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Entry version 124 (17 Jun 2020)
Sequence version 1 (01 Mar 2003)
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Protein

Cyclic GMP-AMP synthase

Gene

Cgas

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

Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (cGAMP) from ATP and GTP and plays a key role in innate immunity (PubMed:23258413, PubMed:23647843, PubMed:23722158, PubMed:26829768, PubMed:28214358). Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p] (PubMed:23258413, PubMed:23647843, PubMed:23722158, PubMed:26829768, PubMed:28214358). Acts as a key cytosolic DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses (PubMed:23722158, PubMed:28363908, PubMed:28314590). Binds cytosolic DNA directly, leading to activation and synthesis of cGAMP, a second messenger that binds to and activates TMEM173/STING, thereby triggering type-I interferon production (PubMed:23722158, PubMed:28363908, PubMed:28314590). Preferentially binds long dsDNA (around 45 bp) and forms ladder-like networks that function cooperatively to stabilize individual cGAS-dsDNA complexes (PubMed:28902841). Has antiviral activity by sensing the presence of dsDNA from DNA viruses in the cytoplasm (PubMed:23258413, PubMed:23647843, PubMed:23722158). Also acts as an innate immune sensor of infection by retroviruses by detecting the presence of reverse-transcribed DNA in the cytosol (PubMed:23929945). Detection of retroviral reverse-transcribed DNA in the cytosol may be indirect and be mediated via interaction with PQBP1, which directly binds reverse-transcribed retroviral DNA (By similarity). Also detects the presence of DNA from bacteria (By similarity). cGAMP can be transferred from producing cells to neighboring cells through gap junctions, leading to promote TMEM173/STING activation and convey immune response to connecting cells (PubMed:24077100). cGAMP can also be transferred between cells by virtue of packaging within viral particles contributing to IFN-induction in newly infected cells in a cGAS-independent but TMEM173/STING-dependent manner (PubMed:26229117). In addition to antiviral activity, also involved in the response to cellular stresses, such as senescence, DNA damage or genome instability (PubMed:28738408, PubMed:28759028). Acts as a regulator of cellular senescence by binding to cytosolic chromatin fragments that are present in senescent cells, leading to trigger type-I interferon production via TMEM173/STING and promote cellular senescence (PubMed:28759028). Also involved in the inflammatory response to genome instability and double-stranded DNA breaks: acts by localizing to micronuclei arising from genome instability (PubMed:28738408). Micronuclei, which as frequently found in cancer cells, consist of chromatin surrounded by its own nuclear membrane: following breakdown of the micronuclear envelope, a process associated with chromothripsis, CGAS binds self-DNA exposed to the cytosol, leading to cGAMP synthesis and subsequent activation of TMEM173/STING and type-I interferon production (PubMed:28738408). Acts as a suppressor of DNA repair in response to DNA damage: translocates to the nucleus following dephosphorylation at Tyr-201 and inhibits homologous recombination repair by interacting with PARP1, the CGAS-PARP1 interaction leading to impede the formation of the PARP1-TIMELESS complex (PubMed:30356214).By similarity14 Publications

Caution

Was reported to homodimerize in presence of double-stranded DNA (dsDNA) (PubMed:24332030). However, this result was based on a structure lacking the N-terminal part (1-146), which caused homodimerization in presence of dsDNA (PubMed:28214358).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Nucleotidyltransferase activity is stimulated by double-stranded DNA but not RNA (By similarity). Acetylation at Lys-372, Lys-382 and Lys-402 inhibits the cyclic GMP-AMP synthase activity (By similarity). The enzyme activity is impaired by the cleavage by CASP1 (PubMed:28314590). Strongly inhibited by compound RU.521, which is specific for mouse protein (PubMed:28963528, PubMed:30007416).By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei197GTP1 Publication1
Binding sitei199ATP1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi211Magnesium; catalytic1 Publication1
Metal bindingi213Magnesium; catalytic1 Publication1
Metal bindingi307Magnesium; catalytic1 Publication1
Binding sitei307GTP1 Publication1
Binding sitei371ATP1 Publication1
Metal bindingi378Zinc; via tele nitrogenCombined sources5 Publications1
Metal bindingi384ZincCombined sources5 Publications1
Metal bindingi385ZincCombined sources5 Publications1
Metal bindingi392ZincCombined sources5 Publications1
Binding sitei402ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi364 – 371GTP1 Publication8
Nucleotide bindingi420 – 424ATP1 Publication5

