Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
2441
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Seq 340-439 Hetero dimer : IID00053 Complex
Region 2ka4 A 340-439 order
Region 2ka4 A 340-341 high_rmsd
Region 2ka4 A 377-377 high_rmsd
Region 2ka4 A 438-439 high_rmsd
Region 1u2n A 340-439 order
Region 1u2n A 340-344 high_rmsd
Region 1u2n A 376-376 high_rmsd
Region 1u2n A 437-439 high_rmsd
Seq 340-439 Hetero dimer : IID00179 Complex
Region 1r8u B 340-439 order
Region 1r8u B 340-343 high_rmsd
Region 1r8u B 374-377 high_rmsd
Seq 340-439 Hetero dimer : Q04207
Region 2lww A 340-439 order
Region 2lww A 340-344 high_rmsd
Region 2lww A 438-439 high_rmsd
Seq 340-439 Monomer : IID00015 Complex
Region 5hou A 340-439 order
Region 5hou A 340-343 high_rmsd
Seq 345-439 Hetero dimer : IID00085 Complex
Region 1l8c A 345-439 order
Region 1l8c A 375-377 high_rmsd
Region 1l8c A 436-439 high_rmsd
Seq 586-666 Hetero dimer : IID50004 Complex
Region 1kdx A 586-666 order
Region 1kdx A 586-586 high_rmsd
Region 1kdx A 666-666 high_rmsd
Seq 586-672 Hetero dimer : P06876
Region 1sb0 A 586-672 order
Seq 586-672 Hetero trimer : IID00379 Complex ,
P06876
Region 2agh B 586-672 order
Region 2agh B 586-588 high_rmsd
Region 2agh B 671-672 high_rmsd
Seq 586-672 Hetero dimer : IID00433 Complex
Region 2lqi A 586-672 order
Region 2lqi A 586-586 high_rmsd
Region 2lqh A 586-672 order
Region 2lqh A 586-586 high_rmsd
Seq 586-672 Hetero dimer : IID00207 Complex
Region 5u4k A 586-672 order
Region 5u4k A 586-586 high_rmsd
Region 5u4k A 671-672 high_rmsd
Region 4i9o A 586-587 disorder
Region 4i9o A 588-665 order
Region 4i9o A 666-672 disorder
Region 5u7g B 1079-1210 order
Region 5u7g B 1211-1272 disorder
Region 5u7g B 1273-1556 order
Region 5u7g A 1079-1210 order
Region 5u7g A 1211-1272 disorder
Region 5u7g A 1273-1556 order
Region 5w0i A 1083-1084 disorder
Region 5w0i A 1085-1198 order
Region 1tot A 1700-1751 order
Region 1f81 A 1764-1850 order
Seq 1764-1855 Hetero dimer : IID00046 Complex
Region 2ka6 A 1764-1855 order
Region 2ka6 A 1855-1855 high_rmsd
Seq 1764-1855 Monomer : IID00015 Complex
Region 5hpd A 1764-1855 order
Seq 1764-1857 Monomer : IID00015 Complex
Region 5hp0 A 1764-1857 order
Region 5hp0 A 1857-1857 high_rmsd
Region 2057-2117 disorder
Region 2kkj A 2059-2117 order
Region 2kkj A 2059-2061 high_rmsd
Region 2kkj A 2107-2117 high_rmsd
Region 1jjs A 2067-2082 order
Region 1jjs A 2082-2082 high_rmsd
Region 1jjs A 2083-2086 disorder
Region 1jjs A 2087-2112 order
Seq 2059-2117 Hetero dimer : IID00015 Complex
Region 2l14 A 2059-2117 order
Region 2l14 A 2059-2061 high_rmsd
Region 2l14 A 2111-2117 high_rmsd
Seq 2059-2117 Hetero dimer : IID00110 Complex
Region 1kbh B 2059-2117 order
Region 1kbh B 2115-2117 high_rmsd
Seq 2059-2117 Hetero dimer : IID00083 Complex
Region 2c52 A 2059-2116 order
Region 2c52 A 2059-2060 high_rmsd
Region 2c52 A 2116-2116 high_rmsd
Region 2c52 A 2117-2117 disorder
Seq ProS verified 2059-2116 Hetero dimer : IID00083 Complex
Region 2c52 A 2059-2116 order
Region 2057-2117 disorder
Seq ProS verified 2059-2117 Hetero dimer : IID00110 Complex
Region 1kbh B 2059-2117 order
Region 2057-2117 disorder
Seq ProS verified 2059-2117 Hetero dimer : IID00015 Complex
