Search Keyword:


Search option:


IID00322
 UniprotQ14839
ProteinChromodomain-helicase-DNA-binding protein 4
GeneCHD4
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1912
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 145-225 Monomer :
 Evidence NMR 2n5n A Reference
       Region 2n5n A 145-225 order
       Region 2n5n A 145-147 high_rmsd
       Region 2n5n A 220-225 high_rmsd
Seq 365-420 Monomer :
 Evidence NMR 2l5u A Reference
       Region 2l5u A 365-420 order
       Region 2l5u A 419-420 high_rmsd
Seq 446-501 Monomer :
 Evidence NMR 1mm3 A Reference
       Region 1mm3 A 446-501 order
       Region 1mm3 A 446-447 high_rmsd
 Evidence NMR 1mm2 A Reference
       Region 1mm2 A 446-501 order
       Region 1mm2 A 446-446 high_rmsd
       Region 1mm2 A 496-501 high_rmsd
Seq 446-501 Hetero dimer : IID00062Complex
 Evidence NMR 2l75 A Reference
       Region 2l75 A 446-501 order
       Region 2l75 A 446-446 high_rmsd
       Region 2l75 A 498-501 high_rmsd
Seq 499-677 Monomer :
 Evidence X-RAY 4o9i X Reference
       Region 4o9i X 499-527 order
       Region 4o9i X 528-531 disorder
       Region 4o9i X 532-585 order
       Region 4o9i X 586-590 disorder
       Region 4o9i X 591-677 order
Seq 618-674 Monomer :
 Evidence NMR 2ee1 A Reference
       Region 2ee1 A 618-674 order
Seqphosphorylation
    44-44 Phosphoserine
    303-303 Phosphoserine
    308-308 Phosphoserine
    309-309 Phosphoserine
    310-310 Phosphoserine
    319-319 Phosphoserine
    367-367 Phosphothreonine
    428-428 Phosphoserine
    515-515 Phosphoserine
    517-517 Phosphothreonine
    529-529 Phosphothreonine
    531-531 Phosphoserine
    703-703 Phosphothreonine
    1209-1209 Phosphoserine
    1308-1308 Phosphoserine
    1349-1349 Phosphoserine
    1370-1370 Phosphoserine
    1531-1531 Phosphoserine
    1535-1535 Phosphoserine
    1537-1537 Phosphoserine
    1542-1542 Phosphothreonine
    1549-1549 Phosphothreonine
    1553-1553 Phosphothreonine
    1570-1570 Phosphoserine
    1576-1576 Phosphoserine
    1602-1602 Phosphoserine
    1653-1653 Phosphothreonine
    1679-1679 Phosphothreonine
Seqacetylation
    1643-1643 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-154,216-368,409-444,515-537,584-592,681-702,1032-1035,1204-1208,1225-1245,1261-1399,1523-1694,1882-1912
Order 155-215,369-408,445-514,538-583,593-680,703-1031,1036-1203,1209-1224,1246-1260,1400-1522,1695-1717,1723-1881
ProS 22-27,107-113,216-220,257-260,356-368,409-435,584-592,697-702,1032-1035,1225-1230,1261-1264,1272-1290,1308-1360,1395-1399,1523-1552,1882-1901
AlphaFold
Disorder 1-148,218-368,406-406,408-408,418-446,518-523,525-525,527-527,530-532,534-534,585-596,598-598,680-699,829-831,906-906,937-938,999-1007,1130-1130,1132-1132,1196-1248,1261-1322,1324-1403,1407-1410,1437-1442,1470-1474,1514-1695,1805-1815,1870-1912
Order 149-217,369-405,407-407,409-417,447-517,524-524,526-526,528-529,533-533,535-584,597-597,599-679,700-828,832-905,907-936,939-998,1008-1129,1131-1131,1133-1195,1249-1260,1323-1323,1404-1406,1411-1436,1443-1469,1475-1513,1696-1804,1816-1869
Pfam Hmmer
PF08073 163-217 2.2e-37
PF00628 372-417 2.4e-19
PF00628 451-496 1.8e-19
PF00385 622-674 7.7e-14
PF00176 729-1025 4.8e-103
PF00271 1085-1164 1.2e-27
PF06465 1288-1353 6.4e-32
PF06461 1366-1523 2.7e-100
PF08074 1724-1896 8e-130
SEG 28-69 ,87-99 ,114-151 ,224-256 ,278-298 ,303-325 ,335-354 ,429-446 ,513-534 ,682-701 ,905-919 ,1051-1063 ,1289-1307 ,1349-1367 ,1533-1547 ,1564-1585 ,1603-1630 ,1660-1671
Function
Function in SwissProt
Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.
Biological Process
See also
Diagram with PDB data
MTA1/HDAC1The structure of HDAC1 in complex with the dimeric ELM2-SANT domain of MTA1 from the NuRD complex