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Q9NWT6

- HIF1N_HUMAN

UniProt

Q9NWT6 - HIF1N_HUMAN

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Protein
Hypoxia-inducible factor 1-alpha inhibitor
Gene
HIF1AN, FIH1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydroxylates HIF-1 alpha at 'Asp-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.8 Publications

Catalytic activityi

Hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 = hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2.3 Publications
Ankyrin-repeat-L-histidine + 2-oxoglutarate + O2 = ankyrin-repeat-(3S)-3-hydroxy-L-histidine + succinate + CO2.3 Publications

Cofactori

Fe2+ ion.

Kineticsi

The kinetic constants are determined for the recombinant FLAG-His-tagged protein.

  1. KM=100 µM for HIF1A (788-822) peptide1 Publication
  2. KM=160 µM for HIF2A (832-866) peptide
  3. KM=0.5 µM for Fe2+
  4. KM=25 µM for 2-oxoglutarate
  5. KM=260 µM for ascorbate
  6. KM=90 µM for O2

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei145 – 14512-oxoglutarate
Binding sitei152 – 1521Substrate
Binding sitei196 – 19612-oxoglutarate
Metal bindingi199 – 1991Iron; via tele nitrogen; catalytic
Metal bindingi201 – 2011Iron; via tele nitrogen; catalytic
Binding sitei205 – 20512-oxoglutarate
Binding sitei214 – 21412-oxoglutarate
Metal bindingi279 – 2791Iron; via tele nitrogen; catalytic
Binding sitei294 – 29412-oxoglutarate
Binding sitei300 – 3001Substrate; via amide nitrogen
Binding sitei321 – 3211Substrate
Sitei340 – 3401Important for dimer formation

GO - Molecular functioni

  1. NF-kappaB binding Source: UniProtKB
  2. Notch binding Source: UniProtKB
  3. ankyrin repeat binding Source: UniProtKB
  4. carboxylic acid binding Source: UniProtKB
  5. cofactor binding Source: UniProtKB
  6. iron ion binding Source: UniProtKB
  7. 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 Source: Reactome
  8. oxygen sensor activity Source: UniProtKB
  9. peptidyl-asparagine 3-dioxygenase activity Source: UniProtKB
  10. peptidyl-histidine dioxygenase activity Source: UniProtKB
  11. protein binding Source: UniProtKB
  12. protein homodimerization activity Source: UniProtKB
  13. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to hypoxia Source: Reactome
  2. negative regulation of Notch signaling pathway Source: UniProtKB
  3. negative regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
  4. oxidation-reduction process Source: UniProtKB
  5. peptidyl-asparagine hydroxylation Source: UniProtKB
  6. peptidyl-aspartic acid hydroxylation Source: UniProtKB
  7. peptidyl-histidine hydroxylation Source: UniProtKB
  8. positive regulation of myoblast differentiation Source: UniProtKB
  9. positive regulation of vasculogenesis Source: UniProtKB
  10. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS15407-MONOMER.
ReactomeiREACT_121226. Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxia-inducible factor 1-alpha inhibitor (EC:1.14.11.30, EC:1.14.11.n4)
Alternative name(s):
Factor inhibiting HIF-1
Short name:
FIH-1
Hypoxia-inducible factor asparagine hydroxylase
Gene namesi
Name:HIF1AN
Synonyms:FIH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:17113. HIF1AN.

