Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilySH3-domain 8033421 3000153 SCOP2B (2022-06-29)
ASCOP2B SuperfamilySH2 domain 8037200 3000197 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyProtein kinase-like (PK-like) 8033424 3000066 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ASH3_1e4k11A3 A: beta barrelsX: SH3H: SH3T: SH3F: SH3_1ECOD (1.6)
ASH2e4k11A2 A: a+b two layersX: SH2 (From Topology)H: SH2 (From Topology)T: SH2F: SH2ECOD (1.6)
APkinase_Tyre4k11A1 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

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.30.30.40 Mainly Beta Roll SH3 type barrels. SH3 DomainsCATH (4.3.0)
A3.30.505.10 Alpha Beta 2-Layer Sandwich SHC Adaptor Protein SH2 domainCATH (4.3.0)
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)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00017SH2 domain (SH2)SH2 domain- Domain
PF00018SH3 domain (SH3_1)SH3 domainSH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase Swiss:P12931. The structure is a partly opened beta barrel.Domain
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
Proto-oncogene tyrosine-protein kinase Src

Protein Modification Annotation

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

RESIDAA0039

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