Egln1
entrez
112405
canonical
uniprot
Q91YE3
canonical
ensembl
ENSMUSG00000031987
resolver
ensp
ENSMUSP00000034469
resolver
ensp
ENSMUSP00000230716
resolver
enst
ENSMUST00000034469
resolver
genesymbol
Egln1
resolver
uniprot
Q8VHJ2
resolver
uniprot
Q922P3
resolver
uniprot_entry
EGLN1_MOUSE
resolver
uniprot_sec
Q8VHJ2
resolver
uniprot_sec
Q922P3
resolver
amino_acid_sequence
MASDSGGPGVLSASERDRQYCELCGKMENLLRCGRCRSSFYCCKEHQRQDWKKHKLVCQGGEAPRAQPAPAQPRVAPPPGGAPGAARAGGAARRGDSAAASRVPGPEDAAQARSGPGPAEPGSEDPPLSRSPGPERASLCPAGGGPGEALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGRETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDQITWIEGKEPGCETIGLLMSSMDDLIRHCSGKLGNYRINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELKPNSVSKDV
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:18096761, ECO:0000269|PubMed:18500250, ECO:0000269|PubMed:21435465}.
uniprot
proteins
mass_dalton
43111
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-300 or Cys-303. {ECO:0000250|UniProtKB:Q9GZT9}.
uniprot
proteins
pubmed
10543731
uniprot
proteins
pubmed
11574160
uniprot
proteins
pubmed
12234095
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18096761
uniprot
proteins
pubmed
18500250
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21435465
uniprot
proteins
sequence_length
400
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZT9}. Nucleus {ECO:0000250|UniProtKB:Q9GZT9}. Note=Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm. Nuclear export requires functional XPO1. {ECO:0000250|UniProtKB:Q9GZT9}.
uniprot
proteins