Subcellular locationi

Nucleus. Cytoplasm. Cytoplasmperinuclear region
Note: Mainly cytoplasmic localization, but interaction with NOTCH1 results in nuclear localization and interaction with ABPA3 results in perinuclear localization in macrophages.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: HPA
  4. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991H → A: Prevents suppression of HIF CAD activity. Strongly stimulates 2-oxoglutarate turnover. No stimulation of 2-oxoglutarate turnover; when associated with R-340. 1 Publication
Mutagenesisi201 – 2011D → A: Prevents suppression of HIF CAD activity. 3 Publications
Mutagenesisi201 – 2011D → E: Loss of HIF1A Asn hydroxylation activity. Slightly stimulates 2-oxoglutarate turnover. 3 Publications
Mutagenesisi201 – 2011D → 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. 3 Publications
Mutagenesisi239 – 2391Q → H: No effect on Asp hydroxylation ability. 1 Publication
Mutagenesisi296 – 2961W → R: Loss of HIF1A Asn hydroxylation activity and slight stimulation of 2-oxoglutarate turnover; when associated with G-201. 1 Publication
Mutagenesisi340 – 3401L → R: Impairs dimer formation, leading to loss of HIF1A Asn hydroxylation activity. No stimulation of 2-oxoglutarate turnover; when associated with A-201. 2 Publications
Mutagenesisi344 – 3441I → R: No effect on dimer formation and HIF1A Asn hydroxylation activity. 1 Publication

Organism-specific databases

PharmGKBiPA29284.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 349348Hypoxia-inducible factor 1-alpha inhibitor
PRO_0000083974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NWT6.
PaxDbiQ9NWT6.
PRIDEiQ9NWT6.

PTM databases

PhosphoSiteiQ9NWT6.

Expressioni

Gene expression databases

ArrayExpressiQ9NWT6.
BgeeiQ9NWT6.
CleanExiHS_HIF1AN.
GenevestigatoriQ9NWT6.

Organism-specific databases

HPAiHPA048742.

Interactioni

Subunit structurei

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.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASB9Q96DX53EBI-745632,EBI-745641
HIF1AQ166654EBI-745632,EBI-447269
TNKSO952712EBI-745632,EBI-1105254
TNKS2Q9H2K23EBI-745632,EBI-4398527

Protein-protein interaction databases

BioGridi120794. 25 interactions.
IntActiQ9NWT6. 9 interactions.
MINTiMINT-1465958.
STRINGi9606.ENSP00000299163.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 98
Turni20 – 223
Beta strandi24 – 263
Helixi29 – 313
Beta strandi39 – 413
Helixi50 – 578
Beta strandi62 – 654
Helixi71 – 755
Helixi78 – 847
Beta strandi85 – 884
Beta strandi90 – 9910
Helixi105 – 1073
Turni108 – 1103
Beta strandi111 – 1133
Beta strandi117 – 1237
Helixi125 – 13814
Beta strandi143 – 1497
Beta strandi151 – 1544
Helixi156 – 1638
Helixi167 – 17610
Beta strandi182 – 1843
Beta strandi186 – 1905
Beta strandi195 – 1995
Beta strandi202 – 21211
Beta strandi214 – 2196
Helixi221 – 2233
Helixi224 – 2274
Turni235 – 2384
Beta strandi239 – 2424
Beta strandi244 – 2463
Turni249 – 2513
Helixi253 – 2575
Beta strandi260 – 2656
Beta strandi270 – 2734
Beta strandi278 – 2836
Beta strandi290 – 2989
Helixi312 – 32918
Beta strandi330 – 3323
Helixi333 – 3353
Helixi336 – 3449
Turni345 – 3473

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2KX-ray2.15A1-349[»]
1H2LX-ray2.25A1-349[»]
1H2MX-ray2.50A1-349[»]
1H2NX-ray2.84A1-349[»]
1IZ3X-ray2.80A1-349[»]
1MZEX-ray2.20A1-349[»]
1MZFX-ray2.40A1-349[»]
1YCIX-ray2.70A1-349[»]
2CGNX-ray2.40A1-349[»]
2CGOX-ray2.30A1-349[»]
2ILMX-ray2.30A1-349[»]
2W0XX-ray2.12A1-349[»]
2WA3X-ray2.50A1-349[»]
2WA4X-ray2.50A1-349[»]
2XUMX-ray2.20A1-349[»]
2Y0IX-ray2.28A1-349[»]
2YC0X-ray2.15A1-349[»]
2YDEX-ray2.28A1-349[»]
3D8CX-ray2.10A11-349[»]
3KCXX-ray2.60A15-349[»]
3KCYX-ray2.59A15-349[»]
3OD4X-ray2.20A1-349[»]
3P3NX-ray2.40A1-349[»]
3P3PX-ray2.60A1-349[»]
4AI8X-ray2.40A1-349[»]
4B7EX-ray2.50A1-349[»]
4B7KX-ray2.39A1-349[»]
4BIOX-ray2.45A1-349[»]
4JAAX-ray2.39A1-349[»]
ProteinModelPortaliQ9NWT6.
SMRiQ9NWT6. Positions 9-349.

