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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8N884: Variant p.Thr35Asn

Cyclic GMP-AMP synthase
Gene: CGAS
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Variant information Variant position: help 35 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Threonine (T) to Asparagine (N) at position 35 (T35N, p.Thr35Asn). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Similar physico-chemical property. Both residues are medium size and polar. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 35 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 522 The length of the canonical sequence.
Location on the sequence: help AGATAPKASARNARGAPMDP T ESPAAPEAALPKAGKFGPAR The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         AGATAPKASARNARGAPMDPTESPAA-PEAALPKAGKFGPAR

Mouse                         ----APRAKKPSAKRA-------PTQ-PSRTRAHAESCGPQ

Pig                           VGAAGPRASARSVNGA-------PTV-PEAARPGARRNGPS

Bovine                        T---ASGVSAPCVEGGLSAEPSEPAAVPEAPRPGARRCGAA

Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 1 – 522 Cyclic GMP-AMP synthase
Region 1 – 160 DNA-binding
Region 1 – 144 Disordered
Modified residue 21 – 21 N6-acetyllysine
Modified residue 37 – 37 Phosphoserine
Modified residue 47 – 47 N6-acetyllysine
Modified residue 50 – 50 N6-acetyllysine
Mutagenesis 18 – 18 T -> E. In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associated with D-13; D-23; E-35; D-37; D-57; D-59; D-64; E-68; E-77; E-91; D-94; E-97; D-98; D-116; D-120; D-129; E-130; D-143 and D-149.
Mutagenesis 23 – 23 S -> D. In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associated with D-13; E-18; E-35; D-37; D-57; D-59; D-64; E-68; E-77; E-91; D-94; E-97; D-98; D-116; D-120; D-129; E-130; D-143 and D-149.
Mutagenesis 33 – 33 D -> A. No effect on type I IFN and RSAD2 induction. No effect on cleavage by CASP1. No effect on cleavage by CASP1; when associated with A-67; A-90 and A-95. Highly decreases cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-67; A-90; A-95 and A-140. Abolishes cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-67; A-90; A-95; A-140 and A-157.
Mutagenesis 35 – 35 T -> E. In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associated with D-13; E-18; D-23; D-37; D-57; D-59; D-64; E-68; E-77; E-91; D-94; E-97; D-98; D-116; D-120; D-129; E-130; D-143 and D-149.
Mutagenesis 37 – 37 S -> D. In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associated with D-13; E-18; D-23; E-35; D-57; D-59; D-64; E-68; E-77; E-91; D-94; E-97; D-98; D-116; D-120; D-129; E-130; D-143 and D-149.
Mutagenesis 47 – 47 K -> R. Decreased acetylation by KAT5, leading to decreased stimulation of interferon production.
Mutagenesis 50 – 50 K -> Q. Acetylation-mimetic mutant; no effect.
Mutagenesis 50 – 50 K -> R. No effect.



Literature citations
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Ota T.; Suzuki Y.; Nishikawa T.; Otsuki T.; Sugiyama T.; Irie R.; Wakamatsu A.; Hayashi K.; Sato H.; Nagai K.; Kimura K.; Makita H.; Sekine M.; Obayashi M.; Nishi T.; Shibahara T.; Tanaka T.; Ishii S.; Yamamoto J.; Saito K.; Kawai Y.; Isono Y.; Nakamura Y.; Nagahari K.; Murakami K.; Yasuda T.; Iwayanagi T.; Wagatsuma M.; Shiratori A.; Sudo H.; Hosoiri T.; Kaku Y.; Kodaira H.; Kondo H.; Sugawara M.; Takahashi M.; Kanda K.; Yokoi T.; Furuya T.; Kikkawa E.; Omura Y.; Abe K.; Kamihara K.; Katsuta N.; Sato K.; Tanikawa M.; Yamazaki M.; Ninomiya K.; Ishibashi T.; Yamashita H.; Murakawa K.; Fujimori K.; Tanai H.; Kimata M.; Watanabe M.; Hiraoka S.; Chiba Y.; Ishida S.; Ono Y.; Takiguchi S.; Watanabe S.; Yosida M.; Hotuta T.; Kusano J.; Kanehori K.; Takahashi-Fujii A.; Hara H.; Tanase T.-O.; Nomura Y.; Togiya S.; Komai F.; Hara R.; Takeuchi K.; Arita M.; Imose N.; Musashino K.; Yuuki H.; Oshima A.; Sasaki N.; Aotsuka S.; Yoshikawa Y.; Matsunawa H.; Ichihara T.; Shiohata N.; Sano S.; Moriya S.; Momiyama H.; Satoh N.; Takami S.; Terashima Y.; Suzuki O.; Nakagawa S.; Senoh A.; Mizoguchi H.; Goto Y.; Shimizu F.; Wakebe H.; Hishigaki H.; Watanabe T.; Sugiyama A.; Takemoto M.; Kawakami B.; Yamazaki M.; Watanabe K.; Kumagai A.; Itakura S.; Fukuzumi Y.; Fujimori Y.; Komiyama M.; Tashiro H.; Tanigami A.; Fujiwara T.; Ono T.; Yamada K.; Fujii Y.; Ozaki K.; Hirao M.; Ohmori Y.; Kawabata A.; Hikiji T.; Kobatake N.; Inagaki H.; Ikema Y.; Okamoto S.; Okitani R.; Kawakami T.; Noguchi S.; Itoh T.; Shigeta K.; Senba T.; Matsumura K.; Nakajima Y.; Mizuno T.; Morinaga M.; Sasaki M.; Togashi T.; Oyama M.; Hata H.; Watanabe M.; Komatsu T.; Mizushima-Sugano J.; Satoh T.; Shirai Y.; Takahashi Y.; Nakagawa K.; Okumura K.; Nagase T.; Nomura N.; Kikuchi H.; Masuho Y.; Yamashita R.; Nakai K.; Yada T.; Nakamura Y.; Ohara O.; Isogai T.; Sugano S.;
Nat. Genet. 36:40-45(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANT ASN-35; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2); VARIANTS ASN-35 AND HIS-261;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.