1SM2,3MIY


Conserved Protein Domain Family
PTKc_Itk

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cd05112: PTKc_Itk 
Click on image for an interactive view with Cn3D
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase
PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, 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, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
Statistics
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PSSM-Id: 133243
View PSSM: cd05112
Aligned: 4 rows
Threshold Bit Score: 531.448
Threshold Setting Gi: 18858911
Created: 12-Jun-2007
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 17 residues -Click on image for an interactive view with Cn3D
Feature 1:ATP binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                ##      #           # #                           #               ###
1SM2_A      2 IDPSELTFVQEIGSGQFGLVHLGYWlnkDKVAIKTIREGAmsEEDFIEEAEVMMKLSHPKLVQLYGVCLeqaPICLVFEF 81  human
NP_571179 356 IHPDEVKLSVELGSGQFGLVWKGSWq-dREVAVKTVREGFmsEEEFKEEAQVMMKLSHNRLVQLYGVVTqrsPIYLVFEF 434 zebrafish
XP_414568 358 INPSELTRVQEIGSGQFGVVYLGYWlekTKVAIKTIREGAmsEEDFIEEAKVLMKLSHPKLVQLYGVCFentPICLVFEF 437 chicken
3MIY_A      4 IDPSELTFVQEIGSGQFGLVHLGYWlnkDKVAIKTIREGAmsEEDFIEEAEVMMKLSHPKLVQLYGVCLeqaPICLVFEF 83  human
Feature 1     #  ##                                           ## #         ##                 
1SM2_A     82 MEHGCLSDYLRTQrglFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGEnQVIKVSDFGMTRFVLDDQYTSSTG 161 human
NP_571179 435 MENGCLTEFLRAKkgkLSQKALLEMCLDVSEGMAYLESSNFIHRDLAARNCLVSEnSVVKIADFGMTRFVLDDQYTSSHG 514 zebrafish
XP_414568 438 MEHGCLSDYLRSQrgsFSKETLLGMCLDVCEGMAYLEQNSVIHRDLAARNCLVGEsQVVKVSDFGMSRIVLDDQYTSSTG 517 chicken
3MIY_A     84 MEHGCLSDYLRTQrglFAAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGEnQVIKVSDFGMTRFVLDDQYTSSTG 163 human
Feature 1                                                                                     
1SM2_A    162 TKFPVKWASPEVFSFsRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKE 241 human
NP_571179 515 SKFPVRWSSPEVIKFgKYSSKSDVWSFGVFMWEVYSEGRTPYDNRSNSEVVETLNAGHRLLKPRLCPQSVYELMQWSWKE 594 zebrafish
XP_414568 518 TKFPVKWSAPEVFSYsNYSTKSDVWSFGVLMWEVFSEGKMPYENRTNGEVVEEINAGFRLYKPKLASKAIYEVMSHCWSM 597 chicken
3MIY_A    164 TKFPVKWASPEVFSFsRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKE 243 human
Feature 1                     
1SM2_A    242 rPEDRPAFSRLLRQLA 257 human
NP_571179 595 kPEDRPSFALLLHELA 610 zebrafish
XP_414568 598 rKEDRPSFSLLLYQLS 613 chicken
3MIY_A    244 rPEDRPAFSRLLRQLA 259 human

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