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Details on Person UniProt:Q8N884 CGAS
| Class:Id | ReferenceGeneProduct:223059 |
|---|---|
| _chainChangeLog | chain:1-522 added on Sat February 7 2015 |
| _displayName | UniProt:Q8N884 CGAS |
| _timestamp | 2026-02-20 22:30:45 |
| chain | chain:1-522 |
| checksum | 808FF6F9F3BF8C50 |
| comment | FUNCTION Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (PubMed:21478870, PubMed:23258413, PubMed:23707061, PubMed:23707065, PubMed:23722159, PubMed:24077100, PubMed:24116191, PubMed:24462292, PubMed:25131990, PubMed:26300263, PubMed:29976794, PubMed:30799039, PubMed:31142647, PubMed:32814054, PubMed:33273464, PubMed:33542149, PubMed:37217469, PubMed:37802025). 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:28214358, PubMed:28363908). Acts as a key DNA sensor: directly binds double-stranded DNA (dsDNA), inducing the formation of liquid-like droplets in which CGAS is activated, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates STING1, thereby triggering type-I interferon production (PubMed:28314590, PubMed:28363908, PubMed:29976794, PubMed:32817552, PubMed:33230297, PubMed:33606975, PubMed:35322803, PubMed:35438208, PubMed:35460603, PubMed:35503863). Preferentially recognizes and binds curved long dsDNAs of a minimal length of 40 bp (PubMed:30007416). Acts as a key foreign DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses (PubMed:28363908). Has antiviral activity by sensing the presence of dsDNA from DNA viruses in the cytoplasm (PubMed:28363908, PubMed:35613581). Also acts as an innate immune sensor of infection by retroviruses, such as HIV-2, by detecting the presence of reverse-transcribed DNA in the cytosol (PubMed:23929945, PubMed:24269171, PubMed:30270045, PubMed:32852081). In contrast, HIV-1 is poorly sensed by CGAS, due to its capsid that cloaks viral DNA from CGAS detection (PubMed:24269171, PubMed:30270045, PubMed:32852081). 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 (PubMed:26046437). Also detects the presence of DNA from bacteria, such as M.tuberculosis (PubMed:26048138). 2',3'-cGAMP can be transferred from producing cells to neighboring cells through gap junctions, leading to promote STING1 activation and convey immune response to connecting cells (PubMed:24077100, PubMed:31992625). 2',3'-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 STING1-dependent manner (PubMed:26229115). Also senses the presence of neutrophil extracellular traps (NETs) that are translocated to the cytosol following phagocytosis, leading to synthesis of 2',3'-cGAMP (PubMed:33688080). In addition to foreign DNA, can also be activated by endogenous nuclear or mitochondrial DNA (PubMed:28738408, PubMed:28759889, PubMed:31299200, PubMed:33031745, PubMed:33230297). When self-DNA leaks into the cytosol during cellular stress (such as mitochondrial stress, SARS-CoV-2 infection causing severe COVID-19 disease, DNA damage, mitotic arrest or senescence), or is present in form of cytosolic micronuclei, CGAS is activated leading to a state of sterile inflammation (PubMed:28738408, PubMed:28759889, PubMed:31299200, PubMed:33031745, PubMed:33230297, PubMed:35045565). 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 STING1 and promote cellular senescence (By similarity). 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, PubMed:28759889). Micronuclei, which are frequently found in cancer cells, consist of chromatin surrounded by their own nuclear membrane: following breakdown of the micronuclear envelope, a process associated with chromothripsis, CGAS binds self-DNA exposed to the cytosol, leading to 2',3'-cGAMP synthesis and subsequent activation of STING1 and type-I interferon production (PubMed:28738408, PubMed:28759889). Activated in response to prolonged mitotic arrest, promoting mitotic cell death (PubMed:31299200). In a healthy cell, CGAS is however kept inactive even in cellular events that directly expose it to self-DNA, such as mitosis, when cGAS associates with chromatin directly after nuclear envelope breakdown or remains in the form of postmitotic persistent nuclear cGAS pools bound to chromatin (PubMed:31299200, PubMed:33542149). Nuclear CGAS is inactivated by chromatin via direct interaction with nucleosomes, which block CGAS from DNA binding and thus prevent CGAS-induced autoimmunity (PubMed:31299200, PubMed:32911482, PubMed:32912999, PubMed:33051594, PubMed:33542149). Also acts as a suppressor of DNA repair in response to DNA damage: inhibits homologous recombination repair by interacting with PARP1, the CGAS-PARP1 interaction leading to impede the formation of the PARP1-TIMELESS complex (PubMed:30356214, PubMed:31544964). In addition to DNA, also sense translation stress: in response to translation stress, translocates to the cytosol and associates with collided ribosomes, promoting its activation and triggering type-I interferon production (PubMed:34111399). In contrast to other mammals, human CGAS displays species-specific mechanisms of DNA recognition and produces less 2',3'-cGAMP, allowing a more fine-tuned response to pathogens (PubMed:30007416).CATALYTIC ACTIVITY GTP + ATP = 2',3'-cGAMP + 2 diphosphateCATALYTIC ACTIVITY GTP + ATP = pppGp(2'-5')A + diphosphateCATALYTIC ACTIVITY pppGp(2'-5')A = 2',3'-cGAMP + diphosphateCOFACTOR Binds 1 Mg(2+) ion per subunit (PubMed:30007416). Is also active with Mn(2+) (PubMed:32814054). Mn(2+)-activated enzyme forms an inverted pppGp(2'-5')A intermediate, suggesting a non-canonical but accelerated 2',3'-cGAMP cyclization without substrate flip-over (By similarity). Mn(2+) ions are coordinated by triphosphate moiety of the inverted substrate, independent of the catalytic triad residues (By similarity).COFACTOR Undergoes a liquid-like phase transition after binding to DNA, which is dependent on zinc.ACTIVITY REGULATION The enzyme activity is strongly increased by double-stranded DNA (dsDNA), but not by single-stranded DNA or RNA (PubMed:23258413, PubMed:23707061, PubMed:26300263). DNA-binding induces the formation of liquid-like droplets in which CGAS is activated (PubMed:29976794, PubMed:33606975). Liquid-like droplets also create a selective environment that restricts entry of negative regulators, such as TREX1 or BANF1/BAF, allowing sensing of DNA (PubMed:33606975). A number of mechanisms exist to restrict its activity toward self-DNA (PubMed:31299200, PubMed:32792394, PubMed:32911482, PubMed:32912999, PubMed:33051594, PubMed:33542149). The nucleotidyltransferase activity is inhibited in the nucleus via its association with nucleosomes: interacts with the acidic patch of histones H2A and H2B, thereby blocking DNA-binding and subsequent activation (PubMed:31299200, PubMed:32911482, PubMed:32912999, PubMed:33051594). CGAS is also inactive when associated with mitotic chromatin (PubMed:33542149). Chromatin-bound CGAS cannot be activated by exogenous DNA in mitotic cells: phosphorylation of the N-terminal disordered part by AURKB during the G2-M transition blocks CGAS liquid phase separation and activation (PubMed:33542149). Activity toward self-DNA is inhibited by BANF1/BAF upon acute loss of nuclear membrane integrity: BANF1/BAF acts by outcompeting CGAS for DNA-binding, thereby preventing CGAS activation (PubMed:32792394). DNA-induced activation at micronuclei is also limited by TREX1, which degrades micronuclear DNA upon nuclear envelope rupture, thereby preventing CGAS activation (PubMed:33476576). CGAS can be released from nucleosomes and activated by MRE11 component of the MRN complex, which displaces CGAS from acidic-patch-mediated sequestration (By similarity). Acetylation at Lys-384, Lys-394 and Lys-414 inhibits the cyclic GMP-AMP synthase activity (PubMed:30799039). Inhibited by aspirin (acetylsalicylate) drug, which acetylates CGAS (PubMed:30799039). Acetylation by KAT5 increases the cyclic GMP-AMP synthase activity by promoting DNA-binding and subsequent activation (PubMed:32817552). Phosphorylation at Ser-305 suppresses the nucleotidyltransferase activity (PubMed:26440888). Phosphorylation at Ser-435 promotes the cyclic GMP-AMP synthase activity (PubMed:32474700). Phosphorylation at Thr-68 and Ser-213 inhibits its cyclic GMP-AMP synthase activity (PubMed:33273464). Ubiquitination at Lys-173 and Lys-384 via 'Lys-27'-linked polyubiquitination enhances the cyclic GMP-AMP synthase activity (PubMed:28273161). Monoubiquitination at Lys-347 promotes oligomerization and subsequent activation (PubMed:29426904). Sumoylation at Lys-347, Lys-384 and Lys-394 prevents DNA-binding, oligomerization and nucleotidyltransferase activity (By similarity). The enzyme activity is impaired by the cleavage at Asp-140 and Asp-157 produced by CASP1 (PubMed:28314590). In addition to DNA, also activated by collided ribosomes upon translation stress: specifically binds collided ribosomes, promoting its activation and triggering type-I interferon production (PubMed:34111399). Strongly inhibited by compound PF-06928215, which is specific for human protein (PubMed:28934246, PubMed:30007416, PubMed:32459092). Inhibited by small-molecule inhibitors with a pyridoindole tricyclic core G108, G140 and G150 (PubMed:31113940).ACTIVITY REGULATION (Microbial infection) Nucleotidyltransferase activity is inhibited by different herpesvirus tegument proteins (Herpes simplex virus 1 tegument protein VP22, herpes virus 8 protein ORF52 and herpesvirus 3 tegument protein VP22/ORF9) (PubMed:34015248, PubMed:34387695). Viral tegument proteins act by disrupting liquid-like droplets in which CGAS is activated, thereby preventing CGAS activity (PubMed:34015248, PubMed:34387695).BIOPHYSICOCHEMICAL PROPERTIES Monomer in the absence of DNA (PubMed:28363908). Homodimer in presence of dsDNA: forms a 2:2 dimer with two enzymes binding to two DNA molecules (PubMed:30007416, PubMed:30799039, PubMed:31142647, PubMed:33273464). Interacts with nucleosomes; interaction is mainly mediated via histones H2A and H2B and inactivates the nucleotidyltransferase activity by blocking DNA-binding and subsequent activation (PubMed:32911480, PubMed:32911481, PubMed:32911482, PubMed:32912999, PubMed:33051594). Interacts with PQBP1 (via WW domain) (PubMed:26046437). Interacts with TRIM14; this interaction recruits USP14, leading to deubiquitinate and stabilize CGAS and promote type I interferon production (PubMed:27666593, PubMed:32404352). Interacts with ZCCHC3; promoting sensing of dsDNA by CGAS (PubMed:30135424). Interacts (when not monomethylated) with (poly-ADP-ribosylated) PARP1; interaction takes place in the nucleus and prevents the formation of the PARP1-TIMELESS complex (PubMed:30356214). Interacts (when monomethylated) with SGF29; interaction with SGF29 prevents interaction with PARP1 (By similarity). Interacts with PCBP2; preventing the formation of liquid-like droplets in which CGAS is activated (PubMed:35322803). Interacts with IRGM; promoting CGAS degradation (PubMed:32715615). Interacts with DDX41 (PubMed:35613581).SUBUNIT (Microbial infection) Interacts with herpes virus 8/HHV-8 protein ORF52; this interaction inhibits cGAS enzymatic activity by preventing the formation of liquid-like droplets by CGAS.SUBUNIT (Microbial infection) Interacts with herpes simplex virus 1 protein UL37; this interaction deaminates CGAS and inhibits its activation.SUBUNIT (Microbial infection) Interacts with vaccinia virus protein OPG067; this interaction promotes CGAS proteasomal degradation.SUBUNIT (Microbial infection) Interacts with cytomegalovirus protein UL31; this interaction promotes dissociation of DNA from CGAS, thereby inhibiting the enzymatic activity of CGAS.SUBUNIT (Microbial infection) Interacts with herpes simplex virus 1 tegument protein VP22 (UL49); this interaction inhibits cGAS enzymatic activity by preventing the formation of liquid-like droplets by CGAS.SUBUNIT (Microbial infection) Interacts with herpesvirus 3 tegument protein VP22 (ORF9); this interaction inhibits cGAS enzymatic activity by preventing the formation of liquid-like droplets by CGAS.SUBUNIT (Microbial infection) Interacts with human cytomegalovirus proteins UL42 and UL83; these interactions result in the inhibition of cGAS-STING signaling.INTERACTION Mainly localizes in the nucleus, and at low level in the cytosol (PubMed:31544964, PubMed:31808743). On chromosomes, enriched on centromeric satellite and LINE DNA repeat elements (PubMed:30811988). Exported from the nucleus to the cytosol in a XPO1/CRM1 via the nuclear export signal in response to DNA stimulation (PubMed:33406424). Outside the nucleus, localizes at the cell membrane as a peripheral membrane protein in resting conditions: association to the cell membrane is mediated via binding to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (PubMed:30827685). Localization at the cell membrane is required to limit the recognition of self-DNA (PubMed:30827685). Following detection of double-stranded DNA (dsDNA), released from the cell membrane into the cytosol in order to signal (PubMed:30827685). Upon transfection with dsDNA forms punctate structures that co-localize with DNA and Beclin-1 (BECN1) (PubMed:26048138). Phosphorylation at Tyr-215 promotes cytosolic retention (PubMed:30356214). In response to translation stress, translocates to the cytosol and associates with collided ribosomes (PubMed:34111399).SUBCELLULAR LOCATION (Microbial infection) Upon infection with virulent M.tuberculosis forms aggregates with dsDNA, non-virulent bacteria (without the ESX-1 locus) do not form these aggregates (PubMed:26048138).ALTERNATIVE PRODUCTS Expressed in the monocytic cell line THP1.INDUCTION By type I interferons.DOMAIN Lys-187 and Leu-195 residues are specific to human and destabilize the interactions with short DNA, shifting the specificity toward the detection of curved long DNAs (PubMed:30007416). Lys-187 and Leu-195 also restrain cGAMP production and, therefore, immune activation, allowing a more fine-tuned response to pathogens (PubMed:30007416).DOMAIN The N-terminal disordered part (1-160) binds unspecifically dsDNA and expands the binding and moving range of CGAS on dsDNA (PubMed:28214358, PubMed:28363908). The disordered and positively charged residues enhance CGAS-DNA phase separation by increasing the valencies of DNA-binding (PubMed:29976794). The N-terminus is required to sense chromatin and its phosphorylation blocks its activation by chromatin DNA (PubMed:33542149). When the N-terminal part (1-160) is missing the protein bound to dsDNA homodimerizes (By similarity).DOMAIN The arginine-anchor tightly binds to the canonical H2A acidic-patch residues.PTM The N-terminal disordered part (1-160) is phosphorylated by AURKB during the G2-M transition, blocking CGAS liquid phase separation and preventing activation (PubMed:33542149). Phosphorylation at Tyr-215 by BLK promotes cytosolic retention (PubMed:30356214). Localizes into the nucleus following dephosphorylation at Tyr-215 (PubMed:30356214). Phosphorylation at Ser-435 activates the nucleotidyltransferase activity (PubMed:32474700). Dephosphorylation at Ser-435 by PPP6C impairs its ability to bind GTP, thereby inactivating it (PubMed:32474700). Phosphorylation at Thr-68 and Ser-213 by PRKDC inhibits its cyclic GMP-AMP synthase activity by impairing homodimerization and activation (PubMed:33273464). Phosphorylation at Ser-305 by AKT (AKT1, AKT2 or AKT3) suppresses the nucleotidyltransferase activity (PubMed:26440888). Phosphorylation at Ser-305 by CDK1 during mitosis leads to its inhibition, thereby preventing CGAS activation by self-DNA during mitosis (PubMed:32351706). Dephosphorylated at Ser-305 by protein phosphatase PP1 upon mitotic exit (PubMed:32351706).PTM Ubiquitinated at Lys-414 via 'Lys-48'-linked polyubiquitin chains, leading to its SQSTM1-mediated autophagic degradation (PubMed:27666593). Interaction with TRIM14 promotes recruitment of USP14, leading to deubiquitinate Lys-414 and stabilize CGAS (PubMed:27666593). Ubiquitinated at Lys-173 and Lys-384 by RNF185 via 'Lys-27'-linked polyubiquitination, promoting CGAS cyclic GMP-AMP synthase activity (PubMed:28273161). Monoubiquitination at Lys-347 by TRIM56 promotes oligomerization and subsequent activation (PubMed:29426904). Monoubiquitination by TRIM41 promotes CGAS activation (PubMed:29760876). Ubiquitination at Lys-285 and Lys-479 via 'Lys-48'-linked polyubiquitination promotes its degradation (By similarity). Deubiquitination at Lys-285 by USP29 promotes its stabilization (By similarity). Deubiquitinated by USP27X, promoting its stabilization (PubMed:31534008). Ubiquitinated at Lys-411 via 'Lys-63'-linked polyubiquitin chains by MARCHF8, leading to the inhibition of its DNA binding ability (PubMed:35503863). In cycling cells, nucleosome-bound CGAS is ubiquitinated at Lys-427 and Lys-428 via 'Lys-48'-linked polyubiquitin chains by the ECS(SPSB3) complex, leading to its degradation: ubiquitination and degradation of nuclear CGAS during G1 and G2 phases is required to promote low intranuclear CGAS abundance before the next mitotic cycle (PubMed:38418882).PTM Sumoylated at Lys-231 and Lys-479 by TRIM38 in uninfected cells and during the early phase of viral infection, promoting its stability by preventing ubiquitination at Lys-285 and Lys-479, and subsequent degradation (By similarity). Desumoylated by SENP2 during the late phase of viral infection (By similarity). Sumoylation at Lys-347, Lys-384 and Lys-394 prevents DNA-binding, oligomerization and nucleotidyltransferase activity (By similarity). Desumoylation at Lys-347, Lys-384 and Lys-394 by SENP7 relieves inhibition and activates CGAS (By similarity).PTM Polyglutamylated by TTLL6 at Glu-286, leading to impair DNA-binding activity. Monoglutamylated at Glu-314 by TTLL4, leading to impair the nucleotidyltransferase activity. Deglutamylated by AGBL5/CCP5 and AGBL6/CCP6.PTM Acetylation at Lys-384, Lys-394 and Lys-414 inhibits the cyclic GMP-AMP synthase activity (PubMed:30799039). Deacetylated upon cytosolic DNA challenge such as viral infections (PubMed:30799039). Acetylation can be mediated by aspirin (acetylsalicylate) drug, which directly acetylates CGAS (PubMed:30799039). Acetylation by aspirin efficiently inhibits CGAS-mediated immune responses and is able to suppress self-DNA-induced autoimmunity (PubMed:30799039). Acetylation at Lys-47, Lys-56, Lys-62 and Lys-83 by KAT5 increases the cyclic GMP-AMP synthase activity by promoting DNA-binding and subsequent activation (PubMed:32817552).PTM Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation (PubMed:30878284). The damage of the nucleus and the mitochondria during apoptosis leads to leakage of nuclear and mitochondrial DNA, which activate CGAS: cleavage and inactivation during apoptosis in required to prevent cytokine overproduction (By similarity). Cleaved by CASP3 at Asp-319 during virus-induced apoptosis, thereby inactivating it and preventing cytokine overproduction (PubMed:30878284). Cleaved by CASP1 at Asp-140 and Asp-157 upon DNA virus infection; the cleavage impairs cGAMP production (PubMed:28314590). Also cleaved by the pyroptotic CASP4 and CASP5 during non-canonical inflammasome activation; they don't cut at the same sites as CASP1 (PubMed:28314590).PTM