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{{About|the protein}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''DNA-binding protein inhibitor ID-1''' is a [[protein]] that in humans is encoded by the ''ID1'' [[gene]].<ref name=HalId>{{cite journal | vauthors = Benezra R, Davis RL, Lockshon D, Turner DL, Weintraub H | title = The protein Id: a negative regulator of helix-loop-helix DNA binding proteins | journal = Cell | volume = 61 | issue = 1 | pages = 49–59 | year = 1990 | pmid = 2156629 | doi = 10.1016/0092-8674(90)90214-Y }}</ref><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 = February 1994 | pmid = 8294468 | pmc = | doi = }}</ref>
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<!-- 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 1, dominant negative helix-loop-helix protein
| HGNCid = 5360
| Symbol = ID1
| AltSymbols =; ID
| OMIM = 600349
| ECnumber = 
| Homologene = 1631
| MGIid = 96396
| GeneAtlas_image1 = PBB_GE_ID1_208937_s_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}}
| 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:0030509 |text = BMP signaling pathway}} {{GNF_GO|id=GO:0043433 |text = negative regulation of transcription factor activity}} {{GNF_GO|id=GO:0045765 |text = regulation of angiogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3397
    | Hs_Ensembl = ENSG00000125968
    | Hs_RefseqProtein = NP_002156
    | Hs_RefseqmRNA = NM_002165
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 29656747
    | Hs_GenLoc_end = 29657979
    | Hs_Uniprot = P41134
    | Mm_EntrezGene = 15901
    | Mm_Ensembl = ENSMUSG00000042745
    | Mm_RefseqmRNA = NM_010495
    | Mm_RefseqProtein = NP_034625
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 152427715
    | Mm_GenLoc_end = 152428851
    | Mm_Uniprot = Q6GTZ3
  }}
}}
'''Inhibitor of DNA binding 1, dominant negative helix-loop-helix protein''', also known as '''ID1''', is a human [[gene]].


The protein encoded by this gene is a helix-loop-helix (HLH) protein that can form heterodimers with members of the [[basic-helix-loop-helix|basic HLH]] family of [[transcription factor]]s. The encoded protein has no DNA binding activity and therefore can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts. This protein may play a role in cell growth, senescence, and differentiation. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3397| accessdate = }}</ref>
The protein encoded by this gene is a helix-loop-helix (HLH) protein that can form heterodimers with members of the [[basic-helix-loop-helix|basic HLH]] family of [[transcription factor]]s.<ref name=HalId /> The encoded protein has no DNA binding activity and therefore can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts.<ref name=HalId /> This protein may play a role in cell growth, senescence, and differentiation.<ref>{{cite journal | vauthors = Ruzinova MB, Benezra R | title = Id proteins in development, cell cycle and cancer | journal = Trends in Cell Biology | volume = 13 | issue = 8 | pages = 410–8 | year = 2003 | pmid = 12888293 | doi = 10.1016/S0962-8924(03)00147-8 }}</ref><ref>{{cite journal | vauthors = Perk J, Iavarone A, Benezra R | title = The Id family of helix-loop-helix proteins in cancer | journal = Nat Rev Cancer | volume = 5 | issue = 8 | pages = 603–614 | year = 2005 | pmid = 16034366 | doi = 10.1038/nrc1673 }}</ref><ref>{{cite journal|last1=Cunningham|first1=Thomas J.|last2=Yu|first2=Michael S.|last3=McKeithan|first3=Wesley L.|last4=Spiering|first4=Sean|last5=Carrette|first5=Florent|last6=Huang|first6=Chun-Teng|last7=Bushway|first7=Paul J.|last8=Tierney|first8=Matthew|last9=Albini|first9=Sonia|last10=Giacca|first10=Mauro|last11=Mano|first11=Miguel|last12=Puri|first12=Pier Lorenzo|last13=Sacco|first13=Alessandra|last14=Ruiz-Lozano|first14=Pilar|last15=Riou|first15=Jean-Francois|last16=Umbhauer|first16=Muriel|last17=Duester|first17=Gregg|last18=Mercola|first18=Mark|last19=Colas|first19=Alexandre R.|title=Id genes are essential for early heart formation|journal=Genes & Development|date=1 July 2017|volume=31|issue=13|pages=1325–1338|doi=10.1101/gad.300400.117}}</ref> Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3397| accessdate = }}</ref>


