2ED0


Conserved Protein Domain Family
SH3_Abi

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cd11826: SH3_Abi 
Click on image for an interactive view with Cn3D
Src homology 3 domain of Abl Interactor proteins
Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. 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: 212760
Aligned: 16 rows
Threshold Bit Score: 93.1548
Created: 31-May-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
peptide ligand
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:peptide ligand binding site [polypeptide binding site]
Evidence:
  • Comment:based on the binding of peptide ligands to the SH3 domains of other superfamily members
  • Comment:SH3 domains typically bind proline-rich ligands, preferentially to PxxP motifs.
  • Citation:PMID 7664083
  • Citation:PMID 7735837
  • 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             # #  #   #                  ##            # ##  
2ED0_A        19 KVVAIYDYTKDKEDELSFQEGAIIYVIKKn-dDGWYEGVMNgVTGLFPGNYVE 70  human
XP_002594719 371 KVVAVYDYEREREDELSFNEGQIIYVIKKn-eDGWYEGVMNgAHGLFPGNYVE 422 Florida lancelet
CAX69750     526 KVITMYEYIRDKDDELTFTENQIIYVIKKn-dDGWWEGIMNgITGLFPGNYVE 577 Schistosoma japonicum
XP_002110190 551 KVRAMYDYRQQRSDELNIDDGDVIYVIKEn-mDGWFEGSLKgKVGKFPGNYVE 602 Trichoplax adhaerens
NP_001070242 400 KVVALYTYDTGKPGDLVFQEGDIIYLTSRn-eDGWCEGVLNgVKGYFPGNYVE 451 zebrafish
7494875      383 KVRVLYDYDAAKEDELTLRENAIVYVLKKn-dDDWYEGVLDgVTGLFPGNYVV 434 Caenorhabditis elegans
XP_002163783 343 KVVAIYDYEKLRDDELQLTEGDVIYVLKKn-dDGWYEGIKDgIQGLFPGNYVY 394 green hydra
1175425      588 YVKALYAYTAQSDMELSIQEGDIIQVTNRnagNGWSEGILNgVTGQFPANYVT 640 fission yeast
XP_003386262 645 KVEALYDYVKDKEDELTFSAGSIIYVVKKn-dDGWYEGVLDgNTGLFPGNYVD 696 Amphimedon queenslandica
XP_003442464 483 KVRALYSYEAVKLDELSFTEGDIIYLTQRh-dDGWYQGILNgRQGYFPENYVE 534 Nile tilapia

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