Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyPLC-like (P variant) 8028334 4002218 SCOP2 (2022-06-29)
ASCOP2 FamilyDual specificity phosphatase-like 8031976 4000437 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyC2 domain (calcium/lipid-binding domain, calb) 8040713 3000965 SCOP2 (2022-06-29)
ASCOP2 Superfamily(Phosphotyrosine protein) phosphatases II 8044354 3000304 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APTEN_C2e1d5rA1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: C2 domain (From Topology)T: C2 domainF: PTEN_C2ECOD (1.6)
AY_phosphatasee1d5rA2 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: (Phosphotyrosine protein) phosphatases IIF: Y_phosphataseECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.90.190.10 Alpha Beta Alpha-Beta Complex Protein-Tyrosine Phosphatase Chain ACATH (4.3.0)
A2.60.40.1110 Mainly Beta Sandwich Immunoglobulin-like CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF22785Polymorphic toxin system, DSP-PTPase phosphatase (Tc-R-P)Polymorphic toxin system, DSP-PTPase phosphataseThis domain occupies the toxin tip position in a subset of polymorphic toxin domains [1,2]. This domain is found at the extreme C-terminal of certain polymorphic toxin-related Tc-like toxins deployed by bacteria against eukaryotic host cells. This po ...This domain occupies the toxin tip position in a subset of polymorphic toxin domains [1,2]. This domain is found at the extreme C-terminal of certain polymorphic toxin-related Tc-like toxins deployed by bacteria against eukaryotic host cells. This position is where the toxin module delivered into the target cells host resides [1].
Domain
PF10409C2 domain of PTEN tumour-suppressor protein (PTEN_C2)C2 domain of PTEN tumour-suppressor proteinThis is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. Th ...This is the C2 domain-like domain, in greek key form, of the PTEN protein, phosphatidyl-inositol triphosphate phosphatase, and it is the C-terminus. This domain may well include a CBR3 loop which means it plays a central role in membrane binding. This domain associates across an extensive interface with the N-terminal phosphatase domain DSPc (Pfam:PF00782) suggesting that the C2 domain productively positions the catalytic part of the protein onto the membrane [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
PHOSPHOINOSITIDE PHOSPHATASE PTEN

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosP60484

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
dual-specificity phosphatase  M-CSA #456

This is a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. It also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Its peptide phosphatase activity requires highly acidic substrates.

Defined by 3 residues: ASP:A-86 [auth A-92]CYS:A-118 [auth A-124]ARG:A-124 [auth A-130]
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