2K79,1QLY,1GL5


Conserved Protein Domain Family
SH3_Tec_like

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cd11768: SH3_Tec_like 
Click on image for an interactive view with Cn3D
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases
The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. 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: 212702
Aligned: 15 rows
Threshold Bit Score: 91.9511
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             # #  #   #                 ##             # ##   
2K79_A         7 LVIALYDYQTNDpqELALRCDEEYYLLDSseIHWWRVQDKnGHEGYAPSSYLVE 60  house mouse
1QLY_A         3 KVVALYDYMPMNanDLQLRKGDEYFILEEsnLPWWRARDKnGQEGYIPSNYVTE 56  human
1GL5_A         4 IVVAMYDFQATEahDLRLERGQEYIILEKndLHWWRARDKyGSEGYIPSNYVTG 57  house mouse
P42681        86 QVKALYDFLPREpcNLALRRAEEYLILEKynPHWWKARDRlGNEGLIPSNYVTE 139 human
XP_002124836  12 SVVALYDFEPQEagDVGLVADEVYTVLETsrPHWWKVRNKrGEEGYVPANYVKY 65  Ciona intestinalis
BAD52302     197 QVVAKFDFPGIEaqDLPLVKGCTYVILDDknPHWWRAQDEeGREGLIPSTYVYP 250 inshore hagfish
XP_002734040 199 VVVALYPYTPTQqgDLALVKGDEYTVLDDsrEHWWKAKNSrGEVGHIPSNFVQE 252 Saccoglossus kowalevskii
AAP82507     257 DVIAMYDYPGLErgDLPLVKGQRVTVFDAtrEFWWRARDEqGSEGYIPSNYVKK 310 Suberites domuncula
EGD72208     200 KVVAMFPFHALEptDLSLSPGEELEVLDAsqEHWWRARNSkGEAGMIPANYVRK 253 Salpingoeca sp. ATCC50818
XP_001745298 221 EVQSLYDYDALEptDLSLSKGERLVIVDQmeEHWWKARNNaGQEGYIPANYVRK 274 Monosiga brevicollis MX1

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