Miscellaneous databases

EvolutionaryTraceiQ9NWT6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini142 – 312171JmjC
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 125124Interaction with VHL
Add
BLAST
Regioni181 – 1833Substrate binding
Regioni201 – 2033Substrate binding
Regioni238 – 2392Substrate binding

Sequence similaritiesi

Contains 1 JmjC domain.

Phylogenomic databases

eggNOGiNOG71927.
HOGENOMiHOG000008146.
HOVERGENiHBG051903.
InParanoidiQ9NWT6.
KOiK18055.
OMAiMIKGRYD.
PhylomeDBiQ9NWT6.
TreeFamiTF329609.

Family and domain databases

Gene3Di1.10.287.1010. 1 hit.
InterProiIPR027445. FIH-1.
IPR027452. FIH-1_domII.
IPR003347. JmjC_dom.
[Graphical view]
PANTHERiPTHR12461:SF19. PTHR12461:SF19. 1 hit.
SMARTiSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEiPS51184. JMJC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NWT6-1 [UniParc]FASTAAdd to Basket

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MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP    50
RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF 100
LYYDEKKMAN FQNFKPRSNR EEMKFHEFVE KLQDIQQRGG EERLYLQQTL 150
NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY 200
DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE 250
RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA 300
PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN 349
Length:349
Mass (Da):40,285
Last modified:June 16, 2003 - v2
Checksum:i96A033BA7B3BD8C7
GO

Mass spectrometryi

Molecular mass is 40566 Da from positions 1 - 349. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411P → A.1 Publication
Corresponds to variant rs2295778 [ dbSNP | Ensembl ].
VAR_051028

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101A → T in BAA91291. 1 Publication
Sequence conflicti28 – 281D → H in BAA91291. 1 Publication
Sequence conflicti156 – 1561R → G in BAA91291. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF395830 mRNA. Translation: AAL27308.1.
AK000622 mRNA. Translation: BAA91291.1.
AL133352 Genomic DNA. Translation: CAH73566.1.
CH471066 Genomic DNA. Translation: EAW49817.1.
CH471066 Genomic DNA. Translation: EAW49818.1.
BC007719 mRNA. Translation: AAH07719.1.
AL359615 mRNA. Translation: CAB94885.1.
CCDSiCCDS7498.1.
PIRiT50633.
RefSeqiNP_060372.2. NM_017902.2.
UniGeneiHs.500788.

Genome annotation databases

EnsembliENST00000299163; ENSP00000299163; ENSG00000166135.
GeneIDi55662.
KEGGihsa:55662.
UCSCiuc001krj.4. human.

