Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
198
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Seq 1-198 Hetero trimer : IID00034 Complex
Region 5uq3 C 1-50 disorder
Region 5uq3 C 51-96 order
Region 5uq3 C 97-198 disorder
Seq 22-106 Hetero trimer : IID00032 Complex ,
IID00034 Complex
Region 1jsu C 23-24 disorder
Region 1jsu C 25-93 order
Region 1jsu C 94-106 disorder
Region 6ath C 22-24 disorder
Region 6ath C 25-48 order
Region 6ath C 49-53 disorder
Region 6ath C 54-79 order
Region 6ath C 80-85 disorder
Seq 25-35 Hetero trimer : IID00032 Complex
Region 1h27 E 25-29 disorder
Region 1h27 E 30-35 order
Region 6p8e C 25-80 order
Region 6p8e C 81-93 disorder
Region 6p8f C 25-79 order
Region 6p8f C 80-89 disorder
Region 6p8f C 93-106 disorder
Region 6p8g C 25-79 order
Region 6p8g C 80-93 disorder
Seq 181-190 Hetero tetramer : IID00309 Complex ,
IID00321 Complex
Region 2ast D 181-190 order
Seq 187-198 Hetero dimer : IID00301 Complex
Region 7or8 P 187-193 disorder
Region 7or8 P 194-198 order
Region 7org P 187-193 disorder
Region 7org P 194-198 order
Region 7orh P 187-193 disorder
Region 7orh P 194-198 order
Region 7ors P 187-193 disorder
Region 7ors P 194-198 order
Region 7ort P 187-193 disorder
Region 7ort P 194-198 order
Region 6p8f C 25-79 order
Region 6p8e C 25-80 order
Region 6p8g C 25-79 order
Seq ProS verified 25-93 Hetero trimer : IID00032 Complex ,
IID00034 Complex
Region 1jsu C 25-93 order
Region 6ath C 25-48 order
Region 6ath C 54-79 order
Seq ProS verified 30-35 Hetero trimer : IID00032 Complex
Region 1h27 E 30-35 order
Seq ProS verified 51-96 Hetero trimer : IID00034 Complex
Region 5uq3 C 51-96 order
Seq ProS verified 181-190 Hetero tetramer : IID00309 Complex ,
IID00321 Complex
Region 2ast D 181-190 order
Seq ProS verified 194-198 Hetero dimer : IID00301 Complex
Region 7org P 194-198 order
Region 7orh P 194-198 order
Region 7ors P 194-198 order
Region 7or8 P 194-198 order
Region 7ort P 194-198 order
10-10 Phosphoserine; by UHMK1
74-74 Phosphotyrosine; by SRC
88-88 Phosphotyrosine; by ABL
157-157 Phosphothreonine; by CaMK1
187-187 Phosphothreonine; by PKB/AKT1
198-198 Phosphothreonine; by CaMK1
Prediction
ProS 1-9,143-149,183-190,195-198
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
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/CKS1B Crystal structure of Skp1-Skp2-Cks1 in complex with a p27 peptide
Diagram without PDB data
CDKN1B Activation of Akt results in phosphorylation p27, which are then transported to the cytoplasm with 14-3-3.