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Literature summary for 3.1.3.53 extracted from
- Interaction of myosin phosphatase target subunit (MYPT1) with myosin phosphatase-RhoA interacting protein (MRIP) a role of glutamic acids in the interaction (2015), PLoS One, 10, e0139875 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O14974 | - |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | interaction of myosin phosphatase target subunit (MYPT1) and myosin phosphatase-RhoA interacting protein (MRIP) causes colocalization of myosin phosphatase and RhoA to actomyosin. The residues 724-837 of MRIP are sufficient for the MYPT1/MRIP interaction. MRIP binds to MYPT1 as either a monomer or a dimer. The leucine repeat region of MYPT1, LR (residues 991-1030) is sufficient to account for the MYPT1/MRIP interaction. Point mutations that replace glutamic acids 998-1000 within LR reduce the binding affinity toward MRIP | Homo sapiens |
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