NCOA3
entrez
8202
canonical
uniprot
Q9Y6Q9
canonical
ensembl
ENSG00000124151
resolver
ensp
ENSP00000361065
resolver
ensp
ENSP00000361066
resolver
ensp
ENSP00000361073
resolver
ensp
ENSP00000558952
resolver
genesymbol
NCOA3
resolver
genesymbol_syn
AIB1
resolver
genesymbol_syn
BHLHE42
resolver
genesymbol_syn
RAC3
resolver
genesymbol_syn
TRAM1
resolver
hgnc
HGNC:7670
resolver
uniprot
A4LAZ5
resolver
uniprot
Q0VF45
resolver
uniprot
Q59EE8
resolver
uniprot
Q5JYD9
resolver
uniprot
Q5JYE0
resolver
uniprot
Q9BR49
resolver
uniprot
Q9UPC9
resolver
uniprot
Q9UPG4
resolver
uniprot
Q9UPG7
resolver
uniprot_entry
NCOA3_HUMAN
resolver
uniprot_entry
Q59EE8_HUMAN
resolver
uniprot_sec
A4LAZ5
resolver
uniprot_sec
Q0VF45
resolver
uniprot_sec
Q5JYD9
resolver
uniprot_sec
Q5JYE0
resolver
uniprot_sec
Q9BR49
resolver
uniprot_sec
Q9UPC9
resolver
uniprot_sec
Q9UPG4
resolver
uniprot_sec
Q9UPG7
resolver
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.
uniprot
proteins
amino_acid_sequence
MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNGVSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGEDLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLADPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNIMISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKESSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVSSSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGNVVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQEKDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLKSSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGSSMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPTLPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQVSHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMNQMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTAGGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQPDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQFAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC
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, which probably acts 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.
uniprot
proteins
mass_dalton
155293
uniprot
proteins
mutagenesis
MUTAGEN 616; /note="K->Q: Strongly reduces acetylation by CREBBP."; /evidence="ECO:0000269|PubMed:10490106"; MUTAGEN 619..620; /note="KK->QQ: Abolishes acetylation by CREBBP."; /evidence="ECO:0000269|PubMed:10490106"; MUTAGEN 647; /note="K->Q: Does not affect acetylation by CREBBP."; /evidence="ECO:0000269|PubMed:10490106"; MUTAGEN 681; /note="K->Q: Does not affect acetylation by CREBBP."; /evidence="ECO:0000269|PubMed:10490106"; MUTAGEN 687; /note="K->Q: Does not affect acetylation by CREBBP."; /evidence="ECO:0000269|PubMed:10490106"; MUTAGEN 700; /note="K->Q: Does not affect acetylation by CREBBP."; /evidence="ECO:0000269|PubMed:10490106"; MUTAGEN 708; /note="K->Q: Does not affect acetylation by CREBBP."; /evidence="ECO:0000269|PubMed:10490106
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. {ECO:0000269|PubMed:10490106}.; PTM: Methylated by CARM1. {ECO:0000250}.; PTM: Phosphorylated by IKK complex. {ECO:0000269|PubMed:11971985}.
uniprot
proteins
protein_family
SRC/p160 nuclear receptor coactivator family
uniprot
proteins
pubmed
10490106
uniprot
proteins
pubmed
11094166
uniprot
proteins
pubmed
11250900
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
11971985
uniprot
proteins
pubmed
12917342
uniprot
proteins
pubmed
14645221
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15698540
uniprot
proteins
pubmed
16951154
uniprot
proteins
pubmed
16957778
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17998543
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18690216
uniprot
proteins
pubmed
19339517
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25452582
uniprot
proteins
pubmed
34718754
uniprot
proteins
pubmed
9238002
uniprot
proteins
pubmed
9252329
uniprot
proteins
pubmed
9267036
uniprot
proteins
pubmed
9346901
uniprot
proteins
pubmed
9727751
uniprot
proteins
sequence_length
1424
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus.
uniprot
proteins