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Entry version 197 (08 May 2019)
Sequence version 3 (07 Dec 2004)
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Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene

DHODH

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>

<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 conversion of dihydroorotate to orotate with quinone as electron acceptor.

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

FMN1 PublicationNote: Binds 1 FMN per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route).
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydroorotate dehydrogenase (quinone), mitochondrial (DHODH), Dihydroorotate dehydrogenase (quinone), mitochondrial (DHODH)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route), the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei99Substrate1
Binding sitei119FMN2 Publications1
Binding sitei180FMN2 Publications1
Binding sitei211FMN2 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei214Nucleophile1
Binding sitei254FMN2 Publications1
Binding sitei282FMN; via carbonyl oxygen2 Publications1
Binding sitei305FMN; via amide nitrogen2 Publications1
Binding sitei334FMN; via amide nitrogen2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi95 – 99FMN2 Publications5
Nucleotide bindingi355 – 356FMN2 Publications2

<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

  • dihydroorotate dehydrogenase activity Source: GO_Central
  • drug binding Source: Ensembl
  • FMN binding Source: Ensembl
  • ubiquinone binding Source: Ensembl

GO - Biological processi

<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 functionOxidoreductase
Biological processPyrimidine biosynthesis
LigandFlavoprotein, FMN

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.5.2 2681
1.3.98.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-500753 Pyrimidine biosynthesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q02127

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00070;UER00946

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrial (EC:1.3.5.2)
Short name:
DHOdehase
Alternative name(s):
Dihydroorotate oxidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DHODH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2867 DHODH

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
126064 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q02127

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 10Mitochondrial matrixBy similarity10
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei11 – 30HelicalBy similarityAdd BLAST20
Topological domaini31 – 395Mitochondrial intermembraneBy similarityAdd BLAST365

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

<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

Postaxial acrofacial dysostosis (POADS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionPOADS 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.
See also OMIM:263750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_06241219G → E in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606765EnsemblClinVar.1
Natural variantiVAR_062413135R → C in POADS. 1 PublicationCorresponds to variant dbSNP:rs201230446EnsemblClinVar.1
Natural variantiVAR_062414152G → R in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606766EnsemblClinVar.1
Natural variantiVAR_062415199R → C in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606769EnsemblClinVar.1
Natural variantiVAR_062416202G → A in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606767EnsemblClinVar.1
Natural variantiVAR_062417202G → D in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606767EnsemblClinVar.1
Natural variantiVAR_062418244R → W in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606768EnsemblClinVar.1
Natural variantiVAR_062419284T → I in POADS. 1 Publication1
Natural variantiVAR_062420346R → W in POADS. 1 PublicationCorresponds to variant dbSNP:rs201947120EnsemblClinVar.1
Natural variantiVAR_062421392D → G in POADS. 1 PublicationCorresponds to variant dbSNP:rs779076692Ensembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
1723

MalaCards human disease database

More...
MalaCardsi
DHODH
MIMi263750 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000102967

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
246 Postaxial acrofacial dysostosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27327

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1966

Drug and drug target database

More...
DrugBanki
DB07561 (2Z)-2-cyano-N-(3'-ethoxybiphenyl-4-yl)-3-hydroxybut-2-enamide
DB08172 (2Z)-N-(3-chloro-2'-methoxybiphenyl-4-yl)-2-cyano-3-hydroxybut-2-enamide
DB08169 (2Z)-N-biphenyl-4-yl-2-cyano-3-cyclopropyl-3-hydroxyprop-2-enamide
DB07443 (2Z)-N-biphenyl-4-yl-2-cyano-3-hydroxybut-2-enamide
DB07976 3-{[(3-FLUORO-3'-METHOXYBIPHENYL-4-YL)AMINO]CARBONYL}THIOPHENE-2-CARBOXYLIC ACID
DB03805 Antiproliferative Agent A771726
DB01117 Atovaquone
DB03480 Brequinar Analog
DB04147 Lauryl Dimethylamine-N-Oxide
DB01097 Leflunomide
DB02262 Orotic Acid
DB03247 Riboflavin Monophosphate
DB05125 SC12267
DB08880 Teriflunomide

