EGLN1
entrez
54583
canonical
uniprot
Q9GZT9
canonical
ensembl
ENSG00000135766
resolver
ensp
ENSP00000355601
resolver
ensp
ENSP00000674651
resolver
genesymbol
EGLN1
resolver
genesymbol_syn
C1orf12
resolver
hgnc
HGNC:1232
resolver
uniprot
Q8N3M8
resolver
uniprot
Q9BZS8
resolver
uniprot
Q9BZT0
resolver
uniprot
R4SCQ0
resolver
uniprot_entry
EGLN1_HUMAN
resolver
uniprot_entry
R4SCQ0_HUMAN
resolver
uniprot_sec
Q8N3M8
resolver
uniprot_sec
Q9BZS8
resolver
uniprot_sec
Q9BZT0
resolver
activity_regulation
ACTIVITY REGULATION: Following exposure to hypoxia, activated in HeLa cells but not in cardiovascular cells. {ECO:0000269|PubMed:12670503, ECO:0000269|PubMed:20840591}.
uniprot
proteins
amino_acid_sequence
MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQGSEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADPAAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF
uniprot
proteins
disease_involvement
DISEASE: Erythrocytosis, familial, 3 (ECYT3) [MIM:609820]: An autosomal dominant disorder characterized by elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels. {ECO:0000269|PubMed:16407130, ECO:0000269|PubMed:17579185}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.14.11.29
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:11595184, ECO:0000269|PubMed:12181324, ECO:0000269|PubMed:12351678, ECO:0000269|PubMed:15897452, ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:21792862, ECO:0000269|PubMed:25129147}.
uniprot
proteins
mass_dalton
46021
uniprot
proteins
mutagenesis
MUTAGEN 201; /note="C->A: Little change in enzyme activity."; /evidence="ECO:0000269|PubMed:21601578"; MUTAGEN 208; /note="C->A: Little change in enzyme activity."; /evidence="ECO:0000269|PubMed:21601578"; MUTAGEN 252; /note="R->A: Reduced C-terminal ODD domain (CODD) hydroxylation of HIF1A."; MUTAGEN 254; /note="D->A,K: Reduced C-terminal ODD domain (CODD) hxdroxylation of HIF1A."; MUTAGEN 266; /note="C->A: Little change in enzyme activity."; /evidence="ECO:0000269|PubMed:21601578"; MUTAGEN 283; /note="C->A: Little change in enzyme activity."; /evidence="ECO:0000269|PubMed:21601578"; MUTAGEN 302; /note="C->A: Slight increase in enzyme activity."; /evidence="ECO:0000269|PubMed:21601578"; MUTAGEN 303; /note="Y->F: No effect."; /evidence="ECO:0000269|PubMed:16782814"; MUTAGEN 323; /note="C->A: Little change in enzyme activity."; /evidence="ECO:0000269|PubMed:21601578"; MUTAGEN 326; /note="C->A: Slight increase in enzyme activity."; /evidence="ECO:0000269|PubMed:21601578"; MUTAGEN 383; /note="R->A: Reduces enzyme activity by 95%."; /evidence="ECO:0000269|PubMed:16782814
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation inhibits the enzyme activity up to 60% under aerobic conditions. Chelation of Fe(2+) has no effect on the S-nitrosylation. It is uncertain whether nitrosylation occurs on Cys-323 or Cys-326. {ECO:0000269|PubMed:21601578}.
uniprot
proteins
pubmed
11056053
uniprot
proteins
pubmed
11574160
uniprot
proteins
pubmed
11595178
uniprot
proteins
pubmed
11595184
uniprot
proteins
pubmed
12163023
uniprot
proteins
pubmed
12181324
uniprot
proteins
pubmed
12351678
uniprot
proteins
pubmed
12615973
uniprot
proteins
pubmed
12670503
uniprot
proteins
pubmed
12788921
uniprot
proteins
pubmed
15247232
uniprot
proteins
pubmed
15897452
uniprot
proteins
pubmed
16407130
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16782814
uniprot
proteins
pubmed
17579185
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18063574
uniprot
proteins
pubmed
19208626
uniprot
proteins
pubmed
19339211
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19604478
uniprot
proteins
pubmed
19631610
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20466884
uniprot
proteins
pubmed
20838600
uniprot
proteins
pubmed
20840591
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21601578
uniprot
proteins
pubmed
21792862
uniprot
proteins
pubmed
22286099
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23836663
uniprot
proteins
pubmed
24681946
uniprot
proteins
pubmed
24711448
uniprot
proteins
pubmed
25129147
uniprot
proteins
pubmed
25974097
uniprot
proteins
pubmed
28594552
uniprot
proteins
sequence_length
426
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12615973, ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:19631610}. Nucleus {ECO:0000269|PubMed:12615973, ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:19631610}. Note=Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm (PubMed:19631610). Nuclear export requires functional XPO1. {ECO:0000269|PubMed:19339211, ECO:0000269|PubMed:19631610}.
uniprot
proteins