KLF11

Protein-coding gene in the species Homo sapiens
KLF11
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1PO4

Identifiers
AliasesKLF11, FKLF, FKLF1, MODY7, TIEG2, Tieg3, Kruppel-like factor 11, Kruppel like factor 11
External IDsOMIM: 603301 MGI: 2653368 HomoloGene: 2668 GeneCards: KLF11
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for KLF11
Genomic location for KLF11
Band2p25.1Start10,042,849 bp[1]
End10,054,836 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for KLF11
Genomic location for KLF11
Band12 A1.3|12 8.49 cMStart24,701,273 bp[2]
End24,712,788 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • monocyte

  • saphenous vein

  • gastric mucosa

  • amniotic fluid

  • abdominal fat

  • body of pancreas

  • subcutaneous adipose tissue

  • skin of abdomen

  • parietal pleura
Top expressed in
  • secondary oocyte

  • superior cervical ganglion

  • hand

  • otolith organ

  • utricle

  • right lung lobe

  • molar

  • trigeminal ganglion

  • sexually immature organism

  • urethra
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • DNA binding
  • protein binding
  • metal ion binding
  • nucleic acid binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • nucleus
  • nucleoplasm
  • cytosol
  • focal adhesion
  • nuclear body
Biological process
  • positive regulation of apoptotic process
  • negative regulation of transcription, DNA-templated
  • regulation of transcription, DNA-templated
  • negative regulation of transcription by RNA polymerase II
  • transcription by RNA polymerase II
  • regulation of transcription involved in G1/S transition of mitotic cell cycle
  • transcription, DNA-templated
  • negative regulation of cell population proliferation
  • apoptotic process
  • cellular response to peptide
  • regulation of transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8462

194655

Ensembl

ENSG00000172059

ENSMUSG00000020653

UniProt

O14901

Q8K1S5

RefSeq (mRNA)

NM_001177716
NM_001177718
NM_003597

NM_178357

RefSeq (protein)

NP_001171187
NP_001171189
NP_003588

NP_848134

Location (UCSC)Chr 2: 10.04 – 10.05 MbChr 12: 24.7 – 24.71 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Krueppel-like factor 11 is a protein that in humans is encoded by the KLF11 gene.[5][6][7]

KLF11 is a mesoderm derived, zinc finger transcription factor in the Krüppel-like factor (KLF) family. It binds to SP1- like GC- rich sequences in epsilon and gamma globin gene promoters inhibiting cellular growth and causing apoptosis. In the regulation of genes, it is involved in cellular inflammation and differentiation, making it an essential factor in early embryonic development. This transcription factor binds to promoters of genes involved in cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism, specifically pancreatic beta cell function. Defects in KLF11 affect glucose metabolism, insulin transcription, insulin processing, and insulin secretion which cause type 2 diabetes in adults and maturity-onset diabetes of the young type 7. These types of diabetes are caused by KLF11 interacting with co-repressors in the pancreatic islet beta cells. KLF11 has recently been shown to be involved in endometriosis since it regulated the expression of extracellular matrix genes. Its absence in extracellular matrix genes created a more fibrogenic response by the tissue. This was proved by creating a “knockout” model. The experiment showed that the absence of KLF11 showed higher amounts of fibrosis indicating that it prevents the growth of endometriotic lesions and inhibits pathological scarring.

[8][9][10]

