1FYN,3CQT,1A0N,1M27,1AVZ


Conserved Protein Domain Family
SH3_Fyn_Yrk

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cd12006: SH3_Fyn_Yrk 
Click on image for an interactive view with Cn3D
Src homology 3 domain of Fyn and Yrk Protein Tyrosine Kinases
Fyn and Yrk (Yes-related kinase) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Statistics
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PSSM-Id: 212939
Aligned: 7 rows
Threshold Bit Score: 116.302
Created: 31-May-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
peptide ligandSAP interaction
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:peptide ligand binding site [polypeptide binding site]
Evidence:
  • Comment:SH3 domains typically bind proline-rich ligands, preferentially to PxxP motifs.
  • Structure:1FYN; Human Fyn tyrosine protein kinase SH3 domain binds proline-rich peptide (ppayppppvp); contacts at 4A.
  • Citation:PMID 7664083
  • Structure:1AVZ; Human Fyn tyr kinase SH3 domain binds V1 Nef-protein; contacts at 4A.
  • Citation:PMID 9351809
  • Structure:1A0N; Human Fyn tyrosine protein kinase SH3 domain binds PI3K P85 subunit peptide (pprplpvapgsskt); contacts at 4A.
  • Citation:PMID 8961927
  • Comment:flanking hinge and loops (RT and n-Src) confer sequence specificity for ligand residues outside the core binding motif

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           # #  ##  #               ####            # # ##   
1FYN_A      5 TLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAP 60  human
3CQT_A      6 TLFEALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSIYLAP 61  chicken
1A0N_B      6 TLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAP 61  human
1M27_C      2 TLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAP 57  human
1AVZ_C      1 TLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAP 56  human
P13406     85 TLFVALYDYEARTEDDLSFQKGEKFQILNSSEGDWWEARSLTTGGTGYIPSNYVAP 140 African clawed frog
P27446     85 TLFVALYDYEARTEDDLSFRKGERFQILNSTEGDWWDARSLTTGGSGYIPSNYVAP 140 green swordtail

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