Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00297
Entry Name
UniProt Accession
Theoretical PI
5.56
Molecular Weight
66739.49
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Interferon-induced guanylate-binding protein 2
Protein Synonyms/Alias
GTP-binding protein 2; GBP-2; mGBP-2; mGBP2; Guanine nucleotide-binding protein 2;
Gene Name
Gbp2
Gene Synonyms/Alias
Created Date
24-OCT-2003
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
586
Canonical
QNKSSGKCTIL****
[1]
S-Geranylgeranylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Vestal DJ, Buss JE, McKercher SR, Jenkins NA, Copeland NG, Kelner GS, AsundiVK, Maki RA. Murine GBP-2: a new IFN-gamma-induced member of the GBP family ofGTPases isolated from macrophages. J Interferon Cytokine Res. 1998Nov;18(11):977-85.[PMID:9858320]
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 (By similarity).
Sequence Annotation
Domain: 35 276 GB1/RHD3-type G.
Nucleotide-binding: 45 52 GTP.
Nucleotide-binding: 67 69 GTP.
Nucleotide-binding: 97 101 GTP.
Region: 1 309 GTPase domain (Globular).
Modified residue: 586 586 Cysteine methyl ester.
Protein Length
589 AA.
Protein Sequence
(Canonical)
MASEIHMSEP MCLIENTEAQ LVINQEALRI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG  60
KRTGFSLGST VQSHTKGIWM WCVPHPKKAG QTLVLLDTEG LEDVEKGDNQ NDCWIFALAV  120
LLSSTFIYNS IGTINQQAMD QLHYVTELTD LIKSKSSPDQ SGVDDSANFV GFFPTFVWTL  180
RDFSLELEVN GKPVTSDEYL EHSLTLKKGA DKKTKSFNEP RLCIRKFFPK RKCFIFDRPA  240
QRKQLSKLET LREEELCGEF VEQVAEFTSY ILSYSSVKTL CGGIIVNGPR LKSLVQTYVG  300
AISNGSLPCM ESAVLTLAQI ENSAAVQKAI THYEEQMNQK IQMPTETLQE LLDLHRPIES  360
EAIEVFLKNS FKDVDQKFQT ELGNLLVAKR DAFIKKNMDV SSARCSDLLE DIFGPLEEEV  420
KLGTFSKPGG YYLFLQMRQE LEKKYNQAPG KGLQAEAMLK NYFDSKADVV ETLLQTDQSL  480
TEAAKEVEEE RTKAEAAEAA NRELEKKQKE FELMMQQKEK SYQEHVKKLT EKMKDEQKQL  540
LAEQENIIAA KLREQEKFLK EGFENESKKL IREIDTLKQN KSSGKCTIL              589
FASTA
(Canonical)
>LipidDB-10090-00297|Q9Z0E6
MASEIHMSEPMCLIENTEAQLVINQEALRILSAITQPVVVVAIVGLYRTGKSYLMNKLAG
KRTGFSLGSTVQSHTKGIWMWCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAV
LLSSTFIYNSIGTINQQAMDQLHYVTELTDLIKSKSSPDQSGVDDSANFVGFFPTFVWTL
RDFSLELEVNGKPVTSDEYLEHSLTLKKGADKKTKSFNEPRLCIRKFFPKRKCFIFDRPA
QRKQLSKLETLREEELCGEFVEQVAEFTSYILSYSSVKTLCGGIIVNGPRLKSLVQTYVG
AISNGSLPCMESAVLTLAQIENSAAVQKAITHYEEQMNQKIQMPTETLQELLDLHRPIES
EAIEVFLKNSFKDVDQKFQTELGNLLVAKRDAFIKKNMDVSSARCSDLLEDIFGPLEEEV
KLGTFSKPGGYYLFLQMRQELEKKYNQAPGKGLQAEAMLKNYFDSKADVVETLLQTDQSL
TEAAKEVEEERTKAEAAEAANRELEKKQKEFELMMQQKEKSYQEHVKKLTEKMKDEQKQL
LAEQENIIAAKLREQEKFLKEGFENESKKLIREIDTLKQNKSSGKCTIL
Gene Ontology
GO:0031410; C:cytoplasmic vesicle; IDA:MGI
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0020005; C:symbiont-containing vacuole membrane; IDA:MGI
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; ISS:MGI
GO:0044406; P:adhesion of symbiont to host; IDA:MGI
GO:0035458; P:cellular response to interferon-beta; IDA:MGI
GO:0071346; P:cellular response to interferon-gamma; IDA:MGI
GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI
GO:0050830; P:defense response to Gram-positive bacterium; IDA:MGI
GO:0042832; P:defense response to protozoan; IDA:MGI
GO:0006184; P:GTP catabolic process; ISS:GOC
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