HIF1AN

HIF1AN
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1H2K, 1H2L, 1H2M, 1H2N, 1IZ3, 1MZE, 1MZF, 1YCI, 2CGN, 2CGO, 2ILM, 2W0X, 2WA3, 2WA4, 2XUM, 2Y0I, 2YC0, 2YDE, 3D8C, 3KCX, 3KCY, 3OD4, 3P3N, 3P3P, 4AI8, 4B7E, 4B7K, 4BIO, 4JAA, 4NR1, 4Z2W, 4Z1V
Identifiers
Aliases	HIF1AN, FIH1, hypoxia inducible factor 1 alpha subunit inhibitor, hypoxia inducible factor 1 subunit alpha inhibitor, HIFAN
External IDs	OMIM: 606615; MGI: 2442345; HomoloGene: 9906; GeneCards: HIF1AN; OMA:HIF1AN - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10q24.31 Start 100,529,072 bp End 100,559,998 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 C3 Start 44,551,289 bp End 44,564,713 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle Skeletal muscle tissue of rectus abdominis muscle of thigh glutes tendon of biceps brachii stromal cell of endometrium triceps brachii muscle quadriceps femoris muscle vastus lateralis muscle islet of Langerhans Top expressed in muscle of thigh knee joint skeletal muscle tissue triceps brachii muscle vastus lateralis muscle sternocleidomastoid muscle tibialis anterior muscle temporal muscle digastric muscle gastrocnemius muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function iron ion binding peptidyl-asparagine 3-dioxygenase activity protein homodimerization activity ankyrin repeat binding zinc ion binding dioxygenase activity metal ion binding NF-kappaB binding Notch binding protein binding carboxylic acid binding oxidoreductase activity peptidyl-histidine dioxygenase activity oxygen gasoreceptor activity 2-oxoglutarate-dependent dioxygenase activity hypoxia-inducible factor-asparagine oxygenase activity Cellular component cytoplasm nucleoplasm perinuclear region of cytoplasm nucleus cytosol Biological process regulation of transcription, DNA-templated peptidyl-histidine hydroxylation transcription, DNA-templated peptidyl-aspartic acid hydroxylation peptidyl-asparagine hydroxylation positive regulation of myoblast differentiation positive regulation of vasculogenesis regulation of transcription from RNA polymerase II promoter in response to hypoxia negative regulation of transcription from RNA polymerase II promoter in response to hypoxia negative regulation of Notch signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 55662 319594 Ensembl ENSG00000166135 ENSMUSG00000036450 UniProt Q9NWT6 Q8BLR9 RefSeq (mRNA) NM_017902 NM_176958 RefSeq (protein) NP_060372 NP_795932 Location (UCSC) Chr 10: 100.53 – 100.56 Mb Chr 19: 44.55 – 44.56 Mb PubMed search
Wikidata
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Hypoxia-inducible factor 1-alpha inhibitor is a protein that in humans is encoded by the HIF1AN gene.

Interactions

HIF1AN has been shown to interact with HIF1A and Von Hippel-Lindau tumor suppressor.

Further reading

• Lando D, Peet DJ, Whelan DA, Gorman JJ, Whitelaw ML (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, Kung AL, Livingston DM, Wagner G, Eck MJ (2002). "Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1α". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5367–72. doi:10.1073/pnas.082117899. PMC 122775. PMID 11959990.
• Hewitson KS, McNeill LA, Riordan MV, Tian YM, Bullock AN, Welford RW, Elkins JM, Oldham NJ, Bhattacharya S, Gleadle JM, Ratcliffe PJ, Pugh CW, Schofield CJ (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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Lando D, Peet DJ, Gorman JJ, Whelan DA, Whitelaw ML, Bruick RK (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. PMC 186346. 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. PMC 137720. PMID 12432100.
• Elkins JM, Hewitson KS, McNeill LA, Seibel JF, Schlemminger I, Pugh CW, Ratcliffe PJ, Schofield CJ (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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Lee C, Kim SJ, Jeong DG, Lee SM, Ryu SE (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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Koivunen P, Hirsilä M, Günzler V, Kivirikko KI, Myllyharju J (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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Linke S, Stojkoski C, Kewley RJ, Booker GW, Whitelaw ML, Peet DJ (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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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, Hewitson KS, McDonough MA, Coleman ML, Coles CH, Yu X, Hay RT, Ley SC, Pugh CW, Oldham NJ, Masson N, Schofield CJ, Ratcliffe PJ (2006). "Posttranslational hydroxylation of ankyrin repeats in IκB 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. PMC 1578504. PMID 17003112.
• Coleman ML, McDonough MA, Hewitson KS, Coles C, Mecinovic J, Edelmann M, Cook KM, Cockman ME, Lancaster DE, Kessler BM, Oldham NJ, Ratcliffe PJ, Schofield CJ (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.{{cite journal}}: CS1 maint: unflagged free DOI (link)