Search Keyword:


Search option:


IID00049
 UniprotP46527
ProteinCyclin-dependent kinase inhibitor 1B
GeneCDKN1B
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
198
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-198 Hetero trimer : IID00034Complex
 Evidence X-RAY 5uq3 C Reference
       Region 5uq3 C 1-50 disorder
       Region 5uq3 C 51-96 order
       Region 5uq3 C 97-198 disorder
Seqdisorder 1-198
 Evidence CD Reference
       Region 1-198 disorder
Seq 23-106 Hetero trimer : IID00032Complex,IID00034Complex
 Evidence X-RAY 1jsu C Reference
       Region 1jsu C 23-24 disorder
       Region 1jsu C 25-93 order
       Region 1jsu C 94-106 disorder
Seq 25-35 Hetero trimer : IID00032Complex
 Evidence X-RAY 1h27 E Reference
       Region 1h27 E 25-29 disorder
       Region 1h27 E 30-35 order
Seq 181-190 Hetero tetramer : IID00309Complex,IID00321Complex
 Evidence X-RAY 2ast D Reference
       Region 2ast D 181-190 order
SeqProS verified 25-93 Hetero trimer : IID00032Complex,IID00034Complex
       Region 1jsu C 25-93 order
       Region 1-198 disorder
SeqProS verified 25-93 Hetero trimer : IID00032Complex
       Region 1h27 E 30-35 order
       Region 1-198 disorder
SeqProS verified 51-96 Hetero trimer : IID00034Complex
       Region 5uq3 C 51-96 order
       Region 1-198 disorder
SeqProS verified 181-190 Hetero tetramer : IID00309Complex,IID00321Complex
       Region 2ast D 181-190 order
       Region 1-198 disorder
Seqphosphorylation
    10-10 Phosphoserine; by UHMK1
    74-74 Phosphotyrosine; by SRC
    88-88 Phosphotyrosine; by ABL
    89-89 Phosphotyrosine
    157-157 Phosphothreonine; by CaMK1
    170-170 Phosphothreonine
    187-187 Phosphothreonine; by PKB/AKT1
    198-198 Phosphothreonine; by CaMK1
 
Prediction
NeProc
Disorder 1-25,90-198
Order 26-89
ProS 1-9,143-149,183-190,195-198
AlphaFold
Disorder 1-1,3-3,6-21,97-164,166-187,189-189,192-194,198-198
Order 2-2,4-5,22-96,165-165,188-188,190-191,195-197
Pfam Hmmer
PF02234 30-80 6.9e-27
Function
Function in SwissProt
Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (PubMed:28666995). Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry.
Biological Process
Diagram with PDB data
CDKN1B/SKP1/SKP2/CKS1BCrystal structure of Skp1-Skp2-Cks1 in complex with a p27 peptide
Diagram without PDB data
CDKN1BActivation of Akt results in phosphorylation p27, which are then transported to the cytoplasm with 14-3-3.