Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Gene Ontology annotation of human sequence-specific DNA binding transcription factors (DbTFs) based on the TFClass database
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Molecular determinants of the estrogen receptor-coactivator interface.
The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding.
Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains.
Cross-repression, a functional consequence of the physical interaction of non-liganded nuclear receptors and POU domain transcription factors.
Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha.
A novel mutation in helix 12 of the vitamin D receptor impairs coactivator interaction and causes hereditary 1,25-dihydroxyvitamin D-resistant rickets without alopecia.
2.1 A crystal structure of human PXR in complex with the St. John's wort compound hyperforin.
Coactivator binding promotes the specific interaction between ligand and the pregnane X receptor.
BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation.
The farnesoid X receptor controls gene expression in a ligand- and promoter-selective fashion.
In vitro farnesoid X receptor ligand sensor assay using surface plasmon resonance and based on ligand-induced coactivator association.
The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors.
Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions.
Activation of ATP-binding cassette transporter A1 transcription by chromatin remodeling complex.
Functional genomics identifies a mechanism for estrogen activation of the retinoic acid receptor alpha1 gene in breast cancer cells.
Synovial sarcoma translocation (SYT) encodes a nuclear receptor coactivator.
T:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif.
A novel partial agonist of peroxisome proliferator-activated receptor-gamma (PPARgamma) recruits PPARgamma-coactivator-1alpha, prevents triglyceride accumulation, and potentiates insulin signaling in vitro.
P38MAPK-dependent phosphorylation and degradation of SRC-3/AIB1 and RARalpha-mediated transcription.
Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor.
The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription.
The vitamin D receptor interacts preferentially with DRIP205-like LxxLL motifs.
The core component of the mammalian SWI/SNF complex SMARCD3/BAF60c is a coactivator for the nuclear retinoic acid receptor.
SIP, a novel ankyrin repeat containing protein, sequesters steroid receptor coactivators in the cytoplasm.
PKA-induced resistance to tamoxifen is associated with an altered orientation of ERalpha towards co-activator SRC-1.
MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid receptor activation.
Structural and functional characterization of a novel type of ligand-independent RXR-USP receptor.
Identification of a potent synthetic FXR agonist with an unexpected mode of binding and activation.
ERAP75 functions as a coactivator to enhance estrogen receptor alpha transactivation in prostate stromal cells.
Identification of COUP-TFII orphan nuclear receptor as a retinoic acid-activated receptor.
GAS, a new glutamate-rich protein, interacts differentially with SRCs and is involved in oestrogen receptor function.
The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors.
Structural basis for hydroxycholesterols as natural ligands of orphan nuclear receptor RORgamma.
A unique secondary-structure switch controls constitutive gene repression by retinoic acid receptor.
Molecular determinants of the interactions between SRC-1 and LXR/RXR heterodimers.
Repression of androgen receptor activity by HEYL, a third member of the Hairy/Enhancer-of-split-related family of Notch effectors.
Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings.
Structural and functional analysis of the human nuclear xenobiotic receptor PXR in complex with RXRα.
Identification and characterization of a ligand-selective mineralocorticoid receptor coactivator.
Modification of ASC1 by UFM1 is crucial for ERα transactivation and breast cancer development.
Tumor suppressor Menin acts as a corepressor of LXRα to inhibit hepatic lipogenesis.
A reference map of the human binary protein interactome.
Sequence and characterization of a coactivator for the steroid hormone receptor superfamily.
A splicing variant of Steroid Receptor Coactivator-1 (SRC-1E): the major isoform of SRC-1 to mediate thyroid hormone action.
Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations.
Recycling of bile acids and salts
Fatty acid ligands activate PPARA
SUMOylation of NCOA1 with SUMO1
NR1H4:DCA,CDCA,LCHA binds RXRA and NCOA1,2
NCOA1(868-1441) binds PAX3(1-319)
NCOA1 binds ESR1:estrogen:TGFA gene
Histone acetyltransferases are recruited to the TFF1 gene
NCOA1 recruits EP300 to TGFA promoter
NCOA1 binds the ABCA1gene:NR1H2,3:RXR:NR1H2,3 ligands complex
NCOA1 recruits EP300 to the ABCA1 promoter
NCOA1 binds the UGT1A3 gene:NR1H2,3:RXR:NR1H2,3 ligand complex
The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1.
Nuclear Receptor Coactivators (NCOAs) and Corepressors (NCORs) in the Brain.
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Nuclear coregulators have broad, context-dependent physiological roles, much of whose causal experimental evidence comes from animal models.
"Studies using genetic animal models started to reveal pivotal roles of NCOAs/NCORs in the brain"
Steroid receptor coactivator-1 is a histone acetyltransferase.