Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Hypoxia-inducible factor 1-alpha inhibitor (EC 1.14.11.30) (EC 1.14.11.n4) (Factor inhibiting HIF-1) (FIH-1) (Hypoxia-inducible factor asparagine hydroxylase)

 HIF1N_HUMAN             Reviewed;         349 AA.
Q9NWT6; D3DR69; Q5W147; Q969Q7; Q9NPV5;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
16-JUN-2003, sequence version 2.
20-DEC-2017, entry version 162.
RecName: Full=Hypoxia-inducible factor 1-alpha inhibitor;
EC=1.14.11.30;
EC=1.14.11.n4;
AltName: Full=Factor inhibiting HIF-1;
Short=FIH-1;
AltName: Full=Hypoxia-inducible factor asparagine hydroxylase;
Name=HIF1AN; Synonyms=FIH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HIF1A; VHL AND
HISTONE DEACETYLASES.
TISSUE=Brain;
PubMed=11641274; DOI=10.1101/gad.924501;
Mahon P.C., Hirota K., Semenza G.L.;
"FIH-1: a novel protein that interacts with HIF-1alpha and VHL to
mediate repression of HIF-1 transcriptional activity.";
Genes Dev. 15:2675-2686(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Signet-ring cell carcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-41.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-349.
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF HIS-199 AND ASP-201.
PubMed=12080085; DOI=10.1101/gad.991402;
Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L.,
Bruick R.K.;
"FIH-1 is an asparaginyl hydroxylase enzyme that regulates the
transcriptional activity of hypoxia-inducible factor.";
Genes Dev. 16:1466-1471(2002).
[8]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=12042299; DOI=10.1074/jbc.C200273200;
Hewitson K.S., McNeill L.A., Riordan M.V., Tian Y.-M., Bullock A.N.,
Welford R.W., Elkins J.M., Oldham N.J., Bhattacharya S., Gleadle J.M.,
Ratcliffe P.J., Pugh C.W., Schofield C.J.;
"Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to
factor inhibiting HIF (FIH) and is related to the cupin structural
family.";
J. Biol. Chem. 277:26351-26355(2002).
[9]
DIMERIZATION, MASS SPECTROMETRY, AND MUTAGENESIS OF LEU-340 AND
ILE-344.
PubMed=15239670; DOI=10.1042/BJ20040735;
Lancaster D.E., McNeill L.A., McDonough M.A., Aplin R.T.,
Hewitson K.S., Pugh C.W., Ratcliffe P.J., Schofield C.J.;
"Disruption of dimerization and substrate phosphorylation inhibit
factor inhibiting hypoxia-inducible factor (FIH) activity.";
Biochem. J. 383:429-437(2004).
[10]
CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=14701857; DOI=10.1074/jbc.M312254200;
Koivunen P., Hirsila M., Gunzler V., Kivirikko K.I., Myllyharju J.;
"Catalytic properties of the asparaginyl hydroxylase (FIH) in the
oxygen sensing pathway are distinct from those of its prolyl 4-
hydroxylases.";
J. Biol. Chem. 279:9899-9904(2004).
[11]
SUBCELLULAR LOCATION.
PubMed=14734545; DOI=10.1074/jbc.M313614200;
Linke S., Stojkoski C., Kewley R.J., Booker G.W., Whitelaw M.L.,
Peet D.J.;
"Substrate requirements of the oxygen-sensing asparaginyl hydroxylase
factor-inhibiting hypoxia-inducible factor.";
J. Biol. Chem. 279:14391-14397(2004).
[12]
FUNCTION, INTERACTION WITH NFKB1 AND NFKBIA, AND CATALYTIC ACTIVITY.
PubMed=17003112; DOI=10.1073/pnas.0606877103;
Cockman M.E., Lancaster D.E., Stolze I.P., Hewitson K.S.,
McDonough M.A., Coleman M.L., Coles C.H., Yu X., Hay R.T., Ley S.C.,
Pugh C.W., Oldham N.J., Masson N., Schofield C.J., Ratcliffe P.J.;
"Posttranslational hydroxylation of ankyrin repeats in IkappaB
proteins by the hypoxia-inducible factor (HIF) asparaginyl
hydroxylase, factor inhibiting HIF (FIH).";
Proc. Natl. Acad. Sci. U.S.A. 103:14767-14772(2006).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=18299578; DOI=10.1073/pnas.0711591105;
Zheng X., Linke S., Dias J.M., Zheng X., Gradin K., Wallis T.P.,
Hamilton B.R., Gustafsson M., Ruas J.L., Wilkins S., Bilton R.L.,
Brismar K., Whitelaw M.L., Pereira T., Gorman J.J., Ericson J.,
Peet D.J., Lendahl U., Poellinger L.;
"Interaction with factor inhibiting HIF-1 defines an additional mode
of cross-coupling between the Notch and hypoxia signaling pathways.";
Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
FUNCTION, INTERACTION WITH PPP1R12A, AND CATALYTIC ACTIVITY.
