UniProtKB - Q9GZT9 (EGLN1_HUMAN)
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- BLAST>sp|Q9GZT9|EGLN1_HUMAN Egl nine homolog 1 OS=Homo sapiens OX=9606 GN=EGLN1 PE=1 SV=1 MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQG SEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADP AAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLR PNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQL VSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMV ACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKF DRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDS VGKDVF
- Align
Egl nine homolog 1
EGLN1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"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. - Ref.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. - Ref.10"Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor."
Ivan M., Haberberger T., Gervasi D.C., Michelson K.S., Guenzler V., Kondo K., Yang H., Sorokina I., Conaway R.C., Conaway J.W., Kaelin W.G. Jr.
Proc. Natl. Acad. Sci. U.S.A. 99:13459-13464(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.15"The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)."
Ozer A., Wu L.C., Bruick R.K.
Proc. Natl. Acad. Sci. U.S.A. 102:7481-7486(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ING4, FUNCTION. - Ref.19"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. - Ref.26"Prolyl hydroxylase-2 (PHD2) exerts tumor-suppressive activity in pancreatic cancer."
Su Y., Loos M., Giese N., Metzen E., Buchler M.W., Friess H., Kornberg A., Buchler P.
Cancer 118:960-972(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION. - Ref.39"A genetic mechanism for Tibetan high-altitude adaptation."
Lorenzo F.R., Huff C., Myllymaeki M., Olenchock B., Swierczek S., Tashi T., Gordeuk V., Wuren T., Ri-Li G., McClain D.A., Khan T.M., Koul P.A., Guchhait P., Salama M.E., Xing J., Semenza G.L., Liberzon E., Wilson A. , Simonson T.S., Jorde L.B., Kaelin W.G. Jr., Koivunen P., Prchal J.T.
Nat. Genet. 46:951-956(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-4 AND SER-127, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, POLYMORPHISM, CHARACTERIZATION OF VARIANTS GLU-4 AND SER-127.
Caution
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.39"A genetic mechanism for Tibetan high-altitude adaptation."
Lorenzo F.R., Huff C., Myllymaeki M., Olenchock B., Swierczek S., Tashi T., Gordeuk V., Wuren T., Ri-Li G., McClain D.A., Khan T.M., Koul P.A., Guchhait P., Salama M.E., Xing J., Semenza G.L., Liberzon E., Wilson A. , Simonson T.S., Jorde L.B., Kaelin W.G. Jr., Koivunen P., Prchal J.T.
Nat. Genet. 46:951-956(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-4 AND SER-127, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, POLYMORPHISM, CHARACTERIZATION OF VARIANTS GLU-4 AND SER-127.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Protein has several cofactor binding sites:- Fe2+PROSITE-ProRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
Combined sources<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.32"Cellular oxygen sensing: crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)."
McDonough M.A., Li V., Flashman E., Chowdhury R., Mohr C., Lienard B.M.R., Zondlo J., Oldham N.J., Clifton I.J., Lewis J., McNeill L.A., Kurzeja R.J., Hewitson K.S., Yang E., Jordan S., Syed R.S., Schofield C.J.
Proc. Natl. Acad. Sci. U.S.A. 103:9814-9819(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 181-417 IN COMPLEXES WITH IRON AND COMPETITIVE INHIBITOR, METAL-BINDING SITES, MUTAGENESIS OF TYR-303 AND ARG-383, SUBUNIT, COFACTOR. - Ref.33"Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases."
Chowdhury R., McDonough M.A., Mecinovic J., Loenarz C., Flashman E., Hewitson K.S., Domene C., Schofield C.J.
Structure 17:981-989(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 OF WILD TYPE AND MUTANTS ALA-252; ALA-254; LYS-254 AND ALA-398 IN COMPLEX WITH HIF1A, IRON, N-OXALYGLYCINE AND MANGANESE, METAL-BINDING SITES, COFACTOR. - Ref.35"1,2,4-Triazolo-[1,5-a]pyridine HIF Prolylhydroxylase Domain-1 (PHD-1) Inhibitors With a Novel Monodentate Binding Interaction."
Ahmed S., Ayscough A., Barker G.R., Canning H.E., Davenport R., Downham R., Harrison D., Jenkins K., Kinsella N., Livermore D.G., Wright S., Ivetac A.D., Skene R., Wilkens S.J., Webster N.A., Hendrick A.G.
J. Med. Chem. 60:5663-5672(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 181-416 IN COMPLEX WITH INHIBITOR AND IRON, COFACTOR.
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
Combined sources<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.32"Cellular oxygen sensing: crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)."
McDonough M.A., Li V., Flashman E., Chowdhury R., Mohr C., Lienard B.M.R., Zondlo J., Oldham N.J., Clifton I.J., Lewis J., McNeill L.A., Kurzeja R.J., Hewitson K.S., Yang E., Jordan S., Syed R.S., Schofield C.J.
Proc. Natl. Acad. Sci. U.S.A. 103:9814-9819(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 181-417 IN COMPLEXES WITH IRON AND COMPETITIVE INHIBITOR, METAL-BINDING SITES, MUTAGENESIS OF TYR-303 AND ARG-383, SUBUNIT, COFACTOR. - Ref.33"Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases."
Chowdhury R., McDonough M.A., Mecinovic J., Loenarz C., Flashman E., Hewitson K.S., Domene C., Schofield C.J.
Structure 17:981-989(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 OF WILD TYPE AND MUTANTS ALA-252; ALA-254; LYS-254 AND ALA-398 IN COMPLEX WITH HIF1A, IRON, N-OXALYGLYCINE AND MANGANESE, METAL-BINDING SITES, COFACTOR. - Ref.35"1,2,4-Triazolo-[1,5-a]pyridine HIF Prolylhydroxylase Domain-1 (PHD-1) Inhibitors With a Novel Monodentate Binding Interaction."
Ahmed S., Ayscough A., Barker G.R., Canning H.E., Davenport R., Downham R., Harrison D., Jenkins K., Kinsella N., Livermore D.G., Wright S., Ivetac A.D., Skene R., Wilkens S.J., Webster N.A., Hendrick A.G.
J. Med. Chem. 60:5663-5672(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 181-416 IN COMPLEX WITH INHIBITOR AND IRON, COFACTOR.
- L-ascorbate1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.33"Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases."
Chowdhury R., McDonough M.A., Mecinovic J., Loenarz C., Flashman E., Hewitson K.S., Domene C., Schofield C.J.
Structure 17:981-989(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 OF WILD TYPE AND MUTANTS ALA-252; ALA-254; LYS-254 AND ALA-398 IN COMPLEX WITH HIF1A, IRON, N-OXALYGLYCINE AND MANGANESE, METAL-BINDING SITES, COFACTOR.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"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. - Ref.21"Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen."
Flashman E., Hoffart L.M., Hamed R.B., Bollinger J.M. Jr., Krebs C., Schofield C.J.
FEBS J. 277:4089-4099(2010) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=70 nM for HIF2A1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.39"A genetic mechanism for Tibetan high-altitude adaptation."
Lorenzo F.R., Huff C., Myllymaeki M., Olenchock B., Swierczek S., Tashi T., Gordeuk V., Wuren T., Ri-Li G., McClain D.A., Khan T.M., Koul P.A., Guchhait P., Salama M.E., Xing J., Semenza G.L., Liberzon E., Wilson A. , Simonson T.S., Jorde L.B., Kaelin W.G. Jr., Koivunen P., Prchal J.T.
Nat. Genet. 46:951-956(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-4 AND SER-127, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, POLYMORPHISM, CHARACTERIZATION OF VARIANTS GLU-4 AND SER-127.
- KM=150 µM for O21 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.39"A genetic mechanism for Tibetan high-altitude adaptation."
Lorenzo F.R., Huff C., Myllymaeki M., Olenchock B., Swierczek S., Tashi T., Gordeuk V., Wuren T., Ri-Li G., McClain D.A., Khan T.M., Koul P.A., Guchhait P., Salama M.E., Xing J., Semenza G.L., Liberzon E., Wilson A. , Simonson T.S., Jorde L.B., Kaelin W.G. Jr., Koivunen P., Prchal J.T.
Nat. Genet. 46:951-956(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-4 AND SER-127, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, POLYMORPHISM, CHARACTERIZATION OF VARIANTS GLU-4 AND SER-127.
- KM=1.3 µM for 2-oxoglutarate1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.39"A genetic mechanism for Tibetan high-altitude adaptation."
Lorenzo F.R., Huff C., Myllymaeki M., Olenchock B., Swierczek S., Tashi T., Gordeuk V., Wuren T., Ri-Li G., McClain D.A., Khan T.M., Koul P.A., Guchhait P., Salama M.E., Xing J., Semenza G.L., Liberzon E., Wilson A. , Simonson T.S., Jorde L.B., Kaelin W.G. Jr., Koivunen P., Prchal J.T.
Nat. Genet. 46:951-956(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-4 AND SER-127, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, POLYMORPHISM, CHARACTERIZATION OF VARIANTS GLU-4 AND SER-127.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 313 | IronCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 315 | IronCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 374 | IronCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 383 | 2-oxoglutarate1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 21 – 58 | MYND-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 38 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- enzyme binding Source: BHF-UCL
- ferrous iron binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- L-ascorbic acid binding Source: UniProtKB-KW
- 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: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- peptidyl-proline 4-dioxygenase activity Source: FlyBase <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- peptidyl-proline dioxygenase activity Source: HGNC <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cardiac muscle tissue morphogenesis Source: Ensembl
- cellular iron ion homeostasis Source: Ensembl
- heart trabecula formation Source: Ensembl
- labyrinthine layer development Source: Ensembl
- negative regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
- negative regulation of DNA binding transcription factor activity Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- oxygen homeostasis Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: FlyBase <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of transcription by RNA polymerase II Source: Ensembl
- regulation of angiogenesis Source: UniProtKB
- regulation of neuron death Source: Ensembl
- regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
- response to hypoxia Source: HGNC <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to nitric oxide Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ventricular septum morphogenesis Source: Ensembl
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Dioxygenase, Oxidoreductase |
| Ligand | Iron, Metal-binding, Vitamin C, Zinc |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.14.11.2 2681 1.14.11.29 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Egl nine homolog 1 (EC:1.14.11.291 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Alternative name(s): Hypoxia-inducible factor prolyl hydroxylase 2 Short name: HIF-PH2 Short name: HIF-prolyl hydroxylase 2 Short name: HPH-2 Prolyl hydroxylase domain-containing protein 2 Short name: PHD2 SM-20 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:EGLN1Imported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Synonyms:C1orf12 ORF Names:PNAS-118, PNAS-137 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000135766.8 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1232 EGLN1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606425 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9GZT9 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.18"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. - Ref.19"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.
- Nucleus 3 Publications
Other locations
- Cytoplasm 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.18"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. - Ref.19"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.
Note: Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm (PubMed:19631610). Nuclear export requires functional XPO1.2 Publications- Cytoplasm 3 Publications
- Ref.18"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. - Ref.19"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.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytosol
- cytosol Source: HPA
Nucleus
- nucleus Source: UniProtKB-SubCell
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Erythrocytosis, familial, 3 (ECYT3)2 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.36"A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis."
Percy M.J., Zhao Q., Flores A., Harrison C., Lappin T.R., Maxwell P.H., McMullin M.F., Lee F.S.
Proc. Natl. Acad. Sci. U.S.A. 103:654-659(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ECYT3 ARG-317, CHARACTERIZATION OF VARIANT ECYT3 ARG-317. - Ref.37"A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove."
Percy M.J., Furlow P.W., Beer P.A., Lappin T.R.J., McMullin M.F., Lee F.S.
Blood 110:2193-2196(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ECYT3 HIS-371, CHARACTERIZATION OF VARIANT EXCYT3 HIS-371.
Percy M.J., Zhao Q., Flores A., Harrison C., Lappin T.R., Maxwell P.H., McMullin M.F., Lee F.S.
Proc. Natl. Acad. Sci. U.S.A. 103:654-659(2006) [PubMed] [Europe PMC] [Abstract]
Percy M.J., Furlow P.W., Beer P.A., Lappin T.R.J., McMullin M.F., Lee F.S.
Blood 110:2193-2196(2007) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_027371 | 317 | P → R in ECYT3; marked decrease in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_045902 | 371 | R → H in ECYT3; decreased interaction with HIF1A and EPAS1 and decreased enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 201 | C → A: Little change in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 208 | C → A: Little change in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 252 | R → A: Reduced C-terminal ODD domain (CODD) hydroxylation of HIF1A. | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 254 | D → A or K: Reduced C-terminal ODD domain (CODD) hxdroxylation of HIF1A. | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 266 | C → A: Little change in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 283 | C → A: Little change in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 302 | C → A: Slight increase in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 303 | Y → F: No effect. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 323 | C → A: Little change in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 326 | C → A: Slight increase in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 383 | R → A: Reduces enzyme activity by 95%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Congenital erythrocytosis, Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 54583 |
MalaCards human disease database More...MalaCardsi | EGLN1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 609820 phenotype |
Open Targets More...OpenTargetsi | ENSG00000135766 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 247511 Autosomal dominant secondary polycythemia |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27670 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5697 |
Drug and drug target database More...DrugBanki | DB04847 FG-4592 DB08687 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE DB07112 N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE DB00126 Vitamin C |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2833 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | EGLN1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 32129514 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000206661 | 2 – 426 | Egl nine homolog 1Add BLAST | 425 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 12 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 125 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 201 | S-nitrosocysteine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 208 | S-nitrosocysteine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 302 | S-nitrosocysteine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 323 | S-nitrosocysteine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 326 | S-nitrosocysteine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.34"Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1)."
Chowdhury R., Flashman E., Mecinovic J., Kramer H.B., Kessler B.M., Frapart Y.M., Boucher J.L., Clifton I.J., McDonough M.A., Schofield C.J.
J. Mol. Biol. 410:268-279(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 IN COMPLEX WITH NITRIC OXIDE OR A NITRIC OXIDE TRANSFER REAGENT, IDENTIFICATION BY MASS SPECTROMETRY, S-NITROSYLATION AT CYS-201; CYS-208; CYS-302; CYS-323 AND CYS-326, MUTAGENESIS OF CYS-201; CYS-208; CYS-266; CYS-283; CYS-302; CYS-323 AND CYS-326.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Phosphoprotein, S-nitrosylationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9GZT9 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9GZT9 |
PeptideAtlas More...PeptideAtlasi | Q9GZT9 |
PRoteomics IDEntifications database More...PRIDEi | Q9GZT9 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 80138 80139 [Q9GZT9-2] 80140 [Q9GZT9-3] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9GZT9 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9GZT9 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Mapping, characterization, and expression analysis of the SM-20 human homologue, C1orf12, and identification of a novel related gene, SCAND2."
Dupuy D., Aubert I., Duperat V.G., Petit J., Taine L., Stef M., Bloch B., Arveiler B.
Genomics 69:348-354(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY. - Ref.3"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] (ISOFORM 3), TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY. - Ref.10"Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor."
Ivan M., Haberberger T., Gervasi D.C., Michelson K.S., Guenzler V., Kondo K., Yang H., Sorokina I., Conaway R.C., Conaway J.W., Kaelin W.G. Jr.
Proc. Natl. Acad. Sci. U.S.A. 99:13459-13464(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.11"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: TISSUE SPECIFICITY. - Ref.12"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.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000135766 |
CleanEx database of gene expression profiles More...CleanExi | HS_EGLN1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9GZT9 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9GZT9 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA022129 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)."
Ozer A., Wu L.C., Bruick R.K.
Proc. Natl. Acad. Sci. U.S.A. 102:7481-7486(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ING4, FUNCTION. - Ref.20"Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical role for residues C-terminal to the hydroxylacceptor proline."
Furlow P.W., Percy M.J., Sutherland S., Bierl C., McMullin M.F., Master S.R., Lappin T.R., Lee F.S.
J. Biol. Chem. 284:9050-9058(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EPAS1. - Ref.27"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, IDENTIFICATION IN A COMPLEX WITH LIMD1; VHL; ELOB AND CUL2. - Ref.30"SIRT2 regulates tumour hypoxia response by promoting HIF-1alpha hydroxylation."
Seo K.S., Park J.H., Heo J.Y., Jing K., Han J., Min K.N., Kim C., Koh G.Y., Lim K., Kang G.Y., Uee Lee J., Yim Y.H., Shong M., Kwak T.H., Kweon G.R.
Oncogene 34:1354-1362(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HIF1A. - Ref.31"Myeloid translocation gene-16 co-repressor promotes degradation of hypoxia-inducible factor 1."
Kumar P., Gullberg U., Olsson I., Ajore R.
PLoS ONE 10:E0123725-E0123725(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CBFA2T3 AND HIF1A. - Ref.32"Cellular oxygen sensing: crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)."
McDonough M.A., Li V., Flashman E., Chowdhury R., Mohr C., Lienard B.M.R., Zondlo J., Oldham N.J., Clifton I.J., Lewis J., McNeill L.A., Kurzeja R.J., Hewitson K.S., Yang E., Jordan S., Syed R.S., Schofield C.J.
Proc. Natl. Acad. Sci. U.S.A. 103:9814-9819(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 181-417 IN COMPLEXES WITH IRON AND COMPETITIVE INHIBITOR, METAL-BINDING SITES, MUTAGENESIS OF TYR-303 AND ARG-383, SUBUNIT, COFACTOR. - Ref.33"Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases."
Chowdhury R., McDonough M.A., Mecinovic J., Loenarz C., Flashman E., Hewitson K.S., Domene C., Schofield C.J.
Structure 17:981-989(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 OF WILD TYPE AND MUTANTS ALA-252; ALA-254; LYS-254 AND ALA-398 IN COMPLEX WITH HIF1A, IRON, N-OXALYGLYCINE AND MANGANESE, METAL-BINDING SITES, COFACTOR. - Ref.34"Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1)."
Chowdhury R., Flashman E., Mecinovic J., Kramer H.B., Kessler B.M., Frapart Y.M., Boucher J.L., Clifton I.J., McDonough M.A., Schofield C.J.
J. Mol. Biol. 410:268-279(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 181-426 IN COMPLEX WITH NITRIC OXIDE OR A NITRIC OXIDE TRANSFER REAGENT, IDENTIFICATION BY MASS SPECTROMETRY, S-NITROSYLATION AT CYS-201; CYS-208; CYS-302; CYS-323 AND CYS-326, MUTAGENESIS OF CYS-201; CYS-208; CYS-266; CYS-283; CYS-302; CYS-323 AND CYS-326.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Q9WMX2 | 3 | EBI-1174818,EBI-6863748 | From Hepatitis C virus genotype 1b (isolate Con1). | |
| EPAS1 | Q99814 | 2 | EBI-1174818,EBI-447470 | |
| FKBP8 | Q14318 | 6 | EBI-1174818,EBI-724839 | |
| HIF1A | Q16665 | 5 | EBI-1174818,EBI-447269 | |
| OS9 | Q13438 | 4 | EBI-1174818,EBI-725454 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- enzyme binding Source: BHF-UCL
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 120060, 39 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9GZT9 |
Database of interacting proteins More...DIPi | DIP-37495N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q9GZT9 |
Protein interaction database and analysis system More...IntActi | Q9GZT9, 16 interactors |
Molecular INTeraction database More...MINTi | Q9GZT9 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000355601 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q9GZT9 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 190 – 196 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 198 – 205 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 206 – 214 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 216 – 231 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 240 – 242 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 247 – 249 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 255 – 259 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 267 – 283 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 284 – 286 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 287 – 289 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 292 – 295 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 298 – 303 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 305 – 313 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 315 – 318 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 321 – 329 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 331 – 333 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 336 – 339 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 343 – 345 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 348 – 351 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 354 – 356 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 362 – 367 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 374 – 381 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 383 – 392 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 393 – 402 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 407 – 409 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9GZT9 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9GZT9 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9GZT9 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 291 – 392 | Fe2OG dioxygenasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 102 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 6 – 20 | Required for nuclear exportAdd BLAST | 15 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 241 – 251 | Beta(2)beta(3) 'finger-like' loop1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 11 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases."
Flashman E., Bagg E.A., Chowdhury R., Mecinovic J., Loenarz C., McDonough M.A., Hewitson K.S., Schofield C.J.
J. Biol. Chem. 283:3808-3815(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBSTRATE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 237-ASP--ILE-251, DOMAIN.
Zinc finger
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 21 – 58 | MYND-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 38 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Zinc-fingerPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3710 Eukaryota ENOG410ZHZN LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000001936 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000004818 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG051455 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9GZT9 |
KEGG Orthology (KO) More...KOi | K09592 |
Identification of Orthologs from Complete Genome Data More...OMAi | KANLYPP |
Database of Orthologous Groups More...OrthoDBi | EOG091G03SP |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9GZT9 |
TreeFam database of animal gene trees More...TreeFami | TF314595 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005123 Oxoglu/Fe-dep_dioxygenase IPR006620 Pro_4_hyd_alph IPR002893 Znf_MYND |
Pfam protein domain database More...Pfami | View protein in Pfam PF13640 2OG-FeII_Oxy_3, 1 hit PF01753 zf-MYND, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00702 P4Hc, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51471 FE2OG_OXY, 1 hit PS01360 ZF_MYND_1, 1 hit PS50865 ZF_MYND_2, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
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.
10 20 30 40 50
MANDSGGPGG PSPSERDRQY CELCGKMENL LRCSRCRSSF YCCKEHQRQD
60 70 80 90 100
WKKHKLVCQG SEGALGHGVG PHQHSGPAPP AAVPPPRAGA REPRKAAARR
110 120 130 140 150
DNASGDAAKG KVKAKPPADP AAAASPCRAA AGGQGSAVAA EAEPGKEEPP
160 170 180 190 200
ARSSLFQEKA NLYPPSNTPG DALSPGGGLR PNGQTKPLPA LKLALEYIVP
210 220 230 240 250
CMNKHGICVV DDFLGKETGQ QIGDEVRALH DTGKFTDGQL VSQKSDSSKD
260 270 280 290 300
IRGDKITWIE GKEPGCETIG LLMSSMDDLI RHCNGKLGSY KINGRTKAMV
310 320 330 340 350
ACYPGNGTGY VRHVDNPNGD GRCVTCIYYL NKDWDAKVSG GILRIFPEGK
360 370 380 390 400
AQFADIEPKF DRLLFFWSDR RNPHEVQPAY ATRYAITVWY FDADERARAK
410 420
VKYLTGEKGV RVELNKPSDS VGKDVF
The sequence of this isoform differs from the canonical sequence as follows:
338-359: Missing.
10 20 30 40 50
MANDSGGPGG PSPSERDRQY CELCGKMENL LRCSRCRSSF YCCKEHQRQD
60 70 80 90 100
WKKHKLVCQG SEGALGHGVG PHQHSGPAPP AAVPPPRAGA REPRKAAARR
110 120 130 140 150
DNASGDAAKG KVKAKPPADP AAAASPCRAA AGGQGSAVAA EAEPGKEEPP
160 170 180 190 200
ARSSLFQEKA NLYPPSNTPG DALSPGGGLR PNGQTKPLPA LKLALEYIVP
210 220 230 240 250
CMNKHGICVV DDFLGKETGQ QIGDEVRALH DTGKFTDGQL VSQKSDSSKD
260 270 280 290 300
IRGDKITWIE GKEPGCETIG LLMSSMDDLI RHCNGKLGSY KINGRTKAMV
310 320 330 340 350
ACYPGNGTGY VRHVDNPNGD GRCVTCIYYL NKDWDAKFDR LLFFWSDRRN
360 370 380 390 400
PHEVQPAYAT RYAITVWYFD ADERARAKVK YLTGEKGVRV ELNKPSDSVG
KDVF
The sequence of this isoform differs from the canonical sequence as follows:
58-175: CQGSEGALGH...SNTPGDALSP → LLGGYRFAFSWNSDERA
10 20 30 40 50
MANDSGGPGG PSPSERDRQY CELCGKMENL LRCSRCRSSF YCCKEHQRQD
60 70 80 90 100
WKKHKLVLLG GYRFAFSWNS DERAGGGLRP NGQTKPLPAL KLALEYIVPC
110 120 130 140 150
MNKHGICVVD DFLGKETGQQ IGDEVRALHD TGKFTDGQLV SQKSDSSKDI
160 170 180 190 200
RGDKITWIEG KEPGCETIGL LMSSMDDLIR HCNGKLGSYK INGRTKAMVA
210 220 230 240 250
CYPGNGTGYV RHVDNPNGDG RCVTCIYYLN KDWDAKVSGG ILRIFPEGKA
260 270 280 290 300
QFADIEPKFD RLLFFWSDRR NPHEVQPAYA TRYAITVWYF DADERARAKV
310 320
KYLTGEKGVR VELNKPSDSV GKDVF
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Identifying signatures of natural selection in Tibetan and Andean populations using dense genome scan data."
Bigham A., Bauchet M., Pinto D., Mao X., Akey J.M., Mei R., Scherer S.W., Julian C.G., Wilson M.J., Lopez Herraez D., Brutsaert T., Parra E.J., Moore L.G., Shriver M.D.
PLoS Genet. 6:E1001116-E1001116(2010) [PubMed] [Europe PMC] [Abstract]Cited for: POLYMORPHISM. - Ref.24"Genetic evidence for high-altitude adaptation in Tibet."
Simonson T.S., Yang Y., Huff C.D., Yun H., Qin G., Witherspoon D.J., Bai Z., Lorenzo F.R., Xing J., Jorde L.B., Prchal J.T., Ge R.
Science 329:72-75(2010) [PubMed] [Europe PMC] [Abstract]Cited for: POLYMORPHISM. - Ref.38"Defective Tibetan PHD2 binding to p23 links high altitude adaption to altered oxygen sensing."
Song D., Li L.S., Arsenault P.R., Tan Q., Bigham A.W., Heaton-Johnson K.J., Master S.R., Lee F.S.
J. Biol. Chem. 289:14656-14665(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-4 AND SER-127, POLYMORPHISM, INTERACTION WITH PTGES3, CHARACTERIZATION OF VARIANTS GLU-4 AND SER-127. - Ref.39"A genetic mechanism for Tibetan high-altitude adaptation."
Lorenzo F.R., Huff C., Myllymaeki M., Olenchock B., Swierczek S., Tashi T., Gordeuk V., Wuren T., Ri-Li G., McClain D.A., Khan T.M., Koul P.A., Guchhait P., Salama M.E., Xing J., Semenza G.L., Liberzon E., Wilson A. , Simonson T.S., Jorde L.B., Kaelin W.G. Jr., Koivunen P., Prchal J.T.
Nat. Genet. 46:951-956(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLU-4 AND SER-127, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, POLYMORPHISM, CHARACTERIZATION OF VARIANTS GLU-4 AND SER-127.
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071858 | 4 | D → E Polymorphism present in the majority of Tibetans; increased protection from polycythemia at high altitude; when associated with S-127. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071859 | 127 | C → S Polymorphism present in the majority of Tibetans; increased protection from polycythemia at high altitude; when associated with E-4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_027371 | 317 | P → R in ECYT3; marked decrease in enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_045902 | 371 | R → H in ECYT3; decreased interaction with HIF1A and EPAS1 and decreased enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_042191 | 58 – 175 | CQGSE…DALSP → LLGGYRFAFSWNSDERA in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 118 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007569 | 338 – 359 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 22 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF246631, AF246630 Genomic DNA Translation: AAG34568.1 AF229245 mRNA Translation: AAG33965.1 AJ310543 mRNA Translation: CAC42509.1 AL833885 mRNA Translation: CAD38741.2 AF277174 mRNA Translation: AAK07534.1 Different initiation. AF277176 mRNA Translation: AAK07536.1 Frameshift. AL117352 Genomic DNA No translation available. AL445524 Genomic DNA No translation available. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1595.1 [Q9GZT9-1] |
NCBI Reference Sequences More...RefSeqi | NP_071334.1, NM_022051.2 [Q9GZT9-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.444450 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000366641; ENSP00000355601; ENSG00000135766 [Q9GZT9-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 54583 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:54583 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9GZT9 | Egl nine homolog 1 (C. elegans) | 426 | |||
| UPI0000E062A8 | 383 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9GZT9 | Egl nine homolog 1 (C. elegans) | 426 | |||
| UPI00057BBB8C | 518 | ||||
| egl nine homolog 1 isoform X1 | 440 | ||||
| UPI000D1F1182 | 225 | ||||
| UPI000C2FD7BD | 439 | ||||
| +63 | |||||
| Q9GZT9-3 | UPI000C8117B4 | 265 | |||
| Egl nine-like protein 1 (Fragment) | 260 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9GZT9 | Egl nine homolog 1 (C. elegans) | 426 | |||
| UPI00057BBB8C | 518 | ||||
| egl nine homolog 1 isoform X1 | 440 | ||||
| UPI000D1F1182 | 225 | ||||
| UPI000C2FD7BD | 439 | ||||
| +123 | |||||
| Q9GZT9-2 | UPI000B7B4E4B | 345 | |||
| UPI000D0A081D | 338 | ||||
| UPI0004422CF3 | 400 | ||||
| UPI0002BCD9AC | 395 | ||||
| UPI000CD5E11B | 370 | ||||
| +66 | |||||
| Q9GZT9-3 | UPI000C8117B4 | 265 | |||
| Egl nine-like protein 1 (Fragment) | 260 | ||||
| UPI0007B9DB21 | 313 | ||||
| egl nine homolog 1-like isoform X2 | 288 | ||||
| UPI0009E4933B | 317 | ||||
| +50 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF246631, AF246630 Genomic DNA Translation: AAG34568.1 AF229245 mRNA Translation: AAG33965.1 AJ310543 mRNA Translation: CAC42509.1 AL833885 mRNA Translation: CAD38741.2 AF277174 mRNA Translation: AAK07534.1 Different initiation. AF277176 mRNA Translation: AAK07536.1 Frameshift. AL117352 Genomic DNA No translation available. AL445524 Genomic DNA No translation available. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1595.1 [Q9GZT9-1] |
NCBI Reference Sequences More...RefSeqi | NP_071334.1, NM_022051.2 [Q9GZT9-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.444450 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2G19 | X-ray | 1.70 | A | 181-417 | [»] | |
| 2G1M | X-ray | 2.20 | A | 181-426 | [»] | |
| 2HBT | X-ray | 1.60 | A | 188-426 | [»] | |
| 2HBU | X-ray | 1.85 | A | 188-426 | [»] | |
| 2Y33 | X-ray | 2.00 | A | 181-426 | [»] | |
| 2Y34 | X-ray | 2.01 | A | 181-426 | [»] | |
| 3HQR | X-ray | 2.00 | A | 181-426 | [»] | |
| 3HQU | X-ray | 2.30 | A | 181-426 | [»] | |
| 3OUH | X-ray | 2.51 | A | 181-416 | [»] | |
| 3OUI | X-ray | 1.70 | A | 181-392 | [»] | |
| 3OUJ | X-ray | 2.30 | A | 181-416 | [»] | |
| 4BQW | X-ray | 1.79 | A | 181-426 | [»] | |
| 4BQX | X-ray | 1.79 | A | 181-426 | [»] | |
| 4BQY | X-ray | 1.53 | A | 181-426 | [»] | |
| 4JZR | X-ray | 2.10 | A | 189-399 | [»] | |
| 4KBZ | X-ray | 2.15 | A | 184-419 | [»] | |
| 4UWD | X-ray | 1.72 | A | 181-426 | [»] | |
| 5A3U | X-ray | 3.30 | A/B/C | 181-426 | [»] | |
| 5L9B | X-ray | 1.95 | A/B | 181-426 | [»] | |
| 5L9R | X-ray | 1.81 | A | 181-426 | [»] | |
| 5L9V | X-ray | 1.83 | A/B | 181-426 | [»] | |
| 5LA9 | X-ray | 2.81 | A/B | 181-426 | [»] | |
| 5LAS | X-ray | 2.10 | A/B | 181-426 | [»] | |
| 5LAT | X-ray | 1.90 | A | 181-426 | [»] | |
| 5LB6 | X-ray | 1.70 | A | 181-426 | [»] | |
| 5LBB | X-ray | 1.70 | A | 181-426 | [»] | |
| 5LBC | X-ray | 1.82 | A | 181-426 | [»] | |
| 5LBE | X-ray | 1.75 | A | 181-426 | [»] | |
| 5LBF | X-ray | 1.90 | A | 181-426 | [»] | |
| 5OX5 | X-ray | 2.25 | A | 181-426 | [»] | |
| 5OX6 | X-ray | 1.99 | A | 181-426 | [»] | |
| 5V18 | X-ray | 2.15 | A | 181-416 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9GZT9 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9GZT9 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 120060, 39 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9GZT9 |
Database of interacting proteins More...DIPi | DIP-37495N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q9GZT9 |
Protein interaction database and analysis system More...IntActi | Q9GZT9, 16 interactors |
Molecular INTeraction database More...MINTi | Q9GZT9 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000355601 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q9GZT9 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5697 |
Drug and drug target database More...DrugBanki | DB04847 FG-4592 DB08687 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE DB07112 N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE DB00126 Vitamin C |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2833 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9GZT9 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9GZT9 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | EGLN1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 32129514 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9GZT9 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9GZT9 |
PeptideAtlas More...PeptideAtlasi | Q9GZT9 |
PRoteomics IDEntifications database More...PRIDEi | Q9GZT9 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 80138 80139 [Q9GZT9-2] 80140 [Q9GZT9-3] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000366641; ENSP00000355601; ENSG00000135766 [Q9GZT9-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 54583 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:54583 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 54583 |
DisGeNET More...DisGeNETi | 54583 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000135766.8 |
GeneCards: human genes, protein and diseases More...GeneCardsi | EGLN1 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0159985 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1232 EGLN1 |
Human Protein Atlas More...HPAi | HPA022129 |
MalaCards human disease database More...MalaCardsi | EGLN1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606425 gene 609820 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9GZT9 |
Open Targets More...OpenTargetsi | ENSG00000135766 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 247511 Autosomal dominant secondary polycythemia |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27670 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3710 Eukaryota ENOG410ZHZN LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000001936 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000004818 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG051455 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9GZT9 |
KEGG Orthology (KO) More...KOi | K09592 |
Identification of Orthologs from Complete Genome Data More...OMAi | KANLYPP |
Database of Orthologous Groups More...OrthoDBi | EOG091G03SP |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9GZT9 |
TreeFam database of animal gene trees More...TreeFami | TF314595 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.14.11.2 2681 1.14.11.29 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | EGLN1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9GZT9 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | EGLN1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 54583 |
Protein Ontology More...PROi | PR:Q9GZT9 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000135766 |
CleanEx database of gene expression profiles More...CleanExi | HS_EGLN1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9GZT9 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9GZT9 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005123 Oxoglu/Fe-dep_dioxygenase IPR006620 Pro_4_hyd_alph IPR002893 Znf_MYND |
Pfam protein domain database More...Pfami | View protein in Pfam PF13640 2OG-FeII_Oxy_3, 1 hit PF01753 zf-MYND, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00702 P4Hc, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51471 FE2OG_OXY, 1 hit PS01360 ZF_MYND_1, 1 hit PS50865 ZF_MYND_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | EGLN1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9GZT9Primary (citable) accession number: Q9GZT9 Secondary accession number(s): Q8N3M8, Q9BZS8, Q9BZT0 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 16, 2003 |
| Last sequence update: | March 1, 2001 | |
| Last modified: | July 18, 2018 | |
| This is version 173 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
