PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16540119-0 2006 Oligomerisation of the developmental regulator proline rich homeodomain (PRH/Hex) is mediated by a novel proline-rich dimerisation domain. Proline 47-54 hematopoietically expressed homeobox Homo sapiens 73-76 18713067-1 2009 The PRH (proline-rich homeodomain) [also known as Hex (haematopoietically expressed homeobox)] protein is a transcription factor that functions as an important regulator of vertebrate development and many other processes in the adult including haematopoiesis. Proline 9-16 hematopoietically expressed homeobox Homo sapiens 50-53 18713067-1 2009 The PRH (proline-rich homeodomain) [also known as Hex (haematopoietically expressed homeobox)] protein is a transcription factor that functions as an important regulator of vertebrate development and many other processes in the adult including haematopoiesis. Proline 9-16 hematopoietically expressed homeobox Homo sapiens 84-92 18498250-1 2008 The PRH (proline-rich homeodomain) [also known as Hex (haematopoietically expressed homeobox)] protein is a critical regulator of vertebrate development. Proline 9-16 hematopoietically expressed homeobox Homo sapiens 50-53 18498250-1 2008 The PRH (proline-rich homeodomain) [also known as Hex (haematopoietically expressed homeobox)] protein is a critical regulator of vertebrate development. Proline 9-16 hematopoietically expressed homeobox Homo sapiens 84-92 16540119-0 2006 Oligomerisation of the developmental regulator proline rich homeodomain (PRH/Hex) is mediated by a novel proline-rich dimerisation domain. Proline 47-54 hematopoietically expressed homeobox Homo sapiens 77-80 16540119-0 2006 Oligomerisation of the developmental regulator proline rich homeodomain (PRH/Hex) is mediated by a novel proline-rich dimerisation domain. Proline 105-112 hematopoietically expressed homeobox Homo sapiens 73-76 16540119-0 2006 Oligomerisation of the developmental regulator proline rich homeodomain (PRH/Hex) is mediated by a novel proline-rich dimerisation domain. Proline 105-112 hematopoietically expressed homeobox Homo sapiens 77-80 16540119-8 2006 We show that this region of PRH contains a novel proline-rich dimerisation domain that mediates oligomerisation. Proline 49-56 hematopoietically expressed homeobox Homo sapiens 28-31 15187083-3 2004 The PRH homeodomain represses transcription by binding to TATA box sequences, whereas the proline-rich N-terminal domain of PRH can repress transcription when attached to a heterologous DNA-binding domain. Proline 90-97 hematopoietically expressed homeobox Homo sapiens 124-127 15657436-8 2005 At the biochemical level, HOXA9 mediates these effects by competing with factors that repress eIF4E function, in particular the proline-rich homeodomain PRH/Hex. Proline 128-135 hematopoietically expressed homeobox Homo sapiens 153-156 15657436-8 2005 At the biochemical level, HOXA9 mediates these effects by competing with factors that repress eIF4E function, in particular the proline-rich homeodomain PRH/Hex. Proline 128-135 hematopoietically expressed homeobox Homo sapiens 157-160 15187083-5 2004 Here we demonstrate that the proline-rich N-terminal domain of PRH binds to TLE1 in vitro and in yeast two-hybrid assays. Proline 29-36 hematopoietically expressed homeobox Homo sapiens 63-66 12650996-2 2003 The PRH protein contains a proline-rich N-terminal domain that can repress transcription when attached to a heterologous DNA binding domain, a central homeodomain that mediates sequence-specific DNA binding, and an acidic C-terminal domain of unknown function. Proline 27-34 hematopoietically expressed homeobox Homo sapiens 4-7 14645512-8 2003 The aberrant nuclear function of eIF4E is due to abnormally large eIF4E bodies and the loss of regulation by the proline-rich homeodomain PRH. Proline 113-120 hematopoietically expressed homeobox Homo sapiens 138-141 12826010-2 2003 We have shown previously that PRH contains two domains that can bring about transcriptional repression independently; the PRH homeodomain represses transcription by binding to TATA box sequences, whereas the proline-rich N-terminal domain can repress transcription by interacting with members of the Groucho/TLE (transducin-like enhancer of split) family of co-repressor proteins. Proline 208-215 hematopoietically expressed homeobox Homo sapiens 30-33 12826010-6 2003 Moreover, we show that PRH is associated with the proteasome in haematopoietic cells and that the proline-rich PRH N-terminal domain is responsible for this interaction. Proline 98-105 hematopoietically expressed homeobox Homo sapiens 23-26 12826010-6 2003 Moreover, we show that PRH is associated with the proteasome in haematopoietic cells and that the proline-rich PRH N-terminal domain is responsible for this interaction. Proline 98-105 hematopoietically expressed homeobox Homo sapiens 111-114 10597310-5 1999 Using yeast 2-hybrid techniques, we found that PML and a related RING protein, Z, bind the proline rich homeodomain protein (PRH) through their RING domains. Proline 91-98 hematopoietically expressed homeobox Homo sapiens 125-128 12554669-3 2003 Surprisingly, we found that a trans cription factor, the proline-rich homeodomain protein PRH, is a negative regulator of eIF4E in myeloid cells, interacting with eIF4E through a conserved binding site typically found in translational regulators. Proline 57-64 hematopoietically expressed homeobox Homo sapiens 90-93 11054411-7 2001 PRH also contains an N-terminal proline-rich repression domain that is separate from the homeodomain. Proline 32-39 hematopoietically expressed homeobox Homo sapiens 0-3 9660787-7 1998 A second series of daughter ions showed that Pro-143 was hydroxylated and derivatized with a potentially linear pentasaccharide, Hex-->Hex-->Fuc-->Hex-->HexNAc-->(HyPro). Proline 45-48 hematopoietically expressed homeobox Homo sapiens 129-132 9660787-7 1998 A second series of daughter ions showed that Pro-143 was hydroxylated and derivatized with a potentially linear pentasaccharide, Hex-->Hex-->Fuc-->Hex-->HexNAc-->(HyPro). Proline 45-48 hematopoietically expressed homeobox Homo sapiens 138-141 9660787-7 1998 A second series of daughter ions showed that Pro-143 was hydroxylated and derivatized with a potentially linear pentasaccharide, Hex-->Hex-->Fuc-->Hex-->HexNAc-->(HyPro). Proline 45-48 hematopoietically expressed homeobox Homo sapiens 138-141 7911091-0 1994 A homology-based molecular model of the proline-rich homeodomain protein Prh, from haematopoietic cells. Proline 40-47 hematopoietically expressed homeobox Homo sapiens 73-76 20675722-2 2010 We have shown previously that the Proline-Rich Homeodomain protein (PRH/Hex) self-assembles to form oligomeric complexes that bind to arrays of PRH binding sites with high affinity and specificity. Proline 34-41 hematopoietically expressed homeobox Homo sapiens 68-71 28604763-2 2017 PRH/HHEX (proline-rich homeodomain/haematopoietically expressed homeobox) is a transcription factor that displays both tumour suppressor and oncogenic activity in different disease contexts; however, the role of PRH in breast cancer is poorly understood. Proline 10-17 hematopoietically expressed homeobox Homo sapiens 0-3 28604763-2 2017 PRH/HHEX (proline-rich homeodomain/haematopoietically expressed homeobox) is a transcription factor that displays both tumour suppressor and oncogenic activity in different disease contexts; however, the role of PRH in breast cancer is poorly understood. Proline 10-17 hematopoietically expressed homeobox Homo sapiens 4-8 28604763-2 2017 PRH/HHEX (proline-rich homeodomain/haematopoietically expressed homeobox) is a transcription factor that displays both tumour suppressor and oncogenic activity in different disease contexts; however, the role of PRH in breast cancer is poorly understood. Proline 10-17 hematopoietically expressed homeobox Homo sapiens 212-215 28134934-1 2017 PRH/HHEX (proline-rich homeodomain protein/haematopoietically expressed homeobox protein) is a transcription factor that controls cell proliferation, cell differentiation and cell migration. Proline 10-17 hematopoietically expressed homeobox Homo sapiens 0-3 28134934-1 2017 PRH/HHEX (proline-rich homeodomain protein/haematopoietically expressed homeobox protein) is a transcription factor that controls cell proliferation, cell differentiation and cell migration. Proline 10-17 hematopoietically expressed homeobox Homo sapiens 4-8 26877867-0 2016 Misregulation of the proline rich homeodomain (PRH/HHEX) protein in cancer cells and its consequences for tumour growth and invasion. Proline 21-28 hematopoietically expressed homeobox Homo sapiens 47-50 26877867-0 2016 Misregulation of the proline rich homeodomain (PRH/HHEX) protein in cancer cells and its consequences for tumour growth and invasion. Proline 21-28 hematopoietically expressed homeobox Homo sapiens 51-55 22540015-0 2012 The proline rich homeodomain protein PRH/Hhex forms stable oligomers that are highly resistant to denaturation. Proline 4-11 hematopoietically expressed homeobox Homo sapiens 37-40 22540015-0 2012 The proline rich homeodomain protein PRH/Hhex forms stable oligomers that are highly resistant to denaturation. Proline 4-11 hematopoietically expressed homeobox Homo sapiens 41-45 22540015-4 2012 PRINCIPAL FINDINGS: Here we show that the proline rich homeodomain protein PRH/Hhex forms predominantly octameric and/or hexadecameric species in solution as well as larger assemblies. Proline 42-49 hematopoietically expressed homeobox Homo sapiens 75-78 22540015-4 2012 PRINCIPAL FINDINGS: Here we show that the proline rich homeodomain protein PRH/Hhex forms predominantly octameric and/or hexadecameric species in solution as well as larger assemblies. Proline 42-49 hematopoietically expressed homeobox Homo sapiens 79-83 20675722-2 2010 We have shown previously that the Proline-Rich Homeodomain protein (PRH/Hex) self-assembles to form oligomeric complexes that bind to arrays of PRH binding sites with high affinity and specificity. Proline 34-41 hematopoietically expressed homeobox Homo sapiens 72-75 20675722-2 2010 We have shown previously that the Proline-Rich Homeodomain protein (PRH/Hex) self-assembles to form oligomeric complexes that bind to arrays of PRH binding sites with high affinity and specificity. Proline 34-41 hematopoietically expressed homeobox Homo sapiens 144-147