C-Terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate Polycomb proteins

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C-Terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate Polycomb proteins is …
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scholarly articleQ13442814

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P356DOI10.1128/MCB.19.1.777
P932PMC publication ID83934
P698PubMed publication ID9858600

P2093author name stringA P Otte
D P Satijn
M J Gunster
J van der Vlag
R G Sewalt
P2860cites workMolecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformationQ24303599
RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressorQ24312810
A novel C-terminal binding protein (CTBP2) is closely related to CTBP1, an adenovirus E1A-binding protein, and maps to human chromosome 21q21.3Q24312935
Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexesQ24315759
Interference with the expression of a novel human polycomb protein, hPc2, results in cellular transformation and apoptosisQ24315842
A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation, tumorigenesis and metastasisQ24321630
Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: indication for separate Pc-G complexesQ24522505
Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeoticQ24646581
The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunitQ27860669
Analysis of the functional role of the Polycomb chromo domain in Drosophila melanogasterQ28281915
Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain.Q28587211
Drosophila CtBP: a Hairy-interacting protein required for embryonic segmentation and hairy-mediated transcriptional repressionQ33888622
Polycomb and polyhomeotic are constituents of a multimeric protein complex in chromatin of Drosophila melanogasterQ33938173
The mouse has a Polycomb-like chromobox geneQ34243273
Assignment of a Polycomb-like chromobox gene (CBX2) to human chromosome 17q25.Q34313097
Identification of Bmi1-interacting proteins as constituents of a multimeric mammalian polycomb complexQ34414481
The CtBP binding domain in the adenovirus E1A protein controls CR1-dependent transactivationQ34601820
Transcriptional silencing by the Polycomb protein in Drosophila embryosQ37695168
Transcriptional repression by Drosophila and mammalian Polycomb group proteins in transfected mammalian cellsQ38310778
Transcriptional regulation of the adenovirus E1A geneQ40411825
Related chromosome binding sites for zeste, suppressors of zeste and Polycomb group proteins in Drosophila and their dependence on Enhancer of zeste functionQ40872575
PcG complexes and chromatin silencingQ41441687
In vivo binding pattern of a trans-regulator of homoeotic genes in Drosophila melanogasterQ41505979
Functions of mammalian Polycomb group and trithorax group related genesQ41600966
Interaction of short-range repressors with Drosophila CtBP in the embryo.Q46037430
Polycomb and bmi-1 homologs are expressed in overlapping patterns in Xenopus embryos and are able to interact with each otherQ48070837
Murine Polycomb- and trithorax-group genes regulate homeotic pathways and beyond.Q52194910
Polycomb in plantsQ95824599
P433issue1
P407language of work or nameEnglishQ1860
P304page(s)777-87
P577publication date1999-01-01
P1433published inMolecular and Cellular BiologyQ3319478
P1476titleC-Terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate Polycomb proteins
P478volume19

Reverse relations

cites work (P2860)
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Q33965793dCtBP-dependent and -independent repression activities of the Drosophila Knirps protein

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