ID3 (gene): Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''DNA-binding protein inhibitor ID-3''' is a [[protein]] that in humans is encoded by the ''ID3'' [[gene]].<ref name="pmid1628620">{{cite journal | vauthors = Ellmeier W, Aguzzi A, Kleiner E, Kurzbauer R, Weith A | title = Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development | journal = EMBO J. | volume = 11 | issue = 7 | pages = 2563–71  | date = Aug 1992 | pmid = 1628620 | pmc = 556731 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3399| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein
| HGNCid = 5362
| Symbol = ID3
| AltSymbols =; HEIR-1
| OMIM = 600277
| ECnumber = 
| Homologene = 1633
| MGIid = 96398
| GeneAtlas_image1 = PBB_GE_ID3_207826_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0019904 |text = protein domain specific binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0030855 |text = epithelial cell differentiation}} {{GNF_GO|id=GO:0043433 |text = negative regulation of transcription factor activity}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3399
    | Hs_Ensembl = ENSG00000117318
    | Hs_RefseqProtein = NP_002158
    | Hs_RefseqmRNA = NM_002167
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 23756996
    | Hs_GenLoc_end = 23758872
    | Hs_Uniprot = Q02535
    | Mm_EntrezGene = 15903
    | Mm_Ensembl = ENSMUSG00000007872
    | Mm_RefseqmRNA = NM_008321
    | Mm_RefseqProtein = NP_032347
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 135415900
    | Mm_GenLoc_end = 135417466
    | Mm_Uniprot = Q545W1
  }}
}}
'''Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein''', also known as '''ID3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3399| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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]<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3399| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
ID3 (gene) has been shown to [[Protein-protein interaction|interact]] with [[TCF3]].<ref name=pmid9525934>{{cite journal | vauthors = Deed RW, Jasiok M, Norton JD | title = Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells | journal = J. Biol. Chem. | volume = 273 | issue = 14 | pages = 8278–86  | date = Apr 1998 | pmid = 9525934 | doi = 10.1074/jbc.273.14.8278 }}</ref><ref name=pmid9242638>{{cite journal | vauthors = Langlands K, Yin X, Anand G, Prochownik EV | title = Differential interactions of Id proteins with basic-helix-loop-helix transcription factors | journal = J. Biol. Chem. | volume = 272 | issue = 32 | pages = 19785–93  | date = Aug 1997 | pmid = 9242638 | doi = 10.1074/jbc.272.32.19785 }}</ref>
 
== Repressors of ID3 ==
 
[[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.<ref name="pmid20020054">{{cite journal | vauthors = Farioli-Vecchioli S, Saraulli D, Costanzi M, Leonardi L, Cinà I, Micheli L, Nutini M, Longone P, Oh SP, Cestari V, Tirone F | title = Impaired terminal differentiation of hippocampal granule neurons and defective contextual memory in PC3/Tis21 knockout mice | journal = PLoS ONE | volume = 4 | issue = 12 | pages = e8339 | year = 2009 | pmid = 20020054 | pmc = 2791842 | doi = 10.1371/journal.pone.0008339 | editor1-last = Okazawa | editor1-first = Hitoshi }}</ref>
 
