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Q02127

- PYRD_HUMAN

UniProt

Q02127 - PYRD_HUMAN

Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene

DHODH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

    Catalytic activityi

    (S)-dihydroorotate + a quinone = orotate + a quinol.1 Publication

    Cofactori

    Binds 1 FMN per subunit.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei99 – 991Substrate
    Binding sitei119 – 1191FMN2 Publications
    Binding sitei180 – 1801FMN2 Publications
    Binding sitei211 – 2111FMN2 Publications
    Active sitei214 – 2141Nucleophile
    Binding sitei254 – 2541FMN2 Publications
    Binding sitei282 – 2821FMN; via carbonyl oxygen2 Publications
    Binding sitei305 – 3051FMN; via amide nitrogen2 Publications
    Binding sitei334 – 3341FMN; via amide nitrogen2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi95 – 995FMN2 Publications
    Nucleotide bindingi355 – 3562FMN2 Publications

    GO - Molecular functioni

    1. dihydroorotate dehydrogenase activity Source: Reactome
    2. dihydroorotate oxidase activity Source: Ensembl
    3. drug binding Source: Ensembl
    4. FMN binding Source: Ensembl
    5. ubiquinone binding Source: Ensembl

    GO - Biological processi

    1. 'de novo' pyrimidine nucleobase biosynthetic process Source: Ensembl
    2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
    3. female pregnancy Source: Ensembl
    4. lactation Source: Ensembl
    5. nucleobase-containing small molecule metabolic process Source: Reactome
    6. positive regulation of apoptotic process Source: Ensembl
    7. pyrimidine nucleobase metabolic process Source: Reactome
    8. pyrimidine nucleoside biosynthetic process Source: Reactome
    9. regulation of mitochondrial fission Source: Ensembl
    10. response to caffeine Source: Ensembl
    11. response to drug Source: Ensembl
    12. response to starvation Source: Ensembl
    13. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    ReactomeiREACT_21376. Pyrimidine biosynthesis.
    SABIO-RKQ02127.
    UniPathwayiUPA00070; UER00946.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydroorotate dehydrogenase (quinone), mitochondrial (EC:1.3.5.2)
    Short name:
    DHOdehase
    Alternative name(s):
    Dihydroorotate oxidase
    Gene namesi
    Name:DHODH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:2867. DHODH.

    Subcellular locationi

    Mitochondrion inner membrane 1 Publication; Single-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: Reactome
    3. neuronal cell body Source: Ensembl

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Postaxial acrofacial dysostosis (POADS) [MIM:263750]: POADS is characterized by severe micrognathia, cleft lip and/or palate, hypoplasia or aplasia of the posterior elements of the limbs, coloboma of the eyelids and supernumerary nipples. POADS is a very rare disorder: only 2 multiplex families, each consisting of 2 affected siblings born to unaffected, nonconsanguineous parents, have been described among a total of around 30 reported cases.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191G → E in POADS. 1 Publication
    VAR_062412
    Natural varianti135 – 1351R → C in POADS. 1 Publication
    VAR_062413
    Natural varianti152 – 1521G → R in POADS. 1 Publication
    VAR_062414
    Natural varianti199 – 1991R → C in POADS. 1 Publication
    VAR_062415
    Natural varianti202 – 2021G → A in POADS. 1 Publication
    VAR_062416
    Natural varianti202 – 2021G → D in POADS. 1 Publication
    VAR_062417
    Natural varianti244 – 2441R → W in POADS. 1 Publication
    VAR_062418
    Natural varianti284 – 2841T → I in POADS. 1 Publication
    VAR_062419
    Natural varianti346 – 3461R → W in POADS. 1 Publication
    VAR_062420
    Natural varianti392 – 3921D → G in POADS. 1 Publication
    VAR_062421

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi263750. phenotype.
    Orphaneti246. Postaxial acrofacial dysostosis.
    PharmGKBiPA27327.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 395395Dihydroorotate dehydrogenase (quinone), mitochondrialPRO_0000029884Add
    BLAST
    Transit peptidei1 – 1010Mitochondrion; not cleavedBy similarity

    Post-translational modificationi

    The uncleaved transit peptide is required for mitochondrial targeting and proper membrane integration.

    Proteomic databases

    MaxQBiQ02127.
    PaxDbiQ02127.
    PRIDEiQ02127.

    PTM databases

    PhosphoSiteiQ02127.

    Expressioni

    Gene expression databases

    ArrayExpressiQ02127.
    BgeeiQ02127.
    CleanExiHS_DHODH.
    GenevestigatoriQ02127.