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2604

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
DHODH

Domain mapping of disease mutations (DMDM)

More...
DMDMi
56405372

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000298841 – 395Dihydroorotate dehydrogenase (quinone), mitochondrialAdd BLAST395
<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 peptidei1 – 10Mitochondrion; not cleavedBy similarity10

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q02127

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q02127

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q02127

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q02127

PeptideAtlas

More...
PeptideAtlasi
Q02127

PRoteomics IDEntifications database

More...
PRIDEi
Q02127

ProteomicsDB human proteome resource

More...
ProteomicsDBi
58051

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
Q02127

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q02127

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q02127

<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
ENSG00000102967 Expressed in 124 organ(s), highest expression level in right lobe of liver

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q02127 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q02127 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA010123
HPA011942

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108068, 24 interactors

Protein interaction database and analysis system

More...
IntActi
Q02127, 4 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000219240

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q02127

<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

1395
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
4LS0X-ray2.07A29-395[»]
4LS1X-ray2.20A29-395[»]
4LS2X-ray2.27A29-395[»]
4OQVX-ray1.23A32-395[»]
4RK8X-ray2.22A29-395[»]
4RKAX-ray2.71A29-395[»]
4RLIX-ray2.50A29-395[»]
4RR4X-ray2.38A29-395[»]
4YLWX-ray1.79A29-395[»]
4ZL1X-ray1.86A29-395[»]
4ZMGX-ray1.90A29-395[»]
5H2ZX-ray1.58A29-395[»]
5H73X-ray1.58A29-395[»]
5HINX-ray1.60A29-395[»]
5HQEX-ray1.62A29-395[»]
5K9CX-ray1.66A29-395[»]
5K9DX-ray1.70A29-395[»]
5MUTX-ray1.75A31-395[»]
5MVCX-ray1.85A29-395[»]
5MVDX-ray1.95A33-395[»]
5TCENMR-A32-65[»]
5ZF4X-ray1.66A29-395[»]
5ZF7X-ray1.79A29-395[»]
5ZF8X-ray1.70A29-395[»]
5ZF9X-ray1.77A29-395[»]
5ZFAX-ray1.75A29-395[»]
5ZFBX-ray2.00A29-395[»]
6CJFX-ray1.63A/B32-395[»]
6CJGX-ray2.85A32-395[»]
6ET4X-ray1.70A29-395[»]
6FMDX-ray1.58A1-395[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q02127

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q02127

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni144 – 148Substrate binding5
Regioni211 – 216Substrate binding6
Regioni283 – 284Substrate binding2

<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

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1436 Eukaryota
COG0167 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00500000044924

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000225103

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q02127

KEGG Orthology (KO)

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KOi
K00254

Identification of Orthologs from Complete Genome Data

More...
OMAi
ALNRMGF

Database of Orthologous Groups

More...
OrthoDBi
1194348at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q02127

TreeFam database of animal gene trees

More...
TreeFami
TF105973

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04738 DHOD_2_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785 Aldolase_TIM
IPR005720 Dihydroorotate_DH
IPR005719 Dihydroorotate_DH_2
IPR001295 Dihydroorotate_DH_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01180 DHO_dh, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01036 pyrD_sub2, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00911 DHODEHASE_1, 1 hit
PS00912 DHODEHASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q02127-1 [UniParc]FASTAAdd to basket
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        10         20         30         40         50
MAWRHLKKRA QDAVIILGGG GLLFASYLMA TGDERFYAEH LMPTLQGLLD
60 70 80 90 100
PESAHRLAVR FTSLGLLPRA RFQDSDMLEV RVLGHKFRNP VGIAAGFDKH
110 120 130 140 150
GEAVDGLYKM GFGFVEIGSV TPKPQEGNPR PRVFRLPEDQ AVINRYGFNS
160 170 180 190 200
HGLSVVEHRL RARQQKQAKL TEDGLPLGVN LGKNKTSVDA AEDYAEGVRV
210 220 230 240 250
LGPLADYLVV NVSSPNTAGL RSLQGKAELR RLLTKVLQER DGLRRVHRPA
260 270 280 290 300
VLVKIAPDLT SQDKEDIASV VKELGIDGLI VTNTTVSRPA GLQGALRSET
310 320 330 340 350
GGLSGKPLRD LSTQTIREMY ALTQGRVPII GVGGVSSGQD ALEKIRAGAS
360 370 380 390
LVQLYTALTF WGPPVVGKVK RELEALLKEQ GFGGVTDAIG ADHRR
Length:395
Mass (Da):42,867
Last modified:December 7, 2004 - 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:i072C3169E78C6440
GO

