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IID00851
 UniprotQ8TF72
ProteinProtein Shroom3
GeneSHROOM3
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1996
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1233-1247 Hetero tetramer : IID00301Complex
 Evidence X-RAY 6fbb P Reference
       Region 6fbb P 1240-1244 order
 Evidence X-RAY 6fcp P Reference
       Region 6fcp P 1233-1238 disorder
       Region 6fcp P 1239-1246 order
       Region 6fcp P 1247-1247 disorder
SeqProS predicted 1239-1246 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero tetramer : IID00301Complex
       Region 6fcp P 1239-1246 order
       Region 6fbb P 1240-1244 order
Seqphosphorylation
    443-443 Phosphoserine
    213-213 Phosphoserine
    439-439 Phosphoserine
    816-816 Phosphoserine
    1441-1441 Phosphoserine
    1221-1221 Phosphoserine
    1072-1072 Phosphoserine
    1069-1069 Phosphoserine
    970-970 Phosphoserine
    913-913 Phosphoserine
    910-910 Phosphoserine
    890-890 Phosphoserine
 
Prediction
NeProc
Disorder 1-21,113-1677,1683-1691,1698-1755,1962-1996
Order 22-112,1678-1682,1692-1697,1756-1961
ProS 113-118,138-171,202-228,234-238,246-264,287-296,302-316,387-396,445-450,459-479,515-521,547-557,575-578,610-616,624-638,662-668,714-714,720-727,755-762,774-791,845-851,874-907,922-927,933-947,959-966,1003-1009,1017-1030,1056-1066,1074-1100,1142-1158,1176-1181,1199-1205,1216-1225,1233-1238,1251-1278,1327-1334,1345-1364,1398-1404,1415-1427,1474-1477,1483-1488,1506-1513,1543-1548,1562-1575,1661-1677,1683-1691,1698-1709,1730-1733,1755-1755,1967-1993
AlphaFold
Disorder 1-23,111-306,311-311,314-314,316-317,321-321,323-921,940-1011,1018-1056,1060-1074,1095-1663,1688-1691,1704-1760,1762-1762,1764-1776,1868-1868,1964-1996
Order 24-110,307-310,312-313,315-315,318-320,322-322,922-939,1012-1017,1057-1059,1075-1094,1664-1687,1692-1703,1761-1761,1763-1763,1777-1867,1869-1963
Pfam Hmmer
PF00595 29-107 2.5e-09
SEG 192-203 ,258-268 ,357-368 ,737-768 ,897-908 ,950-964 ,996-1010 ,1123-1151 ,1176-1191 ,1518-1539
Function
Function in SwissProt
Controls cell shape changes in the neuroepithelium during neural tube closure. Induces apical constriction in epithelial cells by promoting the apical accumulation of F-actin and myosin II, and probably by bundling stress fibers (By similarity). Induces apicobasal cell elongation by redistributing gamma-tubulin and directing the assembly of robust apicobasal microtubule arrays (By similarity).