B2RWS6

SS
Gene name
Ep300 (P300)
Protein name
Histone acetyltransferase p300
Names
p300 HAT , EC 2.3.1.48 , E1A-associated protein p300 , Histone butyryltransferase p300 , EC 2.3.1.- , Histone crotonyltransferase p300 , EC 2.3.1.- , Protein 2-hydroxyisobutyryltransferase p300 , EC 2.3.1.- , Protein lactyltransferas p300 , EC 2.3.1.- , Protein propionyltransferase p300 , EC 2.3.1.-
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:328572
EC number
2.3.1.48: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

Histone acetyltransferase p300 (EP300, also known as p300) is an enzyme that functions as histone acetyltransferase that regulates transcription of genes. It plays an essential role in regulating cell growth and division, prompting cells to mature and assume specialized functions, and preventing the growth of cancerous tumors. EP300 contains several domains including the CH1, KIX, CH3 (ZZ-TAZ2) and NCBD domains, which enable the interaction with numerous transcription factors and the basal transcription machinery. The activity of EP300 is regulated by its RING domain, or autoinhibitory loop within the HAT domain. The RING domain sterically occludes the HAT active site, and the displacement of the RING domain coupled to autoacetylation in trans results in full catalytic activation. Furthermore, the catalytic activity of EP300 is also regulated through acetylation / deacetylation of the autoinhibitory loop in the HAT domain, which impedes the acetyltransferase activity of EP300 but releases the inhibition upon hyper autoacetylation.

Autoinhibitory domains (AIDs)

1167-1241 (RING domain) SS

Target domain

1284-1663 (HAT domain)

Relief mechanism

PTM

Assay

1519-1580 (Autoinhibitory loop) SS

Target domain

1284-1663 (HAT domain)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B2RWS6

Entry ID Method Resolution Chain Position Source
AF-B2RWS6-F1 Predicted AlphaFoldDB