PubMed=19245366; DOI=10.1042/BJ20081905;
Webb J.D., Muranyi A., Pugh C.W., Ratcliffe P.J., Coleman M.L.;
"MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is
a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-
inducible factor (FIH).";
Biochem. J. 420:327-333(2009).
[16]
INTERACTION WITH APBA3, AND SUBCELLULAR LOCATION.
PubMed=19726677; DOI=10.1074/jbc.M109.019216;
Sakamoto T., Seiki M.;
"Mint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in
macrophages by suppressing the activity of factor inhibiting HIF-1.";
J. Biol. Chem. 284:30350-30359(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
INTERACTION WITH UBE3A.
PubMed=22645313; DOI=10.1128/MCB.00201-12;
Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M.,
Harper J.W., Howley P.M.;
"Identification and proteomic analysis of distinct UBE3A/E6AP protein
complexes.";
Mol. Cell. Biol. 32:3095-3106(2012).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
INTERACTION WITH NECAB3.
PubMed=26948053; DOI=10.1038/srep22784;
Nakaoka H.J., Hara T., Yoshino S., Kanamori A., Matsui Y.,
Shimamura T., Sato H., Murakami Y., Seiki M., Sakamoto T.;
"NECAB3 promotes activation of hypoxia-inducible factor-1 during
normoxia and enhances tumourigenicity of cancer cells.";
Sci. Rep. 6:22784-22784(2016).
[22]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH IRON AND
2-OXOGLUTARATE, AND SUBUNIT.
PubMed=12432100; DOI=10.1073/pnas.202614999;
Dann C.E. III, Bruick R.K., Deisenhofer J.;
"Structure of factor-inhibiting hypoxia-inducible factor 1: an
asparaginyl hydroxylase involved in the hypoxic response pathway.";
Proc. Natl. Acad. Sci. U.S.A. 99:15351-15356(2002).
[23]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH 786-826 OF
HIF1A; IRON; ZINC AND 2-OXOGLUTARATE.
PubMed=12446723; DOI=10.1074/jbc.C200644200;
Elkins J.M., Hewitson K.S., McNeill L.A., Seibel J.F.,
Schlemminger I., Pugh C.W., Ratcliffe P.J., Schofield C.J.;
"Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals
mechanism of oxidative modification of HIF-1 alpha.";
J. Biol. Chem. 278:1802-1806(2003).
[24]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND SUBUNIT.
PubMed=12482756; DOI=10.1074/jbc.M210385200;
Lee C., Kim S.J., Jeong D.G., Lee S.M., Ryu S.E.;
"Structure of human FIH-1 reveals a unique active site pocket and
interaction sites for HIF-1 and von Hippel-Lindau.";
J. Biol. Chem. 278:7558-7563(2003).
[25]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH IRON AND
INHIBITOR.
PubMed=15913349; DOI=10.1021/ja050841b;
McDonough M.A., McNeill L.A., Tilliet M., Papamicael C.A., Chen Q.Y.,
Banerji B., Hewitson K.S., Schofield C.J.;
"Selective inhibition of factor inhibiting hypoxia-inducible factor.";
J. Am. Chem. Soc. 127:7680-7681(2005).
[26]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH IRON; SUCCINATE
AND FUMARATE.
PubMed=17135241; DOI=10.1074/jbc.M608337200;
Hewitson K.S., Lienard B.M., McDonough M.A., Clifton I.J., Butler D.,
Soares A.S., Oldham N.J., McNeill L.A., Schofield C.J.;
"Structural and mechanistic studies on the inhibition of the hypoxia-
inducible transcription factor hydroxylases by tricarboxylic acid
cycle intermediates.";
J. Biol. Chem. 282:3293-3301(2007).
[27]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEXES WITH 1930-1949 OR
1997-2016 OF MOUSE NOTCH1; IRON AND 2-OXOGLUTARATE, FUNCTION, SUBUNIT,
AND CATALYTIC ACTIVITY.
PubMed=17573339; DOI=10.1074/jbc.M704102200;
Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J.,
Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M.,
Oldham N.J., Ratcliffe P.J., Schofield C.J.;
"Asparaginyl hydroxylation of the Notch ankyrin repeat domain by
factor inhibiting hypoxia-inducible factor.";
J. Biol. Chem. 282:24027-24038(2007).
[28]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 11-349 OF MUTANTS ALA-201
AND GLY-201 IN COMPLEXES WITH 786-826 OR 788-806 OF HIF1A; IRON OR
ZINC AND 2-OXOGLUTARATE, AND MUTAGENESIS OF ASP-201; TRP-296 AND
LEU-340.
PubMed=18611856; DOI=10.1074/jbc.M804999200;
Hewitson K.S., Holmes S.L., Ehrismann D., Hardy A.P., Chowdhury R.,
Schofield C.J., McDonough M.A.;
"Evidence that two enzyme-derived histidine ligands are sufficient for
iron binding and catalysis by factor inhibiting HIF (FIH).";
J. Biol. Chem. 283:25971-25978(2008).
[29]
X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH IRON AND
2-OXOGLUTARATE ANALOGS.
PubMed=20822901; DOI=10.1016/j.bmcl.2010.08.032;
Conejo-Garcia A., McDonough M.A., Loenarz C., McNeill L.A.,
Hewitson K.S., Ge W., Lienard B.M., Schofield C.J., Clifton I.J.;
"Structural basis for binding of cyclic 2-oxoglutarate analogues to
factor-inhibiting hypoxia-inducible factor.";
Bioorg. Med. Chem. Lett. 20:6125-6128(2010).
[30]
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 15-349 IN COMPLEX WITH IRON
AND QUINOL FAMILY INHIBITORS.
PubMed=20396966; DOI=10.1007/s10059-010-0058-3;
Moon H., Han S., Park H., Choe J.;
"Crystal structures of human FIH-1 in complex with quinol family
inhibitors.";
Mol. Cells 29:471-474(2010).
[31]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON AND
INHIBITORS.
PubMed=21460794; DOI=10.1038/embor.2011.43;
Chowdhury R., Yeoh K.K., Tian Y.M., Hillringhaus L., Bagg E.A.,
Rose N.R., Leung I.K., Li X.S., Woon E.C., Yang M., McDonough M.A.,
King O.N., Clifton I.J., Klose R.J., Claridge T.D., Ratcliffe P.J.,
Schofield C.J., Kawamura A.;
"The oncometabolite 2-hydroxyglutarate inhibits histone lysine
demethylases.";
EMBO Rep. 12:463-469(2011).
[32]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH IRON;
2-OXOGLUTARATE AND 538-558 OF TNKS2, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=21251231; DOI=10.1111/j.1742-4658.2011.08022.x;
Yang M., Chowdhury R., Ge W., Hamed R.B., McDonough M.A.,
Claridge T.D., Kessler B.M., Cockman M.E., Ratcliffe P.J.,
Schofield C.J.;
"Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-
translational hydroxylation of histidinyl residues within ankyrin
repeat domains.";
FEBS J. 278:1086-1097(2011).
[33]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT HIS-239 IN COMPLEX
WITH ZINC; N-OXALYLGLYCINE AND PEPTIDE SUBSTRATE, FUNCTION,
INTERACTION WITH ANK1, MUTAGENESIS OF ASP-201 AND GLN-239, AND
CATALYTIC ACTIVITY.
PubMed=21177872; DOI=10.1074/jbc.M110.193540;
Yang M., Ge W., Chowdhury R., Claridge T.D., Kramer H.B.,
Schmierer B., McDonough M.A., Gong L., Kessler B.M., Ratcliffe P.J.,
Coleman M.L., Schofield C.J.;
"Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin
family is catalyzed by factor-inhibiting hypoxia-inducible factor.";
J. Biol. Chem. 286:7648-7660(2011).
-!- 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}.
-!- CATALYTIC ACTIVITY: Hypoxia-inducible factor-L-asparagine + 2-
oxoglutarate + O(2) = hypoxia-inducible factor-(3S)-3-hydroxy-L-
asparagine + succinate + CO(2). {ECO:0000269|PubMed:12042299,
ECO:0000269|PubMed:12080085, ECO:0000269|PubMed:14701857,
ECO:0000269|PubMed:17573339}.
-!- CATALYTIC ACTIVITY: [Ankyrin-repeat domain protein]-L-histidine +
2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-
hydroxy-L-histidine + succinate + CO(2).
{ECO:0000269|PubMed:21251231}.
-!- CATALYTIC ACTIVITY: [Ankyrin-repeat domain protein]-L-asparagine +
2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-
hydroxy-L-asparagine + succinate + CO(2).
{ECO:0000269|PubMed:17003112, ECO:0000269|PubMed:17573339,
ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:19245366,
ECO:0000269|PubMed:21177872}.
-!- CATALYTIC ACTIVITY: [Ankyrin-repeat domain protein]-L-aspartate +
2-oxoglutarate + O(2) = [ankyrin-repeat domain protein]-(3S)-3-
hydroxy-L-aspartate + succinate + CO(2).
{ECO:0000269|PubMed:21177872}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:15913349,
ECO:0000269|PubMed:17135241, ECO:0000269|PubMed:20396966,
ECO:0000269|PubMed:20822901, ECO:0000269|PubMed:21251231,
ECO:0000269|PubMed:21460794};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=100 uM for HIF1A (788-822) peptide
{ECO:0000269|PubMed:14701857};
KM=160 uM for HIF2A (832-866) peptide
{ECO:0000269|PubMed:14701857};
KM=0.5 uM for Fe(2+) {ECO:0000269|PubMed:14701857};
KM=25 uM for 2-oxoglutarate {ECO:0000269|PubMed:14701857};
KM=260 uM for ascorbate {ECO:0000269|PubMed:14701857};
KM=90 uM for O(2) {ECO:0000269|PubMed:14701857};
Note=The kinetic constants are determined for the recombinant
FLAG-His-tagged protein.;
-!- SUBUNIT: Homodimer; homodimerization is essential for catalytic
activity. Interacts with VHL and HIF1A. Part of a complex with
VHL, HIF1A and HDAC1 or HDAC2 or HDAC3. Interacts with NFKB1 and
NFKBIA. Interacts with NOTCH1, NOTCH2 and NOTCH3 but not with
NOTCH4. Interacts with APBA3; binding inhibits HIF1AN binding to
HIF1A. Interacts with TNKS2. Interacts with PPP1R12A. Interacts
with ASB4 (By similarity). Interacts with UBE3A. Interacts with
ANKS3 (By similarity). Interacts with NECAB3; the interaction is
indirect and seems to be mediated by APBA3.
{ECO:0000250|UniProtKB:Q8BLR9, ECO:0000269|PubMed:11641274,
ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:12482756, ECO:0000269|PubMed:14701857,
ECO:0000269|PubMed:15913349, ECO:0000269|PubMed:17003112,
ECO:0000269|PubMed:17135241, ECO:0000269|PubMed:17573339,
ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:19726677,
ECO:0000269|PubMed:20396966, ECO:0000269|PubMed:20822901,
ECO:0000269|PubMed:21177872, ECO:0000269|PubMed:21251231,
ECO:0000269|PubMed:21460794, ECO:0000269|PubMed:22645313,
ECO:0000269|PubMed:26948053}.
-!- INTERACTION:
O96018:APBA3; NbExp=3; IntAct=EBI-745632, EBI-6115839;
Q96DX5:ASB9; NbExp=3; IntAct=EBI-745632, EBI-745641;
Q9UK73:FEM1B; NbExp=3; IntAct=EBI-745632, EBI-310482;
Q16665:HIF1A; NbExp=12; IntAct=EBI-745632, EBI-447269;
Q13418:ILK; NbExp=2; IntAct=EBI-745632, EBI-747644;
P19838:NFKB1; NbExp=7; IntAct=EBI-745632, EBI-300010;
P25963:NFKBIA; NbExp=5; IntAct=EBI-745632, EBI-307386;
Q96FW1:OTUB1; NbExp=4; IntAct=EBI-745632, EBI-1058491;
O75832:PSMD10; NbExp=2; IntAct=EBI-745632, EBI-752185;
P57078:RIPK4; NbExp=4; IntAct=EBI-745632, EBI-4422308;
O95271:TNKS; NbExp=4; IntAct=EBI-745632, EBI-1105254;
Q9H2K2:TNKS2; NbExp=4; IntAct=EBI-745632, EBI-4398527;
Q9BZF9:UACA; NbExp=2; IntAct=EBI-745632, EBI-350510;
-!- 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.
-!- MASS SPECTROMETRY: Mass=40566; Method=Electrospray; Range=1-349;
Evidence={ECO:0000269|PubMed:15239670};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF395830; AAL27308.1; -; mRNA.
EMBL; AK000622; BAA91291.1; -; mRNA.
EMBL; AL133352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49817.1; -; Genomic_DNA.
EMBL; CH471066; EAW49818.1; -; Genomic_DNA.
EMBL; BC007719; AAH07719.1; -; mRNA.
EMBL; AL359615; CAB94885.1; -; mRNA.
CCDS; CCDS7498.1; -.
PIR; T50633; T50633.
RefSeq; NP_060372.2; NM_017902.2.
UniGene; Hs.500788; -.
PDB; 1H2K; X-ray; 2.15 A; A=1-349.
PDB; 1H2L; X-ray; 2.25 A; A=1-349.
PDB; 1H2M; X-ray; 2.50 A; A=1-349.
PDB; 1H2N; X-ray; 2.84 A; A=1-349.
PDB; 1IZ3; X-ray; 2.80 A; A=1-349.
PDB; 1MZE; X-ray; 2.20 A; A=1-349.
PDB; 1MZF; X-ray; 2.40 A; A=1-349.
PDB; 1YCI; X-ray; 2.70 A; A=1-349.
PDB; 2CGN; X-ray; 2.40 A; A=1-349.
PDB; 2CGO; X-ray; 2.30 A; A=1-349.
PDB; 2ILM; X-ray; 2.30 A; A=1-349.
PDB; 2W0X; X-ray; 2.12 A; A=1-349.
PDB; 2WA3; X-ray; 2.50 A; A=1-349.
PDB; 2WA4; X-ray; 2.50 A; A=1-349.
PDB; 2XUM; X-ray; 2.20 A; A=1-349.
PDB; 2Y0I; X-ray; 2.28 A; A=1-349.
PDB; 2YC0; X-ray; 2.15 A; A=1-349.
PDB; 2YDE; X-ray; 2.28 A; A=1-349.
PDB; 3D8C; X-ray; 2.10 A; A=11-349.
PDB; 3KCX; X-ray; 2.60 A; A=15-349.
PDB; 3KCY; X-ray; 2.59 A; A=15-349.
PDB; 3OD4; X-ray; 2.20 A; A=1-349.
PDB; 3P3N; X-ray; 2.40 A; A=1-349.
PDB; 3P3P; X-ray; 2.60 A; A=1-349.
PDB; 4AI8; X-ray; 2.40 A; A=1-349.
PDB; 4B7E; X-ray; 2.50 A; A=1-349.
PDB; 4B7K; X-ray; 2.39 A; A=1-349.
PDB; 4BIO; X-ray; 2.45 A; A=1-349.
PDB; 4JAA; X-ray; 2.39 A; A=1-349.
PDB; 4NR1; X-ray; 2.68 A; A=1-349.
PDB; 4Z1V; X-ray; 2.10 A; A=1-349.
PDB; 4Z2W; X-ray; 2.50 A; A=1-349.
PDB; 5JWK; X-ray; 2.30 A; A=1-349.
PDB; 5JWL; X-ray; 2.40 A; A=1-349.
PDB; 5JWP; X-ray; 2.10 A; A=1-349.
PDB; 5OP6; X-ray; 2.45 A; A=1-349.
PDB; 5OP8; X-ray; 2.30 A; A=1-349.
PDB; 5OPC; X-ray; 2.30 A; A=1-349.
PDBsum; 1H2K; -.
PDBsum; 1H2L; -.
PDBsum; 1H2M; -.
PDBsum; 1H2N; -.
PDBsum; 1IZ3; -.
PDBsum; 1MZE; -.
PDBsum; 1MZF; -.
PDBsum; 1YCI; -.
PDBsum; 2CGN; -.
PDBsum; 2CGO; -.
PDBsum; 2ILM; -.
PDBsum; 2W0X; -.
PDBsum; 2WA3; -.
PDBsum; 2WA4; -.
PDBsum; 2XUM; -.
PDBsum; 2Y0I; -.
PDBsum; 2YC0; -.
PDBsum; 2YDE; -.
PDBsum; 3D8C; -.
PDBsum; 3KCX; -.
PDBsum; 3KCY; -.
PDBsum; 3OD4; -.
PDBsum; 3P3N; -.
PDBsum; 3P3P; -.
PDBsum; 4AI8; -.
PDBsum; 4B7E; -.
PDBsum; 4B7K; -.
PDBsum; 4BIO; -.
PDBsum; 4JAA; -.
PDBsum; 4NR1; -.
PDBsum; 4Z1V; -.
PDBsum; 4Z2W; -.
PDBsum; 5JWK; -.
PDBsum; 5JWL; -.
PDBsum; 5JWP; -.
PDBsum; 5OP6; -.
PDBsum; 5OP8; -.
PDBsum; 5OPC; -.
ProteinModelPortal; Q9NWT6; -.
SMR; Q9NWT6; -.
BioGrid; 120794; 79.
DIP; DIP-35527N; -.
IntAct; Q9NWT6; 144.
MINT; MINT-1465958; -.
STRING; 9606.ENSP00000299163; -.
BindingDB; Q9NWT6; -.
ChEMBL; CHEMBL5909; -.
DrugBank; DB01694; D-tartaric acid.
DrugBank; DB08263; N-(carboxycarbonyl)-D-phenylalanine.
DrugBank; DB09459; Tartaric acid.
iPTMnet; Q9NWT6; -.
PhosphoSitePlus; Q9NWT6; -.
BioMuta; HIF1AN; -.
DMDM; 32129605; -.
EPD; Q9NWT6; -.
MaxQB; Q9NWT6; -.
PaxDb; Q9NWT6; -.
PeptideAtlas; Q9NWT6; -.
PRIDE; Q9NWT6; -.
DNASU; 55662; -.
Ensembl; ENST00000299163; ENSP00000299163; ENSG00000166135.
GeneID; 55662; -.
KEGG; hsa:55662; -.
UCSC; uc001krj.5; human.
CTD; 55662; -.
DisGeNET; 55662; -.
EuPathDB; HostDB:ENSG00000166135.13; -.
GeneCards; HIF1AN; -.
HGNC; HGNC:17113; HIF1AN.
HPA; CAB069903; -.
HPA; HPA048742; -.
HPA; HPA065302; -.
MIM; 606615; gene.
neXtProt; NX_Q9NWT6; -.
OpenTargets; ENSG00000166135; -.
PharmGKB; PA29284; -.
eggNOG; KOG2132; Eukaryota.
eggNOG; ENOG410XQDR; LUCA.
GeneTree; ENSGT00530000062914; -.
HOGENOM; HOG000008146; -.
HOVERGEN; HBG051903; -.
InParanoid; Q9NWT6; -.
KO; K18055; -.
OMA; MIKGRYD; -.
OrthoDB; EOG091G0C8E; -.
PhylomeDB; Q9NWT6; -.
TreeFam; TF329609; -.
BioCyc; MetaCyc:HS15407-MONOMER; -.
BRENDA; 1.14.11.16; 2681.
Reactome; R-HSA-1234162; Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.
SIGNOR; Q9NWT6; -.
ChiTaRS; HIF1AN; human.
EvolutionaryTrace; Q9NWT6; -.
GeneWiki; HIF1AN; -.
GenomeRNAi; 55662; -.
PRO; PR:Q9NWT6; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000166135; -.
CleanEx; HS_HIF1AN; -.
ExpressionAtlas; Q9NWT6; baseline and differential.
Genevisible; Q9NWT6; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0071532; F:ankyrin repeat binding; IPI:UniProtKB.
GO; GO:0031406; F:carboxylic acid binding; IDA:UniProtKB.
GO; GO:0048037; F:cofactor binding; IDA:UniProtKB.
GO; GO:0102113; F:hypoxia-inducible factor-asparagine oxygenase activity; IEA:UniProtKB-EC.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; EXP:Reactome.
GO; GO:0019826; F:oxygen sensor activity; NAS:UniProtKB.
GO; GO:0036140; F:peptidyl-asparagine 3-dioxygenase activity; IDA:UniProtKB.
GO; GO:0036139; F:peptidyl-histidine dioxygenase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:UniProtKB.
GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0042265; P:peptidyl-asparagine hydroxylation; IDA:UniProtKB.
GO; GO:0042264; P:peptidyl-aspartic acid hydroxylation; IDA:UniProtKB.
GO; GO:0036138; P:peptidyl-histidine hydroxylation; IDA:UniProtKB.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:UniProtKB.
GO; GO:2001214; P:positive regulation of vasculogenesis; NAS:UniProtKB.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.287.1010; -; 1.
InterPro; IPR027445; FIH-1.
InterPro; IPR027452; FIH-1_domII.
InterPro; IPR003347; JmjC_dom.
PANTHER; PTHR12461:SF51; PTHR12461:SF51; 1.
SMART; SM00558; JmjC; 1.
PROSITE; PS51184; JMJC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; Dioxygenase;
Iron; Metal-binding; Nucleus; Oxidoreductase; Polymorphism;
Reference proteome; Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 349 Hypoxia-inducible factor 1-alpha
inhibitor.
/FTId=PRO_0000083974.
DOMAIN 142 312 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
REGION 2 125 Interaction with VHL.
{ECO:0000269|PubMed:11641274}.
REGION 181 183 Substrate binding.
{ECO:0000269|PubMed:21177872}.
REGION 201 203 Substrate binding.
{ECO:0000269|PubMed:21177872}.
REGION 238 239 Substrate binding.
{ECO:0000269|PubMed:21177872}.
METAL 199 199 Iron; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:15913349,
ECO:0000269|PubMed:17135241,
ECO:0000269|PubMed:20396966,
ECO:0000269|PubMed:20822901,
ECO:0000269|PubMed:21251231,
ECO:0000269|PubMed:21460794}.
METAL 201 201 Iron; catalytic.
{ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:15913349,
ECO:0000269|PubMed:17135241,
ECO:0000269|PubMed:20396966,
ECO:0000269|PubMed:20822901,
ECO:0000269|PubMed:21251231,
ECO:0000269|PubMed:21460794}.
METAL 279 279 Iron; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:15913349,
ECO:0000269|PubMed:17135241,
ECO:0000269|PubMed:20396966,
ECO:0000269|PubMed:20822901,
ECO:0000269|PubMed:21251231,
ECO:0000269|PubMed:21460794}.
BINDING 145 145 2-oxoglutarate.
{ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:21251231}.
BINDING 152 152 Substrate. {ECO:0000269|PubMed:21177872}.
BINDING 196 196 2-oxoglutarate.
{ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:21251231}.
BINDING 205 205 2-oxoglutarate.
{ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:21251231}.
BINDING 214 214 2-oxoglutarate.
{ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:21251231}.
BINDING 294 294 2-oxoglutarate.
{ECO:0000269|PubMed:12432100,
ECO:0000269|PubMed:12446723,
ECO:0000269|PubMed:21251231}.
BINDING 300 300 Substrate; via amide nitrogen.
{ECO:0000269|PubMed:21177872}.
BINDING 321 321 Substrate. {ECO:0000269|PubMed:21177872}.
SITE 340 340 Important for dimer formation.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
VARIANT 41 41 P -> A (in dbSNP:rs2295778).
{ECO:0000269|Ref.4}.
/FTId=VAR_051028.
MUTAGEN 199 199 H->A: Prevents suppression of HIF CAD
activity. Strongly stimulates 2-
oxoglutarate turnover. No stimulation of
2-oxoglutarate turnover; when associated
with R-340.
{ECO:0000269|PubMed:12080085}.
MUTAGEN 201 201 D->A: Prevents suppression of HIF CAD
activity. {ECO:0000269|PubMed:12080085,
ECO:0000269|PubMed:18611856,
ECO:0000269|PubMed:21177872}.
MUTAGEN 201 201 D->E: Loss of HIF1A Asn hydroxylation
activity. Slightly stimulates 2-
oxoglutarate turnover.
{ECO:0000269|PubMed:12080085,
ECO:0000269|PubMed:18611856,
ECO:0000269|PubMed:21177872}.
MUTAGEN 201 201 D->G: No impact on HIF1A Asn
hydroxylation activity. Loss of Asp
hydroxylation ability. Strongly
stimulates 2-oxoglutarate turnover. Loss
of HIF1A Asn hydroxylation activity and
slight stimulation of 2-oxoglutarate
turnover; when associated with R-296.
{ECO:0000269|PubMed:12080085,
ECO:0000269|PubMed:18611856,
ECO:0000269|PubMed:21177872}.
MUTAGEN 239 239 Q->H: No effect on Asp hydroxylation
ability. {ECO:0000269|PubMed:21177872}.
MUTAGEN 296 296 W->R: Loss of HIF1A Asn hydroxylation
activity and slight stimulation of 2-
oxoglutarate turnover; when associated
with G-201.
{ECO:0000269|PubMed:18611856}.
MUTAGEN 340 340 L->R: Impairs dimer formation, leading to
loss of HIF1A Asn hydroxylation activity.
No stimulation of 2-oxoglutarate
turnover; when associated with A-201.
{ECO:0000269|PubMed:15239670,
ECO:0000269|PubMed:18611856}.
MUTAGEN 344 344 I->R: No effect on dimer formation and
HIF1A Asn hydroxylation activity.
{ECO:0000269|PubMed:15239670}.
CONFLICT 10 10 A -> T (in Ref. 2; BAA91291).
{ECO:0000305}.
CONFLICT 28 28 D -> H (in Ref. 2; BAA91291).
{ECO:0000305}.
CONFLICT 156 156 R -> G (in Ref. 2; BAA91291).
{ECO:0000305}.
HELIX 2 9 {ECO:0000244|PDB:2YC0}.
TURN 20 22 {ECO:0000244|PDB:3D8C}.
STRAND 24 26 {ECO:0000244|PDB:3OD4}.
HELIX 29 31 {ECO:0000244|PDB:3D8C}.
STRAND 39 41 {ECO:0000244|PDB:3D8C}.
HELIX 50 57 {ECO:0000244|PDB:3D8C}.
STRAND 62 65 {ECO:0000244|PDB:3D8C}.
HELIX 71 75 {ECO:0000244|PDB:3D8C}.
HELIX 78 84 {ECO:0000244|PDB:3D8C}.
STRAND 85 88 {ECO:0000244|PDB:3P3P}.
STRAND 90 99 {ECO:0000244|PDB:3D8C}.
HELIX 105 107 {ECO:0000244|PDB:3D8C}.
TURN 108 110 {ECO:0000244|PDB:2YC0}.
STRAND 111 113 {ECO:0000244|PDB:3KCY}.
STRAND 117 123 {ECO:0000244|PDB:3D8C}.
HELIX 125 138 {ECO:0000244|PDB:3D8C}.
STRAND 143 149 {ECO:0000244|PDB:3D8C}.
STRAND 151 154 {ECO:0000244|PDB:1MZE}.
HELIX 156 163 {ECO:0000244|PDB:3D8C}.
HELIX 167 176 {ECO:0000244|PDB:3D8C}.
STRAND 182 184 {ECO:0000244|PDB:3D8C}.
STRAND 186 190 {ECO:0000244|PDB:3D8C}.
STRAND 195 199 {ECO:0000244|PDB:3D8C}.
