Page last updated: 2024-08-08 00:07:31

CREB-binding protein

A CREB-binding protein that is encoded in the genome of human. [PMID:11331617]

Synonyms

Histone lysine acetyltransferase CREBBP;
2.3.1.48;
Protein-lysine acetyltransferase CREBBP;
2.3.1.-

Research

Bioassay Publications (17)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's14 (82.35)24.3611
2020's3 (17.65)2.80

Compounds (30)

Drugs with Potency Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
altretamineHomo sapiens (human)Potency25.118910
cgs 15943Homo sapiens (human)Potency10.578530
etazolateHomo sapiens (human)Potency5.441530
nocodazoleHomo sapiens (human)Potency1.194630
papaverineHomo sapiens (human)Potency5.690440
ici 136,753Homo sapiens (human)Potency5.298530
colchicineHomo sapiens (human)Potency5.011920
oxoglaucineHomo sapiens (human)Potency1.440330
mrs 1220Homo sapiens (human)Potency1.995020
rolipramHomo sapiens (human)Potency0.039220
4-(1H-benzimidazol-2-ylmethylthio)-2-methylbenzofuro[3,2-d]pyrimidineHomo sapiens (human)Potency0.500420
2-(4-benzofuro[3,2-d]pyrimidinylthio)-1-thiophen-2-ylethanoneHomo sapiens (human)Potency4.601120
4-[2-(9-methyl-6-indolo[3,2-b]quinoxalinyl)ethyl]morpholineHomo sapiens (human)Potency12.174330
N-[4,6-bis(4-morpholinyl)-1,3,5-triazin-2-yl]-2-(methylthio)-1,3-benzothiazol-6-amineHomo sapiens (human)Potency12.779730
fisetinHomo sapiens (human)Potency17.045320

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
3-(5'-hydroxymethyl-2'-furyl)-1-benzylindazoleHomo sapiens (human)IC501.300011
n-methylpyrrolidoneHomo sapiens (human)IC502,300.000011
4-Methyl-1,3,4,5-tetrahydro-2H-1,5-benzodiazepin-2-oneHomo sapiens (human)IC5032.000011
epigallocatechin gallateHomo sapiens (human)IC5050.000022
delphinidinHomo sapiens (human)IC5030.000011
2-methyl-2,3,4,5-tetrahydro-1,5-benzoxazepin-4-oneHomo sapiens (human)IC5010.000011
methyl indole-3-carboxylateHomo sapiens (human)IC5099.000011
curcuminHomo sapiens (human)IC5025.000044
icg 001Homo sapiens (human)IC503.000011
jq1 compoundHomo sapiens (human)IC509.715333
i-bet726Homo sapiens (human)IC5031.622811
rvx 208Homo sapiens (human)IC5010.000022

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
jq1 compoundHomo sapiens (human)Kd9.600011
gsk525762aHomo sapiens (human)Kd46.500022
gsk1210151aHomo sapiens (human)Kd3.084011
i-bet726Homo sapiens (human)Kd6.300011
2-methoxy-n-(3-methyl-2-oxo-1,2,3,4-tetrahydroquinazolin-6-yl)benzenesulfonamideHomo sapiens (human)Kd49.000011
rvx 208Homo sapiens (human)Kd10.000011

Enables

This protein enables 19 target(s):

TargetCategoryDefinition
transcription coactivator bindingmolecular functionBinding to a transcription coactivator, a protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery. [GOC:krc]
p53 bindingmolecular functionBinding to one of the p53 family of proteins. [GOC:hjd]
chromatin bindingmolecular functionBinding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. [GOC:jl, ISBN:0198506732, PMID:20404130]
damaged DNA bindingmolecular functionBinding to damaged DNA. [GOC:jl]
transcription coactivator activitymolecular functionA transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. [GOC:txnOH-2018, PMID:10213677, PMID:16858867]
transcription corepressor activitymolecular functionA transcription coregulator activity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription corepressors modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. [GOC:txnOH-2018, PMID:10213677, PMID:16858867]
histone acetyltransferase activitymolecular functionCatalysis of the reaction: acetyl-CoA + histone = CoA + acetyl-histone. [EC:2.3.1.48]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
zinc ion bindingmolecular functionBinding to a zinc ion (Zn). [GOC:ai]
acetyltransferase activitymolecular functionCatalysis of the transfer of an acetyl group to an acceptor molecule. [GOC:ai]
peptide N-acetyltransferase activitymolecular functionCatalysis of the acetylation of an amino acid residue of a peptide or protein, according to the reaction: acetyl-CoA + peptide = CoA + N-acetylpeptide. [GOC:mah]
MRF bindingmolecular functionBinding to Myogenic Regulatory Factor (MRF), a member of the basic Helix-Loop-Helix (bHLH) superfamily of transcription factors. [PMID:10966875]
histone H3K18 acetyltransferase activitymolecular functionCatalysis of the reaction: acetyl-CoA + histone H3 L-lysine (position 18) = CoA + histone H3 N6-acetyl-L-lysine (position 18). [EC:2.3.1.48]
histone H3K27 acetyltransferase activitymolecular functionCatalysis of the reaction: acetyl-CoA + histone H3 L-lysine (position 27) = CoA + histone H3 N6-acetyl-L-lysine (position 27). [EC:2.3.1.48]
RNA polymerase II-specific DNA-binding transcription factor bindingmolecular functionBinding to a sequence-specific DNA binding RNA polymerase II transcription factor, any of the factors that interact selectively and non-covalently with a specific DNA sequence in order to modulate transcription. [GOC:dph, GOC:vw]
peptide-lysine-N-acetyltransferase activitymolecular functionCatalysis of the reaction: acetyl-CoA + lysine in peptide = CoA + N-acetyl-lysine-peptide. [GOC:dph, RHEA:45948]
peptide lactyltransferase activitymolecular functionCatalysis of the reaction: (L-lysyl-[protein] + lactoyl-CoA = CoA + H+ + N(6)-lactoyl-L-lysyl-[protein]. [GOC:sp, PMID:31645732, RHEA:61996]
DNA-binding transcription factor bindingmolecular functionBinding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription. [GOC:txnOH-2018]
chromatin DNA bindingmolecular functionBinding to DNA that is assembled into chromatin. [GOC:mah]

