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Entry version 236 (29 Sep 2021)
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_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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:ENSG00000084774-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

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

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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

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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

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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

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

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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

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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

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GeneTreei
ENSGT00940000157241

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000513_2_1_1

InParanoid: Eukaryotic Ortholog Groups

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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

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<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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