Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CAD protein

Gene

CAD

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

This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).1 Publication

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).Curated

<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

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an activator while UMP and UTP are inhibitors of the CPSase reaction.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=28 µM for dihydroorotate1 Publication
  2. KM=241 µM for N-carbamoyl-L-aspartate1 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, 2 and 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. CAD protein (CAD)
    2. CAD protein (CAD)
    3. CAD protein (CAD)
    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 (S)-dihydroorotate from bicarbonate, 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei252Nucleophile; for GATase activityPROSITE-ProRule annotation1
    Active sitei336For GATase activityPROSITE-ProRule annotation1
    Active sitei338For GATase activityPROSITE-ProRule annotation1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi668Magnesium or manganese 1PROSITE-ProRule annotation1
    Metal bindingi682Magnesium or manganese 1PROSITE-ProRule annotation1
    Metal bindingi682Magnesium or manganese 2PROSITE-ProRule annotation1
    Metal bindingi684Magnesium or manganese 2PROSITE-ProRule annotation1
    Metal bindingi1202Magnesium or manganese 3PROSITE-ProRule annotation1
    Metal bindingi1214Magnesium or manganese 3PROSITE-ProRule annotation1
    Metal bindingi1214Magnesium or manganese 4PROSITE-ProRule annotation1
    Metal bindingi1216Magnesium or manganese 4PROSITE-ProRule annotation1
    Metal bindingi1471Zinc 1; via tele nitrogen1 Publication1
    Metal bindingi1471Zinc 2; via pros nitrogen1 Publication1
    Metal bindingi1473Zinc 1; via tele nitrogen1 Publication1
    <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 sitei1475N-carbamoyl-L-aspartate1 Publication1
    Binding sitei1505N-carbamoyl-L-aspartate1 Publication1
    Metal bindingi1556Zinc 1; via carbamate group1 Publication1
    Metal bindingi1556Zinc 3; via carbamate group1 Publication1
    Metal bindingi1590Zinc 3; via pros nitrogen1 Publication1
    Metal bindingi1613Zinc 21 Publication1
    Metal bindingi1614Zinc 3; via tele nitrogen1 Publication1
    Metal bindingi1637Zinc 21 Publication1
    Binding sitei1661N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygen1 Publication1
    Metal bindingi1686Zinc 11 Publication1
    Binding sitei1686N-carbamoyl-L-aspartate1 Publication1
    Binding sitei1690N-carbamoyl-L-aspartate1 Publication1

    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 bindingi545 – 600ATPPROSITE-ProRule annotationAdd BLAST56
    Nucleotide bindingi1078 – 1135ATPPROSITE-ProRule annotationAdd BLAST58

    <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

    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 functionAllosteric enzyme, Hydrolase, Ligase, Multifunctional enzyme, Transferase
    Biological processPyrimidine biosynthesis
    LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:ENSG00000084774-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.2.3 2681

    Reactome - a knowledgebase of biological pathways and processes

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

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P27708

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

    More...
    UniPathwayi
    UPA00070;UER00115

    UPA00070;UER00116

    UPA00070;UER00117

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    M38.972

    <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:
    CAD protein
    Including the following 3 domains:
    Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.51 Publication)
    Aspartate carbamoyltransferase (EC:2.1.3.21 Publication)
    Dihydroorotase (EC:3.5.2.31 Publication)
    <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:CADImported
    <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 2

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000084774.13

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:1424 CAD

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    114010 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P27708

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    <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

