- NFE2
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Transcription factor NF-E2 45 kDa subunit is a protein that in humans is encoded by the NFE2 gene.[1][2]
Interactions
NFE2 has been shown to interact with CREB-binding protein.[3]
References
- ^ Ney PA, Andrews NC, Jane SM, Safer B, Purucker ME, Weremowicz S, Morton CC, Goff SC, Orkin SH, Nienhuis AW (Sep 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. PMC 360284. PMID 8355703. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=360284.
- ^ "Entrez Gene: NFE2 nuclear factor (erythroid-derived 2), 45kDa". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4778.
- ^ Hung, H L; Kim A Y, Hong W, Rakowski C, Blobel G A (Apr. 2001). "Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation". J. Biol. Chem. (United States) 276 (14): 10715–21. doi:10.1074/jbc.M007846200. ISSN 0021-9258. PMID 11154691.
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. PMC 364385. PMID 1569944. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=364385.
- 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. doi:10.1073/pnas.92.8.3511. PMC 42197. PMID 7724591. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42197.
- 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. doi:10.1016/0092-8674(95)90531-6. 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. doi:10.1073/pnas.90.23.11366. PMC 47983. PMID 8248255. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=47983.
- 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. doi:10.1074/jbc.272.39.24105. 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- 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. doi:10.1006/bcmd.2002.0550. 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- 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.
External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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, JDP2, 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, L3) · NFIL3 · NRL · NRF (1, 2, 3) · XBP1(1.2) Basic helix-loop-helix (bHLH)ATOH1 · AhR · AHRR · ARNT · ASCL1 · BHLHB2 · BMAL (ARNTL, ARNTL2) · CLOCK · EPAS1 · FIGLA · HAND (1, 2) · HES (5, 6) · HEY (1, 2, L) · HES1 · HIF (1A, 3A) · ID (1, 2, 3, 4) · LYL1 · MESP2 · MXD4 · MYCL1 · MYCN · Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) · Neurogenins (1, 2, 3) · NeuroD (1, 2) · NPAS (1, 2, 3) · OLIG (1, 2) · Pho4 · Scleraxis · SIM (1, 2) · TAL (1, 2) · Twist · USF1(1.3) bHLH-ZIP(1.4) NF-1(1.5) RF-X(1.6) Basic helix-span-helix (bHSH)(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 (Androgen, Estrogen (α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related (α, β, γ))
subfamily 4 NUR (NGFIB, NOR1, NURR1) · subfamily 5 (LRH-1, SF1) · subfamily 6 (GCNF) · subfamily 0 (DAX1, SHP)(2.2) Other Cys4(2.3) Cys2His2General transcription factors (TFIIA, TFIIB, TFIID, TFIIE (1, 2), TFIIF (1, 2), TFIIH (1, 2, 4, 2I, 3A, 3C1, 3C2))
ATBF1 · BCL (6, 11A, 11B) · CTCF · E4F1 · EGR (1, 2, 3, 4) · ERV3 · GFI1 · GLI-Krüppel family (1, 2, 3, REST, S2, YY1) · HIC (1, 2) · HIVEP (1, 2, 3) · IKZF (1, 2, 3) · ILF (2, 3) · KLF (2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 17) · MTF1 · MYT1 · OSR1 · PRDM9 · SALL (1, 2, 3, 4) · SP (1, 2, 4, 7, 8) · TSHZ3 · WT1 · Zbtb7 (7A, 7B) · ZBTB (16, 17, 20, 32, 33, 40) · 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, 300, 318, 330, 346, 350, 365, 366, 384, 423, 451, 452, 471, 593, 638, 644, 649, 655)(2.4) Cys6(2.5) Alternating composition(3) Helix-turn-helix domains (3.1) HomeodomainARX · CDX (1, 2) · CRX · CUTL1 · DBX (1, 2) · DLX (3, 4, 5) · EMX2 · EN (1, 2) · FHL (1, 2, 3) · HESX1 · HHEX · HLX · Homeobox (A1, A2, 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 · IRX (1, 2, 3, 4, 5, 6, MKX) · LMX (1A, 1B) · MEIS (1, 2) · MEOX2 · MNX1 · MSX (1, 2) · NANOG · NKX (2-1, 2-2, 2-3, 2-5, 3-1, 3-2, 6-1, 6-2) · NOBOX · PBX (1, 2, 3) · PHF (1, 3, 6, 8, 10, 16, 17, 20, 21A) · PHOX (2A, 2B) · PITX (1, 2, 3) · POU domain (PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) · OTX (1, 2) · PDX1 · SATB2 · SHOX2 · VAX1 · ZEB (1, 2)(3.2) Paired box(3.3) Fork head / winged helix(3.4) Heat Shock Factors(3.5) Tryptophan clusters(3.6) TEA domain(4) β-Scaffold factors with minor groove contacts (4.1) Rel homology region(4.2) STAT(4.3) p53(4.4) MADS box(4.6) TATA binding proteins(4.7) High-mobility group(4.10) Cold-shock domainCSDA, YBX1(4.11) Runt(0) Other transcription factors (0.2) HMGI(Y)(0.3) Pocket domain(0.6) Miscellaneoussee also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)Categories:- Human proteins
- Transcription factors
- Chromosome 12 gene stubs
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