Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B Superfamily(Phosphotyrosine protein) phosphatases II8040614 3000304 SCOP2B (2022-06-29)
CSCOP2B Superfamily(Phosphotyrosine protein) phosphatases II8040614 3000304 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyProtein kinase-like (PK-like)8039520 3000066 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyProtein kinase-like (PK-like)8039520 3000066 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AY_phosphatasee2b4sA1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: (Phosphotyrosine protein) phosphatases IIF: Y_phosphataseECOD (1.6)
CY_phosphatasee2b4sC1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Flavoproteins/Phosphotyrosine protein phosphatases-likeT: (Phosphotyrosine protein) phosphatases IIF: Y_phosphataseECOD (1.6)
BPkinase_Tyre2b4sB1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: Pkinase_TyrECOD (1.6)
DPkinase_Tyre2b4sD1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: Pkinase_TyrECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, C
PF00102Protein-tyrosine phosphatase (Y_phosphatase)Protein-tyrosine phosphatase- Domain
B, D
PF07714Protein tyrosine and serine/threonine kinase (PK_Tyr_Ser-Thr)Protein tyrosine and serine/threonine kinaseProtein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosph ...Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, C
Tyrosine-protein phosphatase, non-receptor type 1
B, D
Insulin receptor

InterPro: Protein Family Classification InterPro Database Homepage

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, C
PharosP18031
B, D
PharosP06213

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
B, D
PTR Parent Component: TYR

RESIDAA0039

PSI-MOD :  O4'-phospho-L-tyrosine MOD:00048