The Eukaryote Linear Motif resource for Functional Sites in Proteins
Accession:
Functional site class:
SH2 ligand
Functional site description:
Src Homology 2 (SH2) domains recognize small motifs containing a phosphorylated Tyrosine residue.
ELMs with same func. site: LIG_SH2_GRB2  LIG_SH2_PTP2  LIG_SH2_SRC  LIG_SH2_STAT3  LIG_SH2_STAT5  LIG_SH2_STAT6 
ELM Description:
SH-PTP2 and phospholipase C-gamma Src Homology 2 (SH2) domains binding motif.
Pattern: (Y)[IV].[VILP]
Pattern Probability: 0.0002454
Present in taxons: Homo sapiens Magnaporthe grisea Metazoa Mus musculus Rattus norvegicus
Interaction Domain:
SH2 (PF00017) SH2 domain (Stochiometry: 1 : 1)
o See 1 Instance for LIG_SH2_PTP2
o Abstract
Src Homology 2 (SH2) domains are small modular domains found within a great number of proteins involved in different signaling pathways. They are able to bind specific motifs containing a phopshorylated tyrosine residue, propagating the signal downstream promoting protein-protein interaction and/or modifying enzymatic activities. Different families of SH2 domains may have different binding specifity, which is usually determined by few residues C-terminal with respect to the pY (positions +1, +2 and +3. Non-phosphorylated peptides do not bind to the SH2 domains. At least three different binding motifs are known: pYEEI (Src-family SH2 domains), pY[IV].[VILP] (SH-PTP2, phospholipase C-gamma), pY.[EN] (GRB2). The interaction between SH2 domains and their substrates is however dependent also to cooperative contacts of other surface regions.
o 8 selected references:

o 4 GO-Terms:

o 1 Instance for LIG_SH2_PTP2
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
P35570 Irs1
IRS1_RAT
1172 1175 GGLEKSLNYIDLDLVKDVKQ TP 2 Rattus norvegicus (Norway rat)
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

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