Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96KS0 (EGLN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Egl nine homolog 2

EC=1.14.11.29
Alternative name(s):
Estrogen-induced tag 6
HPH-3
Hypoxia-inducible factor prolyl hydroxylase 1
Short name=HIF-PH1
Short name=HIF-prolyl hydroxylase 1
Short name=HPH-1
Prolyl hydroxylase domain-containing protein 1
Short name=PHD1
Gene names
Name:EGLN2
Synonyms:EIT6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length407 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. 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. EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle. Also regulates susceptibility to normoxic oxidative neuronal death. Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation. Hydroxylates IKBKB, mediating NF-kappaB activation in hypoxic conditions. Target proteins are preferencially recognized via a LXXLAP motif. Ref.9 Ref.12 Ref.15 Ref.16 Ref.18 Ref.21

Catalytic activity

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

Cofactor

Binds 1 Fe2+ ion per subunit.

Ascorbate.

Subunit structure

Interacts (preferably isoform p40)with SIAH2; the interaction targets both SIAH2 isoforms for proteasomal degradation in vitro. Interacts with LIMD1, WTIP and AJUBA. Ref.15 Ref.20

Subcellular location

Nucleus Ref.10 Ref.13 Ref.17 Ref.18.

Tissue specificity

Expressed in adult and fetal heart, brain, liver, lung, skeletal muscle, and kidney. Also expressed in testis and placenta. Highest levels in adult brain, placenta, lung, kidney, and testis. Expressed in hormone responsive tissues, including normal and cancerous mammary, ovarian and prostate epithelium. Ref.10

Induction

By estrogen. Isoform p43 is induced by hypoxia leading to protein stability. Isoform p40 repressed by hypoxia. Both isoforms are induced by proteasomal inhibitor MG132 (at protein level). Ref.2 Ref.13 Ref.14 Ref.15

Domain

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

Sequence similarities

Contains 1 Fe2OG dioxygenase domain.

Sequence caution

The sequence AAH01723.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative initiation
   LigandIron
Metal-binding
Vitamin C
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from direct assay Ref.9. Source: UniProtKB

cellular response to hypoxia

Traceable author statement. Source: Reactome

intracellular estrogen receptor signaling pathway

Non-traceable author statement Ref.2. Source: UniProtKB

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

Inferred from direct assay PubMed 11598268. Source: FlyBase

positive regulation of protein catabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of cell growth

Non-traceable author statement Ref.2. Source: UniProtKB

regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 19587290. Source: UniProtKB

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

Traceable author statement. Source: Reactome

response to hypoxia

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.2Ref.13. Source: UniProtKB

   Molecular_functionL-ascorbic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

ferrous iron binding

Non-traceable author statement Ref.11. Source: UniProtKB

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

Inferred from direct assay Ref.9. Source: UniProtKB

oxygen sensor activity

Inferred from direct assay Ref.9. Source: UniProtKB

peptidyl-proline 4-dioxygenase activity

Inferred from direct assay PubMed 11598268. Source: FlyBase

protein binding

Inferred from physical interaction Ref.20. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIF1AQ166652EBI-726614,EBI-447269

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform p43 (identifier: Q96KS0-1)

Also known as: PHD1p43;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform p40 (identifier: Q96KS0-2)

Also known as: PHD1p40;

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407Egl nine homolog 2
PRO_0000206664

Regions

Domain278 – 37699Fe2OG dioxygenase
Region89 – 13446Bipartite nuclear localization signal
Region225 – 23511Beta(2)beta(3) 'finger-like' loop

Sites

Metal binding2971Iron By similarity
Metal binding2991Iron By similarity
Metal binding3581Iron By similarity
Binding site36712-oxoglutarate By similarity

