GFI1

From Wikipedia, the free encyclopedia

Growth factor independent 1

Identifiers

GFI1; ZNF163

External IDs

OMIM: 600871 MGI: 103170 HomoloGene: 3854

Gene ontology
Molecular Function:	• DNA binding • RNA polymerase II transcription factor activity • zinc ion binding • metal ion binding
Cellular Component:	• intracellular • nucleus
Biological Process:	• G1/S-specific transcription in mitotic cell cycle • transcription • regulation of transcription, DNA-dependent • mechanosensory behavior • negative regulation of cell fate specification • viral reproduction • inner ear morphogenesis • auditory receptor cell differentiation • positive regulation of cell fate specification • cell fate commitment

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005263 (mRNA)
NP_005254 (protein)

NM_010278 (mRNA)
NP_034408 (protein)

Location

Chr 1: 92.71 - 92.73 Mb

Chr 5: 107.96 - 107.97 Mb

Pubmed search

[1]

[2]

Growth factor independent 1, also known as GFI1, is a human gene.^[1]

[edit] References

^ Entrez Gene: GFI1 growth factor independent 1.

[edit] Further reading

Bell DW, Taguchi T, Jenkins NA, et al. (1995). "Chromosomal localization of a gene, GF1, encoding a novel zinc finger protein reveals a new syntenic region between man and rodents.". Cytogenet. Cell Genet. 70 (3-4): 263–7. PMID 7789186.
Gilks CB, Bear SE, Grimes HL, Tsichlis PN (1993). "Progression of interleukin-2 (IL-2)-dependent rat T cell lymphoma lines to IL-2-independent growth following activation of a gene (Gfi-1) encoding a novel zinc finger protein.". Mol. Cell. Biol. 13 (3): 1759–68. PMID 8441411.
Zweidler-Mckay PA, Grimes HL, Flubacher MM, Tsichlis PN (1996). "Gfi-1 encodes a nuclear zinc finger protein that binds DNA and functions as a transcriptional repressor.". Mol. Cell. Biol. 16 (8): 4024–34. PMID 8754800.
Roberts T, Cowell JK (1997). "Cloning of the human Gfi-1 gene and its mapping to chromosome region 1p22.". Oncogene 14 (8): 1003–5. doi:10.1038/sj.onc.1200910. PMID 9051000.
Rödel B, Tavassoli K, Karsunky H, et al. (2000). "The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting with the STAT3 inhibitor PIAS3.". EMBO J. 19 (21): 5845–55. doi:10.1093/emboj/19.21.5845. PMID 11060035.
Osawa M, Yamaguchi T, Nakamura Y, et al. (2002). "Erythroid expansion mediated by the Gfi-1B zinc finger protein: role in normal hematopoiesis.". Blood 100 (8): 2769–77. doi:10.1182/blood-2002-01-0182. PMID 12351384.
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.
Person RE, Li FQ, Duan Z, et al. (2003). "Mutations in proto-oncogene GFI1 cause human neutropenia and target ELA2.". Nat. Genet. 34 (3): 308–12. doi:10.1038/ng1170. PMID 12778173.
McGhee L, Bryan J, Elliott L, et al. (2003). "Gfi-1 attaches to the nuclear matrix, associates with ETO (MTG8) and histone deacetylase proteins, and represses transcription using a TSA-sensitive mechanism.". J. Cell. Biochem. 89 (5): 1005–18. doi:10.1002/jcb.10548. PMID 12874834.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Doan LL, Porter SD, Duan Z, et al. (2004). "Targeted transcriptional repression of Gfi1 by GFI1 and GFI1B in lymphoid cells.". Nucleic Acids Res. 32 (8): 2508–19. doi:10.1093/nar/gkh570. PMID 15131254.
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.
Dwivedi PP, Anderson PH, Omdahl JL, et al. (2005). "Identification of growth factor independent-1 (GFI1) as a repressor of 25-hydroxyvitamin D 1-alpha hydroxylase (CYP27B1) gene expression in human prostate cancer cells.". Endocr. Relat. Cancer 12 (2): 351–65. doi:10.1677/erc.1.00920. PMID 15947108.
Duan Z, Zarebski A, Montoya-Durango D, et al. (2005). "Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of histone lysine methyltransferase G9a and histone deacetylase 1.". Mol. Cell. Biol. 25 (23): 10338–51. doi:10.1128/MCB.25.23.10338-10351.2005. PMID 16287849.
Marteijn JA, van der Meer LT, Van Emst L, et al. (2007). "Diminished proteasomal degradation results in accumulation of Gfi1 protein in monocytes.". Blood 109 (1): 100–8. doi:10.1182/blood-2006-02-003590. PMID 16888099.
Dwivedi PP, Anderson PH, Tilley WD, et al. (2007). "Role of oncoprotein growth factor independent-1 (GFI1) in repression of 25-hydroxyvitamin D 1alpha-hydroxylase (CYP27B1): a comparative analysis in human prostate cancer and kidney cells.". J. Steroid Biochem. Mol. Biol. 103 (3-5): 742–6. doi:10.1016/j.jsbmb.2006.12.014. PMID 17207994.
Nakazawa Y, Suzuki M, Manabe N, et al. (2007). "Cooperative interaction between ETS1 and GFI1 transcription factors in the repression of Bax gene expression.". Oncogene 26 (24): 3541–50. doi:10.1038/sj.onc.1210140. PMID 17213822.
Khanna-Gupta A, Sun H, Zibello T, et al. (2007). "Growth factor independence-1 (Gfi-1) plays a role in mediating specific granule deficiency (SGD) in a patient lacking a gene-inactivating mutation in the C/EBPepsilon gene.". Blood 109 (10): 4181–90. doi:10.1182/blood-2005-05-022004. PMID 17244686.
Marteijn JA, van der Meer LT, van Emst L, et al. (2007). "Gfi1 ubiquitination and proteasomal degradation is inhibited by the ubiquitin ligase Triad1.". Blood 110 (9): 3128–35. doi:10.1182/blood-2006-11-058602. PMID 17646546.

[edit] External links

MeSH GFI1+protein,+human

This article on a gene on chromosome 1 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