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:
Members of the non-receptor tyrosine kinase Csk family phosphorylate the C-terminal tyrosine residues of the Src family.
Pattern: [TAD][EA].Q(Y)[QE].[GQA][PEDLS]
Pattern Probability: 2.926e-07
Present in taxon: Metazoa
Interaction Domain:
Pkinase_Tyr (PF07714) Protein tyrosine kinase (Stochiometry: 1 : 1)
o See 12 Instances for MOD_TYR_CSK
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 3 GO-Terms:

o 12 Instances for MOD_TYR_CSK
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Protein NameGene NameStartEndSubsequenceLogic#Ev.OrganismNotes
YES_HUMAN YES1 533 541 SFLEDYFTATEPQYQPGENL TP 1 Homo sapiens (Human)
FGR_HUMAN FGR 519 527 SFLEDYFTSAEPQYQPGDQT TP 1 Homo sapiens (Human)
HCK_HUMAN HCK 518 526 IQSVLDDFYTATESQYQQQP TP 1 Homo sapiens (Human)
SRC_HUMAN SRC 526 534 AFLEDYFTSTEPQYQPGENL TP 1 Homo sapiens (Human)
SRC_CHICK SRC 523 531 AFLEDYFTSTEPQYQPGENL TP 1 Gallus gallus (Chicken)
SRC_RAT Src 526 534 AFLEDYFTSTERQYQPGENL TP 1 Rattus norvegicus (Norway rat)
FYN_MOUSE Fyn 527 535 GFLEDYFTATEPQYQPGENL TP 1 Mus musculus (House mouse)
FYN_HUMAN FYN 527 535 SFLEDYFTATEPQYQPGENL TP 1 Homo sapiens (Human)
LYN_MOUSE Lyn 504 512 LQSVLDDFYTATEGQYQQQP TP 1 Mus musculus (House mouse)
LYN_RAT Lyn 504 512 LQSVLDDFYTATEGQYQQQP TP 1 Rattus norvegicus (Norway rat)
LYN_HUMAN LYN 504 512 LQSVLDDFYTATEGQYQQQP TP 1 Homo sapiens (Human)
BLK_HUMAN BLK 497 505 LQSVLEDFYTATERQYELQP TP 1 Homo sapiens (Human)
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

ELM data can be downloaded and distributed for non-commercial use according to the ELM Software License Agreement
feedback@elm.eu.org