GBP5
entrez
115362
canonical
uniprot
Q96PP8
canonical
ensembl
ENSG00000154451
resolver
ensp
ENSP00000359488
resolver
ensp
ENSP00000403010
resolver
ensp
ENSP00000536445
resolver
genesymbol
GBP5
resolver
hgnc
HGNC:19895
resolver
uniprot
B2RCE1
resolver
uniprot
Q86TM5
resolver
uniprot_entry
GBP5_HUMAN
resolver
uniprot_sec
B2RCE1
resolver
uniprot_sec
Q86TM5
resolver
amino_acid_sequence
MALEIHMSDPMCLIENFNEQLKVNQEALEILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKNKGFSVASTVQSHTKGIWIWCVPHPNWPNHTLVLLDTEGLGDVEKADNKNDIQIFALALLLSSTFVYNTVNKIDQGAIDLLHNVTELTDLLKARNSPDLDRVEDPADSASFFPDLVWTLRDFCLGLEIDGQLVTPDEYLENSLRPKQGSDQRVQNFNLPRLCIQKFFPKKKCFIFDLPAHQKKLAQLETLPDDELEPEFVQQVTEFCSYIFSHSMTKTLPGGIMVNGSRLKNLVLTYVNAISSGDLPCIENAVLALAQRENSAAVQKAIAHYDQQMGQKVQLPMETLQELLDLHRTSEREAIEVFMKNSFKDVDQSFQKELETLLDAKQNDICKRNLEASSDYCSALLKDIFGPLEEAVKQGIYSKPGGHNLFIQKTEELKAKYYREPRKGIQAEEVLQKYLKSKESVSHAILQTDQALTETEKKKKEAQVKAEAEKAEAQRLAAIQRQNEQMMQERERLHQEQVRQMEIAKQNWLAEQQKMQEQQMQEQAAQLSTTFQAQNRSLLSELQHAQRTVNNDDPCVLL
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 (By similarity). Hydrolyzes GTP, but in contrast to other family members, does not produce GMP (PubMed:20180847). 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). As an activator of NLRP3 inflammasome assembly: promotes selective NLRP3 inflammasome assembly in response to microbial and soluble, but not crystalline, agents (PubMed:22461501). 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:26996307, PubMed:31091448). {ECO:0000250|UniProtKB:Q8CFB4, ECO:0000269|PubMed:20180847, ECO:0000269|PubMed:22461501, ECO:0000269|PubMed:26996307, ECO:0000269|PubMed:31091448}.; FUNCTION: Antigenic tumor-specific truncated splice form. {ECO:0000269|PubMed:15175044}.
uniprot
proteins
mass_dalton
66617
uniprot
proteins
mutagenesis
MUTAGEN 51..52; /note="KS->AA: Loss of GTPase activity. No effect on tetramerization. Does not affect ability to inhibit HIV-1 infectivity."; /evidence="ECO:0000269|PubMed:22461501, ECO:0000269|PubMed:26996307"; MUTAGEN 73; /note="S->A: Does not affect GTPase activity."; /evidence="ECO:0000269|PubMed:33876762"; MUTAGEN 75; /note="T->S: Abolished GTPase activity, without affecting ability to inhibit HIV-1 infectivity."; /evidence="ECO:0000269|PubMed:26996307"; MUTAGEN 137..141; /note="GAIDL->QAIDQ: Promotes ubiquitination and degradation by S.flexneri IpaH9.8."; /evidence="ECO:0000269|PubMed:31216343"; MUTAGEN 182; /note="D->N: Decreased nucleotide-binding, without affecting ability to inhibit HIV-1 infectivity."; /evidence="ECO:0000269|PubMed:26996307"; MUTAGEN 356; /note="R->A: No effect."; /evidence="ECO:0000269|PubMed:33876762"; MUTAGEN 417..421; /note="EEAVK->AEAVA: In MMMD mutant; abolished dimerization and ability to restrict HIV-1; when associated with 464-A--A-476."; /evidence="ECO:0000269|PubMed:33876762"; MUTAGEN 464..476; /note="KSKESVSHAILQT->AAAEAASAAILAA: In MMMD mutant; abolished dimerization and ability to restrict HIV-1; when associated with 417-A--A-421."; /evidence="ECO:0000269|PubMed:33876762"; MUTAGEN 583..586; /note="Missing: Loss of isoprenylation and of localization at the Golgi apparatus."; /evidence="ECO:0000269|PubMed:21151871"; MUTAGEN 583; /note="C->A: Loss of isoprenylation and of localization at the Golgi apparatus. Impaired ability to restrict HIV-1."; /evidence="ECO:0000269|PubMed:26996307, ECO:0000269|PubMed:31091448
uniprot
proteins
post_translational_modification
PTM: Isoprenylation is required for proper subcellular location. {ECO:0000269|PubMed:21151871}.
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
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15175044
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17266443
uniprot
proteins
pubmed
20180847
uniprot
proteins
pubmed
21151871
uniprot
proteins
pubmed
22461501
uniprot
proteins
pubmed
26996307
uniprot
proteins
pubmed
31091448
uniprot
proteins
pubmed
31216343
uniprot
proteins
pubmed
33876762
uniprot
proteins
sequence_length
586
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8CFB4}; Lipid-anchor, GPI-like-anchor {ECO:0000269|PubMed:21151871}. Golgi apparatus membrane {ECO:0000269|PubMed:17266443, ECO:0000269|PubMed:21151871, ECO:0000269|PubMed:26996307, ECO:0000269|PubMed:31091448}; Lipid-anchor {ECO:0000269|PubMed:21151871}. Cytoplasm {ECO:0000269|PubMed:17266443, ECO:0000269|PubMed:21151871}.
uniprot
proteins