The Eukaryote Linear Motif resource for Functional Sites in Proteins
Functional site class:
TYR phosphorylation site
Functional site description:
Protein tyrosine kinases (PTKs) catalyze the transfer of the gamma-phosphate of ATP to tyrosine residues of protein substrates.
ELMs with this model: MOD_TYR_CSK  MOD_TYR_DYR 
Description:
The kinase activity of the DYRK (dual specificity kinase) is dependent on the autophosphorylation of the YXY motif in the activation loop.
Pattern: ..[RKTC][IVL]Y[TQHS](Y)[IL]QSR
Pattern Probability: 5.207e-11
Present in taxon: Eukaryota
Interaction Domain:
Pkinase (PF00069) Protein kinase domain (Stochiometry: 1 : 1)
o See 9 Instances for MOD_TYR_DYR
o Abstract
Protein-tyrosine kinases (PTKs) are essential regulators of intracellular signal-transduction pathways in eukaryotes. Tyrosine phosphorylation plays an important role in the control of several cellular processes such as cell proliferation, cell migration, differentiation, immune response, and cell cycle. Their activity is normally tight control and regulated. Perturbation of the PTK signaling by mutation and other genetic alterations result in deregulated kinase activity and malignant transformation.
The mechanism of substrate recognition by the PTKs has been one of the major challenges in phosphorylation research over the years. Peptide library approaches have provided some insight about the role of amino acid immediately surrounding Tyr phosphorylation sites and it has been shown that the specificity of PTKs is dominated by acidic or hydrophobic residues adjacent to the phosphorylated residue (Songyang,1999). Based on a larger set of experimentally verified phosphorylation sites, it was found that some amino acids were not present in some positions, e.g. tryptophan was never found in position -5 to -1. Similarly, cysteine was never found at position -2 and -1, while methionine was always absent in position -2 (Blom,2000). Recently, numerous studies have revealed that the local amino acid sequence is certainly not the sole determinant of substrate specificity but other several factor, including local structure, protein-protein interaction and surface accessibility, also play a main role.
o 3 selected references:

o 5 GO-Terms:

o 9 Instances for MOD_TYR_DYR
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Protein NameGene NameStartEndSubsequenceLogic#Ev.OrganismNotes
DYR1B_HUMAN DYRK1B 267 277 SCQLGQRIYQYIQSRFYRSP TP 1 Homo sapiens (Human)
DYR1A_MOUSE Dyrk1a 315 325 SCQLGQRIYQYIQSRFYRSP TP 1 Mus musculus (House mouse)
DYR1A_RAT Dyrk1a 315 325 SCQLGQRIYQYIQSRFYRSP TP 2 Rattus norvegicus (Norway rat)
DYR1A_HUMAN DYRK1A 315 325 SCQLGQRIYQYIQSRFYRSP TP 1 Homo sapiens (Human)
YAK1_YEAST YAK1 524 534 SCEEARTVYTYIQSRFYRAP TP 3 Saccharomyces cerevisiae (Baker"s yeast)
POM1_SCHPO pom1 853 863 SCFEGECVYTYIQSRFYRSP TP 1 Schizosaccharomyces pombe (Fission yeast)
PPK5_SCHPO ppk5 672 682 SCFYNEKVYTYLQSRFYRAP TP 1 Schizosaccharomyces pombe (Fission yeast)
DYR1B_MOUSE Dyrk1b 267 277 SCQLGQRIYQYIQSRFYRSP TP 1 Mus musculus (House mouse)
DYRK3_DROME Dyrk3 430 440 SCFENQRIYTYIQSRFYRAP TP 1 Drosophila melanogaster (Fruit fly)
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

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