Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyProtein kinase-like (PK-like) 8039520 3000066 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyProtein kinase-like (PK-like) 8039520 3000066 SCOP2B (2022-06-29)
CSCOP2B SuperfamilySH2 domain 8040826 3000197 SCOP2B (2022-06-29)
DSCOP2B SuperfamilySH2 domain 8040826 3000197 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APkinase_Tyre1rqqA1 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)
BPkinase_Tyre1rqqB1 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)
CSH2e1rqqC1 A: a+b two layersX: SH2 (From Topology)H: SH2 (From Topology)T: SH2F: SH2ECOD (1.6)
DSH2e1rqqD1 A: a+b two layersX: SH2 (From Topology)H: SH2 (From Topology)T: SH2F: SH2ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.30.200.20 Alpha Beta 2-Layer Sandwich Phosphorylase Kinase domain 1CATH (4.3.0)
A1.10.510.10 Mainly Alpha Orthogonal Bundle Transferase(Phosphotransferase) domain 1CATH (4.3.0)
B3.30.200.20 Alpha Beta 2-Layer Sandwich Phosphorylase Kinase domain 1CATH (4.3.0)
B1.10.510.10 Mainly Alpha Orthogonal Bundle Transferase(Phosphotransferase) domain 1CATH (4.3.0)
C3.30.505.10 Alpha Beta 2-Layer Sandwich SHC Adaptor Protein SH2 domainCATH (4.3.0)
D3.30.505.10 Alpha Beta 2-Layer Sandwich SHC Adaptor Protein SH2 domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
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
C, D
PF00017SH2 domain (SH2)SH2 domain- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
E, F
BISUBSTRATE INHIBITOR---
A, B
Insulin receptor
C, D
adaptor protein APS

InterPro: Protein Family Classification InterPro Database Homepage

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, B
PharosP06213

Protein Modification Annotation

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

RESIDAA0039

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