Annotations: 3EZZ

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3ezza_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d3ezzb_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d3ezzc_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d3ezzd_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d3ezze_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d3ezzf_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Dual specificity phosphatase-like	8081814	4000437	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	(Phosphotyrosine protein) phosphatases II	8081815	3000304	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8081815	3000304	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8081815	3000304	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8081815	3000304	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8081815	3000304	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8081815	3000304	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00782	e3ezzA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF00782	ECOD (1.6)
B	PF00782	e3ezzB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF00782	ECOD (1.6)
C	PF00782	e3ezzC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF00782	ECOD (1.6)
D	PF00782	e3ezzD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF00782	ECOD (1.6)
E	PF00782	e3ezzE1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF00782	ECOD (1.6)
F	PF00782	e3ezzF1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF00782	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)
C	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
D	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
E	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
F	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, C, D, E A, B, C, D, E, F	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, C, D, E A, B, C, D, E, F	Dual specificity protein phosphatase 4	phosphoric ester hydrolase activity phosphoprotein phosphatase activity protein serine/threonine phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds myosin phosphatase activity phosphatase activity hydrolase activity catalytic activity MAP kinase serine/threonine phosphatase activity MAP kinase phosphatase activity protein tyrosine/threonine phosphatase activity MAP kinase tyrosine phosphatase activity protein tyrosine phosphatase activity phosphoric ester hydrolase activity phosphoprotein phosphatase activity protein serine/threonine phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds myosin phosphatase activity phosphatase activity hydrolase activity catalytic activity MAP kinase serine/threonine phosphatase activity MAP kinase phosphatase activity protein tyrosine/threonine phosphatase activity MAP kinase tyrosine phosphatase activity protein tyrosine 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 developmental process multicellular organismal process formation of primary germ layer embryonic morphogenesis tissue development embryo development gastrulation anatomical structure morphogenesis multicellular organism development endoderm development anatomical structure development anatomical structure formation involved in morphogenesis endoderm formation negative regulation of ERK1 and ERK2 cascade ERK1 and ERK2 cascade regulation of ERK1 and ERK2 cascade dephosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process phosphorus metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR029021	Protein-tyrosine phosphatase-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR001763	Rhodanese-like domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR036873	Rhodanese-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR003595	Protein-tyrosine phosphatase, catalytic	Domain
A, B, C, D, E A, B, C, D, E, F	IPR008343	Mitogen-activated protein (MAP) kinase phosphatase	Family
A, B, C, D, E A, B, C, D, E, F	IPR000387	Tyrosine-specific protein phosphatases domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR020422	Dual specificity protein phosphatase domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR000340	Dual specificity phosphatase, catalytic domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR016130	Protein-tyrosine phosphatase, active site	Active Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: Q13115	juvenile idiopathic arthritis malignant mesothelioma myopathy pituitary cancer tuberculosis adrenal cortex adenoma breast cancer depressive disorder glioblastoma Juvenile arthritis malignant ependymoma medulloblastoma osteosarcoma prostate carcinoma ulcerative colitis juvenile idiopathic arthritis malignant mesothelioma myopathy pituitary cancer tuberculosis adrenal cortex adenoma breast cancer depressive disorder glioblastoma Juvenile arthritis malignant ependymoma medulloblastoma osteosarcoma prostate carcinoma ulcerative colitis atypical teratoid rhabdoid tumor Crohn disease esophageal adenocarcinoma interstitial cystitis lung cancer malignant glioma pancreatic ductal adenocarcinoma psoriasis Barrett esophagus cystic fibrosis facioscapulohumeral muscular dystrophy invasive ductal breast carcinoma malignant colon neoplasm

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.