2JJD

Protein Tyrosine Phosphatase, Receptor Type, E isoform

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8078067	3000304	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8078067	3000304	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8078067	3000304	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8078067	3000304	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8078067	3000304	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8078067	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)
C	Y_phosphatase	e2jjdC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: Y_phosphatase	ECOD (1.6)
A	Y_phosphatase	e2jjdA3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: Y_phosphatase	ECOD (1.6)
B	Y_phosphatase	e2jjdB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: Y_phosphatase	ECOD (1.6)
D	Y_phosphatase	e2jjdD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: Y_phosphatase	ECOD (1.6)
E	Y_phosphatase	e2jjdE1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: Y_phosphatase	ECOD (1.6)
F	Y_phosphatase	e2jjdF1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: Y_phosphatase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
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)
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	PF00102	Protein-tyrosine phosphatase (Y_phosphatase)	Protein-tyrosine phosphatase	-	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	RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE EPSILON	phosphoric ester hydrolase activity molecular transducer activity catalytic activity, acting on a protein phosphatase activity signaling receptor activity hydrolase activity phosphoprotein phosphatase activity hydrolase activity, acting on ester bonds protein tyrosine phosphatase activity transmembrane receptor protein phosphatase activity transmembrane signaling receptor activity transmembrane receptor protein tyrosine phosphatase activity catalytic activity	protein dephosphorylation dephosphorylation primary metabolic process macromolecule modification phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process phosphorus metabolic process cellular response to stimulus cellular response to nitrogen compound regulation of cellular process protein dephosphorylation dephosphorylation primary metabolic process macromolecule modification phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process phosphorus metabolic process cellular response to stimulus cellular response to nitrogen compound regulation of cellular process response to stimulus negative regulation of signaling signaling response to peptide hormone negative regulation of biological process regulation of signal transduction insulin receptor signaling pathway regulation of cellular response to insulin stimulus negative regulation of cell communication cell surface receptor protein tyrosine kinase signaling pathway cell communication cellular response to endogenous stimulus response to hormone negative regulation of cellular process signal transduction enzyme-linked receptor protein signaling pathway cellular response to hormone stimulus regulation of signaling regulation of biological process cell surface receptor signaling pathway negative regulation of response to stimulus response to endogenous stimulus regulation of insulin receptor signaling pathway biological regulation response to oxygen-containing compound cellular response to peptide hormone stimulus response to nitrogen compound negative regulation of signal transduction cellular response to oxygen-containing compound cellular response to chemical stimulus negative regulation of cellular response to insulin stimulus regulation of response to stimulus negative regulation of insulin receptor signaling pathway response to chemical response to insulin regulation of cell communication cellular response to insulin stimulus	cell periphery cellular anatomical structure plasma membrane membrane 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, 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	IPR003595	Protein-tyrosine phosphatase, catalytic	Domain
A, B, C, D, E A, B, C, D, E, F	IPR000242	Tyrosine-specific protein phosphatase, PTPase domain	Domain
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	IPR050348	Protein-Tyrosine Phosphatase	Family
A, B, C, D, E A, B, C, D, E, F	IPR016336	Receptor tyrosine-protein phosphatase, alpha/epsilon-type	Family
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: P23469	atypical teratoid rhabdoid tumor IgA glomerulonephritis lung carcinoma medulloblastoma ovarian cancer psoriasis breast cancer interstitial cystitis malignant ependymoma non-small cell lung carcinoma pilocytic astrocytoma Sjogren syndrome gastric carcinoma large cell medulloblastoma malignant mesothelioma atypical teratoid rhabdoid tumor IgA glomerulonephritis lung carcinoma medulloblastoma ovarian cancer psoriasis breast cancer interstitial cystitis malignant ependymoma non-small cell lung carcinoma pilocytic astrocytoma Sjogren syndrome gastric carcinoma large cell medulloblastoma malignant mesothelioma osteosarcoma pituitary cancer tuberculosis

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.