Degraded via selective autophagy following interaction with IRGM (PubMed:32715615). IRGM promotes CGAS recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagic degradation (PubMed:32715615).PTM Poly-ADP-ribosylation at Asp-191 by PARP1 impairs DNA-binding, thereby preventing the cyclic GMP-AMP synthase activity.PTM Palmitoylation at Cys-474 by ZDHHC18 impairs DNA-binding, thereby preventing the cyclic GMP-AMP synthase activity (PubMed:35438208). Palmitoylation at Cys-404 and Cys-405 by ZDHHC9 promotes homodimerization and cyclic GMP-AMP synthase activity (PubMed:37802025). Depalmitoylation at Cys-404 and Cys-405 by LYPLAL1 impairs homodimerization and cyclic GMP-AMP synthase activity (PubMed:37802025).PTM Monomethylated at Lys-506 by SETD7 (PubMed:35210392). Monomethylation promotes interaction with SGF29, preventing interaction between PARP1 nad SGF29 (By similarity). Demethylation by RIOX1 promotes interaction with PARP1, followed by PARP1 inactivation (By similarity).PTM Lactylation by AARS2 prevents ability to undergo liquid-liquid phase separation (LLPS), thereby inhibiting CGAS activation.PTM (Microbial infection) Deamidated on 'Asn-210' by herpes simplex virus 1 protein UL37. This modification significantly reduces CGAS-dependent cGAMP production and innate immune signaling induced by dsDNA.PTM (Microbial infection) Degraded by an autophagy-mediated mechanism in presence of Chikungunya virus capsid protein.MISCELLANEOUS The cGAS-STING signaling pathway drives sterile inflammation leading to type I interferon immunopathology in severe COVID-19 disease caused by SARS-CoV-2 virus infection (PubMed:35045565). Tissue damages in the lung and skin lesions are caused by activation of the cGAS-STING signaling leading to aberrant inflammation (PubMed:35045565). Endothelial cell damage is also caused by activation of the cGAS-STING pathway: SARS-CoV-2 infection triggers mitochondrial DNA release into the cytosol (PubMed:35045565). Released mitochondrial DNA is then detected by CGAS, leading to activation of the cGAS-STING pathway, triggering type-I interferon production and autoinflammation (PubMed:35045565).SIMILARITY Belongs to the mab-21 family.SEQUENCE CAUTION Extended N-terminus. |
| created | [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 |
| description | recommendedName: fullName evidence="94"Cyclic GMP-AMP synthase shortName evidence="94"cGAMP synthase shortName evidence="94"cGAS shortName evidence="94"h-cGAS ecNumber evidence="6 7 9 16 31 38 44"2.7.7.86 alternativeName: fullName evidence="94"2'3'-cGAMP synthase alternativeName: Mab-21 domain-containing protein 1 |
| geneName | CGAS C6orf150 MB21D1 |
| identifier | Q8N884 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation ADP-ribosylation Alternative splicing Antiviral defense ATP-binding Cell membrane Chromosome Cytoplasm DNA damage DNA repair DNA-binding GTP-binding Host-virus interaction Immunity Innate immunity Isopeptide bond Lipid-binding Lipoprotein Magnesium Membrane Metal-binding Methylation Nucleotide-binding Nucleotidyltransferase Nucleus Palmitate Phosphoprotein Proteomics identification Reference proteome Transferase Ubl conjugation Zinc |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9909836] Weiser, Joel, 2024-05-14 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | CGAS |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9004029] ENSEMBL:ENSG00000164430 CGAS [Homo sapiens] |
| secondaryIdentifier | CGAS_HUMAN L0L2J9 Q14CV6 Q32NC9 Q5SWL0 Q5SWL1 Q96E45 |
| sequenceLength | 522 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:223060] UniProt:Q8N884-2 CGAS [Homo sapiens] [ReferenceIsoform:411370] UniProt:Q8N884-1 CGAS [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:3244653] CGAS [cytosol] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:Q8N884 CGAS (223059)