Polymorphism databases

DMDMi32129605.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF395830 mRNA. Translation: AAL27308.1 .
AK000622 mRNA. Translation: BAA91291.1 .
AL133352 Genomic DNA. Translation: CAH73566.1 .
CH471066 Genomic DNA. Translation: EAW49817.1 .
CH471066 Genomic DNA. Translation: EAW49818.1 .
BC007719 mRNA. Translation: AAH07719.1 .
AL359615 mRNA. Translation: CAB94885.1 .
CCDSi CCDS7498.1.
PIRi T50633.
RefSeqi NP_060372.2. NM_017902.2.
UniGenei Hs.500788.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H2K X-ray 2.15 A 1-349 [» ]
1H2L X-ray 2.25 A 1-349 [» ]
1H2M X-ray 2.50 A 1-349 [» ]
1H2N X-ray 2.84 A 1-349 [» ]
1IZ3 X-ray 2.80 A 1-349 [» ]
1MZE X-ray 2.20 A 1-349 [» ]
1MZF X-ray 2.40 A 1-349 [» ]
1YCI X-ray 2.70 A 1-349 [» ]
2CGN X-ray 2.40 A 1-349 [» ]
2CGO X-ray 2.30 A 1-349 [» ]
2ILM X-ray 2.30 A 1-349 [» ]
2W0X X-ray 2.12 A 1-349 [» ]
2WA3 X-ray 2.50 A 1-349 [» ]
2WA4 X-ray 2.50 A 1-349 [» ]
2XUM X-ray 2.20 A 1-349 [» ]
2Y0I X-ray 2.28 A 1-349 [» ]
2YC0 X-ray 2.15 A 1-349 [» ]
2YDE X-ray 2.28 A 1-349 [» ]
3D8C X-ray 2.10 A 11-349 [» ]
3KCX X-ray 2.60 A 15-349 [» ]
3KCY X-ray 2.59 A 15-349 [» ]
3OD4 X-ray 2.20 A 1-349 [» ]
3P3N X-ray 2.40 A 1-349 [» ]
3P3P X-ray 2.60 A 1-349 [» ]
4AI8 X-ray 2.40 A 1-349 [» ]
4B7E X-ray 2.50 A 1-349 [» ]
4B7K X-ray 2.39 A 1-349 [» ]
4BIO X-ray 2.45 A 1-349 [» ]
4JAA X-ray 2.39 A 1-349 [» ]
ProteinModelPortali Q9NWT6.
SMRi Q9NWT6. Positions 9-349.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120794. 25 interactions.
IntActi Q9NWT6. 9 interactions.
MINTi MINT-1465958.
STRINGi 9606.ENSP00000299163.

Chemistry

BindingDBi Q9NWT6.
ChEMBLi CHEMBL5909.

PTM databases

PhosphoSitei Q9NWT6.

Polymorphism databases

DMDMi 32129605.

Proteomic databases

MaxQBi Q9NWT6.
PaxDbi Q9NWT6.
PRIDEi Q9NWT6.

Protocols and materials databases

DNASUi 55662.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299163 ; ENSP00000299163 ; ENSG00000166135 .
GeneIDi 55662.
KEGGi hsa:55662.
UCSCi uc001krj.4. human.

Organism-specific databases

CTDi 55662.
GeneCardsi GC10P102285.
HGNCi HGNC:17113. HIF1AN.
HPAi HPA048742.
MIMi 606615. gene.
neXtProti NX_Q9NWT6.
PharmGKBi PA29284.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71927.
HOGENOMi HOG000008146.
HOVERGENi HBG051903.
InParanoidi Q9NWT6.
KOi K18055.
OMAi MIKGRYD.
PhylomeDBi Q9NWT6.
TreeFami TF329609.

Enzyme and pathway databases

BioCyci MetaCyc:HS15407-MONOMER.
Reactomei REACT_121226. Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.

Miscellaneous databases

EvolutionaryTracei Q9NWT6.
GeneWikii HIF1AN.
GenomeRNAii 55662.
NextBioi 60403.
PROi Q9NWT6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NWT6.
Bgeei Q9NWT6.
CleanExi HS_HIF1AN.
Genevestigatori Q9NWT6.

