GFI1

Protein-coding gene in the species Homo sapiens
GFI1
Identifiers
AliasesGFI1, GFI-1, GFI1A, SCN2, ZNF163, growth factor independent 1 transcriptional repressor
External IDsOMIM: 600871; MGI: 103170; HomoloGene: 3854; GeneCards: GFI1; OMA:GFI1 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for GFI1
Genomic location for GFI1
Band1p22.1Start92,473,043 bp[1]
End92,486,925 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for GFI1
Genomic location for GFI1
Band5 F|5 52.23 cMStart107,864,523 bp[2]
End107,873,902 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • granulocyte

  • bone marrow

  • bone marrow cells

  • trabecular bone

  • body of pancreas

  • testicle

  • thymus

  • blood

  • lymph node

  • spleen
Top expressed in
  • utricle

  • vestibular sensory epithelium

  • thymus

  • saccule

  • granulocyte

  • spermatocyte

  • bone marrow

  • tongue

  • mesenteric lymph nodes

  • embryo
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • metal ion binding
  • DNA-binding transcription repressor activity, RNA polymerase II-specific
  • protein binding
  • nucleic acid binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • DNA-binding transcription factor activity
Cellular component
  • nuclear body
  • nuclear matrix
  • transcription repressor complex
  • nucleus
  • nucleoplasm
Biological process
  • positive regulation of interleukin-6-mediated signaling pathway
  • negative regulation of neuron projection development
  • regulation of transcription, DNA-templated
  • regulation of toll-like receptor signaling pathway
  • regulation of histone H3-K4 methylation
  • negative regulation of transcription by RNA polymerase II
  • regulation of transcription involved in G1/S transition of mitotic cell cycle
  • transcription, DNA-templated
  • negative regulation of vitamin D biosynthetic process
  • negative regulation of calcidiol 1-monooxygenase activity
  • viral process
  • negative regulation of transcription, DNA-templated
  • negative regulation of NF-kappaB transcription factor activity
  • cellular response to lipopolysaccharide
  • hemopoiesis
  • positive regulation of transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2672

14581

Ensembl

ENSG00000162676

ENSMUSG00000029275

UniProt

Q99684

P70338

RefSeq (mRNA)

NM_001127215
NM_001127216
NM_005263

NM_001267621
NM_010278

RefSeq (protein)

NP_001120687
NP_001120688
NP_005254

NP_001254550
NP_034408

Location (UCSC)Chr 1: 92.47 – 92.49 MbChr 5: 107.86 – 107.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Zinc finger protein Gfi-1 is a transcriptional repressor that in humans is encoded by the GFI1 gene.[5] It is important normal hematopoiesis.[6]

Interactions

GFI1 has been shown to interact with PIAS3[7] and RUNX1T1.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000162676 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029275 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Bell DW, Taguchi T, Jenkins NA, Gilbert DJ, Copeland NG, Gilks CB, Zweidler-McKay P, Grimes HL, Tsichlis PN, Testa JR (July 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. doi:10.1159/000134048. PMID 7789186.
  6. ^ "Entrez Gene: GFI1 growth factor independent 1".
  7. ^ Rödel B, Tavassoli K, Karsunky H, Schmidt T, Bachmann M, Schaper F, Heinrich P, Shuai K, Elsässer HP, Möröy T (November 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. PMC 305799. PMID 11060035.
  8. ^ McGhee L, Bryan J, Elliott L, Grimes HL, Kazanjian A, Davis JN, Meyers S (August 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. S2CID 25450754.

Further reading

  • 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. doi:10.1128/MCB.13.3.1759. PMC 359488. 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. doi:10.1128/MCB.16.8.4024. PMC 231398. 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, Schmidt T, Bachmann M, Schaper F, Heinrich P, Shuai K, Elsässer HP, Möröy T (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. PMC 305799. PMID 11060035.
  • Osawa M, Yamaguchi T, Nakamura Y, Kaneko S, Onodera M, Sawada K, Jegalian A, Wu H, Nakauchi H, Iwama A (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, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA (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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Person RE, Li FQ, Duan Z, Benson KF, Wechsler J, Papadaki HA, Eliopoulos G, Kaufman C, Bertolone SJ, Nakamoto B, Papayannopoulou T, Grimes HL, Horwitz M (2003). "Mutations in proto-oncogene GFI1 cause human neutropenia and target ELA2". Nat. Genet. 34 (3): 308–12. doi:10.1038/ng1170. PMC 2832179. PMID 12778173.
  • McGhee L, Bryan J, Elliott L, Grimes HL, Kazanjian A, Davis JN, Meyers S (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. S2CID 25450754.
  • Doan LL, Porter SD, Duan Z, Flubacher MM, Montoya D, Tsichlis PN, Horwitz M, Gilks CB, Grimes HL (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. PMC 419458. PMID 15131254.
  • Dwivedi PP, Anderson PH, Omdahl JL, Grimes HL, Morris HA, May BK (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, Grimes HL, Horwitz M (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. PMC 1291230. PMID 16287849.
  • Marteijn JA, van der Meer LT, Van Emst L, de Witte T, Jansen JH, van der Reijden BA (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, May BK, Morris HA (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. S2CID 30600875.
  • Nakazawa Y, Suzuki M, Manabe N, Yamada T, Kihara-Negishi F, Sakurai T, Tenen DG, Iwama A, Mochizuki M, Oikawa T (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. S2CID 30476328.
  • Khanna-Gupta A, Sun H, Zibello T, Lee HM, Dahl R, Boxer LA, Berliner N (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/EBPϵ gene". Blood. 109 (10): 4181–90. doi:10.1182/blood-2005-05-022004. PMC 1885490. PMID 17244686.
  • Marteijn JA, van der Meer LT, van Emst L, van Reijmersdal S, Wissink W, de Witte T, Jansen JH, Van der Reijden BA (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. S2CID 19048016.

External links

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

  • v
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  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(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
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies


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