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| Functional site class: | Cyclin recognition site |
| Functional site description: | Functional site that interacts with cyclins, and thereby increases the specificity of phosphorylation by cyclin/CDK complexes. |
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| ELMs: | LIG_CYCLIN_1 |
| Description: | Substrate recognition site that interacts with cyclin and thereby increases phosphorylation by cyclin/cdk complexes. Predicted protein should have the MOD_CDK site. Also used by cyclin inhibitors. |
| Pattern: | [RK].L.{0,1}[FYLIVMP] (Probability: 0.0053239) |
| Present in taxons: | Eukaryota |
PDB Structure: 1H26
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| Interaction Domain: |
Cyclin_N (PF00134) |
See 24 Instances for LIG_CYCLIN_1
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| The cyclin recognition site (alias Cy or RxL motif) is found in a wide range of cyclin/CDK interacting proteins (PMID:11067844). The presence of this motif in CDK substrates substantially increases the level of phosphorylation at (ST)Px(KR) motifs. Example proteins are the retinoblastoma protein, E2F 1-3 and p53. CDK phosphorylation mainly occurs in the nucleus but there also is some evidence for cytoplasmic function. For example, the cytoplasmic SRC and TAU proteins are known cyclin/CDK targets. The motif is recognised by a conserved region in the cyclin protein and binds in a similar manner as the p21Kip cyclin inhibitor (PDB:1JSU ). |
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