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IID00125
 UniprotQ9HB71
ProteinCalcyclin-binding protein
GeneCACYBP
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
228
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-47 Homo dimer :
 Evidence X-RAY 2a26 A Reference
       Region 2a26 A 1-47 order
 Evidence X-RAY 2a26 B Reference
       Region 2a26 B 1-44 order
       Region 2a26 B 45-47 disorder
 Evidence X-RAY 2a26 C Reference
       Region 2a26 C 1-44 order
       Region 2a26 C 45-47 disorder
Seq 58-70 Hetero tetramer : IID00120Complex
 Evidence X-RAY 2a25 B Reference
       Region 2a25 B 58-58 disorder
       Region 2a25 B 59-67 order
       Region 2a25 B 68-70 disorder
Seq 63-176 Monomer :
 Evidence NMR 1x5m A Reference
       Region 1x5m A 63-176 order
       Region 1x5m A 63-69 high_rmsd
SeqProS possible 59-67 Siah-binding motif Hetero tetramer : IID00120Complex
       Region 2a25 B 59-67 order
Seqphosphorylation
    34-34 Phosphoserine
    3-3 Phosphoserine
Seqacetylation
    118-118 N6-acetyllysine
    85-85 N6-acetyllysine
    19-19 N6-acetyllysine
    8-8 N6-acetyllysine
    2-2 N-acetylalanine
 
Prediction
NeProc
Disorder 54-69,170-193,198-210,215-228
Order 1-53,70-169,194-197,211-214
ProS 170-193,198-210,215-219,225-228
AlphaFold
Disorder 1-1,47-70,177-191,193-207,210-210,220-228
Order 2-46,71-176,192-192,208-209,211-219
Pfam Hmmer
PF04969 76-156 1.6e-22
PF05002 161-228 2.3e-34
Function
Function in SwissProt
May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1).