UniProtKB - Q9GZT9 (EGLN1_HUMAN)
Egl nine homolog 1
EGLN1
Functioni
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.
7 PublicationsCaution
Catalytic activityi
- 2-oxoglutarate + L-prolyl-[hypoxia-inducible factor α subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-inducible factor α subunit]1 PublicationEC:1.14.11.291 Publication
Cofactori
Protein has several cofactor binding sites:- Fe2+PROSITE-ProRule annotationCombined sources3 PublicationsNote: Binds 1 Fe2+ ion per subunit.PROSITE-ProRule annotationCombined sources3 Publications
- L-ascorbate1 Publication
Activity regulationi
Kineticsi
- KM=70 nM for HIF2A1 Publication
- KM=150 µM for O21 Publication
- KM=1.3 µM for 2-oxoglutarate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 21 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 24 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 33 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 36 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 42 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 46 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 54 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 58 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 313 | IronCombined sources3 Publications | 1 | |
Metal bindingi | 315 | IronCombined sources3 Publications | 1 | |
Metal bindingi | 374 | IronCombined sources3 Publications | 1 | |
Binding sitei | 383 | 2-oxoglutarate1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 21 – 58 | MYND-type; atypicalPROSITE-ProRule annotationAdd BLAST | 38 |
GO - Molecular functioni
- 2-oxoglutarate-dependent dioxygenase activity Source: MGI
- enzyme binding Source: BHF-UCL
- ferrous iron binding Source: UniProtKB
- L-ascorbic acid binding Source: UniProtKB-KW
- peptidyl-proline 4-dioxygenase activity Source: FlyBase
- peptidyl-proline dioxygenase activity Source: GO_Central
GO - Biological processi
- cellular response to hypoxia Source: GO_Central
- negative regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
- negative regulation of DNA-binding transcription factor activity Source: HGNC-UCL
- oxygen homeostasis Source: HGNC-UCL
- peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: FlyBase
- regulation of angiogenesis Source: UniProtKB
- response to hypoxia Source: HGNC-UCL
- response to nitric oxide Source: UniProtKB
Keywordsi
Molecular function | Dioxygenase, Oxidoreductase |
Ligand | Iron, Metal-binding, Vitamin C, Zinc |
Enzyme and pathway databases
BRENDAi | 1.14.11.2, 2681 1.14.11.29, 2681 |
PathwayCommonsi | Q9GZT9 |
Reactomei | R-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha |
SABIO-RKi | Q9GZT9 |
SignaLinki | Q9GZT9 |
SIGNORi | Q9GZT9 |
Names & Taxonomyi
Protein namesi | Recommended name: Egl nine homolog 1 (EC:1.14.11.291 Publication)Alternative name(s): Hypoxia-inducible factor prolyl hydroxylase 2 Short name: HIF-PH2 Short name: HIF-prolyl hydroxylase 2 Short name: HPH-2 Prolyl hydroxylase domain-containing protein 2 Short name: PHD2 SM-20 |
Gene namesi | ORF Names:PNAS-118, PNAS-137 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:1232, EGLN1 |
MIMi | 606425, gene |
neXtProti | NX_Q9GZT9 |
VEuPathDBi | HostDB:ENSG00000135766 |
Pathology & Biotechi
Involvement in diseasei
Erythrocytosis, familial, 3 (ECYT3)2 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_027371 | 317 | P → R in ECYT3; marked decrease in enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs80358193EnsemblClinVar. | 1 | |
Natural variantiVAR_045902 | 371 | R → H in ECYT3; decreased interaction with HIF1A and EPAS1 and decreased enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs119476044EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 201 | C → A: Little change in enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 208 | C → A: Little change in enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 252 | R → A: Reduced C-terminal ODD domain (CODD) hydroxylation of HIF1A. | 1 | |
Mutagenesisi | 254 | D → A or K: Reduced C-terminal ODD domain (CODD) hxdroxylation of HIF1A. | 1 | |
Mutagenesisi | 266 | C → A: Little change in enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 283 | C → A: Little change in enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 302 | C → A: Slight increase in enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 303 | Y → F: No effect. 1 Publication | 1 | |
Mutagenesisi | 323 | C → A: Little change in enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 326 | C → A: Slight increase in enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 383 | R → A: Reduces enzyme activity by 95%. 1 Publication | 1 |
Keywords - Diseasei
Congenital erythrocytosis, Disease variantOrganism-specific databases
DisGeNETi | 54583 |
MalaCardsi | EGLN1 |
MIMi | 609820, phenotype |
OpenTargetsi | ENSG00000135766 |
Orphaneti | 247511, Autosomal dominant secondary polycythemia |
PharmGKBi | PA27670 |
Miscellaneous databases
Pharosi | Q9GZT9, Tclin |
Chemistry databases
ChEMBLi | CHEMBL5697 |
DrugBanki | DB00126, Ascorbic acid DB14490, Ferrous ascorbate DB14491, Ferrous fumarate DB14488, Ferrous gluconate DB14501, Ferrous glycine sulfate DB14489, Ferrous succinate DB08687, FG-2216 DB01592, Iron DB07112, N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE DB04847, Roxadustat |
DrugCentrali | Q9GZT9 |
GuidetoPHARMACOLOGYi | 2833 |
Genetic variation databases
BioMutai | EGLN1 |
DMDMi | 32129514 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000206661 | 2 – 426 | Egl nine homolog 1Add BLAST | 425 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineCombined sources | 1 | |
Modified residuei | 12 | PhosphoserineCombined sources | 1 | |
Modified residuei | 125 | PhosphoserineCombined sources | 1 | |
Modified residuei | 201 | S-nitrosocysteine1 Publication | 1 | |
Modified residuei | 208 | S-nitrosocysteine1 Publication | 1 | |
Modified residuei | 302 | S-nitrosocysteine1 Publication | 1 | |
Modified residuei | 323 | S-nitrosocysteine1 Publication | 1 | |
Modified residuei | 326 | S-nitrosocysteine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Phosphoprotein, S-nitrosylationProteomic databases
EPDi | Q9GZT9 |
jPOSTi | Q9GZT9 |
MassIVEi | Q9GZT9 |
MaxQBi | Q9GZT9 |
PaxDbi | Q9GZT9 |
PeptideAtlasi | Q9GZT9 |
PRIDEi | Q9GZT9 |
ProteomicsDBi | 80138 [Q9GZT9-1] 80139 [Q9GZT9-2] 80140 [Q9GZT9-3] |
PTM databases
GlyGeni | Q9GZT9, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q9GZT9 |
PhosphoSitePlusi | Q9GZT9 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000135766, Expressed in female gonad and 239 other tissues |
ExpressionAtlasi | Q9GZT9, baseline and differential |
Genevisiblei | Q9GZT9, HS |
Organism-specific databases
HPAi | ENSG00000135766, Tissue enhanced (skeletal) |
Interactioni
Subunit structurei
Monomer.
Interacts with ING4; the interaction inhibits the hydroxylation of HIF alpha proteins.
Interacts with PTGES3 (via PXLE motif); thereby recruiting EGLN1 to the HSP90 pathway to facilitate HIF alpha proteins hydroxylation.
Interacts with LIMD1.
Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2.
Interacts with EPAS1.
Interacts with CBFA2T3 (PubMed:25974097).
Interacts with HIF1A (PubMed:25974097).
8 PublicationsBinary interactionsi
Q9GZT9
GO - Molecular functioni
- enzyme binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 120060, 62 interactors |
CORUMi | Q9GZT9 |
DIPi | DIP-37495N |
ELMi | Q9GZT9 |
IntActi | Q9GZT9, 19 interactors |
MINTi | Q9GZT9 |
STRINGi | 9606.ENSP00000355601 |
Chemistry databases
BindingDBi | Q9GZT9 |
Miscellaneous databases
RNActi | Q9GZT9, protein |
Structurei
Secondary structure
3D structure databases
SMRi | Q9GZT9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9GZT9 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 291 – 392 | Fe2OG dioxygenasePROSITE-ProRule annotationAdd BLAST | 102 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 6 – 20 | Required for nuclear exportAdd BLAST | 15 | |
Regioni | 65 – 129 | DisorderedSequence analysisAdd BLAST | 65 | |
Regioni | 160 – 184 | DisorderedSequence analysisAdd BLAST | 25 | |
Regioni | 241 – 251 | Beta(2)beta(3) 'finger-like' loop1 PublicationAdd BLAST | 11 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 92 – 108 | Basic and acidic residuesSequence analysisAdd BLAST | 17 |
Domaini
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 21 – 58 | MYND-type; atypicalPROSITE-ProRule annotationAdd BLAST | 38 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
eggNOGi | KOG3710, Eukaryota |
GeneTreei | ENSGT00940000155704 |
HOGENOMi | CLU_022206_2_2_1 |
InParanoidi | Q9GZT9 |
OMAi | YQEKANL |
PhylomeDBi | Q9GZT9 |
TreeFami | TF314595 |
Family and domain databases
IDEALi | IID00345 |
InterProi | View protein in InterPro IPR005123, Oxoglu/Fe-dep_dioxygenase IPR006620, Pro_4_hyd_alph IPR044862, Pro_4_hyd_alph_FE2OG_OXY IPR002893, Znf_MYND |
Pfami | View protein in Pfam PF13640, 2OG-FeII_Oxy_3, 1 hit PF01753, zf-MYND, 1 hit |
SMARTi | View protein in SMART SM00702, P4Hc, 1 hit |
PROSITEi | View protein in PROSITE PS51471, FE2OG_OXY, 1 hit PS01360, ZF_MYND_1, 1 hit PS50865, ZF_MYND_2, 1 hit |
s (3+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MANDSGGPGG PSPSERDRQY CELCGKMENL LRCSRCRSSF YCCKEHQRQD
60 70 80 90 100
WKKHKLVCQG SEGALGHGVG PHQHSGPAPP AAVPPPRAGA REPRKAAARR
110 120 130 140 150
DNASGDAAKG KVKAKPPADP AAAASPCRAA AGGQGSAVAA EAEPGKEEPP
160 170 180 190 200
ARSSLFQEKA NLYPPSNTPG DALSPGGGLR PNGQTKPLPA LKLALEYIVP
210 220 230 240 250
CMNKHGICVV DDFLGKETGQ QIGDEVRALH DTGKFTDGQL VSQKSDSSKD
260 270 280 290 300
IRGDKITWIE GKEPGCETIG LLMSSMDDLI RHCNGKLGSY KINGRTKAMV
310 320 330 340 350
ACYPGNGTGY VRHVDNPNGD GRCVTCIYYL NKDWDAKVSG GILRIFPEGK
360 370 380 390 400
AQFADIEPKF DRLLFFWSDR RNPHEVQPAY ATRYAITVWY FDADERARAK
410 420
VKYLTGEKGV RVELNKPSDS VGKDVF
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A590UJ78 | A0A590UJ78_HUMAN | Egl nine homolog 1 | EGLN1 | 175 | Annotation score: | ||
A0A590UJT7 | A0A590UJT7_HUMAN | Egl nine homolog 1 | EGLN1 | 159 | Annotation score: | ||
A0A590UJZ0 | A0A590UJZ0_HUMAN | Egl nine homolog 1 | EGLN1 | 113 | Annotation score: | ||
A0A590UJD6 | A0A590UJD6_HUMAN | Egl nine homolog 1 | EGLN1 | 81 | Annotation score: |
Sequence cautioni
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_071858 | 4 | D → E Increased protection from polycythemia at high altitude; when associated with S-127. 2 PublicationsCorresponds to variant dbSNP:rs186996510EnsemblClinVar. | 1 | |
Natural variantiVAR_071859 | 127 | C → S Increased protection from polycythemia at high altitude; when associated with E-4. 2 PublicationsCorresponds to variant dbSNP:rs12097901EnsemblClinVar. | 1 | |
Natural variantiVAR_027371 | 317 | P → R in ECYT3; marked decrease in enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs80358193EnsemblClinVar. | 1 | |
Natural variantiVAR_045902 | 371 | R → H in ECYT3; decreased interaction with HIF1A and EPAS1 and decreased enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs119476044EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_042191 | 58 – 175 | CQGSE…DALSP → LLGGYRFAFSWNSDERA in isoform 3. 1 PublicationAdd BLAST | 118 | |
Alternative sequenceiVSP_007569 | 338 – 359 | Missing in isoform 2. 1 PublicationAdd BLAST | 22 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF246631, AF246630 Genomic DNA Translation: AAG34568.1 AF229245 mRNA Translation: AAG33965.1 AJ310543 mRNA Translation: CAC42509.1 AL833885 mRNA Translation: CAD38741.2 AF277174 mRNA Translation: AAK07534.1 Different initiation. AF277176 mRNA Translation: AAK07536.1 Frameshift. AL117352 Genomic DNA No translation available. AL445524 Genomic DNA No translation available. |
CCDSi | CCDS1595.1 [Q9GZT9-1] |
RefSeqi | NP_071334.1, NM_022051.2 [Q9GZT9-1] |
Genome annotation databases
Ensembli | ENST00000366641; ENSP00000355601; ENSG00000135766 |
GeneIDi | 54583 |
KEGGi | hsa:54583 |
MANE-Selecti | ENST00000366641.4; ENSP00000355601.3; NM_022051.3; NP_071334.1 |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF246631, AF246630 Genomic DNA Translation: AAG34568.1 AF229245 mRNA Translation: AAG33965.1 AJ310543 mRNA Translation: CAC42509.1 AL833885 mRNA Translation: CAD38741.2 AF277174 mRNA Translation: AAK07534.1 Different initiation. AF277176 mRNA Translation: AAK07536.1 Frameshift. AL117352 Genomic DNA No translation available. AL445524 Genomic DNA No translation available. |
CCDSi | CCDS1595.1 [Q9GZT9-1] |
RefSeqi | NP_071334.1, NM_022051.2 [Q9GZT9-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2G19 | X-ray | 1.70 | A | 181-417 | [»] | |
2G1M | X-ray | 2.20 | A | 181-426 | [»] | |
2HBT | X-ray | 1.60 | A | 188-426 | [»] | |
2HBU | X-ray | 1.85 | A | 188-426 | [»] | |
2Y33 | X-ray | 2.00 | A | 181-426 | [»] | |
2Y34 | X-ray | 2.01 | A | 181-426 | [»] | |
3HQR | X-ray | 2.00 | A | 181-426 | [»] | |
3HQU | X-ray | 2.30 | A | 181-426 | [»] | |
3OUH | X-ray | 2.51 | A | 181-416 | [»] | |
3OUI | X-ray | 1.70 | A | 181-392 | [»] | |
3OUJ | X-ray | 2.30 | A | 181-416 | [»] | |
4BQW | X-ray | 1.79 | A | 181-426 | [»] | |
4BQX | X-ray | 1.79 | A | 181-426 | [»] | |
4BQY | X-ray | 1.53 | A | 181-426 | [»] | |
4JZR | X-ray | 2.10 | A | 189-399 | [»] | |
4KBZ | X-ray | 2.15 | A | 184-419 | [»] | |
4UWD | X-ray | 1.72 | A | 181-426 | [»] | |
5A3U | X-ray | 3.30 | A/B/C | 181-426 | [»] | |
5L9B | X-ray | 1.95 | A/B | 181-426 | [»] | |
5L9R | X-ray | 1.81 | A | 181-426 | [»] | |
5L9V | X-ray | 1.83 | A/B | 181-426 | [»] | |
5LA9 | X-ray | 2.81 | A/B | 181-426 | [»] | |
5LAS | X-ray | 2.10 | A/B | 181-426 | [»] | |
5LAT | X-ray | 1.90 | A | 181-426 | [»] | |
5LB6 | X-ray | 1.70 | A | 181-426 | [»] | |
5LBB | X-ray | 1.70 | A | 181-426 | [»] | |
5LBC | X-ray | 1.82 | A | 181-426 | [»] | |
5LBE | X-ray | 1.75 | A | 181-426 | [»] | |
5LBF | X-ray | 1.90 | A | 181-426 | [»] | |
5OX5 | X-ray | 2.25 | A | 181-426 | [»] | |
5OX6 | X-ray | 1.99 | A | 181-426 | [»] | |
5V18 | X-ray | 2.15 | A | 181-416 | [»] | |
6NMQ | X-ray | 1.58 | A | 180-392 | [»] | |
6QGV | X-ray | 1.40 | A | 181-407 | [»] | |
6ST3 | X-ray | 2.43 | A/B | 181-407 | [»] | |
6YVT | X-ray | 2.85 | A/B/C/D/E/F | 181-426 | [»] | |
6YVW | X-ray | 1.97 | A | 181-426 | [»] | |
6YVX | X-ray | 1.80 | A | 181-426 | [»] | |
6YVZ | X-ray | 1.91 | A | 181-426 | [»] | |
6YW0 | X-ray | 2.20 | A | 181-426 | [»] | |
6YW1 | X-ray | 1.46 | A | 181-407 | [»] | |
6YW2 | X-ray | 2.14 | A | 181-407 | [»] | |
6YW3 | X-ray | 2.28 | A | 181-407 | [»] | |
6YW4 | X-ray | 1.53 | A | 181-407 | [»] | |
