Summary: Cyclin-dependent kinase inhibitor
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This is the Wikipedia entry entitled "Cyclin-dependent kinase inhibitor protein". More...
Cyclin-dependent kinase inhibitor protein Edit Wikipedia article
Cyclin-dependent kinase inhibitor | |||||||||||
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![]() Structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex.[1] | |||||||||||
Identifiers | |||||||||||
Symbol | CDI | ||||||||||
Pfam | PF02234 | ||||||||||
InterPro | IPR003175 | ||||||||||
SCOPe | 1jsu / SUPFAM | ||||||||||
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A cyclin-dependent kinase inhibitor protein is a protein which inhibits the enzyme cyclin-dependent kinase (CDK). Several function as tumor suppressor proteins. Cell cycle progression is delayed or stopped by cyclin-dependent kinase inhibitors, abbreviated CDIs, CKIs or CDKIs. CDIs are involved in cell cycle arrest at the G1 phase.
Seven cyclin-dependent kinase inhibitor proteins have thus far been identified. They are named by the small letter "p" followed by their molecular weight in kilodaltons. They are p15, p16, p18, p19, p21, p27, and p57.
Associated gene and target
References
- ^ Russo AA, Jeffrey PD, Patten AK, Massagué J, Pavletich NP (July 1996). "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex". Nature. 382 (6589): 325–31. doi:10.1038/382325a0. PMID 8684460.
- ^ Hoshino R, Chatani Y, Yamori T, Tsuruo T, Oka H, Yoshida O, Shimada Y, Ari-i S, Wada H, Fujimoto J, Kohno M (January 1999). "Constitutive activation of the 41-/43-kDa mitogen-activated protein kinase signaling pathway in human tumors". Oncogene. 18 (3): 813–22. doi:10.1038/sj.onc.1202367. PMID 9989833.
External links
- Cyclin-Dependent+Kinase+Inhibitor+Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
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Cyclin-dependent kinase inhibitor Provide feedback
Cell cycle progression is negatively controlled by cyclin-dependent kinases inhibitors (CDIs). CDIs are involved in cell cycle arrest at the G1 phase.
Literature references
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Lee MH, Reynisdottir I, Massague J; , Genes Dev 1995;9:639-649.: Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution. PUBMED:7729683 EPMC:7729683
External database links
SCOP: | 1jsu |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003175
Cell cycle progression is negatively controlled by cyclin-dependent kinases inhibitors (CDIs). CDIs are involved in cell cycle arrest at the G1 phase.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | nucleus (GO:0005634) |
Molecular function | cyclin-dependent protein serine/threonine kinase inhibitor activity (GO:0004861) |
Biological process | cell cycle arrest (GO:0007050) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (103) |
Full (1640) |
Representative proteomes | UniProt (2527) |
NCBI (3815) |
Meta (1) |
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RP15 (162) |
RP35 (650) |
RP55 (1185) |
RP75 (1637) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (103) |
Full (1640) |
Representative proteomes | UniProt (2527) |
NCBI (3815) |
Meta (1) |
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RP15 (162) |
RP35 (650) |
RP55 (1185) |
RP75 (1637) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_1698 (release 5.2) & Pfam-B_5787 (Release 8.0) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Bateman A |
Number in seed: | 103 |
Number in full: | 1640 |
Average length of the domain: | 48.70 aa |
Average identity of full alignment: | 32 % |
Average coverage of the sequence by the domain: | 23.70 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 49 | ||||||||||||
Family (HMM) version: | 20 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CDI domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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