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Q9H6Z9

- EGLN3_HUMAN

UniProt

Q9H6Z9 - EGLN3_HUMAN

Protein

Egl nine homolog 3

Gene

EGLN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    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 HIF2A. Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site. 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. EGLN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis. Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation. Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway. Target proteins are preferencially recognized via a LXXLAP motif.11 Publications

    Catalytic activityi

    Hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 = hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.
    Ascorbate.

    Enzyme regulationi

    Activated in cardiovascular cells and Hela cells following exposure to hypoxia. Inhibited by polynitrogen compounds probably by chelation to Fe2+ ions.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi135 – 1351IronPROSITE-ProRule annotation
    Metal bindingi137 – 1371IronPROSITE-ProRule annotation
    Metal bindingi196 – 1961IronPROSITE-ProRule annotation
    Binding sitei205 – 20512-oxoglutaratePROSITE-ProRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. L-ascorbic acid binding Source: UniProtKB-KW
    3. peptidyl-proline 4-dioxygenase activity Source: FlyBase
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. apoptotic process Source: UniProtKB
    3. cellular response to DNA damage stimulus Source: UniProtKB-KW
    4. cellular response to hypoxia Source: Reactome
    5. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: FlyBase
    6. protein hydroxylation Source: UniProtKB
    7. regulation of cell proliferation Source: UniProtKB
    8. regulation of neuron apoptotic process Source: UniProtKB
    9. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    10. response to hypoxia Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Apoptosis, DNA damage

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BRENDAi1.14.11.2. 2681.
    ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Egl nine homolog 3 (EC:1.14.11.29)
    Alternative name(s):
    HPH-1
    Hypoxia-inducible factor prolyl hydroxylase 3
    Short name:
    HIF-PH3
    Short name:
    HIF-prolyl hydroxylase 3
    Short name:
    HPH-3
    Prolyl hydroxylase domain-containing protein 3
    Short name:
    PHD3
    Gene namesi
    Name:EGLN3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:14661. EGLN3.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Colocalizes with WDR83 in the cytoplasm.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 10212ISFLL…IDRLV → RSFLRSLIRRLR: Abolishes interaction with ADRB2 and no increase in cellular abundance of ADRB2. 1 PublicationAdd
    BLAST
    Mutagenesisi135 – 1351H → A: Eliminates hydroxylase activity. 2 Publications
    Mutagenesisi137 – 1371D → A: Eliminates hydroxylase activity. 2 Publications
    Mutagenesisi196 – 1961H → A: Eliminates hydroxylase activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA27672.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 239239Egl nine homolog 3PRO_0000206666Add
    BLAST

    Proteomic databases

    MaxQBiQ9H6Z9.
    PaxDbiQ9H6Z9.
    PRIDEiQ9H6Z9.

    PTM databases

    PhosphoSiteiQ9H6Z9.

    Expressioni

    Tissue specificityi

    Widely expressed at low levels. Expressed at higher levels in adult heart (cardiac myocytes, aortic endothelial cells and coronary artery smooth muscle), lung and placenta, and in fetal spleen, heart and skeletal muscle. Also expressed in pancreas. Localized to pancreatic acini and islet cells.3 Publications

    Inductioni

    Induced by hypoxia in a number of cells including neutrophils and certain cancer cell lines. Up-regulated 10-fold in pancreatic cancers.4 Publications

    Gene expression databases

    ArrayExpressiQ9H6Z9.
    BgeeiQ9H6Z9.
    CleanExiHS_EGLN3.
    GenevestigatoriQ9H6Z9.

    Organism-specific databases

    HPAiCAB012351.

    Interactioni

    Subunit structurei

    Interacts with WDR83; the interaction leads to almost complete elimination of HIF-mediated reporter activity By similarity. Interacts with BCL2 (via its BH4 domain); the interaction disrupts the BAX-BCL4 complex inhibiting the anti-apoptotic activity of BCL2. Interacts with ADRB2; the interaction hydroxylates ADRB2 facilitating its ubiquitination by the VHL-E3 ligase complex. Interacts with PAX2; the interaction targets PAX2 for destruction. Interacts with PKM; the interaction hydroxylates PKM in hypoxia.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIF1AQ166653EBI-1175354,EBI-447269
    PKMP14618-12EBI-1175354,EBI-4304679

    Protein-protein interaction databases

    BioGridi125185. 26 interactions.
    IntActiQ9H6Z9. 8 interactions.
    MINTiMINT-1206284.
    STRINGi9606.ENSP00000250457.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H6Z9.
    SMRiQ9H6Z9. Positions 13-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini116 – 21499Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni62 – 7312Beta(2)beta(3) 'finger-like' loopBy similarityAdd
    BLAST
    Regioni88 – 10417Required for interaction with ADRB2Add
    BLAST

    Domaini

    The Beta2beta3 'finger-like' loop domain is important for substrate (HIFs' CODD/NODD) selectivity.

    Sequence similaritiesi

    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG326511.
    HOGENOMiHOG000004818.
    HOVERGENiHBG051455.
    InParanoidiQ9H6Z9.
    KOiK09592.
    OMAiWIGGTEE.
    OrthoDBiEOG7TBC2W.
    PhylomeDBiQ9H6Z9.
    TreeFamiTF314595.

    Family and domain databases

    InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    [Graphical view]
    PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
    [Graphical view]
    SMARTiSM00702. P4Hc. 1 hit.
    [Graphical view]
    PROSITEiPS51471. FE2OG_OXY. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9H6Z9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLGHIMRLD LEKIALEYIV PCLHEVGFCY LDNFLGEVVG DCVLERVKQL    50
    HCTGALRDGQ LAGPRAGVSK RHLRGDQITW IGGNEEGCEA ISFLLSLIDR 100
    LVLYCGSRLG KYYVKERSKA MVACYPGNGT GYVRHVDNPN GDGRCITCIY 150
    YLNKNWDAKL HGGILRIFPE GKSFIADVEP IFDRLLFFWS DRRNPHEVQP 200
    SYATRYAMTV WYFDAEERAE AKKKFRNLTR KTESALTED 239
    Length:239
    Mass (Da):27,261
    Last modified:March 1, 2001 - v1
    Checksum:i9DA3A0F80168557B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti136 – 1361V → L.
    Corresponds to variant rs17102002 [ dbSNP | Ensembl ].
    VAR_050449
    Natural varianti234 – 2341S → T.
    Corresponds to variant rs17101995 [ dbSNP | Ensembl ].
    VAR_050450

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ310545 mRNA. Translation: CAC42511.1.
    AK025273 mRNA. Translation: BAB15101.1.
    BC010992 mRNA. Translation: AAH10992.3.
    BC064924 mRNA. Translation: AAH64924.2.
    BC105939 mRNA. Translation: AAI05940.1.
    BC111057 mRNA. Translation: AAI11058.2.
    CCDSiCCDS9646.1.
    RefSeqiNP_071356.1. NM_022073.3.
    UniGeneiHs.135507.

    Genome annotation databases

    EnsembliENST00000250457; ENSP00000250457; ENSG00000129521.
    GeneIDi112399.
    KEGGihsa:112399.
    UCSCiuc001wsa.4. human.

    Polymorphism databases

    DMDMi32129515.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ310545 mRNA. Translation: CAC42511.1 .
    AK025273 mRNA. Translation: BAB15101.1 .
    BC010992 mRNA. Translation: AAH10992.3 .
    BC064924 mRNA. Translation: AAH64924.2 .
    BC105939 mRNA. Translation: AAI05940.1 .
    BC111057 mRNA. Translation: AAI11058.2 .
    CCDSi CCDS9646.1.
    RefSeqi NP_071356.1. NM_022073.3.
    UniGenei Hs.135507.

