CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024048
UniProt Accession
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
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
232RKFFPKRKCFIFDRPubiquitination[1]
372VFLKNSFKDVDQKFQacetylation[2]
389LGNLLVAKRDAFIKKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
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
 NP_BIND 45 52 GTP (By similarity).
 NP_BIND 67 69 GTP (By similarity).
 NP_BIND 97 101 GTP (By similarity).
 REGION 1 309 GTPase domain (Globular) (By similarity).
 MOD_RES 586 586 Cysteine methyl ester (Potential).
 LIPID 586 586 S-geranylgeranyl cysteine.  
Keyword
 Complete proteome; Cytoplasm; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Nucleus; Prenylation; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 589 AA 
Protein Sequence
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 
Gene Ontology
 GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 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:0051856; P:adhesion to symbiont; 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. 
Interpro
 IPR003191; Guanylate-bd_C.
 IPR015894; Guanylate-bd_N.
 IPR027417; P-loop_NTPase. 
Pfam
 PF02263; GBP
 PF02841; GBP_C 
SMART
  
PROSITE
  
PRINTS