Histone-binding protein RBBP7 (RBBP7)

The protein contains 425 amino acids for an estimated molecular weight of 47820 Da.

 

Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 100%
Model score: 88
MODL_MODELLER-9.18

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The reference OMIM entry for this protein is 300825

Retinoblastoma-binding protein 7; rbbp7

CLONING

The RB1 protein (614041) interacts with multiple cellular proteins that mediate its functions. RBBP4 (602923) and RBBP7 were the 2 most abundant proteins from HeLa cell lysates that were specifically retained by an RB1 affinity column (Qian et al., 1993). By screening a HeLa cell cDNA expression library with monoclonal antibodies against RBBP7, Qian and Lee (1995) isolated cDNAs encoding RBBP7, which they called RbAp46. Southern blot analysis indicated that the human genome contains a single copy of the RBBP7 gene. The predicted 425-amino acid human RBBP7 protein is identical to mouse Rbbp7 except for 1 conserved amino acid substitution, and it is 89% identical to human RBBP4. RBBP7 contains internal trp-asp (WD) repeats that are conserved with those of RBBP4. By Western blot analysis, RBBP7 from HeLa cell lysates had a molecular mass of 46 kD. RNase protection analysis detected Rbbp7 mRNA in all mouse tissues examined, although the levels varied dramatically between different tissues. Yang et al. (2002) noted that RBBP7 is highly conserved between mammals, flies, and plants, with highest conservation in the WD repeat region. In developing mouse, Rbbp7 expression began at embryonic day 9.5, was dynamic, and persisted throughout embryogenesis. RBBP7 was expressed in all adult mouse tissues and mammalian cell lines examined, including HEK293 and HeLa cells.

GENE FUNCTION

Qian and Lee (1995) showed that RBBP7 formed a complex with RB1 in vitro and in vivo. In yeast, RBBP7 could mimic the function of S. cerevisiae Msi1, a presumed negative regulator of the Ras signal transduction pathway. Using reporter gene assays, Yang et al. (2002) demonstrated that mouse Rbbp7 functioned as a transcriptional repressor that inhibited mitogen-stimulated transactivation of FOS (164810) in transfected COS-1 cells.

MAPPING

By genomic sequence analysis, Yang et al. (2002) mapped the RBBP7 gene to chromosome Xp22.13. They mapped the mouse Rbbp7 gene to the X chromosome. ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 300825 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed