Gene Section Review Atlas Genet Cytogenet Oncol Haematol. 2012; 16(8) 559 INIST-CNRS OPEN ACCESS JOURNAL Atlas of Genetics and Cytogenetics in Oncology and Haematology TIE1 (tyrosine kinase with immunoglobulin-like and EGF-like domains 1) Pipsa Saharinen Molecular Cancer Biology Program, Research Programs Unit, Biomedicum Helsinki, Haartmaninkatu 8, P O B 63, FIN-00014 University of Helsinki, Finland (PS) Published in Atlas Database: March 2012 Online updated version : http://AtlasGeneticsOncology.org/Genes/TIE1ID42560ch1p34.html DOI: 10.4267/2042/47491 This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 France Licence. © 2012 Atlas of Genetics and Cytogenetics in Oncology and Haematology Identity Other names: JTK14, TIE HGNC (Hugo): TIE1 Location: 1p34.2 Note Receptor tyrosine kinase, member of the TIE family (other member: TIE2/TEK). Highly conserved sequence across vertebrate species, with greatest amino acid homology occurring in the kinase domain. DNA/RNA Description The human TIE1 gene spans 22115 bp, encoding for 23 exons in forward strand. Transcription Longest mRNA contains 3882 bp. Alternatively spliced forms have been reported, including transcript variant 5 (EU826590.1) coding for a soluble TIE1 ectodomain (Jin et al., 2008). The genomic (top) and the protein domain structures (below) of human TIE1. Black boxes represent exons with intervening intron sequences (lines), light gray boxes represent non-coding sequences of first and last exons. Exon length (black text) and intron length of the longest introns (pink) are indicated in nucleotides. The protein domain coding regions of exons are indicated with colours according to the TIE1 protein domain structure. SS= signal sequence, Ig= immunoglobulin-like domain, EGF= epidermal growth factor-like domain, FN3= fibronectin type-III domain, TM= transmembrane domain, TK= tyrosine kinase domain. Protein domain prediction was performed using (SMART). The crystal structure for Tie2 shows the existence of a third Ig-like domain, immediately after the SS (Barton et al., 2006), and homology modeling of Tie1 predicts a similar fold (Seegar et al., 2010).