Details for: EGLN1

Gene ID: 54583

Symbol: EGLN1

Ensembl ID: ENSG00000135766

Description: egl-9 family hypoxia inducible factor 1

Associated with

Other Information

Genular Protein ID: 3581941013

Symbol: EGLN1_HUMAN

Name: Egl nine homolog 1

UniProtKB Accession Codes:

Q9GZT9 Q8N3M8 Q9BZS8 Q9BZT0

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BRENDA 2 Bgee 1 BindingDB 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CORUM 1 CTD 1 ChEBI 20 ChEMBL 1 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DrugBank 12 DrugCentral 1 EC 1 ELM 1 EMBL 9 EPD 1 Ensembl 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 29 Gene3D 2 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyGen 1 GuidetoPHARMACOLOGY 1 HGNC 2 HOGENOM 1 HPA 1 IDEAL 1 InParanoid 1 IntAct 1 InterPro 4 KEGG 1 MANE-Select 1 MIM 3 MINT 1 MalaCards 1 MassIVE 1 MaxQB 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 1 OrthoDB 1 PANTHER 2 PDB 65 PDBsum 50 PRO 1 PROSITE 3 PROSITE-ProRule 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 2 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 3 Pumba 1 RNAct 1 Reactome 1 RefSeq 1 Rhea 3 SABIO-RK 1 SAM 1 SIGNOR 1 SMART 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 TreeFam 1 UniProtKB 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 11056053

Title: Mapping, characterization, and expression analysis of the SM-20 human homologue, C1orf12, and identification of a novel related gene, SCAND2.

PubMed ID: 11056053

DOI: 10.1006/geno.2000.6343

PubMed ID: 11574160

Title: Characterization and comparative analysis of the EGLN gene family.

PubMed ID: 11574160

DOI: 10.1016/s0378-1119(01)00633-3

PubMed ID: 12788921

Title: Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor.

PubMed ID: 12788921

DOI: 10.1074/jbc.m304982200

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 11595178

Title: HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus.

PubMed ID: 11595178

DOI: 10.1016/s0092-8674(01)00518-9

PubMed ID: 11595184

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

PubMed ID: 11595184

DOI: 10.1016/s0092-8674(01)00507-4

PubMed ID: 12181324

Title: Sequence determinants in hypoxia-inducible factor-1alpha for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3.

PubMed ID: 12181324

DOI: 10.1074/jbc.m206955200

PubMed ID: 12351678

Title: Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor.

PubMed ID: 12351678

DOI: 10.1073/pnas.192342099

PubMed ID: 12163023

Title: Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors.

PubMed ID: 12163023

DOI: 10.1016/s0006-291x(02)00862-8

PubMed ID: 12670503

Title: Differential regulation of HIF-1alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells.

PubMed ID: 12670503

DOI: 10.1016/s0006-291x(03)00453-4

PubMed ID: 12615973

Title: Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing.

PubMed ID: 12615973

DOI: 10.1242/jcs.00318

PubMed ID: 15247232

Title: Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor.

PubMed ID: 15247232

DOI: 10.1074/jbc.m406026200

PubMed ID: 15897452

Title: The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF).

PubMed ID: 15897452

DOI: 10.1073/pnas.0502716102

PubMed ID: 18063574

Title: Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases.

PubMed ID: 18063574

DOI: 10.1074/jbc.m707411200

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: 19631610

Title: Cellular oxygen sensing: Importins and exportins are mediators of intracellular localisation of prolyl-4-hydroxylases PHD1 and PHD2.

PubMed ID: 19631610

DOI: 10.1016/j.bbrc.2009.07.090

PubMed ID: 19339211

Title: Role of the intracellular localization of HIF-prolyl hydroxylases.

PubMed ID: 19339211

DOI: 10.1016/j.bbamcr.2009.01.014

PubMed ID: 19208626

Title: Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical role for residues C-terminal to the hydroxylacceptor proline.

PubMed ID: 19208626

DOI: 10.1074/jbc.m808737200

PubMed ID: 20840591

Title: Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen.

PubMed ID: 20840591

DOI: 10.1111/j.1742-4658.2010.07804.x

PubMed ID: 20838600

Title: Identifying signatures of natural selection in Tibetan and Andean populations using dense genome scan data.

PubMed ID: 20838600

DOI: 10.1371/journal.pgen.1001116

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 20466884

Title: Genetic evidence for high-altitude adaptation in Tibet.

PubMed ID: 20466884

DOI: 10.1126/science.1189406

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21792862

Title: Prolyl hydroxylase-2 (PHD2) exerts tumor-suppressive activity in pancreatic cancer.

PubMed ID: 21792862

DOI: 10.1002/cncr.26344

PubMed ID: 22286099

Title: The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity.

PubMed ID: 22286099

DOI: 10.1038/ncb2424

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24681946

Title: SIRT2 regulates tumour hypoxia response by promoting HIF-1alpha hydroxylation.

PubMed ID: 24681946

DOI: 10.1038/onc.2014.76

PubMed ID: 25974097

Title: Myeloid translocation gene-16 co-repressor promotes degradation of hypoxia-inducible factor 1.

PubMed ID: 25974097

DOI: 10.1371/journal.pone.0123725

PubMed ID: 16782814

Title: Cellular oxygen sensing: crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2).

PubMed ID: 16782814

DOI: 10.1073/pnas.0601283103

PubMed ID: 19604478

Title: Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases.

PubMed ID: 19604478

DOI: 10.1016/j.str.2009.06.002

PubMed ID: 21601578

Title: Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).

PubMed ID: 21601578

DOI: 10.1016/j.jmb.2011.04.075

PubMed ID: 28594552

Title: 1,2,4-Triazolo-[1,5-a]pyridine HIF Prolylhydroxylase Domain-1 (PHD-1) Inhibitors With a Novel Monodentate Binding Interaction.

PubMed ID: 28594552

DOI: 10.1021/acs.jmedchem.7b00352

PubMed ID: 16407130

Title: A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis.

PubMed ID: 16407130

DOI: 10.1073/pnas.0508423103

PubMed ID: 17579185

Title: A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove.

PubMed ID: 17579185

DOI: 10.1182/blood-2007-04-084434

PubMed ID: 24711448

Title: Defective Tibetan PHD2 binding to p23 links high altitude adaption to altered oxygen sensing.

PubMed ID: 24711448

DOI: 10.1074/jbc.m113.541227

PubMed ID: 25129147

Title: A genetic mechanism for Tibetan high-altitude adaptation.

PubMed ID: 25129147

DOI: 10.1038/ng.3067

Sequence Information:

  • Length: 426
  • Mass: 46021
  • Checksum: 81A97FF772CAA14C
  • Sequence:
    • MANDSGGPGG PSPSERDRQY CELCGKMENL LRCSRCRSSF YCCKEHQRQD WKKHKLVCQG 
SEGALGHGVG PHQHSGPAPP AAVPPPRAGA REPRKAAARR DNASGDAAKG KVKAKPPADP 
AAAASPCRAA AGGQGSAVAA EAEPGKEEPP ARSSLFQEKA NLYPPSNTPG DALSPGGGLR 
PNGQTKPLPA LKLALEYIVP CMNKHGICVV DDFLGKETGQ QIGDEVRALH DTGKFTDGQL 
VSQKSDSSKD IRGDKITWIE GKEPGCETIG LLMSSMDDLI RHCNGKLGSY KINGRTKAMV 
ACYPGNGTGY VRHVDNPNGD GRCVTCIYYL NKDWDAKVSG GILRIFPEGK AQFADIEPKF 
DRLLFFWSDR RNPHEVQPAY ATRYAITVWY FDADERARAK VKYLTGEKGV RVELNKPSDS 
VGKDVF

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.