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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q86WV6: Variant p.His232Arg

Stimulator of interferon genes protein
Gene: STING1
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Variant information Variant position: help 232 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 Histidine (H) to Arginine (R) at position 232 (H232R, p.His232Arg). 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 Change from medium size and polar (H) to large size and basic (R) 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

Variant description: help Activated by both 2'-3' linked cGAMP and 3'-3' linked cGAMP. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 232 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 379 The length of the canonical sequence.
Location on the sequence: help LSMADPNIRFLDKLPQQTGD H AGIKDRVYSNSIYELLENGQ 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                         LSMADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLEN-GQ

Mouse                         LSVVDPNIRFRDMLPQQNIDRAGIKNRVYSNSVYEILEN-G

Rat                           LSVADPNIRFRDMLPQQNTDRAGVKNRAYSNSVYELLEN-G

Pig                           LSVADPNIRFLHELPQQSADRAGIKGRVYTNSIYELLEN-G

Bovine                        LNVADPNIRFLHELPQQSADRAGIKGRVYTNSIYELLEN-G

Chicken                       LEKADSNIQYLADLPETILTRAGIKRRVYKHSLYVIRDK-D

Xenopus tropicalis            LKDVDENITFLKEIPPLYIDRAGIKGRVFKNNVYRILDE-D

Zebrafish                     PEEEDTNVVFHENLPDLKLDRAGVRKRSYTNSVYKITHN-N

Drosophila                    LE--SHLLDKAEPLETQFINRAGVY-RPFKHDVYRMNKKVN

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 – 379 Stimulator of interferon genes protein
Topological domain 135 – 379 Cytoplasmic
Region 153 – 340 Cyclic dinucleotide-binding domain (CBD)
Binding site 238 – 238
Binding site 238 – 238
Modified residue 229 – 229 Phosphothreonine
Modified residue 241 – 241 Phosphoserine
Cross 236 – 236 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Mutagenesis 230 – 230 G -> I. Renders the enzyme sensitive to 5,6-dimethylxanthenone 4-acetic acid (DMXAA) drug, leading to activation of the STING1 pathway.
Mutagenesis 236 – 236 K -> R. Loss of deubiquitination by USP44.
Mutagenesis 238 – 238 R -> A. Abolished cGAMP-binding. Abolished ability to induce autophagy.
Mutagenesis 240 – 240 Y -> A. Abolished cGAMP-binding.
Mutagenesis 240 – 240 Y -> S. Strong decrease in c-di-GMP-binding.
Mutagenesis 242 – 242 N -> A. Strong decrease in c-di-GMP and cGAMP-binding.
Beta strand 228 – 232



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]; VARIANT ARG-232; Ancient origin of cGAS-STING reveals mechanism of universal 2',3' cGAMP signaling.
Kranzusch P.J.; Wilson S.C.; Lee A.S.; Berger J.M.; Doudna J.A.; Vance R.E.;
Mol. Cell 59:891-903(2015)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANT ARG-232;
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.