98 variants for B2RWS6

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3406215366 92 N>D No EVA
rs3406520285 94 N>S No EVA
rs240373534 103 A>V No EVA
rs3389383035 132 T>I No EVA
rs3404772927 174 M>I No EVA
rs221667414 243 L>H No EVA
rs3406445815 250 N>D No EVA
rs3389369722 280 V>D No EVA
rs3406380551 286 S>C No EVA
rs3406305320 291 D>E No EVA
rs3406305347 292 K>I No EVA
rs3389371766 345 L>I No EVA
rs3389294777 430 I>N No EVA
rs3389294777 430 I>S No EVA
rs3389344569 435 P>L No EVA
rs3389378188 449 Q>H No EVA
rs3389383011 453 S>G No EVA
rs3389294741 488 Q>* No EVA
rs3389383041 504 M>I No EVA
rs3389369398 553 S>F No EVA
rs3389373214 591 A>D No EVA
rs3389373147 592 I>T No EVA
rs3389390793 598 P>H No EVA
rs3389337735 606 M>L No EVA
rs264937704 677 G>E No EVA
rs237308330 704 M>I No EVA
rs3389369759 735 Q>H No EVA
rs1131776938 743 S>F No EVA
rs48878190 743 S>P No EVA
rs3389327637 820 C>S No EVA
rs3406684985 838 R>C No EVA
rs3389378218 873 P>L No EVA
rs3551839318 894 P>L No EVA
rs3406684933 968 E>V No EVA
rs224190411 979 S>A No EVA
rs232285898 1001 G>A No EVA
rs257476420 1004 V>A No EVA
rs214616191 1029 P>A No EVA
rs3389369439 1064 L>F No EVA
rs3389371762 1066 R>L No EVA
rs3389294746 1073 P>H No EVA
rs3389376054 1106 D>H No EVA
rs3389374966 1122 L>F No EVA
rs3389376114 1134 T>A No EVA
rs3389383084 1139 K>R No EVA
rs3389344587 1244 V>I No EVA
rs3389378251 1259 L>I No EVA
rs3389390731 1347 E>D No EVA
rs3389369448 1418 I>F No EVA
rs3389378197 1440 S>R No EVA
rs3389344588 1448 H>P No EVA
rs3389366266 1448 H>Q No EVA
rs3389383079 1449 C>R No EVA
rs3413041647 1450 H>P No EVA
rs3389339137 1476 E>* No EVA
rs3389327606 1478 I>M No EVA
rs3389378191 1496 S>N No EVA
rs3389294724 1500 L>I No EVA
rs3389376090 1500 L>P No EVA
rs3389383050 1513 E>* No EVA
rs3389385581 1517 K>N No EVA
rs3389366202 1530 E>* No EVA
rs3389374875 1622 L>M No EVA
rs3389376085 1632 L>I No EVA
rs3406305348 1643 L>V No EVA
rs3389294735 1647 Q>L No EVA
rs3389378180 1684 V>L No EVA
rs3389339093 1692 I>N No EVA
rs3389378196 1694 C>* No EVA
rs3389378238 1699 N>D No EVA
rs3389374874 1717 N>S No EVA
rs3389371758 1733 S>N No EVA
rs3389327625 1740 S>F No EVA
rs3389339096 1745 C>Y No EVA
rs3389369444 1782 K>N No EVA
rs3389390774 1794 H>Y No EVA
rs3389354914 1797 E>K No EVA
rs3389294847 1818 Q>R No EVA
rs3389294864 1833 S>N No EVA
rs3389327621 1867 T>I No EVA
rs3389339080 1874 S>P No EVA
rs3389385552 1876 P>Q No EVA
rs3389294840 1910 T>N No EVA
rs3406684989 1920 P>A No EVA
rs3406422394 1920 P>Q No EVA
rs3389369700 1989 G>* No EVA
rs3389371784 1997 A>G No EVA
rs3389369450 2028 M>K No EVA
rs3389371751 2060 R>M No EVA
rs3389369675 2108 T>S No EVA
rs3389344579 2161 A>V No EVA
rs3389354951 2165 Q>H No EVA
rs3389344581 2245 A>D No EVA
rs3389390726 2270 A>D No EVA
rs232819415 2297 P>A No EVA
rs3389369702 2309 P>A No EVA
rs250482745 2387 S>N No EVA
rs3389369692 2411 I>T No EVA

No associated diseases with B2RWS6

5 regional properties for B2RWS6

Type Name Position InterPro Accession
domain Helicase, C-terminal domain-like 385 - 539 IPR001650
domain DEAD/DEAH box helicase domain 170 - 349 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 165 - 376 IPR014001
domain RNA helicase, DEAD-box type, Q motif 146 - 174 IPR014014
domain Ded1/Dbp1, DEAD-box helicase domain 147 - 367 IPR044763

Functions

Description
EC Number 2.3.1.48 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • In the presence of ALX1 relocalizes from the cytoplasm to the nucleus
  • Colocalizes with ROCK2 in the nucleus
  • Localizes to sites of DNA damage
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
histone acetyltransferase complex A protein complex that possesses histone acetyltransferase activity.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A 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.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
protein-DNA complex A macromolecular complex containing both protein and DNA molecules.
transcription regulator complex A protein complex that is capable of associating with DNA by direct binding, or via other DNA-binding proteins or complexes, and regulating transcription.

