GBP1_HUMAN
ID GBP1_HUMAN Reviewed; 592 AA.
AC P32455; D3DT26; Q5T8M1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Guanylate-binding protein 1;
DE EC=3.6.5.- {ECO:0000269|PubMed:10676968, ECO:0000269|PubMed:16511497};
DE AltName: Full=GTP-binding protein 1;
DE Short=GBP-1;
DE Short=HuGBP-1;
DE AltName: Full=Guanine nucleotide-binding protein 1;
DE AltName: Full=Interferon-induced guanylate-binding protein 1;
DE Flags: Precursor;
GN Name=GBP1;
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 VARIANTS SER-349 AND GLY-409.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-349 AND GLY-409.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-349 AND GLY-409.
RC TISSUE=Uterus;
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 [7]
RP ISOPRENYLATION AT CYS-589.
RX PubMed=8830800; DOI=10.1002/jlb.60.3.423;
RA Nantais D.E., Schwemmle M., Stickney J.T., Vestal D.J., Buss J.E.;
RT "Prenylation of an interferon-gamma-induced GTP-binding protein: the human
RT guanylate binding protein, huGBP1.";
RL J. Leukoc. Biol. 60:423-431(1996).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15937107; DOI=10.1073/pnas.0503227102;
RA Modiano N., Lu Y.E., Cresswell P.;
RT "Golgi targeting of human guanylate-binding protein-1 requires nucleotide
RT binding, isoprenylation, and an IFN-gamma-inducible cofactor.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8680-8685(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16936281; DOI=10.2353/ajpath.2006.060244;
RA Naschberger E., Lubeseder-Martellato C., Meyer N., Gessner R., Kremmer E.,
RA Gessner A., Sturzl M.;
RT "Human guanylate binding protein-1 is a secreted GTPase present in
RT increased concentrations in the cerebrospinal fluid of patients with
RT bacterial meningitis.";
RL Am. J. Pathol. 169:1088-1099(2006).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP SUBCELLULAR LOCATION, DIMERIZATION, ISOPRENYLATION, AND MUTAGENESIS OF
RP LYS-51; 227-ARG-LYS-228 AND 589-CYS--SER-592.
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 [13]
RP FUNCTION.
RX PubMed=22106366; DOI=10.1096/fj.11-189886;
RA Nordmann A., Wixler L., Boergeling Y., Wixler V., Ludwig S.;
RT "A new splice variant of the human guanylate-binding protein 3 mediates
RT anti-influenza activity through inhibition of viral transcription and
RT replication.";
RL FASEB J. 26:1290-1300(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND GTP-BINDING.
RX PubMed=10676968; DOI=10.1038/35000617;
RA Prakash B., Praefcke G.J.K., Renault L., Wittinghofer A., Herrmann C.;
RT "Structure of human guanylate-binding protein 1 representing a unique class
RT of GTP-binding proteins.";
RL Nature 403:567-571(2000).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GTP ANALOG, AND
RP GTP-BINDING.
RX PubMed=10970849; DOI=10.1093/emboj/19.17.4555;
RA Prakash B., Renault L., Praefcke G.J., Herrmann C., Wittinghofer A.;
RT "Triphosphate structure of guanylate-binding protein 1 and implications for
RT nucleotide binding and GTPase mechanism.";
RL EMBO J. 19:4555-4564(2000).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-317, AND SUBUNIT.
RX PubMed=16511497; DOI=10.1038/nature04510;
RA Ghosh A., Praefcke G.J., Renault L., Wittinghofer A., Herrmann C.;
RT "How guanylate-binding proteins achieve assembly-stimulated processive
RT cleavage of GTP to GMP.";
RL Nature 440:101-104(2006).
CC -!- FUNCTION: Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions (By
CC similarity). Confers protection to several pathogens, including the
CC bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG
CC as well as the protozoan pathogen Toxoplasma gondii (By similarity).
CC Promotes IFN-gamma-mediated host defense against bacterial infections
CC by regulating bacteriolytic peptide generation via its interaction with
CC ubiquitin-binding protein SQSTM1, which delivers monoubiquitylated
CC proteins to autolysosomes for the generation of bacteriolytic peptides
CC (By similarity). Exhibits antiviral activity against influenza virus
CC (PubMed:22106366). {ECO:0000250|UniProtKB:Q01514,
CC ECO:0000269|PubMed:22106366}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; 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:10676968, ECO:0000269|PubMed:16511497};
CC -!- SUBUNIT: Homodimer; homodimerization occurs upon GTP-binding and is
CC required for the second hydrolysis step from GDP to GMP. Heterodimer
CC with other family members, including GBP2, GBP3, GBP4 and GBP5.
CC Dimerization regulates subcellular location to membranous structures
CC (PubMed:21151871). Interacts with SQSTM1 (By similarity).
CC {ECO:0000250|UniProtKB:Q01514, ECO:0000269|PubMed:10970849,
CC ECO:0000269|PubMed:16511497, ECO:0000269|PubMed:21151871}.
CC -!- INTERACTION:
CC P32455; P32455: GBP1; NbExp=15; IntAct=EBI-2869161, EBI-2869161;
CC P32455; P32456: GBP2; NbExp=9; IntAct=EBI-2869161, EBI-714388;
CC P32455; Q9H0R5: GBP3; NbExp=3; IntAct=EBI-2869161, EBI-2798916;
CC P32455; Q96PP9: GBP4; NbExp=2; IntAct=EBI-2869161, EBI-20840650;
CC P32455; Q96PP8: GBP5; NbExp=9; IntAct=EBI-2869161, EBI-749932;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21151871}. Golgi
CC apparatus membrane; Lipid-anchor {ECO:0000269|PubMed:21151871};
CC Cytoplasmic side. Cell membrane {ECO:0000269|PubMed:21151871}. Secreted
CC {ECO:0000269|PubMed:16936281}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q01514}. Note=Secreted from endothelial cells in
CC the cerebrospinal fluid, upon bacterial challenge and independently of
CC IFNG induction. Golgi membrane localization requires isoprenylation and
CC the presence of another IFNG-induced factor.
CC -!- INDUCTION: By IFNG during macrophage activation, and by TNF and IL1B.
CC {ECO:0000269|PubMed:17266443}.
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 -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GBP1ID50147ch1p22.html";
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DR EMBL; M55542; AAA35871.1; -; mRNA.
DR EMBL; BT006847; AAP35493.1; -; mRNA.
DR EMBL; AK291783; BAF84472.1; -; mRNA.
DR EMBL; AL160008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73148.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73150.1; -; Genomic_DNA.
DR EMBL; BC002666; AAH02666.1; -; mRNA.
DR CCDS; CCDS718.1; -.
DR PIR; A41268; A41268.
DR RefSeq; NP_002044.2; NM_002053.2.
DR PDB; 1DG3; X-ray; 1.80 A; A=1-592.
DR PDB; 1F5N; X-ray; 1.70 A; A=1-592.
DR PDB; 2B8W; X-ray; 2.22 A; A/B=1-317.
DR PDB; 2B92; X-ray; 3.20 A; A/B=1-317.
DR PDB; 2BC9; X-ray; 2.80 A; A=1-317.
DR PDB; 2D4H; X-ray; 2.90 A; A/B=1-317.
DR PDB; 6K1Z; X-ray; 2.31 A; A=1-592.
DR PDB; 6K2D; X-ray; 3.60 A; A=1-479.
DR PDB; 6LOJ; X-ray; 3.72 A; B=1-592.
DR PDBsum; 1DG3; -.
DR PDBsum; 1F5N; -.
DR PDBsum; 2B8W; -.
DR PDBsum; 2B92; -.
DR PDBsum; 2BC9; -.
DR PDBsum; 2D4H; -.
DR PDBsum; 6K1Z; -.
DR PDBsum; 6K2D; -.
DR PDBsum; 6LOJ; -.
DR AlphaFoldDB; P32455; -.
DR SASBDB; P32455; -.
DR SMR; P32455; -.
DR BioGRID; 108903; 34.
DR DIP; DIP-60423N; -.
DR IntAct; P32455; 13.
DR MINT; P32455; -.
DR STRING; 9606.ENSP00000359504; -.
DR iPTMnet; P32455; -.
DR MetOSite; P32455; -.
DR PhosphoSitePlus; P32455; -.
DR SwissPalm; P32455; -.
DR BioMuta; GBP1; -.
DR DMDM; 311033383; -.
DR EPD; P32455; -.
DR jPOST; P32455; -.
DR MassIVE; P32455; -.
DR MaxQB; P32455; -.
DR PaxDb; P32455; -.
DR PeptideAtlas; P32455; -.
DR PRIDE; P32455; -.
DR ProteomicsDB; 54877; -.
DR Antibodypedia; 4224; 323 antibodies from 34 providers.
DR DNASU; 2633; -.
DR Ensembl; ENST00000370473.5; ENSP00000359504.4; ENSG00000117228.11.
DR GeneID; 2633; -.
DR KEGG; hsa:2633; -.
DR MANE-Select; ENST00000370473.5; ENSP00000359504.4; NM_002053.3; NP_002044.2.
DR UCSC; uc001dmx.3; human.
DR CTD; 2633; -.
DR DisGeNET; 2633; -.
DR GeneCards; GBP1; -.
DR HGNC; HGNC:4182; GBP1.
DR HPA; ENSG00000117228; Tissue enhanced (liver).
DR MIM; 600411; gene.
DR neXtProt; NX_P32455; -.
