Details for: HIF1AN
Associated with
Other Information
Genular Protein ID: 2617169693
Symbol: HIF1N_HUMAN
Name: Hypoxia-inducible factor 1-alpha inhibitor
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 11641274
Title: FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity.
PubMed ID: 11641274
DOI: 10.1101/gad.924501
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 15164054
Title: The DNA sequence and comparative analysis of human chromosome 10.
PubMed ID: 15164054
DOI: 10.1038/nature02462
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 17974005
Title: The full-ORF clone resource of the German cDNA consortium.
PubMed ID: 17974005
PubMed ID: 12080085
Title: FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor.
PubMed ID: 12080085
DOI: 10.1101/gad.991402
PubMed ID: 12042299
Title: Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family.
PubMed ID: 12042299
PubMed ID: 15239670
Title: Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity.
PubMed ID: 15239670
DOI: 10.1042/bj20040735
PubMed ID: 14701857
Title: Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases.
PubMed ID: 14701857
PubMed ID: 14734545
Title: Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor.
PubMed ID: 14734545
PubMed ID: 17003112
Title: Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
PubMed ID: 17003112
PubMed ID: 18299578
Title: Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways.
PubMed ID: 18299578
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19245366
Title: MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH).
PubMed ID: 19245366
DOI: 10.1042/bj20081905
PubMed ID: 19726677
Title: Mint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in macrophages by suppressing the activity of factor inhibiting HIF-1.
PubMed ID: 19726677
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 22645313
Title: Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes.
PubMed ID: 22645313
DOI: 10.1128/mcb.00201-12
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 26948053
Title: NECAB3 promotes activation of hypoxia-inducible factor-1 during normoxia and enhances tumourigenicity of cancer cells.
PubMed ID: 26948053
DOI: 10.1038/srep22784
PubMed ID: 12432100
Title: Structure of factor-inhibiting hypoxia-inducible factor 1: an asparaginyl hydroxylase involved in the hypoxic response pathway.
PubMed ID: 12432100
PubMed ID: 12446723
Title: Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha.
PubMed ID: 12446723
PubMed ID: 12482756
Title: Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau.
PubMed ID: 12482756
PubMed ID: 15913349
Title: Selective inhibition of factor inhibiting hypoxia-inducible factor.
PubMed ID: 15913349
DOI: 10.1021/ja050841b
PubMed ID: 17135241
Title: Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates.
PubMed ID: 17135241
PubMed ID: 17573339
Title: Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
PubMed ID: 17573339
PubMed ID: 18611856
Title: Evidence that two enzyme-derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH).
PubMed ID: 18611856
PubMed ID: 20822901
Title: Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor.
PubMed ID: 20822901
PubMed ID: 20396966
Title: Crystal structures of human FIH-1 in complex with quinol family inhibitors.
PubMed ID: 20396966
PubMed ID: 21460794
Title: The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases.
PubMed ID: 21460794
PubMed ID: 21251231
Title: Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
PubMed ID: 21251231
PubMed ID: 21177872
Title: Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor.
PubMed ID: 21177872
Sequence Information:
- Length: 349
- Mass: 40285
- Checksum: 96A033BA7B3BD8C7
- Sequence:
MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMAN FQNFKPRSNR EEMKFHEFVE KLQDIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.