Interactions

KLF11 has been shown to interact with SIN3A.[11][12]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172059 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020653 – 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. ^ Cook T, Gebelein B, Mesa K, Mladek A, Urrutia R (Oct 1998). "Molecular cloning and characterization of TIEG2 reveals a new subfamily of transforming growth factor-beta-inducible Sp1-like zinc finger-encoding genes involved in the regulation of cell growth". The Journal of Biological Chemistry. 273 (40): 25929–36. doi:10.1074/jbc.273.40.25929. PMID 9748269.
  6. ^ Scohy S, Gabant P, Van Reeth T, Hertveldt V, Drèze PL, Van Vooren P, Rivière M, Szpirer J, Szpirer C (Nov 2000). "Identification of KLF13 and KLF14 (SP6), novel members of the SP/XKLF transcription factor family". Genomics. 70 (1): 93–101. doi:10.1006/geno.2000.6362. PMID 11087666.
  7. ^ "Entrez Gene: KLF11 Kruppel-like factor 11".
  8. ^ Daftary GS, Zheng Y, Tabbaa ZM, Schoolmeester JK, Gada RP, Grzenda AL, Mathison AJ, Keeney GL, Lomberk GA, Urrutia R (2013). "A novel role of the Sp/KLF transcription factor KLF11 in arresting progression of endometriosis". PLOS ONE. 8 (3): e60165. Bibcode:2013PLoSO...860165D. doi:10.1371/journal.pone.0060165. PMC 3610699. PMID 23555910.
  9. ^ Mathison A, Grzenda A, Lomberk G, Velez G, Buttar N, Tietz P, Hendrickson H, Liebl A, Xiong YY, Gores G, Fernandez-Zapico M, Larusso NF, Faubion W, Shah VH, Urrutia R (2013). "Role for Krüppel-like transcription factor 11 in mesenchymal cell function and fibrosis". PLOS ONE. 8 (9): e75311. Bibcode:2013PLoSO...875311M. doi:10.1371/journal.pone.0075311. PMC 3775729. PMID 24069400.
  10. ^ Spittau B, Krieglstein K (2012). "Klf10 and Klf11 as mediators of TGF-beta superfamily signaling". Cell and Tissue Research. 347 (1): 65–72. doi:10.1007/s00441-011-1186-6. PMID 21574058. S2CID 14295737.
  11. ^ Zhang JS, Moncrieffe MC, Kaczynski J, Ellenrieder V, Prendergast FG, Urrutia R (Aug 2001). "A conserved alpha-helical motif mediates the interaction of Sp1-like transcriptional repressors with the corepressor mSin3A". Molecular and Cellular Biology. 21 (15): 5041–9. doi:10.1128/MCB.21.15.5041-5049.2001. PMC 87230. PMID 11438660.
  12. ^ Ellenrieder V, Zhang JS, Kaczynski J, Urrutia R (May 2002). "Signaling disrupts mSin3A binding to the Mad1-like Sin3-interacting domain of TIEG2, an Sp1-like repressor". The EMBO Journal. 21 (10): 2451–60. doi:10.1093/emboj/21.10.2451. PMC 126002. PMID 12006497.