    3D structure databases

    ProteinModelPortali Q9H6Z9.
    SMRi Q9H6Z9. Positions 13-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125185. 26 interactions.
    IntActi Q9H6Z9. 8 interactions.
    MINTi MINT-1206284.
    STRINGi 9606.ENSP00000250457.

    Chemistry

    BindingDBi Q9H6Z9.
    ChEMBLi CHEMBL5705.
    DrugBanki DB00126. Vitamin C.

    PTM databases

    PhosphoSitei Q9H6Z9.

    Polymorphism databases

    DMDMi 32129515.

    Proteomic databases

    MaxQBi Q9H6Z9.
    PaxDbi Q9H6Z9.
    PRIDEi Q9H6Z9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250457 ; ENSP00000250457 ; ENSG00000129521 .
    GeneIDi 112399.
    KEGGi hsa:112399.
    UCSCi uc001wsa.4. human.

    Organism-specific databases

    CTDi 112399.
    GeneCardsi GC14M034393.
    HGNCi HGNC:14661. EGLN3.
    HPAi CAB012351.
    MIMi 606426. gene.
    neXtProti NX_Q9H6Z9.
    PharmGKBi PA27672.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326511.
    HOGENOMi HOG000004818.
    HOVERGENi HBG051455.
    InParanoidi Q9H6Z9.
    KOi K09592.
    OMAi WIGGTEE.
    OrthoDBi EOG7TBC2W.
    PhylomeDBi Q9H6Z9.
    TreeFami TF314595.

    Enzyme and pathway databases

    BRENDAi 1.14.11.2. 2681.
    Reactomei REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.

    Miscellaneous databases

    ChiTaRSi EGLN3. human.
    GeneWikii EGLN3.
    GenomeRNAii 112399.
    NextBioi 78578.
    PROi Q9H6Z9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H6Z9.
    Bgeei Q9H6Z9.
    CleanExi HS_EGLN3.
    Genevestigatori Q9H6Z9.

