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Q96KS0

- EGLN2_HUMAN

UniProt

Q96KS0 - EGLN2_HUMAN

Protein

Egl nine homolog 2

Gene

EGLN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 preferencially 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

    Binds 1 Fe2+ ion per subunit.
    Ascorbate.

    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

    1. ferrous iron binding Source: UniProtKB
    2. L-ascorbic acid binding Source: UniProtKB-KW
    3. 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 Source: UniProtKB
    4. oxygen sensor activity Source: UniProtKB
    5. peptidyl-proline 4-dioxygenase activity Source: FlyBase
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell redox homeostasis Source: UniProtKB
    2. cellular response to hypoxia Source: Reactome
    3. intracellular estrogen receptor signaling pathway Source: UniProtKB
    4. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: FlyBase
    5. positive regulation of protein catabolic process Source: UniProtKB
    6. regulation of cell growth Source: UniProtKB
    7. regulation of neuron apoptotic process Source: UniProtKB
    8. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    9. response to hypoxia Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000171570-MONOMER.
    BRENDAi1.14.11.2. 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: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:14660. EGLN2.

    Subcellular locationi

    Nucleus 4 Publications

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    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.

    PTM / Processingi

    Molecule processing

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

    Proteomic databases

    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.
    GenevestigatoriQ96KS0.

    Organism-specific databases

    HPAiHPA056649.

    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. 20 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
    Regioni89 – 13446Bipartite nuclear localization signalAdd
    BLAST
    Regioni225 – 23511Beta(2)beta(3) 'finger-like' loopAdd
    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.
    HOGENOMiHOG000013099.
    HOVERGENiHBG051456.
    InParanoidiQ96KS0.
    KOiK09592.
    OMAiGGELWPL.
    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. Align

    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

    MDSPCQPQPL SQALPQLPGS SSEPLEPEPG RARMGVESYL PCPLLPSYHC    50
    PGVPSEASAG SGTPRATATS TTASPLRDGF GGQDGGELRP LQSEGAAALV 100
    TKGCQRLAAQ GARPEAPKRK WAEDGGDAPS PSKRPWARQE NQEAEREGGM 150
    SCSCSSGSGE ASAGLMEEAL PSAPERLALD YIVPCMRYYG ICVKDSFLGA 200
    ALGGRVLAEV EALKRGGRLR DGQLVSQRAI PPRSIRGDQI AWVEGHEPGC 250
    RSIGALMAHV DAVIRHCAGR LGSYVINGRT KAMVACYPGN GLGYVRHVDN 300
    PHGDGRCITC IYYLNQNWDV KVHGGLLQIF PEGRPVVANI EPLFDRLLIF 350
    WSDRRNPHEV KPAYATRYAI TVWYFDAKER AAAKDKYQLA SGQKGVQVPV 400
    SQPPTPT 407
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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. [Q96KS0-1]
    ENST00000406058; ENSP00000385253; ENSG00000269858. [Q96KS0-1]
    ENST00000593726; ENSP00000469686; ENSG00000269858. [Q96KS0-1]
    ENST00000594140; ENSP00000472414; ENSG00000269858.
    GeneIDi112398.
    KEGGihsa:112398.
    UCSCiuc002opg.4. human. [Q96KS0-1]

    Polymorphism databases

    DMDMi32129513.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS12567.1. [Q96KS0-1 ]
    RefSeqi NP_444274.1. NM_053046.3. [Q96KS0-1 ]
    NP_542770.2. NM_080732.3. [Q96KS0-1 ]
    UniGenei Hs.515417.
    Hs.631539.
    Hs.730737.

    3D structure databases

    ProteinModelPortali Q96KS0.
    SMRi Q96KS0. Positions 176-387.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125184. 20 interactions.
    IntActi Q96KS0. 6 interactions.
    MINTi MINT-1186497.
    STRINGi 9606.ENSP00000307080.

    Chemistry

    BindingDBi Q96KS0.
    ChEMBLi CHEMBL3028.
    DrugBanki DB00126. Vitamin C.

    PTM databases

    PhosphoSitei Q96KS0.

    Polymorphism databases

    DMDMi 32129513.

    Proteomic databases

    PaxDbi Q96KS0.
    PRIDEi Q96KS0.

    Protocols and materials databases

    DNASUi 112398.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303961 ; ENSP00000307080 ; ENSG00000269858 . [Q96KS0-1 ]
    ENST00000406058 ; ENSP00000385253 ; ENSG00000269858 . [Q96KS0-1 ]
    ENST00000593726 ; ENSP00000469686 ; ENSG00000269858 . [Q96KS0-1 ]
    ENST00000594140 ; ENSP00000472414 ; ENSG00000269858 .
    GeneIDi 112398.
    KEGGi hsa:112398.
    UCSCi uc002opg.4. human. [Q96KS0-1 ]

    Organism-specific databases

    CTDi 112398.
    GeneCardsi GC19P041304.
    HGNCi HGNC:14660. EGLN2.
    HPAi HPA056649.
    MIMi 606424. gene.
    neXtProti NX_Q96KS0.
    PharmGKBi PA27671.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3751.
    HOGENOMi HOG000013099.
    HOVERGENi HBG051456.
    InParanoidi Q96KS0.
    KOi K09592.
    OMAi GGELWPL.
    PhylomeDBi Q96KS0.
    TreeFami TF314595.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000171570-MONOMER.
    BRENDAi 1.14.11.2. 2681.
    Reactomei REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.

    Miscellaneous databases

    ChiTaRSi EGLN2. human.
    GeneWikii EGLN2.
    GenomeRNAii 112398.
    NextBioi 78572.
    PROi Q96KS0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96KS0.
    CleanExi HS_EGLN2.
    Genevestigatori Q96KS0.

    Family and domain databases

    InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR006620. Pro_4_hyd_alph.
    [Graphical view ]
    Pfami PF13640. 2OG-FeII_Oxy_3. 1 hit.
    [Graphical view ]
    SMARTi SM00702. P4Hc. 1 hit.
    [Graphical view ]
    PROSITEi PS51471. FE2OG_OXY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 121 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