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Q02127

- PYRD_HUMAN

UniProt

Q02127 - PYRD_HUMAN

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Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene
DHODH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1191FMN
Binding sitei180 – 1801FMN
Binding sitei211 – 2111FMN
Active sitei214 – 2141Nucleophile
Binding sitei254 – 2541FMN
Binding sitei282 – 2821FMN; via carbonyl oxygen
Binding sitei305 – 3051FMN; via amide nitrogen
Binding sitei334 – 3341FMN; via amide nitrogen

Regions

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

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
Complete GO annotation...

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; Single-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010Mitochondrial matrix By similarity
Transmembranei11 – 3020Helical; By similarityAdd
BLAST
Topological domaini31 – 395365Mitochondrial intermembrane By similarityAdd
BLAST

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 cleaved By 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.

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.

Miscellaneous databases

EvolutionaryTraceiQ02127.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22MA → KLP in AAA50163. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 152 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 (1 Publication), 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.

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

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