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Protein

Egl nine homolog 3

Gene

EGLN3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:

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

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • apoptotic process Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB-KW
  • cellular response to hypoxia Source: Reactome
  • peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: FlyBase
  • protein hydroxylation Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of neuron apoptotic process Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  • 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.
1.14.11.29. 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 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:14661. EGLN3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • 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.

Chemistry

DrugBankiDB00126. Vitamin C.

Polymorphism and mutation databases

BioMutaiEGLN3.
DMDMi32129515.

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

BgeeiQ9H6Z9.
CleanExiHS_EGLN3.
ExpressionAtlasiQ9H6Z9. baseline and differential.
GenevestigatoriQ9H6Z9.

Organism-specific databases

HPAiHPA059256.

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
ABI2Q9NYB93EBI-1175354,EBI-743598
EFHC2Q5JST63EBI-1175354,EBI-2349927
FOXJ2Q9P0K83EBI-1175354,EBI-2869608
HIF1AD0VY793EBI-1175354,EBI-10179332
HIF1AQ166653EBI-1175354,EBI-447269
NCAPH2Q6IBW4-43EBI-1175354,EBI-10247000
PKMP14618-12EBI-1175354,EBI-4304679
RELQ048643EBI-1175354,EBI-307352
SERTAD1Q53GC03EBI-1175354,EBI-2826300
TTC23LQ6PF05-33EBI-1175354,EBI-10182647

Protein-protein interaction databases

BioGridi125185. 34 interactions.
IntActiQ9H6Z9. 16 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.
GeneTreeiENSGT00390000001936.
HOGENOMiHOG000004818.
HOVERGENiHBG051455.
InParanoidiQ9H6Z9.
KOiK09592.
OMAiDKRERRY.
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

        10         20         30         40         50
MPLGHIMRLD LEKIALEYIV PCLHEVGFCY LDNFLGEVVG DCVLERVKQL
60 70 80 90 100
HCTGALRDGQ LAGPRAGVSK RHLRGDQITW IGGNEEGCEA ISFLLSLIDR
110 120 130 140 150
LVLYCGSRLG KYYVKERSKA MVACYPGNGT GYVRHVDNPN GDGRCITCIY
160 170 180 190 200
YLNKNWDAKL HGGILRIFPE GKSFIADVEP IFDRLLFFWS DRRNPHEVQP
210 220 230
SYATRYAMTV WYFDAEERAE AKKKFRNLTR KTESALTED
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi125185. 34 interactions.
IntActiQ9H6Z9. 16 interactions.
MINTiMINT-1206284.
STRINGi9606.ENSP00000250457.

Chemistry

BindingDBiQ9H6Z9.
ChEMBLiCHEMBL5705.
DrugBankiDB00126. Vitamin C.

PTM databases

PhosphoSiteiQ9H6Z9.

Polymorphism and mutation databases

BioMutaiEGLN3.
DMDMi32129515.

Proteomic databases

MaxQBiQ9H6Z9.
PaxDbiQ9H6Z9.
PRIDEiQ9H6Z9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi112399.
GeneCardsiGC14M034393.
HGNCiHGNC:14661. EGLN3.
HPAiHPA059256.
MIMi606426. gene.
neXtProtiNX_Q9H6Z9.
PharmGKBiPA27672.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG326511.
GeneTreeiENSGT00390000001936.
HOGENOMiHOG000004818.
HOVERGENiHBG051455.
InParanoidiQ9H6Z9.
KOiK09592.
OMAiDKRERRY.
OrthoDBiEOG7TBC2W.
PhylomeDBiQ9H6Z9.
TreeFamiTF314595.

Enzyme and pathway databases

BRENDAi1.14.11.2. 2681.
1.14.11.29. 2681.
ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.

Miscellaneous databases

ChiTaRSiEGLN3. human.
GeneWikiiEGLN3.
GenomeRNAii112399.
NextBioi78578.
PROiQ9H6Z9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H6Z9.
CleanExiHS_EGLN3.
ExpressionAtlasiQ9H6Z9. baseline and differential.
GenevestigatoriQ9H6Z9.

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.