GBP1
entrez
2633
canonical
uniprot
P32455
canonical
ensembl
ENSG00000117228
resolver
ensp
ENSP00000359504
resolver
ensp
ENSP00000542794
resolver
ensp
ENSP00000542795
resolver
ensp
ENSP00000542796
resolver
ensp
ENSP00000542797
resolver
ensp
ENSP00000542798
resolver
enst
ENST00000370473
resolver
enst
ENST00000872735
resolver
enst
ENST00000872736
resolver
enst
ENST00000872737
resolver
enst
ENST00000872738
resolver
enst
ENST00000872739
resolver
genesymbol
GBP1
resolver
hgnc
HGNC:4182
resolver
uniprot
D3DT26
resolver
uniprot
Q5T8M1
resolver
uniprot_entry
GBP1_HUMAN
resolver
uniprot_sec
D3DT26
resolver
uniprot_sec
Q5T8M1
resolver
amino_acid_sequence
MASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS
uniprot
proteins
ec_number
3.6.1.-
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:16511497, PubMed:22106366, PubMed:29144452, PubMed:31268602, PubMed:32510692, PubMed:32581219, PubMed:37797010, PubMed:7512561). Hydrolyzes GTP to GMP in two consecutive cleavage reactions: GTP is first hydrolyzed to GDP and then to GMP in a processive manner (PubMed:16511497, PubMed:32510692, PubMed:7512561, PubMed:39394410). Following infection, recruited to the pathogen-containing vacuoles or vacuole-escaped bacteria and promotes both inflammasome assembly and autophagy (PubMed:29144452, PubMed:31268602). Acts as a positive regulator of inflammasome assembly by facilitating the detection of inflammasome ligands from pathogens (PubMed:31268602, PubMed:32510692, PubMed:32581219). Involved in the lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol (By similarity). Following pathogen release in the cytosol, forms a protein coat in a GTPase-dependent manner that encapsulates pathogens and promotes the detection of ligands by pattern recognition receptors (PubMed:32510692, PubMed:32581219). Plays a key role in inflammasome assembly in response to infection by Gram-negative bacteria: following pathogen release in the cytosol, forms a protein coat that encapsulates Gram-negative bacteria and directly binds to lipopolysaccharide (LPS), disrupting the O-antigen barrier and unmasking lipid A that is that detected by the non-canonical inflammasome effector CASP4/CASP11 (PubMed:32510692, PubMed:32581219). Also promotes recruitment of proteins that mediate bacterial cytolysis, leading to release double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (PubMed:31268602). Involved in autophagy by regulating bacteriolytic peptide generation via its interaction with ubiquitin-binding protein SQSTM1, which delivers monoubiquitinated proteins to autolysosomes for the generation of bacteriolytic peptides (By similarity). Confers protection to several pathogens, including the bacterial pathogens L.monocytogenes and M.bovis BCG as well as the protozoan pathogen T.gondii (PubMed:31268602). Exhibits antiviral activity against influenza virus (PubMed:22106366). {ECO:0000250|UniProtKB:Q01514, ECO:0000269|PubMed:16511497, ECO:0000269|PubMed:22106366, ECO:0000269|PubMed:29144452, ECO:0000269|PubMed:31268602, ECO:0000269|PubMed:32510692, ECO:0000269|PubMed:32581219, ECO:0000269|PubMed:37797010, ECO:0000269|PubMed:39394410, ECO:0000269|PubMed:7512561}.
