ID1

This article is about the protein. For other uses, see ID1 (disambiguation).

ID1
Identifiers
Aliases	ID1 , ID, bHLHb24, inhibitor of DNA binding 1, HLH protein
External IDs	OMIM: 600349; MGI: 96396; HomoloGene: 1631; GeneCards: ID1; OMA:ID1 - orthologs
Gene location (Human) Chr. Chromosome 20 (human) [1] Band 20q11.21 Start 31,605,283 bp [1] End 31,606,515 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2 H1|2 75.41 cM Start 152,578,171 bp [2] End 152,579,330 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in seminal vesicula right lung right lobe of thyroid gland olfactory zone of nasal mucosa left lobe of thyroid gland left uterine tube tail of epididymis mucosa of transverse colon gastric mucosa apex of heart Top expressed in mucous cell of stomach epithelium of stomach optic nerve maxillary prominence choroid plexus of fourth ventricle hand molar mandibular prominence pyloric antrum right lung More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity protein dimerization activity DNA-binding transcription factor activity protein self-association protein C-terminus binding protein binding DNA-binding transcription factor activity, RNA polymerase II-specific transcription factor binding protein N-terminus binding proteasome binding Cellular component cytoplasm centrosome Golgi apparatus nucleoplasm nucleus Biological process cell-abiotic substrate adhesion cellular response to transforming growth factor beta stimulus cellular response to nerve growth factor stimulus cellular response to peptide regulation of transcription, DNA-templated regulation of MAPK cascade blood vessel morphogenesis lung morphogenesis response to organic cyclic compound blood vessel endothelial cell migration positive regulation of epithelial cell proliferation rhythmic process cellular response to dopamine response to antibiotic negative regulation of DNA binding endothelial cell morphogenesis collagen metabolic process negative regulation of apoptotic process negative regulation of endothelial cell differentiation negative regulation of transcription by RNA polymerase II regulation of angiogenesis negative regulation of protein binding BMP signaling pathway negative regulation of DNA-binding transcription factor activity transcription, DNA-templated negative regulation of osteoblast differentiation negative regulation of gene expression cellular response to epidermal growth factor stimulus multicellular organism development development of the heart brain development positive regulation of gene expression regulation of vasculature development negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding negative regulation of dendrite morphogenesis circadian rhythm protein destabilization angiogenesis neuron differentiation negative regulation of protein homodimerization activity positive regulation of actin filament bundle assembly negative regulation of transcription by transcription factor localization lung vasculature development negative regulation of transcription, DNA-templated transforming growth factor beta receptor signaling pathway negative regulation of neuron differentiation regulation of cell cycle negative regulation of cold-induced thermogenesis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3397 15901 Ensembl ENSG00000125968 ENSMUSG00000042745 UniProt P41134 P20067 Q6GTZ3 RefSeq (mRNA) NM_181353 NM_002165 NM_010495 NM_001355113 NM_001369018 RefSeq (protein) NP_002156 NP_851998 NP_034625 NP_001342042 NP_001355947 Location (UCSC) Chr 20: 31.61 – 31.61 Mb Chr 2: 152.58 – 152.58 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

DNA-binding protein inhibitor ID-1 is a protein that in humans is encoded by the ID1 gene. ^{[5] [6]}

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. ^[5] 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. ^[5] This protein may play a role in cell growth, senescence, and differentiation. ^{[7] [8] [9]} Two transcript variants encoding different isoforms have been found for this gene. ^[10]

Interactions

ID1 has been shown to interact weakly with MyoD ^{[5] [11] [12] [13] [14] [15] [16]} but very tightly with ubiquitously expressed E proteins. ^[17] 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. ^[18]

Clinical significance

ID1 can be used to mark endothelial progenitor cells which are critical to tumor growth and angiogenesis. ^{[19] [20]} Targeting ID1 results in decreased tumor growth. ^{[21] [22]} ID1 has been shown to be targeted by cannabidiol in certain gliomas and breast cancers. ^{[23] [24]}