== See also ==
* [[Inhibitor of DNA-binding protein]]
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = White PS, Maris JM, Beltinger C, Sulman E, Marshall HN, Fujimori M, Kaufman BA, Biegel JA, Allen C, Hilliard C, Valentine MB, Look AT, Enomoto H, Sakiyama S, Brodeur GM | title = A region of consistent deletion in neuroblastoma maps within human chromosome 1p36.2-36.3 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 12 | pages = 5520–4 | year = 1995 | pmid = 7777541 | pmc = 41727 | doi = 10.1073/pnas.92.12.5520 }}
| citations =
* {{cite journal | vauthors = Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T | title = Construction of a human full-length cDNA bank | journal = Gene | volume = 150 | issue = 2 | pages = 243–50 | year = 1994 | pmid = 7821789 | doi = 10.1016/0378-1119(94)90433-2 }}
*{{cite journal | author=Ellmeier W, Aguzzi A, Kleiner E, ''et al.'' |title=Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development. |journal=EMBO J. |volume=11 |issue= 7 |pages= 2563-71 |year= 1992 |pmid= 1628620 |doi= }}
* {{cite journal | vauthors = Deed RW, Hirose T, Mitchell EL, Santibanez-Koref MF, Norton JD | title = Structural organisation and chromosomal mapping of the human Id-3 gene | journal = Gene | volume = 151 | issue = 1–2 | pages = 309–14 | year = 1994 | pmid = 7828896 | doi = 10.1016/0378-1119(94)90676-9 }}
*{{cite journal | author=White PS, Maris JM, Beltinger C, ''et al.'' |title=A region of consistent deletion in neuroblastoma maps within human chromosome 1p36.2-36.3. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 12 |pages= 5520-4 |year= 1995 |pmid= 7777541 |doi= }}
* {{cite journal | vauthors = Deed RW, Bianchi SM, Atherton GT, Johnston D, Santibanez-Koref M, Murphy JJ, Norton JD | title = 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 | journal = Oncogene | volume = 8 | issue = 3 | pages = 599–607 | year = 1993 | pmid = 8437843 | doi =  }}
*{{cite journal | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi= }}
* {{cite journal | vauthors = Ishiguro A, Spirin K, Shiohara M, Tobler A, Norton JD, Rigolet M, Shimbo T, Koeffler HP | title = Expression of Id2 and Id3 mRNA in human lymphocytes | journal = Leuk. Res. | volume = 19 | issue = 12 | pages = 989–96 | year = 1995 | pmid = 8632670 | doi = 10.1016/0145-2126(95)00084-4 }}
*{{cite journal | author=Deed RW, Hirose T, Mitchell EL, ''et al.'' |title=Structural organisation and chromosomal mapping of the human Id-3 gene. |journal=Gene |volume=151 |issue= 1-2 |pages= 309-14 |year= 1995 |pmid= 7828896 |doi=  }}
* {{cite journal | vauthors = Wibley J, Deed R, Jasiok M, Douglas K, Norton J | title = A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions | journal = Biochim. Biophys. Acta | volume = 1294 | issue = 2 | pages = 138–46 | year = 1996 | pmid = 8645731 | doi = 10.1016/0167-4838(96)00008-8 }}
*{{cite journal | author=Deed RW, Bianchi SM, Atherton GT, ''et al.'' |title=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. |journal=Oncogene |volume=8 |issue= 3 |pages= 599-607 |year= 1993 |pmid= 8437843 |doi= }}
* {{cite journal | vauthors = Loveys DA, Streiff MB, Kato GJ | title = E2A basic-helix-loop-helix transcription factors are negatively regulated by serum growth factors and by the Id3 protein | journal = Nucleic Acids Res. | volume = 24 | issue = 14 | pages = 2813–20 | year = 1996 | pmid = 8759016 | pmc = 145994 | doi = 10.1093/nar/24.14.2813 }}
*{{cite journal | author=Ishiguro A, Spirin K, Shiohara M, ''et al.'' |title=Expression of Id2 and Id3 mRNA in human lymphocytes. |journal=Leuk. Res. |volume=19 |issue= 12 |pages= 989-96 |year= 1996 |pmid= 8632670 |doi= }}
* {{cite journal | vauthors = Deed RW, Armitage S, Norton JD | title = Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism | journal = J. Biol. Chem. | volume = 271 | issue = 39 | pages = 23603–6 | year = 1996 | pmid = 8798572 | doi = 10.1074/jbc.271.39.23603 }}
*{{cite journal | author=Wibley J, Deed R, Jasiok M, ''et al.'' |title=A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions. |journal=Biochim. Biophys. Acta |volume=1294 |issue= 2 |pages= 138-46 |year= 1996 |pmid= 8645731 |doi= }}
* {{cite journal | vauthors = Deed RW, Jasiok M, Norton JD | title = Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism | journal = FEBS Lett. | volume = 393 | issue = 1 | pages = 113–6 | year = 1996 | pmid = 8804437 | doi = 10.1016/0014-5793(96)00868-X }}
*{{cite journal | author=Loveys DA, Streiff MB, Kato GJ |title=E2A basic-helix-loop-helix transcription factors are negatively regulated by serum growth factors and by the Id3 protein. |journal=Nucleic Acids Res. |volume=24 |issue= 14 |pages= 2813-20 |year= 1996 |pmid= 8759016 |doi= }}
* {{cite journal | vauthors = Chen B, Lim RW | title = Physical and functional interactions between the transcriptional inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism regulating muscle-specific gene expression | journal = J. Biol. Chem. | volume = 272 | issue = 4 | pages = 2459–63 | year = 1997 | pmid = 8999959 | doi = 10.1074/jbc.272.4.2459 }}
*{{cite journal | author=Deed RW, Armitage S, Norton JD |title=Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism. |journal=J. Biol. Chem. |volume=271 |issue= 39 |pages= 23603-6 |year= 1996 |pmid= 8798572 |doi= }}
* {{cite journal | vauthors = Langlands K, Yin X, Anand G, Prochownik EV | title = Differential interactions of Id proteins with basic-helix-loop-helix transcription factors | journal = J. Biol. Chem. | volume = 272 | issue = 32 | pages = 19785–93 | year = 1997 | pmid = 9242638 | doi = 10.1074/jbc.272.32.19785 }}