uniprot
proteins
mass_dalton
67931
uniprot
proteins
mutagenesis
MUTAGEN 48; /note="R->A: Abolished GTPase activity."; /evidence="ECO:0000269|PubMed:28645896, ECO:0000269|PubMed:29144452, ECO:0000269|PubMed:32510692"; MUTAGEN 51; /note="K->A: Loss of GTPase activity. Constitutively monomeric. Expressed throughout the cytoplasm, loss of vesicular accumulation. Impaired ability to promote pyroptosis in response to T.gondii infection."; /evidence="ECO:0000269|PubMed:31268602, ECO:0000269|PubMed:32510692, ECO:0000305|PubMed:21151871"; MUTAGEN 61..63; /note="KKK->AAA: Impaired homooligomarization and localization to bacterial surface."; /evidence="ECO:0000269|PubMed:32581219"; MUTAGEN 74; /note="H->A: Abolished GDP hydrolysis."; /evidence="ECO:0000269|PubMed:32510692"; MUTAGEN 76; /note="K->A: Abolished GDPase activity."; /evidence="ECO:0000269|PubMed:28645896"; MUTAGEN 87..88; /note="KK->AA: Does not affect localization to bacterial surface."; /evidence="ECO:0000269|PubMed:32581219"; MUTAGEN 151; /note="R->A: Reduced phosphorylation by PIM1."; /evidence="ECO:0000269|PubMed:37797010"; MUTAGEN 153..158; /note="RSKSSP->ASKSSA: Abolished phosphorylation by PIM1 and interaction with 14-3-3 protein sigma (SFN)."; /evidence="ECO:0000269|PubMed:37797010"; MUTAGEN 153; /note="R->A: Abolished phosphorylation by PIM1."; /evidence="ECO:0000269|PubMed:37797010"; MUTAGEN 155; /note="K->A: Abolished phosphorylation by PIM1."; /evidence="ECO:0000269|PubMed:37797010"; MUTAGEN 156; /note="S->A: Reduced phosphorylation by PIM1, leading to hyperactivation and Golgi fragmentation."; /evidence="ECO:0000269|PubMed:37797010"; MUTAGEN 157; /note="S->A: No effect."; /evidence="ECO:0000269|PubMed:37797010"; MUTAGEN 184; /note="D->N: Strongly decreased nucleotide-binding."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 207..210; /note="KLKK->ALAA: Does not affect localization to bacterial surface."; /evidence="ECO:0000269|PubMed:32581219"; MUTAGEN 207; /note="K->R: In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-209, R-210, R-382, R-562, R-567, R-573 and R-587."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 209; /note="K->R: In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-210, R-382, R-562, R-567, R-573 and R-587."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 210; /note="K->R: In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-382, R-562, R-567, R-573 and R-587."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 227..228; /note="RK->EE: Constitutively dimeric. Localizes at vesicle-like structures at the plasma membrane."; /evidence="ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:31268602"; MUTAGEN 244..246; /note="RRK->AAA: Does not affect localization to bacterial surface."; /evidence="ECO:0000269|PubMed:32581219"; MUTAGEN 308; /note="D->S: Impairs membrane association; alone and when associated with A-309 and A-310."; /evidence="ECO:0000269|PubMed:39394410"; MUTAGEN 309; /note="L->A: Impairs membrane association; when associated with A-308 and A-310."; /evidence="ECO:0000269|PubMed:39394410"; MUTAGEN 310; /note="P->A: Impairs membrane association; when associated with A-308 and A-309."; /evidence="ECO:0000269|PubMed:39394410"; MUTAGEN 382; /note="K->R: In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-562, R-567, R-573 and R-587."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 427; /note="Y->F: No effect."; /evidence="ECO:0000269|PubMed:37797010"; MUTAGEN 562; /note="K->R: In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-382, R-567, R-573 and R-587."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 567; /note="K->R: In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-382, R-562, R-573 and R-587."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 573; /note="K->R: In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-382, R-562, R-567 and R-587."