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Nuclear transcription factor Y, alpha
External IDs OMIM189903 MGI97316 HomoloGene32114 GeneCards: NFYA Gene
RNA expression pattern
PBB GE NFYA 204109 s at tn.png
PBB GE NFYA 204107 at tn.png
PBB GE NFYA 204108 at tn.png
More reference expression data
Species Human Mouse
Entrez 4800 18044
Ensembl ENSG00000001167 ENSMUSG00000023994
UniProt P23511 Q9DBV7
RefSeq (mRNA) NM_002505 NM_010913
RefSeq (protein) NP_002496 NP_035043
Location (UCSC) Chr 6:
41.15 - 41.18 Mb
Chr 17:
47.85 - 47.88 Mb
PubMed search [1] [2]

Nuclear transcription factor Y subunit alpha is a protein that in humans is encoded by the NFYA gene.[1][2]

The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.[3]



NFYA has been shown to interact with Serum response factor[4] and ZHX1.[5][4]


  1. ^ Li XY, Mattei MG, Zaleska-Rutczynska Z, Hooft van Huijsduijnen R, Figueroa F, Nadeau J, Benoist C, Mathis D (Mar 1992). "One subunit of the transcription factor NF-Y maps close to the major histocompatibility complex in murine and human chromosomes". Genomics 11 (3): 630–4. PMID 1774067.  
  2. ^ Maity SN, de Crombrugghe B (Jun 1998). "Role of the CCAAT-binding protein CBF/NF-Y in transcription". Trends Biochem Sci 23 (5): 174–8. PMID 9612081.  
  3. ^ "Entrez Gene: NFYA nuclear transcription factor Y, alpha".  
  4. ^ a b Yamada, K; Osawa H, Granner D K (Oct. 1999). "Identification of proteins that interact with NF-YA". FEBS Lett. (NETHERLANDS) 460 (1): 41–5. ISSN 0014-5793. PMID 10571058.  
  5. ^ Yamada, K; Printz R L, Osawa H, Granner D K (Aug. 1999). "Human ZHX1: cloning, chromosomal location, and interaction with transcription factor NF-Y". Biochem. Biophys. Res. Commun. (UNITED STATES) 261 (3): 614–21. doi:10.1006/bbrc.1999.1087. ISSN 0006-291X. PMID 10441475.  

Further reading

  • Mantovani R (1999). "The molecular biology of the CCAAT-binding factor NF-Y.". Gene 239 (1): 15–27. doi:10.1016/S0378-1119(99)00368-6. PMID 10571030.  
  • Li XY, Mantovani R, Hooft van Huijsduijnen R, et al. (1992). "Evolutionary variation of the CCAAT-binding transcription factor NF-Y.". Nucleic Acids Res. 20 (5): 1087–91. doi:10.1093/nar/20.5.1087. PMID 1549471.  
  • Li XY, Hooft van Huijsduijnen R, Mantovani R, et al. (1992). "Intron-exon organization of the NF-Y genes. Tissue-specific splicing modifies an activation domain.". J. Biol. Chem. 267 (13): 8984–90. PMID 1577736.  
  • Becker DM, Fikes JD, Guarente L (1991). "A cDNA encoding a human CCAAT-binding protein cloned by functional complementation in yeast.". Proc. Natl. Acad. Sci. U.S.A. 88 (5): 1968–72. doi:10.1073/pnas.88.5.1968. PMID 2000400.  
  • Vuorio T, Maity SN, de Crombrugghe B (1991). "Purification and molecular cloning of the "A" chain of a rat heteromeric CCAAT-binding protein. Sequence identity with the yeast HAP3 transcription factor.". J. Biol. Chem. 265 (36): 22480–6. PMID 2266139.  
  • Mantovani R, Li XY, Pessara U, et al. (1994). "Dominant negative analogs of NF-YA.". J. Biol. Chem. 269 (32): 20340–6. PMID 8051128.  
  • Currie RA (1998). "Functional interaction between the DNA binding subunit trimerization domain of NF-Y and the high mobility group protein HMG-I(Y).". J. Biol. Chem. 272 (49): 30880–8. doi:10.1074/jbc.272.49.30880. PMID 9388234.  
  • Currie RA (1998). "Biochemical characterization of the NF-Y transcription factor complex during B lymphocyte development.". J. Biol. Chem. 273 (29): 18220–9. doi:10.1074/jbc.273.29.18220. PMID 9660784.  
  • Roder K, Wolf SS, Larkin KJ, Schweizer M (1999). "Interaction between the two ubiquitously expressed transcription factors NF-Y and Sp1.". Gene 234 (1): 61–9. doi:10.1016/S0378-1119(99)00180-8. PMID 10393239.  
  • Yamada K, Printz RL, Osawa H, Granner DK (1999). "Human ZHX1: cloning, chromosomal location, and interaction with transcription factor NF-Y.". Biochem. Biophys. Res. Commun. 261 (3): 614–21. doi:10.1006/bbrc.1999.1087. PMID 10441475.  
  • Yamada K, Osawa H, Granner DK (1999). "Identification of proteins that interact with NF-YA.". FEBS Lett. 460 (1): 41–5. doi:10.1016/S0014-5793(99)01311-3. PMID 10571058.  
  • Fan W, Jin S, Tong T, et al. (2002). "BRCA1 regulates GADD45 through its interactions with the OCT-1 and CAAT motifs.". J. Biol. Chem. 277 (10): 8061–7. doi:10.1074/jbc.M110225200. PMID 11777930.  
  • Faniello MC, Chirico G, Quaresima B, et al. (2002). "An alternative model of H ferritin promoter transactivation by c-Jun.". Biochem. J. 363 (Pt 1): 53–8. doi:10.1042/0264-6021:3630053. PMID 11903046.  
  • Bevilacqua MA, Faniello MC, Iovine B, et al. (2002). "Transcription factor NF-Y regulates differentiation of CaCo-2 cells.". Arch. Biochem. Biophys. 407 (1): 39–44. doi:10.1016/S0003-9861(02)00436-8. PMID 12392713.  
  • Ge Y, Jensen TL, Matherly LH, Taub JW (2003). "Synergistic regulation of human cystathionine-beta-synthase-1b promoter by transcription factors NF-YA isoforms and Sp1.". Biochim. Biophys. Acta 1579 (2-3): 73–80. PMID 12427542.  
  • 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:10.1073/pnas.242603899. PMID 12477932.  
  • Salsi V, Caretti G, Wasner M, et al. (2003). "Interactions between p300 and multiple NF-Y trimers govern cyclin B2 promoter function.". J. Biol. Chem. 278 (9): 6642–50. doi:10.1074/jbc.M210065200. PMID 12482752.  
  • Peng Y, Jahroudi N (2003). "The NFY transcription factor inhibits von Willebrand factor promoter activation in non-endothelial cells through recruitment of histone deacetylases.". J. Biol. Chem. 278 (10): 8385–94. doi:10.1074/jbc.M213156200. PMID 12511565.  

External links

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



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