    Epileptic encephalopathy, early infantile, 50 (EIEE50)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE50 is an autosomal recessive, progressive disease with onset in infancy and favorable response to treatment with oral uridine.
    See also OMIM:616457
    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_07828933M → R in EIEE50; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs751610198EnsemblClinVar.1
    Natural variantiVAR_0782901789 – 2225Missing in EIEE50; unknown pathological significance. 1 PublicationAdd BLAST437
    Natural variantiVAR_0739552024R → Q in EIEE50. 1 PublicationCorresponds to variant dbSNP:rs763410987Ensembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1471H → A: No zinc-binding and no catalytic activity. 2 Publications1
    Mutagenesisi1471H → N: Abolishes dihydroorotase activity. 2 Publications1
    Mutagenesisi1473H → A: No zinc-binding and no catalytic activity. 1 Publication1
    Mutagenesisi1512D → N: No change in catalytic activity. 1 Publication1
    Mutagenesisi1562T → A: Abolishes dihydroorotase activity. 1 Publication1
    Mutagenesisi1563F → A: Abolishes dihydroorotase activity. 1 Publication1
    Mutagenesisi1590H → A: Abolishes dihydroorotase activity. 2 Publications1
    Mutagenesisi1590H → N: No catalytic activity. 2 Publications1
    Mutagenesisi1613C → S: Reduces dihydroorotase activity. 1 Publication1
    Mutagenesisi1614H → A: Abolishes dihydroorotase activity. 1 Publication1
    Mutagenesisi1637E → T: Abolishes dihydroorotase activity. 1 Publication1
    Mutagenesisi1642H → N: 11.5% of wild-type catalytic activity. 1 Publication1
    Mutagenesisi1686D → N: Abolishes dihydroorotase activity. 1 Publication1
    Mutagenesisi1690H → N: 3% of wild-type catalytic activity. 1 Publication1
    Mutagenesisi1873S → A: Abolishes PMA-induced Thr-456 phosphorylation. 1 Publication1

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation, Epilepsy

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    790

    MalaCards human disease database

    More...
    MalaCardsi
    CAD
    MIMi616457 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000084774

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

    More...
    Orphaneti
    448010 CAD-CDG

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA26023

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3093

    Drug and drug target database

    More...
    DrugBanki
    DB00128 L-Aspartic Acid
    DB00130 L-Glutamine
    DB03459 Sparfosic acid

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    CAD

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    50403731

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
    <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_00001995062 – 2225CAD proteinAdd BLAST2224

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
    Modified residuei456Phosphothreonine; by MAPK11 Publication1
    Modified residuei747N6-acetyllysineCombined sources1
    Modified residuei1038PhosphoserineCombined sources1
    Modified residuei1406Phosphoserine; by PKACombined sources1 Publication1
    Modified residuei1411N6-acetyllysineCombined sources1
    Modified residuei1556N6-carboxylysine1 Publication1
    Modified residuei1859Phosphoserine; by RPS6KB1 and PKACombined sources3 Publications1
    Modified residuei1873Phosphoserine; by PKC; in vitro1 Publication1
    Modified residuei1884PhosphothreonineCombined sources1
    Modified residuei1900PhosphoserineCombined sources1 Publication1
    Modified residuei1938PhosphoserineCombined sources1

    <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

    Activated by MAP kinase (Erk1/2) phosphorylation just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes oligomerization and stimulates dihydroorotase activity. Phosphorylation at Ser-1406 reduces sensitivy to feedback inhibition by UTP.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P27708

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P27708

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

    More...
    PaxDbi
    P27708

    PeptideAtlas

    More...
    PeptideAtlasi
    P27708

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P27708

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    54409

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P27708

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

    More...
    PhosphoSitePlusi
    P27708

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P27708

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...
    PMAP-CutDBi
    P27708

    <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

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Transcriptionally repressed following hypoxia by HIF1A.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000084774 Expressed in 170 organ(s), highest expression level in right lobe of liver

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_CAD

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P27708 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P27708 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB007781
    HPA057266
    HPA069341

    <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

    Homohexamer (PubMed:24332717). Interacts with CIPC (PubMed:26657846).2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-355504,EBI-355504

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    107243, 129 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-39484N

    Protein interaction database and analysis system

    More...
    IntActi
    P27708, 53 interactors

    Molecular INTeraction database

    More...
    MINTi
    P27708

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000264705

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P27708

    <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

    12225
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Database of protein disorder