Natural variations

Alternative sequence1 – 3333Missing in isoform p40.
VSP_038836

Experimental info

Mutagenesis11M → A: Leads to expression of isoform p40 only. Ref.15
Mutagenesis341M → A: Leads to expression of isoform p43 only. Ref.15
Mutagenesis1021K → A: Retained in the nucleus. Ref.18
Mutagenesis1061R → A: Retained in the nucleus. Ref.18
Mutagenesis1131R → A: Retained in the nucleus. Ref.18
Mutagenesis1191R → A: Cytoplasmic and nuclear localization. Reduced transcriptional activity of HIF1A as for wild type. Ref.18
Mutagenesis1341R → A: Retained in the nucleus. Ref.18
Mutagenesis2971H → A: Eliminates hydroxylase activity. Ref.11
Mutagenesis2991D → A: Eliminates hydroxylase activity. Ref.11
Mutagenesis3581H → A: Eliminates hydroxylase activity. Ref.9 Ref.11
Mutagenesis3671R → A: Eliminates hydroxylase activity. Ref.11
Mutagenesis3671R → K: Eliminates hydroxylase activity on a HIF1A peptide. Ref.11
Sequence conflict1761R → P in AAK82943. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform p43 (PHD1p43) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F172E9B0482C9CF3

FASTA40743,650
        10         20         30         40         50         60 
MDSPCQPQPL SQALPQLPGS SSEPLEPEPG RARMGVESYL PCPLLPSYHC PGVPSEASAG 

        70         80         90        100        110        120 
SGTPRATATS TTASPLRDGF GGQDGGELRP LQSEGAAALV TKGCQRLAAQ GARPEAPKRK 

       130        140        150        160        170        180 
WAEDGGDAPS PSKRPWARQE NQEAEREGGM SCSCSSGSGE ASAGLMEEAL PSAPERLALD 

       190        200        210        220        230        240 
YIVPCMRYYG ICVKDSFLGA ALGGRVLAEV EALKRGGRLR DGQLVSQRAI PPRSIRGDQI 

       250        260        270        280        290        300 
AWVEGHEPGC RSIGALMAHV DAVIRHCAGR LGSYVINGRT KAMVACYPGN GLGYVRHVDN 

       310        320        330        340        350        360 
PHGDGRCITC IYYLNQNWDV KVHGGLLQIF PEGRPVVANI EPLFDRLLIF WSDRRNPHEV 

       370        380        390        400 
KPAYATRYAI TVWYFDAKER AAAKDKYQLA SGQKGVQVPV SQPPTPT 

« Hide

Isoform p40 (PHD1p40) [UniParc].

Checksum: 228015782B7DE743
Show »

