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IID00303
UniprotP46100
ProteinTranscriptional regulator ATRX
GeneATRX
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
2492
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 159-296 Monomer :
 Evidence NMR 2jm1 A Reference
       Region 2jm1 A 159-296 order
       Region 2jm1 A 159-165 high_rmsd
       Region 2jm1 A 213-215 high_rmsd
       Region 2jm1 A 295-296 high_rmsd
 Evidence X-RAY 3qln B Reference
       Region 3qln B 167-167 disorder
       Region 3qln B 168-285 order
       Region 3qln B 286-289 disorder
 Evidence X-RAY 3qln A Reference
       Region 3qln A 167-289 order
 Evidence NMR 2ld1 A Reference
       Region 2ld1 A 163-296 order
       Region 2ld1 A 163-166 high_rmsd
       Region 2ld1 A 213-215 high_rmsd
       Region 2ld1 A 295-296 high_rmsd
Seq 163-296 Hetero dimer : IID00062Complex
 Evidence NMR 2lbm A Reference
       Region 2lbm A 163-296 order
       Region 2lbm A 163-166 high_rmsd
       Region 2lbm A 213-214 high_rmsd
       Region 2lbm A 295-296 high_rmsd
Seq 167-289 Hetero dimer : IID00239Complex
 Evidence X-RAY 4w5a E Reference
       Region 4w5a E 167-167 disorder
       Region 4w5a E 168-179 order
       Region 4w5a E 180-185 disorder
       Region 4w5a E 186-287 order
       Region 4w5a E 288-289 disorder
 Evidence X-RAY 4w5a B Reference
       Region 4w5a B 167-286 order
       Region 4w5a B 287-289 disorder
 Evidence X-RAY 4w5a A Reference
       Region 4w5a A 167-288 order
       Region 4w5a A 289-289 disorder
 Evidence X-RAY 3qlc B Reference
       Region 3qlc B 167-287 order
       Region 3qlc B 288-289 disorder
 Evidence X-RAY 3qlc A Reference
       Region 3qlc A 167-287 order
       Region 3qlc A 288-289 disorder
 Evidence X-RAY 3qla D Reference
       Region 3qla D 167-168 disorder
       Region 3qla D 169-287 order
       Region 3qla D 288-289 disorder
 Evidence X-RAY 3qla A Reference
       Region 3qla A 167-287 order
       Region 3qla A 288-289 disorder
 Evidence X-RAY 3ql9 A Reference
       Region 3ql9 A 167-289 order
Seq 1256-1285 Hetero tetramer : IID00398Complex
 Evidence X-RAY 5grq D Reference
       Region 5grq D 1256-1258 disorder
       Region 5grq D 1259-1284 order
       Region 5grq D 1285-1285 disorder
 Evidence X-RAY 5grq C Reference
       Region 5grq C 1256-1285 order
Seq 1265-1288 Homo trimer : IID00398Complex
 Evidence X-RAY 5y6o A Reference
       Region 5y6o A 1265-1266 disorder
       Region 5y6o A 1267-1284 order
       Region 5y6o A 1285-1288 disorder
 Evidence X-RAY 5y6o B Reference
       Region 5y6o B 1265-1265 disorder
       Region 5y6o B 1266-1284 order
       Region 5y6o B 1285-1288 disorder
 Evidence X-RAY 5y6o C Reference
       Region 5y6o C 1265-1284 order
       Region 5y6o C 1285-1288 disorder
Seq 1265-1288 Homo trimer : IID00398Complex
 Evidence X-RAY 5y6o G Reference
       Region 5y6o G 1265-1265 disorder
       Region 5y6o G 1266-1285 order
       Region 5y6o G 1286-1288 disorder
 Evidence X-RAY 5y6o H Reference
       Region 5y6o H 1265-1265 disorder
       Region 5y6o H 1266-1284 order
       Region 5y6o H 1285-1288 disorder
 Evidence X-RAY 5y6o I Reference
       Region 5y6o I 1265-1284 order
       Region 5y6o I 1285-1288 disorder
Seq 1265-1288 Homo trimer : IID00398Complex
 Evidence X-RAY 5y6o D Reference
       Region 5y6o D 1265-1285 order
       Region 5y6o D 1286-1288 disorder
 Evidence X-RAY 5y6o E Reference
       Region 5y6o E 1265-1285 order