<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 functionDNA-binding, Nucleotidyltransferase, Transferase
Biological processAntiviral defense, DNA damage, DNA repair, Immunity, Innate immunity
LigandATP-binding, GTP-binding, Lipid-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.86 3474

<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%5Fand%5Ftaxonomy%5Fsection">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:
Cyclic GMP-AMP synthase1 Publication (EC:2.7.7.864 Publications)
Short name:
cGAMP synthase1 Publication
Short name:
cGAS1 Publication
Short name:
m-cGAS1 Publication
Alternative name(s):
2'3'-cGAMP synthase1 Publication
Mab-21 domain-containing protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Cgas1 PublicationImported
Synonyms:Mb21d1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

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

More...
MGIi
MGI:2442261 Cgas

<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

Cell membrane, Cytoplasm, Membrane, 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi172N → K: Induces alteration of the DNA-binding surface and leads to decreased synthesis of cyclic GMP-AMP (cGAMP); when associated with L-180. 1 Publication1
Mutagenesisi180R → L: Induces alteration of the DNA-binding surface and leads to decreased synthesis of cyclic GMP-AMP (cGAMP); when associated with K-182. 1 Publication1
Mutagenesisi198G → A: Abolishes stimulation of interferon production; when associated with A-199. 1 Publication1
Mutagenesisi199S → A: Abolishes stimulation of interferon production; when associated with A-199. 1 Publication1
Mutagenesisi211E → A: Abolishes ability to promote type-I interferon production. 1 Publication1
Mutagenesisi213D → A: Abolishes ability to promote type-I interferon production. 1 Publication1
Mutagenesisi272E → A: Increased DNA-binding activity. 1 Publication1
Mutagenesisi302E → A: Increased nucleotidyltransferase activity. 1 Publication1
Mutagenesisi419C → S: Gains susceptibility to mouse-specific RU.521; when associated with N-467. 1 Publication1
Mutagenesisi467H → N: Gains susceptibility to mouse-specific RU.521; when associated with S-419. 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 polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004217641 – 507Cyclic GMP-AMP synthaseAdd BLAST507

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 residuei201PhosphotyrosineBy similarity1
Modified residuei2725-glutamyl polyglutamate1 Publication1
Modified residuei3025-glutamyl glutamate1 Publication1
Modified residuei372N6-acetyllysineBy similarity1
Modified residuei382N6-acetyllysineBy similarity1
Modified residuei402N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Polyglutamylated by TTLL6 at Glu-272, leading to impair DNA-binding activity. Monoglutamylated at Glu-302 by TTLL4, leading to impair the nucleotidyltransferase activity. Deglutamylated by AGBL5/CCP5 and AGBL6/CCP6.1 Publication
Cleaved by CASP1 upon DNA virus infection; the cleavage impairs cGAMP production (PubMed:28314590). Also cleaved by the pyroptotic CASP4 during non-canonical inflammasome activation; does not cut at the same sites than CASP1 (PubMed:28314590).1 Publication
Phosphorylation at Tyr-201 by BLK promotes cytosolic retention. Translocates into the nucleus following dephosphorylation at Tyr-201.By similarity
Acetylation at Lys-372, Lys-382 and Lys-402 inhibits the cyclic GMP-AMP synthase activity. Deacetylated upon cytosolic DNA challenge such as viral infections.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8C6L5

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q8C6L5

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

More...
PaxDbi
Q8C6L5

PRoteomics IDEntifications database

More...
PRIDEi
Q8C6L5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8C6L5

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

More...
PhosphoSitePlusi
Q8C6L5

<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

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Bgeei
ENSMUSG00000032344 Expressed in embryo and 119 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q8C6L5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8C6L5 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer in the absence of DNA (PubMed:28214358). Homodimer in presence of dsDNA: forms a 2:2 dimer with two enzymes binding to two DNA molecules (PubMed:28902841).

Interacts with PQBP1 (via WW domain) (By similarity).

Interacts with TRIM14; this interaction stabilizes CGAS and promotes type I interferon production (By similarity).

Interacts with ZCCHC3; promoting sensing of dsDNA by CGAS (By similarity).

Interacts with PARP1; interaction takes place in the nucleus and prevents the formation of the PARP1-TIMELESS complex (By similarity).

By similarity2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000063331

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q8C6L5 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1507
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q8C6L5

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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>Regioni1 – 146DNA-binding1 PublicationAdd BLAST146
Regioni48 – 59Required for association with the cell membraneBy similarityAdd BLAST12
Regioni119 – 132Required for activation upon DNA viral infection1 PublicationAdd BLAST14
Regioni158 – 201DNA-bindingCombined sources3 PublicationsAdd BLAST44
Regioni372 – 395DNA-bindingCombined sources3 PublicationsAdd BLAST24

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi281 – 291Nuclear localization signalBy similarityAdd BLAST11

<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 N-terminal part (1-146) binds unspecifically dsDNA and expand the binding and moving range of CGAS on dsDNA. Enhances the enzyme activity and activation of innate immune signaling upon cytosolic recognition of dsDNA (PubMed:28363908, PubMed:28214358, PubMed:28314590). When the N-terminal part (1-146) is missing the protein bound to dsDNA homodimerizes (PubMed:28214358).3 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the mab-21 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IE27 Eukaryota
ENOG410XTKD LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00980000198551

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_040428_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8C6L5

KEGG Orthology (KO)

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KOi
K17834

Identification of Orthologs from Complete Genome Data

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OMAi
VKCCRKE

Database of Orthologous Groups

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OrthoDBi
759341at2759

TreeFam database of animal gene trees

More...
TreeFami
TF331255

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR024810 Mab-21_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03281 Mab-21, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01265 Mab-21, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q8C6L5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEDPRRRTTA PRAKKPSAKR APTQPSRTRA HAESCGPQRG ARSRRAERDG
60 70 80 90 100
DTTEKPRAPG PRVHPARATE LTKDAQPSAM DAAGATARPA VRVPQQQAIL
110 120 130 140 150
DPELPAVREP QPPADPEARK VVRGPSHRRG ARSTGQPRAP RGSRKEPDKL
160 170 180 190 200
KKVLDKLRLK RKDISEAAET VNKVVERLLR RMQKRESEFK GVEQLNTGSY
210 220 230 240 250
YEHVKISAPN EFDVMFKLEV PRIELQEYYE TGAFYLVKFK RIPRGNPLSH
260 270 280 290 300
FLEGEVLSAT KMLSKFRKII KEEVKEIKDI DVSVEKEKPG SPAVTLLIRN
310 320 330 340 350
PEEISVDIIL ALESKGSWPI STKEGLPIQG WLGTKVRTNL RREPFYLVPK
360 370 380 390 400
NAKDGNSFQG ETWRLSFSHT EKYILNNHGI EKTCCESSGA KCCRKECLKL
410 420 430 440 450
MKYLLEQLKK EFQELDAFCS YHVKTAIFHM WTQDPQDSQW DPRNLSSCFD
460 470 480 490 500
KLLAFFLECL RTEKLDHYFI PKFNLFSQEL IDRKSKEFLS KKIEYERNNG

FPIFDKL
Length:507
Mass (Da):58,194
Last modified:March 1, 2003 - 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:i9FDA84DF5E4859CA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6ZBV6F6ZBV6_MOUSE
Cyclic GMP-AMP synthase
Cgas E330016A19Rik
230Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D3Z5R0D3Z5R0_MOUSE
Cyclic GMP-AMP synthase
Cgas E330016A19Rik
394Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti6R → I in BAE26335 (PubMed:16141072).Curated1
Sequence conflicti471P → R in BAE26335 (PubMed:16141072).Curated1

Sequence databases

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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
KC294567 mRNA Translation: AGB51854.1
AK054330 mRNA Translation: BAC35733.1
AK145268 mRNA Translation: BAE26335.1
AC158987 Genomic DNA No translation available.
CH466522 Genomic DNA Translation: EDL26396.1
BC052196 mRNA Translation: AAH52196.1
BC145651 mRNA Translation: AAI45652.1
BC145653 mRNA Translation: AAI45654.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS40702.1

NCBI Reference Sequences

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RefSeqi
NP_775562.2, NM_173386.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000070742; ENSMUSP00000063331; ENSMUSG00000032344

Database of genes from NCBI RefSeq genomes

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GeneIDi
214763

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:214763

UCSC genome browser

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UCSCi
uc009quj.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
KC294567 mRNA Translation: AGB51854.1
AK054330 mRNA Translation: BAC35733.1
AK145268 mRNA Translation: BAE26335.1
AC158987 Genomic DNA No translation available.
CH466522 Genomic DNA Translation: EDL26396.1
BC052196 mRNA Translation: AAH52196.1
BC145651 mRNA Translation: AAI45652.1
BC145653 mRNA Translation: AAI45654.1
CCDSiCCDS40702.1
RefSeqiNP_775562.2, NM_173386.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4K8VX-ray2.00A/B/C/D147-507[»]
4K96X-ray2.08A/B147-507[»]
4K97X-ray2.41A147-507[»]
4K98X-ray1.94A147-507[»]
4K99X-ray1.95A147-507[»]
4K9AX-ray2.26A147-507[»]
4K9BX-ray2.26A147-507[»]
4LEYX-ray2.50A/B/C/D142-507[»]
4LEZX-ray2.36A/C142-507[»]
4O6AX-ray1.86A/B147-507[»]
5N6IX-ray3.60A/B/C/D/E/F139-507[»]
5XZBX-ray2.13A149-505[»]
5XZEX-ray2.18A147-507[»]
5XZGX-ray1.83A147-507[»]
SMRiQ8C6L5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000063331

PTM databases

iPTMnetiQ8C6L5
PhosphoSitePlusiQ8C6L5

Proteomic databases

EPDiQ8C6L5
MaxQBiQ8C6L5
PaxDbiQ8C6L5
PRIDEiQ8C6L5

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
31341 198 antibodies

Genome annotation databases

EnsembliENSMUST00000070742; ENSMUSP00000063331; ENSMUSG00000032344
GeneIDi214763
KEGGimmu:214763
UCSCiuc009quj.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
115004
MGIiMGI:2442261 Cgas

Phylogenomic databases

eggNOGiENOG410IE27 Eukaryota
ENOG410XTKD LUCA
GeneTreeiENSGT00980000198551
HOGENOMiCLU_040428_2_0_1
InParanoidiQ8C6L5
KOiK17834
OMAiVKCCRKE
OrthoDBi759341at2759
TreeFamiTF331255

Enzyme and pathway databases

BRENDAi2.7.7.86 3474

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
214763 1 hit in 12 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Cgas mouse

Protein Ontology

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PROi
PR:Q8C6L5
RNActiQ8C6L5 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000032344 Expressed in embryo and 119 other tissues
ExpressionAtlasiQ8C6L5 baseline and differential
GenevisibleiQ8C6L5 MM

Family and domain databases

InterProiView protein in InterPro
IPR024810 Mab-21_dom
PfamiView protein in Pfam
PF03281 Mab-21, 1 hit
SMARTiView protein in SMART
SM01265 Mab-21, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiCGAS_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: Q8C6L5
Secondary accession number(s): Q3ULW3
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 1, 2003
Last modified: June 17, 2020
This is version 124 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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