| General information | | DisProt: | DP00016 | | Name: | Cyclin-dependent kinase inhibitor 1 | | Synonym(s): | CDN1A_HUMAN
CDK-interacting protein 1
Cyclin-dependent kinase inhibitor p21
p21
Melanoma differentiation-associated protein 6
MDA-6
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P38936 | | UniGene: | Hs.370771 | | SwissProt: | CDN1A_HUMAN | | TrEMBL: | | | NCBI (GI): | 729143 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 164 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSEPAGDVRQ NPCGSKACRR LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLE - 60
GDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLV - 120
PRSGEQAEGS PGGPGDSQGR KRRQTSMTDF YHSKRRLIFS KRKP
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| Functional narrative |
CDK-inhibitor 1 is a member of the CDI family with a subcellular location in the nucleus. p21 mediates G1/S arrest through inhibition of Cdks and possibly through inhibition of DNA replication. CDK-inhibitor 1 (p21) interacts with Zinc and it will attach to multiple families of cyclin-Cdks including cyclin E-Cdk2 and cyclin D-Cdk4. Amino acids 17-77 have been shown to be the binding region of the sequence.
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| 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.
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| Region 1 | | Type: | Disordered - Extended | | Name: | p21-F (full length) | | Location: | 1 - 164 | | Length: | 164 | | Region sequence: |
MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLE
GDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLV
PRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- SDS-PAGE gel, Aberrant mobility on
- Circular dichroism (CD) spectroscopy, far-UV
- Size exclusion/gel filtration chromatography
- Stability at pH extremes
- Mass spectrometry-based high resolution hydrogen-deuterium exchange
- Nuclear magnetic resonance (NMR)
- Sensitivity to proteolysis
| References:
- Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. "Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity." Proc Natl Acad Sci U S A. 1996; 93(21): 11504-9. PubMed: 8876165
- Kriwacki RW, Wu J, Tennant L, Wright PE, Siuzdak G. "Probing protein structure using biochemical and biophysical methods. Proteolysis, matrix-assisted laser desorption/ionization mass spectrometry, high-performance liquid chromatography and size-exclusion chromatography of p21Waf1/Cip1/Sdi1." J Chromatogr A. 1997; 777(1): 23-30. PubMed: 9297835
| Comments:
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| References |
- Harper JW, Adami GR, Wei N, Keyomarsi K, Elledge SJ. "The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases." Cell. 1993; 75(4): 805-16. PubMed: 8242751
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