ID2: Difference between revisions

ID2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4AYA
Identifiers
Aliases	ID2, GIG8, ID2A, ID2H, bHLHb26, inhibitor of DNA binding 2, HLH protein, inhibitor of DNA binding 2
External IDs	OMIM: 600386; MGI: 96397; HomoloGene: 1632; GeneCards: ID2; OMA:ID2 - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	8,684,461 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	25,147,139 bp
RNA expression pattern
	Top expressed in
	popliteal artery; ; tibial arteries; ; saphenous vein; ; pericardium; ; right lobe of liver; ; granulocyte; ; trachea; ; lower lobe of lung; ; renal medulla; ; seminal vesicula;
	Top expressed in
	vas deferens; ; seminal vesicula; ; lobe of cerebellum; ; migratory enteric neural crest cell; ; cerebellar vermis; ; abdominal wall; ; dermis; ; left lung lobe; ; hand; ; parotid gland;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	protein dimerization activity; transmembrane transporter binding; protein binding; DNA-binding transcription factor activity, RNA polymerase II-specific; DNA-binding transcription factor activity; transcription factor binding;
Cellular component	nucleus; cytosol; cytoplasm; protein-containing complex;
Biological process	regulation of G1/S transition of mitotic cell cycle; rhythmic process; negative regulation of DNA-binding transcription factor activity; regulation of transcription, DNA-templated; positive regulation of transcription involved in G1/S transition of mitotic cell cycle; multicellular organism development; negative regulation of transcription, DNA-templated; transcription, DNA-templated; negative regulation of transcription by RNA polymerase II; metanephros development; natural killer cell differentiation; thigmotaxis; leukocyte differentiation; membranous septum morphogenesis; bundle of His development; heart development; circadian rhythm; adult locomotory behavior; entrainment of circadian clock; positive regulation of gene expression; negative regulation of gene expression; oligodendrocyte development; regulation of lipid metabolic process; olfactory bulb development; circadian regulation of gene expression; mammary gland epithelial cell proliferation; regulation of circadian rhythm; entrainment of circadian clock by photoperiod; enucleate erythrocyte differentiation; negative regulation of DNA binding; locomotor rhythm; negative regulation of B cell differentiation; positive regulation of fat cell differentiation; positive regulation of erythrocyte differentiation; positive regulation of macrophage differentiation; negative regulation of neuron differentiation; negative regulation of osteoblast differentiation; positive regulation of blood pressure; positive regulation of transcription, DNA-templated; cell development; cell maturation; Peyer's patch development; embryonic digestive tract morphogenesis; positive regulation of smooth muscle cell proliferation; neuron fate commitment; cell morphogenesis involved in neuron differentiation; positive regulation of astrocyte differentiation; negative regulation of oligodendrocyte differentiation; adipose tissue development; mammary gland alveolus development; epithelial cell differentiation involved in mammary gland alveolus development; endodermal digestive tract morphogenesis; cellular response to lithium ion; cellular senescence; negative regulation of neural precursor cell proliferation; neuron differentiation; regulation of cell cycle;
	Sources:Amigo / QuickGO
Orthologs
	3398
	15902
	ENSG00000115738
	ENSMUSG00000020644
	Q02363
	P41136
	NM_002166
	NM_010496
	NP_002157
	NP_034626
	Wikidata
View/Edit Human	View/Edit Mouse

Browse history interactively

← Previous edit Next edit →

Content deleted Content added

VisualWikitext

Inline

Revision as of 15:52, 6 March 2024

DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.^[5]

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.^[6] The ID2 protein may play a role in the development and resistance to therapies of glioblastoma, the most aggressive of brain cancers.^[7]

Interactions

ID2 has been shown to interact with MyoD^[8] and NEDD9.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000115738 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020644 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. doi:10.1016/S0021-9258(17)42146-6. PMID 8294468.
^ "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".
^ Lee, Sang Bae; Frattini, Veronique; Bansal, Mukesh; Castano, Angelica M.; Sherman, Dan; Hutchinson, Keino; Bruce, Jeffrey N.; Califano, Andrea; Liu, Guangchao; Cardozo, Timothy; Iavarone, Antonio; Lasorella, Anna (2016). "An ID2-dependent mechanism for VHL inactivation in cancer". Nature. 529 (7585): 172–177. Bibcode:2016Natur.529..172L. doi:10.1038/nature16475. PMC 5384647. PMID 26735018.
^ 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.
^ 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.