*{{cite journal | author=Deed RW, Jasiok M, Norton JD |title=Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism. |journal=FEBS Lett. |volume=393 |issue= 1 |pages= 113-6 |year= 1996 |pmid= 8804437 |doi= }}
* {{cite journal | vauthors = Deed RW, Hara E, Atherton GT, Peters G, Norton JD | title = Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation | journal = Mol. Cell. Biol. | volume = 17 | issue = 12 | pages = 6815–21 | year = 1997 | pmid = 9372912 | pmc = 232537 | doi =  }}
*{{cite journal | author=Chen B, Lim RW |title=Physical and functional interactions between the transcriptional inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism regulating muscle-specific gene expression. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2459-63 |year= 1997 |pmid= 8999959 |doi= }}
* {{cite journal | vauthors = Deed RW, Jasiok M, Norton JD | title = Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells | journal = J. Biol. Chem. | volume = 273 | issue = 14 | pages = 8278–86 | year = 1998 | pmid = 9525934 | doi = 10.1074/jbc.273.14.8278 }}
*{{cite journal | author=Langlands K, Yin X, Anand G, Prochownik EV |title=Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. |journal=J. Biol. Chem. |volume=272 |issue= 32 |pages= 19785-93 |year= 1997 |pmid= 9242638 |doi=  }}
* {{cite journal | vauthors = Asp J, Thornemo M, Inerot S, Lindahl A | title = The helix-loop-helix transcription factors Id1 and Id3 have a functional role in control of cell division in human normal and neoplastic chondrocytes | journal = FEBS Lett. | volume = 438 | issue = 1–2 | pages = 85–90 | year = 1998 | pmid = 9821964 | doi = 10.1016/S0014-5793(98)01268-X }}
*{{cite journal | author=Deed RW, Hara E, Atherton GT, ''et al.'' |title=Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 6815-21 |year= 1997 |pmid= 9372912 |doi= }}
* {{cite journal | vauthors = Yates PR, Atherton GT, Deed RW, Norton JD, Sharrocks AD | title = Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors | journal = EMBO J. | volume = 18 | issue = 4 | pages = 968–76 | year = 1999 | pmid = 10022839 | pmc = 1171189 | doi = 10.1093/emboj/18.4.968 }}
*{{cite journal | author=Deed RW, Jasiok M, Norton JD |title=Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells. |journal=J. Biol. Chem. |volume=273 |issue= 14 |pages= 8278-86 |year= 1998 |pmid= 9525934 |doi= }}
* {{cite journal | vauthors = Moldes M, Boizard M, Liepvre XL, Fève B, Dugail I, Pairault J | title = Functional antagonism between inhibitor of DNA binding (Id) and adipocyte determination and differentiation factor 1/sterol regulatory element-binding protein-1c (ADD1/SREBP-1c) trans-factors for the regulation of fatty acid synthase promoter in adipocytes | journal = Biochem. J. | volume = 344 Pt 3 | issue = 3| pages = 873–80 | year = 1999 | pmid = 10585876 | pmc = 1220711 | doi = 10.1042/0264-6021:3440873 | series = 344 }}
*{{cite journal | author=Asp J, Thornemo M, Inerot S, Lindahl A |title=The helix-loop-helix transcription factors Id1 and Id3 have a functional role in control of cell division in human normal and neoplastic chondrocytes. |journal=FEBS Lett. |volume=438 |issue= 1-2 |pages= 85-90 |year= 1998 |pmid= 9821964 |doi= }}
* {{cite journal | vauthors = Bounpheng MA, Dimas JJ, Dodds SG, Christy BA | title = Degradation of Id proteins by the ubiquitin-proteasome pathway | journal = FASEB J. | volume = 13 | issue = 15 | pages = 2257–64 | year = 1999 | pmid = 10593873 | doi =  }}
*{{cite journal | author=Yates PR, Atherton GT, Deed RW, ''et al.'' |title=Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors. |journal=EMBO J. |volume=18 |issue= 4 |pages= 968-76 |year= 1999 |pmid= 10022839 |doi= 10.1093/emboj/18.4.968 }}
* {{cite journal | vauthors = Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y | title = Protein-protein interaction panel using mouse full-length cDNAs | journal = Genome Res. | volume = 11 | issue = 10 | pages = 1758–65 | year = 2001 | pmid = 11591653 | pmc = 311163 | doi = 10.1101/gr.180101 }}
*{{cite journal | author=Moldes M, Boizard M, Liepvre XL, ''et al.'' |title=Functional antagonism between inhibitor of DNA binding (Id) and adipocyte determination and differentiation factor 1/sterol regulatory element-binding protein-1c (ADD1/SREBP-1c) trans-factors for the regulation of fatty acid synthase promoter in adipocytes. |journal=Biochem. J. |volume=344 Pt 3 |issue=  |pages= 873-80 |year= 2000 |pmid= 10585876 |doi=  }}
* {{cite journal | vauthors = Jögi A, Persson P, Grynfeld A, Påhlman S, Axelson H | title = Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation | journal = J. Biol. Chem. | volume = 277 | issue = 11 | pages = 9118–26 | year = 2002 | pmid = 11756408 | doi = 10.1074/jbc.M107713200 }}
*{{cite journal | author=Bounpheng MA, Dimas JJ, Dodds SG, Christy BA |title=Degradation of Id proteins by the ubiquitin-proteasome pathway. |journal=FASEB J. |volume=13 |issue= 15 |pages= 2257-64 |year= 2000 |pmid= 10593873 |doi= }}
*{{cite journal | author=Suzuki H, Fukunishi Y, Kagawa I, ''et al.'' |title=Protein-protein interaction panel using mouse full-length cDNAs. |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758-65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101 }}
*{{cite journal  | author=Jögi A, Persson P, Grynfeld A, ''et al.'' |title=Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9118-26 |year= 2002 |pmid= 11756408 |doi= 10.1074/jbc.M107713200 }}
}}
{{refend}}
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* {{MeshName|ID3+protein,+human}}
* {{MeshName|ID3+protein,+human}}


