×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Protein tyrosine phosphatase superfamily
Functional Family Protein phosphatase Slingshot homolog 2

Enzyme Information

3.1.3.16
Protein-serine/threonine phosphatase.
based on mapping to UniProt Q76I76
[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).
3.1.3.48
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q76I76
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.

UniProtKB Entries (1)

Q76I76
SSH2_HUMAN
Homo sapiens
Protein phosphatase Slingshot homolog 2

PDB Structure

PDB 2NT2
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of human slingshot phosphatase 2.
Jung, S.K., Jeong, D.G., Yoon, T.S., Kim, J.H., Ryu, S.E., Kim, S.J.
Proteins
CATH-Gene3D is a Global Biodata Core Resource Learn more...