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Q8N465

- D2HDH_HUMAN

UniProt

Q8N465 - D2HDH_HUMAN

Protein

D-2-hydroxyglutarate dehydrogenase, mitochondrial

Gene

D2HGDH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate.1 Publication

    Catalytic activityi

    (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor.

    Cofactori

    FAD.Curated

    Enzyme regulationi

    Activated by zinc and cobalt.1 Publication

    GO - Molecular functioni

    1. (R)-2-hydroxyglutarate dehydrogenase activity Source: HGNC
    2. flavin adenine dinucleotide binding Source: InterPro
    3. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: Reactome
    2. cellular metabolic process Source: Reactome
    3. cellular protein metabolic process Source: HGNC
    4. response to cobalt ion Source: HGNC
    5. response to manganese ion Source: HGNC
    6. response to zinc ion Source: HGNC
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_25367. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-2-hydroxyglutarate dehydrogenase, mitochondrial (EC:1.1.99.-)
    Gene namesi
    Name:D2HGDH
    Synonyms:D2HGD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:28358. D2HGDH.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: HGNC

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    D-2-hydroxyglutaric aciduria 1 (D2HGA1) [MIM:600721]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti147 – 1471I → S in D2HGA1; severe phenotype; loss of catalytic activity. 1 Publication
    VAR_025890
    Natural varianti375 – 3751D → Y in D2HGA1. 1 Publication
    VAR_025891
    Natural varianti439 – 4391N → D in D2HGA1; mild phenotype; altered catalytic activity. 1 Publication
    VAR_025893
    Natural varianti444 – 4441V → A in D2HGA1; severe phenotype; altered catalytic activity. 1 Publication
    VAR_025894

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi600721. phenotype.
    Orphaneti79315. D-2-hydroxyglutaric aciduria.
    PharmGKBiPA143485446.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1313MitochondrionSequence AnalysisAdd
    BLAST
    Chaini14 – 521508D-2-hydroxyglutarate dehydrogenase, mitochondrialPRO_0000231674Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiQ8N465.
    PaxDbiQ8N465.
    PeptideAtlasiQ8N465.
    PRIDEiQ8N465.

    PTM databases

    PhosphoSiteiQ8N465.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8N465.
    BgeeiQ8N465.
    CleanExiHS_D2HGDH.
    GenevestigatoriQ8N465.

    Organism-specific databases

    HPAiHPA056216.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAB25P577351EBI-1053783,EBI-1050500

    Protein-protein interaction databases

    BioGridi608722. 3 interactions.
    STRINGi9606.ENSP00000315351.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N465.
    SMRiQ8N465. Positions 61-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini96 – 275180FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0277.
    HOGENOMiHOG000230997.
    HOVERGENiHBG079809.
    InParanoidiQ8N465.
    OMAiVYEWTAR.
    OrthoDBiEOG7BS49D.
    PhylomeDBiQ8N465.
    TreeFamiTF323342.

    Family and domain databases

    Gene3Di1.10.45.10. 1 hit.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR016164. FAD-linked_Oxase-like_C.
    IPR004113. FAD-linked_oxidase_C.
    IPR006094. Oxid_FAD_bind_N.
    IPR016171. Vanillyl_alc_oxidase_C-sub2.
    [Graphical view]
    PfamiPF02913. FAD-oxidase_C. 1 hit.
    PF01565. FAD_binding_4. 1 hit.
    [Graphical view]
    SUPFAMiSSF55103. SSF55103. 1 hit.
    SSF56176. SSF56176. 1 hit.
    PROSITEiPS51387. FAD_PCMH. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N465-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLPRRPLAWP AWLLRGAPGA AGSWGRPVGP LARRGCCSAP GTPEVPLTRE    50
    RYPVRRLPFS TVSKQDLAAF ERIVPGGVVT DPEALQAPNV DWLRTLRGCS 100
    KVLLRPRTSE EVSHILRHCH ERNLAVNPQG GNTGMVGGSV PVFDEIILST 150
    ARMNRVLSFH SVSGILVCQA GCVLEELSRY VEERDFIMPL DLGAKGSCHI 200
    GGNVATNAGG LRFLRYGSLH GTVLGLEVVL ADGTVLDCLT SLRKDNTGYD 250
    LKQLFIGSEG TLGIITTVSI LCPPKPRAVN VAFLGCPGFA EVLQTFSTCK 300
    GMLGEILSAF EFMDAVCMQL VGRHLHLASP VQESPFYVLI ETSGSNAGHD 350
    AEKLGHFLEH ALGSGLVTDG TMATDQRKVK MLWALRERIT EALSRDGYVY 400
    KYDLSLPVER LYDIVTDLRA RLGPHAKHVV GYGHLGDGNL HLNVTAEAFS 450
    PSLLAALEPH VYEWTAGQQG SVSAEHGVGF RKRDVLGYSK PPGALQLMQQ 500
    LKALLDPKGI LNPYKTLPSQ A 521
    Length:521
    Mass (Da):56,416
    Last modified:April 4, 2006 - v3
    Checksum:i65D88C4315FA45CE
    GO
    Isoform 2 (identifier: Q8N465-2) [UniParc]FASTAAdd 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.

    Note: No experimental confirmation available.

    Show »
    Length:307
    Mass (Da):32,933
    Checksum:i2EA2EA997C5E4968
    GO
    Isoform 3 (identifier: Q8N465-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         285-319: GCPGFAEVLQTFSTCKGMLGEILSAFEFMDAVCMQ → VTCVPPACGPGSPRPARLPHPALRTPGVCPQPLRL
         320-521: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:319
    Mass (Da):34,173
    Checksum:i6C7BDA672635D743
    GO

    Sequence cautioni

    The sequence AAX82020.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551R → Q in AAH36604. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151R → G.1 Publication
    Corresponds to variant rs4675887 [ dbSNP | Ensembl ].
    VAR_025889
    Natural varianti147 – 1471I → S in D2HGA1; severe phenotype; loss of catalytic activity. 1 Publication
    VAR_025890
    Natural varianti338 – 3381V → I.
    Corresponds to variant rs1106639 [ dbSNP | Ensembl ].
    VAR_050433
    Natural varianti361 – 3611A → V.
    Corresponds to variant rs1105273 [ dbSNP | Ensembl ].
    VAR_050434
    Natural varianti375 – 3751D → Y in D2HGA1. 1 Publication
    VAR_025891
    Natural varianti436 – 4361G → V.1 Publication
    VAR_025892
    Natural varianti439 – 4391N → D in D2HGA1; mild phenotype; altered catalytic activity. 1 Publication
    VAR_025893
    Natural varianti444 – 4441V → A in D2HGA1; severe phenotype; altered catalytic activity. 1 Publication
    VAR_025894

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei165 – 1728ILVCQAGC → GL in isoform 2. 1 PublicationVSP_017876
    Alternative sequencei285 – 31935GCPGF…AVCMQ → VTCVPPACGPGSPRPARLPH PALRTPGVCPQPLRL in isoform 3. 1 PublicationVSP_054389Add
    BLAST
    Alternative sequencei285 – 31329GCPGF…AFEFM → VTCVLPACGPGSPRPARLPH PALRTPGLR in isoform 2. 1 PublicationVSP_017877Add
    BLAST
    Alternative sequencei314 – 521208Missing in isoform 2. 1 PublicationVSP_017878Add
    BLAST
    Alternative sequencei320 – 521202Missing in isoform 3. 1 PublicationVSP_054390Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSiCCDS33426.1. [Q8N465-1]
    RefSeqiNP_001274178.1. NM_001287249.1.
    NP_689996.4. NM_152783.4. [Q8N465-1]
    UniGeneiHs.516813.

    Genome annotation databases

    EnsembliENST00000321264; ENSP00000315351; ENSG00000180902. [Q8N465-1]
    GeneIDi728294.
    KEGGihsa:728294.
    UCSCiuc002wce.1. human. [Q8N465-1]

    Polymorphism databases

    DMDMi91208273.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 ]
    UniGenei Hs.516813.

    3D structure databases

    ProteinModelPortali Q8N465.
    SMRi Q8N465. Positions 61-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 608722. 3 interactions.
    STRINGi 9606.ENSP00000315351.

    PTM databases

    PhosphoSitei Q8N465.

    Polymorphism databases

    DMDMi 91208273.

    Proteomic databases

    MaxQBi Q8N465.
    PaxDbi Q8N465.
    PeptideAtlasi Q8N465.
    PRIDEi Q8N465.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321264 ; ENSP00000315351 ; ENSG00000180902 . [Q8N465-1 ]
    GeneIDi 728294.
    KEGGi hsa:728294.
    UCSCi uc002wce.1. human. [Q8N465-1 ]

    Organism-specific databases

    CTDi 728294.
    GeneCardsi GC02P242673.
    H-InvDB HIX0023187.
    HGNCi HGNC:28358. D2HGDH.
    HPAi HPA056216.
    MIMi 600721. phenotype.
    609186. gene.
    neXtProti NX_Q8N465.
    Orphaneti 79315. D-2-hydroxyglutaric aciduria.
    PharmGKBi PA143485446.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0277.
    HOGENOMi HOG000230997.
    HOVERGENi HBG079809.
    InParanoidi Q8N465.
    OMAi VYEWTAR.
    OrthoDBi EOG7BS49D.
    PhylomeDBi Q8N465.
    TreeFami TF323342.

    Enzyme and pathway databases

    Reactomei REACT_25367. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

    Miscellaneous databases

    GeneWikii D2HGDH.
    GenomeRNAii 728294.
    NextBioi 126719.
    PROi Q8N465.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N465.
    Bgeei Q8N465.
    CleanExi HS_D2HGDH.
    Genevestigatori Q8N465.

    Family and domain databases

    Gene3Di 1.10.45.10. 1 hit.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    InterProi IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR016164. FAD-linked_Oxase-like_C.
    IPR004113. FAD-linked_oxidase_C.
    IPR006094. Oxid_FAD_bind_N.
    IPR016171. Vanillyl_alc_oxidase_C-sub2.
    [Graphical view ]
    Pfami PF02913. FAD-oxidase_C. 1 hit.
    PF01565. FAD_binding_4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55103. SSF55103. 1 hit.
    SSF56176. SSF56176. 1 hit.
    PROSITEi PS51387. FAD_PCMH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Uterus.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus and Placenta.
    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, ENZYME REGULATION, SUBCELLULAR LOCATION.
    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.
    6. Cited for: VARIANT D2HGA1 ASP-439, CHARACTERIZATION OF VARIANT D2HGA1 ASP-439.
    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.
    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.

    Entry informationi

    Entry nameiD2HDH_HUMAN
    AccessioniPrimary (citable) accession number: Q8N465
    Secondary accession number(s): B4E3L6
    , E7ENP2, Q6IQ24, Q8N5Q8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 111 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3