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Details on Person UniProt:P32456 GBP2
| Class:Id | ReferenceGeneProduct:55452 |
|---|---|
| _chainChangeLog | chain:1-588 added on Sat February 7 2015;propeptide:589-591 added on Sat February 7 2015 |
| _displayName | UniProt:P32456 GBP2 |
| _timestamp | 2025-02-21 20:09:18 |
| chain | chain:1-588 propeptide:589-591 |
| checksum | B09B3C2F3C3E1EA2 |
| comment | FUNCTION Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:31091448). Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (PubMed:8706832). Following infection, recruited to the pathogen-containing vacuoles or vacuole-escaped bacteria and acts as a positive regulator of inflammasome assembly by promoting the release of inflammasome ligands from bacteria (By similarity). Acts by promoting lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol (By similarity). Following pathogen release in the cytosol, promotes recruitment of proteins that mediate bacterial cytolysis: this liberates ligands that are detected by inflammasomes, such as lipopolysaccharide (LPS) that activates the non-canonical CASP4/CASP11 inflammasome or double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (By similarity). Confers protection to the protozoan pathogen Toxoplasma gondii (By similarity). Independently of its GTPase activity, acts as an inhibitor of various viruses infectivity, such as HIV-1, Zika and influenza A viruses, by inhibiting FURIN-mediated maturation of viral envelope proteins (PubMed:31091448).CATALYTIC ACTIVITY GTP + H2O = GDP + phosphate + H(+)BIOPHYSICOCHEMICAL PROPERTIES Homodimer; homodimerization occurs upon GTP-binding and is required for the association with membranous structures (PubMed:21151871). Heterodimer with other family members, including GBP1, GBP3, GBP4 and GBP5 (PubMed:21151871).INTERACTION GBP2-GBP5 dimers localize to the Golgi apparatus.INDUCTION By IFNG/IFN-gamma during macrophage activation, and by TNF and IL1B.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.PTM Isoprenylation is required for proper subcellular location.SIMILARITY Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. GB1 subfamily. |
| description | recommendedName: Guanylate-binding protein 2 ecNumber evidence="14"3.6.5.- alternativeName: fullName evidence="17"GTP-binding protein 2 shortName evidence="17"GBP-2 shortName: HuGBP-2 alternativeName: fullName evidence="17"Guanine nucleotide-binding protein 2 alternativeName: Interferon-induced guanylate-binding protein 2 |
| geneName | GBP2 |
| identifier | P32456 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Antimicrobial Cytoplasm Cytoplasmic vesicle Golgi apparatus GTP-binding Hydrolase Immunity Innate immunity Lipoprotein Membrane Methylation Nucleotide-binding Prenylation Proteomics identification Reference proteome Ubl conjugation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | GBP2 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8962500] ENSEMBL:ENSG00000162645 GBP2 [Homo sapiens] |
| secondaryIdentifier | GBP2_HUMAN Q6GPH0 Q6IAU2 Q86TB0 |
| sequenceLength | 591 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:1015673] GBP2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:9947851] GGC-C588-GBP2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:9955197] K48polyUb-GBP2 [cytosol] [Homo sapiens] |
| (referenceSequence) | [GroupModifiedResidue:9947858] S-geranylgeranyl-L-cysteine (geranylgeranyl group) at 588 [GroupModifiedResidue:9955158] ubiquitinylated lysine (K48polyUb [cytosol]) at unknown position |
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No pathways have been reviewed or authored by UniProt:P32456 GBP2 (55452)
