| + |
POMT1 | form complex 
binding
|
POMT |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265428 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16698797 |
Here we have shown that POMT1 forms a complex with POMT2 and the complex possesses protein O-mannosyltransferase activity. Results indicate that POMT1 and POMT2 associate physically and functionally in vivo. Mutations in the POMT1 and POMT2 genes are considered to be the cause of Walker-Warburg syndrome. Here, we have demonstrated that POMT1 and POMT2 form a functional complex in vivo using immunoprecipitating techniques. Furthermore, we showed that the mutations of POMT1 protein found in WWS patients do not prevent complex formation with POMT2 but they do abolish activity of the complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POMT | up-regulates activity 
glycosylation
|
DGC |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265431 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14699049 |
we showed that coexpression of both POMT1 and POMT2 (another gene homologous to yeast protein O-mannosyltransferases) was necessary for the enzyme activity, but expression of either POMT1 or POMT2 alone was insufficient. The requirement of an active enzyme complex of POMT1 and POMT2 suggests that the regulation of protein O-mannosylation is complex. Further, protein O-mannosylation appears to be required for normal structure and function of α-dystroglycan in muscle and brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POMT2 | form complex
binding
|
POMT |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265429 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16698797 |
Here we have shown that POMT1 forms a complex with POMT2 and the complex possesses protein O-mannosyltransferase activity. Results indicate that POMT1 and POMT2 associate physically and functionally in vivo. Mutations in the POMT1 and POMT2 genes are considered to be the cause of Walker-Warburg syndrome. Here, we have demonstrated that POMT1 and POMT2 form a functional complex in vivo using immunoprecipitating techniques. Furthermore, we showed that the mutations of POMT1 protein found in WWS patients do not prevent complex formation with POMT2 but they do abolish activity of the complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POMT | up-regulates activity
glycosylation
|
DAG1 |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265430 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14699049 |
we showed that coexpression of both POMT1 and POMT2 (another gene homologous to yeast protein O-mannosyltransferases) was necessary for the enzyme activity, but expression of either POMT1 or POMT2 alone was insufficient. The requirement of an active enzyme complex of POMT1 and POMT2 suggests that the regulation of protein O-mannosylation is complex. Further, protein O-mannosylation appears to be required for normal structure and function of α-dystroglycan in muscle and brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
POMT
CPX-2659