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Inhibitor of DNA binding 1, dominant negative helix-loop-helix protein
Symbols ID1; ID
External IDs OMIM600349 MGI96396 HomoloGene1631 GeneCards: ID1 Gene
RNA expression pattern
PBB GE ID1 208937 s at tn.png
More reference expression data
Species Human Mouse
Entrez 3397 15901
Ensembl ENSG00000125968 ENSMUSG00000042745
UniProt P41134 Q6GTZ3
RefSeq (mRNA) NM_002165 NM_010495
RefSeq (protein) NP_002156 NP_034625
Location (UCSC) Chr 20:
29.66 - 29.66 Mb
Chr 2:
152.43 - 152.43 Mb
PubMed search [1] [2]

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

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. 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.[2]


See also


ID1 has been shown to interact with MyoD[3][4][5][6][7][8] and CASK.[9]


  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: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein".  
  3. ^ Garkavtsev, Igor; Kozin Sergey V, Chernova Olga, Xu Lei, Winkler Frank, Brown Edward, Barnett Gene H, Jain Rakesh K (Mar. 2004). "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis". Nature (England) 428 (6980): 328–32. doi:10.1038/nature02329. PMID 15029197.  
  4. ^ Langlands, K; Yin X, Anand G, Prochownik E V (Aug. 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. (UNITED STATES) 272 (32): 19785–93. ISSN 0021-9258. PMID 9242638.  
  5. ^ Finkel, T; Duc J, Fearon E R, Dang C V, Tomaselli G F (Jan. 1993). "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". J. Biol. Chem. (UNITED STATES) 268 (1): 5–8. ISSN 0021-9258. PMID 8380166.  
  6. ^ Gupta, K; Anand G, Yin X, Grove L, Prochownik E V (Mar. 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene (ENGLAND) 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. ISSN 0950-9232. PMID 9528857.  
  7. ^ McLoughlin, Patricia; Ehler Elisabeth, Carlile Graeme, Licht Jonathan D, Schäfer Beat W (Oct. 2002). "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". J. Biol. Chem. (United States) 277 (40): 37045–53. doi:10.1074/jbc.M203336200. ISSN 0021-9258. PMID 12145280.  
  8. ^ Ling, Ming-Tat; Chiu Yung-Tuen, Lee Terence Kin Wah, Leung Steve Chin Lung, Fung Maggie Ka Lai, Wang Xianghong, Wong Kwong Fai, Wong Yong-Chuan (Sep. 2008). "Id-1 induces proteasome-dependent degradation of the HBX protein". J. Mol. Biol. (England) 382 (1): 34–43. doi:10.1016/j.jmb.2007.06.020. PMID 18674781.  
  9. ^ Qi, Jie; Su Yongyue, Sun Rongju, Zhang Fang, Luo Xiaofeng, Yang Zongcheng, Luo Xiangdong (Mar. 2005). "CASK inhibits ECV304 cell growth and interacts with Id1". Biochem. Biophys. Res. Commun. (United States) 328 (2): 517–21. doi:10.1016/j.bbrc.2005.01.014. ISSN 0006-291X. PMID 15694377.  

Further reading

  • Zhu W, Dahmen J, Bulfone A, et al. (1995). "Id gene expression during development and molecular cloning of the human Id-1 gene.". Brain Res. Mol. Brain Res. 30 (2): 312–26. PMID 7637581.  
  • Deed RW, Jasiok M, Norton JD (1994). "Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins.". Biochim. Biophys. Acta 1219 (1): 160–2. PMID 8086456.  
  • Mathew S, Chen W, Murty VV, et al. (1996). "Chromosomal assignment of human ID1 and ID2 genes.". Genomics 30 (2): 385–7. doi:10.1006/geno.1995.0037. PMID 8586447.  
  • Nehlin JO, Hara E, Kuo WL, et al. (1997). "Genomic organization, sequence, and chromosomal localization of the human helix-loop-helix Id1 gene.". Biochem. Biophys. Res. Commun. 231 (3): 628–34. doi:10.1006/bbrc.1997.6152. PMID 9070860.  
  • Anand G, Yin X, Shahidi AK, et al. (1997). "Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26 S proteasome.". J. Biol. Chem. 272 (31): 19140–51. PMID 9235903.  
  • Langlands K, Yin X, Anand G, Prochownik EV (1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors.". J. Biol. Chem. 272 (32): 19785–93. PMID 9242638.  
  • Yates PR, Atherton GT, Deed RW, et al. (1999). "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors.". EMBO J. 18 (4): 968–76. doi:10.1093/emboj/18.4.968. PMID 10022839.  
  • Outinen PA, Sood SK, Pfeifer SI, et al. (1999). "Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells.". Blood 94 (3): 959–67. PMID 10419887.  
  • Langlands K, Down GA, Kealey T (2000). "Id proteins are dynamically expressed in normal epidermis and dysregulated in squamous cell carcinoma.". Cancer Res. 60 (21): 5929–33. PMID 11085505.  
  • Ohtani N, Zebedee Z, Huot TJ, et al. (2001). "Opposing effects of Ets and Id proteins on p16INK4a expression during cellular senescence.". Nature 409 (6823): 1067–70. doi:10.1038/35059131. PMID 11234019.  
  • Suzuki H, Fukunishi Y, Kagawa I, et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs.". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMID 11591653.  
  • Korchynskyi O, ten Dijke P (2002). "Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter.". J. Biol. Chem. 277 (7): 4883–91. doi:10.1074/jbc.M111023200. PMID 11729207.  
  • Jögi A, Persson P, Grynfeld A, et al. (2002). "Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation.". J. Biol. Chem. 277 (11): 9118–26. doi:10.1074/jbc.M107713200. PMID 11756408.  
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.  
  • Singh J, Murata K, Itahana Y, Desprez PY (2002). "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.". Oncogene 21 (12): 1812–22. doi:10.1038/sj.onc.1205252. PMID 11896613.  
  • Liu CJ, Ding B, Wang H, Lengyel P (2002). "The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins.". Mol. Cell. Biol. 22 (9): 2893–905. PMID 11940648.  
  • Ouyang XS, Wang X, Ling MT, et al. (2002). "Id-1 stimulates serum independent prostate cancer cell proliferation through inactivation of p16(INK4a)/pRB pathway.". Carcinogenesis 23 (5): 721–5. PMID 12016143.  
  • Ling MT, Wang X, Tsao SW, Wong YC (2002). "Down-regulation of Id-1 expression is associated with TGF beta 1-induced growth arrest in prostate epithelial cells.". Biochim. Biophys. Acta 1570 (3): 145–52. PMID 12020803.  
  • Wang X, Xu K, Ling MT, et al. (2002). "Evidence of increased Id-1 expression and its role in cell proliferation in nasopharyngeal carcinoma cells.". Mol. Carcinog. 35 (1): 42–9. doi:10.1002/mc.10072. PMID 12203366.  

External links

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



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