ID GBP2_HUMAN Reviewed; 591 AA. AC P32456; Q6GPH0; Q6IAU2; Q86TB0; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 3. DT 09-APR-2025, entry version 198. DE RecName: Full=Guanylate-binding protein 2; DE EC=3.6.5.- {ECO:0000269|PubMed:8706832}; DE AltName: Full=GTP-binding protein 2 {ECO:0000303|PubMed:8706832}; DE Short=GBP-2 {ECO:0000303|PubMed:8706832}; DE Short=HuGBP-2; DE AltName: Full=Guanine nucleotide-binding protein 2 {ECO:0000303|PubMed:8706832}; DE AltName: Full=Interferon-induced guanylate-binding protein 2; DE Flags: Precursor; GN Name=GBP2 {ECO:0000303|PubMed:8706832, ECO:0000312|HGNC:HGNC:4183}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-285. RC TISSUE=Keratinocyte; RX PubMed=1715024; DOI=10.1128/mcb.11.9.4717-4725.1991; RA Cheng Y.-S.E., Patterson C.E., Staeheli P.; RT "Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus RT motif and bind GMP in addition to GDP and GTP."; RL Mol. Cell. Biol. 11:4717-4725(1991). RN [2] RP SEQUENCE REVISION. RC TISSUE=Foreskin; RA Schwemmle M.; RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-285 AND GLY-303. RC TISSUE=Spinal cord; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-285 AND GLY-303. RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-285 AND GLY-303. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-285 AND RP GLY-303. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=8706832; DOI=10.1016/0014-5793(96)00628-x; RA Neun R., Richter M.F., Staeheli P., Schwemmle M.; RT "GTPase properties of the interferon-induced human guanylate-binding RT protein 2."; RL FEBS Lett. 390:69-72(1996). RN [10] RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=17266443; DOI=10.1089/jir.2007.0086; RA Tripal P., Bauer M., Naschberger E., Mortinger T., Hohenadl C., Cornali E., RA Thurau M., Sturzl M.; RT "Unique features of different members of the human guanylate-binding RT protein family."; RL J. Interferon Cytokine Res. 27:44-52(2007). RN [11] RP SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-588, METHYLATION AT CYS-588, RP DIMERIZATION, AND MUTAGENESIS OF 588-CYS--LEU-591. RX PubMed=21151871; DOI=10.1371/journal.pone.0014246; RA Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A., RA Reipschlager S., Naschberger E., Herrmann C., Sturzl M.; RT "Intracellular trafficking of guanylate-binding proteins is regulated by RT heterodimerization in a hierarchical manner."; RL PLoS ONE 5:E14246-E14246(2010). RN [12] RP UBIQUITINATION (MICROBIAL INFECTION). RX PubMed=29024643; DOI=10.1016/j.chom.2017.09.007; RA Wandel M.P., Pathe C., Werner E.I., Ellison C.J., Boyle K.B., RA von der Malsburg A., Rohde J., Randow F.; RT "GBPs inhibit motility of Shigella flexneri but are targeted for RT degradation by the bacterial ubiquitin ligase IpaH9.8."; RL Cell Host Microbe 22:507-518(2017). RN [13] RP UBIQUITINATION (MICROBIAL INFECTION). RX PubMed=29144452; DOI=10.1038/nature24467; RA Li P., Jiang W., Yu Q., Liu W., Zhou P., Li J., Xu J., Xu B., Wang F., RA Shao F.; RT "Ubiquitination and degradation of GBPs by a Shigella effector to suppress RT host defence."; RL Nature 551:378-383(2017). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-588, AND MUTAGENESIS RP OF CYS-588. RX PubMed=31091448; DOI=10.1016/j.celrep.2019.04.063; RA Braun E., Hotter D., Koepke L., Zech F., Gross R., Sparrer K.M.J., RA Mueller J.A., Pfaller C.K., Heusinger E., Wombacher R., Sutter K., RA Dittmer U., Winkler M., Simmons G., Jakobsen M.R., Conzelmann K.K., RA Poehlmann S., Muench J., Fackler O.T., Kirchhoff F., Sauter D.; RT "Guanylate-binding proteins 2 and 5 exert broad antiviral activity by RT inhibiting furin-mediated processing of viral envelope proteins."; RL Cell Rep. 27:2092-2104(2019). RN [15] {ECO:0007744|PDB:7E58} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS). RX PubMed=33876762; DOI=10.1073/pnas.2022269118; RA Cui W., Braun E., Wang W., Tang J., Zheng Y., Slater B., Li N., Chen C., RA Liu Q., Wang B., Li X., Duan Y., Xiao Y., Ti R., Hotter D., Ji X., RA Zhang L., Cui J., Xiong Y., Sauter D., Wang Z., Kirchhoff F., Yang H.; RT "Structural basis for GTP-induced dimerization and antiviral function of RT guanylate-binding proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). CC -!- FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles CC in innate immunity against a diverse range of bacterial, viral and CC protozoan pathogens (PubMed:31091448). Hydrolyzes GTP to GMP in 2 CC consecutive cleavage reactions, but the major reaction product is GDP CC (PubMed:8706832). Following infection, recruited to the pathogen- CC containing vacuoles or vacuole-escaped bacteria and acts as a positive CC regulator of inflammasome assembly by promoting the release of CC inflammasome ligands from bacteria (By similarity). Acts by promoting CC lysis of pathogen-containing vacuoles, releasing pathogens into the CC cytosol (By similarity). Following pathogen release in the cytosol, CC promotes recruitment of proteins that mediate bacterial cytolysis: this CC liberates ligands that are detected by inflammasomes, such as CC lipopolysaccharide (LPS) that activates the non-canonical CASP4/CASP11 CC inflammasome or double-stranded DNA (dsDNA) that activates the AIM2 CC inflammasome (By similarity). Confers protection to the protozoan CC pathogen Toxoplasma gondii (By similarity). Independently of its GTPase CC activity, acts as an inhibitor of various viruses infectivity, such as CC HIV-1, Zika and influenza A viruses, by inhibiting FURIN-mediated CC maturation of viral envelope proteins (PubMed:31091448). CC {ECO:0000250|UniProtKB:Q9Z0E6, ECO:0000269|PubMed:31091448, CC ECO:0000269|PubMed:8706832}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000269|PubMed:8706832}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=313 uM for GTP {ECO:0000269|PubMed:8706832}; CC -!- SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is CC required for the association with membranous structures CC (PubMed:21151871). Heterodimer with other family members, including CC GBP1, GBP3, GBP4 and GBP5 (PubMed:21151871). CC {ECO:0000269|PubMed:21151871}. CC -!- INTERACTION: CC P32456; P32455: GBP1; NbExp=11; IntAct=EBI-714388, EBI-2869161; CC P32456; P32456: GBP2; NbExp=5; IntAct=EBI-714388, EBI-714388; CC P32456; Q9H0R5: GBP3; NbExp=5; IntAct=EBI-714388, EBI-2798916; CC P32456; Q96PP9: GBP4; NbExp=2; IntAct=EBI-714388, EBI-20840650; CC P32456; Q96PP8: GBP5; NbExp=7; IntAct=EBI-714388, EBI-749932; CC P32456; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-714388, EBI-6863741; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane CC {ECO:0000250|UniProtKB:Q9Z0E6}; Lipid-anchor CC {ECO:0000269|PubMed:21151871}. Golgi apparatus membrane CC {ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:31091448}; Lipid- CC anchor {ECO:0000269|PubMed:21151871}. Cytoplasm CC {ECO:0000269|PubMed:21151871}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:21151871}. Note=GBP2-GBP5 dimers localize to the CC Golgi apparatus. {ECO:0000269|PubMed:21151871}. CC -!- INDUCTION: By IFNG/IFN-gamma during macrophage activation, and by TNF CC and IL1B. {ECO:0000269|PubMed:17266443}. CC -!- PTM: (Microbial infection) Ubiquitinated by S.flexneri IpaH9.8, leading CC to its degradation by the proteasome, thereby preventing its ability to CC promote host defense against bacterial infection. CC {ECO:0000269|PubMed:29024643, ECO:0000269|PubMed:29144452}. CC -!- PTM: Isoprenylation is required for proper subcellular location. CC {ECO:0000269|PubMed:21151871}. CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU01052}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M55543; AAA67323.1; -; mRNA. DR EMBL; AL832451; CAD89925.1; -; mRNA. DR EMBL; AK314325; BAG36973.1; -; mRNA. DR EMBL; CR457062; CAG33343.1; -; mRNA. DR EMBL; AC104459; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW73146.1; -; Genomic_DNA. DR EMBL; BC073163; AAH73163.1; -; mRNA. DR CCDS; CCDS719.1; -. DR PIR; S70524; S70524. DR RefSeq; NP_004111.2; NM_004120.4. DR PDB; 6VKJ; X-ray; 2.10 A; A=5-309. DR PDB; 7E58; X-ray; 2.60 A; A/B=1-591. DR PDB; 7M1S; X-ray; 2.91 A; A=1-591. DR PDBsum; 6VKJ; -. DR PDBsum; 7E58; -. DR PDBsum; 7M1S; -. DR AlphaFoldDB; P32456; -. DR SMR; P32456; -. DR BioGRID; 108904; 55. DR IntAct; P32456; 39. DR MINT; P32456; -. DR STRING; 9606.ENSP00000359497; -. DR iPTMnet; P32456; -. DR PhosphoSitePlus; P32456; -. DR BioMuta; GBP2; -. DR DMDM; 226694187; -. DR jPOST; P32456; -. DR MassIVE; P32456; -. DR PaxDb; 9606-ENSP00000359497; -. DR PeptideAtlas; P32456; -. DR ProteomicsDB; 54878; -. DR Pumba; P32456; -. DR Antibodypedia; 33611; 455 antibodies from 29 providers. DR DNASU; 2634; -. DR Ensembl; ENST00000370466.4; ENSP00000359497.3; ENSG00000162645.13. DR Ensembl; ENST00000464839.5; ENSP00000434282.1; ENSG00000162645.13. DR GeneID; 2634; -. DR KEGG; hsa:2634; -. DR MANE-Select; ENST00000370466.4; ENSP00000359497.3; NM_004120.5; NP_004111.2. DR UCSC; uc001dmz.3; human. DR AGR; HGNC:4183; -. DR CTD; 2634; -. DR DisGeNET; 2634; -. DR GeneCards; GBP2; -. DR HGNC; HGNC:4183; GBP2. DR HPA; ENSG00000162645; Low tissue specificity. DR MIM; 600412; gene. DR neXtProt; NX_P32456; -. DR OpenTargets; ENSG00000162645; -. DR PharmGKB; PA28597; -. DR VEuPathDB; HostDB:ENSG00000162645; -. DR eggNOG; KOG2037; Eukaryota. DR GeneTree; ENSGT00940000162297; -. DR HOGENOM; CLU_018608_2_2_1; -. DR InParanoid; P32456; -. DR OMA; QPTCHIL; -. DR OrthoDB; 2135133at2759; -. DR PhylomeDB; P32456; -. DR TreeFam; TF331602; -. DR PathwayCommons; P32456; -. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR SignaLink; P32456; -. DR BioGRID-ORCS; 2634; 22 hits in 1157 CRISPR screens. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; GBP2; human. DR GeneWiki; GBP2; -. DR GenomeRNAi; 2634; -. DR Pharos; P32456; Tbio. DR PRO; PR:P32456; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P32456; protein. DR Bgee; ENSG00000162645; Expressed in tendon of biceps brachii and 197 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProt. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:UniProt. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0140678; F:molecular function inhibitor activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB. DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:UniProtKB. DR GO; GO:0051715; P:cytolysis in another organism; ISS:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central. DR GO; GO:0042832; P:defense response to protozoan; IBA:GO_Central. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0140973; P:positive regulation of AIM2 inflammasome complex assembly; ISS:UniProtKB. DR GO; GO:0140639; P:positive regulation of pyroptotic inflammatory response; ISS:UniProtKB. DR GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB. DR CDD; cd01851; GBP; 1. DR CDD; cd16269; GBP_C; 1. DR FunFam; 1.20.1000.10:FF:000001; Guanylate binding protein 1; 1. DR FunFam; 3.40.50.300:FF:000422; Guanylate-binding protein 1; 1. DR Gene3D; 1.20.1000.10; Guanylate-binding protein, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR030386; G_GB1_RHD3_dom. DR InterPro; IPR037684; GBP_C. DR InterPro; IPR003191; Guanylate-bd/ATL_C. DR InterPro; IPR036543; Guanylate-bd_C_sf. DR InterPro; IPR015894; Guanylate-bd_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10751; GUANYLATE BINDING PROTEIN; 1. DR Pfam; PF02263; GBP; 1. DR Pfam; PF02841; GBP_C; 1. DR SUPFAM; SSF48340; Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51715; G_GB1_RHD3; 1. PE 1: Evidence at protein level; KW 3D-structure; Antimicrobial; Cytoplasm; Cytoplasmic vesicle; KW Golgi apparatus; GTP-binding; Hydrolase; Immunity; Innate immunity; KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation; KW Proteomics identification; Reference proteome; Ubl conjugation. FT CHAIN 1..588 FT /note="Guanylate-binding protein 2" FT /id="PRO_0000190964" FT PROPEP 589..591 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000370782" FT DOMAIN 35..276 FT /note="GB1/RHD3-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052" FT REGION 1..309 FT /note="GTPase domain (Globular)" FT /evidence="ECO:0000250|UniProtKB:P32455" FT BINDING 45..52 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q96PP8" FT BINDING 181..182 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q96PP8" FT BINDING 245 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q96PP8" FT MOD_RES 588 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000305|PubMed:21151871" FT LIPID 588 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:21151871, FT ECO:0000305|PubMed:31091448" FT VARIANT 281 FT /note="S -> P (in dbSNP:rs2230336)" FT /id="VAR_054815" FT VARIANT 285 FT /note="P -> A (in dbSNP:rs1803632)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:1715024, ECO:0000269|PubMed:17974005, FT ECO:0000269|Ref.5, ECO:0000269|Ref.7" FT /id="VAR_054816" FT VARIANT 303 FT /note="S -> G (in dbSNP:rs2230338)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.5, FT ECO:0000269|Ref.7" FT /id="VAR_054817" FT MUTAGEN 588..591 FT /note="Missing: No effect on subcellular location by FT confocal microscopy, but loss of membrane-association by FT subcellular fractionation." FT /evidence="ECO:0000269|PubMed:21151871" FT MUTAGEN 588 FT /note="C->A: Loss of isoprenylation and of localization at FT the Golgi apparatus." FT /evidence="ECO:0000269|PubMed:31091448" FT CONFLICT 310 FT /note="M -> R (in Ref. 8; AAH73163)" FT /evidence="ECO:0000305" FT STRAND 11..15 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 25..32 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 36..44 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 51..59 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:7M1S" FT STRAND 77..84 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 92..99 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:6VKJ" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 114..122 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 124..133 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 136..154 FT /evidence="ECO:0007829|PDB:6VKJ" FT TURN 157..161 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 167..172 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 175..182 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 196..204 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:6VKJ" FT TURN 215..217 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 218..227 FT /evidence="ECO:0007829|PDB:6VKJ" FT STRAND 230..235 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 242..250 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 253..255 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 258..274 FT /evidence="ECO:0007829|PDB:6VKJ" FT TURN 281..283 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 288..303 FT /evidence="ECO:0007829|PDB:6VKJ" FT HELIX 310..340 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 348..368 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 377..412 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 414..421 FT /evidence="ECO:0007829|PDB:7E58" FT TURN 423..425 FT /evidence="ECO:0007829|PDB:7M1S" FT HELIX 430..447 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 455..465 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 467..476 FT /evidence="ECO:0007829|PDB:7E58" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:7M1S" FT HELIX 482..560 FT /evidence="ECO:0007829|PDB:7E58" FT HELIX 564..581 FT /evidence="ECO:0007829|PDB:7E58" SQ SEQUENCE 591 AA; 67209 MW; B09B3C2F3C3E1EA2 CRC64; MAPEINLPGP MSLIDNTKGQ LVVNPEALKI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG KKNGFSLGST VKSHTKGIWM WCVPHPKKPE HTLVLLDTEG LGDIEKGDNE NDSWIFALAI LLSSTFVYNS MGTINQQAMD QLHYVTELTD RIKANSSPGN NSVDDSADFV SFFPAFVWTL RDFTLELEVD GEPITADDYL ELSLKLRKGT DKKSKSFNDP RLCIRKFFPK RKCFVFDWPA PKKYLAHLEQ LKEEELNPDF IEQVAEFCSY ILSHSNVKTL SGGIPVNGPR LESLVLTYVN AISSGDLPCM ENAVLALAQI ENSAAVEKAI AHYEQQMGQK VQLPTETLQE LLDLHRDSER EAIEVFMKNS FKDVDQMFQR KLGAQLEARR DDFCKQNSKA SSDCCMALLQ DIFGPLEEDV KQGTFSKPGG YRLFTQKLQE LKNKYYQVPR KGIQAKEVLK KYLESKEDVA DALLQTDQSL SEKEKAIEVE RIKAESAEAA KKMLEEIQKK NEEMMEQKEK SYQEHVKQLT EKMERDRAQL MAEQEKTLAL KLQEQERLLK EGFENESKRL QKDIWDIQMR SKSLEPICNI L //