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{{For|the ISO/IEC 7810 identification card standard|ID-2 format}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''DNA-binding protein inhibitor ID-2''' is a [[protein]] that in humans is encoded by the ''ID2'' [[gene]].<ref name="pmid8294468">{{cite journal | vauthors = Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, Oda K | title = Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts | journal = J Biol Chem | volume = 269 | issue = 3 | pages = 2139–45 | date = Feb 1994 | pmid = 8294468 | pmc = | doi = }}</ref>
| 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 2, dominant negative helix-loop-helix protein
| HGNCid = 5361
| Symbol = ID2
| AltSymbols =; GIG8; ID2A; ID2H; MGC26389
| OMIM = 600386
| ECnumber = 
| Homologene = 1632
| MGIid = 96397
| GeneAtlas_image1 = PBB_GE_ID2_201565_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ID2_201566_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{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:0043433 |text = negative regulation of transcription factor activity}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3398
    | Hs_Ensembl = ENSG00000115738
    | Hs_RefseqProtein = NP_002157
    | Hs_RefseqmRNA = NM_002166
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 8736791
    | Hs_GenLoc_end = 8741997
    | Hs_Uniprot = Q02363
    | Mm_EntrezGene = 15902
    | Mm_Ensembl = ENSMUSG00000020644
    | Mm_RefseqmRNA = NM_010496
    | Mm_RefseqProtein = NP_034626
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 25682881
    | Mm_GenLoc_end = 25685170
    | Mm_Uniprot = Q545T4
  }}
}}
'''Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein''', also known as '''ID2''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene belongs to the inhibitor of DNA binding (ID) family, members of which are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative manner by suppressing their heterodimerization partners through the HLH domains. This protein may play a role in negatively regulating cell differentiation. A pseudogene has been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3398| accessdate = }}</ref>
{{PBB_Summary
A research published by "Nature" in 01/2016, authored by italian researchers Antonio Iavarone and Anna Lasorella, from Columbia University, states that ID2 protein has a relevant role in the development and resistance to therapies of glioblastoma, the most aggressive of brain cancers.<ref name="nature">{{cite web | title = An ID2-dependent mechanism for VHL inactivation in cancer| url = http://www.nature.com/nature/journal/vaop/ncurrent/full/nature16475.html| accessdate = }}</ref>
| section_title =
| summary_text = The protein encoded by this gene belongs to the inhibitor of DNA binding (ID) family, members of which are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative manner by suppressing their heterodimerization partners through the HLH domains. This protein may play a role in negatively regulating cell differentiation. A pseudogene has been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3398| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}


ID2 has been shown to [[Protein-protein interaction|interact]] with [[MyoD]]<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> and [[NEDD9]].<ref name=pmid10502414>{{cite journal | vauthors = Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA | title = Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain | journal = Exp. Cell Res. | volume = 252 | issue = 1 | pages = 224–35 | date = Oct 1999 | pmid = 10502414 | doi = 10.1006/excr.1999.4609 }}</ref>


==Further reading==
== See also ==
* [[Inhibitor of DNA-binding protein]]
 
