HIF1AN

Protein-coding gene in the species Homo sapiens
HIF1AN
Available structures
PDBOrtholog 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
AliasesHIF1AN, FIH1, hypoxia inducible factor 1 alpha subunit inhibitor, hypoxia inducible factor 1 subunit alpha inhibitor, HIFAN
External IDsOMIM: 606615; MGI: 2442345; HomoloGene: 9906; GeneCards: HIF1AN; OMA:HIF1AN - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for HIF1AN
Genomic location for HIF1AN
Band10q24.31Start100,529,072 bp[1]
End100,559,998 bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for HIF1AN
Genomic location for HIF1AN
Band19|19 C3Start44,551,289 bp[2]
End44,564,713 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 19: 44.55 – 44.56 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Hypoxia-inducible factor 1-alpha inhibitor is a protein that in humans is encoded by the HIF1AN gene.[5][6]

Interactions

HIF1AN has been shown to interact with HIF1A[5] and Von Hippel-Lindau tumor suppressor.[5] Additionally, asparaginyl hydroxylation of HIF1α by FIH-1 (HIF1AN) at N803 impairs its interaction with CBP/P300.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000166135 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036450 – 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. ^ a b c Mahon PC, Hirota K, Semenza GL (Oct 2001). "FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity". Genes Dev. 15 (20): 2675–86. doi:10.1101/gad.924501. PMC 312814. PMID 11641274.
  6. ^ "Entrez Gene: HIF1AN hypoxia-inducible factor 1, alpha subunit inhibitor".
  7. ^ Chen C, Lou T (2017). "Hypoxia inducible factors in hepatocellular carcinoma". Oncotarget. 8 (28): 46691–703. doi:10.18632/oncotarget.17358. PMC 5542303. PMID 28493839.

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. Bibcode:2002Sci...295..858L. doi:10.1126/science.1068592. PMID 11823643. S2CID 24045310.
  • 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. Bibcode:2002PNAS...99.5367F. 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • 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. Bibcode:2006PNAS..10314767C. 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.
  • Chen C, Lou T (2017). "Hypoxia inducible factors in hepatocellular carcinoma". Oncotarget. 8 (28): 46691–703. doi:10.18632/oncotarget.17358. PMC 5542303. PMID 28493839.


  • v
  • t
  • e
  • 1h2k: FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT PEPTIDE
    1h2k: FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT PEPTIDE
  • 1h2l: FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT PEPTIDE
    1h2l: FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT PEPTIDE
  • 1h2m: FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT PEPTIDE
    1h2m: FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT PEPTIDE
  • 1h2n: FACTOR INHIBITING HIF-1 ALPHA
    1h2n: FACTOR INHIBITING HIF-1 ALPHA
  • 1iz3: Dimeric structure of FIH (Factor inhibiting HIF)
    1iz3: Dimeric structure of FIH (Factor inhibiting HIF)
  • 1mze: Human Factor Inhibiting HIF (FIH1)
    1mze: Human Factor Inhibiting HIF (FIH1)
  • 1mzf: Human Factor inhibiting HIF (FIH1) in Complex with 2-oxoglutarate
    1mzf: Human Factor inhibiting HIF (FIH1) in Complex with 2-oxoglutarate
  • 1yci: Factor inhibiting HIF-1 alpha in complex with N-(carboxycarbonyl)-D-phenylalanine
    1yci: Factor inhibiting HIF-1 alpha in complex with N-(carboxycarbonyl)-D-phenylalanine
  • 2cgn: FACTOR INHIBITING HIF-1 ALPHA WITH SUCCINATE
    2cgn: FACTOR INHIBITING HIF-1 ALPHA WITH SUCCINATE
  • 2cgo: FACTOR INHIBITING HIF-1 ALPHA WITH FUMARATE
    2cgo: FACTOR INHIBITING HIF-1 ALPHA WITH FUMARATE


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