Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins.
| dc.contributor.author | Deed, Richard W | |
| dc.contributor.author | Jasiok, Michelle | |
| dc.contributor.author | Norton, John D | |
| dc.date.accessioned | 2010-04-09T10:38:35Z | |
| dc.date.available | 2010-04-09T10:38:35Z | |
| dc.date.issued | 1994-09-13 | |
| dc.identifier.citation | Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins. 1994, 1219 (1):160-2 Biochim. Biophys. Acta | en |
| dc.identifier.issn | 0006-3002 | |
| dc.identifier.pmid | 8086456 | |
| dc.identifier.uri | http://hdl.handle.net/10541/96090 | |
| dc.description.abstract | We have determined the cDNA sequence encoding a 154 amino acid human Id-1 helix-loop-helix protein. Comparison with the amino acid sequences of human and mouse Id-2 and Id-3 proteins, reveals conservation/divergence of several residues in the helix-loop-helix domain known to be important for heterodimerisation, together with a common casein kinase II phosphorylation site. | |
| dc.language.iso | en | en |
| dc.subject.mesh | Amino Acid Sequence | |
| dc.subject.mesh | Base Sequence | |
| dc.subject.mesh | Casein Kinase II | |
| dc.subject.mesh | Conserved Sequence | |
| dc.subject.mesh | DNA, Complementary | |
| dc.subject.mesh | DNA-Binding Proteins | |
| dc.subject.mesh | Helix-Loop-Helix Motifs | |
| dc.subject.mesh | Humans | |
| dc.subject.mesh | Inhibitor of Differentiation Protein 1 | |
| dc.subject.mesh | Molecular Sequence Data | |
| dc.subject.mesh | Phosphorylation | |
| dc.subject.mesh | Protein-Serine-Threonine Kinases | |
| dc.subject.mesh | Repressor Proteins | |
| dc.subject.mesh | Sequence Homology, Amino Acid | |
| dc.subject.mesh | Transcription Factors | |
| dc.title | Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins. | en |
| dc.type | Article | en |
| dc.contributor.department | CRC Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester, UK. | en |
| dc.identifier.journal | Biochimica et Biophysica Acta | en |
| html.description.abstract | We have determined the cDNA sequence encoding a 154 amino acid human Id-1 helix-loop-helix protein. Comparison with the amino acid sequences of human and mouse Id-2 and Id-3 proteins, reveals conservation/divergence of several residues in the helix-loop-helix domain known to be important for heterodimerisation, together with a common casein kinase II phosphorylation site. |