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
ID1 has been shown to [[Protein-protein interaction|interact]] weakly with [[MyoD]]<ref name=HalId /><ref name="pmid15029197">{{cite journal | vauthors = Garkavtsev I, Kozin SV, Chernova O, Xu L, Winkler F, Brown E, Barnett GH, Jain RK | title = The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis | journal = Nature | volume = 428 | issue = 6980 | pages = 328–32 | date = March 2004 | pmid = 15029197 | doi = 10.1038/nature02329 }}</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 = August 1997 | pmid = 9242638 | doi = 10.1074/jbc.272.32.19785 }}</ref><ref name="pmid8380166">{{cite journal | vauthors = Finkel T, Duc J, Fearon ER, Dang CV, Tomaselli GF | title = Detection and modulation in vivo of helix-loop-helix protein-protein interactions | journal = J. Biol. Chem. | volume = 268 | issue = 1 | pages = 5–8 | date = January 1993 | pmid = 8380166 | doi =  }}</ref><ref name="pmid9528857">{{cite journal | vauthors = Gupta K, Anand G, Yin X, Grove L, Prochownik EV | title = Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc | journal = Oncogene | volume = 16 | issue = 9 | pages = 1149–59 | date = March 1998 | pmid = 9528857 | doi = 10.1038/sj.onc.1201634 }}</ref><ref name="pmid12145280">{{cite journal | vauthors = McLoughlin P, Ehler E, Carlile G, Licht JD, Schäfer BW | title = The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein | journal = J. Biol. Chem. | volume = 277 | issue = 40 | pages = 37045–53 | date = October 2002 | pmid = 12145280 | doi = 10.1074/jbc.M203336200 }}</ref><ref name="pmid18674781">{{cite journal | vauthors = Ling MT, Chiu YT, Lee TK, Leung SC, Fung MK, Wang X, Wong KF, Wong YC | title = Id-1 induces proteasome-dependent degradation of the HBX protein | journal = J. Mol. Biol. | volume = 382 | issue = 1 | pages = 34–43 | date = September 2008 | pmid = 18674781 | doi = 10.1016/j.jmb.2007.06.020 }}</ref> but very tightly with ubiquitously expressed E proteins.<ref name="pmid1644289">{{cite journal | vauthors = Jen Y, Weintraub H, Benezra R | title = Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins | journal = Genes Dev. | volume = 6 | issue = 8 | pages = 1466–79 | date = August 1992 | pmid = 1644289 | doi = 10.1101/gad.6.8.1466 }}</ref> E proteins heterodimerize with tissue restricted bHLH proteins such as Myod, NeuroD, etc. to form active transcription complexes so by sequestering E proteins, Id proteins can inhibit tissue restricted gene expression in multiple cell lineages using the same biochemical mechanism. Other interacting partners include [[CASK]].<ref name="pmid15694377">{{cite journal | vauthors = Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z, Luo X | title = CASK inhibits ECV304 cell growth and interacts with Id1 | journal = Biochem. Biophys. Res. Commun. | volume = 328 | issue = 2 | pages = 517–21 | date = March 2005 | pmid = 15694377 | doi = 10.1016/j.bbrc.2005.01.014 }}</ref>
{{refbegin | 2}}
 
{{PBB_Further_reading
== Clinical significance ==
| citations =  
 
*{{cite journal | author=Zhu W, Dahmen J, Bulfone A, ''et al.'' |title=Id gene expression during development and molecular cloning of the human Id-1 gene. |journal=Brain Res. Mol. Brain Res. |volume=30 |issue= 2 |pages= 312-26 |year= 1995 |pmid= 7637581 |doi= }}
ID1 can be used to mark [[endothelial progenitor cell]]s which are critical to tumor growth and [[angiogenesis]].<ref name="pmid10537105">{{cite journal | vauthors = Lyden D, Young AZ, Zagzag D, Yan W, Gerald W, O'Reilly R, Bader BL, Hynes RO, Zhuang Y, Manova K, Benezra R | title = Id1 and Id3 are required for neurogenesis, angiogenesis and vascularization of tumour xenografts | journal = Nature | volume = 401 | issue = 6754 | pages = 670–7 | date = October 1999 | pmid = 10537105 | doi = 10.1038/44334 }}</ref><ref name="pmid11689883">{{cite journal | vauthors = Lyden D, Hattori K, Dias S, Costa C, Blaikie P, Butros L, Chadburn A, Heissig B, Marks W, Witte L, Wu Y, Hicklin D, Zhu Z, Hackett NR, Crystal RG, Moore MA, Hajjar KA, Manova K, Benezra R, Rafii S | title = Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth | journal = Nat. Med. | volume = 7 | issue = 11 | pages = 1194–201 | date = November 2001 | pmid = 11689883 | doi = 10.1038/nm1101-1194 }}</ref> Targeting ID1 results in decreased tumor growth.<ref name="pmid18176556">{{cite journal | vauthors = Henke E, Perk J, Vider J, de Candia P, Chin Y, Solit DB, Ponomarev V, Cartegni L, Manova K, Rosen N, Benezra R | title = Peptide-conjugated antisense oligonucleotides for targeted inhibition of a transcriptional regulator in vivo | journal = Nat. Biotechnol. | volume = 26 | issue = 1 | pages = 91–100 | date = January 2008 | pmid = 18176556 | doi = 10.1038/nbt1366 }}</ref><ref name="pmid20807818">{{cite journal | vauthors = Mellick AS, Plummer PN, Nolan DJ, Gao D, Bambino K, Hahn M, Catena R, Turner V, McDonnell K, Benezra R, Brink R, Swarbrick A, Mittal V | title = Using the transcription factor inhibitor of DNA binding 1 to selectively target endothelial progenitor cells offers novel strategies to inhibit tumour angiogenesis and growth | journal = Cancer Res. | volume = 70 | issue = 18 | pages = 7273–82 | date = September 2010 | pmid = 20807818 | pmc = 3058751 | doi = 10.1158/0008-5472.CAN-10-1142 }}</ref>
*{{cite journal | author=Deed RW, Jasiok M, Norton JD |title=Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins. |journal=Biochim. Biophys. Acta |volume=1219 |issue= 1 |pages= 160-2 |year= 1994 |pmid= 8086456 |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= }}
== See also ==
*{{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 }}
* [[Inhibitor of DNA-binding protein]]
*{{cite journal | author=Nehlin JO, Hara E, Kuo WL, ''et al.'' |title=Genomic organization, sequence, and chromosomal localization of the human helix-loop-helix Id1 gene. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 3 |pages= 628-34 |year= 1997 |pmid= 9070860 |doi= 10.1006/bbrc.1997.6152 }}
{{Clear}}
*{{cite journal | author=Anand G, Yin X, Shahidi AK, ''et al.'' |title=Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26 S proteasome. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19140-51 |year= 1997 |pmid= 9235903 |doi= }}
 
*{{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= }}
== References ==
*{{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 }}
{{reflist|35em}}
*{{cite journal | author=Outinen PA, Sood SK, Pfeifer SI, ''et al.'' |title=Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells. |journal=Blood |volume=94 |issue= 3 |pages= 959-67 |year= 1999 |pmid= 10419887 |doi= }}
 
