Dual specificity/tyrosine protein phosphatase, N-terminal (IPR029260)

Short name: DSPn

Overlapping homologous superfamilies

Domain relationships



The active core of the dual specificity protein phosphatase is made up of two globular domains both with the DSP-like fold. This domain represents the N-terminal half of the core (DSPn). These domains are arranged in tandem, and are associated via an extensive interface to form a single globular whole.

The conserved PTP signature motif (Cys-[X]5-Arg) that defines the catalytic centre of all PTP-family members is located within the C-terminal domain, DSPc (PF00782). Although the centre of the catalytic site is formed from DSPc, two loops from the N-terminal domain, DSPn, also contribute to the catalytic site, facilitating peptide substrate specificity [PMID: 12853468].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.