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UniProtKB - P27708 (PYR1_HUMAN)

Entry version 232 (02 Dec 2020)
Sequence version 3 (19 Jul 2004)
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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%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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%5Fsection">'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), Aspartate carbamoyltransferase (CAD)
    3. CAD protein (CAD), Aspartate carbamoyltransferase (CAD), Aspartate carbamoyltransferase (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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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

    Pathway Commons web resource for biological pathway data

    More...    PathwayCommonsi    		P27708

    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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 and Host 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 & Seán O’Donoghue; 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.
    Related information in OMIM
    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:rs763410987EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...    Pharosi    		P27708, Tchem

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3093

    Drug and drug target database

    More...    DrugBanki    		DB00128, 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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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 sensitivity to feedback inhibition by UTP.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    The CPTAC Assay portal

    More...    CPTACi    		CPTAC-466
    CPTAC-467

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P27708

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P27708

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...    MassIVEi    		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: a multi-organism proteome resource

    More...    ProteomicsDBi    		54409

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P27708

    MetOSite database of methionine sulfoxide sites

    More...    MetOSitei    		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

    <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 right lobe of liver and 185 other tissues

    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    		ENSG00000084774, Low tissue specificity

    <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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    P27708
    With#Exp.IntAct
    itself3EBI-355504,EBI-355504

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		107243, 196 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-39484N

    Protein interaction database and analysis system

    More...    IntActi    		P27708, 85 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

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...    RNActi    		P27708, protein

    <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

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

    More...    SMRi    		P27708

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		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%5Fand%5Fdomains%5Fsection">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

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000157241

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_000513_2_1_1

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P27708

    Database of Orthologous Groups

    More...    OrthoDBi    		273358at2759

    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

    Database of protein disorder

    More...    DisProti    		DP01024

    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
    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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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
    Aspartate carbamoyltransferase
    CAD
    		2,162Annotation score:

    Annotation score:4 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
    Aspartate carbamoyltransferase
    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:rs763410987EnsemblClinVar.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

    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%5Freferences%5Fsection">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

    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[»]
    SMRiP27708
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi107243, 196 interactors
    DIPiDIP-39484N
    IntActiP27708, 85 interactors
    MINTiP27708
    STRINGi9606.ENSP00000264705

    Chemistry databases

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

    Protein family/group databases

    MEROPSiM38.972

    PTM databases

    iPTMnetiP27708
    MetOSiteiP27708
    PhosphoSitePlusiP27708
    SwissPalmiP27708

    Polymorphism and mutation databases

    BioMutaiCAD
    DMDMi50403731

    Proteomic databases

    CPTACiCPTAC-466
    CPTAC-467
    EPDiP27708
    jPOSTiP27708
    MassIVEiP27708
    MaxQBiP27708
    PaxDbiP27708
    PeptideAtlasiP27708
    PRIDEiP27708
    ProteomicsDBi54409

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...    Antibodypediai    		28293, 296 antibodies

    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
    HPAiENSG00000084774, Low tissue specificity
    MalaCardsiCAD
    MIMi114010, gene
    616457, phenotype
    neXtProtiNX_P27708
    OpenTargetsiENSG00000084774
    Orphaneti448010, CAD-CDG
    PharmGKBiPA26023

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG0370, Eukaryota
    GeneTreeiENSGT00940000157241
    HOGENOMiCLU_000513_2_1_1
    InParanoidiP27708
    OrthoDBi273358at2759
    PhylomeDBiP27708
    TreeFamiTF105604

    Enzyme and pathway databases

    UniPathwayiUPA00070;UER00115
    UPA00070;UER00116
    UPA00070;UER00117
    BioCyciMetaCyc:ENSG00000084774-MONOMER
    BRENDAi3.5.2.3, 2681
    PathwayCommonsiP27708
    ReactomeiR-HSA-500753, Pyrimidine biosynthesis
    SIGNORiP27708

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...    BioGRID-ORCSi    		790, 244 hits in 853 CRISPR screens

    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
    PharosiP27708, Tchem

    Protein Ontology

    More...    PROi    		PR:P27708
    RNActiP27708, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000084774, Expressed in right lobe of liver and 185 other tissues
    ExpressionAtlasiP27708, baseline and differential
    GenevisibleiP27708, HS

    Family and domain databases

    CDDicd01744, GATase1_CPSase, 1 hit
    DisProtiDP01024
    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
    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...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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%5Fand%5Fisoforms">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 2, 2020
    This is version 232 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, Direct protein sequencing, Reference proteome

    Documents

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