*{{cite journal | author=Langlands K, Down GA, Kealey T |title=Id proteins are dynamically expressed in normal epidermis and dysregulated in squamous cell carcinoma. |journal=Cancer Res. |volume=60 |issue= 21 |pages= 5929-33 |year= 2000 |pmid= 11085505 |doi= }}
== Further reading ==
*{{cite journal | author=Ohtani N, Zebedee Z, Huot TJ, ''et al.'' |title=Opposing effects of Ets and Id proteins on p16INK4a expression during cellular senescence. |journal=Nature |volume=409 |issue= 6823 |pages= 1067-70 |year= 2001 |pmid= 11234019 |doi= 10.1038/35059131 }}
{{refbegin|35em}}
*{{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 | vauthors = Zhu W, Dahmen J, Bulfone A, Rigolet M, Hernandez MC, Kuo WL, Puelles L, Rubenstein JL, Israel MA | title = Id gene expression during development and molecular cloning of the human Id-1 gene | journal = Brain Res. Mol. Brain Res. | volume = 30 | issue = 2 | pages = 312–26 | year = 1995 | pmid = 7637581 | doi = 10.1016/0169-328X(95)00017-M }}
*{{cite journal | author=Korchynskyi O, ten Dijke P |title=Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4883-91 |year= 2002 |pmid= 11729207 |doi= 10.1074/jbc.M111023200 }}
* {{cite journal | vauthors = Deed RW, Jasiok M, Norton JD | title = Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins | journal = Biochim. Biophys. Acta | volume = 1219 | issue = 1 | pages = 160–2 | year = 1994 | pmid = 8086456 | doi = 10.1016/0167-4781(94)90261-5 }}
*{{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 }}
* {{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=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
* {{cite journal | vauthors = Nehlin JO, Hara E, Kuo WL, Collins C, Campisi J | title = Genomic organization, sequence, and chromosomal localization of the human helix-loop-helix Id1 gene | journal = Biochem. Biophys. Res. Commun. | volume = 231 | issue = 3 | pages = 628–34 | year = 1997 | pmid = 9070860 | doi = 10.1006/bbrc.1997.6152 }}
*{{cite journal | author=Singh J, Murata K, Itahana Y, Desprez PY |title=Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex. |journal=Oncogene |volume=21 |issue= 12 |pages= 1812-22 |year= 2002 |pmid= 11896613 |doi= 10.1038/sj.onc.1205252 }}
* {{cite journal | vauthors = Anand G, Yin X, Shahidi AK, Grove L, Prochownik EV | title = Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26 S proteasome | journal = J. Biol. Chem. | volume = 272 | issue = 31 | pages = 19140–51 | year = 1997 | pmid = 9235903 | doi = 10.1074/jbc.272.31.19140 }}
*{{cite journal | author=Liu CJ, Ding B, Wang H, Lengyel P |title=The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins. |journal=Mol. Cell. Biol. |volume=22 |issue= 9 |pages= 2893-905 |year= 2002 |pmid= 11940648 |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 = 19785–19793 | year = 1997 | pmid = 9242638 | doi = 10.1074/jbc.272.32.19785 }}
*{{cite journal | author=Ouyang XS, Wang X, Ling MT, ''et al.'' |title=Id-1 stimulates serum independent prostate cancer cell proliferation through inactivation of p16(INK4a)/pRB pathway. |journal=Carcinogenesis |volume=23 |issue= 5 |pages= 721-5 |year= 2002 |pmid= 12016143 |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=Ling MT, Wang X, Tsao SW, Wong YC |title=Down-regulation of Id-1 expression is associated with TGF beta 1-induced growth arrest in prostate epithelial cells. |journal=Biochim. Biophys. Acta |volume=1570 |issue= 3 |pages= 145-52 |year= 2002 |pmid= 12020803 |doi=  }}
* {{cite journal | vauthors = Outinen PA, Sood SK, Pfeifer SI, Pamidi S, Podor TJ, Li J, Weitz JI, Austin RC | title = Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells | journal = Blood | volume = 94 | issue = 3 | pages = 959–67 | year = 1999 | pmid = 10419887 | doi =  }}
*{{cite journal  | author=Wang X, Xu K, Ling MT, ''et al.'' |title=Evidence of increased Id-1 expression and its role in cell proliferation in nasopharyngeal carcinoma cells. |journal=Mol. Carcinog. |volume=35 |issue= 1 |pages= 42-9 |year= 2002 |pmid= 12203366 |doi= 10.1002/mc.10072 }}
* {{cite journal | vauthors = Langlands K, Down GA, Kealey T | title = Id proteins are dynamically expressed in normal epidermis and dysregulated in squamous cell carcinoma | journal = Cancer Res. | volume = 60 | issue = 21 | pages = 5929–33 | year = 2000 | pmid = 11085505 | doi =  }}
}}
* {{cite journal | vauthors = Ohtani N, Zebedee Z, Huot TJ, Stinson JA, Sugimoto M, Ohashi Y, Sharrocks AD, Peters G, Hara E | title = Opposing effects of Ets and Id proteins on p16INK4a expression during cellular senescence | journal = Nature | volume = 409 | issue = 6823 | pages = 1067–70 | year = 2001 | pmid = 11234019 | doi = 10.1038/35059131 }}
* {{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 | vauthors = Korchynskyi O, ten Dijke P | title = Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter | journal = J. Biol. Chem. | volume = 277 | issue = 7 | pages = 4883–4891 | year = 2002 | pmid = 11729207 | doi = 10.1074/jbc.M111023200 }}
* {{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 | vauthors = Singh J, Murata K, Itahana Y, Desprez PY | title = Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex | journal = Oncogene | volume = 21 | issue = 12 | pages = 1812–1822 | year = 2002 | pmid = 11896613 | doi = 10.1038/sj.onc.1205252 }}
* {{cite journal | vauthors = Liu CJ, Ding B, Wang H, Lengyel P | title = The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins | journal = Mol. Cell. Biol. | volume = 22 | issue = 9 | pages = 2893–2905 | year = 2002 | pmid = 11940648 | pmc = 133750 | doi = 10.1128/MCB.22.9.2893-2905.2002 }}
* {{cite journal | vauthors = Ouyang XS, Wang X, Ling MT, Wong HL, Tsao SW, Wong YC | title = Id-1 stimulates serum independent prostate cancer cell proliferation through inactivation of p16(INK4a)/pRB pathway | journal = Carcinogenesis | volume = 23 | issue = 5 | pages = 721–5 | year = 2002 | pmid = 12016143 | doi = 10.1093/carcin/23.5.721 }}
* {{cite journal | vauthors = Ling MT, Wang X, Tsao SW, Wong YC | title = Down-regulation of Id-1 expression is associated with TGF beta 1-induced growth arrest in prostate epithelial cells | journal = Biochim. Biophys. Acta | volume = 1570 | issue = 3 | pages = 145–52 | year = 2002 | pmid = 12020803 | doi = 10.1016/S0304-4165(02)00189-7 }}
* {{cite journal | vauthors = Wang X, Xu K, Ling MT, Wong YC, Feng HC, Nicholls J, Tsao SW | title = Evidence of increased Id-1 expression and its role in cell proliferation in nasopharyngeal carcinoma cells | journal = Mol. Carcinog. | volume = 35 | issue = 1 | pages = 42–9 | year = 2002 | pmid = 12203366 | doi = 10.1002/mc.10072 }}
{{refend}}
{{refend}}


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* {{MeshName|ID1+protein,+human}}
* {{MeshName|ID1+protein,+human}}


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


{{protein-stub}}
{{DEFAULTSORT:Id1}}
{{NLM content}}
{{Transcription factors}}
[[Category:Transcription factors]]
[[Category:Transcription factors]]
{{WikiDoc Sources}}
[[Category:Aging-related genes]]

Latest revision as of 09:10, 13 November 2017

This article is about the protein. For other uses, see ID1 (disambiguation).
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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
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Wikidata
View/Edit Human

DNA-binding protein inhibitor ID-1 is a protein that in humans is encoded by the ID1 gene.[1][2]

Function

The protein encoded by this gene is a helix-loop-helix (HLH) protein that can form heterodimers with members of the basic HLH family of transcription factors.[1] The encoded protein has no DNA binding activity and therefore can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts.[1] This protein may play a role in cell growth, senescence, and differentiation.[3][4][5] Two transcript variants encoding different isoforms have been found for this gene.[6]

Interactions

ID1 has been shown to interact weakly with MyoD[1][7][8][9][10][11][12] but very tightly with ubiquitously expressed E proteins.[13] E proteins heterodimerize with tissue restricted bHLH proteins such as Myod, NeuroD, etc. to form active transcription complexes so by sequestering E proteins, Id proteins can inhibit tissue restricted gene expression in multiple cell lineages using the same biochemical mechanism. Other interacting partners include CASK.[14]

Clinical significance

ID1 can be used to mark endothelial progenitor cells which are critical to tumor growth and angiogenesis.[15][16] Targeting ID1 results in decreased tumor growth.[17][18]

See also

References

  1. ↑ 1.0 1.1 1.2 1.3 Benezra R, Davis RL, Lockshon D, Turner DL, Weintraub H (1990). "The protein Id: a negative regulator of helix-loop-helix DNA binding proteins". Cell. 61 (1): 49–59. doi:10.1016/0092-8674(90)90214-Y. PMID 2156629.
  2. ↑ Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, Oda K (February 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.
  3. ↑ Ruzinova MB, Benezra R (2003). "Id proteins in development, cell cycle and cancer". Trends in Cell Biology. 13 (8): 410–8. doi:10.1016/S0962-8924(03)00147-8. PMID 12888293.
  4. ↑ Perk J, Iavarone A, Benezra R (2005). "The Id family of helix-loop-helix proteins in cancer". Nat Rev Cancer. 5 (8): 603–614. doi:10.1038/nrc1673. PMID 16034366.
  5. ↑ Cunningham, Thomas J.; Yu, Michael S.; McKeithan, Wesley L.; Spiering, Sean; Carrette, Florent; Huang, Chun-Teng; Bushway, Paul J.; Tierney, Matthew; Albini, Sonia; Giacca, Mauro; Mano, Miguel; Puri, Pier Lorenzo; Sacco, Alessandra; Ruiz-Lozano, Pilar; Riou, Jean-Francois; Umbhauer, Muriel; Duester, Gregg; Mercola, Mark; Colas, Alexandre R. (1 July 2017). "Id genes are essential for early heart formation". Genes & Development. 31 (13): 1325–1338. doi:10.1101/gad.300400.117.
  6. ↑ "Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein".
  7. ↑ Garkavtsev I, Kozin SV, Chernova O, Xu L, Winkler F, Brown E, Barnett GH, Jain RK (March 2004). "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis". Nature. 428 (6980): 328–32. doi:10.1038/nature02329. PMID 15029197.
  8. ↑ Langlands K, Yin X, Anand G, Prochownik EV (August 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.
  9. ↑ Finkel T, Duc J, Fearon ER, Dang CV, Tomaselli GF (January 1993). "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". J. Biol. Chem. 268 (1): 5–8. PMID 8380166.
  10. ↑ Gupta K, Anand G, Yin X, Grove L, Prochownik EV (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
  11. ↑ McLoughlin P, Ehler E, Carlile G, Licht JD, Schäfer BW (October 2002). "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". J. Biol. Chem. 277 (40): 37045–53. doi:10.1074/jbc.M203336200. PMID 12145280.
  12. ↑ Ling MT, Chiu YT, Lee TK, Leung SC, Fung MK, Wang X, Wong KF, Wong YC (September 2008). "Id-1 induces proteasome-dependent degradation of the HBX protein". J. Mol. Biol. 382 (1): 34–43. doi:10.1016/j.jmb.2007.06.020. PMID 18674781.
  13. ↑ Jen Y, Weintraub H, Benezra R (August 1992). "Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins". Genes Dev. 6 (8): 1466–79. doi:10.1101/gad.6.8.1466. PMID 1644289.
  14. ↑ Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z, Luo X (March 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochem. Biophys. Res. Commun. 328 (2): 517–21. doi:10.1016/j.bbrc.2005.01.014. PMID 15694377.
  15. ↑ Lyden D, Young AZ, Zagzag D, Yan W, Gerald W, O'Reilly R, Bader BL, Hynes RO, Zhuang Y, Manova K, Benezra R (October 1999). "Id1 and Id3 are required for neurogenesis, angiogenesis and vascularization of tumour xenografts". Nature. 401 (6754): 670–7. doi:10.1038/44334. PMID 10537105.
  16. ↑ Lyden D, Hattori K, Dias S, Costa C, Blaikie P, Butros L, Chadburn A, Heissig B, Marks W, Witte L, Wu Y, Hicklin D, Zhu Z, Hackett NR, Crystal RG, Moore MA, Hajjar KA, Manova K, Benezra R, Rafii S (November 2001). "Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth". Nat. Med. 7 (11): 1194–201. doi:10.1038/nm1101-1194. PMID 11689883.
  17. ↑ Henke E, Perk J, Vider J, de Candia P, Chin Y, Solit DB, Ponomarev V, Cartegni L, Manova K, Rosen N, Benezra R (January 2008). "Peptide-conjugated antisense oligonucleotides for targeted inhibition of a transcriptional regulator in vivo". Nat. Biotechnol. 26 (1): 91–100. doi:10.1038/nbt1366. PMID 18176556.
  18. ↑ Mellick AS, Plummer PN, Nolan DJ, Gao D, Bambino K, Hahn M, Catena R, Turner V, McDonnell K, Benezra R, Brink R, Swarbrick A, Mittal V (September 2010). "Using the transcription factor inhibitor of DNA binding 1 to selectively target endothelial progenitor cells offers novel strategies to inhibit tumour angiogenesis and growth". Cancer Res. 70 (18): 7273–82. doi:10.1158/0008-5472.CAN-10-1142. PMC 3058751. PMID 20807818.

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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