    Organism-specific databases

    HPAiHPA010123.
    HPA011942.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi108068. 13 interactions.
    IntActiQ02127. 2 interactions.
    STRINGi9606.ENSP00000219240.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi34 – 396
    Helixi41 – 488
    Helixi51 – 6313
    Helixi76 – 783
    Beta strandi80 – 823
    Beta strandi85 – 939
    Turni95 – 1006
    Beta strandi101 – 1033
    Helixi104 – 1096
    Beta strandi113 – 1208
    Beta strandi133 – 1364
    Helixi137 – 1393
    Beta strandi141 – 1444
    Helixi153 – 1619
    Helixi164 – 1729
    Beta strandi177 – 1815
    Helixi190 – 20112
    Helixi202 – 2043
    Beta strandi206 – 2127
    Helixi220 – 2245
    Helixi226 – 24116
    Helixi245 – 2473
    Beta strandi250 – 2556
    Helixi261 – 27414
    Beta strandi278 – 2814
    Turni295 – 2984
    Beta strandi299 – 3057
    Helixi306 – 3083
    Helixi309 – 32214
    Turni323 – 3253
    Beta strandi329 – 3346
    Helixi338 – 34710
    Beta strandi350 – 3556
    Helixi356 – 3616
    Helixi365 – 37915
    Helixi385 – 3884
    Helixi391 – 3933

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D3GX-ray1.60A29-395[»]
    1D3HX-ray1.80A29-395[»]
    2B0MX-ray2.00A29-395[»]
    2BXVX-ray2.15A29-395[»]
    2FPTX-ray2.40A29-395[»]
    2FPVX-ray1.80A29-395[»]
    2FPYX-ray2.00A29-395[»]
    2FQIX-ray1.95A29-395[»]
    2PRHX-ray2.40A29-395[»]
    2PRLX-ray2.10A29-395[»]
    2PRMX-ray3.00A29-395[»]
    2WV8X-ray1.90A31-395[»]
    3F1QX-ray2.00A29-395[»]
    3FJ6X-ray1.80A29-395[»]
    3FJLX-ray1.90A29-395[»]
    3G0UX-ray2.00A29-395[»]
    3G0XX-ray1.80A29-395[»]
    3KVJX-ray1.94A29-395[»]
    3KVKX-ray2.05A29-395[»]
    3KVLX-ray1.85A29-395[»]
    3KVMX-ray2.00A29-395[»]
    3U2OX-ray2.18A1-395[»]
    3W7RX-ray1.68A29-395[»]
    3ZWSX-ray1.60A29-395[»]
    3ZWTX-ray1.55A29-395[»]
    4IGHX-ray1.30A32-395[»]
    4JGDX-ray2.05A29-395[»]
    4JS3X-ray2.00A29-395[»]
    4JTSX-ray2.21A29-395[»]
    4JTTX-ray2.10A29-395[»]
    4JTUX-ray1.90A29-395[»]
    4OQVX-ray1.23A32-395[»]
    ProteinModelPortaliQ02127.
    SMRiQ02127. Positions 29-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02127.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1010Mitochondrial matrixBy similarity
    Topological domaini31 – 395365Mitochondrial intermembraneBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3020HelicalBy similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 1485Substrate binding
    Regioni211 – 2166Substrate binding
    Regioni283 – 2842Substrate binding

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0167.
    HOGENOMiHOG000225103.
    HOVERGENiHBG006898.
    InParanoidiQ02127.
    KOiK00254.
    OMAiVTDIVAM.
    PhylomeDBiQ02127.
    TreeFamiTF105973.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR012135. Dihydroorotate_DH_1_2.
    IPR005719. Dihydroorotate_DH_2.
    IPR001295. Dihydroorotate_DH_CS.
    [Graphical view]
    PfamiPF01180. DHO_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
    TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
    PROSITEiPS00911. DHODEHASE_1. 1 hit.
    PS00912. DHODEHASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q02127-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWRHLKKRA QDAVIILGGG GLLFASYLMA TGDERFYAEH LMPTLQGLLD    50
    PESAHRLAVR FTSLGLLPRA RFQDSDMLEV RVLGHKFRNP VGIAAGFDKH 100
    GEAVDGLYKM GFGFVEIGSV TPKPQEGNPR PRVFRLPEDQ AVINRYGFNS 150
    HGLSVVEHRL RARQQKQAKL TEDGLPLGVN LGKNKTSVDA AEDYAEGVRV 200
    LGPLADYLVV NVSSPNTAGL RSLQGKAELR RLLTKVLQER DGLRRVHRPA 250
    VLVKIAPDLT SQDKEDIASV VKELGIDGLI VTNTTVSRPA GLQGALRSET 300
    GGLSGKPLRD LSTQTIREMY ALTQGRVPII GVGGVSSGQD ALEKIRAGAS 350
    LVQLYTALTF WGPPVVGKVK RELEALLKEQ GFGGVTDAIG ADHRR 395
    Length:395
    Mass (Da):42,867
    Last modified:December 7, 2004 - v3
    Checksum:i072C3169E78C6440
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 22MA → KLP in AAA50163. (PubMed:1446837)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71K → Q.2 Publications
    Corresponds to variant rs3213422 [ dbSNP | Ensembl ].
    VAR_022094
    Natural varianti19 – 191G → E in POADS. 1 Publication
    VAR_062412
    Natural varianti135 – 1351R → C in POADS. 1 Publication
    VAR_062413
    Natural varianti152 – 1521G → R in POADS. 1 Publication
    VAR_062414
    Natural varianti199 – 1991R → C in POADS. 1 Publication
    VAR_062415
    Natural varianti202 – 2021G → A in POADS. 1 Publication
    VAR_062416
    Natural varianti202 – 2021G → D in POADS. 1 Publication
    VAR_062417
    Natural varianti244 – 2441R → W in POADS. 1 Publication
    VAR_062418
    Natural varianti284 – 2841T → I in POADS. 1 Publication
    VAR_062419
    Natural varianti346 – 3461R → W in POADS. 1 Publication
    VAR_062420
    Natural varianti392 – 3921D → G in POADS. 1 Publication
    VAR_062421

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94065 mRNA. Translation: AAA50163.1.
    AK292293 mRNA. Translation: BAF84982.1.
    BC065245 mRNA. Translation: AAH65245.1.
    CCDSiCCDS42192.1.
    PIRiPC1219.
    RefSeqiNP_001352.2. NM_001361.4.
    UniGeneiHs.654427.

    Genome annotation databases

    EnsembliENST00000219240; ENSP00000219240; ENSG00000102967.
    GeneIDi1723.
    KEGGihsa:1723.
    UCSCiuc002fbp.3. human.

    Polymorphism databases

    DMDMi56405372.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M94065 mRNA. Translation: AAA50163.1 .
    AK292293 mRNA. Translation: BAF84982.1 .
    BC065245 mRNA. Translation: AAH65245.1 .
    CCDSi CCDS42192.1.
    PIRi PC1219.
    RefSeqi NP_001352.2. NM_001361.4.
    UniGenei Hs.654427.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D3G X-ray 1.60 A 29-395 [» ]
    1D3H X-ray 1.80 A 29-395 [» ]
    2B0M X-ray 2.00 A 29-395 [» ]
    2BXV X-ray 2.15 A 29-395 [» ]
    2FPT X-ray 2.40 A 29-395 [» ]
    2FPV X-ray 1.80 A 29-395 [» ]
    2FPY X-ray 2.00 A 29-395 [» ]
    2FQI X-ray 1.95 A 29-395 [» ]
    2PRH X-ray 2.40 A 29-395 [» ]
    2PRL X-ray 2.10 A 29-395 [» ]
    2PRM X-ray 3.00 A 29-395 [» ]
    2WV8 X-ray 1.90 A 31-395 [» ]
    3F1Q X-ray 2.00 A 29-395 [» ]
    3FJ6 X-ray 1.80 A 29-395 [» ]
    3FJL X-ray 1.90 A 29-395 [» ]
    3G0U X-ray 2.00 A 29-395 [» ]
    3G0X X-ray 1.80 A 29-395 [» ]
    3KVJ X-ray 1.94 A 29-395 [» ]
    3KVK X-ray 2.05 A 29-395 [» ]
    3KVL X-ray 1.85 A 29-395 [» ]
    3KVM X-ray 2.00 A 29-395 [» ]
    3U2O X-ray 2.18 A 1-395 [» ]
    3W7R X-ray 1.68 A 29-395 [» ]
    3ZWS X-ray 1.60 A 29-395 [» ]
    3ZWT X-ray 1.55 A 29-395 [» ]
    4IGH X-ray 1.30 A 32-395 [» ]
    4JGD X-ray 2.05 A 29-395 [» ]
    4JS3 X-ray 2.00 A 29-395 [» ]
    4JTS X-ray 2.21 A 29-395 [» ]
    4JTT X-ray 2.10 A 29-395 [» ]
    4JTU X-ray 1.90 A 29-395 [» ]
    4OQV X-ray 1.23 A 32-395 [» ]
    ProteinModelPortali Q02127.
    SMRi Q02127. Positions 29-395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108068. 13 interactions.
    IntActi Q02127. 2 interactions.
    STRINGi 9606.ENSP00000219240.

