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| Functional site class: | SH2 ligand |
| Functional site description: | Src Homology 2 (SH2) domains recognize small motifs containing a phosphorylated Tyrosine residue |
|---|---|
| ELMs: | LIG_SH2_GRB2 LIG_SH2_PTP2 LIG_SH2_SRC LIG_SH2_STAT3 LIG_SH2_STAT5 LIG_SH2_STAT6 |
| Description: | GRB2-like Src Homology 2 (SH2) domains binding motif. |
| Pattern: | (Y).N. (Probability: 0.0004787) |
| Present in taxons: |
Homo sapiens
Mesocricetus auratus
Metazoa
Mus musculus
Rattus norvegicus
Torpedo californica
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PDB Structure: 1QG1
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| Interaction Domain: |
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See 15 Instances for LIG_SH2_GRB2
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| 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. |
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Please cite: ELM - the database of eukaryotic linear motifs (PMID:
22110040)
ELM data can be downloaded and distributed for non-commercial use according to the ELM Software License Agreement