Further reading

  • Asano H, Li XS, Stamatoyannopoulos G (May 1999). "FKLF, a novel Krüppel-like factor that activates human embryonic and fetal beta-like globin genes". Molecular and Cellular Biology. 19 (5): 3571–9. doi:10.1128/MCB.19.5.3571. PMC 84149. PMID 10207080.
  • Zhang JS, Moncrieffe MC, Kaczynski J, Ellenrieder V, Prendergast FG, Urrutia R (Aug 2001). "A conserved alpha-helical motif mediates the interaction of Sp1-like transcriptional repressors with the corepressor mSin3A". Molecular and Cellular Biology. 21 (15): 5041–9. doi:10.1128/MCB.21.15.5041-5049.2001. PMC 87230. PMID 11438660.
  • Jia L, Young MF, Powell J, Yang L, Ho NC, Hotchkiss R, Robey PG, Francomano CA (Jan 2002). "Gene expression profile of human bone marrow stromal cells: high-throughput expressed sequence tag sequencing analysis". Genomics. 79 (1): 7–17. doi:10.1006/geno.2001.6683. PMID 11827452.
  • Ellenrieder V, Zhang JS, Kaczynski J, Urrutia R (May 2002). "Signaling disrupts mSin3A binding to the Mad1-like Sin3-interacting domain of TIEG2, an Sp1-like repressor". The EMBO Journal. 21 (10): 2451–60. doi:10.1093/emboj/21.10.2451. PMC 126002. PMID 12006497.
  • Ou XM, Chen K, Shih JC (May 2004). "Dual functions of transcription factors, transforming growth factor-beta-inducible early gene (TIEG)2 and Sp3, are mediated by CACCC element and Sp1 sites of human monoamine oxidase (MAO) B gene". The Journal of Biological Chemistry. 279 (20): 21021–8. doi:10.1074/jbc.M312638200. PMID 15024015.
  • Ellenrieder V, Buck A, Harth A, Jungert K, Buchholz M, Adler G, Urrutia R, Gress TM (Aug 2004). "KLF11 mediates a critical mechanism in TGF-beta signaling that is inactivated by Erk-MAPK in pancreatic cancer cells". Gastroenterology. 127 (2): 607–20. doi:10.1053/j.gastro.2004.05.018. PMID 15300592.
  • Cao S, Fernandez-Zapico ME, Jin D, Puri V, Cook TA, Lerman LO, Zhu XY, Urrutia R, Shah V (Jan 2005). "KLF11-mediated repression antagonizes Sp1/sterol-responsive element-binding protein-induced transcriptional activation of caveolin-1 in response to cholesterol signaling". The Journal of Biological Chemistry. 280 (3): 1901–10. doi:10.1074/jbc.M407941200. PMID 15531587.
  • Neve B, Fernandez-Zapico ME, Ashkenazi-Katalan V, Dina C, Hamid YH, Joly E, Vaillant E, Benmezroua Y, Durand E, Bakaher N, Delannoy V, Vaxillaire M, Cook T, Dallinga-Thie GM, Jansen H, Charles MA, Clément K, Galan P, Hercberg S, Helbecque N, Charpentier G, Prentki M, Hansen T, Pedersen O, Urrutia R, Melloul D, Froguel P (Mar 2005). "Role of transcription factor KLF11 and its diabetes-associated gene variants in pancreatic beta cell function". Proceedings of the National Academy of Sciences of the United States of America. 102 (13): 4807–12. doi:10.1073/pnas.0409177102. PMC 554843. PMID 15774581.
  • Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
  • Buck A, Buchholz M, Wagner M, Adler G, Gress T, Ellenrieder V (Nov 2006). "The tumor suppressor KLF11 mediates a novel mechanism in transforming growth factor beta-induced growth inhibition that is inactivated in pancreatic cancer". Molecular Cancer Research. 4 (11): 861–72. doi:10.1158/1541-7786.MCR-06-0081. PMID 17114344.
  • Florez JC, Saxena R, Winckler W, Burtt NP, Almgren P, Bengtsson Boström K, Tuomi T, Gaudet D, Ardlie KG, Daly MJ, Altshuler D, Hirschhorn JN, Groop L (Dec 2006). "The Krüppel-like factor 11 (KLF11) Q62R polymorphism is not associated with type 2 diabetes in 8,676 people". Diabetes. 55 (12): 3620–4. doi:10.2337/db06-0867. PMID 17130512.
  • Spittau B, Wang Z, Boinska D, Krieglstein K (Jun 2007). "Functional domains of the TGF-beta-inducible transcription factor Tieg3 and detection of two putative nuclear localization signals within the zinc finger DNA-binding domain". Journal of Cellular Biochemistry. 101 (3): 712–22. doi:10.1002/jcb.21228. PMID 17252542. S2CID 9730806.
  • Niu X, Perakakis N, Laubner K, Limbert C, Stahl T, Brendel MD, Bretzel RG, Seufert J, Päth G (Jul 2007). "Human Krüppel-like factor 11 inhibits human proinsulin promoter activity in pancreatic beta cells". Diabetologia. 50 (7): 1433–41. doi:10.1007/s00125-007-0667-3. PMID 17479246.

External links

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


  • v
  • t
  • 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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