Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
2004
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Region 2ln0 A 204-313 order
Region 4ljn A 194-269 order
Region 4ljn A 270-273 disorder
Region 4ljn A 274-316 order
Region 4ljn A 317-323 disorder
Seq 194-323 Hetero dimer : IID00062 Complex
Region 3v43 A 204-313 order
Region 4llb B 194-312 order
Region 4llb B 313-323 disorder
Region 4llb A 194-312 order
Region 4llb A 313-323 disorder
Region 4lka A 194-315 order
Region 4lka A 316-323 disorder
Region 4lk9 A 194-315 order
Region 4lk9 A 316-323 disorder
Seq 194-323 Hetero dimer : K7EMV3
Region 5b78 A 194-311 order
Region 5b78 A 312-323 disorder
Region 5b77 A 194-196 disorder
Region 5b77 A 197-312 order
Region 5b77 A 313-323 disorder
Region 5b76 A 194-312 order
Region 5b76 A 313-323 disorder
Region 5b75 A 194-312 order
Region 5b75 A 313-323 disorder
Region 2rc4 A 501-506 disorder
Region 2rc4 A 507-738 order
Region 2rc4 A 739-747 disorder
Region 2rc4 A 748-779 order
Region 2rc4 A 780-784 disorder
Region 2ozu A 497-506 disorder
Region 2ozu A 507-706 order
Region 2ozu A 707-711 disorder
Region 2ozu A 712-737 order
Region 2ozu A 738-746 disorder
Region 2ozu A 747-762 order
Region 2ozu A 763-764 disorder
Region 2ozu A 765-776 order
Region 2ozu A 777-780 disorder
Region 1m36 A 533-563 order
369-369 Phosphothreonine; by PKB/AKT1
604-604 N6-acetyllysine; by autocatalysis
1007-1007 N6-acetyllysine
Prediction
Disorder 1-2,80-91,173-206,314-502,785-2004
Order 3-79,92-172,207-313,503-784
ProS 1-2,314-417,427-439,449-490,495-499,785-788,968-977,1027-1033,1113-1116,1149-1154,1349-1353,1908-1928,1936-1945,1950-1953,1963-1968,1979-1990,1996-2004
Disorder 1-3,76-96,134-134,136-141,171-191,199-199,272-273,312-320,323-324,327-327,330-482,492-492,495-506,709-709,780-2004
Order 4-75,97-133,135-135,142-170,192-198,200-271,274-311,321-322,325-326,328-329,483-491,493-494,507-708,710-779
SEG 181-195
,371-379
,788-810
,985-1003
,1011-1029
,1031-1044
,1061-1083
,1098-1118
,1147-1160
,1221-1310
,1312-1321
,1367-1376
,1403-1415
,1481-1503
,1534-1548
,1574-1602
,1607-1623
,1647-1701
,1803-1814
,1951-1959
Function
Function in SwissProt
Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML.