HIF1AN
entrez
55662
canonical
uniprot
Q9NWT6
canonical
ensembl
ENSG00000166135
resolver
ensp
ENSP00000299163
resolver
ensp
ENSP00000530909
resolver
enst
ENST00000299163
resolver
genesymbol
HIF1AN
resolver
genesymbol_syn
FIH1
resolver
hgnc
HGNC:17113
resolver
uniprot
D3DR69
resolver
uniprot
Q5W147
resolver
uniprot
Q969Q7
resolver
uniprot
Q9NPV5
resolver
uniprot_entry
HIF1N_HUMAN
resolver
uniprot_sec
D3DR69
resolver
uniprot_sec
Q5W147
resolver
uniprot_sec
Q969Q7
resolver
uniprot_sec
Q9NPV5
resolver
amino_acid_sequence
MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN
uniprot
proteins
ec_number
1.14.11.30
uniprot
proteins
ec_number
1.14.11.n4
uniprot
proteins
function
FUNCTION: Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation. {ECO:0000269|PubMed:12042299, ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:17003112, ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:21177872, ECO:0000269|PubMed:21251231}.
uniprot
proteins
mass_dalton
40285
uniprot
proteins
mutagenesis
MUTAGEN 199; /note="H->A: Prevents suppression of HIFCAD activity. Strongly stimulates 2-oxoglutarate turnover. No stimulation of 2-oxoglutarate turnover; when associated with R-340."; /evidence="ECO:0000269|PubMed:12080085"; MUTAGEN 201; /note="D->A: Prevents suppression of HIFCAD activity."; /evidence="ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:18611856, ECO:0000269|PubMed:21177872"; MUTAGEN 201; /note="D->E: Loss of HIF1AAsn hydroxylation activity. Slightly stimulates 2-oxoglutarate turnover."; /evidence="ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:18611856, ECO:0000269|PubMed:21177872"; MUTAGEN 201; /note="D->G: No impact on HIF1AAsn hydroxylation activity. Loss of Asp hydroxylation ability. Strongly stimulates 2-oxoglutarate turnover. Loss of HIF1AAsn hydroxylation activity and slight stimulation of 2-oxoglutarate turnover; when associated with R-296."; /evidence="ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:18611856, ECO:0000269|PubMed:21177872"; MUTAGEN 239; /note="Q->H: No effect on Asp hydroxylation ability."; /evidence="ECO:0000269|PubMed:21177872"; MUTAGEN 296; /note="W->R: Loss of HIF1AAsn hydroxylation activity and slight stimulation of 2-oxoglutarate turnover; when associated with G-201."; /evidence="ECO:0000269|PubMed:18611856"; MUTAGEN 340; /note="L->R: Impairs dimer formation, leading to loss of HIF1AAsn hydroxylation activity. No stimulation of 2-oxoglutarate turnover; when associated with A-201."; /evidence="ECO:0000269|PubMed:15239670, ECO:0000269|PubMed:18611856"; MUTAGEN 344; /note="I->R: No effect on dimer formation and HIF1AAsn hydroxylation activity."; /evidence="ECO:0000269|PubMed:15239670
uniprot
proteins
pubmed
11641274
uniprot
proteins
pubmed
12042299
uniprot
proteins
pubmed
12080085
uniprot
proteins
pubmed
12432100
uniprot
proteins
pubmed
12446723
uniprot
proteins
pubmed
12482756
uniprot
proteins
pubmed
14701857
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14734545
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15239670
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15913349
uniprot
proteins
pubmed
17003112
uniprot
proteins
pubmed
17135241
uniprot
proteins
pubmed
17573339
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18299578
uniprot
proteins
pubmed
18611856
uniprot
proteins
pubmed
19245366
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19726677
uniprot
proteins
pubmed
20396966
uniprot
proteins
pubmed
20822901
uniprot
proteins
pubmed
21177872
uniprot
proteins
pubmed
21251231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21460794
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22645313
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
26948053
uniprot
proteins
sequence_length
349
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Mainly cytoplasmic localization, but interaction with NOTCH1 results in nuclear localization and interaction with ABPA3 results in perinuclear localization in macrophages.
uniprot
proteins