43 GO annotations of molecular function

Name Definition
acetylation-dependent protein binding Binding to a protein upon acetylation of the target protein.
acetyltransferase activity Catalysis of the transfer of an acetyl group to an acceptor molecule.
antigen binding Binding to an antigen, any substance which is capable of inducing a specific immune response and of reacting with the products of that response, the specific antibody or specifically sensitized T-lymphocytes, or both. Binding may counteract the biological activity of the antigen.
beta-catenin binding Binding to a catenin beta subunit.
bHLH transcription factor binding Binding to a basic Helix-Loop-Helix (bHLH) superfamily of transcription factors, important regulatory components in transcriptional networks of many developmental pathways.
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
chromatin DNA binding Binding to DNA that is assembled into chromatin.
cis-regulatory region sequence-specific DNA binding Binding to a specific upstream regulatory DNA sequence (transcription factor recognition sequence or binding site) located in cis relative to the transcription start site (i.e., on the same strand of DNA) of a gene transcribed by some RNA polymerase. The proximal promoter is in cis with and relatively close to the core promoter.
damaged DNA binding Binding to damaged DNA.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-binding transcription factor binding 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.
histone acetyltransferase activity Catalysis of the reaction
histone butyryltransferase activity Catalysis of the reaction
histone crotonyltransferase activity Catalysis of the reaction
histone H2B acetyltransferase activity Catalysis of the reaction
histone H3K122 acetyltransferase activity Catalysis of the reaction
histone H3K18 acetyltransferase activity Catalysis of the reaction
histone H3K27 acetyltransferase activity Catalysis of the reaction
histone H4 acetyltransferase activity Catalysis of the reaction
histone lactyltransferase activity Catalysis of the reaction
lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Catalysis of the reaction
mitogen-activated protein kinase binding Binding to a mitogen-activated protein kinase.
NF-kappaB binding Binding to NF-kappaB, a transcription factor for eukaryotic RNA polymerase II promoters.
nuclear androgen receptor binding Binding to a nuclear androgen receptor.
nuclear glucocorticoid receptor binding Binding to a nuclear glucocorticoid receptor.
p53 binding Binding to one of the p53 family of proteins.
peptide 2-hydroxyisobutyryltransferase activity Catalysis of the reaction
peptide-lysine-N-acetyltransferase activity Catalysis of the reaction
peroxisome proliferator activated receptor binding Binding to a peroxisome proliferator activated receptor, alpha, beta or gamma.
pre-mRNA intronic binding Binding to an intronic sequence of a pre-messenger RNA (pre-mRNA).
promoter-specific chromatin binding Binding to a section of chromatin that is associated with gene promoter sequences of DNA.
protein antigen binding Binding to a protein antigen.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
protein propionyltransferase activity Catalysis of the reaction
protein-containing complex binding Binding to a macromolecular complex.
RNA polymerase II cis-regulatory region sequence-specific DNA binding Binding to a specific upstream regulatory DNA sequence (transcription factor recognition sequence or binding site) located in cis relative to the transcription start site (i.e., on the same strand of DNA) of a gene transcribed by RNA polymerase II.
RNA polymerase II-specific DNA-binding transcription factor binding 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.
SMAD binding Binding to a SMAD signaling protein.
STAT family protein binding Binding to a member of the signal transducers and activators of transcription (STAT) protein family. STATs are, as the name indicates, both signal transducers and transcription factors. STATs are activated by cytokines and some growth factors and thus control important biological processes including cell growth, cell differentiation, apoptosis and immune responses.
transcription coactivator activity 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.
transcription coactivator binding 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.
transcription coregulator binding Binding to a transcription coregulator, a protein involved in regulation of transcription via protein-protein interactions with transcription factors and other transcription regulatory proteins. Cofactors do not bind DNA directly, but rather mediate protein-protein interactions between regulatory transcription factors and the basal transcription machinery.
zinc ion binding Binding to a zinc ion (Zn).