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Biggs J, Murphy EV, Israel MA | title = A human Id-like helix-loop-helix protein expressed during early development | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 89 | issue = 4 | pages = 1512–6 | year = 1992 | pmid = 1741406 | pmc = 48481 | doi = 10.1073/pnas.89.4.1512 }}
| citations =
* {{cite journal | vauthors = Iavarone A, Garg P, Lasorella A, Hsu J, Israel MA | title = The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein | journal = Genes Dev. | volume = 8 | issue = 11 | pages = 1270–84 | year = 1994 | pmid = 7926730 | doi = 10.1101/gad.8.11.1270 }}
*{{cite journal | author=Biggs J, Murphy EV, Israel MA |title=A human Id-like helix-loop-helix protein expressed during early development. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 4 |pages= 1512-6 |year= 1992 |pmid= 1741406 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Iavarone A, Garg P, Lasorella A, ''et al.'' |title=The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein. |journal=Genes Dev. |volume=8 |issue= 11 |pages= 1270-84 |year= 1994 |pmid= 7926730 |doi= }}
* {{cite journal | vauthors = Kurabayashi M, Jeyaseelan R, Kedes L | title = Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2 | journal = Gene | volume = 133 | issue = 2 | pages = 305–6 | year = 1993 | pmid = 8224921 | doi = 10.1016/0378-1119(93)90658-P }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Mathew S, Chen W, Murty VV, Benezra R, Chaganti RS | title = Chromosomal assignment of human ID1 and ID2 genes | journal = Genomics | volume = 30 | issue = 2 | pages = 385–7 | year = 1996 | pmid = 8586447 | doi = 10.1006/geno.1995.0037 }}
*{{cite journal | author=Kurabayashi M, Jeyaseelan R, Kedes L |title=Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2. |journal=Gene |volume=133 |issue= 2 |pages= 305-6 |year= 1993 |pmid= 8224921 |doi= }}
* {{cite journal | vauthors = Lasorella A, Iavarone A, Israel MA | title = Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins | journal = Mol. Cell. Biol. | volume = 16 | issue = 6 | pages = 2570–8 | year = 1996 | pmid = 8649364 | pmc = 231247 | doi = }}
*{{cite journal | author=Hara E, Yamaguchi T, Nojima H, ''et al.'' |title=Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts. |journal=J. Biol. Chem. |volume=269 |issue= 3 |pages= 2139-45 |year= 1994 |pmid= 8294468 |doi= }}
* {{cite journal | vauthors = Hara E, Hall M, Peters G | title = Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors | journal = EMBO J. | volume = 16 | issue = 2 | pages = 332–42 | year = 1997 | pmid = 9029153 | pmc = 1169639 | doi = 10.1093/emboj/16.2.332 }}
*{{cite journal | author=Mathew S, Chen W, Murty VV, ''et al.'' |title=Chromosomal assignment of human ID1 and ID2 genes. |journal=Genomics |volume=30 |issue= 2 |pages= 385-7 |year= 1996 |pmid= 8586447 |doi= 10.1006/geno.1995.0037 }}
* {{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=Lasorella A, Iavarone A, Israel MA |title=Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins. |journal=Mol. Cell. Biol. |volume=16 |issue= 6 |pages= 2570-8 |year= 1996 |pmid= 8649364 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Hara E, Hall M, Peters G |title=Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors. |journal=EMBO J. |volume=16 |issue= 2 |pages= 332-42 |year= 1997 |pmid= 9029153 |doi= 10.1093/emboj/16.2.332 }}
* {{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=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 = Yokota Y, Mansouri A, Mori S, Sugawara S, Adachi S, Nishikawa S, Gruss P | title = Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2 | journal = Nature | volume = 397 | issue = 6721 | pages = 702–6 | year = 1999 | pmid = 10067894 | doi = 10.1038/17812 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA | title = Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain | journal = Exp. Cell Res. | volume = 252 | issue = 1 | pages = 224–35 | year = 1999 | pmid = 10502414 | doi = 10.1006/excr.1999.4609 }}
*{{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 = 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 = Pt 3 | pages = 873–80 | year = 2000 | pmid = 10585876 | pmc = 1220711 | doi = 10.1042/0264-6021:3440873 }}
*{{cite journal | author=Yokota Y, Mansouri A, Mori S, ''et al.'' |title=Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2. |journal=Nature |volume=397 |issue= 6721 |pages= 702-6 |year= 1999 |pmid= 10067894 |doi= 10.1038/17812 }}
* {{cite journal | vauthors = Liu J, Shi W, Warburton D | title = A cysteine residue in the helix-loop-helix domain of Id2 is critical for homodimerization and function | journal = Biochem. Biophys. Res. Commun. | volume = 273 | issue = 3 | pages = 1042–7 | year = 2000 | pmid = 10891368 | doi = 10.1006/bbrc.2000.3055 }}
*{{cite journal | author=Law SF, Zhang YZ, Fashena SJ, ''et al.'' |title=Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain. |journal=Exp. Cell Res. |volume=252 |issue= 1 |pages= 224-35 |year= 1999 |pmid= 10502414 |doi= 10.1006/excr.1999.4609 }}
* {{cite journal | vauthors = Lasorella A, Noseda M, Beyna M, Yokota Y, Iavarone A | title = Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins | journal = Nature | volume = 407 | issue = 6804 | pages = 592–8 | year = 2000 | pmid = 11034201 | doi = 10.1038/35036504 }}
*{{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 = Roberts EC, Deed RW, Inoue T, Norton JD, Sharrocks AD | title = Id Helix-Loop-Helix Proteins Antagonize Pax Transcription Factor Activity by Inhibiting DNA Binding | journal = Mol. Cell. Biol. | volume = 21 | issue = 2 | pages = 524–33 | year = 2001 | pmid = 11134340 | pmc = 86614 | doi = 10.1128/MCB.21.2.524-533.2001 }}
*{{cite journal | author=Liu J, Shi W, Warburton D |title=A cysteine residue in the helix-loop-helix domain of Id2 is critical for homodimerization and function. |journal=Biochem. Biophys. Res. Commun. |volume=273 |issue= 3 |pages= 1042-7 |year= 2000 |pmid= 10891368 |doi= 10.1006/bbrc.2000.3055 }}
* {{cite journal | vauthors = Wang S, Sdrulla A, Johnson JE, Yokota Y, Barres BA | title = A role for the helix-loop-helix protein Id2 in the control of oligodendrocyte development | journal = Neuron | volume = 29 | issue = 3 | pages = 603–14 | year = 2001 | pmid = 11301021 | doi = 10.1016/S0896-6273(01)00237-9 }}
*{{cite journal | author=Lasorella A, Noseda M, Beyna M, ''et al.'' |title=Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins. |journal=Nature |volume=407 |issue= 6804 |pages= 592-8 |year= 2000 |pmid= 11034201 |doi= 10.1038/35036504 }}
* {{cite journal | vauthors = Wong J, Funes-Duran M, Ahlberg J, Round J, O'Connell R, Miller R, Chen E, Richmond PA, Vierra CA | title = Characterization of a basic helix-loop-helix protein, ABF-1: nuclear localization, transcriptional properties, and interaction with Id-2 | journal = DNA Cell Biol. | volume = 20 | issue = 8 | pages = 465–71 | year = 2001 | pmid = 11560778 | doi = 10.1089/104454901316976091 }}
*{{cite journal | author=Roberts EC, Deed RW, Inoue T, ''et al.'' |title=Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding. |journal=Mol. Cell. Biol. |volume=21 |issue= 2 |pages= 524-33 |year= 2001 |pmid= 11134340 |doi= 10.1128/MCB.21.2.524-533.2001 }}
* {{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=Wang S, Sdrulla A, Johnson JE, ''et al.'' |title=A role for the helix-loop-helix protein Id2 in the control of oligodendrocyte development. |journal=Neuron |volume=29 |issue= 3 |pages= 603-14 |year= 2001 |pmid= 11301021 |doi= }}
*{{cite journal | author=Wong J, Funes-Duran M, Ahlberg J, ''et al.'' |title=Characterization of a basic helix-loop-helix protein, ABF-1: nuclear localization, transcriptional properties, and interaction with Id-2. |journal=DNA Cell Biol. |volume=20 |issue= 8 |pages= 465-71 |year= 2001 |pmid= 11560778 |doi= 10.1089/104454901316976091 }}
*{{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 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* {{MeshName|ID2+protein,+human}}
 
