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IID50089
 UniprotQ60520
ProteinPaired amphipathic helix protein Sin3a
GeneSin3a
OrganismMus musculus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1274
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 119-189 Hetero dimer : IID50088Complex
 Evidence NMR 2rms A Reference
       Region 2rms A 119-189 order
       Region 2rms A 119-119 high_rmsd
Seq 119-189 Monomer :
 Evidence NMR 2rmr A Reference
       Region 2rmr A 119-189 order
       Region 2rmr A 119-122 high_rmsd
Seq 295-383 Hetero dimer : IID00165Complex
 Evidence NMR 1g1e B Reference
       Region 1g1e B 295-383 order
       Region 1g1e B 295-300 high_rmsd
 Evidence NMR 1s5q B Reference
       Region 1s5q B 295-383 order
       Region 1s5q B 295-299 high_rmsd
       Region 1s5q B 383-383 high_rmsd
Seq 295-383 Hetero dimer : IID50097Complex
 Evidence NMR 1s5r B Reference
       Region 1s5r B 295-383 order
       Region 1s5r B 295-299 high_rmsd
Seq 295-385 Hetero dimer : IID00326Complex
 Evidence NMR 2l9s B Reference
       Region 2l9s B 295-385 order
       Region 2l9s B 295-299 high_rmsd
       Region 2l9s B 382-385 high_rmsd
Seq 456-528 Hetero dimer : IID50061Complex
 Evidence NMR 2ld7 B Reference
       Region 2ld7 B 456-528 order
       Region 2ld7 B 456-460 high_rmsd
Seq 608-729 Hetero dimer : Q8BR65
 Evidence NMR 2n2h B Reference
       Region 2n2h B 608-729 order
       Region 2n2h B 608-613 high_rmsd
       Region 2n2h B 725-729 high_rmsd
Seqphosphorylation
    861-861 Phosphoserine
    1113-1113 Phosphoserine
    1090-1090 Phosphoserine
    941-941 Phosphoserine
    833-833 Phosphoserine
    284-284 Phosphothreonine
    277-277 Phosphoserine
    10-10 Phosphoserine
Seqacetylation
    876-876 N6-acetyllysine
    866-866 N6-acetyllysine
    470-470 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-120,201-301,334-461,535-539,764-768,840-875,1120-1152,1271-1274
Order 121-200,302-333,462-534,540-644,649-763,769-839,876-1119,1153-1270
ProS 1-8,334-346,352-382,535-539,764-768,840-875,1120-1140,1148-1152
AlphaFold
Disorder 1-121,195-200,205-303,342-352,381-462,526-546,590-602,768-773,833-871,935-952,1086-1099,1102-1117,1119-1162,1171-1171,1173-1173,1175-1175,1190-1190,1268-1274
Order 122-194,201-204,304-341,353-380,463-525,547-589,603-767,774-832,872-934,953-1085,1100-1101,1118-1118,1163-1170,1172-1172,1174-1174,1176-1189,1191-1267
Pfam Hmmer
PF02671 141-187 4.1e-19
PF02671 322-381 1.2e-12
PF02671 478-524 1.8e-12
PF08295 551-651 3.6e-57
SEG 98-119 ,217-248 ,267-282 ,834-847 ,915-930 ,1135-1151
Function
Function in SwissProt
Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in the control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression (PubMed:22476904). Required for cortical neuron differentiation and callosal axon elongation (PubMed:27399968).
Biological Process
See also
Diagram with PDB data
MXD1/Sin3bStructure of the complex of the Mad1-Sin3B interaction domains
Sap25/Sin3aSolution structure of the mSin3A PAH1-SAP25 SID complex
Hbp1/Sin3aSolution Structure of HBP1 SID-mSin3A PAH2 Complex