    Family and domain databases

    InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    [Graphical view ]
    Pfami PF13640. 2OG-FeII_Oxy_3. 1 hit.
    [Graphical view ]
    SMARTi SM00702. P4Hc. 1 hit.
    [Graphical view ]
    PROSITEi PS51471. FE2OG_OXY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and comparative analysis of the EGLN gene family."
      Taylor M.S.
      Gene 275:125-132(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor."
      Hirsila M., Koivunen P., Gunzler V., Kivirikko K.I., Myllyharju J.
      J. Biol. Chem. 278:30772-30780(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBSTRATE SPECIFICITY.
      Tissue: Aorta, Colon and Lung.
    3. "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: Colon.
    4. "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: Ovary and Retinoblastoma.
    5. Cited for: FUNCTION, ENZYME REGULATION.
    6. "HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus."
      Semenza G.L.
      Cell 107:1-3(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    7. "A conserved family of prolyl-4-hydroxylases that modify HIF."
      Bruick R.K., McKnight S.L.
      Science 294:1337-1340(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-135; ASP-137 AND HIS-196.
    8. "Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors."
      Oehme F., Ellinghaus P., Kolkhof P., Smith T.J., Ramakrishnan S., Huetter J., Schramm M., Flamme I.
      Biochem. Biophys. Res. Commun. 296:343-349(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "Sequence determinants in hypoxia-inducible factor-1alpha for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3."
      Huang J., Zhao Q., Mooney S.M., Lee F.S.
      J. Biol. Chem. 277:39792-39800(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE RECOGNITION MOTIF.
    10. "Differential regulation of HIF-1alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells."
      Cioffi C.L., Qin Liu X., Kosinski P.A., Garay M., Bowen B.R.
      Biochem. Biophys. Res. Commun. 303:947-953(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, ENZYME REGULATION.
    11. Cited for: SUBCELLULAR LOCATION, INDUCTION.
    12. "Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor."
      Appelhoff R.J., Tian Y.M., Raval R.R., Turley H., Harris A.L., Pugh C.W., Ratcliffe P.J., Gleadle J.M.
      J. Biol. Chem. 279:38458-38465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, SUBSTRATE SPECIFICITY.
    13. "Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer."
      Lee S., Nakamura E., Yang H., Wei W., Linggi M.S., Sajan M.P., Farese R.V., Freeman R.S., Carter B.D., Kaelin W.G. Jr., Schlisio S.
      Cancer Cell 8:155-167(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL."
      Xie L., Xiao K., Whalen E.J., Forrester M.T., Freeman R.S., Fong G., Gygi S.P., Lefkowitz R.J., Stamler J.S.
      Sci. Signal. 2:RA33-RA33(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADRB2, FUNCTION, MUTAGENESIS OF 91-ILE--VAL-102.
    15. "Prolyl hydroxylase 3 interacts with Bcl-2 to regulate doxorubicin-induced apoptosis in H9c2 cells."
      Liu Y., Huo Z., Yan B., Lin X., Zhou Z.N., Liang X., Zhu W., Liang D., Li L., Liu Y., Zhao H., Sun Y., Chen Y.H.
      Biochem. Biophys. Res. Commun. 401:231-237(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCL2, FUNCTION.
    16. "PHD3 regulates differentiation, tumour growth and angiogenesis in pancreatic cancer."
      Su Y., Loos M., Giese N., Hines O.J., Diebold I., Gorlach A., Metzen E., Pastorekova S., Friess H., Buchler P.
      Br. J. Cancer 103:1571-1579(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    17. "Prolyl hydroxylase domain protein 3 targets Pax2 for destruction."
      Yan B., Jiao S., Zhang H.S., Lv D.D., Xue J., Fan L., Wu G.H., Fang J.
      Biochem. Biophys. Res. Commun. 409:315-320(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAX2, TISSUE SPECIFICITY, FUNCTION.
    18. "Biochemical characterization of human HIF hydroxylases using HIF protein substrates that contain all three hydroxylation sites."
      Pappalardi M.B., McNulty D.E., Martin J.D., Fisher K.E., Jiang Y., Burns M.C., Zhao H., Ho T., Sweitzer S., Schwartz B., Annan R.S., Copeland R.A., Tummino P.J., Luo L.
      Biochem. J. 436:363-369(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
    19. "Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1."
      Luo W., Hu H., Chang R., Zhong J., Knabel M., O'Meally R., Cole R.N., Pandey A., Semenza G.L.
      Cell 145:732-744(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKM, FUNCTION.
    20. "The oxygen sensor PHD3 limits glycolysis under hypoxia via direct binding to pyruvate kinase."
      Chen N., Rinner O., Czernik D., Nytko K.J., Zheng D., Stiehl D.P., Zamboni N., Gstaiger M., Frei C.
      Cell Res. 21:983-986(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKM, FUNCTION.
    21. Cited for: FUNCTION, INDUCTION.
    22. "Effects of polynitrogen compounds on the activity of recombinant human HIF-1alpha prolyl hydroxylase 3 in E. coli."
      Geng Z., Zhu J., Cao J., Geng J., Song X., Zhang Z., Bian N., Wang Z.
      J. Inorg. Biochem. 105:391-399(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ENZYME REGULATION.
    23. "PHD3-dependent hydroxylation of HCLK2 promotes the DNA damage response."
      Xie L., Pi X., Mishra A., Fong G., Peng J., Patterson C.
      J. Clin. Invest. 122:2827-2836(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. Cited for: INTERACTION WITH LIMD1; WTIP AND AJUBA.

    Entry informationi

    Entry nameiEGLN3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H6Z9
    Secondary accession number(s): Q2TA79, Q3B8N4, Q6P1R2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

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