FASTA37440,168

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] (ISOFORM P43).
[2]"Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression)."
Seth P., Krop I., Porter D., Polyak K.
Oncogene 21:836-843(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P43), INDUCTION.
Tissue: Mammary cancer.
[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] (ISOFORM P43).
Tissue: Fetal brain.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P43).
Tissue: Endometrium.
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM P43).
Tissue: Lung and Testis.
[8]"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.
[9]"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, MUTAGENESIS OF HIS-358.
[10]"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.
[11]"The use of dioxygen by HIF prolyl hydroxylase (PHD1)."
McNeill L.A., Hewitson K.S., Gleadle J.M., Horsfall L.E., Oldham N.J., Maxwell P.H., Pugh C.W., Ratcliffe P.J., Schofield C.J.
Bioorg. Med. Chem. Lett. 12:1547-1550(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-297; ASP-299; HIS-358 AND ARG-367.
[12]"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.
[13]"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.
[14]"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.
[15]"Characterization of different isoforms of the HIF prolyl hydroxylase PHD1 generated by alternative initiation."
Tian Y.M., Mole D.R., Ratcliffe P.J., Gleadle J.M.
Biochem. J. 397:179-186(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SIAH2, ALTERNATIVE INITIATION, INDUCTION, MUTAGENESIS OF MET-1 AND MET-34.
[16]"Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity."
Cummins E.P., Berra E., Comerford K.M., Ginouves A., Fitzgerald K.T., Seeballuck F., Godson C., Nielsen J.E., Moynagh P., Pouyssegur J., Taylor C.T.
Proc. Natl. Acad. Sci. U.S.A. 103:18154-18159(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Cellular oxygen sensing: Importins and exportins are mediators of intracellular localisation of prolyl-4-hydroxylases PHD1 and PHD2."
Steinhoff A., Pientka F.K., Mockel S., Kettelhake A., Hartmann E., Kohler M., Depping R.
Biochem. Biophys. Res. Commun. 387:705-711(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[18]"Role of the intracellular localization of HIF-prolyl hydroxylases."
Yasumoto K., Kowata Y., Yoshida A., Torii S., Sogawa K.
Biochim. Biophys. Acta 1793:792-797(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-102; ARG-106; ARG-113; ARG-119 AND ARG-134.
[19]"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.
[20]"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.
[21]"PHD1 links cell-cycle progression to oxygen sensing through hydroxylation of the centrosomal protein Cep192."
Moser S.C., Bensaddek D., Ortmann B., Maure J.F., Mudie S., Blow J.J., Lamond A.I., Swedlow J.R., Rocha S.
Dev. Cell 26:381-392(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ310544 mRNA. Translation: CAC42510.1.
AY040565 mRNA. Translation: AAK82943.1.
AK291385 mRNA. Translation: BAF84074.1.
AL832506 mRNA. No translation available.
AC008537 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW57008.1.
BC001723 mRNA. Translation: AAH01723.1. Different initiation.
BC036051 mRNA. Translation: AAH36051.1.
CCDSCCDS12567.1. [Q96KS0-1]
RefSeqNP_444274.1. NM_053046.3. [Q96KS0-1]
NP_542770.2. NM_080732.3. [Q96KS0-1]
UniGeneHs.515417.
Hs.631539.
Hs.730737.

3D structure databases

ProteinModelPortalQ96KS0.
SMRQ96KS0. Positions 176-387.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125184. 20 interactions.
IntActQ96KS0. 6 interactions.
MINTMINT-1186497.
STRING9606.ENSP00000307080.

Chemistry

BindingDBQ96KS0.
ChEMBLCHEMBL3028.
DrugBankDB00126. Vitamin C.

PTM databases

PhosphoSiteQ96KS0.

Polymorphism databases

DMDM32129513.

Proteomic databases

PaxDbQ96KS0.
PRIDEQ96KS0.

Protocols and materials databases

DNASU112398.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303961; ENSP00000307080; ENSG00000269858. [Q96KS0-1]
ENST00000406058; ENSP00000385253; ENSG00000269858. [Q96KS0-1]
ENST00000593726; ENSP00000469686; ENSG00000269858. [Q96KS0-1]
ENST00000594140; ENSP00000472414; ENSG00000269858.
GeneID112398.
KEGGhsa:112398.
UCSCuc002opg.4. human. [Q96KS0-1]

Organism-specific databases

CTD112398.
GeneCardsGC19P041304.
HGNCHGNC:14660. EGLN2.
HPAHPA056649.
MIM606424. gene.
neXtProtNX_Q96KS0.
PharmGKBPA27671.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3751.
HOGENOMHOG000013099.
HOVERGENHBG051456.
InParanoidQ96KS0.
KOK09592.
OMAGGELWPL.
PhylomeDBQ96KS0.
TreeFamTF314595.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000171570-MONOMER.
BRENDA1.14.11.2. 2681.
ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

BgeeQ96KS0.
CleanExHS_EGLN2.
GenevestigatorQ96KS0.

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

ChiTaRSEGLN2. human.
GeneWikiEGLN2.
GenomeRNAi112398.
NextBio78572.
PROQ96KS0.
SOURCESearch...

Entry information

Entry nameEGLN2_HUMAN
AccessionPrimary (citable) accession number: Q96KS0
Secondary accession number(s): A8K5S0, Q8WWY4, Q9BV14
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 119 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 chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM