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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1ir3a_ Alpha and beta proteins (a+b) Protein kinase-like (PK-like) Protein kinase-like (PK-like) Protein kinases, catalytic subunit Insulin receptor human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

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)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APkinase_Tyre1ir3A1 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)
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
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
INSULIN RECEPTOR
PEPTIDE SUBSTRATE---

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosP06213

Protein Modification Annotation

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

RESIDAA0039

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

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

ChainsEnzyme NameDescriptionCatalytic Residues
receptor protein-tyrosine kinase  M-CSA #246

Phosphorylated insulin receptor tyrosine kinase from Homo sapiens catalyses the phosphorylation of Tyr on intracellular proteins that are related to the STATK pathway. The phosphoryl group is transferred from ATP to form ADP. On carrying out this function, the enzyme activates the signalling cascade inside the cell. Insulin receptor tyrosine kinase is thought to have a restricted range of protein substrates, with a consensus YMXM phosphorylation motif having been defined [PMID:17085043].

There are two alternative mechanisms suggested for this enzyme, and there is still some debate as to whether this enzyme works via the associative (SN2-type) mechanism or the dissociative (SN1-type) mechanism. However, experimental and QM/MM studies, as well as crystallographic evidence, seems to support the dissociative mechanism [PMID:17085043, PMID:16023488, PMID:19334696 and Pichierri et al.].

Defined by 4 residues: ASP:A-155 [auth A-1132]ARG:A-159 [auth A-1136]ASN:A-160 [auth A-1137]ASP:A-173 [auth A-1150]
 | 
 
Explore in 3DM-CSA Motif Definition