Located In

This protein is located in 5 target(s):

TargetCategoryDefinition
nucleuscellular componentA membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
nucleoplasmcellular componentThat part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
nuclear bodycellular componentExtra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins. [GOC:ma, PMID:10330182]

Active In

This protein is active in 1 target(s):

TargetCategoryDefinition
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]

Part Of

This protein is part of 3 target(s):

TargetCategoryDefinition
chromatincellular componentThe ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. [GOC:elh, PMID:20404130]
histone acetyltransferase complexcellular componentA protein complex that possesses histone acetyltransferase activity. [GOC:mah]
transcription regulator complexcellular componentA protein complex that is capable of associating with DNA by direct binding, or via other DNA-binding proteins or complexes, and regulating transcription. [GOC:jl]

Involved In

This protein is involved in 24 target(s):

TargetCategoryDefinition
negative regulation of transcription by RNA polymerase IIbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. [GOC:go_curators, GOC:txnOH]
response to hypoxiabiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. [GOC:hjd]
stimulatory C-type lectin receptor signaling pathwaybiological processThe series of molecular signals initiated by the binding of C-type lectin to its receptor on the surface of a target cell, and resulting in cellular activation. [GO_REF:0000022, GOC:add, ISBN:0781735149]
chromatin remodelingbiological processA dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication. [GOC:jid, GOC:vw, PMID:12042764, PMID:12697820]
regulation of DNA-templated transcriptionbiological processAny process that modulates the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH]
protein acetylationbiological processThe addition of an acetyl group to a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid. [GOC:ai]
signal transductionbiological processThe cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. [GOC:go_curators, GOC:mtg_signaling_feb11]
canonical NF-kappaB signal transductionbiological processAn intracellular signaling cassette characterized by the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB, also known as the canonical NF-kappaB signaling cascade. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. The canonical NF-kappaB pathway is mainly stimulated by proinflammatory cytokines such as IL-1beta, tumor necrosis factor (TNF)-alpha, antigen ligands, and toll-like receptors (TLRs). [GOC:bf, PMID:12773372, PMID:34659217]
regulation of smoothened signaling pathwaybiological processAny process that modulates the frequency, rate or extent of smoothened signaling. [GOC:go_curators]
negative regulation of transcription by RNA polymerase Ibiological processAny process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase I. [GOC:go_curators]
N-terminal peptidyl-lysine acetylationbiological processThe acetylation of the N-terminal lysine of proteins. [GOC:ai]
positive regulation of transforming growth factor beta receptor signaling pathwaybiological processAny process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity. [GOC:go_curators]
protein destabilizationbiological processAny process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation. [GOC:mah]
cellular response to nutrient levelsbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients. [GOC:mah]
cellular response to UVbiological processAny process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers. [GOC:mah]
homeostatic processbiological processAny biological process involved in the maintenance of an internal steady state. [GOC:jl, ISBN:0395825172]
embryonic digit morphogenesisbiological processThe process, occurring in the embryo, by which the anatomical structures of the digit are generated and organized. A digit is one of the terminal divisions of an appendage, such as a finger or toe. [GOC:bf, GOC:jl, UBERON:0002544]
positive regulation of DNA-templated transcriptionbiological processAny process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH]
positive regulation of transcription by RNA polymerase IIbiological processAny process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH]
rhythmic processbiological processAny process pertinent to the generation and maintenance of rhythms in the physiology of an organism. [GOC:jid]
protein-containing complex assemblybiological processThe aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex. [GOC:jl]
regulation of cellular response to heatbiological processAny process that modulates the frequency, rate or extent of cellular response to heat. [GOC:TermGenie, GOC:yaf]
positive regulation of protein localization to nucleusbiological processAny process that activates or increases the frequency, rate or extent of protein localization to nucleus. [GOC:TermGenie]
positive regulation of double-strand break repair via homologous recombinationbiological processAny process that activates or increases the frequency, rate or extent of double-strand break repair via homologous recombination. [GO_REF:0000058, GOC:TermGenie, PMID:12023299]