| alternative products:The splicing pattern is cell-lineage dependent,disease:A chromosomal aberration involving TAL1 may be a cause of some T-cell acute lymphoblastic leukemias (T-ALL). Translocation t(1,14)(p32,q11) with T-cell receptor alpha chain (TCRA) genes.,domain:The helix-loop-helix domain is necessary and sufficient for the interaction with DRG1.,function:Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation.,PTM:Phosphorylated on serine residues. Phosphorylation of Ser-122 is strongly stimulated by hypoxia.,PTM:Ubiquitinated, subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system. This process may be characteristic for microvascular endothelial cells, since it could not be observed in large vessel endothelial cells.,similarity:Contains 1 basic helix-loop-helix (bHLH) domain.,subunit:Efficient DNA binding requires dimerization with another bHLH protein. Forms heterodimers with TCF3. Binds to the LIM domain containing protein LMO2 and to DRG1. Can assemble in a complex with LDB1 and LMO2. Component of a TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.,tissue specificity:Leukemic stem cell.,alternative products:The splicing pattern is cell-lineage dependent,disease:A chromosomal aberration involving TAL1 may be a cause of some T-cell acute lymphoblastic leukemias (T-ALL). Translocation t(1,14)(p32,q11) with T-cell receptor alpha chain (TCRA) genes.,domain:The helix-loop-helix domain is necessary and sufficient for the interaction with DRG1.,function:Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation.,PTM:Phosphorylated on serine residues. Phosphorylation of Ser-122 is strongly stimulated by hypoxia.,PTM:Ubiquitinated, subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system. This process may be characteristic for microvascular endothelial cells, since it could not be observed in large vessel endothelial cells.,similarity:Contains 1 basic helix-loop-helix (bHLH) domain.,subunit:Efficient DNA binding requires dimerization with another bHLH protein. Forms heterodimers with TCF3. Binds to the LIM domain containing protein LMO2 and to DRG1. Can assemble in a complex with LDB1 and LMO2. Component of a TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.,tissue specificity:Leukemic stem cell., |
