TEC HOMOLOGY (TH) ADJACENT TO THE PH DOMAIN
(1994) In FEBS Letters 350(2-3). p.263-265- Abstract
- The pleckstrin homology (PH) domain is extended in the Btk kinase family by a region designated the TH (Tee 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 Pas GTPase activating protein and a human interferon-gamma 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... (More)
- The pleckstrin homology (PH) domain is extended in the Btk kinase family by a region designated the TH (Tee 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 Pas GTPase activating protein and a human interferon-gamma 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3853371
- author
- Vihinen, Mauno LU ; NILSSON, L and SMITH, CIE
- publishing date
- 1994
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- CYTOPLASMIC TYROSINE KINASE, SIGNAL TRANSDUCTION, BTK, BRUTONS AGAMMAGLOBULINEMIA TYROSINE KINASE, XLA, X-LINKED AGAMMAGLOBULINEMIA
- in
- FEBS Letters
- volume
- 350
- issue
- 2-3
- pages
- 263 - 265
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:A1994PD82000026
- scopus:0027941128
- ISSN
- 1873-3468
- DOI
- 10.1016/0014-5793(94)00783-7
- language
- English
- LU publication?
- no
- id
- 99651cf6-330b-4962-bb7b-7b5e1615740f (old id 3853371)
- date added to LUP
- 2016-04-01 15:45:04
- date last changed
- 2021-01-03 04:03:10
@article{99651cf6-330b-4962-bb7b-7b5e1615740f, abstract = {{The pleckstrin homology (PH) domain is extended in the Btk kinase family by a region designated the TH (Tee 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 Pas GTPase activating protein and a human interferon-gamma 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.}}, author = {{Vihinen, Mauno and NILSSON, L and SMITH, CIE}}, issn = {{1873-3468}}, keywords = {{CYTOPLASMIC TYROSINE KINASE; SIGNAL TRANSDUCTION; BTK; BRUTONS AGAMMAGLOBULINEMIA TYROSINE KINASE; XLA; X-LINKED AGAMMAGLOBULINEMIA}}, language = {{eng}}, number = {{2-3}}, pages = {{263--265}}, publisher = {{Wiley-Blackwell}}, series = {{FEBS Letters}}, title = {{TEC HOMOLOGY (TH) ADJACENT TO THE PH DOMAIN}}, url = {{http://dx.doi.org/10.1016/0014-5793(94)00783-7}}, doi = {{10.1016/0014-5793(94)00783-7}}, volume = {{350}}, year = {{1994}}, }