HIF1AN

From Wikipedia, the free encyclopedia

Hypoxia-inducible factor 1, alpha subunit inhibitor

PDB rendering based on 1h2k.

Available structures: 1h2k, 1h2l, 1h2m, 1h2n, 1iz3, 1mze, 1mzf, 1yci, 2cgn, 2cgo

Identifiers

Symbol(s)

HIF1AN; DKFZp762F1811; FIH1; FLJ20615; FLJ22027

External IDs

OMIM: 606615 MGI: 2442345 HomoloGene: 9906

Gene ontology
Molecular Function:	• peptide-aspartate beta-dioxygenase activity • iron ion binding • protein binding • oxidoreductase activity • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen • metal ion binding
Cellular Component:	• nucleus
Biological Process:	• transcription • regulation of transcription, DNA-dependent

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_017902 (mRNA)
NP_060372 (protein)

NM_176958 (mRNA)
NP_795932 (protein)

Location

Chr 10: 102.29 - 102.3 Mb

Chr 19: 44.62 - 44.63 Mb

Pubmed search

[1]

[2]

Hypoxia-inducible factor 1, alpha subunit inhibitor, also known as HIF1AN, is a human gene.^[1]

[edit] References

^ Entrez Gene: HIF1AN hypoxia-inducible factor 1, alpha subunit inhibitor.

[edit] Further reading

Mahon PC, Hirota K, Semenza GL (2001). "FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity.". Genes Dev. 15 (20): 2675–86. doi:10.1101/gad.924501. PMID 11641274.
Lando D, Peet DJ, Whelan DA, et al. (2002). "Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch.". Science 295 (5556): 858–61. doi:10.1126/science.1068592. PMID 11823643.
Freedman SJ, Sun ZY, Poy F, et al. (2002). "Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha.". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5367–72. doi:10.1073/pnas.082117899. PMID 11959990.
Hewitson KS, McNeill LA, Riordan MV, et al. (2002). "Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family.". J. Biol. Chem. 277 (29): 26351–5. doi:10.1074/jbc.C200273200. PMID 12042299.
Lando D, Peet DJ, Gorman JJ, et al. (2002). "FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor.". Genes Dev. 16 (12): 1466–71. doi:10.1101/gad.991402. PMID 12080085.
Dann CE, Bruick RK, Deisenhofer J (2003). "Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway.". Proc. Natl. Acad. Sci. U.S.A. 99 (24): 15351–6. doi:10.1073/pnas.202614999. PMID 12432100.
Elkins JM, Hewitson KS, McNeill LA, et al. (2003). "Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha.". J. Biol. Chem. 278 (3): 1802–6. doi:10.1074/jbc.C200644200. PMID 12446723.
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.
Lee C, Kim SJ, Jeong DG, et al. (2003). "Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau.". J. Biol. Chem. 278 (9): 7558–63. doi:10.1074/jbc.M210385200. PMID 12482756.
Koivunen P, Hirsilä M, Günzler V, et al. (2004). "Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases.". J. Biol. Chem. 279 (11): 9899–904. doi:10.1074/jbc.M312254200. PMID 14701857.
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.
Linke S, Stojkoski C, Kewley RJ, et al. (2004). "Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor.". J. Biol. Chem. 279 (14): 14391–7. doi:10.1074/jbc.M313614200. PMID 14734545.
Kato H, Tamamizu-Kato S, Shibasaki F (2004). "Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity.". J. Biol. Chem. 279 (40): 41966–74. doi:10.1074/jbc.M406320200. PMID 15280364.
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.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Cockman ME, Lancaster DE, Stolze IP, et al. (2006). "Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).". Proc. Natl. Acad. Sci. U.S.A. 103 (40): 14767–72. doi:10.1073/pnas.0606877103. PMID 17003112.
Fukuba H, Yamashita H, Nagano Y, et al. (2007). "Siah-1 facilitates ubiquitination and degradation of factor inhibiting HIF-1alpha (FIH).". Biochem. Biophys. Res. Commun. 353 (2): 324–9. doi:10.1016/j.bbrc.2006.12.051. PMID 17188242.
Coleman ML, McDonough MA, Hewitson KS, et al. (2007). "Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.". J. Biol. Chem. 282 (33): 24027–38. doi:10.1074/jbc.M704102200. PMID 17573339.