Annotations: 2J17

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	DSPc	e2j17A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)
B	DSPc	e2j17B1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: DSPc	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
B	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00782	Dual specificity phosphatase, catalytic domain (DSPc)	Dual specificity phosphatase, catalytic domain	Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	TYROSINE-PROTEIN PHOSPHATASE YIL113W	phosphoric ester hydrolase activity phosphoprotein phosphatase activity MAP kinase tyrosine phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds MAP kinase phosphatase activity phosphatase activity protein tyrosine phosphatase activity hydrolase activity catalytic activity protein tyrosine/threonine phosphatase activity MAP kinase tyrosine/serine/threonine phosphatase activity protein tyrosine/serine/threonine phosphatase activity	cellular response to stimulus regulation of cellular process response to stimulus signaling negative regulation of signaling negative regulation of intracellular signal transduction negative regulation of biological process regulation of signal transduction intracellular signal transduction negative regulation of cell communication cell communication regulation of intracellular signal transduction intracellular signaling cassette negative regulation of cellular process cellular response to stimulus regulation of cellular process response to stimulus signaling negative regulation of signaling negative regulation of intracellular signal transduction negative regulation of biological process regulation of signal transduction intracellular signal transduction negative regulation of cell communication cell communication regulation of intracellular signal transduction intracellular signaling cassette negative regulation of cellular process signal transduction regulation of biological process regulation of signaling negative regulation of response to stimulus biological regulation regulation of MAPK cascade negative regulation of signal transduction regulation of response to stimulus MAPK cascade regulation of cell communication cellular process negative regulation of MAPK cascade cell integrity MAPK cascade stress-activated MAPK cascade stress-activated protein kinase signaling cascade cellular response to stress response to stress	cellular anatomical structure intracellular anatomical structure cytoplasm membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029021	Protein-tyrosine phosphatase-like	Homologous Superfamily
A, B	IPR000387	Tyrosine-specific protein phosphatases domain	Domain
A, B	IPR020422	Dual specificity protein phosphatase domain	Domain
A, B	IPR000340	Dual specificity phosphatase, catalytic domain	Domain
A, B	IPR016130	Protein-tyrosine phosphatase, active site	Active Site

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.