<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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I3NI32I3NI32_HUMAN
Dihydroorotate dehydrogenase (quino...
DHODH
393Annotation score:

Annotation score:3 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>
I3L449I3L449_HUMAN
Dihydroorotate dehydrogenase (quino...
DHODH
193Annotation score:

Annotation score:2 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>
J3QRQ3J3QRQ3_HUMAN
Dihydroorotate dehydrogenase (quino...
DHODH
144Annotation 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>
J3QRJ4J3QRJ4_HUMAN
Dihydroorotate dehydrogenase (quino...
DHODH
76Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti1 – 2MA → KLP in AAA50163 (PubMed:1446837).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0220947K → Q2 PublicationsCorresponds to variant dbSNP:rs3213422EnsemblClinVar.1
Natural variantiVAR_06241219G → E in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606765EnsemblClinVar.1
Natural variantiVAR_062413135R → C in POADS. 1 PublicationCorresponds to variant dbSNP:rs201230446EnsemblClinVar.1
Natural variantiVAR_062414152G → R in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606766EnsemblClinVar.1
Natural variantiVAR_062415199R → C in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606769EnsemblClinVar.1
Natural variantiVAR_062416202G → A in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606767EnsemblClinVar.1
Natural variantiVAR_062417202G → D in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606767EnsemblClinVar.1
Natural variantiVAR_062418244R → W in POADS. 1 PublicationCorresponds to variant dbSNP:rs267606768EnsemblClinVar.1
Natural variantiVAR_062419284T → I in POADS. 1 Publication1
Natural variantiVAR_062420346R → W in POADS. 1 PublicationCorresponds to variant dbSNP:rs201947120EnsemblClinVar.1
Natural variantiVAR_062421392D → G in POADS. 1 PublicationCorresponds to variant dbSNP:rs779076692Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M94065 mRNA Translation: AAA50163.1
AK292293 mRNA Translation: BAF84982.1
BC065245 mRNA Translation: AAH65245.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS42192.1

Protein sequence database of the Protein Information Resource

More...
PIRi
PC1219

NCBI Reference Sequences

More...
RefSeqi
NP_001352.2, NM_001361.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000219240; ENSP00000219240; ENSG00000102967

Database of genes from NCBI RefSeq genomes

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GeneIDi
1723

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1723

UCSC genome browser

More...
UCSCi
uc002fbp.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
M94065 mRNA Translation: AAA50163.1
AK292293 mRNA Translation: BAF84982.1
BC065245 mRNA Translation: AAH65245.1
CCDSiCCDS42192.1
PIRiPC1219
RefSeqiNP_001352.2, NM_001361.4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4LS0X-ray2.07A29-395[»]
4LS1X-ray2.20A29-395[»]
4LS2X-ray2.27A29-395[»]
4OQVX-ray1.23A32-395[»]
4RK8X-ray2.22A29-395[»]
4RKAX-ray2.71A29-395[»]
4RLIX-ray2.50A29-395[»]
4RR4X-ray2.38A29-395[»]
4YLWX-ray1.79A29-395[»]
4ZL1X-ray1.86A29-395[»]
4ZMGX-ray1.90A29-395[»]
5H2ZX-ray1.58A29-395[»]
5H73X-ray1.58A29-395[»]
5HINX-ray1.60A29-395[»]
5HQEX-ray1.62A29-395[»]
5K9CX-ray1.66A29-395[»]
5K9DX-ray1.70A29-395[»]
5MUTX-ray1.75A31-395[»]
5MVCX-ray1.85A29-395[»]
5MVDX-ray1.95A33-395[»]
5TCENMR-A32-65[»]
5ZF4X-ray1.66A29-395[»]
5ZF7X-ray1.79A29-395[»]
5ZF8X-ray1.70A29-395[»]
5ZF9X-ray1.77A29-395[»]
5ZFAX-ray1.75A29-395[»]
5ZFBX-ray2.00A29-395[»]
6CJFX-ray1.63A/B32-395[»]
6CJGX-ray2.85A32-395[»]
6ET4X-ray1.70A29-395[»]
6FMDX-ray1.58A1-395[»]
SMRiQ02127
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108068, 24 interactors
IntActiQ02127, 4 interactors
STRINGi9606.ENSP00000219240

