v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | Slingshot homologue 1 (SSH1) is a dual specificity protein phosphatase which regulates actin filament dynamics. It dephosphorylates and activates the actin binding/depolymerising factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly [ , , ]. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses [, , , ]. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. They also contain C-terminal tails, differing in the lengths of the tail. This entry represents the dual specificity phosphatase domain (DSP) of SSH1. |
| Short Name | DSP_SSH1 |