DR OpenTargets; ENSG00000117228; -.
DR PharmGKB; PA28596; -.
DR VEuPathDB; HostDB:ENSG00000117228; -.
DR eggNOG; KOG2037; Eukaryota.
DR GeneTree; ENSGT00940000156840; -.
DR HOGENOM; CLU_018608_2_2_1; -.
DR InParanoid; P32455; -.
DR OMA; SSMLNWL; -.
DR OrthoDB; 1027269at2759; -.
DR PhylomeDB; P32455; -.
DR TreeFam; TF331602; -.
DR PathwayCommons; P32455; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; P32455; -.
DR BioGRID-ORCS; 2633; 21 hits in 1068 CRISPR screens.
DR ChiTaRS; GBP1; human.
DR EvolutionaryTrace; P32455; -.
DR GeneWiki; GBP1; -.
DR GenomeRNAi; 2633; -.
DR Pharos; P32455; Tbio.
DR PRO; PR:P32455; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P32455; protein.
DR Bgee; ENSG00000117228; Expressed in pericardium and 194 other tissues.
DR Genevisible; P32455; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012506; C:vesicle membrane; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0019955; F:cytokine binding; IPI:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:CAFA.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:CAFA.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; IPI:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:UniProtKB.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0072665; P:protein localization to vacuole; IDA:UniProtKB.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IGI:UniProtKB.
DR CDD; cd16269; GBP_C; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF02263; GBP; 1.
DR Pfam; PF02841; GBP_C; 1.
DR SUPFAM; SSF48340; SSF48340; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Hydrolase; Immunity;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome; Secreted.
FT CHAIN 1..589
FT /note="Guanylate-binding protein 1"
FT /id="PRO_0000190963"
FT PROPEP 590..592
FT /note="Removed in mature form"
FT /id="PRO_0000396777"
FT DOMAIN 35..278
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..311
FT /note="GTPase domain (Globular)"
FT /evidence="ECO:0000305|PubMed:10676968"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:10676968,
FT ECO:0000269|PubMed:10970849, ECO:0007744|PDB:1F5N"
FT BINDING 67..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:10676968,
FT ECO:0000269|PubMed:10970849, ECO:0007744|PDB:1F5N"
FT BINDING 97..101
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:10676968,
FT ECO:0000269|PubMed:10970849, ECO:0007744|PDB:1F5N"
FT MOD_RES 589
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 589
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:8830800"
FT VARIANT 78
FT /note="I -> V (in dbSNP:rs1048401)"
FT /id="VAR_033950"
FT VARIANT 166
FT /note="E -> D (in dbSNP:rs17130717)"
FT /id="VAR_033951"
FT VARIANT 349
FT /note="T -> S (in dbSNP:rs1048425)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:1715024, ECO:0000269|Ref.2"
FT /id="VAR_014849"
FT VARIANT 409
FT /note="A -> G (in dbSNP:rs1048443)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:1715024, ECO:0000269|Ref.2"
FT /id="VAR_046550"
FT MUTAGEN 51
FT /note="K->A: Loss of GTPase activity. Constitutively
FT monomeric. Expressed throughout the cytoplasm, loss of
FT vesicular accumulation."
FT /evidence="ECO:0000305|PubMed:21151871"
FT MUTAGEN 227..228
FT /note="RK->EE: Constitutively dimeric. Localizes at
FT vesicle-like structures at the plasma membrane."
FT /evidence="ECO:0000269|PubMed:21151871"
FT MUTAGEN 589..592
FT /note="Missing: Loss of association with membranes."
FT /evidence="ECO:0000269|PubMed:21151871"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1DG3"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2B8W"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1F5N"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1DG3"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2D4H"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 214..229
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:1F5N"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 290..306
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 312..342
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 350..371
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 379..423
FT /evidence="ECO:0007829|PDB:1F5N"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 432..449
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 457..467
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 469..478
FT /evidence="ECO:0007829|PDB:1F5N"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 484..563
FT /evidence="ECO:0007829|PDB:1F5N"
FT HELIX 566..582
FT /evidence="ECO:0007829|PDB:1F5N"
SQ SEQUENCE 592 AA; 67931 MW; 3A06741218360732 CRC64;
MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG KSYLMNKLAG
KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG LGDVEKGDNQ NDSWIFALAV
LLSSTFVYNS IGTINQQAMD QLYYVTELTH RIRSKSSPDE NENEVEDSAD FVSFFPDFVW
TLRDFSLDLE ADGQPLTPDE YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR
PVHRRKLAQL EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY
VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTETL QELLDLHRDS
EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ EASSDRCSAL LQVIFSPLEE
EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE PRKGIQAEEI LQTYLKSKES MTDAILQTDQ
TLTEKEKEIE VERVKAESAQ ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV
QLLKEQERTL ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKACT IS
