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Q9H6Z9

- EGLN3_HUMAN

UniProt

Q9H6Z9 - EGLN3_HUMAN

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Protein

Egl nine homolog 3

Gene
EGLN3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1351Iron By similarity
Metal bindingi137 – 1371Iron By similarity
Metal bindingi196 – 1961Iron By similarity
Binding sitei205 – 20512-oxoglutarate By similarity

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
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

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

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. 1 Publication
Mutagenesisi137 – 1371D → A: Eliminates hydroxylase activity. 1 Publication
Mutagenesisi196 – 1961H → A: Eliminates hydroxylase activity. 1 Publication

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.7 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.6 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 21499Fe2OG dioxygenaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 7312Beta(2)beta(3) 'finger-like' loop By 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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 124 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

Dasty 3

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