Q96KS0 (EGLN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.9 Ref.14 Ref.16
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.14 Ref.18
Subcellular location	Nucleus Ref.10 Ref.12 Ref.15 Ref.16.
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.12 Ref.13 Ref.14
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 component	Nucleus
Coding sequence diversity	Alternative initiation
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from direct assay Ref.9. Source: UniProtKB 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
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	L-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 single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW oxygen sensor activity Inferred from direct assay Ref.9. Source: UniProtKB peptidyl-proline 4-dioxygenase activity Inferred from direct assay PubMed 11598268. Source: FlyBase
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 407	407	Egl nine homolog 2		PRO_0000206664
Regions
	Domain	278 – 376	99	Fe2OG dioxygenase
	Region	89 – 134	46	Bipartite nuclear localization signal
	Region	225 – 235	11	Beta(2)beta(3) 'finger-like' loop
Sites
	Metal binding	297	1	Iron By similarity
	Metal binding	299	1	Iron By similarity
	Metal binding	358	1	Iron By similarity
	Binding site	367	1	2-oxoglutarate By similarity
Natural variations
	Alternative sequence	1 – 33	33	Missing in isoform p40.		VSP_038836
Experimental info
	Mutagenesis	1	1	M → A: Leads to expression of isoform p40 only. Ref.14
	Mutagenesis	34	1	M → A: Leads to expression of isoform p43 only. Ref.14
	Mutagenesis	102	1	K → A: Retained in the nucleus. Ref.16
	Mutagenesis	106	1	R → A: Retained in the nucleus. Ref.16
	Mutagenesis	113	1	R → A: Retained in the nucleus. Ref.16
	Mutagenesis	119	1	R → A: Cytoplasmic and nuclear localization. Reduced transcriptional activity of HIF1A as for wild type. Ref.16
	Mutagenesis	134	1	R → A: Retained in the nucleus. Ref.16
	Mutagenesis	297	1	H → A: Eliminates hydroxylase activity. Ref.11
	Mutagenesis	299	1	D → A: Eliminates hydroxylase activity. Ref.11
	Mutagenesis	358	1	H → A: Eliminates hydroxylase activity. Ref.9 Ref.11
	Mutagenesis	367	1	R → A: Eliminates hydroxylase activity. Ref.11
	Mutagenesis	367	1	R → K: Eliminates hydroxylase activity on a HIF1A peptide. Ref.11
	Sequence conflict	176	1	R → P in AAK82943. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform p43 (PHD1p43) [UniParc]. Last modified December 1, 2001. Version 1. Checksum: F172E9B0482C9CF3	FASTA	407	43,650
	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
	Isoform p40 (PHD1p40) [UniParc]. Checksum: 228015782B7DE743	FASTA	374	40,168
	10 20 30 40 50 60 MGVESYLPCP LLPSYHCPGV PSEASAGSGT PRATATSTTA SPLRDGFGGQ DGGELRPLQS 70 80 90 100 110 120 EGAAALVTKG CQRLAAQGAR PEAPKRKWAE DGGDAPSPSK RPWARQENQE AEREGGMSCS 130 140 150 160 170 180 CSSGSGEASA GLMEEALPSA PERLALDYIV PCMRYYGICV KDSFLGAALG GRVLAEVEAL 190 200 210 220 230 240 KRGGRLRDGQ LVSQRAIPPR SIRGDQIAWV EGHEPGCRSI GALMAHVDAV IRHCAGRLGS 250 260 270 280 290 300 YVINGRTKAM VACYPGNGLG YVRHVDNPHG DGRCITCIYY LNQNWDVKVH GGLLQIFPEG 310 320 330 340 350 360 RPVVANIEPL FDRLLIFWSD RRNPHEVKPA YATRYAITVW YFDAKERAAA KDKYQLASGQ 370 KGVQVPVSQP PTPT

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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, MASS SPECTROMETRY.
[18]	"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	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.
IPI	IPI00074957. IPI00955972.
RefSeq	NP_444274.1. NM_053046.3. NP_542770.2. NM_080732.3.
UniGene	Hs.515417. Hs.631539. Hs.730737.
3D structure databases
ProteinModelPortal	Q96KS0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96KS0. 2 interactions.
MINT	MINT-1186497.
STRING	9606.ENSP00000307080.
PTM databases
PhosphoSite	Q96KS0.
Polymorphism databases
DMDM	32129513.
Proteomic databases
PaxDb	Q96KS0.
PRIDE	Q96KS0.
Protocols and materials databases
DNASU	112398.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000303961; ENSP00000307080; ENSG00000269858. ENST00000406058; ENSP00000385253; ENSG00000269858. ENST00000593726; ENSP00000469686; ENSG00000269858. ENST00000594140; ENSP00000472414; ENSG00000269858.
GeneID	112398.
KEGG	hsa:112398.
UCSC	uc002opg.4. human.
Organism-specific databases
CTD	112398.
GeneCards	GC19P041305.
HGNC	HGNC:14660. EGLN2.
MIM	606424. gene.
neXtProt	NX_Q96KS0.
PharmGKB	PA27671.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3751.
HOGENOM	HOG000013099.
HOVERGEN	HBG051456.
InParanoid	Q96KS0.
KO	K09592.
OMA	GGELWPL.
OrthoDB	EOG4HHP2P.
PhylomeDB	Q96KS0.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000171570-MONOMER.
BRENDA	1.14.11.2. 2681.
Pathway_Interaction_DB	hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.
Reactome	REACT_120956. Cellular responses to stress.
Gene expression databases
Bgee	Q96KS0.
CleanEx	HS_EGLN2.
Genevestigator	Q96KS0.
GermOnline	ENSG00000171570. Homo sapiens.
Family and domain databases
InterPro	IPR005123. Oxoglu/Fe-dep_dioxygenase. IPR006620. Pro_4_hyd_alph. [Graphical view]
Pfam	PF13640. 2OG-FeII_Oxy_3. 1 hit. [Graphical view]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
PROSITE	PS51471. FE2OG_OXY. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q96KS0.
ChEMBL	CHEMBL3028.
ChiTaRS	EGLN2. human.
DrugBank	DB00126. Vitamin C.
GenomeRNAi	112398.
NextBio	78572.
SOURCE	Search...

Entry information

Entry name

EGLN2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.