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Protein Page:
EGLN1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
EGLN1 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. Monomer. Interacts with ING4; the interaction inhibits the hydroxylation of HIFs. Interacts with LIMD1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with EPAS1. According to PubMed:11056053, widely expressed with highest levels in skeletal muscle and heart, moderate levels in pancreas, brain (dopaminergic neurons of adult and fetal substantia nigra) and kidney, and lower levels in lung and liver. According to PubMed:12351678 widely expressed with highest levels in brain, kidney and adrenal gland. Expressed in cardiac myocytes, aortic endothelial cells and coronary artery smooth muscle. According to PubMed:12788921; expressed in adult and fetal heart, brain, liver, lung, skeletal muscle and kidney. Also expressed in placenta. Highest levels in adult heart, brain, lung and liver and fetal brain, heart spleen and skeletal muscle. Following exposure to hypoxia, activated in HeLa cells but not in cardiovascular cells. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 1.14.11.29; EC 1.14.11.-; Oxidoreductase
Cellular Component: cytoplasm; cytosol; nucleus
Molecular Function: peptidyl-proline dioxygenase activity; protein binding; enzyme binding; L-ascorbic acid binding; iron ion binding; peptidyl-proline 4-dioxygenase activity
Biological Process: oxygen homeostasis; negative regulation of cAMP catabolic process; negative regulation of transcription factor activity; cardiac muscle morphogensis; response to hypoxia; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; negative regulation of cyclic-nucleotide phosphodiesterase activity; regulation of angiogenesis
Reference #:  Q9GZT9 (UniProtKB)
Alt. Names/Synonyms: C1orf12; DKFZp761F179; ECYT3; Egl nine homolog 1; egl nine homolog 1 (C. elegans); egl nine-like protein 1; EGLN1; HIF prolyl hydroxylase 2; HIF-PH2; HIF-prolyl hydroxylase 2; HIFPH2; HPH-2; HPH2; Hypoxia-inducible factor prolyl hydroxylase 2; PHD2; Prolyl hydroxylase domain-containing protein 2; SM-20; SM20; zinc finger MYND domain-containing protein 6; ZMYND6
Gene Symbols: EGLN1
Molecular weight: 46,021 Da
Basal Isoelectric point: 8.83  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

EGLN1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S12-p SGGPGGPsPSERDRQ
0 11 S125-p ADPAAAAsPCRAAAG
0 1 R152 GKEEPPARSSLFQEK
0 1 S154 EEPPARSSLFQEKAN
0 1 S174-p NTPGDALsPGGGLRP
0 1 T232-p EVRALHDtGkFTDGQ
0 1 K234-ub RALHDtGkFTDGQLV
0 1 K244-m1 DGQLVSQkSDSSKDI
0 1 T405-p RAKVKYLtGEKGVRV
  mouse

 
S12 SGGPGVLSASERDRQ
S114 EDAAQARSGPGPAEP
S129-p GSEDPPLsRsPGPER
S131-p EDPPLsRsPGPERAS
S151 GGPGEALSPGGGLRP
T209 EVRALHDTGKFTDGQ
K211 RALHDTGKFTDGQLV
K221 DGQLVSQKSDSSKDI
T382 RAKVKYLTGEKGVRV
  rat

 
- gap
- gap
- gap
- gap
- gap
T31 EVRALHDTGKFTDGQ
K33 RALHDTGKFTDGQLV
K43 DGQLVSQKSDSSKDI
T204 RAKVKYLTGEKGVRV
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