Annotations: 2DKQ

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2dkqa1	All beta proteins	PH domain-like barrel	PH domain-like	Phosphotyrosine-binding domain (PTB)	Tensin	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2dkqa3	Artifacts	Tags	Tags	Tags	C-terminal Tags	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2dkqa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	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	Phosphotyrosine-binding domain (PTB)	8027428	4002427	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PH domain-like	8039807	3000134	SCOP2 (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	PTB	e2dkqA1	A: beta barrels	X: PH domain-like	H: PH domain-like (From Topology)	T: PH domain-like	F: PTB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.29.30	Mainly Beta	Roll	PH-domain like	Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08416	Phosphotyrosine-binding domain (PTB)	Phosphotyrosine-binding domain	The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molec ...	The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (Pfam:PF00017) domain and a region similar to the tumour suppressor PTEN [1]. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	KIAA1075 protein	phosphoric ester hydrolase activity phosphoprotein phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds protein tyrosine phosphatase activity phosphatase activity hydrolase activity catalytic activity protein binding binding kinase binding enzyme binding lipid binding cation binding phosphoric ester hydrolase activity phosphoprotein phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds protein tyrosine phosphatase activity phosphatase activity hydrolase activity catalytic activity protein binding binding kinase binding enzyme binding lipid binding cation binding ion binding metal ion binding small molecule binding identical protein binding	response to stimulus response to activity response to muscle activity cellular homeostasis homeostatic process cellular response to stimulus cellular response to nitrogen compound response to organic substance regulation of cellular process negative regulation of signaling signaling response to peptide hormone negative regulation of biological process regulation of signal transduction response to stimulus response to activity response to muscle activity cellular homeostasis homeostatic process cellular response to stimulus cellular response to nitrogen compound response to organic substance regulation of cellular process 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 cellular response to organic substance 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 response to organonitrogen compound 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 cellular response to organonitrogen compound regulation of response to stimulus negative regulation of insulin receptor signaling pathway response to chemical response to insulin regulation of cell communication cellular process cellular response to insulin stimulus multicellular organismal process multicellular organismal-level homeostasis negative regulation of cell population proliferation cell population proliferation regulation of cell population proliferation collagen metabolic process metabolic process protein dephosphorylation organonitrogen compound metabolic process dephosphorylation cellular metabolic process primary metabolic process organic substance metabolic process macromolecule modification phosphate-containing compound metabolic process protein metabolic process macromolecule metabolic process protein modification process phosphorus metabolic process peptidyl-tyrosine dephosphorylation developmental process multicellular organism growth developmental growth growth multicellular organism development anatomical structure development animal organ development kidney development renal system development system development	anchoring junction cell junction cellular anatomical entity focal adhesion cell-substrate junction cell periphery plasma membrane membrane intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036860	SH2 domain superfamily	Homologous Superfamily
A	IPR000980	SH2 domain	Domain
A	IPR035012	Tensin-like, SH2 domain	Domain
A	IPR029023	Tensin-type phosphatase domain	Domain
A	IPR011993	PH-like domain superfamily	Homologous Superfamily
A	IPR014020	Tensin phosphatase, C2 domain	Domain
A	IPR033929	Tensin, phosphotyrosine-binding domain	Domain
A	IPR006020	PTB/PI domain	Domain
A	IPR029021	Protein-tyrosine phosphatase-like	Homologous Superfamily
A	IPR002219	Protein kinase C-like, phorbol ester/diacylglycerol-binding domain	Domain
A	IPR013625	Tensin/EPS8 phosphotyrosine-binding domain	Domain
A	IPR035892	C2 domain superfamily	Homologous Superfamily
A	IPR046349	C1-like domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q63HR2	breast carcinoma ductal breast carcinoma in situ lung cancer breast fibroadenoma invasive ductal breast carcinoma non-small cell lung carcinoma cleft lip lung adenocarcinoma psoriasis

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.