Chemistry databases

BindingDBiQ02127
ChEMBLiCHEMBL1966
DrugBankiDB07561 (2Z)-2-cyano-N-(3'-ethoxybiphenyl-4-yl)-3-hydroxybut-2-enamide
DB08172 (2Z)-N-(3-chloro-2'-methoxybiphenyl-4-yl)-2-cyano-3-hydroxybut-2-enamide
DB08169 (2Z)-N-biphenyl-4-yl-2-cyano-3-cyclopropyl-3-hydroxyprop-2-enamide
DB07443 (2Z)-N-biphenyl-4-yl-2-cyano-3-hydroxybut-2-enamide
DB07976 3-{[(3-FLUORO-3'-METHOXYBIPHENYL-4-YL)AMINO]CARBONYL}THIOPHENE-2-CARBOXYLIC ACID
DB03805 Antiproliferative Agent A771726
DB01117 Atovaquone
DB03480 Brequinar Analog
DB04147 Lauryl Dimethylamine-N-Oxide
DB01097 Leflunomide
DB02262 Orotic Acid
DB03247 Riboflavin Monophosphate
DB05125 SC12267
DB08880 Teriflunomide
GuidetoPHARMACOLOGYi2604

PTM databases

iPTMnetiQ02127
PhosphoSitePlusiQ02127

Polymorphism and mutation databases

BioMutaiDHODH
DMDMi56405372

Proteomic databases

EPDiQ02127
jPOSTiQ02127
MaxQBiQ02127
PaxDbiQ02127
PeptideAtlasiQ02127
PRIDEiQ02127
ProteomicsDBi58051
TopDownProteomicsiQ02127

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219240; ENSP00000219240; ENSG00000102967
GeneIDi1723
KEGGihsa:1723
UCSCiuc002fbp.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1723
DisGeNETi1723

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DHODH
HGNCiHGNC:2867 DHODH
HPAiHPA010123
HPA011942
MalaCardsiDHODH
MIMi126064 gene
263750 phenotype
neXtProtiNX_Q02127
OpenTargetsiENSG00000102967
Orphaneti246 Postaxial acrofacial dysostosis
PharmGKBiPA27327

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1436 Eukaryota
COG0167 LUCA
GeneTreeiENSGT00500000044924
HOGENOMiHOG000225103
InParanoidiQ02127
KOiK00254
OMAiALNRMGF
OrthoDBi1194348at2759
PhylomeDBiQ02127
TreeFamiTF105973

Enzyme and pathway databases

UniPathwayi
UPA00070;UER00946

BRENDAi1.3.5.2 2681
1.3.98.1 2681
ReactomeiR-HSA-500753 Pyrimidine biosynthesis
SABIO-RKiQ02127

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
DHODH human
EvolutionaryTraceiQ02127

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
1723

Protein Ontology

More...
PROi
PR:Q02127

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000102967 Expressed in 124 organ(s), highest expression level in right lobe of liver
ExpressionAtlasiQ02127 baseline and differential
GenevisibleiQ02127 HS

Family and domain databases

CDDicd04738 DHOD_2_like, 1 hit
Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR005720 Dihydroorotate_DH
IPR005719 Dihydroorotate_DH_2
IPR001295 Dihydroorotate_DH_CS
PfamiView protein in Pfam
PF01180 DHO_dh, 1 hit
TIGRFAMsiTIGR01036 pyrD_sub2, 1 hit
PROSITEiView protein in PROSITE
PS00911 DHODEHASE_1, 1 hit
PS00912 DHODEHASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPYRD_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>AccessioniPrimary (citable) accession number: Q02127
Secondary accession number(s): A8K8C8, Q6P176
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 7, 2004
Last modified: May 8, 2019
This is version 197 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 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.

<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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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