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Protein

Egl nine homolog 2

Gene

EGLN2

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. 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 preferentially recognized via a LXXLAP motif.6 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi297 – 2971IronPROSITE-ProRule annotation
Metal bindingi299 – 2991IronPROSITE-ProRule annotation
Metal bindingi358 – 3581IronPROSITE-ProRule annotation
Binding sitei367 – 36712-oxoglutaratePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: UniProtKB
  • cellular response to hypoxia Source: Reactome
  • intracellular estrogen receptor signaling pathway Source: UniProtKB
  • peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: FlyBase
  • positive regulation of protein catabolic process Source: UniProtKB
  • regulation of cell growth 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 - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000171570-MONOMER.
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 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 namesi
Name:EGLN2
Synonyms:EIT6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:14660. EGLN2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → A: Leads to expression of isoform p40 only. 1 Publication
Mutagenesisi34 – 341M → A: Leads to expression of isoform p43 only. 1 Publication
Mutagenesisi102 – 1021K → A: Retained in the nucleus. 1 Publication
Mutagenesisi106 – 1061R → A: Retained in the nucleus. 1 Publication
Mutagenesisi113 – 1131R → A: Retained in the nucleus. 1 Publication
Mutagenesisi119 – 1191R → A: Cytoplasmic and nuclear localization. Reduced transcriptional activity of HIF1A as for wild type. 1 Publication
Mutagenesisi134 – 1341R → A: Retained in the nucleus. 1 Publication
Mutagenesisi297 – 2971H → A: Eliminates hydroxylase activity. 1 Publication
Mutagenesisi299 – 2991D → A: Eliminates hydroxylase activity. 1 Publication
Mutagenesisi358 – 3581H → A: Eliminates hydroxylase activity. 2 Publications
Mutagenesisi367 – 3671R → A: Eliminates hydroxylase activity. 1 Publication
Mutagenesisi367 – 3671R → K: Eliminates hydroxylase activity on a HIF1A peptide. 1 Publication

Organism-specific databases

PharmGKBiPA27671.

Chemistry

DrugBankiDB00126. Vitamin C.

Polymorphism and mutation databases

BioMutaiEGLN2.
DMDMi32129513.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Egl nine homolog 2PRO_0000206664Add
BLAST

Proteomic databases

MaxQBiQ96KS0.
PaxDbiQ96KS0.
PRIDEiQ96KS0.

PTM databases

PhosphoSiteiQ96KS0.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

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).4 Publications

Gene expression databases

BgeeiQ96KS0.
CleanExiHS_EGLN2.
ExpressionAtlasiQ96KS0. baseline.
GenevisibleiQ96KS0. HS.

Interactioni

Subunit structurei

Interacts (preferably isoform p40) with SIAH2; the interaction targets both SIAH2 isoforms for proteasomal degradation in vitro. Interacts with LIMD1, WTIP and AJUBA.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIF1AQ166652EBI-726614,EBI-447269

Protein-protein interaction databases

BioGridi125184. 18 interactions.
IntActiQ96KS0. 6 interactions.
MINTiMINT-1186497.
STRINGi9606.ENSP00000307080.

Structurei

3D structure databases

ProteinModelPortaliQ96KS0.
SMRiQ96KS0. Positions 176-387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini278 – 37699Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 23511Beta(2)beta(3) 'finger-like' loopAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 13446Bipartite nuclear localization signalAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3751.
GeneTreeiENSGT00390000001936.
HOGENOMiHOG000013099.
HOVERGENiHBG051456.
InParanoidiQ96KS0.
KOiK09592.
OMAiEGGMSCG.
PhylomeDBiQ96KS0.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform p43 (identifier: Q96KS0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDSPCQPQPL SQALPQLPGS SSEPLEPEPG RARMGVESYL PCPLLPSYHC
60 70 80 90 100
PGVPSEASAG SGTPRATATS TTASPLRDGF GGQDGGELRP LQSEGAAALV
110 120 130 140 150
TKGCQRLAAQ GARPEAPKRK WAEDGGDAPS PSKRPWARQE NQEAEREGGM
160 170 180 190 200
SCSCSSGSGE ASAGLMEEAL PSAPERLALD YIVPCMRYYG ICVKDSFLGA
210 220 230 240 250
ALGGRVLAEV EALKRGGRLR DGQLVSQRAI PPRSIRGDQI AWVEGHEPGC
260 270 280 290 300
RSIGALMAHV DAVIRHCAGR LGSYVINGRT KAMVACYPGN GLGYVRHVDN
310 320 330 340 350
PHGDGRCITC IYYLNQNWDV KVHGGLLQIF PEGRPVVANI EPLFDRLLIF
360 370 380 390 400
WSDRRNPHEV KPAYATRYAI TVWYFDAKER AAAKDKYQLA SGQKGVQVPV

SQPPTPT
Length:407
Mass (Da):43,650
Last modified:December 1, 2001 - v1
Checksum:iF172E9B0482C9CF3
GO
Isoform p40 (identifier: Q96KS0-2) [UniParc]FASTAAdd to basket

Also known as: PHD1p40

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

Show »
Length:374
Mass (Da):40,168
Checksum:i228015782B7DE743
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761R → P in AAK82943 (PubMed:11850811).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333Missing in isoform p40. CuratedVSP_038836Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12567.1. [Q96KS0-1]
RefSeqiNP_444274.1. NM_053046.3. [Q96KS0-1]
NP_542770.2. NM_080732.3. [Q96KS0-1]
UniGeneiHs.515417.
Hs.631539.
Hs.730737.

Genome annotation databases

EnsembliENST00000303961; ENSP00000307080; ENSG00000269858.
ENST00000406058; ENSP00000385253; ENSG00000269858.
ENST00000593726; ENSP00000469686; ENSG00000269858.
GeneIDi112398.
KEGGihsa:112398.
UCSCiuc002opg.4. human. [Q96KS0-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12567.1. [Q96KS0-1]
RefSeqiNP_444274.1. NM_053046.3. [Q96KS0-1]
NP_542770.2. NM_080732.3. [Q96KS0-1]
UniGeneiHs.515417.
Hs.631539.
Hs.730737.

3D structure databases

ProteinModelPortaliQ96KS0.
SMRiQ96KS0. Positions 176-387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125184. 18 interactions.
IntActiQ96KS0. 6 interactions.
MINTiMINT-1186497.
STRINGi9606.ENSP00000307080.

Chemistry

BindingDBiQ96KS0.
ChEMBLiCHEMBL3028.
DrugBankiDB00126. Vitamin C.

PTM databases

PhosphoSiteiQ96KS0.

Polymorphism and mutation databases

BioMutaiEGLN2.
DMDMi32129513.

Proteomic databases

MaxQBiQ96KS0.
PaxDbiQ96KS0.
PRIDEiQ96KS0.

Protocols and materials databases

DNASUi112398.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303961; ENSP00000307080; ENSG00000269858.
ENST00000406058; ENSP00000385253; ENSG00000269858.
ENST00000593726; ENSP00000469686; ENSG00000269858.
GeneIDi112398.
KEGGihsa:112398.
UCSCiuc002opg.4. human. [Q96KS0-1]

Organism-specific databases

CTDi112398.
GeneCardsiGC19P041304.
HGNCiHGNC:14660. EGLN2.
MIMi606424. gene.
neXtProtiNX_Q96KS0.
PharmGKBiPA27671.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3751.
GeneTreeiENSGT00390000001936.
HOGENOMiHOG000013099.
HOVERGENiHBG051456.
InParanoidiQ96KS0.
KOiK09592.
OMAiEGGMSCG.
PhylomeDBiQ96KS0.
TreeFamiTF314595.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000171570-MONOMER.
BRENDAi1.14.11.2. 2681.
1.14.11.29. 2681.
ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.

Miscellaneous databases

ChiTaRSiEGLN2. human.
GeneWikiiEGLN2.
GenomeRNAii112398.
NextBioi78572.
PROiQ96KS0.
SOURCEiSearch...

Gene expression databases

BgeeiQ96KS0.
CleanExiHS_EGLN2.
ExpressionAtlasiQ96KS0. baseline.
GenevisibleiQ96KS0. HS.

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] (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. 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiEGLN2_HUMAN
AccessioniPrimary (citable) accession number: Q96KS0
Secondary accession number(s): A8K5S0, Q8WWY4, Q9BV14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 131 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.