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Search results 901 to 976 out of 976 for Crebbp

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Type Details Score
Publication
25653165 | -
First Author: Itoh T
Year: 2015
Journal: Nucleic Acids Res
Title: Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting.
Volume: 43
Issue: 4
Pages: 2033-44
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Publication
16885027 | -
First Author: Yang M
Year: 2006
Journal: Mol Cell
Title: Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase.
Volume: 23
Issue: 3
Pages: 377-87
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Publication
11171972 | -
First Author: You A
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: CoREST is an integral component of the CoREST- human histone deacetylase complex.
Volume: 98
Issue: 4
Pages: 1454-8
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Protein Domain
IPR009349 | TRIP4/RQT4_C2HC5_Znf
Type: Domain
Description: This entry represents a C2HC5-type zinc finger found in human activating signal cointegrator 1 (ASC-1, also known as TRIP4) and its orthologue from yeast RQC trigger complex subunit RQT4 which function as part of the RQC trigger (RQT) complex that activates the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation [, , ]. TRIP4 has also been described as a transcription coactivator which associates with nuclear receptors and transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription [, ].Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead, they bind other metals, such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog); however, they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g., some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
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Protein
Q9QXN3
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
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Protein
Q3UJV0
Organism: Mus musculus/domesticus
Length: 581  
Fragment?: false
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Publication
10454579 | -
First Author: Kim HJ
Year: 1999
Journal: Mol Cell Biol
Title: Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation.
Volume: 19
Issue: 9
Pages: 6323-32
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Publication
32099016 | -
First Author: Hashimoto S
Year: 2020
Journal: Sci Rep
Title: Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells.
Volume: 10
Issue: 1
Pages: 3422
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Publication
36302773 | -
First Author: Narita M
Year: 2022
Journal: Nat Commun
Title: A distinct mammalian disome collision interface harbors K63-linked polyubiquitination of uS10 to trigger hRQT-mediated subunit dissociation.
Volume: 13
Issue: 1
Pages: 6411
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Publication
25219498 | J:215542
First Author: Yoo HM
Year: 2014
Journal: Mol Cell
Title: Modification of ASC1 by UFM1 is crucial for ER? transactivation and breast cancer development.
Volume: 56
Issue: 2
Pages: 261-274
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Publication
32579943 | -
First Author: Juszkiewicz S
Year: 2020
Journal: Mol Cell
Title: The ASC-1 Complex Disassembles Collided Ribosomes.
Volume: 79
Issue: 4
Pages: 603-614.e8
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Protein
Q6GQV9
Organism: Mus musculus/domesticus
Length: 1589  
Fragment?: true
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Protein
A0A0A6YX54
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
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Protein
A0A0A6YXI3
Organism: Mus musculus/domesticus
Length: 55  
Fragment?: true
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Protein
D3YUX3
Organism: Mus musculus/domesticus
Length: 76  
Fragment?: true
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Publication
22654911 | J:389650
 
First Author: Marchbank K
Year: 2012
Journal: Int J Cell Biol
Title: MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network.
Volume: 2012
Pages: 208014
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Publication
26765567 | -
   
First Author: Dagdas YF
Year: 2016
Journal: Elife
Title: An effector of the Irish potato famine pathogen antagonizes a host autophagy cargo receptor.
Volume: 5
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Publication
29932422 | -
   
First Author: Dagdas YF
Year: 2018
Journal: Elife
Title: Host autophagy machinery is diverted to the pathogen interface to mediate focal defense responses against the Irish potato famine pathogen.
Volume: 7
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Publication
24692539 | -
First Author: Walinda E
Year: 2014
Journal: J Biol Chem
Title: Solution structure of the ubiquitin-associated (UBA) domain of human autophagy receptor NBR1 and its interaction with ubiquitin and polyubiquitin.
Volume: 289
Issue: 20
Pages: 13890-902
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Protein
B2RWS6
Organism: Mus musculus/domesticus
Length: 2412  
Fragment?: false
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Protein
F8VPR5
Organism: Mus musculus/domesticus
Length: 2441  
Fragment?: false
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Protein
A0A0U1RQB6
Organism: Mus musculus/domesticus
Length: 2403  
Fragment?: false
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Protein
Q8QZV8
Organism: Mus musculus/domesticus
Length: 2429  
Fragment?: true
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Protein
Q3TT38
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
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Protein
A0A3B2W3W9
Organism: Mus musculus/domesticus
Length: 223  
Fragment?: false
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Protein
A0A3B2WCT9
Organism: Mus musculus/domesticus
Length: 238  
Fragment?: false
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Protein
B2KF52
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
B2KF54
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
A0A3B2W3Q3
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
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Protein
B2RPS0
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
A0A087WPR8
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
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Protein
A0A0A6YXP4
Organism: Mus musculus/domesticus
Length: 281  
Fragment?: true
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Protein
A0A0U1RPQ3
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: true
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Protein
F6S397
Organism: Mus musculus/domesticus
Length: 712  
Fragment?: true
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Protein
Q8CFE3
Organism: Mus musculus/domesticus
Length: 480  
Fragment?: false
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Protein
Q6PGA0
Organism: Mus musculus/domesticus
Length: 451  
Fragment?: false
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Protein
Q8C796
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
A0A0A6YWP7
Organism: Mus musculus/domesticus
Length: 447  
Fragment?: false
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Protein
A0A0A6YWY4
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
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Protein
A0A0A6YXM5
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
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Protein
A0A0R4J1I0
Organism: Mus musculus/domesticus
Length: 479  
Fragment?: false
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Protein
A0A140T8R7
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
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Protein
B2RSN6
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
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Protein
Q3U224
Organism: Mus musculus/domesticus
Length: 1011  
Fragment?: true
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Protein
Q8BJ14
Organism: Mus musculus/domesticus
Length: 714  
Fragment?: false
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Protein
Q8BUZ9
Organism: Mus musculus/domesticus
Length: 1010  
Fragment?: true
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Protein
A2A4N5
Organism: Mus musculus/domesticus
Length: 906  
Fragment?: false
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Protein
E9Q2I4
Organism: Mus musculus/domesticus
Length: 1089  
Fragment?: false
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Protein
Q05BC8
Organism: Mus musculus/domesticus
Length: 888  
Fragment?: false
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Protein
Q6ZQK3
Organism: Mus musculus/domesticus
Length: 915  
Fragment?: true
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Protein
Q91ZQ8
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: true
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Protein
A0A1Y7VP67
Organism: Mus musculus/domesticus
Length: 1071  
Fragment?: true
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Protein
G3UXB2
Organism: Mus musculus/domesticus
Length: 888  
Fragment?: false
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Publication
- | J:237616
     
