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UniProtKB - P27708 (PYR1_HUMAN)

Entry version 236 (29 Sep 2021)
Sequence version 3 (19 Jul 2004)
Previous versions | rss
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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_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 <a href="http://www.uniprot.org/help/function_section">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_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 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_section">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_section">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_section">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_section">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		2.1.3.2, 2681
3.5.2.3, 2681
6.3.5.5, 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

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P27708

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 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_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

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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000084774

<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

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

Developmental and epileptic encephalopathy 50 (DEE50)2 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe early-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. DEE50 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 DEE50; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs751610198EnsemblClinVar.1
Natural variantiVAR_0782901789 – 2225Missing in DEE50; unknown pathological significance. 1 PublicationAdd BLAST437
Natural variantiVAR_0739552024R → Q in DEE50. 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_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 variant, 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

Genetic variation 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 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_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 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

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P27708, 3 sites, 1 O-linked glycan (3 sites)

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 186 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_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">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, 259 interactors

Database of interacting proteins

More...DIPi		DIP-39484N

Protein interaction database and analysis system

More...IntActi		P27708, 91 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_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
Regioni1811 – 1899DisorderedSequence analysisAdd BLAST89
Regioni1918 – 2225ATCase (Aspartate transcarbamylase)By similarityAdd BLAST308

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1850 – 1877Basic and acidic residuesSequence analysisAdd BLAST28

<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

Identification of Orthologs from Complete Genome Data

More...OMAi		DAIYCTF

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_length">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_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
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 DEE50; 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 DEE50; unknown pathological significance. 1 PublicationAdd BLAST437
Natural variantiVAR_0739552024R → Q in DEE50. 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

<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

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, 259 interactors
DIPiDIP-39484N
IntActiP27708, 91 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

GlyGeniP27708, 3 sites, 1 O-linked glycan (3 sites)
iPTMnetiP27708
MetOSiteiP27708
PhosphoSitePlusiP27708
SwissPalmiP27708

Genetic variation 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, 312 antibodies

The DNASU plasmid repository

More...DNASUi		790

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		790
DisGeNETi790

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
VEuPathDBiHostDB:ENSG00000084774

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0370, Eukaryota
GeneTreeiENSGT00940000157241
HOGENOMiCLU_000513_2_1_1
InParanoidiP27708
OMAiDAIYCTF
OrthoDBi273358at2759
PhylomeDBiP27708
TreeFamiTF105604

Enzyme and pathway databases

UniPathwayiUPA00070;UER00115
UPA00070;UER00116
UPA00070;UER00117
BioCyciMetaCyc:ENSG00000084774-MONOMER
BRENDAi2.1.3.2, 2681
3.5.2.3, 2681
6.3.5.5, 2681
PathwayCommonsiP27708
ReactomeiR-HSA-500753, Pyrimidine biosynthesis
SABIO-RKiP27708
SIGNORiP27708

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		790, 274 hits in 1036 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 186 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

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_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: September 29, 2021
This is version 236 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 chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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