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Search results 601 to 625 out of 625 for Ncoa1

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Type Details Score
Protein Domain
IPR037077 | Nuc_rcpt_coact_Ncoa_int_sf
Type: Homologous_superfamily
Description: This entry represents the interlockingdomain superfamily of the eukaryotic nuclear receptor coactivators Ncoa1, Ncoa2 and Ncoa3. The interlocking domain forms a 3-helical non-globular array that forms interlocked heterodimers with its target.Nuclear receptors are ligand-activated transcription factors involved in the regulation of many processes, including development, reproduction and homeostasis. Nuclear receptor coactivators act to modulate the function of nuclear receptors. Coactivators associate with promoters and enhancers primarily through protein-protein contacts to facilitate the interaction between DNA-bound transcription factors and the transcription machinery. In addition to their role as coactivators of various nuclear receptors, Ncoa1 and Ncoa3 both have histone acetyltransferase activity (), but Ncoa2 does not [, ].
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Publication
15145939 | -
First Author: Arimura A
Year: 2004
Journal: J Biol Chem
Title: The transcriptional co-activator p/CIP (NCoA-3) is up-regulated by STAT6 and serves as a positive regulator of transcriptional activation by STAT6.
Volume: 279
Issue: 30
Pages: 31105-12
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Publication
27958775 | J:356789
First Author: Manesia JK
Year: 2017
Journal: Stem Cells Dev
Title: Distinct Molecular Signature of Murine Fetal Liver and Adult Hematopoietic Stem Cells Identify Novel Regulators of Hematopoietic Stem Cell Function.
Volume: 26
Issue: 8
Pages: 573-584
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Publication
14757047 | -
First Author: Razeto A
Year: 2004
Journal: J Mol Biol
Title: Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain.
Volume: 336
Issue: 2
Pages: 319-29
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Protein Domain
IPR009110 | Nuc_rcpt_coact
Type: Homologous_superfamily
Description: This superfamily represents the interlocking domain of various eukaryotic nuclear receptor coactivators, including CREBP, P300, Ncoa1, Ncoa2 and Ncoa3. The interlocking domain forms a 3-helical non-globular array that forms interlocked heterodimers with its target.Nuclear receptors are ligand-activated transcription factors involved in the regulation of many processes, including development, reproduction and homeostasis. Nuclear receptor coactivators act to modulate the function of nuclear receptors. Coactivators associate with promoters and enhancers primarily through protein-protein contacts to facilitate the interaction between DNA-bound transcription factors and the transcription machinery. Many of these coactivators are structurally related, including CBP (CREB-binding protein), P300 and ACTR (activator for thyroid and retinoid receptors) []. CBP and P300 both have histone acetyltransferase activity (). CBP/P300 proteins function synergistically to activate transcription, acting to remodel chromatin and to recruit RNA polymerase II and the basal transcription machinery. CBP is required for proper cell cycle control, differentiation and apoptosis. The interaction of CBP/P300 with transcription factors involves several small domains. The IBiD domain in the C-terminal of CBP is responsible for CBP interaction with IRF-3, as well as with the adenoviral oncoprotein E1A, TIF-2 coactivator, and the IRF homologue KSHV IRF-1 [].Ncoa1, Ncoa2 and Ncoa3 are all coactivators of various nuclear receptors. In addition, Ncoa1 and Ncoa3 both have histone acetyltransferase activity, but Ncoa2 does not [, ].
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Protein
Q8CBM5
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: true
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Protein
A5D6Q2
Organism: Mus musculus/domesticus
Length: 1353  
Fragment?: true
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Publication
11823864 | J:230369
First Author: Demarest SJ
Year: 2002
Journal: Nature
Title: Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators.
Volume: 415
Issue: 6871
Pages: 549-53
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Publication
11583620 | J:71923
First Author: Lin CH
Year: 2001
Journal: Mol Cell
Title: A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies.
Volume: 8
Issue: 3
Pages: 581-90
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Protein
Q61026
Organism: Mus musculus/domesticus
Length: 1462  
Fragment?: false
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Protein
O09000
Organism: Mus musculus/domesticus
Length: 1398  
Fragment?: false
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Protein
Q05BA5
Organism: Mus musculus/domesticus
Length: 1403  
Fragment?: false
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Protein
Q3UQL7
Organism: Mus musculus/domesticus
Length: 1403  
Fragment?: false
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Protein
B2RUJ1
Organism: Mus musculus/domesticus
Length: 1397  
Fragment?: false
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Protein
A2A468
Organism: Mus musculus/domesticus
Length: 1402  
Fragment?: false
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Protein
Q7TPU7
Organism: Mus musculus/domesticus
Length: 1393  
Fragment?: false
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Protein
A6P3E3
Organism: Mus musculus/domesticus
Length: 1393  
Fragment?: false
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Protein
E9PV80
Organism: Mus musculus/domesticus
Length: 1393  
Fragment?: false
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Protein
P52633
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
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Protein
Q8R4D4
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
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Protein
B2RWS6
Organism: Mus musculus/domesticus
Length: 2412  
Fragment?: false
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Protein
P45481
Organism: Mus musculus/domesticus
Length: 2441  
Fragment?: false
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Protein
Q8QZV8
Organism: Mus musculus/domesticus
Length: 2429  
Fragment?: true
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Protein
A0A0U1RQB6
Organism: Mus musculus/domesticus
Length: 2403  
Fragment?: false
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Protein
F8VPR5
Organism: Mus musculus/domesticus
Length: 2441  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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