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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Bd2iuib1 Alpha and beta proteins (a+b) SH2-like SH2 domain SH2 domain automated matches Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd2iuib2 Artifacts Tags Tags Tags N-terminal Tags Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ad2iuia1 Alpha and beta proteins (a+b) SH2-like SH2 domain SH2 domain automated matches Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ad2iuia2 Artifacts Tags Tags Tags N-terminal Tags Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilySH2 domain8052378 3000197 SCOP2B (2022-06-29)
ASCOP2B SuperfamilySH2 domain8052378 3000197 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BPF00017e2iuiB1 A: a+b two layersX: SH2 (From Topology)H: SH2 (From Topology)T: SH2F: PF00017ECOD (1.6)
APF00017e2iuiA1 A: a+b two layersX: SH2 (From Topology)H: SH2 (From Topology)T: SH2F: PF00017ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B3.30.505.10 Alpha Beta 2-Layer Sandwich SHC Adaptor Protein SH2 domainCATH (4.3.0)
A3.30.505.10 Alpha Beta 2-Layer Sandwich SHC Adaptor Protein SH2 domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00017SH2 domain (SH2)SH2 domain- Domain
A, B
PF16454Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain (PI3K_P85_iSH2)Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domainThis domain is found between the two SH2 domains in phosphatidylinositol 3-kinase regulatory subunit P85. It forms a complex with the adaptor-binding domain of phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha [1].Domain
C, 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, B
Phosphatidylinositol 3-kinase regulatory subunit alpha
C, D
Platelet-derived growth factor receptor beta

InterPro: Protein Family Classification InterPro Database Homepage

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, B
PharosP27986
C, D
PharosP09619

Protein Modification Annotation

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

RESIDAA0039

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