    Chemistry

    BindingDBi Q02127.
    ChEMBLi CHEMBL1966.
    DrugBanki DB01117. Atovaquone.
    DB01097. Leflunomide.
    GuidetoPHARMACOLOGYi 2604.

    PTM databases

    PhosphoSitei Q02127.

    Polymorphism databases

    DMDMi 56405372.

    Proteomic databases

    MaxQBi Q02127.
    PaxDbi Q02127.
    PRIDEi Q02127.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219240 ; ENSP00000219240 ; ENSG00000102967 .
    GeneIDi 1723.
    KEGGi hsa:1723.
    UCSCi uc002fbp.3. human.

    Organism-specific databases

    CTDi 1723.
    GeneCardsi GC16P072042.
    HGNCi HGNC:2867. DHODH.
    HPAi HPA010123.
    HPA011942.
    MIMi 126064. gene.
    263750. phenotype.
    neXtProti NX_Q02127.
    Orphaneti 246. Postaxial acrofacial dysostosis.
    PharmGKBi PA27327.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0167.
    HOGENOMi HOG000225103.
    HOVERGENi HBG006898.
    InParanoidi Q02127.
    KOi K00254.
    OMAi VTDIVAM.
    PhylomeDBi Q02127.
    TreeFami TF105973.

    Enzyme and pathway databases

    UniPathwayi UPA00070 ; UER00946 .
    Reactomei REACT_21376. Pyrimidine biosynthesis.
    SABIO-RK Q02127.

    Miscellaneous databases

    EvolutionaryTracei Q02127.
    GenomeRNAii 1723.
    NextBioi 6971.
    PROi Q02127.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02127.
    Bgeei Q02127.
    CleanExi HS_DHODH.
    Genevestigatori Q02127.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR012135. Dihydroorotate_DH_1_2.
    IPR005719. Dihydroorotate_DH_2.
    IPR001295. Dihydroorotate_DH_CS.
    [Graphical view ]
    Pfami PF01180. DHO_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000164. DHO_oxidase. 1 hit.
    TIGRFAMsi TIGR01036. pyrD_sub2. 1 hit.
    PROSITEi PS00911. DHODEHASE_1. 1 hit.
    PS00912. DHODEHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a human cDNA coding for dihydroorotate dehydrogenase by complementation of the corresponding yeast mutant."
      Minet M., Dufour M.E., Lacroute F.
      Gene 121:393-396(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-7.
    2. "Recombinant human dihydroorotate dehydrogenase: expression, purification, and characterization of a catalytically functional truncated enzyme."
      Copeland R.A., Davis J.P., Dowling R.L., Lombardo D., Murphy K.B., Patterson T.A.
      Arch. Biochem. Biophys. 323:79-86(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-7.
      Tissue: Testis.
    4. "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].
      Tissue: Skin.
    5. "Functional expression of a fragment of human dihydroorotate dehydrogenase by means of the baculovirus expression vector system, and kinetic investigation of the purified recombinant enzyme."
      Knecht W., Bergjohann U., Gonski S., Kirschbaum B., Loeffler M.
      Eur. J. Biochem. 240:292-301(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY.
    6. "Requirements for the mitochondrial import and localization of dihydroorotate dehydrogenase."
      Rawls J., Knecht W., Diekert K., Lill R., Loeffler M.
      Eur. J. Biochem. 267:2079-2087(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents."
      Liu S., Neidhardt E.A., Grossman T.H., Ocain T., Clardy J.
      Structure 8:25-33(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-395 IN COMPLEX WITH FMN; DIHYDROOROTATE AND INHIBITORS, COFACTOR.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-395 IN COMPLEX WITH FMN AND INHIBITORS.
    10. Cited for: VARIANTS POADS GLU-19; CYS-135; ARG-152; CYS-199; ALA-202; ASP-202; TRP-244; ILE-284; TRP-346 AND GLY-392.

    Entry informationi

    Entry nameiPYRD_HUMAN
    AccessioniPrimary (citable) accession number: Q02127
    Secondary accession number(s): A8K8C8, Q6P176
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 153 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

    Miscellaneous

    The identification of DHODH defects as the cause of postaxial acrofacial dysostosis (POADS) was obtained via exome sequencing (PubMed:19915526), demonstrating that this method is a powerful tool for identifying genes underlying rare Mendelian disorders. Exome sequencing consists of targeted resequencing of all protein-coding subsequences, which requires around 5% as much sequencing as a whole human genome.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3