Table 4 |
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|
Domain pair enrichment |
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|
AD domain |
BD domain |
Domain pairings |
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|
|
|
|
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|
Name |
Exp |
Rand |
Fold |
P |
Name |
Exp |
Rand |
Fold |
P |
Exp |
Rand |
Fold |
P |
|
|
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|
Cyclin |
8 |
0.5 |
16 |
<0.00002 |
Protein kinase |
30 |
1.7 |
18 |
<0.00002 |
38 |
0.6 |
60 |
<0.00002 |
|
F-box |
17 |
1.2 |
15 |
<0.00002 |
Skp1 |
4 |
0.1 |
75 |
<0.00002 |
34 |
0.3 |
123 |
<0.00002 |
|
F-box |
17 |
1.2 |
15 |
<0.00002 |
Skp1_POZ |
4 |
0.1 |
65 |
<0.00002 |
34 |
0.3 |
123 |
<0.00002 |
|
Homeobox |
9 |
2.9 |
3 |
0.00080 |
Protein kinase |
30 |
1.7 |
18 |
<0.00002 |
33 |
3.7 |
9 |
0.00002 |
|
Extensin_2 |
20 |
11.0 |
2 |
0.00316 |
Protein kinase |
30 |
1.7 |
18 |
<0.00002 |
33 |
14.0 |
2 |
0.01536 |
|
Cyclin_C |
4 |
0.3 |
15 |
<0.00002 |
Protein kinase |
30 |
1.7 |
18 |
<0.00002 |
26 |
0.3 |
76 |
<0.00002 |
|
Drf_FH1 |
11 |
4.3 |
3 |
0.00128 |
Protein kinase |
30 |
1.7 |
18 |
<0.00002 |
19 |
5.5 |
3 |
0.01278 |
|
Cyclin |
8 |
0.5 |
16 |
<0.00002 |
RIO1 |
11 |
0.3 |
39 |
<0.00002 |
19 |
0.3 |
59 |
<0.00002 |
|
Rrm |
12 |
4.3 |
3 |
0.00032 |
Protein kinase |
30 |
1.7 |
18 |
<0.00002 |
18 |
5.5 |
3 |
0.01692 |
|
|
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|
The top 10 domain pairs observed in the interaction list are shown. As expected from interaction profiles (see text), cyclin and protein kinase domains are significantly associated, as are F-box and Skp domains. RIO1 is a recently described kinase domain [62] while the Extensin_2 domain is a proline-rich sequence. Drf_FH1 is the Diaphanous-related formin domain, a low-complexity 12-residue repeat found in proteins involved with cytoskeletal dynamics and the Rho-family GTPases [63], and the Rrm is an RNA-recognition motif. There are also additional associations between protein kinase domains and nucleic acid metabolism domains (see Additional data file 5). These data demonstrate the capacity of relatively small sets of proteins to generate high-confidence domain associations. A complete list of all domains and domain pairs found in the interaction data is in Additional data file 5. |
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|
Stanyon et al. Genome Biology 2004 5:R96 doi:10.1186/gb-2004-5-12-r96 |
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