{{NLM content}}
{{Transcription factors|g1}}


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{{Transcription factors}}
[[Category:Transcription factors]]
[[Category:Transcription factors]]
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Latest revision as of 23:34, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

DNA-binding protein inhibitor ID-3 is a protein that in humans is encoded by the ID3 gene.[1][2]

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][2]

Interactions

ID3 (gene) has been shown to interact with TCF3.[3][4]

Repressors of ID3

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.[5]

See also

References

  1. ↑ Ellmeier W, Aguzzi A, Kleiner E, Kurzbauer R, Weith A (Aug 1992). "Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development". EMBO J. 11 (7): 2563–71. PMC 556731. PMID 1628620.
  2. ↑ 2.0 2.1 "Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein".
  3. ↑ Deed RW, Jasiok M, Norton JD (Apr 1998). "Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells". J. Biol. Chem. 273 (14): 8278–86. doi:10.1074/jbc.273.14.8278. PMID 9525934.
  4. ↑ Langlands K, Yin X, Anand G, Prochownik EV (Aug 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. PMID 9242638.
  5. ↑ Farioli-Vecchioli S, Saraulli D, Costanzi M, Leonardi L, Cinà I, Micheli L, Nutini M, Longone P, Oh SP, Cestari V, Tirone F (2009). Okazawa H, ed. "Impaired terminal differentiation of hippocampal granule neurons and defective contextual memory in PC3/Tis21 knockout mice". PLoS ONE. 4 (12): e8339. doi:10.1371/journal.pone.0008339. PMC 2791842. PMID 20020054.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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