Conserved Protein Domain Family
PTKc_Tec_Rlk

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cd05114: PTKc_Tec_Rlk (this model, PSSM-Id:173658 is obsolete and has been replaced by 270685)
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase
Protein Tyrosine Kinase (PTK) family; Tyrosine kinase expressed in hepatocellular carcinoma (Tec) and Resting lymphocyte kinase (Rlk); catalytic (c) domain. The PTKc family is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec subfamily of proteins, which are cytoplasmic (or nonreceptor) tyr kinases 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. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation.
Statistics
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PSSM-Id: 173658
View PSSM: cd05114
Aligned: 6 rows
Threshold Bit Score: 525.186
Threshold Setting Gi: 126331769
Created: 12-Jun-2007
Updated: 17-Jan-2013
Structure
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Aligned Rows:
 
Feature 1:active site [active site]
Evidence:
  • Comment:Based on the structures of other PTK family members bound to substrate peptides and ATP analogs as well as, the structure of human Itk bound with staurosporine inhibitor at the ATP binding site (1SM2_A).
  • Citation:PMID 9312016

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                   #####   #           # #                                           ###
gi 116242835 266 IDPSELAFIKEIGSGQFGVVHLGEWrshIQVAIKAINEGSmsEEDFIEEAKVMMKLSHSKLVQLYGVCIqrkPLYIVTEF 345
gi 71896327  366 INPSELTFMRELGSGLFGVVRLGKWraqYKVAIKAIREGAmyEEDFIEEAKVMMKLTHPKLVQLYGVCTqqrPIYIVTEF 445
gi 118090547 234 LNPSELTFMKELGRGQFGIVHLGKWkttIKVAIKKINEGAmsEDDFMEEAKLMMKLSHPKLVQLYGVCTrqkPLYVVTEF 313
gi 83405107  366 INPSELTFMKELGSGLFGVVRLGKWraqYKVAIKAIREGAmsEEDFIEEAKVMMKLTHPKLVQLYGVCTqqrPIYIVTEF 445
gi 126331769 263 IDPSELTFIKELGKGQFGVVHLGKWrshISVAIKAINQGAmsEDDFFEEAKVMTKLSHPRLVQLYGVCIqqkPLYIVTEF 342
gi 158518392 365 INPSELTFMRELGSGLFGVVRLGKWraqYKVAIKAIREGAmcEEDFIEEAKVMMKLTHPKLVQLYGVCTqqkPIYIVTEF 444
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        #  #                                        #   ## #         ##                #
gi 116242835 346 MENGCLLNYLRENkgkLRKEMLLSVCQDICEGMEYLERNGYIHRDLAARNCLVSStCIVKISDFGMTRYVLDDEYVSSFG 425
gi 71896327  446 MEHGCLLNYLRQKrgvLSKDVLLTMCQDVCEGMEYLERNSFIHRDLAARNCLVNDlGVVKVSDFGMTRYVLDDQYTSSSG 525
gi 118090547 314 LENGCLLNYLRQRrgkLSRDMLLGMCLDVCEGMEYLERNNFIHRDLAARNCLVNAeHTVKVSDFGMARYVIDDEYVSSSG 393
gi 83405107  446 MEHGCLLNYLRQRygqFSPDILLSMCQDVCEAMSYLEQSNFIHRDLAARNCLVNDtGVVKVSDFGMTRYVLDDQYTSSCG 525
gi 126331769 343 MENGSLLHFLRQKqgrIGKEMLLSICQDVCEGMEYLERSSFIHRDLAARNCLVSStGIVKISDFGMTRFVLDDEYISSSG 422
gi 158518392 445 MERGCLLNFLRQRqghFSRDVLLSMCQDVCEGMEYLERNSFIHRDLAARNCLVSEaGVVKVSDFGMARYVLDDQYTSSSG 524
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        ####        #                                 #                                 
gi 116242835 426 AKFPIKWSPPEVFLFnKYSSKSDVWSFGVLMWEVFTEGKMPFENKSNLQVVEAISEGFRLYRPHLAPMSIYEVMYSCWHE 505
gi 71896327  526 AKFPVKWCPPEVFNYsRFSSKSDVWSFGVLMWEVFTEGKMPFEKSSNYDVVTMVSQGHRLYRPKLACKQVYEVMMMCWQE 605
gi 118090547 394 AKFPIKWSSPEVFHFkKYSSKSDIWSFGVLMWEVFTEGKMPFESKSNYEVVREISAGNRLYRPHLASHTVYKVMYSCWHE 473
gi 83405107  526 AKFPVKWSPPEVFNYsKFSSKSDVWSFGVLMWEVFTEGKMPFESYSNVEVVEMVTRGDRLYRPKLATKIIYSVMMACWHE 605
gi 126331769 423 AKFPVKWSAPEVFHFnKYSSKSDVWSFGILMWEVFSEGKMPFAKESNLQVMEAISKGFRLYRPQLASMTVYEVMYSCWHE 502
gi 158518392 525 AKFPVKWCPPEVFNYsRFSSKSDVWSFGVLMWEVFTEGRMPFEKYTNYEVVTMVTRGHRLYQPKLASNYVYEVMLRCWQE 604
                        250
                 ....*....|....*.
Feature 1                        
gi 116242835 506 KPEGRPTFAELLRAVT 521
gi 71896327  606 KPEGRPTFEDLLHIII 621
gi 118090547 474 KPEGRPTFAELVETLT 489
gi 83405107  606 KPEGRPKFLDLMKQIG 621
gi 126331769 503 KPKGRPTFAELTQALS 518
gi 158518392 605 KPEGRPSFEDLLRTID 620

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