KLF2

From Wikipedia, the free encyclopedia

Kruppel-like factor 2 (lung)

Identifiers

KLF2; LKLF

External IDs

OMIM: 602016 MGI: 1342772 HomoloGene: 7395

Gene ontology
Molecular Function:	• transcription factor activity • protein binding • zinc ion binding • transcription activator activity • metal ion binding
Cellular Component:	• intracellular • nucleus
Biological Process:	• transcription • regulation of transcription, DNA-dependent • positive regulation of transcription

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_016270 (mRNA)
NP_057354 (protein)

XM_982078 (mRNA)
XP_987172 (protein)

Location

Chr 19: 16.3 - 16.3 Mb

Chr 8: 75.25 - 75.25 Mb

Pubmed search

[1]

[2]

Kruppel-like factor 2 (lung), also known as KLF2, is a human gene.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Kruppel-like factors

[edit] References

^ Entrez Gene: KLF2 Kruppel-like factor 2 (lung).

[edit] Further reading

Anderson KP, Kern CB, Crable SC, Lingrel JB (1995). "Isolation of a gene encoding a functional zinc finger protein homologous to erythroid Krüppel-like factor: identification of a new multigene family.". Mol. Cell. Biol. 15 (11): 5957–65. PMID 7565748.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Kozyrev SV, Hansen LL, Poltaraus AB, et al. (1999). "Structure of the human CpG-island-containing lung Kruppel-like factor (LKLF) gene and its location in chromosome 19p13.11-13 locus.". FEBS Lett. 448 (1): 149–52. PMID 10217429.
Wani MA, Conkright MD, Jeffries S, et al. (1999). "cDNA isolation, genomic structure, regulation, and chromosomal localization of human lung Kruppel-like factor.". Genomics 60 (1): 78–86. doi:10.1006/geno.1999.5888. PMID 10458913.
Conkright MD, Wani MA, Lingrel JB (2001). "Lung Krüppel-like factor contains an autoinhibitory domain that regulates its transcriptional activation by binding WWP1, an E3 ubiquitin ligase.". J. Biol. Chem. 276 (31): 29299–306. doi:10.1074/jbc.M103670200. PMID 11375995.
Denkinger DJ, Cushman-Vokoun AM, Kawahara RS (2002). "Regulation of the vav proto-oncogene by LKLF.". Gene 281 (1-2): 133–42. PMID 11750135.
Dekker RJ, van Soest S, Fontijn RD, et al. (2002). "Prolonged fluid shear stress induces a distinct set of endothelial cell genes, most specifically lung Krüppel-like factor (KLF2).". Blood 100 (5): 1689–98. doi:10.1182/blood-2002-01-0046. PMID 12176889.
Banerjee SS, Feinberg MW, Watanabe M, et al. (2003). "The Krüppel-like factor KLF2 inhibits peroxisome proliferator-activated receptor-gamma expression and adipogenesis.". J. Biol. Chem. 278 (4): 2581–4. doi:10.1074/jbc.M210859200. PMID 12426306.
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.
SenBanerjee S, Lin Z, Atkins GB, et al. (2004). "KLF2 Is a novel transcriptional regulator of endothelial proinflammatory activation.". J. Exp. Med. 199 (10): 1305–15. doi:10.1084/jem.20031132. PMID 15136591.
Haaland RE, Yu W, Rice AP (2005). "Identification of LKLF-regulated genes in quiescent CD4+ T lymphocytes.". Mol. Immunol. 42 (5): 627–41. doi:10.1016/j.molimm.2004.09.012. PMID 15607822.
Lin Z, Kumar A, SenBanerjee S, et al. (2005). "Kruppel-like factor 2 (KLF2) regulates endothelial thrombotic function.". Circ. Res. 96 (5): e48–57. doi:10.1161/01.RES.0000159707.05637.a1. PMID 15718498.
Wang F, Zhu Y, Huang Y, et al. (2005). "Transcriptional repression of WEE1 by Kruppel-like factor 2 is involved in DNA damage-induced apoptosis.". Oncogene 24 (24): 3875–85. doi:10.1038/sj.onc.1208546. PMID 15735666.
Huddleson JP, Ahmad N, Srinivasan S, Lingrel JB (2005). "Induction of KLF2 by fluid shear stress requires a novel promoter element activated by a phosphatidylinositol 3-kinase-dependent chromatin-remodeling pathway.". J. Biol. Chem. 280 (24): 23371–9. doi:10.1074/jbc.M413839200. PMID 15834135.
Parmar KM, Nambudiri V, Dai G, et al. (2005). "Statins exert endothelial atheroprotective effects via the KLF2 transcription factor.". J. Biol. Chem. 280 (29): 26714–9. doi:10.1074/jbc.C500144200. PMID 15878865.
Basu P, Morris PE, Haar JL, et al. (2005). "KLF2 is essential for primitive erythropoiesis and regulates the human and murine embryonic beta-like globin genes in vivo.". Blood 106 (7): 2566–71. doi:10.1182/blood-2005-02-0674. PMID 15947087.
Bhattacharya R, Senbanerjee S, Lin Z, et al. (2005). "Inhibition of vascular permeability factor/vascular endothelial growth factor-mediated angiogenesis by the Kruppel-like factor KLF2.". J. Biol. Chem. 280 (32): 28848–51. doi:10.1074/jbc.C500200200. PMID 15980434.
Zhang P, Basu P, Redmond LC, et al. (2006). "A functional screen for Krüppel-like factors that regulate the human gamma-globin gene through the CACCC promoter element.". Blood Cells Mol. Dis. 35 (2): 227–35. doi:10.1016/j.bcmd.2005.04.009. PMID 16023392.
Sen-Banerjee S, Mir S, Lin Z, et al. (2006). "Kruppel-like factor 2 as a novel mediator of statin effects in endothelial cells.". Circulation 112 (5): 720–6. doi:10.1161/CIRCULATIONAHA.104.525774. PMID 16043642.

[edit] External links

MeSH KLF2+protein,+human

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

This article on a gene on chromosome 19 is a stub. You can help Wikipedia by expanding it.

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