FOXA3

Protein-coding gene in the species Homo sapiens
FOXA3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1VTN

Identifiers
AliasesFOXA3, FKHH3, HNF3G, TCF3G, forkhead box A3
External IDsOMIM: 602295 MGI: 1347477 HomoloGene: 3308 GeneCards: FOXA3
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for FOXA3
Genomic location for FOXA3
Band19q13.32Start45,863,989 bp[1]
End45,873,797 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for FOXA3
Genomic location for FOXA3
Band7 A3|7 9.46 cMStart18,747,209 bp[2]
End18,757,463 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • pancreatic ductal cell

  • body of pancreas

  • rectum

  • islet of Langerhans

  • palpebral conjunctiva

  • body of stomach

  • duodenum

  • tibia

  • pylorus
Top expressed in
  • mucous cell of stomach

  • crypt of lieberkuhn of small intestine

  • epithelium of stomach

  • pyloric antrum

  • liver

  • left lobe of liver

  • large intestine

  • left colon

  • yolk sac

  • Hindgut
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • sequence-specific DNA binding
  • DNA binding
  • transcription factor binding
  • protein domain specific binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • nucleoplasm
  • actin cytoskeleton
  • nucleus
Biological process
  • cellular glucose homeostasis
  • regulation of transcription by RNA polymerase II
  • cellular response to starvation
  • multicellular organism development
  • regulation of transcription, DNA-templated
  • transcription, DNA-templated
  • spermatogenesis
  • positive regulation of transcription by RNA polymerase II
  • anatomical structure morphogenesis
  • cell differentiation
  • chromatin organization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3171

15377

Ensembl

ENSG00000170608

ENSMUSG00000040891

UniProt

P55318

P35584

RefSeq (mRNA)

NM_004497

NM_008260

RefSeq (protein)

NP_004488

NP_032286

Location (UCSC)Chr 19: 45.86 – 45.87 MbChr 7: 18.75 – 18.76 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Hepatocyte nuclear factor 3-gamma (HNF-3G), also known as forkhead box protein A3 (FOXA3) or transcription factor 3G (TCF-3G) is a protein that in humans is encoded by the FOXA3 gene.[5][6]

Function

HNF-3G is a member of the forkhead class of DNA-binding proteins. These hepatocyte nuclear factors are transcriptional activators for liver-specific transcripts such as albumin and transthyretin, and they also interact with chromatin. Similar family members in mice have roles in the regulation of metabolism and in the differentiation of the pancreas and liver.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000170608 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040891 – 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. ^ a b "Entrez Gene: forkhead box A3".
  6. ^ Mincheva A, Lichter P, Schütz G, Kaestner KH (February 1997). "Assignment of the human genes for hepatocyte nuclear factor 3-alpha, -beta, and -gamma (HNF3A, HNF3B, HNF3G) to 14q12-q13, 20p11, and 19q13.2-q13.4". Genomics. 39 (3): 417–9. doi:10.1006/geno.1996.4477. PMID 9119385.

Further reading

  • Corrocher R, Tedesco F, Rabusin P, De Sandre G (1975). "Effect of human erythrocyte stromata on complement activation". Br. J. Haematol. 29 (2): 235–41. doi:10.1111/j.1365-2141.1975.tb01817.x. PMID 33. S2CID 45491647.
  • Verschuur M, de Jong M, Felida L, et al. (2005). "A hepatocyte nuclear factor-3 site in the fibrinogen beta promoter is important for interleukin 6-induced expression, and its activity is influenced by the adjacent -148C/T polymorphism" (PDF). J. Biol. Chem. 280 (17): 16763–71. doi:10.1074/jbc.M501973200. PMID 15737987.
  • Clark KL, Halay ED, Lai E, Burley SK (1993). "Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5". Nature. 364 (6436): 412–20. Bibcode:1993Natur.364..412C. doi:10.1038/364412a0. PMID 8332212. S2CID 4363526.
  • Qian X, Costa RH (1995). "Analysis of hepatocyte nuclear factor-3 beta protein domains required for transcriptional activation and nuclear targeting". Nucleic Acids Res. 23 (7): 1184–91. doi:10.1093/nar/23.7.1184. PMC 306829. PMID 7739897.
  • Rodríguez-Antona C, Bort R, Jover R, et al. (2003). "Transcriptional regulation of human CYP3A4 basal expression by CCAAT enhancer-binding protein alpha and hepatocyte nuclear factor-3 gamma". Mol. Pharmacol. 63 (5): 1180–9. doi:10.1124/mol.63.5.1180. PMID 12695546. S2CID 34628968.
  • Lamba V, Panetta JC, Strom S, Schuetz EG (2010). "Genetic predictors of interindividual variability in hepatic CYP3A4 expression". J. Pharmacol. Exp. Ther. 332 (3): 1088–99. doi:10.1124/jpet.109.160804. PMC 2835441. PMID 19934400.
  • Hori Y, Gu X, Xie X, Kim SK (2005). "Differentiation of insulin-producing cells from human neural progenitor cells". PLOS Med. 2 (4): e103. doi:10.1371/journal.pmed.0020103. PMC 1087208. PMID 15839736.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Motallebipour M, Ameur A, Reddy Bysani MS, et al. (2009). "Differential binding and co-binding pattern of FOXA1 and FOXA3 and their relation to H3K4me3 in HepG2 cells revealed by ChIP-seq". Genome Biol. 10 (11): R129. doi:10.1186/gb-2009-10-11-r129. PMC 3091322. PMID 19919681.
  • Zhou B, Zhong Q, Minoo P, et al. (2008). "Foxp2 inhibits Nkx2.1-mediated transcription of SP-C via interactions with the Nkx2.1 homeodomain". Am. J. Respir. Cell Mol. Biol. 38 (6): 750–8. doi:10.1165/rcmb.2007-0350OC. PMC 2396252. PMID 18239190.
  • Navas MA, Vaisse C, Boger S, et al. (2000). "The human HNF-3 genes: cloning, partial sequence and mutation screening in patients with impaired glucose homeostasis". Hum. Hered. 50 (6): 370–81. doi:10.1159/000022943. PMID 10899756. S2CID 24745151.
  • Kaestner KH (2000). "The hepatocyte nuclear factor 3 (HNF3 or FOXA) family in metabolism". Trends Endocrinol. Metab. 11 (7): 281–5. doi:10.1016/S1043-2760(00)00271-X. PMID 10920385. S2CID 40600315.
  • Lin B, Morris DW, Chou JY (1997). "The role of HNF1alpha, HNF3gamma, and cyclic AMP in glucose-6-phosphatase gene activation". Biochemistry. 36 (46): 14096–106. doi:10.1021/bi9703249. PMID 9369482.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Dintilhac A, Bernués J (2002). "HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences". J. Biol. Chem. 277 (9): 7021–8. doi:10.1074/jbc.M108417200. hdl:10261/112516. PMID 11748221.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Kaestner KH, Hiemisch H, Schütz G (1998). "Targeted disruption of the gene encoding hepatocyte nuclear factor 3gamma results in reduced transcription of hepatocyte-specific genes". Mol. Cell. Biol. 18 (7): 4245–51. doi:10.1128/mcb.18.7.4245. PMC 109008. PMID 9632808.
  • Hromas R, Moore J, Johnston T, et al. (1993). "Drosophila forkhead homologues are expressed in a lineage-restricted manner in human hematopoietic cells". Blood. 81 (11): 2854–9. doi:10.1182/blood.V81.11.2854.2854. PMID 8499623.

External links

  • Overview of all the structural information available in the PDB for UniProt: P55318 (Hepatocyte nuclear factor 3-gamma) at the PDBe-KB.

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

  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies