| General information | | DisProt: | DP00018 | | Name: | Cyclin-dependent kinase inhibitor 1B | | Synonym(s): | CDN1B_HUMAN
Cyclin-dependent kinase inhibitor p27
p27Kip1
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P46527 | | UniGene: | Hs.238990 | | SwissProt: | CDN1B_HUMAN | | TrEMBL: | | | NCBI (GI): | 1168871 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 198 | | Percent disordered: | 13% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVDHEE LTRDLEKHCR DMEEASQRKW - 60
NFDFQNHKPL EGKYEWQEVE KGSLPEFYYR PPRPPKGACK VPAQESQDVS GSRPAAPLIG - 120
APANSEDTHL VDPKTDPSDS QTGLAEQCAG IRKRPATDDS STQNKRANRT EENVSDGSPN - 180
AGSVEQTPKK PGLRRRQT
|
| Functional narrative |
Important regulator of cell cycle progression. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Positive regulator of cyclin D-dependent kinases such as CDK4. Regulated by phosphorylation and degradation events.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | domain 1 | | Location: | 22 - 34 | | Length: | 13 | | Region sequence: |
EHPKPSACRNLFG | | Modification type: | Native
| | PDB: | 1JSU:C | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition scavengers
| | Functional subclasses: | Phosphorylation
Protein inhibitor
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.5; 2H2O (v/v) 5 %; DTT 5 mM; NaN3 (w/v) 0.02 %; potassium phosphate (buffer) 50 mM; protein (sample) 1 mM; Varian Inova 600-MHz (spectrometer))
| References:
- Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. "p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding." Nat Struct Mol Biol. 2004; 11(4): 358-64. PubMed: 15024385
- Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP. "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex." Nature. 1996; 382(6589): 325-31. PubMed: 8684460
| Comments:
|
| Region 2 | | Type: | Disordered | | Name: | | | Location: | 96 - 108 | | Length: | 13 | | Region sequence: |
KGACKVPAQESQD | | Modification type: | Native
| | PDB: | 1JSU:C | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Phosphorylation
Protein inhibitor
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.5; 2H2O (v/v) 5 %; DTT 5 mM; NaN3 (w/v) 0.02 %; potassium phosphate (buffer) 50 mM; protein (sample) 1 mM; Varian Inova 600-MHz (spectrometer))
| References:
- Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. "p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding." Nat Struct Mol Biol. 2004; 11(4): 358-64. PubMed: 15024385
| Comments:
|
| References |
- Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. "p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding." Nat Struct Mol Biol. 2004; 11(4): 358-64. PubMed: 15024385
|
| Comments |
Sent for AV (6-15-2010) PubMed: 15024385
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
