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Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene

Cps1

Organism
Mus musculus (Mouse)
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.1 Publication

Caution

Was initially reported to be deacetylated by Sirt5 (PubMed:19410549). However, it was later shown that Sirt5 has poor deacetylase activity and mediates desuccinylation of Cps1 instead (PubMed:22076378).2 Publications

<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.By similarity

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 activatorBy similarity1
Binding sitei1394Allosteric activatorBy similarity1
Binding sitei1410Allosteric activatorBy similarity1
Binding sitei1437Allosteric activatorBy similarity1
Binding sitei1440Allosteric activatorBy similarity1
Binding sitei1449Allosteric activatorBy similarity1

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.4.16 3474

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q8C196

<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 1

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:891996 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; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Nucleus

<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_000002989839 – 1500Carbamoyl-phosphate synthase [ammonia], mitochondrialBy similarityAdd 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 residuei44N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei44N6-succinyllysine; alternateCombined sources1 Publication1
Modified residuei55N6-acetyllysine; alternateCombined sources1
Modified residuei55N6-glutaryllysine; alternateBy similarity1
Modified residuei55N6-succinyllysine; alternateCombined sources1
Modified residuei57N6-acetyllysine; alternateCombined sources1
Modified residuei57N6-succinyllysine; alternateCombined sources1
Modified residuei119N6-acetyllysine; alternateCombined sources1
Modified residuei119N6-succinyllysine; alternateCombined sources1
Modified residuei148PhosphoserineCombined sources1
Modified residuei157N6-acetyllysine; alternateCombined sources1
Modified residuei157N6-succinyllysine; alternateCombined sources1
Modified residuei171N6-acetyllysine; alternateCombined sources1
Modified residuei171N6-glutaryllysine; alternateBy similarity1
Modified residuei176N6-glutaryllysineBy similarity1
Modified residuei182N6-acetyllysineCombined sources1
Modified residuei189PhosphoserineBy similarity1
Modified residuei197N6-acetyllysineCombined sources1
Modified residuei207N6-acetyllysine; alternateCombined sources1
Modified residuei207N6-glutaryllysine; alternateBy similarity1
Modified residuei207N6-succinyllysine; alternateCombined sources1
Modified residuei210N6-acetyllysine; alternateCombined sources1
Modified residuei210N6-glutaryllysine; alternateBy similarity1
Modified residuei214N6-acetyllysine; alternateCombined sources1
Modified residuei214N6-glutaryllysine; alternateBy similarity1
Modified residuei214N6-succinyllysine; alternateCombined sources1
Modified residuei219N6-acetyllysine; alternateCombined sources1
Modified residuei219N6-glutaryllysine; alternateBy similarity1
Modified residuei228N6-acetyllysine; alternateCombined sources1
Modified residuei228N6-glutaryllysine; alternateBy similarity1
Modified residuei237N6-glutaryllysineBy similarity1
Modified residuei279N6-acetyllysineCombined sources1
Modified residuei280N6-acetyllysine; alternateCombined sources1
Modified residuei280N6-glutaryllysine; alternateBy similarity1
Modified residuei287N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei287N6-succinyllysine; alternateCombined sources1 Publication1
Modified residuei307N6-acetyllysine; alternateCombined sources1
Modified residuei307N6-glutaryllysine; alternateBy similarity1
Modified residuei307N6-succinyllysine; alternateCombined sources1
Modified residuei310N6-acetyllysine; alternateCombined sources1
Modified residuei310N6-glutaryllysine; alternateBy similarity1
Modified residuei400N6-succinyllysineCombined sources1
Modified residuei402N6-glutaryllysine; alternateBy similarity1
Modified residuei402N6-succinyllysine; alternateCombined sources1
Modified residuei412N6-acetyllysine; alternateCombined sources1
Modified residuei412N6-glutaryllysine; alternateBy similarity1
Modified residuei412N6-succinyllysine; alternateCombined sources1
Modified residuei453N6-acetyllysine; alternateCombined sources1
Modified residuei453N6-glutaryllysine; alternateBy similarity1
Modified residuei458N6-acetyllysine; alternateCombined sources1
Modified residuei458N6-glutaryllysine; alternateBy similarity1
Modified residuei458N6-succinyllysine; alternateCombined sources1
Modified residuei522N6-acetyllysine; alternateCombined sources1
Modified residuei522N6-succinyllysine; alternateCombined sources1
Modified residuei527N6-acetyllysine; alternateCombined sources1
Modified residuei527N6-glutaryllysine; alternateBy similarity1
Modified residuei527N6-succinyllysine; alternateCombined sources1
Modified residuei532N6-acetyllysine; alternateCombined sources1
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; alternateBy similarity1
Modified residuei540PhosphoserineBy similarity1
Modified residuei553N6-acetyllysine; alternateCombined sources1
Modified residuei553N6-glutaryllysine; alternateBy similarity1
Modified residuei553N6-succinyllysine; alternateCombined sources1
Modified residuei560N6-acetyllysine; alternateCombined sources1
Modified residuei560N6-succinyllysine; alternateCombined sources1
Modified residuei569PhosphoserineBy similarity1
Modified residuei575N6-acetyllysine; alternateCombined sources1
Modified residuei575N6-succinyllysine; alternateCombined sources1
