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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 290-301 Hetero dimer : IID00979Complex
 Evidence NMR 6bgg A Reference
       Region 6bgg A 290-301 order
Seq 365-420 Monomer :
 Evidence NMR 2l5u A Reference
       Region 2l5u A 365-420 order
       Region 2l5u A 419-420 high_rmsd
Seq 444-679 Homo tetramer :
 Evidence X-RAY 6q3m A Reference
       Region 6q3m A 444-445 disorder
       Region 6q3m A 446-586 order
       Region 6q3m A 587-601 disorder
       Region 6q3m A 602-676 order
       Region 6q3m A 677-679 disorder
 Evidence X-RAY 6q3m B Reference
       Region 6q3m B 444-445 disorder
       Region 6q3m B 446-586 order
       Region 6q3m B 587-602 disorder
       Region 6q3m B 603-675 order
       Region 6q3m B 676-679 disorder
 Evidence X-RAY 6q3m C Reference
       Region 6q3m C 444-444 disorder
       Region 6q3m C 445-585 order
       Region 6q3m C 586-600 disorder
       Region 6q3m C 601-678 order
       Region 6q3m C 679-679 disorder
 Evidence X-RAY 6q3m D Reference
       Region 6q3m D 444-444 disorder
       Region 6q3m D 445-517 order
       Region 6q3m D 518-535 disorder
       Region 6q3m D 536-586 order
       Region 6q3m D 587-599 disorder
       Region 6q3m D 600-674 order
       Region 6q3m D 675-679 disorder
Seq 446-501 Monomer :
 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
 Evidence NMR 1mm3 A Reference
       Region 1mm3 A 446-501 order
       Region 1mm3 A 446-447 high_rmsd
       Region 1mm3 A 494-501 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
Seq 1380-1810 Homo dimer :
 Evidence X-RAY 8d4y A Reference
       Region 8d4y A 1380-1399 disorder
       Region 8d4y A 1400-1439 order
       Region 8d4y A 1440-1444 disorder
       Region 8d4y A 1445-1468 order
       Region 8d4y A 1469-1487 disorder
       Region 8d4y A 1488-1520 order
       Region 8d4y A 1521-1695 disorder
       Region 8d4y A 1696-1808 order
       Region 8d4y A 1809-1810 disorder
 Evidence X-RAY 8d4y B Reference
       Region 8d4y B 1380-1399 disorder
       Region 8d4y B 1400-1438 order
       Region 8d4y B 1439-1440 disorder
       Region 8d4y B 1441-1468 order
       Region 8d4y B 1469-1486 disorder
       Region 8d4y B 1487-1522 order
       Region 8d4y B 1523-1693 disorder
       Region 8d4y B 1694-1807 order
       Region 8d4y B 1808-1810 disorder
SeqProS predicted 290-301 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero dimer : IID00979Complex
       Region 6bgg A 290-301 order
Seqphosphorylation
    1679-1679 Phosphothreonine
    1653-1653 Phosphothreonine
    1602-1602 Phosphoserine
    1576-1576 Phosphoserine
    1570-1570 Phosphoserine
    1553-1553 Phosphothreonine
    1549-1549 Phosphothreonine
    1542-1542 Phosphothreonine
    1537-1537 Phosphoserine
    1535-1535 Phosphoserine
    1531-1531 Phosphoserine
    1370-1370 Phosphoserine
    1349-1349 Phosphoserine
    1308-1308 Phosphoserine
    1209-1209 Phosphoserine
    703-703 Phosphothreonine
    531-531 Phosphoserine
    529-529 Phosphothreonine
    517-517 Phosphothreonine
    515-515 Phosphoserine
    428-428 Phosphoserine
    367-367 Phosphothreonine
    319-319 Phosphoserine
    310-310 Phosphoserine
    309-309 Phosphoserine
    308-308 Phosphoserine
    44-44 Phosphoserine
    303-303 Phosphoserine
    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
    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
ATP-dependent helicase that binds and distorts nucleosomal DNA (PubMed:28977666, PubMed:32543371). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:17626165, PubMed:9804427, PubMed:16428440, PubMed:28977666). Localizes to acetylated damaged chromatin in a ZMYND8-dependent manner, to promote transcriptional repression and double-strand break repair by homologous recombination (PubMed:25593309). Involved in neurogenesis (By similarity).
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