{{NLM content}}
{{Transcription factors|g1}}
 
[[Category:Transcription factors]]
 
 
{{gene-2-stub}}

Revision as of 23:34, 31 August 2017

For the ISO/IEC 7810 identification card standard, see ID-2 format.
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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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Wikidata
View/Edit Human

DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.[1]

Function

The protein encoded by this gene belongs to the inhibitor of DNA binding (ID) family, members of which are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative manner by suppressing their heterodimerization partners through the HLH domains. This protein may play a role in negatively regulating cell differentiation. A pseudogene has been identified for this gene.[2] A research published by "Nature" in 01/2016, authored by italian researchers Antonio Iavarone and Anna Lasorella, from Columbia University, states that ID2 protein has a relevant role in the development and resistance to therapies of glioblastoma, the most aggressive of brain cancers.[3]

Interactions

ID2 has been shown to interact with MyoD[4] and NEDD9.[5]

See also

References

  1. ↑ Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, Oda K (Feb 1994). "Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts". J Biol Chem. 269 (3): 2139–45. PMID 8294468.
  2. ↑ "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".
  3. ↑ "An ID2-dependent mechanism for VHL inactivation in cancer".
  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. ↑ Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (Oct 1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. 252 (1): 224–35. doi:10.1006/excr.1999.4609. PMID 10502414.

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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