O09000
uniprot
O09000
canonical
activity_regulation
ACTIVITY REGULATION: Coactivator activity on nuclear receptors and NF-kappa-B pathways is enhanced by various hormones, and the TNF cytokine, respectively. TNF stimulation probably enhances phosphorylation, which in turn activates coactivator function. In contrast, acetylation by CREBBP apparently suppresses coactivation of target genes by disrupting its association with nuclear receptors (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MSGLGESSLDPLAAESRKRKLPCDAPGQGLVYSGEKWRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISSDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYSILHEPRRKDFLNTYQNPQLMEFLGLMRTRDKKAPYILIVRMLMKTHDILEDVNASPETRQRYETMQCFALSQPRAMLEEGEDLQCCMICVARRVTAPFPSSPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYVHGHAETPVYRFSLADGTIVSAQTKSKLFRNPVTNDRHGFISTHFLQREQNGYRPNPIPQDKGIRPPAAGCGVSMSPNQNVQMMGSRTYGVPDPSNTGQMGGARYGASSSVASLTPGQSLQSPSSYQNSSYGLSMSSPPHGSPGLGPNQQNIMISPRNRGSPKMASHQFSPAAGAHSPMGPSGNTGSHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNISQPSKVSGQDSKSPLGLYCEQNPVESSVCQSNSRDPQVKKESKESSGEVSETPRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDPNCKDSSVSVTSPSGVSSSTSGTVSSTSNVHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSTASCGEGTTRQEQLSPKKKENNALLRYLLDRDDPSDVLAKELQPQADSGDSKLSQCSCSTNPSSGQEKDPKIKTETNDEVSGDLDNLDAILGDLTSSDFYNNPTNGGHPGAKQQMFAGPSSLGLRSPQPVQSVRPPYNRAVSLDSPVSVGSGPPVKNVSAFPGLPKQPILAGNPRMMDSQENYGANMGPNRNVPVNPTSSPGDWGLANSRASRMEPLASSPLGRTGADYSATLPRPAMGGSVPTLPLRSNRLPGARPSLQQQQQQQQQQQQQQQQQQQQQQQMLQMRTGEIPMGMGVNPYSPAVQSNQPGSWPEGMLSMEQGPHGSQNRPLLRNSLDDLLGPPSNAEGQSDERALLDQLHTFLSNTDATGLEEIDRALGIPELVNQGQALESKQDVFQGQEAAVMMDQKAALYGQTYPAQGPPLQGGFNLQGQSPSFNSMMGQISQQGSFPLQGMHPRAGLVRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALEMKMENPAGTAVMRPMMPQAFFNAQMAAQQKRELMSHHLQQQRMAMMMSQPQPQAFSPPPNVTASPSMDGVLAGSAMPQAPPQQFPYPANYGMGQPPEPAFGRGSSPPSAMMSSRMGPSQNAMVQHPQPTPMYQPSDMKGWPSGNLARNGSFPQQQFAPQGNPAAYNMVHMNSSGGHLGQMAMTPMPMSGMPMGPDQKYC
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit (By similarity). {ECO:0000250, ECO:0000269|PubMed:10823921}.
uniprot
proteins
mass_dalton
151574
uniprot
proteins
post_translational_modification
PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function (By similarity). {ECO:0000250}.; PTM: Methylated by CARM1. {ECO:0000269|PubMed:11701890}.; PTM: Phosphorylated by IKK complex (By similarity). {ECO:0000250|UniProtKB:Q9Y6Q9}.
uniprot
proteins
protein_family
SRC/p160 nuclear receptor coactivator family
uniprot
proteins
pubmed
10381882
uniprot
proteins
pubmed
10823921
uniprot
proteins
pubmed
11701890
uniprot
proteins
pubmed
12709428
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23019124
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
9192892
uniprot
proteins
sequence_length
1398
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus (By similarity). {ECO:0000250}.
uniprot
proteins