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IID00402
UniprotQ9UPS6
ProteinHistone-lysine N-methyltransferase SETD1B
GeneSETD1B
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1966
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1741-1755 Hetero dimer : IID00377Complex
 Evidence X-RAY 3uvo B Reference
       Region 3uvo B 1745-1745 disorder
       Region 3uvo B 1746-1754 order
       Region 3uvo B 1755-1755 disorder
 Evidence X-RAY 4es0 C Reference
       Region 4es0 C 1741-1744 disorder
       Region 4es0 C 1745-1751 order
       Region 4es0 C 1752-1754 disorder
Seqphosphorylation
    1031-1031 Phosphoserine
    986-986 Phosphoserine
    994-994 Phosphoserine
    1663-1663 Phosphoserine
    1659-1659 Phosphoserine
    1335-1335 Phosphoserine
    1283-1283 Phosphoserine
    1265-1265 Phosphoserine
 
Prediction
NeProc
Disorder 1-26,198-846,904-1173,1203-1666,1769-1801
Order 27-197,847-903,1174-1202,1667-1768,1802-1966
ProS 249-299,316-323,346-349,438-441,498-505,514-521,568-573,653-659,750-777,788-799,806-813,819-824,832-846,904-908,935-965,1024-1030,1273-1281,1313-1319,1362-1369,1405-1410,1426-1431,1437-1444,1543-1551,1566-1575,1650-1655,1776-1782,1792-1801
AlphaFold
Disorder 1-31,40-44,53-90,205-855,906-1668,1708-1712,1727-1738,1761-1761,1763-1801,1804-1825
Order 32-39,45-52,91-204,856-905,1669-1707,1713-1726,1739-1760,1762-1762,1802-1803,1826-1966
Pfam Hmmer
PF00076 105-176 9.8e-12
PF00856 1821-1950 2.7e-54
SEG 5-18 ,230-242 ,335-345 ,355-365 ,376-391 ,408-419 ,431-457 ,531-543 ,555-568 ,573-607 ,659-756 ,799-807 ,937-959 ,988-1001 ,1040-1065 ,1068-1087 ,1094-1124 ,1127-1141 ,1148-1204 ,1213-1224 ,1307-1341 ,1383-1427 ,1465-1529 ,1539-1554 ,1580-1601 ,1795-1807 ,1816-1833
Function
Function in SwissProt
Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1A suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Specifically tri-methylates 'Lys-4' of histone H3 in vitro.