82 GO annotations of biological process

Name Definition
animal organ morphogenesis Morphogenesis of an animal organ. An organ is defined as a tissue or set of tissues that work together to perform a specific function or functions. Morphogenesis is the process in which anatomical structures are generated and organized. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions.
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
B cell differentiation The process in which a precursor cell type acquires the specialized features of a B cell. A B cell is a lymphocyte of B lineage with the phenotype CD19-positive and capable of B cell mediated immunity.
behavioral defense response A behavioral response seeking to protect an organism from an a perceived external threat to that organism.
canonical NF-kappaB signal transduction The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. 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.
cartilage development The process whose specific outcome is the progression of a cartilage element over time, from its formation to the mature structure. Cartilage elements are skeletal elements that consist of connective tissue dominated by extracellular matrix containing collagen type II and large amounts of proteoglycan, particularly chondroitin sulfate.
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cellular response to interleukin-1 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 interleukin-1 stimulus.
cellular response to leucine 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 leucine stimulus.
cellular response to nutrient levels 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.
cellular response to UV 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.
chromatin remodeling 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.
circadian rhythm Any biological process in an organism that recurs with a regularity of approximately 24 hours.
face morphogenesis The process in which the anatomical structures of the face are generated and organized. The face is the ventral division of the head.
fat cell differentiation The process in which a relatively unspecialized cell acquires specialized features of an adipocyte, an animal connective tissue cell specialized for the synthesis and storage of fat.
heart development The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
internal protein amino acid acetylation The addition of an acetyl group to a non-terminal amino acid in a protein.
intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator The series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage, and ends when the execution phase of apoptosis is triggered.
learning or memory The acquisition and processing of information and/or the storage and retrieval of this information over time.
lung development The process whose specific outcome is the progression of the lung over time, from its formation to the mature structure. In all air-breathing vertebrates the lungs are developed from the ventral wall of the oesophagus as a pouch which divides into two sacs. In amphibians and many reptiles the lungs retain very nearly this primitive sac-like character, but in the higher forms the connection with the esophagus becomes elongated into the windpipe and the inner walls of the sacs become more and more divided, until, in the mammals, the air spaces become minutely divided into tubes ending in small air cells, in the walls of which the blood circulates in a fine network of capillaries. In mammals the lungs are more or less divided into lobes, and each lung occupies a separate cavity in the thorax.
macrophage derived foam cell differentiation The process in which a monocyte acquires the specialized features of a foam cell. A foam cell is a type of cell containing lipids in small vacuoles and typically seen in atherosclerotic lesions, as well as other conditions.
megakaryocyte development The process whose specific outcome is the progression of a megakaryocyte cell over time, from its formation to the mature structure. Megakaryocyte development does not include the steps involved in committing a cell to a megakaryocyte fate. A megakaryocyte is a giant cell 50 to 100 micron in diameter, with a greatly lobulated nucleus, found in the bone marrow.
multicellular organism growth The increase in size or mass of an entire multicellular organism, as opposed to cell growth.
N-terminal peptidyl-lysine acetylation The acetylation of the N-terminal lysine of proteins.
negative regulation of autophagy Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
negative regulation of gluconeogenesis Any process that stops, prevents, or reduces the frequency, rate or extent of gluconeogenesis.
negative regulation of miRNA metabolic process Any process that stops, prevents or reduces the frequency, rate or extent of miRNA metabolic process.
negative regulation of protein-containing complex assembly Any process that stops, prevents, or reduces the frequency, rate or extent of protein complex assembly.
negative regulation of transcription by RNA polymerase II Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
peptidyl-lysine butyrylation The butyrylation of a lysine residue in a protein. Butyryl is the univalent radical C3H7COO- derived from butyric acid.
peptidyl-lysine crotonylation The crotonylation of a lysine residue in a protein. Crotonyl is the univalent radical CH3-CH=CH-CO- derived from crotonic acid.
peptidyl-lysine propionylation The propionylation of peptidyl-lysine.
platelet formation The process in which platelets bud from long processes extended by megakaryocytes.
positive regulation by host of viral transcription Any process in which a host organism activates or increases the frequency, rate or extent of viral transcription, the synthesis of either RNA on a template of DNA or DNA on a template of RNA.
positive regulation of axon extension Any process that activates or increases the frequency, rate or extent of axon extension.
positive regulation of cell growth Any process that activates or increases the frequency, rate, extent or direction of cell growth.
positive regulation of cell growth involved in cardiac muscle cell development Any process that increases the rate, frequency, or extent of the growth of a cardiac muscle cell, where growth contributes to the progression of the cell over time from its initial formation to its mature state.
positive regulation of cell size Any process that increases cell size.
positive regulation of cellular response to hypoxia Any process that activates or increases the frequency, rate or extent of cellular response to hypoxia.
positive regulation of collagen biosynthetic process Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of collagen, any of a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals.
positive regulation of DNA-binding transcription factor activity Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription.
positive regulation of DNA-templated transcription Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
positive regulation of gene expression Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).
positive regulation of glycoprotein biosynthetic process Any process that increases the rate, frequency, or extent of the chemical reactions and pathways resulting in the formation of a glycoprotein, a protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
positive regulation of hydrogen peroxide-mediated programmed cell death Any process that activates or increases the frequency, rate or extent of hydrogen peroxide-mediated programmed cell death.
positive regulation of muscle atrophy Any process that activates or increases the frequency, rate or extent of muscle atrophy.
positive regulation of neuron projection development Any process that increases the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
positive regulation of protein acetylation Any process that activates or increases the frequency, rate or extent of protein acetylation.
positive regulation of protein import into nucleus Any process that activates or increases the frequency, rate or extent of movement of proteins from the cytoplasm into the nucleus.
positive regulation of protein phosphorylation Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.
positive regulation of protein secretion Any process that activates or increases the frequency, rate or extent of the controlled release of a protein from a cell.
positive regulation of proteolysis Any process that activates or increases the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
positive regulation of receptor signaling pathway via JAK-STAT Any process that activates or increases the frequency, rate or extent of the JAK-STAT signaling pathway activity.
positive regulation of sarcomere organization Any process that increases the rate, frequency or extent of myofibril assembly by organization of muscle actomyosin into sarcomeres. The sarcomere is the repeating unit of a myofibril in a muscle cell, composed of an array of overlapping thick and thin filaments between two adjacent Z discs.
positive regulation of T-helper 17 cell lineage commitment Any process that activates or increases the frequency, rate or extent of T-helper 17 cell lineage commitment.
positive regulation of TORC1 signaling Any process that activates or increases the frequency, rate or extent of TORC1 signaling.
positive regulation of transcription by RNA polymerase II Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
positive regulation of transforming growth factor beta receptor signaling pathway Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
positive regulation of translation Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
protein acetylation The addition of an acetyl group to a protein amino acid. An acetyl group is CH3CO-, derived from acetic acid.
protein destabilization Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.
protein modification process The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
protein stabilization Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
protein-DNA complex assembly The aggregation, arrangement and bonding together of proteins and DNA molecules to form a protein-DNA complex.
regulation of androgen receptor signaling pathway Any process that modulates the rate, frequency, or extent of the androgen receptor signaling pathway.
regulation of angiotensin metabolic process Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving angiotensin.
regulation of glycolytic process Any process that modulates the frequency, rate or extent of glycolysis.
regulation of mitochondrion organization Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a mitochondrion.
regulation of transcription by RNA polymerase II Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.
regulation of tubulin deacetylation Any process that modulates the frequency, rate or extent of tubulin deacetylation. Tubulin deacetylation is the removal of an acetyl group from a protein amino acid.
response to calcium ion 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 calcium ion stimulus.
