ARID3A
From Wikipedia, the free encyclopedia
AT rich interactive domain 3A (BRIGHT-like)
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Identifiers | ||||||||||||||
Symbol(s) | ARID3A; BRIGHT; DRIL1; DRIL3; E2FBP1 | |||||||||||||
External IDs | OMIM: 603265 MGI: 1328360 HomoloGene: 3827 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 1820 | 13496 | ||||||||||||
Ensembl | ENSG00000116017 | ENSMUSG00000019564 | ||||||||||||
Uniprot | Q99856 | Q3U338 | ||||||||||||
Refseq | NM_005224 (mRNA) NP_005215 (protein) |
NM_007880 (mRNA) NP_031906 (protein) |
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Location | Chr 19: 0.88 - 0.92 Mb | Chr 10: 79.33 - 79.36 Mb | ||||||||||||
Pubmed search | [1] | [2] |
AT rich interactive domain 3A (BRIGHT-like), also known as ARID3A, is a human gene.[1]
This gene encodes a member of the ARID (AT-rich interaction domain) family of DNA binding proteins. It was found by homology to the Drosophila dead ringer gene, which is important for normal embryogenesis. Other ARID family members have roles in embryonic patterning, cell lineage gene regulation, cell cycle control, transcriptional regulation, and possibly in chromatin structure modification.[1]
[edit] References
[edit] Further reading
- Kortschak RD, Tucker PW, Saint R (2000). "ARID proteins come in from the desert.". Trends Biochem. Sci. 25 (6): 294–9. PMID 10838570.
- Kortschak RD, Reimann H, Zimmer M, et al. (1998). "The human dead ringer/bright homolog, DRIL1: cDNA cloning, gene structure, and mapping to D19S886, a marker on 19p13.3 that is strictly linked to the Peutz-Jeghers syndrome.". Genomics 51 (2): 288–92. doi: . PMID 9722953.
- Suzuki M, Okuyama S, Okamoto S, et al. (1998). "A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer.". Oncogene 17 (7): 853–65. doi: . PMID 9780002.
- Peeper DS, Shvarts A, Brummelkamp T, et al. (2002). "A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence.". Nat. Cell Biol. 4 (2): 148–53. doi: . PMID 11812999.
- Kaiwen M (2002). "[Involvement of E2FBP1, an ARID family member protein, in the p53 regulatory pathway]". Kokubyo Gakkai Zasshi 69 (2): 152–61. PMID 12136662.
- Goebel P, Montalbano A, Ayers N, et al. (2002). "High frequency of matrix attachment regions and cut-like protein x/CCAAT-displacement protein and B cell regulator of IgH transcription binding sites flanking Ig V region genes.". J. Immunol. 169 (5): 2477–87. PMID 12193717.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: . PMID 12477932.
- Ma K, Araki K, Ichwan SJ, et al. (2004). "E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53.". Mol. Cancer Res. 1 (6): 438–44. PMID 12692263.
- Fukuyo Y, Mogi K, Tsunematsu Y, Nakajima T (2005). "E2FBP1/hDril1 modulates cell growth through downregulation of promyelocytic leukemia bodies.". Cell Death Differ. 11 (7): 747–59. doi: . PMID 15017387.
- Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529–35. doi: . PMID 15057824.
- Nixon JC, Rajaiya JB, Ayers N, et al. (2004). "The transcription factor, Bright, is not expressed in all human B lymphocyte subpopulations.". Cell. Immunol. 228 (1): 42–53. doi: . PMID 15203319.
- Rajaiya J, Nixon JC, Ayers N, et al. (2006). "Induction of immunoglobulin heavy-chain transcription through the transcription factor Bright requires TFII-I.". Mol. Cell. Biol. 26 (12): 4758–68. doi: . PMID 16738337.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi: . PMID 17081983.
- Lin D, Ippolito GC, Zong RT, et al. (2007). "Bright/ARID3A contributes to chromatin accessibility of the immunoglobulin heavy chain enhancer.". Mol. Cancer 6: 23. doi: . PMID 17386101.
[edit] External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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