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IID00110
 UniprotQ9Y6Q9
ProteinNuclear receptor coactivator 3
GeneNCOA3
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1424
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 618-629 Hetero dimer : IID00020Complex
 Evidence X-RAY 3l3x B Reference
       Region 3l3x B 618-629 order
Seq 735-746 Hetero dimer : IID00020Complex
 Evidence X-RAY 3l3z B Reference
       Region 3l3z B 735-746 order
Seqdisorder 1018-1088
 Evidence NMR Reference
       Region 1018-1088 disorder
Seq 1045-1091 Hetero dimer : IID50008Complex
 Evidence NMR 1kbh A Reference
       Region 1kbh A 1045-1091 order
SeqProS possible 618-629 LXXLL motif Hetero dimer : IID00020Complex
       Region 3l3x B 618-629 order
SeqProS possible 735-746 LXXLL motif Hetero dimer : IID00020Complex
       Region 3l3z B 735-746 order
SeqProS verified 1045-1091 Hetero dimer : IID50008Complex
       Region 1kbh A 1045-1091 order
       Region 1018-1088 disorder
Seqphosphorylation
    860-860 Phosphoserine
    728-728 Phosphoserine
    214-214 Phosphoserine
    551-551 Phosphoserine
    569-569 Phosphoserine
    601-601 Phosphoserine; by CK1
    694-694 Phosphoserine
    857-857 Phosphoserine
    867-867 Phosphoserine
    1033-1033 Phosphoserine
    1330-1330 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
    616-616 N6-acetyllysine; by CREBBP
    619-619 N6-acetyllysine; by CREBBP
    620-620 N6-acetyllysine; by CREBBP
    687-687 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-42,78-102,178-217,373-1239,1280-1424
Order 43-58,64-77,103-177,218-256,264-372,1240-1279
ProS 1-10,28-42,78-85,91-97,178-186,192-204,473-477,498-503,679-704,732-746,751-759,797-808,869-873,1009-1013,1033-1038,1048-1059,1068-1080,1220-1224,1417-1424
AlphaFold
Disorder 1-32,54-66,85-108,174-191,204-218,231-244,254-264,288-290,307-311,372-1049,1077-1077,1079-1171,1173-1224,1269-1424
Order 33-53,67-84,109-173,192-203,219-230,245-253,265-287,291-306,312-371,1050-1076,1078-1078,1172-1172,1225-1268
Pfam Hmmer
PF07469 1291-1348 2.5e-30
SEG 509-530 ,535-543 ,649-671 ,767-779 ,856-870 ,975-984 ,1131-1149 ,1169-1186 ,1248-1276 ,1302-1313 ,1400-1419
Function
Function in SwissProt
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.
Biological Process
Diagram with PDB data
NCOA3/CREBBPStructure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins
NCOA3/ARCrystal structure of DHT-bound androgen receptor in complex with the first motif of steroid receptor coactivator 3
See also
Diagram with PDB data
Crebbp/NCOA3Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR
CREBBP/NCOA3Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins