NFE2

From Wikipedia, the free encyclopedia

Nuclear factor (erythroid-derived 2), 45kDa

Identifiers

NFE2; NF-E2; p45

External IDs

OMIM: 601490 MGI: 97308 HomoloGene: 4491

Gene ontology
Molecular Function:	• transcription factor activity • transcription coactivator activity • sequence-specific DNA binding • protein dimerization activity
Cellular Component:	• nucleus
Biological Process:	• transcription • regulation of transcription from RNA polymerase II promoter • multicellular organismal development • hemostasis • circulation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_006163 (mRNA)
NP_006154 (protein)

NM_008685 (mRNA)
NP_032711 (protein)

Location

Chr 12: 52.97 - 52.98 Mb

Chr 15: 103.08 - 103.08 Mb

Pubmed search

[1]

[2]

Nuclear factor (erythroid-derived 2), 45kDa, also known as NFE2, is a human gene.^[1]

[edit] References

^ Entrez Gene: NFE2 nuclear factor (erythroid-derived 2), 45kDa.

[edit] Further reading

Strauss EC, Andrews NC, Higgs DR, Orkin SH (1992). "In vivo footprinting of the human alpha-globin locus upstream regulatory element by guanine and adenine ligation-mediated polymerase chain reaction.". Mol. Cell. Biol. 12 (5): 2135–42. PMID 1569944.
Pischedda C, Cocco S, Melis A, et al. (1995). "Isolation of a differentially regulated splicing isoform of human NF-E2.". Proc. Natl. Acad. Sci. U.S.A. 92 (8): 3511–5. PMID 7724591.
Shivdasani RA, Rosenblatt MF, Zucker-Franklin D, et al. (1995). "Transcription factor NF-E2 is required for platelet formation independent of the actions of thrombopoietin/MGDF in megakaryocyte development.". Cell 81 (5): 695–704. PMID 7774011.
Igarashi K, Kataoka K, Itoh K, et al. (1994). "Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins.". Nature 367 (6463): 568–72. doi:10.1038/367568a0. PMID 8107826.
Chan JY, Han XL, Kan YW (1994). "Isolation of cDNA encoding the human NF-E2 protein.". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 11366–70. PMID 8248255.
Ney PA, Andrews NC, Jane SM, et al. (1993). "Purification of the human NF-E2 complex: cDNA cloning of the hematopoietic cell-specific subunit and evidence for an associated partner.". Mol. Cell. Biol. 13 (9): 5604–12. PMID 8355703.
Toki T, Itoh J, Kitazawa J, et al. (1997). "Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif.". Oncogene 14 (16): 1901–10. doi:10.1038/sj.onc.1201024. PMID 9150357.
Blank V, Kim MJ, Andrews NC (1997). "Human MafG is a functional partner for p45 NF-E2 in activating globin gene expression.". Blood 89 (11): 3925–35. PMID 9166829.
Gavva NR, Gavva R, Ermekova K, et al. (1997). "Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II.". J. Biol. Chem. 272 (39): 24105–8. PMID 9305852.
Mosser EA, Kasanov JD, Forsberg EC, et al. (1998). "Physical and functional interactions between the transactivation domain of the hematopoietic transcription factor NF-E2 and WW domains.". Biochemistry 37 (39): 13686–95. doi:10.1021/bi981310l. PMID 9753456.
Hung HL, Kim AY, Hong W, et al. (2001). "Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation.". J. Biol. Chem. 276 (14): 10715–21. doi:10.1074/jbc.M007846200. PMID 11154691.
Gavva NR, Wen SC, Daftari P, et al. (2002). "NAPP2, a peroxisomal membrane protein, is also a transcriptional corepressor.". Genomics 79 (3): 423–31. doi:10.1006/geno.2002.6714. PMID 11863372.
Boulanger L, Sabatino DE, Wong EY, et al. (2003). "Erythroid expression of the human alpha-spectrin gene promoter is mediated by GATA-1- and NF-E2-binding proteins.". J. Biol. Chem. 277 (44): 41563–70. doi:10.1074/jbc.M208184200. PMID 12196550.
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.
Marini MG, Asunis I, Chan K, et al. (2003). "Cloning MafF by recognition site screening with the NFE2 tandem repeat of HS2: analysis of its role in globin and GCSl genes regulation.". Blood Cells Mol. Dis. 29 (2): 145–58. PMID 12490281.
Onishi Y, Kiyama R (2003). "Interaction of NF-E2 in the human beta-globin locus control region before chromatin remodeling.". J. Biol. Chem. 278 (10): 8163–71. doi:10.1074/jbc.M209612200. PMID 12509425.
Newman JR, Keating AE (2003). "Comprehensive identification of human bZIP interactions with coiled-coil arrays.". Science 300 (5628): 2097–101. doi:10.1126/science.1084648. PMID 12805554.
Chuen CK, Li K, Yang M, et al. (2004). "Interleukin-1beta up-regulates the expression of thrombopoietin and transcription factors c-Jun, c-Fos, GATA-1, and NF-E2 in megakaryocytic cells.". J. Lab. Clin. Med. 143 (2): 75–88. doi:10.1016/j.lab.2003.09.006. PMID 14966463.
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. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

[edit] External links

MeSH NFE2+protein,+human

This article on a gene on chromosome 12 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