The Eukaryote Linear Motif resource for Functional Sites in Proteins
Accession:
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 same func. site: MOD_TYR_CSK  MOD_TYR_DYR 
ELM 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)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
P83102 Dyrk3
DYRK3_DROME
430 440 SCFENQRIYTYIQSRFYRAP TP 1 Drosophila melanogaster (Fruit fly)
Q9Z188 Dyrk1b
DYR1B_MOUSE
267 277 SCQLGQRIYQYIQSRFYRSP TP 1 Mus musculus (House mouse)
Q09815 ppk5
PPK5_SCHPO
672 682 SCFYNEKVYTYLQSRFYRAP TP 1 Schizosaccharomyces pombe (Fission yeast)
Q09690 pom1
POM1_SCHPO
853 863 SCFEGECVYTYIQSRFYRSP TP 1 Schizosaccharomyces pombe (Fission yeast)
P14680 YAK1
YAK1_YEAST
524 534 SCEEARTVYTYIQSRFYRAP TP 3 Saccharomyces cerevisiae (Baker"s yeast)
Q13627 DYRK1A
DYR1A_HUMAN
315 325 SCQLGQRIYQYIQSRFYRSP TP 1 Homo sapiens (Human)
Q63470 Dyrk1a
DYR1A_RAT
315 325 SCQLGQRIYQYIQSRFYRSP TP 2 Rattus norvegicus (Norway rat)
Q61214 Dyrk1a
DYR1A_MOUSE
315 325 SCQLGQRIYQYIQSRFYRSP TP 1 Mus musculus (House mouse)
Q9Y463 DYRK1B
DYR1B_HUMAN
267 277 SCQLGQRIYQYIQSRFYRSP TP 1 Homo sapiens (Human)
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

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