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Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene

CPS1

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

Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.

<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 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

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator. Activated by glycerol in the absence of NAG, whereas in the presence of NAG it is inhibited by increasing concentrations of glycerol.2 Publications

<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=0.47 mM for ATP1 Publication
  2. KM=4.0 mM for HCO3-1 Publication
  3. KM=1.00 mM for NH4+1 Publication
  1. Vmax=1.22 µmol/min/mg enzyme for ATP1 Publication
  2. Vmax=1.23 µmol/min/mg enzyme for HCO3-1 Publication
  3. Vmax=1.19 µmol/min/mg enzyme for NH4+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1391Allosteric activatorCurated1
Binding sitei1394Allosteric activatorCurated1
Binding sitei1410Allosteric activatorCurated1
Binding sitei1437Allosteric activatorCurated1
Binding sitei1440Allosteric activatorCurated1
Binding sitei1449Allosteric activatorCurated1

<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, Ligase
Biological processUrea cycle
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS00415-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
6.3.4.16 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-70635 Urea cycle

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P31327

Protein family/group databases

MEROPS protease database

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MEROPSi
C26.951

<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:
Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC:6.3.4.162 Publications)
Alternative name(s):
Carbamoyl-phosphate synthetase I
Short name:
CPSase I
<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:CPS1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000021826.14

Human Gene Nomenclature Database

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HGNCi
HGNC:2323 CPS1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608307 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P31327

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Keywords - Cellular componenti

Mitochondrion, 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

Carbamoyl phosphate synthetase 1 deficiency (CPS1D)15 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder of the urea cycle causing hyperammonemia. It can present as a devastating metabolic disease dominated by severe hyperammonemia in neonates or as a more insidious late-onset condition, generally manifesting as life-threatening hyperammonemic crises under catabolic situations. Clinical features include protein intolerance, intermittent ataxia, seizures, lethargy, developmental delay and mental retardation.
See also OMIM:237300
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_06617143A → V in CPS1D. 1 Publication1
Natural variantiVAR_06617258G → D in CPS1D. 1 Publication1
Natural variantiVAR_06617365S → F in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs375979196Ensembl.1
Natural variantiVAR_06617471V → G in CPS1D. 1 Publication1
Natural variantiVAR_06356079G → E in CPS1D. 1 Publication1
Natural variantiVAR_06617587P → S in CPS1D. 1 Publication1
Natural variantiVAR_06617689Y → D in CPS1D. 1 Publication1
Natural variantiVAR_064062123S → F in CPS1D; modestly decreases enzyme activity. 1 Publication1
Natural variantiVAR_075404123S → Y in CPS1D; unknown pathological significance. 1 Publication1
Natural variantiVAR_066177165D → G in CPS1D. 1 Publication1
Natural variantiVAR_075405174R → W in CPS1D; unknown pathological significance. 1 Publication1
Natural variantiVAR_063561212Y → N in CPS1D. 1 Publication1
Natural variantiVAR_066178224D → V in CPS1D. 1 Publication1
Natural variantiVAR_066179233R → C in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs767905306EnsemblClinVar.1
Natural variantiVAR_066180243H → P in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs752902711Ensembl.1
Natural variantiVAR_066181258G → E in CPS1D. 1 Publication1
Natural variantiVAR_066182263G → E in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1471393474Ensembl.1
Natural variantiVAR_063562280K → N in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs753751183Ensembl.1
Natural variantiVAR_066104301G → E in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs973321068EnsemblClinVar.1
Natural variantiVAR_066183304A → V in CPS1D; associated with T-986. 1 PublicationCorresponds to variant dbSNP:rs775920437Ensembl.1
Natural variantiVAR_066184317G → E in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1273594946Ensembl.1
Natural variantiVAR_014077337H → R in CPS1D; modestly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs28940283EnsemblClinVar.1
Natural variantiVAR_075806341L → S in CPS1D. 1 Publication1
Natural variantiVAR_075406355N → D in CPS1D; around 80% decrease in enzyme activity; significant reduction in thermal stability; approximately 4-fold decrease in the apparent Vmax for ATP, bicarbonate and ammonia. 1 PublicationCorresponds to variant dbSNP:rs1472190012Ensembl.1
Natural variantiVAR_066185358D → H in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs149930500Ensembl.1
Natural variantiVAR_066186382P → L in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs201407486EnsemblClinVar.1
Natural variantiVAR_066105389Y → C in CPS1D; around 40% decrease in enzyme activity; significant loss of thermal stability. 2 Publications1
Natural variantiVAR_066106390L → R in CPS1D; significant loss of protein stability. 2 Publications1
Natural variantiVAR_066187401G → R in CPS1D; unknown pathological significance; associated with N-937 in a patient. 2 PublicationsCorresponds to variant dbSNP:rs760895692EnsemblClinVar.1
Natural variantiVAR_066188431G → R in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs778766382Ensembl.1
Natural variantiVAR_066189432G → V in CPS1D. 1 Publication1
Natural variantiVAR_063563438A → P in CPS1D; almost complete loss of enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs772497399EnsemblClinVar.1
Natural variantiVAR_066190438A → T in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs772497399EnsemblClinVar.1
Natural variantiVAR_066191450K → E in CPS1D. 1 Publication1
Natural variantiVAR_017562457V → G in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs371350538Ensembl.1
Natural variantiVAR_064063471T → N in CPS1D. 1 Publication1
Natural variantiVAR_066192498A → P in CPS1D. 1 Publication1
Natural variantiVAR_066193531V → E in CPS1D. 1 Publication1
Natural variantiVAR_066194531V → G in CPS1D. 1 Publication1
Natural variantiVAR_006835544T → M in CPS1D; almost complete loss of enzyme activity; approximately 60-fold increase in the apparent Km for bicarbonate and approximately 4-fold respective decrease and increase in the apparent Vmax and Km for ammonia. 3 PublicationsCorresponds to variant dbSNP:rs121912592EnsemblClinVar.1
Natural variantiVAR_066195587R → C in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1242028775Ensembl.1
Natural variantiVAR_063564587R → H in CPS1D. 2 Publications1
Natural variantiVAR_066196587R → L in CPS1D. 1 Publication1
Natural variantiVAR_066142589A → T in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs777233486Ensembl.1
Natural variantiVAR_063565593G → R in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1048119191Ensembl.1
Natural variantiVAR_066197597S → L in CPS1D. 1 Publication1
Natural variantiVAR_066198622V → M in CPS1D. 1 Publication1
Natural variantiVAR_066199628G → D in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1275599086Ensembl.1
Natural variantiVAR_066200632I → R in CPS1D. 2 Publications1
Natural variantiVAR_066201638R → P in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs757205958EnsemblClinVar.1
Natural variantiVAR_066143640A → S in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs142693704Ensembl.1
Natural variantiVAR_066202648C → Y in CPS1D. 1 Publication1
Natural variantiVAR_063566651E → K in CPS1D. 1 Publication1
Natural variantiVAR_066203654D → V in CPS1D. 1 Publication1
Natural variantiVAR_075807661G → R in CPS1D. 1 Publication1
Natural variantiVAR_063567674N → I in CPS1D. 1 Publication1
Natural variantiVAR_066204674N → K in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1248368809Ensembl.1
Natural variantiVAR_064064678Q → P in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding. 1 Publication1
Natural variantiVAR_066205698N → S in CPS1D. 1 Publication1
Natural variantiVAR_066144716N → K in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs369061090EnsemblClinVar.1
Natural variantiVAR_066107718R → K in CPS1D. 1 Publication1
Natural variantiVAR_066108721R → Q in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs752339705Ensembl.1
Natural variantiVAR_066109724A → P in CPS1D. 1 Publication1
Natural variantiVAR_066110726A → T in CPS1D. 1 Publication1
Natural variantiVAR_066111767D → V in CPS1D. 1 Publication1
Natural variantiVAR_064065774P → L in CPS1D; the enzyme is inactive. 1 Publication1
Natural variantiVAR_063568780R → H in CPS1D. 2 PublicationsCorresponds to variant dbSNP:rs758724746EnsemblClinVar.1
Natural variantiVAR_066112792M → I in CPS1D. 1 Publication1
Natural variantiVAR_066145803R → C in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs201716417EnsemblClinVar.1
Natural variantiVAR_066146803R → G in CPS1D. 2 PublicationsCorresponds to variant dbSNP:rs201716417EnsemblClinVar.1
Natural variantiVAR_066147803R → S in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs201716417EnsemblClinVar.1
Natural variantiVAR_066148805F → L in CPS1D. 1 Publication1
Natural variantiVAR_066149805F → S in CPS1D. 1 Publication1
Natural variantiVAR_017563810Q → R in CPS1D. 1 Publication1
Natural variantiVAR_066150814R → W in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs772782772EnsemblClinVar.1
Natural variantiVAR_066151816C → R in CPS1D. 1 Publication1
Natural variantiVAR_017564843L → S in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield. 3 Publications1
Natural variantiVAR_063569850R → C in CPS1D; moderate decrease in protein yield and partial loss of enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs1015051007Ensembl.1
Natural variantiVAR_030675850R → H in CPS1D; partial loss of enzyme activity. 4 PublicationsCorresponds to variant dbSNP:rs767694281Ensembl.1
Natural variantiVAR_075407871T → P in CPS1D; significant decrease in protein yield and enzyme activity. 1 Publication1
Natural variantiVAR_066152911G → E in CPS1D; significant decrease in protein yield and enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs1388955593Ensembl.1
Natural variantiVAR_066153911G → V in CPS1D; significant decrease in protein yield and enzyme activity. 2 Publications1
Natural variantiVAR_066154913S → L in CPS1D; significant decrease in protein yield and partial loss of enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs754706559EnsemblClinVar.1
Natural variantiVAR_066155914D → G in CPS1D; significant decrease in protein yield and enzyme activity. 2 Publications1
Natural variantiVAR_066156914D → H in CPS1D; significant decrease in protein yield and enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs765484849EnsemblClinVar.1
Natural variantiVAR_030676918S → P in CPS1D; significant decrease in protein yield and enzyme activity. 2 Publications1
Natural variantiVAR_066157932R → T in CPS1D; significant decrease in protein yield and partial loss of enzyme activity. 2 Publications1
Natural variantiVAR_075408937I → N in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs760714614EnsemblClinVar.1
Natural variantiVAR_066158949A → T in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability. 2 PublicationsCorresponds to variant dbSNP:rs537170841EnsemblClinVar.1
Natural variantiVAR_066159958L → P in CPS1D; significant decrease in protein yield and enzyme activity. 2 Publications1
Natural variantiVAR_066160959Y → C in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs1191587211Ensembl.1
Natural variantiVAR_066161962Y → C in CPS1D; significant decrease in protein yield and partial loss of enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs955666400Ensembl.1
Natural variantiVAR_075409964G → D in CPS1D; significant decrease in protein yield and enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs534815243Ensembl.1
Natural variantiVAR_066113978V → E in CPS1D. 1 Publication1
Natural variantiVAR_063570982G → D in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs121912595EnsemblClinVar.1
Natural variantiVAR_066162982G → S in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs757059355EnsemblClinVar.1
Natural variantiVAR_066114982G → V in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs121912595EnsemblClinVar.1
Natural variantiVAR_066115984Y → H in CPS1D. 1 Publication1
Natural variantiVAR_066116986I → T in CPS1D; associated with V-304. 1 Publication1
Natural variantiVAR_066117987G → C in CPS1D; may affect splicing. 1 Publication1
Natural variantiVAR_066118992F → S in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs990390709Ensembl.1
Natural variantiVAR_066163998S → F in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1404696893Ensembl.1
Natural variantiVAR_0661191016N → S in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs749238466EnsemblClinVar.1
Natural variantiVAR_0661201017P → L in CPS1D. 1 Publication1
Natural variantiVAR_0661211022T → I in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1437651658Ensembl.1
Natural variantiVAR_0661221034E → G in CPS1D. 1 Publication1
Natural variantiVAR_0661231045H → R in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1241423400Ensembl.1
Natural variantiVAR_0661641054I → R in CPS1D. 1 Publication1
Natural variantiVAR_0661241059Q → R in CPS1D. 1 Publication1
Natural variantiVAR_0661251065A → E in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs770471782EnsemblClinVar.1
Natural variantiVAR_0661261089R → C in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1392559810Ensembl.1
Natural variantiVAR_0661651089R → L in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1280211937Ensembl.1
Natural variantiVAR_0635711103Q → R in CPS1D. 1 Publication1
Natural variantiVAR_0635721141V → G in CPS1D. 1 Publication1
Natural variantiVAR_0661271155A → E in CPS1D. 1 Publication1
Natural variantiVAR_0661281155A → V in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs766125631EnsemblClinVar.1
Natural variantiVAR_0758081167T → R in CPS1D. 1 Publication1
Natural variantiVAR_0754101194E → D in CPS1D. 1 Publication1
Natural variantiVAR_0635731195H → P in CPS1D. 1 Publication1
Natural variantiVAR_0661291203S → L in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs149518280Ensembl.1
Natural variantiVAR_0661661203S → P in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1319489001Ensembl.1
Natural variantiVAR_0661671205D → N in CPS1D. 1 Publication1
Natural variantiVAR_0635741215I → V in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs141373204EnsemblClinVar.1
Natural variantiVAR_0661301228R → Q in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs778117194EnsemblClinVar.1
Natural variantiVAR_0635751241N → K in CPS1D. 1 Publication1
Natural variantiVAR_0754111254I → F in CPS1D; unknown pathological significance. 1 Publication1
Natural variantiVAR_0661311255E → D in CPS1D. 1 Publication1
Natural variantiVAR_0661321262R → P in CPS1D. 1 Publication1
Natural variantiVAR_0661331262R → Q in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs750670270EnsemblClinVar.1
Natural variantiVAR_0661341274D → H in CPS1D. 1 Publication1
Natural variantiVAR_0661351327C → R in CPS1D. 1 Publication1
Natural variantiVAR_0661681331S → P in CPS1D. 1 Publication1
Natural variantiVAR_0661361333G → E in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs372645328Ensembl.1
Natural variantiVAR_0754121363 – 1366Missing in CPS1D; unknown pathological significance. 1 Publication4
Natural variantiVAR_0661371371R → L in CPS1D. 1 Publication1
Natural variantiVAR_0661691378A → T in CPS1D; significant reduction in thermal stability. 2 PublicationsCorresponds to variant dbSNP:rs1245373037Ensembl.1
Natural variantiVAR_0754131381L → S in CPS1D; significant loss of protein stability. 1 Publication1
Natural variantiVAR_0661381391T → M in CPS1D. 1 PublicationCorresponds to variant dbSNP:rs1392934477Ensembl.1
Natural variantiVAR_0661391398L → V in CPS1D. 1 Publication1
Natural variantiVAR_0640661411P → L in CPS1D; modestly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs1202306773Ensembl.1
Natural variantiVAR_0661401439P → L in CPS1D. 1 Publication1
Natural variantiVAR_0661701443T → A in CPS1D; almost complete loss of enzyme activity; approximately 10-fold decrease in the apparent Vmax for bicarbonate, ammonia and ATP; decreased affinity for NAG. 2 Publications1
Natural variantiVAR_0640671453R → Q in CPS1D; the enzyme is inactive. 1 Publication1
Natural variantiVAR_0640681453R → W in CPS1D; the enzyme is inactive. 2 PublicationsCorresponds to variant dbSNP:rs933813349Ensembl.1
Natural variantiVAR_0661411462P → R in CPS1D. 2 Publications1
Natural variantiVAR_0640691491Y → H in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG). 1 Publication1
Pulmonary hypertension, neonatal (PHN)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry. CPS1 variants influence the availability of precursors for nitric oxide (NO) synthesis and play a role in clinical situations where endogenous NO production is critically important, such as neonatal pulmonary hypertension, increased pulmonary artery pressure following surgical repair of congenital heart defects or hepatovenocclusive disease following bone marrow transplantation. Infants with neonatal pulmonary hypertension homozygous for Thr-1406 have lower L-arginine concentrations than neonates homozygous for Asn-1406 (PubMed:11407344).1 Publication
Disease descriptionA disease characterized by elevated pulmonary artery pressure. Pulmonary hypertension in the neonate is associated with multiple underlying problems such as respiratory distress syndrome, meconium aspiration syndrome, congenital diaphragmatic hernia, bronchopulmonary dysplasia, sepsis, or congenital heart disease.
See also OMIM:615371

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
1373

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
CPS1

MalaCards human disease database

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MalaCardsi
CPS1
MIMi237300 phenotype
615371 phenotype

Open Targets

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OpenTargetsi
ENSG00000021826

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

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Orphaneti
147 Carbamoyl-phosphate synthetase 1 deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26840

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2362990

Drug and drug target database

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DrugBanki
DB06775 Carglumic Acid

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CPS1

Domain mapping of disease mutations (DMDM)

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DMDMi
4033707

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 38MitochondrionBy similarityAdd BLAST38
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002989739 – 1500Carbamoyl-phosphate synthase [ammonia], mitochondrialAdd BLAST1462

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 residuei55N6-acetyllysine; alternateBy similarity1
Modified residuei55N6-glutaryllysine; alternate1 Publication1
Modified residuei55N6-succinyllysine; alternateBy similarity1
Modified residuei57N6-acetyllysine; alternateBy similarity1
Modified residuei57N6-succinyllysine; alternateBy similarity1
Modified residuei119N6-acetyllysine; alternateBy similarity1
Modified residuei119N6-succinyllysine; alternateBy similarity1
Modified residuei148PhosphoserineCombined sources1
Modified residuei157N6-acetyllysine; alternateBy similarity1
Modified residuei157N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysine; alternateBy similarity1
Modified residuei171N6-glutaryllysine; alternate1 Publication1
Modified residuei176N6-glutaryllysine1 Publication1
Modified residuei182N6-acetyllysineBy similarity1
Modified residuei197N6-acetyllysineBy similarity1
Modified residuei207N6-acetyllysine; alternateBy similarity1
Modified residuei207N6-glutaryllysine; alternate1 Publication1
Modified residuei207N6-succinyllysine; alternateBy similarity1
Modified residuei210N6-acetyllysine; alternateBy similarity1
Modified residuei210N6-glutaryllysine; alternate1 Publication1
Modified residuei214N6-acetyllysine; alternateBy similarity1
Modified residuei214N6-glutaryllysine; alternate1 Publication1
Modified residuei214N6-succinyllysine; alternateBy similarity1
Modified residuei219N6-acetyllysine; alternateBy similarity1
Modified residuei219N6-glutaryllysine; alternate1 Publication1
Modified residuei228N6-acetyllysine; alternateBy similarity1
Modified residuei228N6-glutaryllysine; alternate1 Publication1
Modified residuei237N6-glutaryllysine1 Publication1
Modified residuei280N6-acetyllysine; alternateBy similarity1
Modified residuei280N6-glutaryllysine; alternate1 Publication1
Modified residuei287N6-acetyllysine; alternateBy similarity1
Modified residuei287N6-succinyllysine; alternateBy similarity1
Modified residuei307N6-acetyllysine; alternateBy similarity1
Modified residuei307N6-glutaryllysine; alternate1 Publication1
Modified residuei307N6-succinyllysine; alternateBy similarity1
Modified residuei310N6-acetyllysine; alternateBy similarity1
Modified residuei310N6-glutaryllysine; alternate1 Publication1
Modified residuei400N6-succinyllysineBy similarity1
Modified residuei402N6-glutaryllysine; alternate1 Publication1
Modified residuei402N6-succinyllysine; alternateBy similarity1
Modified residuei412N6-acetyllysine; alternateBy similarity1
Modified residuei412N6-glutaryllysine; alternate1 Publication1
Modified residuei412N6-succinyllysine; alternateBy similarity1
Modified residuei453N6-acetyllysine; alternateBy similarity1
Modified residuei453N6-glutaryllysine; alternate1 Publication1
Modified residuei458N6-acetyllysine; alternateBy similarity1
Modified residuei458N6-glutaryllysine; alternate1 Publication1
Modified residuei458N6-succinyllysine; alternateBy similarity1
Modified residuei522N6-acetyllysine; alternateBy similarity1
Modified residuei522N6-succinyllysine; alternateBy similarity1
Modified residuei527N6-acetyllysine; alternateBy similarity1
Modified residuei527N6-glutaryllysine; alternate1 Publication1
Modified residuei527N6-succinyllysine; alternateBy similarity1
Modified residuei532N6-acetyllysine; alternateBy similarity1
Modified residuei532N6-glutaryllysine; alternate1 Publication1
Modified residuei537Phosphoserine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi537O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei540PhosphoserineBy similarity1
Modified residuei553N6-acetyllysine; alternateBy similarity1
Modified residuei553N6-glutaryllysine; alternate1 Publication1
Modified residuei553N6-succinyllysine; alternateBy similarity1
Modified residuei560N6-acetyllysine; alternateBy similarity1
Modified residuei560N6-succinyllysine; alternateBy similarity1
Modified residuei569PhosphoserineCombined sources1
Modified residuei575N6-acetyllysine; alternateBy similarity1
Modified residuei575N6-succinyllysine; alternateBy similarity1
Modified residuei612N6-acetyllysine; alternateBy similarity1
Modified residuei612N6-succinyllysine; alternateBy similarity1
Modified residuei630N6-acetyllysineBy similarity1
Modified residuei728N6-glutaryllysine1 Publication1
Modified residuei751N6-acetyllysine; alternateBy similarity1
Modified residuei751N6-succinyllysine; alternateBy similarity1
Modified residuei757N6-acetyllysine; alternateBy similarity1
Modified residuei757N6-glutaryllysine; alternate1 Publication1
Modified residuei757N6-succinyllysine; alternateBy similarity1
Modified residuei772N6-acetyllysine; alternateBy similarity1
Modified residuei772N6-glutaryllysine; alternate1 Publication1
Modified residuei793N6-acetyllysine; alternateBy similarity1
Modified residuei793N6-glutaryllysine; alternate1 Publication1
Modified residuei793N6-succinyllysine; alternateBy similarity1
Modified residuei811N6-acetyllysine; alternateBy similarity1
Modified residuei811N6-glutaryllysine; alternate1 Publication1
Modified residuei831N6-acetyllysine; alternateBy similarity1
Modified residuei831N6-succinyllysine; alternateBy similarity1
Modified residuei835PhosphoserineCombined sources1
Modified residuei841N6-acetyllysine; alternateBy similarity1
Modified residuei841N6-glutaryllysine; alternate1 Publication1
Modified residuei856N6-acetyllysine; alternateBy similarity1
Modified residuei856N6-glutaryllysine; alternate1 Publication1
Modified residuei869N6-glutaryllysine1 Publication1
Modified residuei875N6-acetyllysine; alternateBy similarity1
Modified residuei875N6-glutaryllysine; alternate1 Publication1
Modified residuei875N6-succinyllysine; alternateBy similarity1
Modified residuei889N6-acetyllysine; alternateBy similarity1
Modified residuei889N6-glutaryllysine; alternate1 Publication