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This article is about the protein. For other uses, see ID1 (disambiguation).
Inhibitor of DNA binding 1, dominant negative helix-loop-helix protein
Symbols ID1 ; ID; bHLHb24
External IDs OMIM600349 MGI96396 HomoloGene1631 ChEMBL: 1075116 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:
30.19 – 30.19 Mb
Chr 2:
152.74 – 152.74 Mb
PubMed search [1] [2]

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


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] Two transcript variants encoding different isoforms have been found for this gene.[5]


ID1 has been shown to interact weakly with MyoD[1][6][7][8][9][10][11] but very tightly with ubiquitously expressed E proteins.[12] 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.[13]

Clinical significance[edit]

ID1 can be used to mark endothelial progenitor cells which are critical to tumor growth and angiogenesis.[14][15] Targeting ID1 results in decreased tumor growth.[16][17]

See also[edit]


  1. ^ a b c d 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 et al. (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. ^ "Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein". 
  6. ^ Garkavtsev I, Kozin SV, Chernova O, Xu L, Winkler F, Brown E et al. (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. 
  7. ^ 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. 
  8. ^ 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. 
  9. ^ 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. 
  10. ^ 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. 
  11. ^ Ling MT, Chiu YT, Lee TK, Leung SC, Fung MK, Wang X et al. (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. 
  12. ^ 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. 
  13. ^ Qi J, Su Y, Sun R, Zhang F, Luo X, Yang Z et al. (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. 
  14. ^ Lyden D, Young AZ, Zagzag D, Yan W, Gerald W, O'Reilly R et al. (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. 
  15. ^ Lyden D, Hattori K, Dias S, Costa C, Blaikie P, Butros L et al. (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. 
  16. ^ Henke E, Perk J, Vider J, de Candia P, Chin Y, Solit DB et al. (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. 
  17. ^ Mellick AS, Plummer PN, Nolan DJ, Gao D, Bambino K, Hahn M et al. (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[edit]

External links[edit]

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