See also

• Inhibitor of DNA-binding protein

References

1. GRCh38: Ensembl release 89: ENSG00000125968 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000042745 – 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.
5. Benezra R, Davis RL, Lockshon D, Turner DL, Weintraub H (April 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. S2CID   29514374.
6. Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, Oda K (January 1994). "Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts". The Journal of Biological Chemistry. 269 (3): 2139–45. doi: 10.1016/S0021-9258(17)42146-6 . PMID   8294468.
7. Ruzinova MB, Benezra R (August 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.
8. Perk J, Iavarone A, Benezra R (August 2005). "Id family of helix-loop-helix proteins in cancer". Nature Reviews. Cancer. 5 (8): 603–14. doi:10.1038/nrc1673. PMID   16034366. S2CID   19850793.
9. Cunningham TJ, Yu MS, McKeithan WL, Spiering S, Carrette F, Huang CT, et al. (July 2017). "Id genes are essential for early heart formation". Genes & Development. 31 (13): 1325–1338. doi:10.1101/gad.300400.117. PMC   5580654 . PMID   28794185.
10. "Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein".
11. 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. Bibcode:2004Natur.428..328G. doi:10.1038/nature02329. PMID   15029197. S2CID   4427531.
12. Langlands K, Yin X, Anand G, Prochownik EV (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". The Journal of Biological Chemistry. 272 (32): 19785–93. doi: 10.1074/jbc.272.32.19785 . PMID   9242638.
13. Finkel T, Duc J, Fearon ER, Dang CV, Tomaselli GF (January 1993). "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". The Journal of Biological Chemistry. 268 (1): 5–8. doi: 10.1016/S0021-9258(18)54105-3 . PMID   8380166.
14. 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.
15. 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". The Journal of Biological Chemistry. 277 (40): 37045–53. doi: 10.1074/jbc.M203336200 . PMID   12145280.
16. 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". Journal of Molecular Biology. 382 (1): 34–43. doi:10.1016/j.jmb.2007.06.020. PMID   18674781.
17. 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 & Development. 6 (8): 1466–79. doi: 10.1101/gad.6.8.1466 . PMID   1644289.
18. 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". Biochemical and Biophysical Research Communications. 328 (2): 517–21. Bibcode:2005BBRC..328..517Q. doi:10.1016/j.bbrc.2005.01.014. PMID   15694377.
19. 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. Bibcode:1999Natur.401..670L. doi:10.1038/44334. PMID   10537105. S2CID   4396535.
20. 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". Nature Medicine. 7 (11): 1194–201. doi:10.1038/nm1101-1194. PMID   11689883. S2CID   12961562.
21. 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". Nature Biotechnology. 26 (1): 91–100. doi:10.1038/nbt1366. PMID   18176556. S2CID   205273623.
22. 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 tumor angiogenesis and growth". Cancer Research. 70 (18): 7273–82. doi:10.1158/0008-5472.CAN-10-1142. PMC   3058751 . PMID   20807818.
23. Yadav VN, Harris MK, Messinger D, Thomas C, Cummings JR, Yang T, Woo R, Siddaway R, Burkert M, Stallard S, Qin T (June 2021). "Therapeutic reversal of prenatal pontine ID1 signaling in DIPG". Neuro Oncol. 23 (supplement 1): i48. doi:10.1093/neuonc/noab090.193. PMC   8168201 .
24. McAllister SD, Christian RT, Horowitz MP, Garcia A, Desprez PY (November 2007). "Cannabidiol as a novel inhibitor of Id-1 gene expression in aggressive breast cancer cells". Molecular Cancer Therapeutics. 6 (11): 2921–7. doi: 10.1158/1535-7163.MCT-07-0371 . PMID   18025276. S2CID   2192838.

Further reading

• Zhu W, Dahmen J, Bulfone A, Rigolet M, Hernandez MC, Kuo WL, et al. (June 1995). "Id gene expression during development and molecular cloning of the human Id-1 gene". Brain Research. Molecular Brain Research. 30 (2): 312–26. doi:10.1016/0169-328X(95)00017-M. PMID   7637581.
• Deed RW, Jasiok M, Norton JD (September 1994). "Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1219 (1): 160–2. doi:10.1016/0167-4781(94)90261-5. PMID   8086456.
• Mathew S, Chen W, Murty VV, Benezra R, Chaganti RS (November 1995). "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, Collins C, Campisi J (February 1997). "Genomic organization, sequence, and chromosomal localization of the human helix-loop-helix Id1 gene". Biochemical and Biophysical Research Communications. 231 (3): 628–34. Bibcode:1997BBRC..231..628N. doi:10.1006/bbrc.1997.6152. PMID   9070860.
• Anand G, Yin X, Shahidi AK, Grove L, Prochownik EV (August 1997). "Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26 S proteasome". The Journal of Biological Chemistry. 272 (31): 19140–51. doi: 10.1074/jbc.272.31.19140 . PMID   9235903.
• Langlands K, Yin X, Anand G, Prochownik EV (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". The Journal of Biological Chemistry. 272 (32): 19785–93. doi: 10.1074/jbc.272.32.19785 . PMID   9242638.
• Yates PR, Atherton GT, Deed RW, Norton JD, Sharrocks AD (February 1999). "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors". The EMBO Journal. 18 (4): 968–76. doi:10.1093/emboj/18.4.968. PMC   1171189 . PMID   10022839.
• Outinen PA, Sood SK, Pfeifer SI, Pamidi S, Podor TJ, Li J, et al. (August 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. doi:10.1182/blood.V94.3.959.415k20_959_967. PMID   10419887.
• Langlands K, Down GA, Kealey T (November 2000). "Id proteins are dynamically expressed in normal epidermis and dysregulated in squamous cell carcinoma". Cancer Research. 60 (21): 5929–33. PMID   11085505.
• Ohtani N, Zebedee Z, Huot TJ, Stinson JA, Sugimoto M, Ohashi Y, et al. (February 2001). "Opposing effects of Ets and Id proteins on p16INK4a expression during cellular senescence". Nature. 409 (6823): 1067–70. Bibcode:2001Natur.409.1067O. doi:10.1038/35059131. PMID   11234019. S2CID   4352931.
• Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, et al. (October 2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Research. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC   311163 . PMID   11591653.
• Korchynskyi O, ten Dijke P (February 2002). "Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter". The Journal of Biological Chemistry. 277 (7): 4883–91. doi: 10.1074/jbc.M111023200 . PMID   11729207.
• Jögi A, Persson P, Grynfeld A, Påhlman S, Axelson H (March 2002). "Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation". The Journal of Biological Chemistry. 277 (11): 9118–26. doi: 10.1074/jbc.M107713200 . PMID   11756408.
• Singh J, Murata K, Itahana Y, Desprez PY (March 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 (May 2002). "The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins". Molecular and Cellular Biology. 22 (9): 2893–905. doi:10.1128/MCB.22.9.2893-2905.2002. PMC   133750 . PMID   11940648.
• Ouyang XS, Wang X, Ling MT, Wong HL, Tsao SW, Wong YC (May 2002). "Id-1 stimulates serum independent prostate cancer cell proliferation through inactivation of p16(INK4a)/pRB pathway". Carcinogenesis. 23 (5): 721–5. doi: 10.1093/carcin/23.5.721 . PMID   12016143.
• Ling MT, Wang X, Tsao SW, Wong YC (April 2002). "Down-regulation of Id-1 expression is associated with TGF beta 1-induced growth arrest in prostate epithelial cells". Biochimica et Biophysica Acta (BBA) - General Subjects. 1570 (3): 145–52. doi:10.1016/S0304-4165(02)00189-7. PMID   12020803.
• Wang X, Xu K, Ling MT, Wong YC, Feng HC, Nicholls J, Tsao SW (September 2002). "Evidence of increased Id-1 expression and its role in cell proliferation in nasopharyngeal carcinoma cells". Molecular Carcinogenesis. 35 (1): 42–9. doi:10.1002/mc.10072. PMID   12203366. S2CID   33701077.

External links

• ID1+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 : P20067 (Mouse DNA-binding protein inhibitor ID-1) at the PDBe-KB .

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