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Tec homology (TH) adjacent to the PH domain
Author(s) -
Vihinen Mauno,
Nilsson Lennart,
Smith C.I.Edvard
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00783-7
Subject(s) - pleckstrin homology domain , bruton's tyrosine kinase , sh3 domain , homology (biology) , gtpase , biochemistry , biology , protein subunit , grb2 , peptide sequence , chemistry , kinase , microbiology and biotechnology , amino acid , signal transduction , proto oncogene tyrosine protein kinase src , gene , tyrosine kinase
The pleckstrin homology (PH) domain is extended in the Btk kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain. The TH domain contains a conserved 27 amino acid stretch designated the Btk motif and a proline‐rich region. Sequence similarity was found to a putative Ras GTPase activating protein and a human interferon‐γ binding protein both in the PH domain and the Btk motif region. SLK1/SSP31 protein kinase and a non‐catalytic p85 subunit of PI‐3 kinase had similarity only with the proline rich region. The identification of a PH domain extension in some signal transduction proteins in different species suggests that this region is involved in protein—protein interactions.