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* {{cite journal | vauthors = Kortschak RD, Tucker PW, Saint R | title = ARID proteins come in from the desert | journal = Trends in Biochemical Sciences | volume = 25 | issue = 6 | pages = 294–9 | date = Jun 2000 | pmid = 10838570 | doi = 10.1016/S0968-0004(00)01597-8 }}
* {{cite journal | vauthors = Kortschak RD, Tucker PW, Saint R | title = ARID proteins come in from the desert | journal = Trends in Biochemical Sciences | volume = 25 | issue = 6 | pages = 294–9 | date = Jun 2000 | pmid = 10838570 | doi = 10.1016/S0968-0004(00)01597-8 }}
* {{cite journal | vauthors = Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K | title = A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer | journal = Oncogene | volume = 17 | issue = 7 | pages = 853–65 | date = Aug 1998 | pmid = 9780002 | doi = 10.1038/sj.onc.1202163 }}
* {{cite journal | vauthors = Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K | title = A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer | journal = Oncogene | volume = 17 | issue = 7 | pages = 853–65 | date = Aug 1998 | pmid = 9780002 | doi = 10.1038/sj.onc.1202163 }}
* {{cite journal | vauthors = Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R | title = A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence | journal = Nature Cell Biology | volume = 4 | issue = 2 | pages = 148–53 | date = Feb 2002 | pmid = 11812999 | doi = 10.1038/ncb742 }}
* {{cite journal | vauthors = Peeper DS, Shvarts A, Brummelkamp T, Douma S, Koh EY, Daley GQ, Bernards R | title = A functional screen identifies hDRIL1 as an oncogene that rescues RAS-induced senescence | journal = Nature Cell Biology | volume = 4 | issue = 2 | pages = 148–53 | date = Feb 2002 | pmid = 11812999 | doi = 10.1038/ncb742 | hdl = 1874/15575 }}
* {{cite journal | vauthors = Kaiwen M | title = [Involvement of E2FBP1, an ARID family member protein, in the p53 regulatory pathway] | journal = Kōkūbyō Gakkai Zasshi. The Journal of the Stomatological Society, Japan | volume = 69 | issue = 2 | pages = 152–61 | date = Jun 2002 | pmid = 12136662 | doi = 10.5357/koubyou.69.152 }}
* {{cite journal | vauthors = Kaiwen M | title = [Involvement of E2FBP1, an ARID family member protein, in the p53 regulatory pathway] | journal = Kōkūbyō Gakkai Zasshi. The Journal of the Stomatological Society, Japan | volume = 69 | issue = 2 | pages = 152–61 | date = Jun 2002 | pmid = 12136662 | doi = 10.5357/koubyou.69.152 }}
* {{cite journal | vauthors = Goebel P, Montalbano A, Ayers N, Kompfner E, Dickinson L, Webb CF, Feeney AJ | title = 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 | journal = Journal of Immunology | volume = 169 | issue = 5 | pages = 2477–87 | date = Sep 2002 | pmid = 12193717 | doi = 10.4049/jimmunol.169.5.2477 }}
* {{cite journal | vauthors = Goebel P, Montalbano A, Ayers N, Kompfner E, Dickinson L, Webb CF, Feeney AJ | title = 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 | journal = Journal of Immunology | volume = 169 | issue = 5 | pages = 2477–87 | date = Sep 2002 | pmid = 12193717 | doi = 10.4049/jimmunol.169.5.2477 }}

Revision as of 13:21, 30 June 2019

ARID3A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesARID3A, BRIGHT, DRIL1, DRIL3, E2FBP1, AT-rich interaction domain 3A
External IDsOMIM: 603265; MGI: 1328360; HomoloGene: 124247; GeneCards: ARID3A; OMA:ARID3A - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005224

NM_001288625
NM_001288626
NM_007880

RefSeq (protein)

NP_005215

NP_001275554
NP_001275555
NP_031906

Location (UCSC)Chr 19: 0.93 – 0.98 MbChr 10: 79.76 – 79.79 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

AT-rich interactive domain-containing protein 3A is a protein that in humans is encoded by the ARID3A gene.[5][6]

Function

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.[6]

Interactions

ARID3A has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116017Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019564Ensembl, 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. ^ Kortschak RD, Reimann H, Zimmer M, Eyre HJ, Saint R, Jenne DE (Jul 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:10.1006/geno.1998.5259. PMID 9722953.
  6. ^ a b "Entrez Gene: ARID3A AT rich interactive domain 3A (BRIGHT-like)".
  7. ^ Nixon JC, Rajaiya JB, Ayers N, Evetts S, Webb CF (Mar 2004). "The transcription factor, Bright, is not expressed in all human B lymphocyte subpopulations". Cellular Immunology. 228 (1): 42–53. doi:10.1016/j.cellimm.2004.03.004. PMID 15203319.
  8. ^ Suzuki M, Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K (Aug 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:10.1038/sj.onc.1202163. PMID 9780002.

Further reading

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