STRAND 202 212 {ECO:0000244|PDB:3D8C}.
STRAND 214 219 {ECO:0000244|PDB:3D8C}.
HELIX 221 223 {ECO:0000244|PDB:3D8C}.
HELIX 224 227 {ECO:0000244|PDB:3D8C}.
TURN 235 238 {ECO:0000244|PDB:4Z1V}.
STRAND 239 242 {ECO:0000244|PDB:4Z1V}.
STRAND 244 246 {ECO:0000244|PDB:4Z1V}.
TURN 249 251 {ECO:0000244|PDB:3D8C}.
HELIX 253 257 {ECO:0000244|PDB:3D8C}.
STRAND 260 265 {ECO:0000244|PDB:3D8C}.
STRAND 270 273 {ECO:0000244|PDB:3D8C}.
STRAND 278 283 {ECO:0000244|PDB:3D8C}.
STRAND 290 298 {ECO:0000244|PDB:3D8C}.
HELIX 312 329 {ECO:0000244|PDB:3D8C}.
STRAND 330 332 {ECO:0000244|PDB:2WA3}.
HELIX 333 335 {ECO:0000244|PDB:3D8C}.
HELIX 336 344 {ECO:0000244|PDB:3D8C}.
TURN 345 347 {ECO:0000244|PDB:3D8C}.
SEQUENCE 349 AA; 40285 MW; 96A033BA7B3BD8C7 CRC64;
MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE
PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMAN FQNFKPRSNR
EEMKFHEFVE KLQDIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG
QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS
QVDFDNPDYE RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA
PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN


Related products :

Catalog number Product name Quantity
18-003-43264 Hypoxia-inducible factor 1 alpha inhibitor - EC 1.14.11.16; Hypoxia-inducible factor asparagine hydroxylase; Factor inhibiting HIF-1; FIH-1 Polyclonal 0.05 mg Aff Pur
RPR-662 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor 10
EH921 Hypoxia-inducible factor 1-alpha inhibitor Elisa Kit 96T
pro-662 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor 1mg
pro-662 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor 50
pro-662 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor 10
OETPRO662 Hypoxia-Inducible Factor-1 Alpha Inhibitor Human Recombinant 10
pro-662 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor HIF1AN 10
228-10708-1 Recombinant Human Hypoxia-Inducible Factor-1 alpha Inhibitor 10
18-003-43831 Hypoxia-inducible factor 1. alpha subunit inhibitor - N_A Polyclonal 0.1 mg Protein A
18-003-42306 Hypoxia-inducible factor 1. alpha subunit inhibitor - N_A Polyclonal 0.05 mg Aff Pur
pro-662 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor HIF1AN 50
7-05340 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor 1mg
7-05338 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor 10
228-10708-3 Recombinant Human Hypoxia-Inducible Factor-1 alpha Inhibitor 1 mg
pro-662 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor HIF1AN 1mg
OETPRO662 Hypoxia-Inducible Factor-1 Alpha Inhibitor Human Recombinant 50
7-05339 Recombinant Human Hypoxia-Inducible Factor-1 Alpha Inhibitor 50
228-10708-2 Recombinant Human Hypoxia-Inducible Factor-1 alpha Inhibitor 50
U2004m CLIA kit Endothelial PAS domain-containing protein 1,Epas1,EPAS-1,HIF-1-alpha-like factor,Hif2a,HIF-2-alpha,HIF2-alpha,HIF-related factor,HLF,HRF,Hypoxia-inducible factor 2-alpha,mHLF,Mouse,Mus muscu 96T
U2004m CLIA Endothelial PAS domain-containing protein 1,Epas1,EPAS-1,HIF-1-alpha-like factor,Hif2a,HIF-2-alpha,HIF2-alpha,HIF-related factor,HLF,HRF,Hypoxia-inducible factor 2-alpha,mHLF,Mouse,Mus musculus 96T
E2004m ELISA Endothelial PAS domain-containing protein 1,Epas1,EPAS-1,HIF-1-alpha-like factor,Hif2a,HIF-2-alpha,HIF2-alpha,HIF-related factor,HLF,HRF,Hypoxia-inducible factor 2-alpha,mHLF,Mouse,Mus musculus 96T
E2004m ELISA kit Endothelial PAS domain-containing protein 1,Epas1,EPAS-1,HIF-1-alpha-like factor,Hif2a,HIF-2-alpha,HIF2-alpha,HIF-related factor,HLF,HRF,Hypoxia-inducible factor 2-alpha,mHLF,Mouse,Mus musc 96T
YHB1601Hu Human Hypoxia-inducible factor 1-alpha inhibitor,HIF1AN ELISA Kit 96T
HIGD1A HIF1AN Gene hypoxia inducible factor 1, alpha subunit inhibitor


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur