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UniProtKB - Q8N465 (D2HDH_HUMAN)
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>sp|Q8N465|D2HDH_HUMAN D-2-hydroxyglutarate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=D2HGDH PE=1 SV=3 MLPRRPLAWPAWLLRGAPGAAGSWGRPVGPLARRGCCSAPGTPEVPLTRERYPVRRLPFS TVSKQDLAAFERIVPGGVVTDPEALQAPNVDWLRTLRGCSKVLLRPRTSEEVSHILRHCH ERNLAVNPQGGNTGMVGGSVPVFDEIILSTARMNRVLSFHSVSGILVCQAGCVLEELSRY VEERDFIMPLDLGAKGSCHIGGNVATNAGGLRFLRYGSLHGTVLGLEVVLADGTVLDCLT SLRKDNTGYDLKQLFIGSEGTLGIITTVSILCPPKPRAVNVAFLGCPGFAEVLQTFSTCK GMLGEILSAFEFMDAVCMQLVGRHLHLASPVQESPFYVLIETSGSNAGHDAEKLGHFLEH ALGSGLVTDGTMATDQRKVKMLWALRERITEALSRDGYVYKYDLSLPVERLYDIVTDLRA RLGPHAKHVVGYGHLGDGNLHLNVTAEAFSPSLLAALEPHVYEWTAGQQGSVSAEHGVGF RKRDVLGYSKPPGALQLMQQLKALLDPKGILNPYKTLPSQACommunity curation ()Add a publicationFeedback
Protein
D-2-hydroxyglutarate dehydrogenase, mitochondrial
Gene
D2HGDH
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
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
Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HG) to alpha-ketoglutarate (PubMed:15070399, PubMed:15609246, PubMed:16037974, PubMed:20020533, PubMed:33431826).
Also catalyzes the oxidation of other D-2-hydroxyacids, such as D-malate (D-MAL) and D-lactate (D-LAC) (PubMed:33431826).
Exhibits high activities towards D-2-HG and D-MAL but a very weak activity towards D-LAC (PubMed:33431826).
5 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.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY. - Ref.5"Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria."
Struys E.A., Salomons G.S., Achouri Y., van Schaftingen E., Grosso S., Craigen W.J., Verhoeven N.M., Jakobs C.
Am. J. Hum. Genet. 76:358-360(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 SER-147 AND ALA-444, CHARACTERIZATION OF VARIANTS D2HGA1 SER-147 AND ALA-444, FUNCTION, CATALYTIC ACTIVITY. - Ref.6"Mutations in phenotypically mild D-2-hydroxyglutaric aciduria."
Struys E.A., Korman S.H., Salomons G.S., Darmin P.S., Achouri Y., van Schaftingen E., Verhoeven N.M., Jakobs C.
Ann. Neurol. 58:626-630(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT D2HGA1 ASP-439, CHARACTERIZATION OF VARIANT D2HGA1 ASP-439, FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Evidence for genetic heterogeneity in D-2-hydroxyglutaric aciduria."
Kranendijk M., Struys E.A., Gibson K.M., Wickenhagen W.V., Abdenur J.E., Buechner J., Christensen E., de Kremer R.D., Errami A., Gissen P., Gradowska W., Hobson E., Islam L., Korman S.H., Kurczynski T., Maranda B., Meli C., Rizzo C. , Sansaricq C., Trefz F.K., Webster R., Jakobs C., Salomons G.S.
Hum. Mutat. 31:279-283(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; 169-GLN--ALA-521 DEL; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; 400-TYR--ALA-521 DEL; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; VAL-153; TYR-172; 400-TYR--ALA-521 DEL; HIS-419 AND THR-426, FUNCTION, CATALYTIC ACTIVITY. - Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- (R)-2-hydroxyglutarateEC:1.1.99.39
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<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
- Ref.8"D-2-Hydroxyglutaric aciduria in three patients with proven SSADH deficiency: genetic coincidence or a related biochemical epiphenomenon?"
Struys E.A., Verhoeven N.M., Salomons G.S., Berthelot J., Vianay-Saban C., Chabrier S., Thomas J.A., Tsai A.C.-H., Gibson K.M., Jakobs C.
Mol. Genet. Metab. 88:53-57(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLY-15 AND VAL-436, CATALYTIC ACTIVITY.
Manual assertion based on experiment ini
- Ref.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY. - Ref.5"Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria."
Struys E.A., Salomons G.S., Achouri Y., van Schaftingen E., Grosso S., Craigen W.J., Verhoeven N.M., Jakobs C.
Am. J. Hum. Genet. 76:358-360(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 SER-147 AND ALA-444, CHARACTERIZATION OF VARIANTS D2HGA1 SER-147 AND ALA-444, FUNCTION, CATALYTIC ACTIVITY. - Ref.6"Mutations in phenotypically mild D-2-hydroxyglutaric aciduria."
Struys E.A., Korman S.H., Salomons G.S., Darmin P.S., Achouri Y., van Schaftingen E., Verhoeven N.M., Jakobs C.
Ann. Neurol. 58:626-630(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT D2HGA1 ASP-439, CHARACTERIZATION OF VARIANT D2HGA1 ASP-439, FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Evidence for genetic heterogeneity in D-2-hydroxyglutaric aciduria."
Kranendijk M., Struys E.A., Gibson K.M., Wickenhagen W.V., Abdenur J.E., Buechner J., Christensen E., de Kremer R.D., Errami A., Gissen P., Gradowska W., Hobson E., Islam L., Korman S.H., Kurczynski T., Maranda B., Meli C., Rizzo C. , Sansaricq C., Trefz F.K., Webster R., Jakobs C., Salomons G.S.
Hum. Mutat. 31:279-283(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; 169-GLN--ALA-521 DEL; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; 400-TYR--ALA-521 DEL; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; VAL-153; TYR-172; 400-TYR--ALA-521 DEL; HIS-419 AND THR-426, FUNCTION, CATALYTIC ACTIVITY. - Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
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Manual assertion inferred by curator fromi
- Ref.8"D-2-Hydroxyglutaric aciduria in three patients with proven SSADH deficiency: genetic coincidence or a related biochemical epiphenomenon?"
Struys E.A., Verhoeven N.M., Salomons G.S., Berthelot J., Vianay-Saban C., Chabrier S., Thomas J.A., Tsai A.C.-H., Gibson K.M., Jakobs C.
Mol. Genet. Metab. 88:53-57(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS GLY-15 AND VAL-436, CATALYTIC ACTIVITY.
Manual assertion based on experiment ini
- Ref.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY. - Ref.5"Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria."
Struys E.A., Salomons G.S., Achouri Y., van Schaftingen E., Grosso S., Craigen W.J., Verhoeven N.M., Jakobs C.
Am. J. Hum. Genet. 76:358-360(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 SER-147 AND ALA-444, CHARACTERIZATION OF VARIANTS D2HGA1 SER-147 AND ALA-444, FUNCTION, CATALYTIC ACTIVITY. - Ref.6"Mutations in phenotypically mild D-2-hydroxyglutaric aciduria."
Struys E.A., Korman S.H., Salomons G.S., Darmin P.S., Achouri Y., van Schaftingen E., Verhoeven N.M., Jakobs C.
Ann. Neurol. 58:626-630(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT D2HGA1 ASP-439, CHARACTERIZATION OF VARIANT D2HGA1 ASP-439, FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Evidence for genetic heterogeneity in D-2-hydroxyglutaric aciduria."
Kranendijk M., Struys E.A., Gibson K.M., Wickenhagen W.V., Abdenur J.E., Buechner J., Christensen E., de Kremer R.D., Errami A., Gissen P., Gradowska W., Hobson E., Islam L., Korman S.H., Kurczynski T., Maranda B., Meli C., Rizzo C. , Sansaricq C., Trefz F.K., Webster R., Jakobs C., Salomons G.S.
Hum. Mutat. 31:279-283(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; 169-GLN--ALA-521 DEL; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; 400-TYR--ALA-521 DEL; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; VAL-153; TYR-172; 400-TYR--ALA-521 DEL; HIS-419 AND THR-426, FUNCTION, CATALYTIC ACTIVITY. - Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
Source: Rhea- Search for this reaction in UniProtKB.
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(R)-2-hydroxyglutarate- Search proteins in UniProtKB for this molecule.
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+A- Search proteins in UniProtKB for this molecule.
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=2-oxoglutarate- Search proteins in UniProtKB for this molecule.
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+AH2- Search proteins in UniProtKB for this molecule.
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- (R)-malate
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Manual assertion based on experiment ini
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
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(R)-malate- Search proteins in UniProtKB for this molecule.
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+oxaloacetate- Search proteins in UniProtKB for this molecule.
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<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
FAD
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<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Activated by zinc and cobalt ions.1 Publication
Manual assertion based on experiment ini
- Ref.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
<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=0.12 mM for D-2-hydroxyglutarate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
- KM=0.17 mM for D-malate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
- KM=0.15 mM for D-lactate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
- Vmax=2.29 µmol/min/mg enzyme towards D-2-hydroxyglutarate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
- Vmax=2.96 µmol/min/mg enzyme towards D-malate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
- Vmax=0.17 µmol/min/mg enzyme towards D-lactate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 | 386 | D-2-hydroxyglutarateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 386 | D-lactateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 386 | D-malateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 390 | D-2-hydroxyglutarateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 390 | D-malateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 401 | D-2-hydroxyglutarateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 401 | D-malateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 | 434 | Zinc1 Publication Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 441 | Zinc1 Publication Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 443 | D-2-hydroxyglutarateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 475 | Zinc1 Publication Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 476 | D-2-hydroxyglutarateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 476 | D-lactateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 476 | D-malateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 |
<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
- (R)-2-hydroxyglutarate dehydrogenase activity Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.10"Evidence for genetic heterogeneity in D-2-hydroxyglutaric aciduria."
Kranendijk M., Struys E.A., Gibson K.M., Wickenhagen W.V., Abdenur J.E., Buechner J., Christensen E., de Kremer R.D., Errami A., Gissen P., Gradowska W., Hobson E., Islam L., Korman S.H., Kurczynski T., Maranda B., Meli C., Rizzo C. , Sansaricq C., Trefz F.K., Webster R., Jakobs C., Salomons G.S.
Hum. Mutat. 31:279-283(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; 169-GLN--ALA-521 DEL; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; 400-TYR--ALA-521 DEL; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; VAL-153; TYR-172; 400-TYR--ALA-521 DEL; HIS-419 AND THR-426, FUNCTION, CATALYTIC ACTIVITY. - Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
- FAD binding Source: InterPro
- zinc ion 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
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
GO - Biological processi
- 2-oxoglutarate metabolic process Source: Reactome
- cellular protein metabolic process Source: HGNC-UCL
<p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p>
Inferred from sequence or structural similarityi
- Ref.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
- malate metabolic process Source: UniProtKBInferred from direct assayi
- Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
- response to cobalt ion Source: HGNC-UCLInferred from sequence or structural similarityi
- Ref.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
- response to manganese ion Source: HGNC-UCLInferred from sequence or structural similarityi
- Ref.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
- response to zinc ion Source: HGNC-UCLInferred from sequence or structural similarityi
- Ref.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
<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 | Oxidoreductase |
| Ligand | FAD, Flavoprotein, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.1.99.39, 2681 |
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | Q8N465 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-880009, Interconversion of 2-oxoglutarate and 2-hydroxyglutarate |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q8N465 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q8N465 |
<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%5Fand%5Ftaxonomy%5Fsection">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: D-2-hydroxyglutarate dehydrogenase, mitochondrial (EC:1.1.99.39
Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:D2HGDH Synonyms:D2HGD |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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
Human Gene Nomenclature Database More...HGNCi | HGNC:28358, D2HGDH |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 609186, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q8N465 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000180902 |
<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
Mitochondrion
- Mitochondrion 1 Publication
Manual assertion inferred by curator fromi
- Ref.4"Identification of a dehydrogenase acting on D-2-hydroxyglutarate."
Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.
Biochem. J. 381:35-42(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
- Mitochondrion 1 Publication
Mitochondrion
- mitochondrial matrix Source: Reactome
- mitochondrion Source: HPA
Keywords - Cellular componenti
Mitochondrion<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
D-2-hydroxyglutaric aciduria 1 (D2HGA1)6 PublicationsManual assertion based on experiment ini
- Ref.5"Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria."
Struys E.A., Salomons G.S., Achouri Y., van Schaftingen E., Grosso S., Craigen W.J., Verhoeven N.M., Jakobs C.
Am. J. Hum. Genet. 76:358-360(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 SER-147 AND ALA-444, CHARACTERIZATION OF VARIANTS D2HGA1 SER-147 AND ALA-444, FUNCTION, CATALYTIC ACTIVITY. - Ref.6"Mutations in phenotypically mild D-2-hydroxyglutaric aciduria."
Struys E.A., Korman S.H., Salomons G.S., Darmin P.S., Achouri Y., van Schaftingen E., Verhoeven N.M., Jakobs C.
Ann. Neurol. 58:626-630(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT D2HGA1 ASP-439, CHARACTERIZATION OF VARIANT D2HGA1 ASP-439, FUNCTION, CATALYTIC ACTIVITY. - Ref.7"Phenotypic heterogeneity in the presentation of D-2-hydroxyglutaric aciduria in monozygotic twins."
Misra V.K., Struys E.A., O'brien W., Salomons G.S., Glover T., Jakobs C., Innis J.W.
Mol. Genet. Metab. 86:200-205(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT D2HGA1 TYR-375. - Ref.9"Peripheral neuropathy in a patient with D-2-hydroxyglutaric aciduria."
Haliloglu G., Temucin C.M., Oguz K.K., Celiker A., Coskun T., Sass J.O., Fischer J., Topcu M.
J. Inherit. Metab. Dis. 32:S21-S25(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT D2HGA1 THR-153. - Ref.10"Evidence for genetic heterogeneity in D-2-hydroxyglutaric aciduria."
Kranendijk M., Struys E.A., Gibson K.M., Wickenhagen W.V., Abdenur J.E., Buechner J., Christensen E., de Kremer R.D., Errami A., Gissen P., Gradowska W., Hobson E., Islam L., Korman S.H., Kurczynski T., Maranda B., Meli C., Rizzo C. , Sansaricq C., Trefz F.K., Webster R., Jakobs C., Salomons G.S.
Hum. Mutat. 31:279-283(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; 169-GLN--ALA-521 DEL; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; 400-TYR--ALA-521 DEL; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; VAL-153; TYR-172; 400-TYR--ALA-521 DEL; HIS-419 AND THR-426, FUNCTION, CATALYTIC ACTIVITY. - Ref.11"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
Ref.5
"Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria."
Struys E.A., Salomons G.S., Achouri Y., van Schaftingen E., Grosso S., Craigen W.J., Verhoeven N.M., Jakobs C.
Am. J. Hum. Genet. 76:358-360(2005) [PubMed] [Europe PMC] [Abstract]
Struys E.A., Salomons G.S., Achouri Y., van Schaftingen E., Grosso S., Craigen W.J., Verhoeven N.M., Jakobs C.
Am. J. Hum. Genet. 76:358-360(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS D2HGA1 SER-147 AND ALA-444, CHARACTERIZATION OF VARIANTS D2HGA1 SER-147 AND ALA-444, FUNCTION, CATALYTIC ACTIVITY.
Ref.6
"Mutations in phenotypically mild D-2-hydroxyglutaric aciduria."
Struys E.A., Korman S.H., Salomons G.S., Darmin P.S., Achouri Y., van Schaftingen E., Verhoeven N.M., Jakobs C.
Ann. Neurol. 58:626-630(2005) [PubMed] [Europe PMC] [Abstract]
Struys E.A., Korman S.H., Salomons G.S., Darmin P.S., Achouri Y., van Schaftingen E., Verhoeven N.M., Jakobs C.
Ann. Neurol. 58:626-630(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT D2HGA1 ASP-439, CHARACTERIZATION OF VARIANT D2HGA1 ASP-439, FUNCTION, CATALYTIC ACTIVITY.
Ref.7
"Phenotypic heterogeneity in the presentation of D-2-hydroxyglutaric aciduria in monozygotic twins."
Misra V.K., Struys E.A., O'brien W., Salomons G.S., Glover T., Jakobs C., Innis J.W.
Mol. Genet. Metab. 86:200-205(2005) [PubMed] [Europe PMC] [Abstract]
Misra V.K., Struys E.A., O'brien W., Salomons G.S., Glover T., Jakobs C., Innis J.W.
Mol. Genet. Metab. 86:200-205(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT D2HGA1 TYR-375.
Ref.9
"Peripheral neuropathy in a patient with D-2-hydroxyglutaric aciduria."
Haliloglu G., Temucin C.M., Oguz K.K., Celiker A., Coskun T., Sass J.O., Fischer J., Topcu M.
J. Inherit. Metab. Dis. 32:S21-S25(2009) [PubMed] [Europe PMC] [Abstract]
Haliloglu G., Temucin C.M., Oguz K.K., Celiker A., Coskun T., Sass J.O., Fischer J., Topcu M.
J. Inherit. Metab. Dis. 32:S21-S25(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT D2HGA1 THR-153.
Ref.10
"Evidence for genetic heterogeneity in D-2-hydroxyglutaric aciduria."
Kranendijk M., Struys E.A., Gibson K.M., Wickenhagen W.V., Abdenur J.E., Buechner J., Christensen E., de Kremer R.D., Errami A., Gissen P., Gradowska W., Hobson E., Islam L., Korman S.H., Kurczynski T., Maranda B., Meli C., Rizzo C. , Sansaricq C., Trefz F.K., Webster R., Jakobs C., Salomons G.S.
Hum. Mutat. 31:279-283(2010) [PubMed] [Europe PMC] [Abstract]
Kranendijk M., Struys E.A., Gibson K.M., Wickenhagen W.V., Abdenur J.E., Buechner J., Christensen E., de Kremer R.D., Errami A., Gissen P., Gradowska W., Hobson E., Islam L., Korman S.H., Kurczynski T., Maranda B., Meli C., Rizzo C. , Sansaricq C., Trefz F.K., Webster R., Jakobs C., Salomons G.S.
Hum. Mutat. 31:279-283(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; 169-GLN--ALA-521 DEL; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; 400-TYR--ALA-521 DEL; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; VAL-153; TYR-172; 400-TYR--ALA-521 DEL; HIS-419 AND THR-426, FUNCTION, CATALYTIC ACTIVITY.
Ref.11
"Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations."
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]
Yang J., Zhu H., Zhang T., Ding J.
Cell Discov. 7:3-3(2021) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 51-521 IN COMPLEX WITH D-2-HYDROXYGLUTARATE; D-MALATE; D-LACTATE; L-2-HYDROXYGLUTARATE AND 2-OXOGLUTARATE, FUNCTION, CATALYTIC ACTIVITY, ZINC-BINDING SITES, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-386; THR-390; LYS-401; HIS-434; HIS-441; ASN-443; GLU-475 AND HIS-476, CHARACTERIZATION OF VARIANTS D2HGA1 TRP-109; LYS-127; VAL-131; SER-147; THR-153; VAL-153; TYR-172; LEU-189; VAL-205; VAL-231; SER-233; TYR-375; MET-399; HIS-419; THR-426; ASP-439; ALA-444; VAL-446 AND ARG-477, CHARACTERIZATION OF VARIANT VAL-436.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine.
Related information in OMIM| 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_084974 | 109 | S → W in D2HGA1; unknown pathological significance; significant loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084975 | 127 | N → K in D2HGA1; unknown pathological significance; complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084976 | 131 | G → V in D2HGA1; unknown pathological significance; complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025890 | 147 | I → S in D2HGA1; severe phenotype; unknown pathological significance; almost complete loss of catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084977 | 153 | M → T in D2HGA1; unknown pathological significance; significant loss of catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084978 | 153 | M → V in D2HGA1; unknown pathological significance; significant loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084979 | 169 – 521 | Missing in D2HGA1; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 353 | |
| Natural variantiVAR_084980 | 172 | C → Y in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084981 | 189 | P → L in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084982 | 205 | A → V in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084983 | 231 | A → V in D2HGA1; unknown pathological significance; significant loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084984 | 233 | G → S in D2HGA1; unknown pathological significance; no effect on catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025891 | 375 | D → Y in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084985 | 399 | V → M in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084986 | 400 – 521 | Missing in D2HGA1; unknown pathological significance; complete loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 122 | |
| Natural variantiVAR_084987 | 419 | R → H in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084988 | 426 | A → T in D2HGA1; unknown pathological significance; no effect on catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025893 | 439 | N → D in D2HGA1; mild phenotype; unknown pathological significance; moderate reduction in catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025894 | 444 | V → A in D2HGA1; severe phenotype; unknown pathological significance; significant reduction in catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084989 | 446 | A → V in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084990 | 477 | G → R in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity. 2 Publications 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%5Fand%5Fbiotech%5Fsection">'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 | 386 | R → A: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 390 | T → A: Significantly reduced catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 401 | K → A: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 434 | H → A: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 441 | H → A: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 443 | N → A: Significantly reduced catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 475 | E → A: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 476 | H → A: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNET More...DisGeNETi | 728294 |
MalaCards human disease database More...MalaCardsi | D2HGDH |
| MIMi | 600721, phenotype |
Open Targets More...OpenTargetsi | ENSG00000180902 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 79315, D-2-hydroxyglutaric aciduria |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA143485446 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | Q8N465, Tbio |
Genetic variation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | D2HGDH |
Domain mapping of disease mutations (DMDM) More...DMDMi | 91208273 |
<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 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei | 1 – 13 | MitochondrionSequence analysisAdd BLAST | 13 | |
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000231674 | 14 – 521 | D-2-hydroxyglutarate dehydrogenase, mitochondrialAdd BLAST | 508 |
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 | 101 | N6-succinyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q8N465 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | Q8N465 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | Q8N465 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q8N465 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q8N465 |
PeptideAtlas More...PeptideAtlasi | Q8N465 |
PRoteomics IDEntifications database More...PRIDEi | Q8N465 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 5910 71889 [Q8N465-1] 71890 [Q8N465-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q8N465 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q8N465 |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000180902, Expressed in right uterine tube and 194 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q8N465, baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q8N465, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000180902, Low tissue specificity |
<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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 608722, 176 interactors |
Protein interaction database and analysis system More...IntActi | Q8N465, 11 interactors |
Molecular INTeraction database More...MINTi | Q8N465 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000315351 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | Q8N465, protein |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 64 – 73 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 82 – 85 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 86 – 89 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 109 – 122 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> 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 | 126 – 132 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 135 – 137 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 142 – 144 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 146 – 149 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 156 – 159 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 161 – 163 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 165 – 169 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 174 – 182 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Turni | 183 – 185 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 193 – 197 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 200 – 206 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 213 – 216 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 219 – 222 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 223 – 229 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 235 – 238 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 252 – 255 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 264 – 271 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 277 – 288 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 289 – 302 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
| Helixi | 304 – 306 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 307 – 314 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 315 – 325 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 335 – 345 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 347 – 363 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
| Beta strandi | 368 – 373 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 376 – 387 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 389 – 394 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 396 – 405 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 408 – 410 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 413 – 422 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 423 – 425 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 426 – 434 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 435 – 437 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 439 – 448 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 451 – 457 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 460 – 467 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 471 – 476 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 479 – 484 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 486 – 488 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 492 – 505 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 515 – 517 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
AlphaFold Protein Structure Database More...AlphaFoldDBi | Q8N465 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8N465 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<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%5Fand%5Fdomains%5Fsection">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 | 96 – 275 | FAD-binding PCMH-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 | 180 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the FAD-binding oxidoreductase/transferase type 4 family.Curated
Keywords - Domaini
Transit peptidePhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1232, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00550000075086 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q8N465 |
Identification of Orthologs from Complete Genome Data More...OMAi | CNDNMLA |
Database of Orthologous Groups More...OrthoDBi | 515900at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q8N465 |
TreeFam database of animal gene trees More...TreeFami | TF323342 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.45.10, 1 hit 3.30.43.10, 1 hit 3.30.465.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR016166, FAD-bd_PCMH IPR036318, FAD-bd_PCMH-like_sf IPR016167, FAD-bd_PCMH_sub1 IPR016169, FAD-bd_PCMH_sub2 IPR016164, FAD-linked_Oxase-like_C IPR004113, FAD-linked_oxidase_C IPR006094, Oxid_FAD_bind_N IPR016171, Vanillyl_alc_oxidase_C-sub2 |
Pfam protein domain database More...Pfami | View protein in Pfam PF02913, FAD-oxidase_C, 1 hit PF01565, FAD_binding_4, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF55103, SSF55103, 1 hit SSF56176, SSF56176, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51387, FAD_PCMH, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 basketThis entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: Q8N465-1) [UniParc]FASTAAdd to basketAdded to basket
This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
« Hide
Show »10 20 30 40 50
MLPRRPLAWP AWLLRGAPGA AGSWGRPVGP LARRGCCSAP GTPEVPLTRE
60 70 80 90 100
RYPVRRLPFS TVSKQDLAAF ERIVPGGVVT DPEALQAPNV DWLRTLRGCS
110 120 130 140 150
KVLLRPRTSE EVSHILRHCH ERNLAVNPQG GNTGMVGGSV PVFDEIILST
160 170 180 190 200
ARMNRVLSFH SVSGILVCQA GCVLEELSRY VEERDFIMPL DLGAKGSCHI
210 220 230 240 250
GGNVATNAGG LRFLRYGSLH GTVLGLEVVL ADGTVLDCLT SLRKDNTGYD
260 270 280 290 300
LKQLFIGSEG TLGIITTVSI LCPPKPRAVN VAFLGCPGFA EVLQTFSTCK
310 320 330 340 350
GMLGEILSAF EFMDAVCMQL VGRHLHLASP VQESPFYVLI ETSGSNAGHD
360 370 380 390 400
AEKLGHFLEH ALGSGLVTDG TMATDQRKVK MLWALRERIT EALSRDGYVY
410 420 430 440 450
KYDLSLPVER LYDIVTDLRA RLGPHAKHVV GYGHLGDGNL HLNVTAEAFS
460 470 480 490 500
PSLLAALEPH VYEWTAGQQG SVSAEHGVGF RKRDVLGYSK PPGALQLMQQ
510 520
LKALLDPKGI LNPYKTLPSQ A
Length:521
Mass (Da):56,416
Last modified:April 4, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i65D88C4315FA45CE
Isoform 2 (identifier: Q8N465-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
165-172: ILVCQAGC → GL
285-313: GCPGFAEVLQTFSTCKGMLGEILSAFEFM → VTCVLPACGPGSPRPARLPHPALRTPGLR
314-521: Missing.
« Hide
Show »10 20 30 40 50
MLPRRPLAWP AWLLRGAPGA AGSWGRPVGP LARRGCCSAP GTPEVPLTRE
60 70 80 90 100
RYPVRRLPFS TVSKQDLAAF ERIVPGGVVT DPEALQAPNV DWLRTLRGCS
110 120 130 140 150
KVLLRPRTSE EVSHILRHCH ERNLAVNPQG GNTGMVGGSV PVFDEIILST
160 170 180 190 200
ARMNRVLSFH SVSGGLVLEE LSRYVEERDF IMPLDLGAKG SCHIGGNVAT
210 220 230 240 250
NAGGLRFLRY GSLHGTVLGL EVVLADGTVL DCLTSLRKDN TGYDLKQLFI
260 270 280 290 300
GSEGTLGIIT TVSILCPPKP RAVNVAFLVT CVLPACGPGS PRPARLPHPA
LRTPGLR
Isoform 3 (identifier: Q8N465-3) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
285-319: GCPGFAEVLQTFSTCKGMLGEILSAFEFMDAVCMQ → VTCVPPACGPGSPRPARLPHPALRTPGVCPQPLRL
320-521: Missing.
« Hide
Show »10 20 30 40 50
MLPRRPLAWP AWLLRGAPGA AGSWGRPVGP LARRGCCSAP GTPEVPLTRE
60 70 80 90 100
RYPVRRLPFS TVSKQDLAAF ERIVPGGVVT DPEALQAPNV DWLRTLRGCS
110 120 130 140 150
KVLLRPRTSE EVSHILRHCH ERNLAVNPQG GNTGMVGGSV PVFDEIILST
160 170 180 190 200
ARMNRVLSFH SVSGILVCQA GCVLEELSRY VEERDFIMPL DLGAKGSCHI
210 220 230 240 250
GGNVATNAGG LRFLRYGSLH GTVLGLEVVL ADGTVLDCLT SLRKDNTGYD
260 270 280 290 300
LKQLFIGSEG TLGIITTVSI LCPPKPRAVN VAFLVTCVPP ACGPGSPRPA
310
RLPHPALRTP GVCPQPLRL
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket| Entry | Entry name | Protein names | Gene names | Length | Annotation | ||
|---|---|---|---|---|---|---|---|
| F8WCF9 | F8WCF9_HUMAN | D-2-hydroxyglutarate dehydrogenase,... D-2-hydroxyglutarate dehydrogenase, mitochondrial | D2HGDH | 243 | Annotation score: Annotation score:1 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> | ||
| B5MCV2 | B5MCV2_HUMAN | D-2-hydroxyglutarate dehydrogenase,... D-2-hydroxyglutarate dehydrogenase, mitochondrial | D2HGDH | 387 | Annotation score: Annotation score:1 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> | ||
| G5E9E8 | G5E9E8_HUMAN | D-2-hydroxyglutarate dehydrogenase,... D-2-hydroxyglutarate dehydrogenase, isoform CRA_b (D-2-hydroxyglutarate dehydrogenase, mitochondrial) | D2HGDH hCG_31745 | 320 | Annotation score: Annotation score:1 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> | ||
| H7C021 | H7C021_HUMAN | D-2-hydroxyglutarate dehydrogenase,... D-2-hydroxyglutarate dehydrogenase, mitochondrial | D2HGDH | 152 | Annotation score: Annotation score:1 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> | ||
| H7C3L2 | H7C3L2_HUMAN | D-2-hydroxyglutarate dehydrogenase,... D-2-hydroxyglutarate dehydrogenase, mitochondrial | D2HGDH | 89 | Annotation score: Annotation score:1 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> | ||
| H7C0N1 | H7C0N1_HUMAN | D-2-hydroxyglutarate dehydrogenase,... D-2-hydroxyglutarate dehydrogenase, mitochondrial | D2HGDH | 189 | Annotation score: Annotation score:1 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> | ||
| H7C290 | H7C290_HUMAN | D-2-hydroxyglutarate dehydrogenase,... D-2-hydroxyglutarate dehydrogenase, mitochondrial | D2HGDH | 78 | Annotation score: Annotation score:1 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> | ||
<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
The sequence AAX82020 differs from that shown. Reason: Erroneous gene model prediction.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 55 | R → Q in AAH36604 (PubMed:15489334).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_025889 | 15 | R → G1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084974 | 109 | S → W in D2HGA1; unknown pathological significance; significant loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084975 | 127 | N → K in D2HGA1; unknown pathological significance; complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084976 | 131 | G → V in D2HGA1; unknown pathological significance; complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025890 | 147 | I → S in D2HGA1; severe phenotype; unknown pathological significance; almost complete loss of catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084977 | 153 | M → T in D2HGA1; unknown pathological significance; significant loss of catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084978 | 153 | M → V in D2HGA1; unknown pathological significance; significant loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084979 | 169 – 521 | Missing in D2HGA1; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 353 | |
| Natural variantiVAR_084980 | 172 | C → Y in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084981 | 189 | P → L in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084982 | 205 | A → V in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084983 | 231 | A → V in D2HGA1; unknown pathological significance; significant loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084984 | 233 | G → S in D2HGA1; unknown pathological significance; no effect on catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_050433 | 338 | V → I. Corresponds to variant dbSNP:rs1106639EnsemblClinVar. | 1 | |
| Natural variantiVAR_050434 | 361 | A → V. Corresponds to variant dbSNP:rs1105273EnsemblClinVar. | 1 | |
| Natural variantiVAR_025891 | 375 | D → Y in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084985 | 399 | V → M in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084986 | 400 – 521 | Missing in D2HGA1; unknown pathological significance; complete loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 122 | |
| Natural variantiVAR_084987 | 419 | R → H in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084988 | 426 | A → T in D2HGA1; unknown pathological significance; no effect on catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025892 | 436 | G → V Slight reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025893 | 439 | N → D in D2HGA1; mild phenotype; unknown pathological significance; moderate reduction in catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025894 | 444 | V → A in D2HGA1; severe phenotype; unknown pathological significance; significant reduction in catalytic activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084989 | 446 | A → V in D2HGA1; unknown pathological significance; moderate reduction in catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_084990 | 477 | G → R in D2HGA1; unknown pathological significance; almost complete loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 |
Alternative sequence
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 | AK304773 mRNA Translation: BAG65528.1 AC114730 Genomic DNA Translation: AAX82020.1 Sequence problems. BC036604 mRNA Translation: AAH36604.2 BC071598 mRNA Translation: AAH71598.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS33426.1 [Q8N465-1] |
NCBI Reference Sequences More...RefSeqi | NP_001274178.1, NM_001287249.1 NP_689996.4, NM_152783.4 [Q8N465-1] XP_011510062.1, XM_011511760.2 [Q8N465-3] |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000321264.9; ENSP00000315351.4; ENSG00000180902.18 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 728294 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:728294 |
Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one More...MANE-Selecti | ENST00000321264.9; ENSP00000315351.4; NM_152783.5; NP_689996.4 |
UCSC genome browser More...UCSCi | uc002wce.3, human [Q8N465-1] |
Keywords - Coding sequence diversityi
Alternative splicing<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 | Source | |
|---|---|---|---|---|---|---|
| Q8N465 | D-2-hydroxyglutarate dehydrogenase, mitochondrial | 387 | UniRef100_Q8N465 | |||
| +1 | ||||||
<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
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK304773 mRNA Translation: BAG65528.1 AC114730 Genomic DNA Translation: AAX82020.1 Sequence problems. BC036604 mRNA Translation: AAH36604.2 BC071598 mRNA Translation: AAH71598.1 |
| CCDSi | CCDS33426.1 [Q8N465-1] |
| RefSeqi | NP_001274178.1, NM_001287249.1 NP_689996.4, NM_152783.4 [Q8N465-1] XP_011510062.1, XM_011511760.2 [Q8N465-3] |
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 |
| 6LPN | X-ray | 2.21 | A/B | 51-521 | [»] | |
| 6LPP | X-ray | 2.65 | A/B | 51-521 | [»] | |
| 6LPQ | X-ray | 2.80 | A/B | 51-521 | [»] | |
| 6LPT | X-ray | 2.62 | A/B | 51-521 | [»] | |
| 6LPU | X-ray | 2.92 | A/B | 51-521 | [»] | |
| 6LPX | X-ray | 2.80 | A/B | 51-521 | [»] | |
| AlphaFoldDBi | Q8N465 | |||||
| SMRi | Q8N465 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 608722, 176 interactors |
| IntActi | Q8N465, 11 interactors |
| MINTi | Q8N465 |
| STRINGi | 9606.ENSP00000315351 |
PTM databases
| iPTMneti | Q8N465 |
| PhosphoSitePlusi | Q8N465 |
Genetic variation databases
| BioMutai | D2HGDH |
| DMDMi | 91208273 |
Proteomic databases
| EPDi | Q8N465 |
| jPOSTi | Q8N465 |
| MassIVEi | Q8N465 |
| MaxQBi | Q8N465 |
| PaxDbi | Q8N465 |
| PeptideAtlasi | Q8N465 |
| PRIDEi | Q8N465 |
| ProteomicsDBi | 5910 71889 [Q8N465-1] 71890 [Q8N465-2] |
Protocols and materials databases
Antibodypedia a portal for validated antibodies More...Antibodypediai | 34576, 113 antibodies from 18 providers |
The DNASU plasmid repository More...DNASUi | 728294 |
Genome annotation databases
| Ensembli | ENST00000321264.9; ENSP00000315351.4; ENSG00000180902.18 |
| GeneIDi | 728294 |
| KEGGi | hsa:728294 |
| MANE-Selecti | ENST00000321264.9; ENSP00000315351.4; NM_152783.5; NP_689996.4 |
| UCSCi | uc002wce.3, human [Q8N465-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 728294 |
| DisGeNETi | 728294 |
GeneCards: human genes, protein and diseases More...GeneCardsi | D2HGDH |
| HGNCi | HGNC:28358, D2HGDH |
| HPAi | ENSG00000180902, Low tissue specificity |
| MalaCardsi | D2HGDH |
| MIMi | 600721, phenotype 609186, gene |
| neXtProti | NX_Q8N465 |
| OpenTargetsi | ENSG00000180902 |
| Orphaneti | 79315, D-2-hydroxyglutaric aciduria |
| PharmGKBi | PA143485446 |
| VEuPathDBi | HostDB:ENSG00000180902 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
| eggNOGi | KOG1232, Eukaryota |
| GeneTreei | ENSGT00550000075086 |
| InParanoidi | Q8N465 |
| OMAi | CNDNMLA |
| OrthoDBi | 515900at2759 |
| PhylomeDBi | Q8N465 |
| TreeFami | TF323342 |
Enzyme and pathway databases
| BRENDAi | 1.1.99.39, 2681 |
| PathwayCommonsi | Q8N465 |
| Reactomei | R-HSA-880009, Interconversion of 2-oxoglutarate and 2-hydroxyglutarate |
| SignaLinki | Q8N465 |
| SIGNORi | Q8N465 |
Miscellaneous databases
BioGRID ORCS database of CRISPR phenotype screens More...BioGRID-ORCSi | 728294, 10 hits in 1079 CRISPR screens |
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | D2HGDH, human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | D2HGDH |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 728294 |
| Pharosi | Q8N465, Tbio |
Protein Ontology More...PROi | PR:Q8N465 |
| RNActi | Q8N465, protein |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
| Bgeei | ENSG00000180902, Expressed in right uterine tube and 194 other tissues |
| ExpressionAtlasi | Q8N465, baseline and differential |
| Genevisiblei | Q8N465, HS |
Family and domain databases
| Gene3Di | 1.10.45.10, 1 hit 3.30.43.10, 1 hit 3.30.465.10, 1 hit |
| InterProi | View protein in InterPro IPR016166, FAD-bd_PCMH IPR036318, FAD-bd_PCMH-like_sf IPR016167, FAD-bd_PCMH_sub1 IPR016169, FAD-bd_PCMH_sub2 IPR016164, FAD-linked_Oxase-like_C IPR004113, FAD-linked_oxidase_C IPR006094, Oxid_FAD_bind_N IPR016171, Vanillyl_alc_oxidase_C-sub2 |
| Pfami | View protein in Pfam PF02913, FAD-oxidase_C, 1 hit PF01565, FAD_binding_4, 1 hit |
| SUPFAMi | SSF55103, SSF55103, 1 hit SSF56176, SSF56176, 1 hit |
| PROSITEi | View protein in PROSITE PS51387, FAD_PCMH, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | 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 | D2HDH_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 | Q8N465Primary (citable) accession number: Q8N465 Secondary accession number(s): B4E3L6 , E7ENP2, Q6IQ24, Q8N5Q8 | |
| <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 4, 2006 |
| Last sequence update: | April 4, 2006 | |
| Last modified: | May 25, 2022 | |
| This is version 168 of the entry and version 3 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
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - 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 - SIMILARITY comments
Index of protein domains and families