    More...
    DisProti
    DP01024

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P27708

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

    More...
    SMRi
    P27708

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini177 – 363Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST187
    Domaini519 – 711ATP-grasp 1PROSITE-ProRule annotationAdd BLAST193
    Domaini1052 – 1243ATP-grasp 2PROSITE-ProRule annotationAdd BLAST192
    Domaini1308 – 1462MGS-likePROSITE-ProRule annotationAdd BLAST155

    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>Regioni2 – 365GATase (Glutamine amidotransferase)By similarityAdd BLAST364
    Regioni366 – 394LinkerBy similarityAdd BLAST29
    Regioni395 – 1455CPSase (Carbamoyl-phosphate synthase)By similarityAdd BLAST1061
    Regioni395 – 933CPSase ABy similarityAdd BLAST539
    Regioni934 – 1455CPSase BBy similarityAdd BLAST522
    Regioni1456 – 1788DHOase (dihydroorotase)By similarityAdd BLAST333
    Regioni1789 – 1917LinkerBy similarityAdd BLAST129
    Regioni1918 – 2225ATCase (Aspartate transcarbamylase)By similarityAdd BLAST308

    <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

    In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0370 Eukaryota
    COG0458 LUCA
    COG0505 LUCA
    COG0540 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157241

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000234584

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG000279

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P27708

    KEGG Orthology (KO)

    More...
    KOi
    K11540

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G00DC

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P27708

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105604

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01744 GATase1_CPSase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.1030.10, 1 hit
    3.30.1490.20, 1 hit
    3.40.50.1370, 2 hits
    3.40.50.1380, 1 hit
    3.40.50.880, 1 hit
    3.50.30.20, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00001 Asp_carb_tr, 1 hit
    MF_01209 CPSase_S_chain, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006680 Amidohydro-rel
    IPR006132 Asp/Orn_carbamoyltranf_P-bd
    IPR006130 Asp/Orn_carbamoylTrfase
    IPR036901 Asp/Orn_carbamoylTrfase_sf
    IPR002082 Asp_carbamoyltransf
    IPR006131 Asp_carbamoyltransf_Asp/Orn-bd
    IPR011761 ATP-grasp
    IPR013815 ATP_grasp_subdomain_1
    IPR006275 CarbamoylP_synth_lsu
    IPR005480 CarbamoylP_synth_lsu_oligo
    IPR036897 CarbamoylP_synth_lsu_oligo_sf
    IPR006274 CarbamoylP_synth_ssu
    IPR002474 CarbamoylP_synth_ssu_N
    IPR036480 CarbP_synth_ssu_N_sf
    IPR005479 CbamoylP_synth_lsu-like_ATP-bd
    IPR005483 CbamoylP_synth_lsu_CPSase_dom
    IPR029062 Class_I_gatase-like
    IPR035686 CPSase_GATase1
    IPR002195 Dihydroorotase_CS
    IPR017926 GATASE
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase
    IPR011607 MGS-like_dom
    IPR036914 MGS-like_dom_sf
    IPR016185 PreATP-grasp_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01979 Amidohydro_1, 1 hit
    PF02786 CPSase_L_D2, 2 hits
    PF02787 CPSase_L_D3, 1 hit
    PF00988 CPSase_sm_chain, 1 hit
    PF00117 GATase, 1 hit
    PF02142 MGS, 1 hit
    PF00185 OTCace, 1 hit
    PF02729 OTCace_N, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00100 AOTCASE
    PR00101 ATCASE
    PR00098 CPSASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01096 CPSase_L_D3, 1 hit
    SM01097 CPSase_sm_chain, 1 hit
    SM00851 MGS, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48108 SSF48108, 1 hit
    SSF51338 SSF51338, 1 hit
    SSF51556 SSF51556, 1 hit
    SSF52021 SSF52021, 1 hit
    SSF52317 SSF52317, 1 hit
    SSF52335 SSF52335, 1 hit
    SSF52440 SSF52440, 2 hits
    SSF53671 SSF53671, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00670 asp_carb_tr, 1 hit
    TIGR01369 CPSaseII_lrg, 1 hit
    TIGR01368 CPSaseIIsmall, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50975 ATP_GRASP, 2 hits
    PS00097 CARBAMOYLTRANSFERASE, 1 hit
    PS00866 CPSASE_1, 2 hits
    PS00867 CPSASE_2, 2 hits
    PS00482 DIHYDROOROTASE_1, 1 hit
    PS00483 DIHYDROOROTASE_2, 1 hit
    PS51273 GATASE_TYPE_1, 1 hit
    PS51855 MGS, 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

    P27708-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL
    60 70 80 90 100
    VLTYPLIGNY GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA
    110 120 130 140 150
    TRTLHEWLQQ HGIPGLQGVD TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF
    160 170 180 190 200
    LDPNARPLVP EVSIKTPRVF NTGGAPRILA LDCGLKYNQI RCLCQRGAEV
    210 220 230 240 250
    TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL SEPNPRPVFG
    260 270 280 290 300
    ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE
    310 320 330 340 350
    TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF
    360 370 380 390 400
    DIFLETVKEA TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG
    410 420 430 440 450
    SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV
    460 470 480 490 500
    YFLPITPHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR
    510 520 530 540 550
    VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY
    560 570 580 590 600
    PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI
    610 620 630 640 650
    EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRQ
    660 670 680 690 700
    TAIKVTQHLG IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY
    710 720 730 740 750
    PLAYVAAKLA LGIPLPELRN SVTGGTAAFE PSVDYCVVKI PRWDLSKFLR
    760 770 780 790 800
    VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL RMVDENCVGF DHTVKPVSDM
    810 820 830 840 850
    ELETPTDKRI FVVAAALWAG YSVDRLYELT RIDRWFLHRM KRIIAHAQLL
    860 870 880 890 900
    EQHRGQPLPP DLLQQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
    910 920 930 940 950
    KQIDTVAAEW PAQTNYLYLT YWGTTHDLTF RTPHVLVLGS GVYRIGSSVE
    960 970 980 990 1000
    FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM
    1010 1020 1030 1040 1050
    DIYELENPEG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK
    1060 1070 1080 1090 1100
    FSRLLDTIGI SQPQWRELSD LESARQFCQT VGYPCVVRPS YVLSGAAMNV
    1110 1120 1130 1140 1150
    AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ASDGVVAAIA
    1160 1170 1180 1190 1200
    ISEHVENAGV HSGDATLVTP PQDITAKTLE RIKAIVHAVG QELQVTGPFN
    1210 1220 1230 1240 1250
    LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR VIMGEEVEPV
    1260 1270 1280 1290 1300
    GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL
    1310 1320 1330 1340 1350
    KAMLSTGFKI PKKNILLTIG SYKNKSELLP TVRLLESLGY SLYASLGTAD
    1360 1370 1380 1390 1400
    FYTEHGVKVT AVDWHFEEAV DGECPPQRSI LEQLAEKNFE LVINLSMRGA
    1410 1420 1430 1440 1450
    GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL GQIGPAPPLK
    1460 1470 1480 1490 1500
    VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGITMV
    1510 1520 1530 1540 1550
    CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGTVAG
    1560 1570 1580 1590 1600
    SAAGLKLYLN ETFSELRLDS VVQWMEHFET WPSHLPIVAH AEQQTVAAVL
    1610 1620 1630 1640 1650
    MVAQLTQRSV HICHVARKEE ILLIKAAKAR GLPVTCEVAP HHLFLSHDDL
    1660 1670 1680 1690 1700
    ERLGPGKGEV RPELGSRQDV EALWENMAVI DCFASDHAPH TLEEKCGSRP
    1710 1720 1730 1740 1750
    PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPPQEDTYV
    1760 1770 1780 1790 1800
    EVDLEHEWTI PSHMPFSKAH WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
    1810 1820 1830 1840 1850
    VPPGYGQDVR KWPQGAVPQL PPSAPATSEM TTTPERPRRG IPGLPDGRFH
    1860 1870 1880 1890 1900
    LPPRIHRASD PGLPAEEPKE KSSRKVAEPE LMGTPDGTCY PPPPVPRQAS
    1910 1920 1930 1940 1950
    PQNLGTPGLL HPQTSPLLHS LVGQHILSVQ QFTKDQMSHL FNVAHTLRMM
    1960 1970 1980 1990 2000
    VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS
    2010 2020 2030 2040 2050
    VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR PVINAGDGVG
    2060 2070 2080 2090 2100
    EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
    2110 2120 2130 2140 2150
    LRYVAPPSLR MPPTVRAFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE
    2160 2170 2180 2190 2200
    RFGSTQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR
    2210 2220
    AAYFRQAENG MYIRMALLAT VLGRF
    Length:2,225
    Mass (Da):242,984
    Last modified:July 19, 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:i2AB8E8413E825A8F
    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
    F8VPD4F8VPD4_HUMAN
    CAD protein
    CAD
    2,162Annotation 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>
    H7C2E4H7C2E4_HUMAN
    CAD protein
    CAD
    293Annotation 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>
    H7BZB3H7BZB3_HUMAN
    CAD protein
    CAD
    279Annotation 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>
    H7C3Z5H7C3Z5_HUMAN
    CAD protein
    CAD
    269Annotation 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 conflicti505P → T in BAA11423 (PubMed:8619816).Curated1
    Sequence conflicti535A → G in BAA11423 (PubMed:8619816).Curated1
    Sequence conflicti560L → V in BAA11423 (PubMed:8619816).Curated1
    Sequence conflicti1103T → A in BAA11423 (PubMed:8619816).Curated1
    Sequence conflicti1513A → G in BAA11423 (PubMed:8619816).Curated1
    Sequence conflicti1676N → D in BAA11423 (PubMed:8619816).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07828933M → R in EIEE50; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs751610198EnsemblClinVar.1
    Natural variantiVAR_035897177R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs374122292Ensembl.1
    Natural variantiVAR_035898735Y → C in a colorectal cancer sample; somatic mutation. 1 Publication1
    Natural variantiVAR_0782901789 – 2225Missing in EIEE50; unknown pathological significance. 1 PublicationAdd BLAST437
    Natural variantiVAR_0739552024R → Q in EIEE50. 1 PublicationCorresponds to variant dbSNP:rs763410987Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    D78586 mRNA Translation: BAA11423.1
    CH471053 Genomic DNA Translation: EAX00612.1
    CH471053 Genomic DNA Translation: EAX00613.1
    CH471053 Genomic DNA Translation: EAX00614.1
    BC014178 mRNA Translation: AAH14178.2
    BC065510 mRNA Translation: AAH65510.1
    M38561 Genomic DNA Translation: AAA51907.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS1742.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A36240

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001293008.1, NM_001306079.1
    NP_004332.2, NM_004341.4

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.377010

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000264705; ENSP00000264705; ENSG00000084774

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    790

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:790

    UCSC genome browser

    More...
    UCSCi
    uc002rji.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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Wikipedia

    Aspartate carbamoyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D78586 mRNA Translation: BAA11423.1
    CH471053 Genomic DNA Translation: EAX00612.1
    CH471053 Genomic DNA Translation: EAX00613.1
    CH471053 Genomic DNA Translation: EAX00614.1
    BC014178 mRNA Translation: AAH14178.2
    BC065510 mRNA Translation: AAH65510.1
    M38561 Genomic DNA Translation: AAA51907.1
    CCDSiCCDS1742.1
    PIRiA36240
    RefSeqiNP_001293008.1, NM_001306079.1
    NP_004332.2, NM_004341.4
    UniGeneiHs.377010

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4BY3X-ray1.73A1456-1846[»]
    4C6BX-ray1.66A1456-1846[»]
    4C6CX-ray1.45A1456-1846[»]
    4C6DX-ray1.30A1456-1846[»]
    4C6EX-ray1.26A1456-1846[»]
    4C6FX-ray1.26A1456-1846[»]
    4C6IX-ray1.35A1456-1846[»]
    4C6JX-ray1.30A1456-1846[»]
    4C6KX-ray1.48A1456-1846[»]
    4C6LX-ray1.55A1456-1846[»]
    4C6MX-ray1.62A1456-1846[»]
    4C6NX-ray1.90A1456-1846[»]
    4C6OX-ray1.65A1456-1846[»]
    4C6PX-ray1.52A1456-1846[»]
    4C6QX-ray1.66A1456-1846[»]
    5G1NX-ray2.10A/B/C/D/E/F1915-2225[»]
    5G1OX-ray2.10A/B/C/D/E/F1915-2225[»]
    5G1PX-ray3.19A/B/C/D/E/F1915-2225[»]
    5YNZX-ray2.77A1456-1846[»]
    6HFDX-ray1.87A1456-1846[»]
    6HFEX-ray1.48A1456-1846[»]
    6HFFX-ray1.51A1456-1846[»]
    6HFHX-ray1.45A1456-1846[»]
    6HFIX-ray1.46A1456-1846[»]
    6HFJX-ray1.20A1456-1846[»]
    6HFKX-ray1.46A1456-1846[»]
    6HFLX-ray1.35A1456-1846[»]
    6HFNX-ray1.45A1456-1846[»]
    6HFPX-ray1.20A1456-1846[»]
    6HFQX-ray1.15A1456-1846[»]
    6HFRX-ray1.30A1456-1846[»]
    6HFSX-ray1.35A1456-1846[»]
    6HFUX-ray1.40A1456-1846[»]
    6HG1X-ray2.12A1460-1559[»]
    A1571-1826[»]
    DisProtiDP01024
    ProteinModelPortaliP27708
    SMRiP27708
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107243, 129 interactors
    DIPiDIP-39484N
    IntActiP27708, 53 interactors
    MINTiP27708
    STRINGi9606.ENSP00000264705

    Chemistry databases

    BindingDBiP27708
    ChEMBLiCHEMBL3093
    DrugBankiDB00128 L-Aspartic Acid
    DB00130 L-Glutamine
    DB03459 Sparfosic acid

    Protein family/group databases

    MEROPSiM38.972

    PTM databases

    iPTMnetiP27708
    PhosphoSitePlusiP27708
    SwissPalmiP27708

    Polymorphism and mutation databases

    BioMutaiCAD
    DMDMi50403731

    Proteomic databases

    EPDiP27708
    MaxQBiP27708
    PaxDbiP27708
    PeptideAtlasiP27708
    PRIDEiP27708
    ProteomicsDBi54409

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264705; ENSP00000264705; ENSG00000084774
    GeneIDi790
    KEGGihsa:790
    UCSCiuc002rji.4 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    790
    DisGeNETi790
    EuPathDBiHostDB:ENSG00000084774.13

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    CAD
    HGNCiHGNC:1424 CAD
    HPAiCAB007781
    HPA057266
    HPA069341
    MalaCardsiCAD
    MIMi114010 gene
    616457 phenotype
    neXtProtiNX_P27708
    OpenTargetsiENSG00000084774
    Orphaneti448010 CAD-CDG
    PharmGKBiPA26023

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0370 Eukaryota
    COG0458 LUCA
    COG0505 LUCA
    COG0540 LUCA
    GeneTreeiENSGT00940000157241
    HOGENOMiHOG000234584
    HOVERGENiHBG000279
    InParanoidiP27708
    KOiK11540
    OrthoDBiEOG091G00DC
    PhylomeDBiP27708
    TreeFamiTF105604

    Enzyme and pathway databases

    UniPathwayi
    UPA00070;UER00115

    UPA00070;UER00116

    UPA00070;UER00117

    BioCyciMetaCyc:ENSG00000084774-MONOMER
    BRENDAi3.5.2.3 2681
    ReactomeiR-HSA-500753 Pyrimidine biosynthesis
    SIGNORiP27708

    Miscellaneous databases

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

    More...
    ChiTaRSi
    CAD human

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

    More...
    GenomeRNAii
    790
    PMAP-CutDBiP27708

    Protein Ontology

    More...
    PROi
    PR:P27708

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000084774 Expressed in 170 organ(s), highest expression level in right lobe of liver
    CleanExiHS_CAD
    ExpressionAtlasiP27708 baseline and differential
    GenevisibleiP27708 HS

