Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01412
Entry Name
UniProt Accession
Theoretical PI
5.97
Molecular Weight
67930.73
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Interferon-induced guanylate-binding protein 1
Protein Synonyms/Alias
GTP-binding protein 1; GBP-1; HuGBP-1; Guanine nucleotide-binding protein 1;
Gene Name
GBP1
Gene Synonyms/Alias
Created Date
01-OCT-1993
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
589
Canonical
KMRRRKACTIS****
[1]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Nantais DE, Schwemmle M, Stickney JT, Vestal DJ, Buss JE. Prenylation of aninterferon-gamma-induced GTP-binding protein: the human guanylate bindingprotein, huGBP1. J Leukoc Biol. 1996 Sep;60(3):423-31.[PMID:8830800]
Functional Description
Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.
Sequence Annotation
Domain: 35 278 GB1/RHD3-type G.
Nucleotide-binding: 45 52 GTP.
Nucleotide-binding: 67 69 GTP.
Nucleotide-binding: 97 101 GTP.
Region: 1 311 GTPase domain (Globular).
Modified residue: 589 589 Cysteine methyl ester.
Protein Length
592 AA.
Protein Sequence
(Canonical)
MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG KSYLMNKLAG  60
KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG LGDVEKGDNQ NDSWIFALAV  120
LLSSTFVYNS IGTINQQAMD QLYYVTELTH RIRSKSSPDE NENEVEDSAD FVSFFPDFVW  180
TLRDFSLDLE ADGQPLTPDE YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR  240
PVHRRKLAQL EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY  300
VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTETL QELLDLHRDS  360
EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ EASSDRCSAL LQVIFSPLEE  420
EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE PRKGIQAEEI LQTYLKSKES MTDAILQTDQ  480
TLTEKEKEIE VERVKAESAQ ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV  540
QLLKEQERTL ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKACT IS          592
FASTA
(Canonical)
>LipidDB-9606-01412|P32455
MASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAG
KKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAV
LLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVW
TLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDR
PVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTY
VNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDS
EREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEE
EVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQ
TLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRV
QLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS
Gene Ontology
GO:0005829; C:cytosol; TAS:Reactome
GO:0005576; C:extracellular region; IEA:UniProtKB-KW
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005525; F:GTP binding; TAS:ProtInc
GO:0003924; F:GTPase activity; IEA:InterPro
GO:0042802; F:identical protein binding; IPI:IntAct
GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome
GO:0051607; P:defense response to virus; IEA:UniProtKB-KW
GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome
Interpro
InterPro; IPR003191; Guanylate-bd_C
InterPro; IPR015894; Guanylate-bd_N
InterPro; IPR027417; P-loop_NTPase
Pfam
Pfam; PF02263; GBP;
Pfam; PF02841; GBP_C;
SMART
PROSITE
PROSITE; PS51715; G_GB1_RHD3;
PRINTS