NFYA

From Wikipedia, the free encyclopedia

Nuclear transcription factor Y, alpha

Identifiers

NFYA; CBF-A; CBF-B; HAP2; NF-YA

External IDs

OMIM: 189903 MGI: 97316 HomoloGene: 32114

Gene ontology
Molecular Function:	• transcription factor activity • protein binding • transcription activator activity
Cellular Component:	• nucleus • CCAAT-binding factor complex
Biological Process:	• transcription • positive regulation of transcription from RNA polymerase II promoter

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002505 (mRNA)
NP_002496 (protein)

NM_010913 (mRNA)
NP_035043 (protein)

Location

Chr 6: 41.15 - 41.18 Mb

Chr 17: 47.85 - 47.88 Mb

Pubmed search

[1]

[2]

Nuclear transcription factor Y, alpha, also known as NFYA, is a human 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.^[1]

[edit] References

^ Entrez Gene: NFYA nuclear transcription factor Y, alpha.

[edit] Further reading

Mantovani R (1999). "The molecular biology of the CCAAT-binding factor NF-Y.". Gene 239 (1): 15–27. 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. 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.
Li XY, Mattei MG, Zaleska-Rutczynska Z, et al. (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.
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. 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. 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. 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. 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. 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. 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. 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.

[edit] External links

MeSH NFYA+protein,+human

This article on a gene on chromosome 6 is a stub. You can help Wikipedia by expanding it.

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

v • d • e

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1

(1.3) bHLH-ZIP	MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)

(1.6) Basic helix-span-helix (bHSH)	AP-2

(2) Zinc finger
DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)

(2.3) Cys₂His₂	ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1, 2

(4) β-Scaffold factors with
minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	Rb • RBL1 • RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 • EREBP • B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD