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Entry version 176 (11 Dec 2019)
Sequence version 1 (01 Aug 1988)
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Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene

Cps1

Organism
Rattus norvegicus (Rat)
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 <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

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator. N-acetyl-L-beta-phenylglutamate (Phe-NAG) can also activate CPSase I, but with an activation constant that is 2-fold higher than that for NAG.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

The activation constant Ka of N-acetyl-L-glutamate for the reaction is 0.11 mM.
  1. KM=1.06 mM for ATP1 Publication
  2. KM=6.43 mM for HCO3-1 Publication
  3. KM=1.07 mM for NH4+1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei1391Allosteric activator1
    Binding sitei1394Allosteric activator1
    Binding sitei1410Allosteric activator1
    Binding sitei1437Allosteric activator1
    Binding sitei1440Allosteric activator1
    Binding sitei1449Allosteric activator1

    <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

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-RNO-70635 Urea cycle

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P07756

    <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:6.3.4.16)
    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>OrganismiRattus norvegicus (Rat)
    <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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    <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
    • UP000002494 <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 9

    Organism-specific databases

    Rat genome database

    More...
    RGDi
    2395 Cps1

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

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

    Keywords - Cellular componenti

    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

    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>Mutagenesisi1391T → V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. 1 Publication1
    Mutagenesisi1394T → A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. 1 Publication1
    Mutagenesisi1410W → K: 60-fold increase in the activation constant of NAG. 1 Publication1
    Mutagenesisi1437N → D: 70-fold increase in the activation constant of NAG. 1 Publication1
    Mutagenesisi1440N → D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG. 1 Publication1

    <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 – 38MitochondrionAdd 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_000002989939 – 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; alternateBy similarity1
    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; alternateBy similarity1
    Modified residuei176N6-glutaryllysineBy similarity1
    Modified residuei182N6-acetyllysineBy similarity1
    Modified residuei189PhosphoserineCombined sources1
    Modified residuei197N6-acetyllysineBy similarity1
    Modified residuei207N6-acetyllysine; alternateBy similarity1
    Modified residuei207N6-glutaryllysine; alternateBy similarity1
    Modified residuei207N6-succinyllysine; alternateBy similarity1
    Modified residuei210N6-acetyllysine; alternateBy similarity1
    Modified residuei210N6-glutaryllysine; alternateBy similarity1
    Modified residuei214N6-acetyllysine; alternateBy similarity1
    Modified residuei214N6-glutaryllysine; alternateBy similarity1
    Modified residuei214N6-succinyllysine; alternateBy similarity1
    Modified residuei219N6-acetyllysine; alternateBy similarity1
    Modified residuei219N6-glutaryllysine; alternateBy similarity1
    Modified residuei228N6-acetyllysine; alternateBy similarity1
    Modified residuei228N6-glutaryllysine; alternateBy similarity1
    Modified residuei237N6-glutaryllysineBy similarity1
    Modified residuei279N6-acetyllysineBy similarity1
    Modified residuei280N6-acetyllysine; alternateBy similarity1
    Modified residuei280N6-glutaryllysine; alternateBy similarity1
    Modified residuei287N6-acetyllysine; alternateBy similarity1
    Modified residuei287N6-succinyllysine; alternateBy similarity1
    Modified residuei307N6-acetyllysine; alternateBy similarity1
    Modified residuei307N6-glutaryllysine; alternateBy similarity1
    Modified residuei307N6-succinyllysine; alternateBy similarity1
    Modified residuei310N6-acetyllysine; alternateBy similarity1
    Modified residuei310N6-glutaryllysine; alternateBy similarity1
    Modified residuei400N6-succinyllysineBy similarity1
    Modified residuei402N6-glutaryllysine; alternateBy similarity1
    Modified residuei402N6-succinyllysine; alternateBy similarity1
    Modified residuei412N6-acetyllysine; alternateBy similarity1
    Modified residuei412N6-glutaryllysine; alternateBy similarity1
    Modified residuei412N6-succinyllysine; alternateBy similarity1
    Modified residuei453N6-acetyllysine; alternateBy similarity1
    Modified residuei453N6-glutaryllysine; alternateBy similarity1
    Modified residuei458N6-acetyllysine; alternateBy similarity1
    Modified residuei458N6-glutaryllysine; alternateBy similarity1
    Modified residuei458N6-succinyllysine; alternateBy similarity1
    Modified residuei522N6-acetyllysine; alternateBy similarity1
    Modified residuei522N6-succinyllysine; alternateBy similarity1
    Modified residuei527N6-acetyllysine; alternateBy similarity1
    Modified residuei527N6-glutaryllysine; alternateBy similarity1
    Modified residuei527N6-succinyllysine; alternateBy similarity1
    Modified residuei532N6-acetyllysine; alternateBy similarity1
    Modified residuei532N6-glutaryllysine; alternateBy similarity1
    Modified residuei537Phosphoserine; alternateCombined sources1
    <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; alternate1 Publication1
    Modified residuei540PhosphoserineCombined sources1
    Modified residuei553N6-acetyllysine; alternateBy similarity1
    Modified residuei553N6-glutaryllysine; alternateBy similarity1
    Modified residuei553N6-succinyllysine; alternateBy similarity1
    Modified residuei560N6-acetyllysine; alternateBy similarity1
    Modified residuei560N6-succinyllysine; alternateBy similarity1
    Modified residuei569PhosphoserineBy similarity1
    Modified residuei575N6-acetyllysine; alternateBy similarity1
    Modified residuei575N6-succinyllysine; alternateBy similarity1
    Modified residuei603N6-acetyllysine; alternateBy similarity1
    Modified residuei603N6-succinyllysine; alternateBy similarity1
    Modified residuei612N6-acetyllysine; alternateBy similarity1
    Modified residuei612N6-succinyllysine; alternateBy similarity1
    Modified residuei630N6-acetyllysineBy similarity1
    Modified residuei728N6-glutaryllysineBy similarity1
    Modified residuei751N6-acetyllysine; alternateBy similarity1
    Modified residuei751N6-succinyllysine; alternateBy similarity1
    Modified residuei757N6-acetyllysine; alternateBy similarity1
    Modified residuei757N6-glutaryllysine; alternateBy similarity1
    Modified residuei757N6-succinyllysine; alternateBy similarity1
    Modified residuei772N6-acetyllysine; alternateBy similarity1
    Modified residuei772N6-glutaryllysine; alternateBy similarity1
    Modified residuei793N6-acetyllysine; alternateBy similarity1
    Modified residuei793N6-glutaryllysine; alternateBy similarity1
    Modified residuei793N6-succinyllysine; alternateBy similarity1
    Modified residuei811N6-acetyllysine; alternateBy similarity1
    Modified residuei811N6-glutaryllysine; alternateBy similarity1
    Modified residuei831N6-acetyllysine; alternateBy similarity1
    Modified residuei831N6-succinyllysine; alternateBy similarity1
    Modified residuei841N6-acetyllysine; alternateBy similarity1
    Modified residuei841N6-glutaryllysine; alternateBy similarity1
    Modified residuei856N6-acetyllysine; alternateBy similarity1
    Modified residuei856N6-glutaryllysine; alternateBy similarity1
    Modified residuei869N6-glutaryllysineBy similarity1
    Modified residuei875N6-acetyllysine; alternateBy similarity1
    Modified residuei875N6-glutaryllysine; alternateBy similarity1
    Modified residuei875N6-succinyllysine; alternateBy similarity1
    Modified residuei889N6-acetyllysine; alternateBy similarity1
    Modified residuei889N6-glutaryllysine; alternateBy similarity1
    Modified residuei889N6-succinyllysine; alternateBy similarity1
    Modified residuei892N6-acetyllysine; alternateBy similarity1
    Modified residuei892N6-glutaryllysine; alternateBy similarity1
    Modified residuei892N6-succinyllysine; alternateBy similarity1
    Modified residuei896PhosphoserineCombined sources1
    Modified residuei898PhosphoserineCombined sources1
    Modified residuei908N6-acetyllysine; alternateBy similarity1
    Modified residuei908N6-glutaryllysine; alternateBy similarity1
    Modified residuei915N6-acetyllysine; alternateBy similarity1
    Modified residuei915N6-glutaryllysine; alternateBy similarity1
    Modified residuei915N6-succinyllysine; alternateBy similarity1
    Modified residuei919N6-acetyllysine; alternateBy similarity1
    Modified residuei919N6-glutaryllysine; alternateBy similarity1
    Modified residuei919N6-succinyllysine; alternateBy similarity1
    Modified residuei935N6-acetyllysineBy similarity1
    Modified residuei1036PhosphoserineCombined sources1
    Modified residuei1074N6-acetyllysine; alternateBy similarity1
    Modified residuei1074N6-glutaryllysine; alternateBy similarity1
    Modified residuei1074N6-succinyllysine; alternateBy similarity1
    Modified residuei1079PhosphoserineBy similarity1
    Modified residuei1090PhosphoserineCombined sources1
    Modified residuei1093PhosphoserineCombined sources1
    Modified residuei1100N6-acetyllysine; alternateBy similarity1
    Modified residuei1100N6-succinyllysine; alternateBy similarity1
    Modified residuei1149N6-succinyllysineBy similarity1
    Modified residuei1168N6-acetyllysine; alternateBy similarity1
    Modified residuei1168N6-glutaryllysine; alternateBy similarity1
    Modified residuei1168N6-succinyllysine; alternateBy similarity1
    Modified residuei1183N6-acetyllysine; alternateBy similarity1
    Modified residuei1183N6-glutaryllysine; alternateBy similarity1
    Modified residuei1183N6-succinyllysine; alternateBy similarity1
    Modified residuei1203PhosphoserineBy similarity1
    Modified residuei1222N6-acetyllysineBy similarity1
    Modified residuei1224N6-glutaryllysineBy similarity1
    Modified residuei1232N6-acetyllysine; alternateBy similarity1
    Modified residuei1232N6-succinyllysine; alternateBy similarity1
    Modified residuei1269N6-acetyllysine; alternateBy similarity1
    Modified residuei1269N6-succinyllysine; alternateBy similarity1
    Modified residuei1291N6-acetyllysine; alternateBy similarity1
    Modified residuei1291N6-succinyllysine; alternateBy similarity1
    Glycosylationi1331O-linked (GlcNAc) serine1 Publication1
    Glycosylationi1332O-linked (GlcNAc) threonine1 Publication1
    Modified residuei1356N6-acetyllysine; alternateBy similarity1
    Modified residuei1356N6-glutaryllysine; alternateBy similarity1
    Modified residuei1356N6-succinyllysine; alternateBy similarity1
    Modified residuei1360N6-glutaryllysine; alternateBy similarity1
    Modified residuei1360N6-succinyllysine; alternateBy similarity1
    Modified residuei1419PhosphoserineBy similarity1
    Modified residuei1431PhosphoserineCombined sources1
    Modified residuei1444N6-acetyllysine; alternateBy similarity1
    Modified residuei1444N6-succinyllysine; alternateBy similarity1
    Modified residuei1471N6-acetyllysine; alternateBy similarity1
    Modified residuei1471N6-succinyllysine; alternateBy similarity1
    Modified residuei1479N6-acetyllysine; alternateBy similarity1
    Modified residuei1479N6-glutaryllysine; alternateBy similarity1
    Modified residuei1479N6-succinyllysine; alternateBy similarity1
    Modified residuei1486N6-acetyllysine; alternateBy similarity1
    Modified residuei1486N6-glutaryllysine; alternateBy similarity1
    Modified residuei1486N6-succinyllysine; alternateBy similarity1

    <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

    50% of the mature protein that was isolated had Leu-39 as its N-terminal residue and 50% had Ser-40 suggesting two adjacent processing sites. However, the possibility of proteolytic removal of Leu-39 during the isolation of the enzyme cannot be excluded. Undergoes proteolytic cleavage in the C-terminal region corresponding to the loss of approximately 12 AA residues from the C-terminus (PubMed:23649895).1 Publication
    Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation (By similarity).By similarity
    Glutarylated. Glutarylation levels increase during fasting. Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-892, Lys-915, Lys-1360 and Lys-1486, leading to activation.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P07756

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

    More...
    PaxDbi
    P07756

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P07756

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P07756

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P07756

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

    More...
    PhosphoSitePlusi
    P07756

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P07756

    <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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Primarily in the liver and small intestine.

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSRNOG00000013704 Expressed in 6 organ(s), highest expression level in liver

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P07756 RN

    <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

    Can form homooligomers (monomers as predominant form and dimers).

    By similarity

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P07756, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    10116.ENSRNOP00000019021

    <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

    3D structure databases

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

    More...
    SMRi
    P07756

    Database of comparative protein structure models

    More...
    ModBasei
    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>Domaini219 – 404Glutamine amidotransferase type-1Add BLAST186
    Domaini551 – 743ATP-grasp 1Add BLAST193
    Domaini1093 – 1284ATP-grasp 2Add BLAST192
    Domaini1355 – 1500MGS-likePROSITE-ProRule annotationAdd BLAST146

    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>Regioni39 – 218Anthranilate phosphoribosyltransferase homologAdd BLAST180

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The type-1 glutamine amidotransferase domain is defective.

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0370 Eukaryota
    COG0458 LUCA
    COG0505 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157192

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000234583

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P07756

    KEGG Orthology (KO)

    More...
    KOi
    K01948

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    AVFPFNK

    Database of Orthologous Groups

    More...
    OrthoDBi
    273358at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P07756

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01744 GATase1_CPSase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.1030.10, 1 hit
    3.30.1490.20, 1 hit
    3.40.50.1380, 1 hit
    3.40.50.880, 1 hit
    3.50.30.20, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01209 CPSase_S_chain, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    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
    IPR041557 CPSase_C
    IPR035686 CPSase_GATase1
    IPR017926 GATASE
    IPR011607 MGS-like_dom
    IPR036914 MGS-like_dom_sf
    IPR016185 PreATP-grasp_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF18302 CPSase_C, 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

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    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
    SSF52021 SSF52021, 1 hit
    SSF52317 SSF52317, 1 hit
    SSF52335 SSF52335, 1 hit
    SSF52440 SSF52440, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    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
    PS00866 CPSASE_1, 2 hits
    PS00867 CPSASE_2, 2 hits
    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>Sequencei

    <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.

    P07756-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL
    60 70 80 90 100
    EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI
    110 120 130 140 150
    IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSHDY NHWLATKSLG
    160 170 180 190 200
    QWLQEEKVPA IYGVDTRMLT KIIRDKGTML GKIEFEGQSV DFVDPNKQNL
    210 220 230 240 250
    IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA EVHLVPWNHD
    260 270 280 290 300
    FTQMDYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT
    310 320 330 340 350
    GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK
    360 370 380 390 400
    PLFVNVNDQT NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK
    410 420 430 440 450
    GKGTTITSVL PKPALVASRV EVSKVLILGS GGLSIGQAGE FDYSGSQAVK
    460 470 480 490 500
    AMKEENVKTV LMNPNIASVQ TNEVGLKQAD AVYFLPITPQ FVTEVIKAER
    510 520 530 540 550
    PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES IMATEDRQLF
    560 570 580 590 600
    SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC
    610 620 630 640 650
    PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM
    660 670 680 690 700
    ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ
    710 720 730 740 750
    FALHPTSMEY CIIEVNARLS RSSALASKAT GYPLAFIAAK IALGIPLPEI
    760 770 780 790 800
    KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR FHGTSSRIGS SMKSVGEVMA
    810 820 830 840 850
    IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR KELSEPSSTR
    860 870 880 890 900
    IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT
    910 920 930 940 950
    EETLRQAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE
    960 970 980 990 1000
    YPSVTNYLYV TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI
    1010 1020 1030 1040 1050
    RTLRQLGKKT VVVNCNPETV STDFDECDKL YFEELSLERI LDIYHQEACN
    1060 1070 1080 1090 1100
    GCIISVGGQI PNNLAVPLYK NGVKIMGTSP LQIDRAEDRS IFSAVLDELK
    1110 1120 1130 1140 1150
    VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN VVFSEDEMKR
    1160 1170 1180 1190 1200
    FLEEATRVSQ EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG
    1210 1220 1230 1240 1250
    VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND
    1260 1270 1280 1290 1300
    VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI
    1310 1320 1330 1340 1350
    IPSDYVAIKA PMFSWPRLRD ADPILRCEMA STGEVACFGE GIHTAFLKAM
    1360 1370 1380 1390 1400
    LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ LHNEGFKLFA TEATSDWLNA
    1410 1420 1430 1440 1450
    NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN NNTKFVHDNY
    1460 1470 1480 1490 1500
    VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA
    Length:1,500
    Mass (Da):164,580
    Last modified:August 1, 1988 - v1
    <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:i038E8F893DE1C34D
    GO

    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
    M12335 M12328 Genomic DNA Translation: AAB59717.1
    J02805 Genomic DNA Translation: AAA40959.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A28481 SYRTCA

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_058768.1, NM_017072.2
    XP_017452081.1, XM_017596592.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    497840

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:497840

    UCSC genome browser

    More...
    UCSCi
    RGD:2395 rat

    <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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M12335 M12328 Genomic DNA Translation: AAB59717.1
    J02805 Genomic DNA Translation: AAA40959.1
    PIRiA28481 SYRTCA
    RefSeqiNP_058768.1, NM_017072.2
    XP_017452081.1, XM_017596592.1

    3D structure databases

    SMRiP07756
    ModBaseiSearch...

    Protein-protein interaction databases

    IntActiP07756, 1 interactor
    STRINGi10116.ENSRNOP00000019021

    PTM databases

    CarbonylDBiP07756
    iPTMnetiP07756
    PhosphoSitePlusiP07756
    SwissPalmiP07756

    Proteomic databases

    jPOSTiP07756
    PaxDbiP07756
    PRIDEiP07756

    Genome annotation databases

    EnsembliENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704
    GeneIDi497840
    KEGGirno:497840
    UCSCiRGD:2395 rat

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    1373
    RGDi2395 Cps1

    Phylogenomic databases

    eggNOGiKOG0370 Eukaryota
    COG0458 LUCA
    COG0505 LUCA
    GeneTreeiENSGT00940000157192
    HOGENOMiHOG000234583
    InParanoidiP07756
    KOiK01948
    OMAiAVFPFNK
    OrthoDBi273358at2759
    PhylomeDBiP07756

    Enzyme and pathway databases

    ReactomeiR-RNO-70635 Urea cycle
    SABIO-RKiP07756

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P07756

    Gene expression databases

    BgeeiENSRNOG00000013704 Expressed in 6 organ(s), highest expression level in liver
    GenevisibleiP07756 RN

    Family and domain databases

    CDDicd01744 GATase1_CPSase, 1 hit
    Gene3Di1.10.1030.10, 1 hit
    3.30.1490.20, 1 hit
    3.40.50.1380, 1 hit
    3.40.50.880, 1 hit
    3.50.30.20, 1 hit
    HAMAPiMF_01209 CPSase_S_chain, 1 hit
    InterProiView protein in InterPro
    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
    IPR041557 CPSase_C
    IPR035686 CPSase_GATase1
    IPR017926 GATASE
    IPR011607 MGS-like_dom
    IPR036914 MGS-like_dom_sf
    IPR016185 PreATP-grasp_dom_sf
    PfamiView protein in Pfam
    PF18302 CPSase_C, 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
    PRINTSiPR00098 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
    SSF52021 SSF52021, 1 hit
    SSF52317 SSF52317, 1 hit
    SSF52335 SSF52335, 1 hit
    SSF52440 SSF52440, 2 hits
    TIGRFAMsiTIGR01369 CPSaseII_lrg, 1 hit
    TIGR01368 CPSaseIIsmall, 1 hit
    PROSITEiView protein in PROSITE
    PS50975 ATP_GRASP, 2 hits
    PS00866 CPSASE_1, 2 hits
    PS00867 CPSASE_2, 2 hits
    PS51273 GATASE_TYPE_1, 1 hit
    PS51855 MGS, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCPSM_RAT
    <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: P07756
    <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, 1988
    Last sequence update: August 1, 1988
    Last modified: December 11, 2019
    This is version 176 of the entry and version 1 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

    <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

    Reference proteome
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