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IID00988
 UniprotQ7Z3K3
ProteinPogo transposable element with ZNF domain
GenePOGZ
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1410
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 370-405 Monomer :
 Evidence NMR 2e72 A Reference
       Region 2e72 A 370-405 order
       Region 2e72 A 370-372 high_rmsd
       Region 2e72 A 404-405 high_rmsd
Seq 1370-1404 Hetero dimer : IID00408Complex
 Evidence NMR 6emp A Reference
       Region 6emp A 1370-1404 order
       Region 6emp A 1370-1377 high_rmsd
       Region 6emp A 1392-1393 high_rmsd
       Region 6emp A 1403-1404 high_rmsd
Seqdisorder 1373-1410
 Evidence NMR¸ limited proteolysis The presence of an unstructured region at the C-terminus (residues 1373 - 1410) was confirmed by limited proteolysis and by the presence of more than 30 backbone amide signals in the 2D 15N/1H HSQC spectrum that are considerably sharper and less well-dispersed than the majority of amide signals from the structured part of the protein. Reference
       Region 1373-1410 disorder
Seq 1389-1404 Hetero dimer : IID00408Complex
 Evidence NMR 2n3a A Reference
       Region 2n3a A 1389-1404 order
SeqProS verified 1378-1402 The N- and C-terminal residues with high_rmsd are excluded from the ProS; IBD (Integrase-binding domain) binding Hetero dimer : IID00408Complex
       Region 6emp A 1370-1404 order
       Region 1373-1410 disorder
SeqProS verified 1389-1404 IBD (Integrase-binding domain) binding Hetero dimer : IID00408Complex
       Region 2n3a A 1389-1404 order
       Region 1373-1410 disorder
Seqphosphorylation
    439-439 Phosphothreonine
    425-425 Phosphoserine
    363-363 Phosphoserine
    333-333 Phosphoserine
    1368-1368 Phosphothreonine
    1373-1373 Phosphoserine
    1374-1374 Phosphoserine
    1378-1378 Phosphothreonine
    1392-1392 Phosphoserine; by CK2
    1394-1394 Phosphothreonine
    1396-1396 Phosphoserine; by CK2
    1367-1367 Phosphoserine
    1364-1364 Phosphoserine
    1338-1338 Phosphoserine
    856-856 Phosphoserine
    463-463 Phosphothreonine
    445-445 Phosphoserine
 
Prediction
NeProc
Disorder 1-399,407-461,674-748,796-802,842-969,1335-1410
Order 400-406,462-673,749-795,803-841,970-1334
ProS 2-26,31-42,84-88,145-154,173-187,194-200,369-399,413-432,439-461,674-693,699-705,725-748,796-802,842-885,911-916,925-930,937-946,962-969,1335-1343,1350-1362,1379-1389,1396-1410
AlphaFold
Disorder 1-379,381-464,481-491,520-529,555-558,643-645,675-688,693-750,796-813,846-972,1013-1022,1060-1064,1083-1087,1090-1090,1152-1152,1181-1184,1221-1221,1232-1233,1288-1292,1332-1338,1359-1410
Order 380-380,465-480,492-519,530-554,559-642,646-674,689-692,751-795,814-845,973-1012,1023-1059,1065-1082,1088-1089,1091-1151,1153-1180,1185-1220,1222-1231,1234-1287,1293-1331,1339-1358
SEG 9-16 ,39-54 ,239-266 ,337-344 ,413-431 ,892-935 ,959-968 ,997-1009 ,1296-1313 ,1364-1378
Function
Function in SwissProt
Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms (PubMed:20562864). Promotes the repair of DNA double-strand breaks through the homologous recombination pathway (PubMed:26721387).