| Type |
Details |
Score |
| Publication |
| First Author: |
Ciccarelli FD |
| Year: |
2003 |
| Journal: |
Trends Biochem Sci |
| Title: |
The KIND module: a putative signalling domain evolved from the C lobe of the protein kinase fold. |
| Volume: |
28 |
| Issue: |
7 |
| Pages: |
349-52 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The KIND (kinase non-catalytic C-lobe domain) is a putative protein interaction domain, which has been identified as being similar to the C-terminal protein kinase catalytic fold (C lobe) (see ).The presence of the KIND domain at the N terminus of signalling proteins and the absence of the active site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of the domain only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features [, ]. In SPIRE1 (protein spire homologue 1) this domain interacts with FMN2 (formin-2) [, ]. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Katoh M |
| Year: |
2004 |
| Journal: |
Int J Mol Med |
| Title: |
Identification and characterization of human FHDC1, mouse Fhdc1 and zebrafish fhdc1 genes in silico. |
| Volume: |
13 |
| Issue: |
6 |
| Pages: |
929-34 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chaum E |
| Year: |
2015 |
| Journal: |
Mamm Genome |
| Title: |
Genomic regulation of senescence and innate immunity signaling in the retinal pigment epithelium. |
| Volume: |
26 |
| Issue: |
5-6 |
| Pages: |
210-21 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mees A |
| Year: |
2005 |
| Journal: |
Gene Expr Patterns |
| Title: |
Very-KIND is a novel nervous system specific guanine nucleotide exchange factor for Ras GTPases. |
| Volume: |
6 |
| Issue: |
1 |
| Pages: |
79-85 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
247
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
572
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
396
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
598
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
743
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
643
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Vizcarra CL |
| Year: |
2011 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Structure and function of the interacting domains of Spire and Fmn-family formins. |
| Volume: |
108 |
| Issue: |
29 |
| Pages: |
11884-9 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
718
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1742
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
639
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1742
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1015
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1113
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1392
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2453
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2451
 |
| Fragment?: |
false |
|
•
•
•
•
•
|