ID1

ID1
Identifiers
Aliases	ID1, ID, bHLHb24, inhibitor of DNA binding 1, HLH protein
External IDs	OMIM: 600349 MGI: 96396 HomoloGene: 1631 GeneCards: ID1
Gene location (Human)
Chr.	Chromosome 20 (human)[1]
End	31,606,515 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	152,737,410 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• protein homodimerization activity; • protein dimerization activity; • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity; • protein self-association; • protein C-terminus binding; • GO:0001948 protein binding; • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific; • transcription factor binding; • protein N-terminus binding; • proteasome binding; • RNA polymerase II transcription factor binding;
Cellular component	• cytoplasm; • centrosome; • Golgi apparatus; • nucleoplasm; • cell 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 from RNA polymerase II promoter; • regulation of angiogenesis; • negative regulation of protein binding; • BMP signaling pathway; • negative regulation of sequence-specific 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; • heart development; • 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
	3397
	15901
	ENSG00000125968
	ENSMUSG00000042745
	P41134
	P20067; Q6GTZ3
	NM_181353; NM_002165
	NM_010495; NM_001355113; NM_001369018
	NP_002156; NP_851998
	NP_034625; NP_001342042; NP_001355947
	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]

References

GRCh38: Ensembl release 89: ENSG00000125968 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000042745 - 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.
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.
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.
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.
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.
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. PMC 5580654. PMID 28794185.
"Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein".
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.

External links

ID1+protein,+human at the US 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.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000125968 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[HalId-5] 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.

[pmid8294468-6] 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.

[7] 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.

[8] 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.

[9] 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. PMC 5580654. PMID 28794185.

[10] "Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein".

[pmid15029197-11] 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.

[pmid9242638-12] 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.

[pmid8380166-13] Finkel T, Duc J, Fearon ER, Dang CV, Tomaselli GF (January 1993). "Detection and modulation in vivo of helix-loop-helix protein-protein interactions". J. Biol. Chem. 268 (1): 5–8. PMID 8380166.

[pmid9528857-14] 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.

[pmid12145280-15] 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". J. Biol. Chem. 277 (40): 37045–53. doi:10.1074/jbc.M203336200. PMID 12145280.

[pmid18674781-16] 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.

[pmid1644289-17] 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 Dev. 6 (8): 1466–79. doi:10.1101/gad.6.8.1466. PMID 1644289.

[pmid15694377-18] 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". Biochem. Biophys. Res. Commun. 328 (2): 517–21. doi:10.1016/j.bbrc.2005.01.014. PMID 15694377.

[pmid10537105-19] 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.

[pmid11689883-20] 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.

[pmid18176556-21] 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.

[pmid20807818-22] 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.

ID1

Function

Interactions

Clinical significance

See also

References

Further reading

External links