A CREB-binding protein that is encoded in the genome of human. [PMID:11331617]
Target | Category | Definition |
transcription coactivator binding | molecular function | Binding 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 binding | molecular function | Binding to one of the p53 family of proteins. [GOC:hjd] |
chromatin binding | molecular function | Binding 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 binding | molecular function | Binding to damaged DNA. [GOC:jl] |
transcription coactivator activity | molecular function | A 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 activity | molecular function | A 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 activity | molecular function | Catalysis of the reaction: acetyl-CoA + histone = CoA + acetyl-histone. [EC:2.3.1.48] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
acetyltransferase activity | molecular function | Catalysis of the transfer of an acetyl group to an acceptor molecule. [GOC:ai] |
peptide N-acetyltransferase activity | molecular function | Catalysis 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 binding | molecular function | Binding to Myogenic Regulatory Factor (MRF), a member of the basic Helix-Loop-Helix (bHLH) superfamily of transcription factors. [PMID:10966875] |
histone H3K18 acetyltransferase activity | molecular function | Catalysis 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 activity | molecular function | Catalysis 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 binding | molecular function | Binding 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 activity | molecular function | Catalysis of the reaction: acetyl-CoA + lysine in peptide = CoA + N-acetyl-lysine-peptide. [GOC:dph, RHEA:45948] |
peptide lactyltransferase activity | molecular function | Catalysis 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 binding | molecular function | Binding 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 binding | molecular function | Binding to DNA that is assembled into chromatin. [GOC:mah] |
Target | Category | Definition |
negative regulation of transcription by RNA polymerase II | biological process | Any 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 hypoxia | biological process | Any 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 pathway | biological process | The 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 remodeling | biological process | A 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 transcription | biological process | Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |
protein acetylation | biological process | The addition of an acetyl group to a protein amino acid. An acetyl group is CH3CO-, derived from acetic [ethanoic] acid. [GOC:ai] |
signal transduction | biological process | The 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 transduction | biological process | An 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 pathway | biological process | Any process that modulates the frequency, rate or extent of smoothened signaling. [GOC:go_curators] |
negative regulation of transcription by RNA polymerase I | biological process | Any 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 acetylation | biological process | The acetylation of the N-terminal lysine of proteins. [GOC:ai] |
positive regulation of transforming growth factor beta receptor signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity. [GOC:go_curators] |
protein destabilization | biological process | Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation. [GOC:mah] |
cellular response to nutrient levels | biological process | Any 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 UV | biological process | Any 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 process | biological process | Any biological process involved in the maintenance of an internal steady state. [GOC:jl, ISBN:0395825172] |
embryonic digit morphogenesis | biological process | The 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 transcription | biological process | Any 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 II | biological process | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH] |
rhythmic process | biological process | Any process pertinent to the generation and maintenance of rhythms in the physiology of an organism. [GOC:jid] |
protein-containing complex assembly | biological process | The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex. [GOC:jl] |
regulation of cellular response to heat | biological process | Any process that modulates the frequency, rate or extent of cellular response to heat. [GOC:TermGenie, GOC:yaf] |
positive regulation of protein localization to nucleus | biological process | Any 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 recombination | biological process | Any 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] |