6ZBN | X-ray | 2.01 | A/B/C/D/E/F | 181-407 | [»] | |
6ZBO | X-ray | 1.79 | A/B/C/D/E/F | 181-407 | [»] | |
SMRi | Q9GZT9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 120060, 62 interactors |
CORUMi | Q9GZT9 |
DIPi | DIP-37495N |
ELMi | Q9GZT9 |
IntActi | Q9GZT9, 19 interactors |
MINTi | Q9GZT9 |
STRINGi | 9606.ENSP00000355601 |
Chemistry databases
BindingDBi | Q9GZT9 |
ChEMBLi | CHEMBL5697 |
DrugBanki | DB00126, Ascorbic acid DB14490, Ferrous ascorbate DB14491, Ferrous fumarate DB14488, Ferrous gluconate DB14501, Ferrous glycine sulfate DB14489, Ferrous succinate DB08687, FG-2216 DB01592, Iron DB07112, N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE DB04847, Roxadustat |
DrugCentrali | Q9GZT9 |
GuidetoPHARMACOLOGYi | 2833 |
PTM databases
GlyGeni | Q9GZT9, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q9GZT9 |
PhosphoSitePlusi | Q9GZT9 |
Genetic variation databases
BioMutai | EGLN1 |
DMDMi | 32129514 |
Proteomic databases
EPDi | Q9GZT9 |
jPOSTi | Q9GZT9 |
MassIVEi | Q9GZT9 |
MaxQBi | Q9GZT9 |
PaxDbi | Q9GZT9 |
PeptideAtlasi | Q9GZT9 |
PRIDEi | Q9GZT9 |
ProteomicsDBi | 80138 [Q9GZT9-1] 80139 [Q9GZT9-2] 80140 [Q9GZT9-3] |
Protocols and materials databases
Antibodypediai | 20799, 656 antibodies from 37 providers |
DNASUi | 54583 |
Genome annotation databases
Ensembli | ENST00000366641; ENSP00000355601; ENSG00000135766 |
GeneIDi | 54583 |
KEGGi | hsa:54583 |
MANE-Selecti | ENST00000366641.4; ENSP00000355601.3; NM_022051.3; NP_071334.1 |
Organism-specific databases
CTDi | 54583 |
DisGeNETi | 54583 |
GeneCardsi | EGLN1 |
HGNCi | HGNC:1232, EGLN1 |
HPAi | ENSG00000135766, Tissue enhanced (skeletal) |
MalaCardsi | EGLN1 |
MIMi | 606425, gene 609820, phenotype |
neXtProti | NX_Q9GZT9 |
OpenTargetsi | ENSG00000135766 |
Orphaneti | 247511, Autosomal dominant secondary polycythemia |
PharmGKBi | PA27670 |
VEuPathDBi | HostDB:ENSG00000135766 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3710, Eukaryota |
GeneTreei | ENSGT00940000155704 |
HOGENOMi | CLU_022206_2_2_1 |
InParanoidi | Q9GZT9 |
OMAi | YQEKANL |
PhylomeDBi | Q9GZT9 |
TreeFami | TF314595 |
Enzyme and pathway databases
BRENDAi | 1.14.11.2, 2681 1.14.11.29, 2681 |
PathwayCommonsi | Q9GZT9 |
Reactomei | R-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha |
SABIO-RKi | Q9GZT9 |
SignaLinki | Q9GZT9 |
SIGNORi | Q9GZT9 |
Miscellaneous databases
BioGRID-ORCSi | 54583, 94 hits in 1054 CRISPR screens |
ChiTaRSi | EGLN1, human |
EvolutionaryTracei | Q9GZT9 |
GeneWikii | EGLN1 |
GenomeRNAii | 54583 |
Pharosi | Q9GZT9, Tclin |
PROi | PR:Q9GZT9 |
RNActi | Q9GZT9, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000135766, Expressed in female gonad and 239 other tissues |
ExpressionAtlasi | Q9GZT9, baseline and differential |
Genevisiblei | Q9GZT9, HS |
Family and domain databases
IDEALi | IID00345 |
InterProi | View protein in InterPro IPR005123, Oxoglu/Fe-dep_dioxygenase IPR006620, Pro_4_hyd_alph IPR044862, Pro_4_hyd_alph_FE2OG_OXY IPR002893, Znf_MYND |
Pfami | View protein in Pfam PF13640, 2OG-FeII_Oxy_3, 1 hit PF01753, zf-MYND, 1 hit |
SMARTi | View protein in SMART SM00702, P4Hc, 1 hit |
PROSITEi | View protein in PROSITE PS51471, FE2OG_OXY, 1 hit PS01360, ZF_MYND_1, 1 hit PS50865, ZF_MYND_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | EGLN1_HUMAN | |
Accessioni | Q9GZT9Primary (citable) accession number: Q9GZT9 Secondary accession number(s): Q8N3M8, Q9BZS8, Q9BZT0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 16, 2003 |
Last sequence update: | March 1, 2001 | |
Last modified: | February 23, 2022 | |
This is version 197 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references