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 584..586; /note="RRR->AAA: Abolished localization to pathogen-containing vacuoles. Abolished binding to bacterial surface."; /evidence="ECO:0000269|PubMed:29233899, ECO:0000269|PubMed:32510692"; MUTAGEN 584..586; /note="Missing: Abolished localization to pathogen-containing vacuoles."; /evidence="ECO:0000269|PubMed:29233899"; MUTAGEN 587; /note="K->R: In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-382, R-562, R-567 and R-573."; /evidence="ECO:0000269|PubMed:29144452"; MUTAGEN 589..592; /note="Missing: Loss of association with membranes."; /evidence="ECO:0000269|PubMed:21151871"; MUTAGEN 589; /note="C->S: Abolished farnesylation and recruitment to the pathogen-containing vacuoles or vacuole-escaped bacteria. Impaired ability to promote pyroptosis in response to T.gondii infection."; /evidence="ECO:0000269|PubMed:29144452, ECO:0000269|PubMed:31268602"; MUTAGEN 590; /note="T->A: Does not affect interaction with 14-3-3 protein sigma (SFN)."; /evidence="ECO:0000269|PubMed:37797010
uniprot
proteins
post_translational_modification
PTM: Isoprenylation is required for proper subcellular location. {ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:28645896, ECO:0000269|PubMed:31268602, ECO:0000269|PubMed:32510692}.; PTM: Phosphorylated at Ser-156 by PIM1 in absence of infection, inhibits GBP1: phosphorylation promotes interaction with 14-3-3 protein sigma (SFN), leading to GBP1 retention in the cytosol (PubMed:37797010). Dephosphorylated in response to infection, liberating GBP1 (PubMed:37797010). {ECO:0000269|PubMed:37797010}.; PTM: (Microbial infection) Ubiquitinated by S.flexneri IpaH9.8, leading to its degradation by the proteasome, thereby preventing its ability to promote host defense against bacterial infection. {ECO:0000269|PubMed:29024643, ECO:0000269|PubMed:29144452, ECO:0000269|PubMed:31216343, ECO:0000269|PubMed:33303953, ECO:0000269|PubMed:37014865}.
uniprot
proteins
protein_family
GB1 subfamily
uniprot
proteins
protein_family
GB1/RHD3 GTPase family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
10676968
uniprot
proteins
pubmed
10970849
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15937107
uniprot
proteins
pubmed
16511497
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16936281
uniprot
proteins
pubmed
1715024
uniprot
proteins
pubmed
17266443
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21151871
uniprot
proteins
pubmed
22106366
uniprot
proteins
pubmed
28645896
uniprot
proteins
pubmed
29024643
uniprot
proteins
pubmed
29144452
uniprot
proteins
pubmed
29233899
uniprot
proteins
pubmed
31216343
uniprot
proteins
pubmed
31268602
uniprot
proteins
pubmed
32510692
uniprot
proteins
pubmed
32581219
uniprot
proteins
pubmed
33303953
uniprot
proteins
pubmed
37014865
uniprot
proteins
pubmed
37797010
uniprot
proteins
pubmed
39394410
uniprot
proteins
pubmed
7512561
uniprot
proteins
pubmed
8830800
uniprot
proteins
sequence_length
592
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:29144452, ECO:0000269|PubMed:29233899, ECO:0000269|PubMed:31268602}; Lipid-anchor {ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:39394410}; Cytoplasmic side {ECO:0000269|PubMed:21151871}. Golgi apparatus membrane {ECO:0000269|PubMed:15937107}; Lipid-anchor {ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:39394410}; Cytoplasmic side {ECO:0000269|PubMed:21151871}. Cell membrane {ECO:0000269|PubMed:21151871}; Lipid-anchor {ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:39394410}; Cytoplasmic side {ECO:0000269|PubMed:21151871}. Cytoplasm, cytosol {ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:37797010}. Secreted {ECO:0000269|PubMed:16936281}. Note=Localizes to pathogen-containing vacuoles or to the cell surface of bacteria that escaped vacuoles (PubMed:29144452, PubMed:31268602, PubMed:32510692, PubMed:32581219). Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of IFNG induction (PubMed:16936281). Golgi membrane localization requires isoprenylation and the presence of another IFNG-induced factor (PubMed:15937107). Sequestered in the cytosol following phosphorylation by PIM1 and subsequent interaction with 14-3-3 protein sigma (SFN) (PubMed:37797010). {ECO:0000269|PubMed:15937107, ECO:0000269|PubMed:16936281, ECO:0000269|PubMed:29144452, ECO:0000269|PubMed:31268602, ECO:0000269|PubMed:32510692, ECO:0000269|PubMed:32581219, ECO:0000269|PubMed:37797010}.
uniprot
proteins