External links

ID2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Overview of all the structural information available in the PDB for UniProt: Q02363 (DNA-binding protein inhibitor ID-2) at the PDBe-KB.

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

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000115738 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020644 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8294468-5] 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. doi:10.1016/S0021-9258(17)42146-6. PMID 8294468.

[entrez-6] "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".

[nature-7] Lee, Sang Bae; Frattini, Veronique; Bansal, Mukesh; Castano, Angelica M.; Sherman, Dan; Hutchinson, Keino; Bruce, Jeffrey N.; Califano, Andrea; Liu, Guangchao; Cardozo, Timothy; Iavarone, Antonio; Lasorella, Anna (2016). "An ID2-dependent mechanism for VHL inactivation in cancer". Nature. 529 (7585): 172–177. Bibcode:2016Natur.529..172L. doi:10.1038/nature16475. PMC 5384647. PMID 26735018.

[pmid9242638-8] 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.

[pmid10502414-9] 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.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

@@ Line 1: / Line 1: @@
+{{short description|Protein-coding gene in the species Homo sapiens}}
-{{For|the ISO/IEC 7810 identification card standard|ID-2 format}}
+{{For multi|the ISO/IEC 7810 identification card standard|ID-2 format|the electric concept car|Volkswagen ID.2all}}
 {{Infobox_gene}}
-'''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>
+'''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 | doi = 10.1016/S0021-9258(17)42146-6 | pmid = 8294468 | doi-access = free }}</ref>
 == 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.<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>
+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}}</ref>
-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>
+The ID2 protein may play a role in the development and resistance to therapies of [[glioblastoma]], the most aggressive of brain cancers.<ref name="nature">{{cite journal | title = An ID2-dependent mechanism for VHL inactivation in cancer| journal = Nature| volume = 529| issue = 7585| pages = 172–177| doi = 10.1038/nature16475| pmid = 26735018| pmc = 5384647| year = 2016| last1 = Lee| first1 = Sang Bae| last2 = Frattini| first2 = Veronique| last3 = Bansal| first3 = Mukesh| last4 = Castano| first4 = Angelica M.| last5 = Sherman| first5 = Dan| last6 = Hutchinson| first6 = Keino| last7 = Bruce| first7 = Jeffrey N.| last8 = Califano| first8 = Andrea| last9 = Liu| first9 = Guangchao| last10 = Cardozo| first10 = Timothy| last11 = Iavarone| first11 = Antonio| last12 = Lasorella| first12 = Anna| bibcode = 2016Natur.529..172L}}</ref>
 == Interactions ==
-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>
+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 | doi-access = free }}</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>
 == See also ==
@@ Line 17: / Line 18: @@
 == References ==
 {{reflist}}
-{{Clear}}
 == Further reading ==
 {{refbegin | 2}}
-* {{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 }}
+* {{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 | bibcode = 1992PNAS...89.1512B | doi-access = free }}
-* {{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 | 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 | doi-access = free }}
 * {{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 | 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 | 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 | 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 | 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 =  10.1128/MCB.16.6.2570}}
 * {{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 | 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 | 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 | doi-access = free }}
 * {{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 | 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 | 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 | 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 | bibcode = 1999Natur.397..702Y | s2cid = 4428856 }}
 * {{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 | 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 | 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 | issue = 3 | pages = 873–80 | year = 2000 | pmid = 10585876 | pmc = 1220711 | doi = 10.1042/0264-6021:3440873 }}
 * {{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 | 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 | 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 | bibcode = 2000Natur.407..592L | s2cid = 4335368 }}
 * {{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 | 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 | vauthors = Wang S, Sdrulla A, Johnson JE, Yokota Y, [[Ben Barres|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 | s2cid = 7978661 | doi-access = free }}
 * {{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 | 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 }}
@@ Line 44: / Line 44: @@
 == External links ==
 * {{MeshName|ID2+protein,+human}}
+* {{PDBe-KB2|Q02363|DNA-binding protein inhibitor ID-2}}
 {{NLM content}}