       Region 5y6o E 1286-1288 disorder
 Evidence X-RAY 5y6o F Reference
       Region 5y6o F 1265-1283 order
       Region 5y6o F 1284-1288 disorder
Seqphosphorylation
    2220-2220 Phosphoserine
    1992-1992 Phosphoserine
    1996-1996 Phosphoserine
    1906-1906 Phosphoserine
    1913-1913 Phosphoserine
    1529-1529 Phosphothreonine
    1527-1527 Phosphoserine
    1348-1348 Phosphoserine
    1352-1352 Phosphoserine
    1326-1326 Phosphoserine
    1322-1322 Phosphoserine
    1324-1324 Phosphoserine
    1245-1245 Phosphoserine
    1253-1253 Phosphoserine
    1244-1244 Phosphoserine
    1013-1013 Phosphoserine
    1061-1061 Phosphoserine
    1063-1063 Phosphotyrosine
    1012-1012 Phosphoserine
    1011-1011 Phosphoserine
    974-974 Phosphoserine
    977-977 Phosphothreonine
    962-962 Phosphoserine
    876-876 Phosphoserine
    889-889 Phosphoserine
    850-850 Phosphoserine
    875-875 Phosphoserine
    819-819 Phosphoserine
    849-849 Phosphoserine
    731-731 Phosphoserine
    784-784 Phosphoserine
    729-729 Phosphoserine
    677-677 Phosphoserine
    675-675 Phosphoserine
    634-634 Phosphoserine
    674-674 Phosphothreonine
    598-598 Phosphoserine
    594-594 Phosphoserine
    316-316 Phosphoserine
    591-591 Phosphothreonine
    92-92 Phosphoserine
    112-112 Phosphoserine
    213-213 Phosphoserine
    89-89 Phosphotyrosine
    34-34 Phosphoserine
    25-25 Phosphoserine
Seqacetylation
    967-967 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-161,291-334,427-1424,1474-1483,1525-1529,1895-1994,2215-2227,2286-2320,2349-2362,2396-2492
Order 162-290,335-378,384-426,1425-1473,1484-1524,1530-1859,1867-1894,1995-2214,2228-2285,2321-2348,2363-2395
ProS 8-26,38-52,84-91,114-154,306-334,427-439,450-461,483-488,514-519,538-549,584-596,656-667,732-740,759-768,844-849,866-871,927-933,993-1000,1022-1028,1071-1076,1141-1148,1225-1232,1239-1251,1264-1286,1303-1309,1336-1344,1355-1360,1383-1387,1401-1405,1420-1424,1479-1483,1525-1529,1895-1932,1939-1969,1975-1994,2223-2227,2291-2300,2349-2362,2416-2421
AlphaFold
Disorder 1-167,207-207,259-259,294-294,296-348,350-350,352-352,356-356,366-367,370-370,377-385,391-391,395-395,398-398,413-413,416-417,419-1485,1487-1487,1512-1536,1543-1546,1694-1694,1750-1753,1788-1792,1855-1870,1899-1999,2059-2070,2072-2075,2121-2123,2181-2181,2184-2205,2213-2231,2256-2266,2283-2311,2424-2426,2428-2492
Order 168-206,208-258,260-293,295-295,349-349,351-351,353-355,357-365,368-369,371-376,386-390,392-394,396-397,399-412,414-415,418-418,1486-1486,1488-1511,1537-1542,1547-1693,1695-1749,1754-1787,1793-1854,1871-1898,2000-2058,2071-2071,2076-2120,2124-2180,2182-2183,2206-2212,2232-2255,2267-2282,2312-2423,2427-2427
Pfam Hmmer
PF00176 1563-1889 1.9e-140
PF00271 2075-2155 4.2e-21
SEG 25-34 ,60-84 ,104-115 ,636-653 ,742-750 ,772-789 ,793-807 ,942-956 ,982-1004 ,1044-1058 ,1070-1083 ,1127-1138 ,1151-1163 ,1166-1185 ,1199-1216 ,1259-1266 ,1285-1299 ,1322-1331 ,1354-1367 ,1375-1399 ,1420-1429 ,1432-1472 ,1474-1489 ,1498-1524 ,1913-1949 ,1990-1999 ,2262-2283 ,2409-2430 ,2467-2480
Function
Function in SwissProt
Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomeres. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according to a report, it is not sufficient to decrease chromatin condensation at telomeres nor to increase expression of telomeric RNA in fibroblasts (PubMed:24500201). May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes (PubMed:27029610).