form predominantly associated with the NuRD complex (Zhang et al. 1998, Feng & Zhang 2001), although CHD3 is a member of the NuRD complex in a variety of human cell lines (Le Guezennec et al. 2006b). It is not clear whether functional differences exist between CHD3 and CHD4-containing complexes (McDonel et al. 2009). Further components are MBD3 (methyl CpG-binding domain 3), and a metastasis-associated (MTA) protein subunit. MTA subunits (e.g. Mta1, Mta2 or Mta3) appear to be mutually exclusive, possibly contributing to functional diversity of NuRD complexes (Bowen et al. 2004, Fujita et al. 2004). GATAD2A and GATAD2B proteins (formerly known as p66alpha and p66beta) are often reported as members of NuRD. MBD3 can be replaced by related protein MBD2, forming the MeCP1 complex (Feng & Zhang 2001, Le Guezennec et al. 2006b). The MeCP1 complex represents only a small proportion of the total NuRD complex in mammalian cells (Refs. in McDonel et al. 2009); MBD2 has been shown to be dispensable for normal mammalian development (Hendrich et al. 2001).

NuRD is recruited via MDB3 for DNA methylation-dependent gene silencing. It associates with MeCP1 (methyl CpG-binding protein 1) and MeCP2 to provide an intimate connection with DNA methylation (Denslow & Wade 2007, Klose & Bird 2006).

The CoREST complex minimally contains the HDAC1-2 catalytic core, REST (RE1-silencing transcription factor), RCOR1 (CoREST, KIAA0071) and KDM1A (BHC110, LSD1) (Andres et al. 1999, Humphrey et al. 2001). The BRAF–HDAC (BHC) complex consists of HDAC1-2, RCOR1, KDM1A, HMG20B (BRAF35) and PHF21A (BHC80) (Hakimi et al. 2002, Yang & Seto 2008).

This reaction represents a theoretical complete deacetylation of histone.

Complex (4 results from a total of 4)

Identifier: R-HSA-3662333
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5225642
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-606330
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-606319
Species: Homo sapiens
Compartment: nucleoplasm

Icon (1 results from a total of 1)

Species: Homo sapiens
Curator: Bruce May
Designer: Cristoffer Sevilla
RBBP4,7 icon
Set of histone-binding protein RBBP4 adn RBBP7
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