FOXK2

Forkhead box protein K2 is a protein that in humans is encoded by the FOXK2 gene.[5][6]

FOXK2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1JXS, 2C6Y
Identifiers
Aliases	FOXK2, ILF, ILF-1, ILF1, forkhead box K2, nGTBP
External IDs	OMIM: 147685 MGI: 1916087 HomoloGene: 18748 GeneCards: FOXK2
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q25.3 Start 82,519,713 bp[1] End 82,644,662 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 E2 Start 121,259,990 bp[2] End 121,309,896 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding • sequence-specific DNA binding • DNA binding • GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific • GO:0001948 protein binding • magnesium ion binding • metal ion binding • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific • transcription regulatory region sequence-specific DNA binding • GO:0001078, GO:0001214, GO:0001206 DNA-binding transcription repressor activity, RNA polymerase II-specific Cellular component • cell nucleus • nucleoplasm • cytoplasm Biological process • regulation of transcription from RNA polymerase II promoter • regulation of transcription, DNA-templated • positive regulation of transcription from RNA polymerase II promoter • transcription, DNA-templated • transcription from RNA polymerase II promoter • protein deubiquitination • anatomical structure morphogenesis • cell differentiation • negative regulation of transcription from RNA polymerase II promoter • cellular glucose homeostasis • negative regulation of autophagy • regulation of glucose metabolic process • response to starvation • negative regulation of transcription, DNA-templated • positive regulation of transcription, DNA-templated • canonical glycolysis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3607	68837
Ensembl	ENSG00000141568	ENSMUSG00000039275
UniProt	Q01167	Q3UCQ1
RefSeq (mRNA)	NM_004514 NM_181430 NM_181431	NM_001080932 NM_001363033
RefSeq (protein)	NP_004505	NP_001074401 NP_001349962
Location (UCSC)	Chr 17: 82.52 – 82.64 Mb	Chr 11: 121.26 – 121.31 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene contains a fork head DNA binding domain. This protein can bind to the purine-rich motifs of the HIV long terminal repeat (LTR), and to the similar purine-rich motif in the interleukin 2 (IL2) promoter. It may be involved in the regulation of viral and cellular promoter elements.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000141568 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039275 - 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. Durand DB, Shaw JP, Bush MR, Replogle RE, Belagaje R, Crabtree GR (Jul 1988). "Characterization of antigen receptor response elements within the interleukin-2 enhancer". Mol Cell Biol. 8 (4): 1715–24. PMC 363332. PMID 3260003.
6. "Entrez Gene: FOXK2 forkhead box K2".

Further reading

• Li C, Lusis AJ, Sparkes R, et al. (1992). "Characterization and chromosomal mapping of the gene encoding the cellular DNA binding protein ILF". Genomics. 13 (3): 665–71. doi:10.1016/0888-7543(92)90139-J. PMID 1339390.
• Li C, Lai CF, Sigman DS, Gaynor RB (1991). "Cloning of a cellular factor, interleukin binding factor, that binds to NFAT-like motifs in the human immunodeficiency virus long terminal repeat". Proc. Natl. Acad. Sci. U.S.A. 88 (17): 7739–43. doi:10.1073/pnas.88.17.7739. PMC 52378. PMID 1909027.
• Nirula A, Moore DJ, Gaynor RB (1997). "Constitutive binding of the transcription factor interleukin-2 (IL-2) enhancer binding factor to the IL-2 promoter". J. Biol. Chem. 272 (12): 7736–45. doi:10.1074/jbc.272.12.7736. PMID 9065434.
• Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
• Liu PP, Chen YC, Li C, et al. (2003). "Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a)". Proteins. 49 (4): 543–53. doi:10.1002/prot.10227. PMID 12402362.
• 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.
• 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.
• Tsai KL, Huang CY, Chang CH, et al. (2006). "Crystal structure of the human FOXK1a-DNA complex and its implications on the diverse binding specificity of winged helix/forkhead proteins". J. Biol. Chem. 281 (25): 17400–9. doi:10.1074/jbc.M600478200. PMID 16624804.
• Zody MC, Garber M, Adams DJ, et al. (2006). "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage". Nature. 440 (7087): 1045–9. doi:10.1038/nature04689. PMC 2610434. PMID 16625196.
• Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.

External links

• FOXK2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
• Overview of all the structural information available in the PDB for UniProt: Q01167 (Forkhead box protein K2) at the PDBe-KB.

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