| + |
FKTN | form complex 
binding
|
Fukutin-FKRP-TMEM5 multienzyme complex |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281091 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29477842 |
Functions of the dystroglycanopathy genes fukutin, fukutin-related protein (FKRP), and transmembrane protein 5 (TMEM5) were most recently identified; fukutin and FKRP are ribitol-phosphate transferases and TMEM5 is a ribitol xylosyltransferase. In this study, we show that fukutin, FKRP, and TMEM5 form a complex while maintaining each of their enzyme activities. Our data showed for the first time that endogenous fukutin and FKRP enzyme activities coexist with TMEM5 enzyme activity, and suggest the possibility that formation of this enzyme complex may contribute to specific and prompt biosynthesis of glycans that are required for dystroglycan function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FKRP | form complex
binding
|
Fukutin-FKRP-TMEM5 multienzyme complex |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281092 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29477842 |
Functions of the dystroglycanopathy genes fukutin, fukutin-related protein (FKRP), and transmembrane protein 5 (TMEM5) were most recently identified; fukutin and FKRP are ribitol-phosphate transferases and TMEM5 is a ribitol xylosyltransferase. In this study, we show that fukutin, FKRP, and TMEM5 form a complex while maintaining each of their enzyme activities. Our data showed for the first time that endogenous fukutin and FKRP enzyme activities coexist with TMEM5 enzyme activity, and suggest the possibility that formation of this enzyme complex may contribute to specific and prompt biosynthesis of glycans that are required for dystroglycan function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RXYLT1 | form complex
binding
|
Fukutin-FKRP-TMEM5 multienzyme complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281093 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29477842 |
Functions of the dystroglycanopathy genes fukutin, fukutin-related protein (FKRP), and transmembrane protein 5 (TMEM5) were most recently identified; fukutin and FKRP are ribitol-phosphate transferases and TMEM5 is a ribitol xylosyltransferase. In this study, we show that fukutin, FKRP, and TMEM5 form a complex while maintaining each of their enzyme activities. Our data showed for the first time that endogenous fukutin and FKRP enzyme activities coexist with TMEM5 enzyme activity, and suggest the possibility that formation of this enzyme complex may contribute to specific and prompt biosynthesis of glycans that are required for dystroglycan function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Fukutin-FKRP-TMEM5 multienzyme complex | up-regulates activity 
glycosylation
|
DAG1 |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281094 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29477842 |
Our data showed for the first time that endogenous fukutin and FKRP enzyme activities coexist with TMEM5 enzyme activity, and suggest the possibility that formation of this enzyme complex may contribute to specific and prompt biosynthesis of glycans that are required for dystroglycan function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
Fukutin-FKRP-TMEM5 multienzyme complex