First Author: MGI and IMPC
Year: 2017
Journal: MGI Direct Data Submission
Title: MGI Curation of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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Protein
P97432
Organism: Mus musculus/domesticus
Length: 988  
Fragment?: false
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Protein
Q0GGX2
Organism: Mus musculus/domesticus
Length: 1363  
Fragment?: false
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Protein
Q8BXJ2
Organism: Mus musculus/domesticus
Length: 1205  
Fragment?: false
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Protein
A1L329
Organism: Mus musculus/domesticus
Length: 988  
Fragment?: false
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Protein
A2A4N7
Organism: Mus musculus/domesticus
Length: 963  
Fragment?: false
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Protein
A2A4N8
Organism: Mus musculus/domesticus
Length: 951  
Fragment?: false
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Protein
K3W4P1
Organism: Mus musculus/domesticus
Length: 988  
Fragment?: false
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Publication
20412781 | J:140465
First Author: Guo G
Year: 2010
Journal: Dev Cell
Title: Resolution of cell fate decisions revealed by single-cell gene expression analysis from zygote to blastocyst.
Volume: 18
Issue: 4
Pages: 675-85
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Publication
12904583 | J:85162
First Author: Hansen J
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A large-scale, gene-driven mutagenesis approach for the functional analysis of the mouse genome.
Volume: 100
Issue: 17
Pages: 9918-22
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Publication
- | J:384794
     
First Author: MGI and IMPC
Year: 2026
Journal: Database Release
Title: MGI Load of Molecular Notes for Endonuclease-Mediated (CRISPR) Alleles from the International Mouse Phenotyping Consortium (IMPC)
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Publication
- | J:342612
       
First Author: UniProt curators
Year: 2014
Title: Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
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Publication
38355793 | J:345621
First Author: Adams DJ
Year: 2024
Journal: Nature
Title: Genetic determinants of micronucleus formation in vivo.
Volume: 627
Issue: 8002
Pages: 130-136
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Publication
- | J:211773
     
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
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Publication
18799693 | J:142754
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
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Publication
16602821 | J:162220
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
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Publication
12665246 | -
First Author: Matthews JM
Year: 2002
Journal: IUBMB Life
Title: Zinc fingers--folds for many occasions.
Volume: 54
Issue: 6
Pages: 351-5
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Publication
17210253 | -
First Author: Gamsjaeger R
Year: 2007
Journal: Trends Biochem Sci
Title: Sticky fingers: zinc-fingers as protein-recognition motifs.
Volume: 32
Issue: 2
Pages: 63-70
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Publication
15963892 | -
First Author: Hall TM
Year: 2005
Journal: Curr Opin Struct Biol
Title: Multiple modes of RNA recognition by zinc finger proteins.
Volume: 15
Issue: 3
Pages: 367-73
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Publication
15718139 | -
First Author: Brown RS
Year: 2005
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: getting a grip on RNA.
Volume: 15
Issue: 1
Pages: 94-8
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Publication
10529348 | -
First Author: Klug A
Year: 1999
Journal: J Mol Biol
Title: Zinc finger peptides for the regulation of gene expression.
Volume: 293
Issue: 2
Pages: 215-8
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Publication
11179890 | -
First Author: Laity JH
Year: 2001
Journal: Curr Opin Struct Biol
Title: Zinc finger proteins: new insights into structural and functional diversity.
Volume: 11
Issue: 1
Pages: 39-46
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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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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