NFYB

Nuclear transcription factor Y, beta
PDB rendering based on 1n1j.
Available structures PDB 1n1j
Identifiers
Symbols	NFYB; CBF-A; CBF-B; HAP3; NF-YB
External IDs	OMIM: 189904 MGI: 97317 HomoloGene: 38149 GeneCards: NFYB Gene
Gene Ontology Molecular function • DNA binding • sequence-specific DNA binding transcription factor activity • protein binding • sequence-specific DNA binding • repressing transcription factor binding Cellular component • intracellular • nucleus • CCAAT-binding factor complex Biological process • transcription, DNA-dependent • regulation of transcription, DNA-dependent • regulation of transcription, DNA-dependent • positive regulation of transcription, DNA-dependent Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4801	18045
Ensembl	ENSG00000120837	ENSMUSG00000020248
UniProt	P25208	Q8C590
RefSeq (mRNA)	NM_006166.3	NM_010914.2
RefSeq (protein)	NP_006157.1	NP_035044.1
Location (UCSC)	Chr 12: 104.51 – 104.53 Mb	Chr 10: 82.21 – 82.23 Mb
PubMed search	[1]	[2]

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

The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions in a variety of genes. This gene product, subunit B, forms a tight dimer with the C subunit, a prerequisite for subunit A association. The resulting trimer binds to DNA with high specificity and affinity. Subunits B and C each contain a histone-like motif. Observation of the histone nature of these subunits is supported by two types of evidence; protein sequence alignments and experiments with mutants.^[3]

Interactions

NFYB has been shown to interact with CCAAT/enhancer binding protein zeta,^[4] CNTN2,^[5] TATA binding protein^[6] and Myc.^[7]

References

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. doi:10.1016/0888-7543(91)90070-U. 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. doi:10.1016/S0968-0004(98)01201-8. PMID 9612081. 
3. ^ "Entrez Gene: NFYB nuclear transcription factor Y, beta". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4801. 
4. ^ Imbriano, C; Bolognese F, Gurtner A, Piaggio G, Mantovani R (Jul. 2001). "HSP-CBF is an NF-Y-dependent coactivator of the heat shock promoters CCAAT boxes". J. Biol. Chem. (United States) 276 (28): 26332–9. doi:10.1074/jbc.M101553200. ISSN 0021-9258. PMID 11306579. 
5. ^ Pise-Masison, C A; Dittmer J, Clemens K E, Brady J N (Mar. 1997). "Physical and functional interaction between the human T-cell lymphotropic virus type 1 Tax1 protein and the CCAAT binding protein NF-Y". Mol. Cell. Biol. (UNITED STATES) 17 (3): 1236–43. ISSN 0270-7306. PMC 231848. PMID 9032250. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231848. 
6. ^ Bellorini, M; Lee D K, Dantonel J C, Zemzoumi K, Roeder R G, Tora L, Mantovani R (Jun. 1997). "CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues". Nucleic Acids Res. (ENGLAND) 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. ISSN 0305-1048. PMC 146709. PMID 9153318. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=146709. 
7. ^ Izumi, H; Molander C, Penn L Z, Ishisaki A, Kohno K, Funa K (Apr. 2001). "Mechanism for the transcriptional repression by c-Myc on PDGF beta-receptor". J. Cell. Sci. (England) 114 (Pt 8): 1533–44. ISSN 0021-9533. PMID 11282029. 

Further reading

• Lloberas J, Soler C, Celada A (1998). "Repression mechanisms of the I-A beta gene of the major histocompatibility complex.". Immunobiology 198 (1–3): 249–63. PMID 9442396. 
• 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. 
• Lloberas J, Maki RA, Celada A (1995). "Repression of major histocompatibility complex I-A beta gene expression by dbpA and dbpB (mYB-1) proteins". Mol. Cell. Biol. 15 (9): 5092–9. PMC 230756. PMID 7651426. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230756. 
• Chang ZF, Liu CJ (1994). "Human thymidine kinase CCAAT-binding protein is NF-Y, whose A subunit expression is serum-dependent in human IMR-90 diploid fibroblasts". J. Biol. Chem. 269 (27): 17893–8. PMID 8027044. 
• Mantovani R, Li XY, Pessara U, et al. (1994). "Dominant negative analogs of NF-YA". J. Biol. Chem. 269 (32): 20340–6. PMID 8051128. 
• Pise-Masison CA, Dittmer J, Clemens KE, Brady JN (1997). "Physical and functional interaction between the human T-cell lymphotropic virus type 1 Tax1 protein and the CCAAT binding protein NF-Y". Mol. Cell. Biol. 17 (3): 1236–43. PMC 231848. PMID 9032250. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231848. 
• Bellorini M, Lee DK, Dantonel JC, et al. (1997). "CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues". Nucleic Acids Res. 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. PMC 146709. PMID 9153318. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=146709. 
• 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). "NF-Y is associated with the histone acetyltransferases GCN5 and P/CAF". J. Biol. Chem. 273 (3): 1430–4. doi:10.1074/jbc.273.3.1430. PMID 9430679. 
• 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. 
• Bemark M, Olsson H, Heinegård D, Leanderson T (1998). "Purification and characterization of a protein binding to the SP6 kappa promoter. A potential role for CArG-box binding factor-A in kappa transcription". J. Biol. Chem. 273 (30): 18881–90. doi:10.1074/jbc.273.30.18881. PMID 9668064. 
• Faniello MC, Bevilacqua MA, Condorelli G, et al. (1999). "The B subunit of the CAAT-binding factor NFY binds the central segment of the Co-activator p300". J. Biol. Chem. 274 (12): 7623–6. doi:10.1074/jbc.274.12.7623. PMID 10075648. 
• Hake SB, Masternak K, Kammerbauer C, et al. (2000). "CIITA leucine-rich repeats control nuclear localization, in vivo recruitment to the major histocompatibility complex (MHC) class II enhanceosome, and MHC class II gene transactivation". Mol. Cell. Biol. 20 (20): 7716–25. doi:10.1128/MCB.20.20.7716-7725.2000. PMC 86349. PMID 11003667. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86349. 
• Liang F, Schaufele F, Gardner DG (2001). "Functional interaction of NF-Y and Sp1 is required for type a natriuretic peptide receptor gene transcription". J. Biol. Chem. 276 (2): 1516–22. doi:10.1074/jbc.M006350200. PMID 11022037. 
• Izumi H, Molander C, Penn LZ, et al. (2001). "Mechanism for the transcriptional repression by c-Myc on PDGF beta-receptor". J. Cell. Sci. 114 (Pt 8): 1533–44. PMID 11282029. 

External links

• MeSH NFYB+protein,+human
• FactorBook NF-YB

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