DNA-binding protein inhibitor ID-3 is a
protein that in humans is encoded by the ID3gene.[5][6]
Function
Members of the ID family of helix-loop-helix (HLH) proteins lack a basic DNA-binding domain and inhibit transcription through formation of nonfunctional dimers that are incapable of binding to DNA.[supplied by OMIM][6]
BTG2 binds to the promoter of Id3 and represses its activity. By this mechanism, the upregulation of Id3 in the hippocampus caused by BTG2 ablation prevents terminal differentiation of hippocampal neurons.[9]
Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (1994). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50.
doi:
10.1016/0378-1119(94)90433-2.
PMID7821789.
Deed RW, Hirose T, Mitchell EL, Santibanez-Koref MF, Norton JD (1994). "Structural organisation and chromosomal mapping of the human Id-3 gene". Gene. 151 (1–2): 309–14.
doi:
10.1016/0378-1119(94)90676-9.
PMID7828896.
Deed RW, Bianchi SM, Atherton GT, Johnston D, Santibanez-Koref M, Murphy JJ, Norton JD (1993). "An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types". Oncogene. 8 (3): 599–607.
PMID8437843.
Ishiguro A, Spirin K, Shiohara M, Tobler A, Norton JD, Rigolet M, Shimbo T, Koeffler HP (1995). "Expression of Id2 and Id3 mRNA in human lymphocytes". Leuk. Res. 19 (12): 989–96.
doi:
10.1016/0145-2126(95)00084-4.
PMID8632670.
Wibley J, Deed R, Jasiok M, Douglas K, Norton J (1996). "A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions". Biochim. Biophys. Acta. 1294 (2): 138–46.
doi:
10.1016/0167-4838(96)00008-8.
PMID8645731.
Deed RW, Jasiok M, Norton JD (1996). "Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism". FEBS Lett. 393 (1): 113–6.
doi:
10.1016/0014-5793(96)00868-X.
PMID8804437.
S2CID27733563.
DNA-binding protein inhibitor ID-3 is a
protein that in humans is encoded by the ID3gene.[5][6]
Function
Members of the ID family of helix-loop-helix (HLH) proteins lack a basic DNA-binding domain and inhibit transcription through formation of nonfunctional dimers that are incapable of binding to DNA.[supplied by OMIM][6]
BTG2 binds to the promoter of Id3 and represses its activity. By this mechanism, the upregulation of Id3 in the hippocampus caused by BTG2 ablation prevents terminal differentiation of hippocampal neurons.[9]
Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (1994). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50.
doi:
10.1016/0378-1119(94)90433-2.
PMID7821789.
Deed RW, Hirose T, Mitchell EL, Santibanez-Koref MF, Norton JD (1994). "Structural organisation and chromosomal mapping of the human Id-3 gene". Gene. 151 (1–2): 309–14.
doi:
10.1016/0378-1119(94)90676-9.
PMID7828896.
Deed RW, Bianchi SM, Atherton GT, Johnston D, Santibanez-Koref M, Murphy JJ, Norton JD (1993). "An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types". Oncogene. 8 (3): 599–607.
PMID8437843.
Ishiguro A, Spirin K, Shiohara M, Tobler A, Norton JD, Rigolet M, Shimbo T, Koeffler HP (1995). "Expression of Id2 and Id3 mRNA in human lymphocytes". Leuk. Res. 19 (12): 989–96.
doi:
10.1016/0145-2126(95)00084-4.
PMID8632670.
Wibley J, Deed R, Jasiok M, Douglas K, Norton J (1996). "A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions". Biochim. Biophys. Acta. 1294 (2): 138–46.
doi:
10.1016/0167-4838(96)00008-8.
PMID8645731.
Deed RW, Jasiok M, Norton JD (1996). "Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism". FEBS Lett. 393 (1): 113–6.
doi:
10.1016/0014-5793(96)00868-X.
PMID8804437.
S2CID27733563.