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Q9H6Z9 (EGLN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EGLN3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.9 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23

Catalytic activity

Hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 = hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2. Ref.7

Cofactor

Binds 1 Fe2+ ion per subunit.

Ascorbate.

Enzyme regulation

Activated in cardiovascular cells and Hela cells following exposure to hypoxia. Inhibited by polynitrogen compounds probably by chelation to Fe2+ ions. Ref.5 Ref.10 Ref.22

Subunit structure

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. Ref.14 Ref.15 Ref.17 Ref.19 Ref.20 Ref.24

Subcellular location

Nucleus. Cytoplasm. Note: Colocalizes with WDR83 in the cytoplasm By similarity. Ref.8 Ref.11

Tissue specificity

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. Ref.8 Ref.10 Ref.17

Induction

Induced by hypoxia in a number of cells including neutrophils and certain cancer cell lines. Up-regulated 10-fold in pancreatic cancers. Ref.5 Ref.10 Ref.11 Ref.12 Ref.16 Ref.21 Ref.22

Domain

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

Sequence similarities

Contains 1 Fe2OG dioxygenase domain.

Ontologies

Keywords
   Biological processApoptosis
DNA damage
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandIron
Metal-binding
Vitamin C
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from expression pattern Ref.16. Source: UniProtKB

apoptotic process

Inferred from expression pattern Ref.16. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to hypoxia

Traceable author statement. Source: Reactome

peptidyl-proline hydroxylation to 4-hydroxy-L-proline

Inferred from direct assay Ref.7. Source: FlyBase

protein hydroxylation

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of cell proliferation

Inferred from expression pattern Ref.16. Source: UniProtKB

regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

response to hypoxia

Inferred from expression pattern Ref.16. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionL-ascorbic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

iron ion binding

Inferred from electronic annotation. Source: InterPro

peptidyl-proline 4-dioxygenase activity

Inferred from direct assay Ref.7. Source: FlyBase

protein binding

Inferred from physical interaction Ref.14Ref.15Ref.17Ref.24. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 239239Egl nine homolog 3
PRO_0000206666

Regions

Domain116 – 21499Fe2OG dioxygenase
Region62 – 7312Beta(2)beta(3) 'finger-like' loop By similarity
Region88 – 10417Required for interaction with ADRB2

Sites

Metal binding1351Iron By similarity
Metal binding1371Iron By similarity
Metal binding1961Iron By similarity
Binding site20512-oxoglutarate By similarity

Natural variations

Natural variant1361V → L.
Corresponds to variant rs17102002 [ dbSNP | Ensembl ].
VAR_050449
Natural variant2341S → T.
Corresponds to variant rs17101995 [ dbSNP | Ensembl ].
VAR_050450

Experimental info

Mutagenesis91 – 10212ISFLL…IDRLV → RSFLRSLIRRLR: Abolishes interaction with ADRB2 and no increase in cellular abundance of ADRB2. Ref.14
Mutagenesis1351H → A: Eliminates hydroxylase activity. Ref.7
Mutagenesis1371D → A: Eliminates hydroxylase activity. Ref.7
Mutagenesis1961H → A: Eliminates hydroxylase activity. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q9H6Z9 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9DA3A0F80168557B

FASTA23927,261
        10         20         30         40         50         60 
MPLGHIMRLD LEKIALEYIV PCLHEVGFCY LDNFLGEVVG DCVLERVKQL HCTGALRDGQ 

        70         80         90        100        110        120 
LAGPRAGVSK RHLRGDQITW IGGNEEGCEA ISFLLSLIDR LVLYCGSRLG KYYVKERSKA 

       130        140        150        160        170        180 
MVACYPGNGT GYVRHVDNPN GDGRCITCIY YLNKNWDAKL HGGILRIFPE GKSFIADVEP 

       190        200        210        220        230 
IFDRLLFFWS DRRNPHEVQP SYATRYAMTV WYFDAEERAE AKKKFRNLTR KTESALTED 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation."
Epstein A.C.R., Gleadle J.M., McNeill L.A., Hewitson K.S., O'Rourke J., Mole D.R., Mukherji M., Metzen E., Wilson M.I., Dhanda A., Tian Y.M., Masson N., Hamilton D.L., Jaakkola P., Barstead R., Hodgkin J., Maxwell P.H., Pugh C.W., Schofield C.J., Ratcliffe P.J.
Cell 107:43-54(2001) [PubMed] [Europe PMC] [Abstract]
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]"Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing."
Metzen E., Berchner-Pfannschmidt U., Stengel P., Marxsen J.H., Stolze I., Klinger M., Huang W.Q., Wotzlaw C., Hellwig-Burgel T., Jelkmann W., Acker H., Fandrey J.
J. Cell Sci. 116:1319-1326(2003) [PubMed] [Europe PMC] [Abstract]
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]"Prolyl hydroxylase 3 (PHD3) is essential for hypoxic regulation of neutrophilic inflammation in humans and mice."
Walmsley S.R., Chilvers E.R., Thompson A.A., Vaughan K., Marriott H.M., Parker L.C., Shaw G., Parmar S., Schneider M., Sabroe I., Dockrell D.H., Milo M., Taylor C.T., Johnson R.S., Pugh C.W., Ratcliffe P.J., Maxwell P.H., Carmeliet P., Whyte M.K.
J. Clin. Invest. 121:1053-1063(2011) [PubMed] [Europe PMC] [Abstract]
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]"The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity."
Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V.
Nat. Cell Biol. 14:201-208(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIMD1; WTIP AND AJUBA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9646.1.
RefSeqNP_071356.1. NM_022073.3.
UniGeneHs.135507.

3D structure databases

ProteinModelPortalQ9H6Z9.
SMRQ9H6Z9. Positions 13-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125185. 26 interactions.
IntActQ9H6Z9. 8 interactions.
MINTMINT-1206284.
STRING9606.ENSP00000250457.

Chemistry

BindingDBQ9H6Z9.
ChEMBLCHEMBL5705.
DrugBankDB00126. Vitamin C.

PTM databases

PhosphoSiteQ9H6Z9.

Polymorphism databases

DMDM32129515.

Proteomic databases

MaxQBQ9H6Z9.
PaxDbQ9H6Z9.
PRIDEQ9H6Z9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250457; ENSP00000250457; ENSG00000129521.
GeneID112399.
KEGGhsa:112399.
UCSCuc001wsa.4. human.

Organism-specific databases

CTD112399.
GeneCardsGC14M034393.
HGNCHGNC:14661. EGLN3.
HPACAB012351.
MIM606426. gene.
neXtProtNX_Q9H6Z9.
PharmGKBPA27672.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326511.
HOGENOMHOG000004818.
HOVERGENHBG051455.
InParanoidQ9H6Z9.
KOK09592.
OMAWIGGTEE.
OrthoDBEOG7TBC2W.
PhylomeDBQ9H6Z9.
TreeFamTF314595.

Enzyme and pathway databases

BRENDA1.14.11.2. 2681.
ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ9H6Z9.
BgeeQ9H6Z9.
CleanExHS_EGLN3.
GenevestigatorQ9H6Z9.

Family and domain databases

InterProIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
[Graphical view]
PfamPF13640. 2OG-FeII_Oxy_3. 1 hit.
[Graphical view]
SMARTSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEGLN3. human.
GeneWikiEGLN3.
GenomeRNAi112399.
NextBio78578.
PROQ9H6Z9.
SOURCESearch...

Entry information

Entry nameEGLN3_HUMAN
AccessionPrimary (citable) accession number: Q9H6Z9
Secondary accession number(s): Q2TA79, Q3B8N4, Q6P1R2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM