Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins.

2.50
Hdl Handle:
http://hdl.handle.net/10541/96090
Title:
Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins.
Authors:
Deed, Richard W; Jasiok, Michelle; Norton, John D
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.
Affiliation:
CRC Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester, UK.
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
Journal:
Biochimica et Biophysica Acta
Issue Date:
13-Sep-1994
URI:
http://hdl.handle.net/10541/96090
PubMed ID:
8086456
Type:
Article
Language:
en
ISSN:
0006-3002
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorDeed, Richard Wen
dc.contributor.authorJasiok, Michelleen
dc.contributor.authorNorton, John Den
dc.date.accessioned2010-04-09T10:38:35Z-
dc.date.available2010-04-09T10:38:35Z-
dc.date.issued1994-09-13-
dc.identifier.citationNucleotide 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. Actaen
dc.identifier.issn0006-3002-
dc.identifier.pmid8086456-
dc.identifier.urihttp://hdl.handle.net/10541/96090-
dc.description.abstractWe 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.en
dc.language.isoenen
dc.subject.meshAmino Acid Sequence-
dc.subject.meshBase Sequence-
dc.subject.meshCasein Kinase II-
dc.subject.meshConserved Sequence-
dc.subject.meshDNA, Complementary-
dc.subject.meshDNA-Binding Proteins-
dc.subject.meshHelix-Loop-Helix Motifs-
dc.subject.meshHumans-
dc.subject.meshInhibitor of Differentiation Protein 1-
dc.subject.meshMolecular Sequence Data-
dc.subject.meshPhosphorylation-
dc.subject.meshProtein-Serine-Threonine Kinases-
dc.subject.meshRepressor Proteins-
dc.subject.meshSequence Homology, Amino Acid-
dc.subject.meshTranscription Factors-
dc.titleNucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins.en
dc.typeArticleen
dc.contributor.departmentCRC Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester, UK.en
dc.identifier.journalBiochimica et Biophysica Actaen

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