Region 2l14 A 2059-2117 order
Region 2057-2117 disorder
1387-1387 Phosphoserine; by IKKA
1383-1383 Phosphoserine; by IKKA
1742-1742 N6-acetyllysine
1745-1745 N6-acetyllysine
1598-1598 N6-acetyllysine
1596-1596 N6-acetyllysine
1593-1593 N6-acetyllysine
1584-1584 N6-acetyllysine
1592-1592 N6-acetyllysine
1217-1217 N6-acetyllysine
1015-1015 N6-acetyllysine
Prediction
Disorder 1-349,438-1083,1560-1611,1745-1767,1857-2190,2219-2441
Order 350-437,1084-1318,1324-1559,1612-1744,1768-1856,2191-2218
ProS 1-50,345-349,551-555,589-592,653-659,1574-1611,1745-1750,1857-1869,2067-2074,2086-2098,2431-2441
Disorder 1-348,367-382,424-424,434-588,590-590,610-610,612-624,664-664,668-668,670-1082,1218-1219,1253-1259,1420-1426,1568-1568,1570-1615,1700-1706,1713-1717,1738-1738,1746-1769,1789-1789,1794-1794,1812-1816,1866-1866,1869-2084,2086-2441
Order 349-366,383-423,425-433,589-589,591-609,611-611,625-663,665-667,669-669,1083-1217,1220-1252,1260-1419,1427-1567,1569-1569,1616-1699,1707-1712,1718-1737,1739-1745,1770-1788,1790-1793,1795-1811,1817-1865,1867-1868,2085-2085
PF00439 1091-1181 5.4e-43
PF06001 1182-1242 2.2e-29
PF06010 1317-1554 3.8e-173
PF00569 1702-1743 1.8e-20
PF02135 1765-1844 1.2e-39
SEG 47-58
,75-89
,95-105
,213-233
,261-272
,494-516
,874-893
,909-958
,1045-1065
,1551-1574
,1584-1598
,1847-1877
,1884-1914
,1942-1971
,2018-2039
,2077-2086
,2113-2138
,2147-2161
,2197-2216
,2260-2279
,2286-2304
,2343-2378
Function
Function in SwissProt
Acetylates histones, giving a specific tag for transcriptional activation (By similarity). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10207073, PubMed:11701890, PubMed:16287980, PubMed:15220471). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes (By similarity). Acts as a coactivator of ALX1 (By similarity). Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers (By similarity). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24737000). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region (By similarity). Acetylates DDX21, thereby inhibiting DDX21 helicase activity (By similarity). Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) (By similarity). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity).
Biological Process
Diagram with PDB data
Crebbp/NCOA3 Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR
Crebbp/TP53 Structure of CBP nuclear coactivator binding domain in complex with p53 TAD
See also
Diagram with PDB data
TP53/EP300 Structural Basis for the Regulation of p53 Function by p300
TP53/CREBBP NMR Structure of CBP Bromodomain in complex with p53 peptide
TP53/SETD7 Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH
TP53/SMYD2 Structure of SMYD2 in complex with p53 and SAH
Creb1/Crebbp KIX DOMAIN OF MOUSE CBP (CREB BINDING
PROTEIN) IN COMPLEX WITH PHOSPHORYLATED KINASE INDUCIBLE DOMAIN (PKID)
OF RAT CREB (CYCLIC AMP RESPONSE ELEMENT BINDING PROTEIN), NMR 17
STRUCTURES
STAT1/CREBBP NMR structure of the CBP-TAZ2/STAT1-TAD complex
STAT2/Crebbp NMR structure of the CBP-TAZ1/STAT2-TAD complex
HIF1A/EP300 NMR Structures of the HIF-1alpha CTAD/p300 CH1 Complex
CITED2/EP300 Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2
NCOA3/CREBBP Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins