NFYA

Nuclear transcription factor Y, alpha
Identifiers
Symbols	NFYA; CBF-A; CBF-B; FLJ11236; HAP2; NF-YA
External IDs	OMIM: 189903 MGI: 97316 HomoloGene: 32114 GeneCards: NFYA Gene
Gene Ontology Molecular function • DNA binding • sequence-specific DNA binding transcription factor activity • protein binding Cellular component • nucleus • CCAAT-binding factor complex Biological process • regulation of transcription, DNA-dependent • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter • positive regulation of transcription from RNA polymerase II promoter Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4800	18044
Ensembl	ENSG00000001167	ENSMUSG00000023994
UniProt	P23511	Q9DBV7
RefSeq (mRNA)	NM_002505.4	NM_010913
RefSeq (protein)	NP_002496.1	NP_035043
Location (UCSC)	Chr 6: 41.04 – 41.07 Mb	Chr 17: 48.53 – 48.55 Mb
PubMed search	[1]	[2]

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

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.

Interactions

NFYA has been shown to interact with Serum response factor and ZHX1.

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. PMC 312095. PMID 1549471. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=312095. 
• 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. PMC 51147. PMID 2000400. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=51147. 
• 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. PMC 1222450. PMID 11903046. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222450. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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

• MeSH NFYA+protein,+human
• FactorBook NF-YA

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