    Family and domain databases

    CDDicd01744 GATase1_CPSase, 1 hit
    Gene3Di1.10.1030.10, 1 hit
    3.30.1490.20, 1 hit
    3.40.50.1370, 2 hits
    3.40.50.1380, 1 hit
    3.40.50.880, 1 hit
    3.50.30.20, 1 hit
    HAMAPiMF_00001 Asp_carb_tr, 1 hit
    MF_01209 CPSase_S_chain, 1 hit
    InterProiView protein in InterPro
    IPR006680 Amidohydro-rel
    IPR006132 Asp/Orn_carbamoyltranf_P-bd
    IPR006130 Asp/Orn_carbamoylTrfase
    IPR036901 Asp/Orn_carbamoylTrfase_sf
    IPR002082 Asp_carbamoyltransf
    IPR006131 Asp_carbamoyltransf_Asp/Orn-bd
    IPR011761 ATP-grasp
    IPR013815 ATP_grasp_subdomain_1
    IPR006275 CarbamoylP_synth_lsu
    IPR005480 CarbamoylP_synth_lsu_oligo
    IPR036897 CarbamoylP_synth_lsu_oligo_sf
    IPR006274 CarbamoylP_synth_ssu
    IPR002474 CarbamoylP_synth_ssu_N
    IPR036480 CarbP_synth_ssu_N_sf
    IPR005479 CbamoylP_synth_lsu-like_ATP-bd
    IPR005483 CbamoylP_synth_lsu_CPSase_dom
    IPR029062 Class_I_gatase-like
    IPR035686 CPSase_GATase1
    IPR002195 Dihydroorotase_CS
    IPR017926 GATASE
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase
    IPR011607 MGS-like_dom
    IPR036914 MGS-like_dom_sf
    IPR016185 PreATP-grasp_dom_sf
    PfamiView protein in Pfam
    PF01979 Amidohydro_1, 1 hit
    PF02786 CPSase_L_D2, 2 hits
    PF02787 CPSase_L_D3, 1 hit
    PF00988 CPSase_sm_chain, 1 hit
    PF00117 GATase, 1 hit
    PF02142 MGS, 1 hit
    PF00185 OTCace, 1 hit
    PF02729 OTCace_N, 1 hit
    PRINTSiPR00100 AOTCASE
    PR00101 ATCASE
    PR00098 CPSASE
    SMARTiView protein in SMART
    SM01096 CPSase_L_D3, 1 hit
    SM01097 CPSase_sm_chain, 1 hit
    SM00851 MGS, 1 hit
    SUPFAMiSSF48108 SSF48108, 1 hit
    SSF51338 SSF51338, 1 hit
    SSF51556 SSF51556, 1 hit
    SSF52021 SSF52021, 1 hit
    SSF52317 SSF52317, 1 hit
    SSF52335 SSF52335, 1 hit
    SSF52440 SSF52440, 2 hits
    SSF53671 SSF53671, 1 hit
    TIGRFAMsiTIGR00670 asp_carb_tr, 1 hit
    TIGR01369 CPSaseII_lrg, 1 hit
    TIGR01368 CPSaseIIsmall, 1 hit
    PROSITEiView protein in PROSITE
    PS50975 ATP_GRASP, 2 hits
    PS00097 CARBAMOYLTRANSFERASE, 1 hit
    PS00866 CPSASE_1, 2 hits
    PS00867 CPSASE_2, 2 hits
    PS00482 DIHYDROOROTASE_1, 1 hit
    PS00483 DIHYDROOROTASE_2, 1 hit
    PS51273 GATASE_TYPE_1, 1 hit
    PS51855 MGS, 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 nameiPYR1_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: P27708
    Secondary accession number(s): D6W552, Q6P0Q0, Q96CK3
    <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: August 1, 1992
    Last sequence update: July 19, 2004
    Last modified: December 5, 2018
    This is version 217 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, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    7. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again