Family and domain databases

Gene3Di 1.10.287.1010. 1 hit.
InterProi IPR027445. FIH-1.
IPR027452. FIH-1_domII.
IPR003347. JmjC_dom.
[Graphical view ]
PANTHERi PTHR12461:SF19. PTHR12461:SF19. 1 hit.
SMARTi SM00558. JmjC. 1 hit.
[Graphical view ]
PROSITEi PS51184. JMJC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity."
    Mahon P.C., Hirota K., Semenza G.L.
    Genes Dev. 15:2675-2686(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HIF1A; VHL AND HISTONE DEACETYLASES.
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Signet-ring cell carcinoma.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    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.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-41.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-349.
    Tissue: Melanoma.
  7. "FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor."
    Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L., Bruick R.K.
    Genes Dev. 16:1466-1471(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF HIS-199 AND ASP-201.
  8. "Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family."
    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.
    J. Biol. Chem. 277:26351-26355(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION.
  9. "Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity."
    Lancaster D.E., McNeill L.A., McDonough M.A., Aplin R.T., Hewitson K.S., Pugh C.W., Ratcliffe P.J., Schofield C.J.
    Biochem. J. 383:429-437(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DIMERIZATION, MASS SPECTROMETRY, MUTAGENESIS OF LEU-340 AND ILE-344.
  10. "Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases."
    Koivunen P., Hirsila M., Gunzler V., Kivirikko K.I., Myllyharju J.
    J. Biol. Chem. 279:9899-9904(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor."
    Linke S., Stojkoski C., Kewley R.J., Booker G.W., Whitelaw M.L., Peet D.J.
    J. Biol. Chem. 279:14391-14397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 103:14767-14772(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NFKB1 AND NFKBIA.
  13. "Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)."
    Webb J.D., Muranyi A., Pugh C.W., Ratcliffe P.J., Coleman M.L.
    Biochem. J. 420:327-333(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1R12A.
  16. "Mint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in macrophages by suppressing the activity of factor inhibiting HIF-1."
    Sakamoto T., Seiki M.
    J. Biol. Chem. 284:30350-30359(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APBA3, SUBCELLULAR LOCATION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes."
    Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M., Harper J.W., Howley P.M.
    Mol. Cell. Biol. 32:3095-3106(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE3A.
  19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Structure of factor-inhibiting hypoxia-inducible factor 1: an asparaginyl hydroxylase involved in the hypoxic response pathway."
    Dann C.E. III, Bruick R.K., Deisenhofer J.
    Proc. Natl. Acad. Sci. U.S.A. 99:15351-15356(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH IRON AND 2-OXOGLUTARATE, SUBUNIT.
  22. "Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha."
    Elkins J.M., Hewitson K.S., McNeill L.A., Seibel J.F., Schlemminger I., Pugh C.W., Ratcliffe P.J., Schofield C.J.
    J. Biol. Chem. 278:1802-1806(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH 786-826 OF HIF1A; IRON; ZINC AND 2-OXOGLUTARATE.
  23. "Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau."
    Lee C., Kim S.J., Jeong D.G., Lee S.M., Ryu S.E.
    J. Biol. Chem. 278:7558-7563(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT.
  24. Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH IRON AND INHIBITOR.
  25. "Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates."
    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.
    J. Biol. Chem. 282:3293-3301(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH IRON; SUCCINATE AND FUMARATE.
  26. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEXES WITH 1930-1949 OR 1997-2016 OF MOUSE NOTCH1; IRON AND 2-OXOGLUTARATE, FUNCTION, SUBUNIT.
  27. "Evidence that two enzyme-derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH)."
    Hewitson K.S., Holmes S.L., Ehrismann D., Hardy A.P., Chowdhury R., Schofield C.J., McDonough M.A.
    J. Biol. Chem. 283:25971-25978(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, MUTAGENESIS OF ASP-201; TRP-296 AND LEU-340.
  28. "Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor."
    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.
    Bioorg. Med. Chem. Lett. 20:6125-6128(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH IRON AND 2-OXOGLUTARATE ANALOGS.
  29. "Crystal structures of human FIH-1 in complex with quinol family inhibitors."
    Moon H., Han S., Park H., Choe J.
    Mol. Cells 29:471-474(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 15-349 IN COMPLEX WITH IRON AND QUINOL FAMILY INHIBITORS.
  30. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON AND INHIBITORS.
  31. "Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains."
    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.
    FEBS J. 278:1086-1097(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH IRON; 2-OXOGLUTARATE AND 538-558 OF TNKS2, FUNCTION.
  32. "Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor."
    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.
    J. Biol. Chem. 286:7648-7660(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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.

Entry informationi

Entry nameiHIF1N_HUMAN
AccessioniPrimary (citable) accession number: Q9NWT6
Secondary accession number(s): D3DR69
, Q5W147, Q969Q7, Q9NPV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: September 3, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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