Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803 (Q24306213)

Gene Ontology release 2020-05-02

Gene Ontology ID

GO:0036140

Hypoxia inducible factor 1 subunit alpha inhibitor

1 reference

GOA release 2020-03-11

author

Christopher J. Schofield

6

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Louise E Horsfall

object named as

Louise E Horsfall

5

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author name string

Luke A McNeill

1

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Kirsty S Hewitson

2

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Timothy D Claridge

3

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Jürgen F Seibel

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

4

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language of work or name

English

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publication date

1 November 2002

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published in

Biochemical Journal

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volume

367

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page(s)

571-5

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issue

Pt 3

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cites work

1 reference

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19 March 2017

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Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

19 March 2017

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Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha

19 March 2017

1 reference

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FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity

19 March 2017

1 reference

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A conserved family of prolyl-4-hydroxylases that modify HIF

19 March 2017

1 reference

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C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

19 March 2017

1 reference

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HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation

19 March 2017

1 reference

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HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

19 March 2017

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Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma

19 March 2017

1 reference

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Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

19 March 2017

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Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response

19 March 2017

1 reference

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Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

19 March 2017

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Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family

19 March 2017

1 reference

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Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

19 March 2017

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Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation

19 March 2017

1 reference

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Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1

19 March 2017

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Partial purification and characterization of bovine liver aspartyl beta-hydroxylase

19 March 2017

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Occurrence of beta-hydroxylated asparagine residues in non-vitamin K-dependent proteins containing epidermal growth factor-like domains

19 March 2017

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Hydroxylation of aspartic acid in domains homologous to the epidermal growth factor precursor is catalyzed by a 2-oxoglutarate-dependent dioxygenase

27 September 2017

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1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X.

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27 September 2017

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Asymmetric synthesis of orthogonally protected L-threo-beta-hydroxyasparagine

27 September 2017

1 reference

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A model for the complex between the hypoxia-inducible factor-1 (HIF-1) and its consensus DNA sequence

29 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12215170