Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00476
Entry Name
UniProt Accession
Theoretical PI
5.54
Molecular Weight
67109.05
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Interferon-induced guanylate-binding protein 2
Protein Synonyms/Alias
GTP-binding protein 2; GBP-2; Guanine nucleotide-binding protein 2; p67;
Gene Name
Gbp2
Gene Synonyms/Alias
Created Date
24-OCT-2003
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
586
Canonical
RRQSPGKCTIL****
[1]
S-Geranylgeranylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Asundi VK, Stahl RC, Showalter L, Conner KJ, Carey DJ. Molecular cloning andcharacterization of an isoprenylated 67 kDa protein. Biochim Biophys Acta. 1994Apr 6;1217(3):257-65.[PMID:8148370]
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)
MASEIHMLQP MCLIENTEAH LVINQEALRI LSAINQPVVV VAIVGLYRTG KSYLMNKLAG  60
KRTGFSLGST VQSHTKGIWM WCVPHPKKAG QTLVLLDTEG LEDVEKGDNQ NDCWIFALAV  120
LLSSTFVYNS MGTINQQAMD QLHYVTELTD LIKSKSSPDQ SGIDDSANFV GFFPTFVWAL  180
RDFSLELEVN GKLVTPDEYL EHSLTLKKGA DKKTKSFNEP RLCIRKFFPK RKCFIFDRPA  240
LRKQLCKLET LGEEELCSEF VEQVAEFTSY IFSYSAVKTL SGGIIVNGPR LKSLVQTYVG  300
AISSGSLPCM ESAVLTLAQI ENSAAVQKAI THYEEQMNQK IQMPTETLQE LLDLHRLIER  360
EAIEIFLKNS FKDVDQKFQT ELGNLLISKR DAFIKKNSDV SSAHCSDLIE DIFGPLEEEV  420
KQGTFSKPGG YFLFLQMRQE LEKKYNQAPG KGLEAEAVLK KYFESKEDIV ETLLKTDQSL  480
TEAAKEIEVE RIKAETAEAA NRELAEKQEK FELMMQQKEE SYQEHVRQLT EKMKEEQKKL  540
IEEQDNIIAL KLREQEKFLR EGYENESKKL LREIENMKRR QSPGKCTIL              589
FASTA
(Canonical)
>LipidDB-10116-00476|Q63663
MASEIHMLQPMCLIENTEAHLVINQEALRILSAINQPVVVVAIVGLYRTGKSYLMNKLAG
KRTGFSLGSTVQSHTKGIWMWCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAV
LLSSTFVYNSMGTINQQAMDQLHYVTELTDLIKSKSSPDQSGIDDSANFVGFFPTFVWAL
RDFSLELEVNGKLVTPDEYLEHSLTLKKGADKKTKSFNEPRLCIRKFFPKRKCFIFDRPA
LRKQLCKLETLGEEELCSEFVEQVAEFTSYIFSYSAVKTLSGGIIVNGPRLKSLVQTYVG
AISSGSLPCMESAVLTLAQIENSAAVQKAITHYEEQMNQKIQMPTETLQELLDLHRLIER
EAIEIFLKNSFKDVDQKFQTELGNLLISKRDAFIKKNSDVSSAHCSDLIEDIFGPLEEEV
KQGTFSKPGGYFLFLQMRQELEKKYNQAPGKGLEAEAVLKKYFESKEDIVETLLKTDQSL
TEAAKEIEVERIKAETAEAANRELAEKQEKFELMMQQKEESYQEHVRQLTEKMKEEQKKL
IEEQDNIIALKLREQEKFLREGYENESKKLLREIENMKRRQSPGKCTIL
Gene Ontology
GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl
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; IEA:Ensembl
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IEA:InterPro
GO:0044406; P:adhesion of symbiont to host; IEA:Ensembl
GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl
GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl
GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl
GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl
GO:0042832; P:defense response to protozoan; IEA:Ensembl
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