CATH Classification

Domain Context

CATH Clusters

Superfamily Rhodanese-like domain
Functional Family Dual specificity phosphatase 10 (Predicted)

Enzyme Information

3.1.3.48
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q9Y6W6
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
-!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.
3.1.3.16
Protein-serine/threonine phosphatase.
based on mapping to UniProt Q9Y6W6
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
-!- A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). -!- The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).

UniProtKB Entries (2)

P47811
MK14_MOUSE
Mus musculus
Mitogen-activated protein kinase 14
Q9Y6W6
DUS10_HUMAN
Homo sapiens
Dual specificity protein phosphatase 10

PDB Structure

PDB 3TG1
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38alpha with the MAPK Binding Domain of the Phosphatase MKP5.
Zhang, Y.Y., Wu, J.W., Wang, Z.X.
Sci.Signal.