response to dexamethasone 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 dexamethasone stimulus.
response to estrogen 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 stimulus by an estrogen, C18 steroid hormones that can stimulate the development of female sexual characteristics.
response to glucose 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 glucose stimulus.
response to hypoxia 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.
response to xenobiotic stimulus 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 from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
skeletal muscle tissue development The developmental sequence of events leading to the formation of adult skeletal muscle tissue. The main events are
somitogenesis The formation of mesodermal clusters that are arranged segmentally along the anterior posterior axis of an embryo.
swimming Self-propelled movement of an organism from one location to another through water, often by means of active fin movement.
thigmotaxis The directed movement of an animal in response to touch.
transcription by RNA polymerase II The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs).
transcription initiation-coupled chromatin remodeling An epigenetic mechanism of regulation of gene expression that involves chromatin remodeling to capacitate gene expression by either modifying the chromatin fiber, the nucleosomal histones, or the DNA.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q92793 CREBBP CREB-binding protein Homo sapiens (Human) SS
Q09472 EP300 Histone acetyltransferase p300 Homo sapiens (Human) EV
P45481 Crebbp Histone lysine acetyltransferase CREBBP Mus musculus (Mouse) SS
Q6JHU9 Crebbp Histone lysine acetyltransferase CREBBP Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD
70 80 90 100 110 120
ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQAMASQAQQ NSPGLSLINS
130 140 150 160 170 180
MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA
190 200 210 220 230 240
AGNGQGIMPN QVMNGSIGAG RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP
250 260 270 280 290 300
QPLKMGMMNN PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM
310 320 330 340 350 360
PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH KCQRREQANG
370 380 390 400 410 420
EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKN
430 440 450 460 470 480
AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ
490 500 510 520 530 540
IPPQPQVQAK NQQSQPSGQS PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS
550 560 570 580 590 600
QNPMMSENAG VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA
610 620 630 640 650 660
LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR TRLQKQNMLP
670 680 690 700 710 720
NAPGMGPVPM NTGSNMGQQP TGMTTNGPVP DPSMIRGSVP NHMMPRMTPQ PGLNQFGQMN
730 740 750 760 770 780
MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN
790 800 810 820 830 840
MPLAPSSGQA PVSQAQMSSS SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP
850 860 870 880 890 900
TPHHTPPSIG NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL
910 920 930 940 950 960
PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV SNPPSTSSTE
970 980 990 1000 1010 1020
VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK GEDVKVEPTE MEERGPELKT
1030 1040 1050 1060 1070 1080
DGKEEEEQPS TSATQSSPAP GQSKKKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP
1090 1100 1110 1120 1130 1140
QLLGIPDYFD IVKSPMDLST IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY
1150 1160 1170 1180 1190 1200
CSKLSEVFEQ EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC
1210 1220 1230 1240 1250 1260
EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG RKMHQICVLH
1270 1280 1290 1300 1310 1320
HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF LENRVNDFLR RQNHPESGEV
1330 1340 1350 1360 1370 1380
TVRVVHASDK TVEVKPGMKA RFVDSGEMAE SFPYRTKALF AFEEIDGVDL CFFGMHVQEY
1390 1400 1410 1420 1430 1440
GSDCPPPNQR RVYISYLDSV HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS
1450 1460 1470 1480 1490 1500
EGDDYIFHCH PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL
1510 1520 1530 1540 1550 1560
PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK NNKKTSKNKS
1570 1580 1590 1600 1610 1620
SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI ACPAPNSLPP IVDPDPLIPC
1630 1640 1650 1660 1670 1680
DLMDGRDAFL TLARDKHLEF SSLRRAQWST MCMLVELHTQ SQDRFVYTCN ECKHHVETRW
1690 1700 1710 1720 1730 1740
HCTVCEDYDL CITCYNTKNH DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS
1750 1760 1770 1780 1790 1800
LVHACQCRNA NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC
1810 1820 1830 1840 1850 1860
PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT PATPTTPTGQ
1870 1880 1890 1900 1910 1920
QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG KAPGQVTPPT PPQTAQAPLP
1930 1940 1950 1960 1970 1980
GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ RPIQHQMPQM SPMAPMGMNP PPMARGPGGH
1990 2000 2010 2020 2030 2040
LDPGIGPAGM QQQPPWAQGG MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS
2050 2060 2070 2080 2090 2100
PLKPGTVSQQ ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP
2110 2120 2130 2140 2150 2160
LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ PQQQLQPPMG
2170 2180 2190 2200 2210 2220
AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP GMANQFQQPQ GIGYPPQQQQ
2230 2240 2250 2260 2270 2280
QQRMQHHMQQ MQQGNMGQMG QLPQALGAEA GASLQAYQQR LLQQQMGSPA QPNPMSPQQH
2290 2300 2310 2320 2330 2340
MLPNQAQSPH LQGQQIPNSL SNQVRSPQPV PSPRPQSQPP HSSPSPRMQP QPSPHHVSPQ
2350 2360 2370 2380 2390 2400
TSSPHPGLVA AQAANPMEQG HFASPDQNSM LSQLASNPGM ANLHGASATD LGLSSDNADL
2410
NSNLSQSTLD IH