Modified residuei603N6-acetyllysine; alternateCombined sources1
Modified residuei603N6-succinyllysine; alternateCombined sources1
Modified residuei612N6-acetyllysine; alternateCombined sources1
Modified residuei612N6-succinyllysine; alternateCombined sources1
Modified residuei630N6-acetyllysineCombined sources1
Modified residuei728N6-glutaryllysineBy similarity1
Modified residuei751N6-acetyllysine; alternateCombined sources1
Modified residuei751N6-succinyllysine; alternateCombined sources1
Modified residuei757N6-acetyllysine; alternateCombined sources1
Modified residuei757N6-glutaryllysine; alternateBy similarity1
Modified residuei757N6-succinyllysine; alternateCombined sources1
Modified residuei772N6-acetyllysine; alternateCombined sources1
Modified residuei772N6-glutaryllysine; alternateBy similarity1
Modified residuei793N6-acetyllysine; alternateCombined sources1
Modified residuei793N6-glutaryllysine; alternateBy similarity1
Modified residuei793N6-succinyllysine; alternateCombined sources1
Modified residuei811N6-acetyllysine; alternateCombined sources1
Modified residuei811N6-glutaryllysine; alternateBy similarity1
Modified residuei831N6-acetyllysine; alternateCombined sources1
Modified residuei831N6-succinyllysine; alternateCombined sources1
Modified residuei840N6-acetyllysine; alternateCombined sources1
Modified residuei840N6-succinyllysine; alternateCombined sources1
Modified residuei841N6-acetyllysine; alternateCombined sources1
Modified residuei841N6-glutaryllysine; alternateBy similarity1
Modified residuei856N6-acetyllysine; alternateCombined sources1
Modified residuei856N6-glutaryllysine; alternateBy similarity1
Modified residuei875N6-acetyllysine; alternateCombined sources1
Modified residuei875N6-glutaryllysine; alternateBy similarity1
Modified residuei875N6-succinyllysine; alternateCombined sources1
Modified residuei889N6-acetyllysine; alternateCombined sources1
Modified residuei889N6-glutaryllysine; alternateBy similarity1
Modified residuei889N6-succinyllysine; alternateCombined sources1
Modified residuei892N6-acetyllysine; alternateCombined sources1
Modified residuei892N6-glutaryllysine; alternateBy similarity1
Modified residuei892N6-succinyllysine; alternateCombined sources1
Modified residuei896PhosphoserineBy similarity1
Modified residuei898PhosphoserineBy similarity1
Modified residuei908N6-acetyllysine; alternateCombined sources1
Modified residuei908N6-glutaryllysine; alternateBy similarity1
Modified residuei915N6-acetyllysine; alternateCombined sources1
Modified residuei915N6-glutaryllysine; alternateBy similarity1
Modified residuei915N6-succinyllysine; alternateCombined sources1
Modified residuei919N6-acetyllysine; alternateCombined sources1
Modified residuei919N6-glutaryllysine; alternateBy similarity1
Modified residuei919N6-succinyllysine; alternateCombined sources1
Modified residuei935N6-acetyllysineCombined sources1
Modified residuei1036PhosphoserineBy similarity1
Modified residuei1074N6-acetyllysine; alternateCombined sources1
Modified residuei1074N6-glutaryllysine; alternateBy similarity1
Modified residuei1074N6-succinyllysine; alternateCombined sources1
Modified residuei1079PhosphoserineCombined sources1
Modified residuei1090PhosphoserineBy similarity1
Modified residuei1093PhosphoserineBy similarity1
Modified residuei1100N6-acetyllysine; alternateCombined sources1
Modified residuei1100N6-succinyllysine; alternateCombined sources1
Modified residuei1149N6-succinyllysineCombined sources1
Modified residuei1168N6-acetyllysine; alternateCombined sources1
Modified residuei1168N6-glutaryllysine; alternateBy similarity1
Modified residuei1168N6-succinyllysine; alternateCombined sources1
Modified residuei1183N6-acetyllysine; alternateCombined sources1
Modified residuei1183N6-glutaryllysine; alternateBy similarity1
Modified residuei1183N6-succinyllysine; alternateCombined sources1
Modified residuei1203PhosphoserineBy similarity1
Modified residuei1222N6-acetyllysineCombined sources1
Modified residuei1224N6-glutaryllysineBy similarity1
Modified residuei1232N6-acetyllysine; alternateCombined sources1
Modified residuei1232N6-succinyllysine; alternateCombined sources1
Modified residuei1269N6-acetyllysine; alternateCombined sources1
Modified residuei1269N6-succinyllysine; alternateCombined sources1
Modified residuei1291N6-acetyllysine; alternateCombined sources2 Publications1
Modified residuei1291N6-succinyllysine; alternateCombined sources1 Publication1
Glycosylationi1331O-linked (GlcNAc) serineBy similarity1
Glycosylationi1332O-linked (GlcNAc) threonineBy similarity1
Modified residuei1356N6-acetyllysine; alternateCombined sources1
Modified residuei1356N6-glutaryllysine; alternateBy similarity1
Modified residuei1356N6-succinyllysine; alternateCombined sources1
Modified residuei1360N6-glutaryllysine; alternateBy similarity1
Modified residuei1360N6-succinyllysine; alternateCombined sources1
Modified residuei1419PhosphoserineBy similarity1
Modified residuei1431PhosphoserineBy similarity1
Modified residuei1444N6-acetyllysine; alternateCombined sources1
Modified residuei1444N6-succinyllysine; alternateCombined sources1
Modified residuei1471N6-acetyllysine; alternateCombined sources1
Modified residuei1471N6-succinyllysine; alternateCombined sources1
Modified residuei1479N6-acetyllysine; alternateCombined sources1
Modified residuei1479N6-glutaryllysine; alternateBy similarity1
Modified residuei1479N6-succinyllysine; alternateCombined sources1
Modified residuei1486N6-acetyllysine; alternateCombined sources1
Modified residuei1486N6-glutaryllysine; alternateBy similarity1
Modified residuei1486N6-succinyllysine; alternateCombined 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

Undergoes proteolytic cleavage in the C-terminal region corresponding to the loss of approximately 12 AA residues from the C-terminus.By similarity
Acetylation of Lys-287, Lys-603, Lys-841 and Lys-1291 is observed in liver mitochondria from fasted mice but not from fed mice.2 Publications
Succinylated at Lys-44, Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation.1 Publication
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 similarity1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
Q8C196

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

More...
PaxDbi
Q8C196

PeptideAtlas

More...
PeptideAtlasi
Q8C196

PRoteomics IDEntifications database

More...
PRIDEi
Q8C196

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8C196

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

More...
PhosphoSitePlusi
Q8C196

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8C196

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000025991 Expressed in 76 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

More...
CleanExi
MM_CPS1

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8C196 MM

<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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Sirt5Q8K2C62EBI-2348828,EBI-2348809

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
230602, 1 interactor

Protein interaction database and analysis system

More...
IntActi
Q8C196, 5 interactors

Molecular INTeraction database

More...
MINTi
Q8C196

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000027144

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q8C196

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

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SMRi
Q8C196

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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.By similarity

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

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000279

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8C196

KEGG Orthology (KO)

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KOi
K01948

Identification of Orthologs from Complete Genome Data

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OMAi
AVFPFNK

Database of Orthologous Groups

More...
OrthoDBi
EOG091G00DC

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8C196

TreeFam database of animal gene trees

More...
TreeFami
TF331485

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

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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
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
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

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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

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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

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TIGRFAMsi
TIGR01369 CPSaseII_lrg, 1 hit
TIGR01368 CPSaseIIsmall, 1 hit

PROSITE; a protein domain and family database

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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>.<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.

Q8C196-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTRILTACKV VKTLKSGFGF ANVTTKRQWD FSRPGIRLLS VKAKTAHIVL
60 70 80 90 100
EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY PEALTDPAYK GQILTMANPI
110 120 130 140 150
IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSNDY 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
FTQMEYDGLL 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
PNKETLIDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM
660 670 680 690 700
ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSVNVVRH 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 KEWPANLDLK KELSEPSSTR
860 870 880 890 900
IYAIAKALEN NMSLDEIVRL TSIDKWFLYK MRDILNMDKT LKGLNSDSVT
910 920 930 940 950
EETLRKAKEI 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 EHPVVLTKFV EGAREVEMDA VGKEGRVISH AISEHVEDAG
1210 1220 1230 1240 1250
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND
1260 1270 1280 1290 1300
VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESIDE KRLPTLEQPI
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 KLFAEAVQKS RTVDSKSLFH YRQYSAGKAA
Length:1,500
Mass (Da):164,618
Last modified:August 30, 2005 - v2
<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:i84A7268C1D7E8101
GO

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 conflicti931 – 934LRLK → HASE in AAH67211 (PubMed:15489334).Curated4

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AC101854 Genomic DNA No translation available.
AC133187 Genomic DNA No translation available.
BC067211 mRNA Translation: AAH67211.1
BC126969 mRNA Translation: AAI26970.1
AK028683 mRNA Translation: BAC26064.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS35605.1

NCBI Reference Sequences

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RefSeqi
NP_001074278.1, NM_001080809.2
XP_011236802.1, XM_011238500.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.343942

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000027144; ENSMUSP00000027144; ENSMUSG00000025991

Database of genes from NCBI RefSeq genomes

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GeneIDi
227231

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:227231

UCSC genome browser

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UCSCi
uc007biy.2 mouse

<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
AC101854 Genomic DNA No translation available.
AC133187 Genomic DNA No translation available.
BC067211 mRNA Translation: AAH67211.1
BC126969 mRNA Translation: AAI26970.1
AK028683 mRNA Translation: BAC26064.1
CCDSiCCDS35605.1
RefSeqiNP_001074278.1, NM_001080809.2
XP_011236802.1, XM_011238500.1
UniGeneiMm.343942

3D structure databases

ProteinModelPortaliQ8C196
SMRiQ8C196
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230602, 1 interactor
IntActiQ8C196, 5 interactors
MINTiQ8C196
STRINGi10090.ENSMUSP00000027144

PTM databases

iPTMnetiQ8C196
PhosphoSitePlusiQ8C196
SwissPalmiQ8C196

Proteomic databases

MaxQBiQ8C196
PaxDbiQ8C196
PeptideAtlasiQ8C196
PRIDEiQ8C196

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027144; ENSMUSP00000027144; ENSMUSG00000025991
GeneIDi227231
KEGGimmu:227231
UCSCiuc007biy.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1373
MGIiMGI:891996 Cps1

Phylogenomic databases

eggNOGiKOG0370 Eukaryota
COG0458 LUCA
COG0505 LUCA
GeneTreeiENSGT00940000157192
HOGENOMiHOG000234583
HOVERGENiHBG000279
InParanoidiQ8C196
KOiK01948
OMAiAVFPFNK
OrthoDBiEOG091G00DC
PhylomeDBiQ8C196
TreeFamiTF331485

Enzyme and pathway databases

BRENDAi6.3.4.16 3474
ReactomeiR-MMU-70635 Urea cycle
SABIO-RKiQ8C196

Miscellaneous databases

Protein Ontology

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PROi
PR:Q8C196

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000025991 Expressed in 76 organ(s), highest expression level in liver
CleanExiMM_CPS1
GenevisibleiQ8C196 MM

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
IPR035686 CPSase_GATase1
IPR017926 GATASE
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR016185 PreATP-grasp_dom_sf
PfamiView protein in Pfam
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

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ProtoNeti
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_MOUSE
<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: Q8C196
Secondary accession number(s): A0JNU4, Q6NX75
<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 30, 2005
Last sequence update: August 30, 2005
Last modified: December 5, 2018
This is version 144 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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