Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01414
Entry Name
UniProt Accession
Theoretical PI
5.54
Molecular Weight
67209.02
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Interferon-induced guanylate-binding protein 2
Protein Synonyms/Alias
GTP-binding protein 2; GBP-2; HuGBP-2; Guanine nucleotide-binding protein 2;
Gene Name
GBP2
Gene Synonyms/Alias
Created Date
01-OCT-1993
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
588
Canonical
SKSLEPICNIL****
[1]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Britzen-Laurent N, Bauer M, Berton V, Fischer N, Syguda A, Reipschläger S,Naschberger E, Herrmann C, Stürzl M. Intracellular trafficking ofguanylate-binding proteins is regulated by heterodimerization in a hierarchicalmanner. PLoS One. 2010 Dec 7;5(12):e14246. doi: 10.1371/journal.pone.0014246.[PMID:21151871]
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: 588 588 Cysteine methyl ester.
Protein Length
591 AA.
Protein Sequence
(Canonical)
MAPEINLPGP MSLIDNTKGQ LVVNPEALKI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG  60
KKNGFSLGST VKSHTKGIWM WCVPHPKKPE HTLVLLDTEG LGDIEKGDNE NDSWIFALAI  120
LLSSTFVYNS MGTINQQAMD QLHYVTELTD RIKANSSPGN NSVDDSADFV SFFPAFVWTL  180
RDFTLELEVD GEPITADDYL ELSLKLRKGT DKKSKSFNDP RLCIRKFFPK RKCFVFDWPA  240
PKKYLAHLEQ LKEEELNPDF IEQVAEFCSY ILSHSNVKTL SGGIPVNGPR LESLVLTYVN  300
AISSGDLPCM ENAVLALAQI ENSAAVEKAI AHYEQQMGQK VQLPTETLQE LLDLHRDSER  360
EAIEVFMKNS FKDVDQMFQR KLGAQLEARR DDFCKQNSKA SSDCCMALLQ DIFGPLEEDV  420
KQGTFSKPGG YRLFTQKLQE LKNKYYQVPR KGIQAKEVLK KYLESKEDVA DALLQTDQSL  480
SEKEKAIEVE RIKAESAEAA KKMLEEIQKK NEEMMEQKEK SYQEHVKQLT EKMERDRAQL  540
MAEQEKTLAL KLQEQERLLK EGFENESKRL QKDIWDIQMR SKSLEPICNI L           591
FASTA
(Canonical)
>LipidDB-9606-01414|P32456
MAPEINLPGPMSLIDNTKGQLVVNPEALKILSAITQPVVVVAIVGLYRTGKSYLMNKLAG
KKNGFSLGSTVKSHTKGIWMWCVPHPKKPEHTLVLLDTEGLGDIEKGDNENDSWIFALAI
LLSSTFVYNSMGTINQQAMDQLHYVTELTDRIKANSSPGNNSVDDSADFVSFFPAFVWTL
RDFTLELEVDGEPITADDYLELSLKLRKGTDKKSKSFNDPRLCIRKFFPKRKCFVFDWPA
PKKYLAHLEQLKEEELNPDFIEQVAEFCSYILSHSNVKTLSGGIPVNGPRLESLVLTYVN
AISSGDLPCMENAVLALAQIENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSER
EAIEVFMKNSFKDVDQMFQRKLGAQLEARRDDFCKQNSKASSDCCMALLQDIFGPLEEDV
KQGTFSKPGGYRLFTQKLQELKNKYYQVPRKGIQAKEVLKKYLESKEDVADALLQTDQSL
SEKEKAIEVERIKAESAEAAKKMLEEIQKKNEEMMEQKEKSYQEHVKQLTEKMERDRAQL
MAEQEKTLALKLQEQERLLKEGFENESKRLQKDIWDIQMRSKSLEPICNIL
Gene Ontology
GO:0005829; C:cytosol; TAS:Reactome
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005525; F:GTP binding; TAS:ProtInc
GO:0003924; F:GTPase activity; IEA:InterPro
GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome
GO:0006955; P:immune response; TAS:ProtInc
GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome
GO:0060337; P:type I interferon 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