Entry - *600412 - GUANYLATE-BINDING PROTEIN 2, INTERFERON-INDUCIBLE; GBP2 - OMIM
 
* 600412

GUANYLATE-BINDING PROTEIN 2, INTERFERON-INDUCIBLE; GBP2


Alternative titles; symbols

GUANYLATE-BINDING PROTEIN 1, MOUSE, HOMOLOG OF; GBP1


HGNC Approved Gene Symbol: GBP2

Cytogenetic location: 1p22.2     Genomic coordinates (GRCh38): 1:89,106,132-89,126,114 (from NCBI)


TEXT

Description

Guanylate-binding proteins, such as GBP2, are induced by interferon and hydrolyze GTP to both GDP and GMP (Vestal, 2005).


Cloning and Expression

Cheng et al. (1991) cloned cDNAs for GBP1 (600411) and GBP2.

Vestal (2005) reported that the 592-amino acid GBP2 protein shares 76% and 64% identity with GBP1 (600411) and GBP5 (611467), respectively. Like GBP1 and GBP5, GBP2 has a C-terminal CaaX isoprenylation motif.

Olszewski et al. (2006) found that GBP2 shares 76% amino acid identity with GBP3 (600413), but only 54% and 57% identity with GBP6 (612467) and GBP7 (612468), respectively. All GBPs, including GBP2, have a conserved N-terminal globular GTP-binding domain containing 2 consensus sequences and a third T(L/V)RD sequence not found in other GTPases. EST database analysis indicated wide expression of GBP2 in human tissues.


Gene Function

Using RT-PCR, Tripal et al. (2007) detected high expression of GBP1, GBP2, and GBP3 in endothelial cells after stimulation with IFNG (147570), TNF (191160), or IL1B (147720). Immunofluorescence analysis demonstrated cytoplasmic expression of GBP2. In the presence of aluminum fluoride, IFNG induced translocation of GBP2 to the Golgi apparatus.

Kim et al. (2011) examined a complete mouse 65-kD guanylate-binding protein (Gbp) gene family as part of a 43-member interferon-gamma-inducible guanosine triphosphatase superfamily in mouse and human genomes. Family-wide loss of function analysis found that at least 4 Gbps--Gbp1, Gbp6, Gbp7 (612468), and Gbp10--conferred cell-autonomous immunity to listerial or mycobacterial infection within macrophages and gene-deficient animals. These Gbps solicited host defense proteins, including the phagocyte oxidase, antimicrobial peptides, and autophagy effectors, to kill intracellular bacteria. Thus, Kim et al. (2011) concluded that specific 65-kD Gbps coordinate a potent oxidative and vesicular trafficking program to protect the host from infection.


Gene Structure

Olszewski et al. (2006) determined that, like other GBPs, the GBP2 gene contains 11 exons and begins translation in exon 2.


Mapping

By genomic sequence analysis, Olszewski et al. (2006) mapped the GBP2 gene to the GBP gene cluster on chromosome 1p22.2. It is located telomeric to GBP7 and centromeric to GBP1.


REFERENCES

  1. Cheng, Y.-S. E., Patterson, C. E., Staeheli, P. Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP. Molec. Cell. Biol. 11: 4717-4725, 1991. [PubMed: 1715024, related citations] [Full Text]

  2. Kim, B.-H., Shenoy, A. R., Kumar, P., Das, R., Tiwari, S., MacMicking, J. D. A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection. Science 332: 717-721, 2011. [PubMed: 21551061, related citations] [Full Text]

  3. Olszewski, M. A., Gray, J., Vestal, D. J. In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters. J. Interferon Cytokine Res. 26: 328-352, 2006. [PubMed: 16689661, related citations] [Full Text]

  4. Tripal, P., Bauer, M., Naschberger, E., Mortinger, T., Hohenadl, C., Cornali, E., Thurau, M., Sturzl, M. Unique features of different members of the human guanylate-binding protein family. J. Interferon Cytokine Res. 27: 44-52, 2007. [PubMed: 17266443, related citations] [Full Text]

  5. Vestal, D. J. The guanylate-binding proteins (GBPs): proinflammatory cytokine-induced members of the dynamin superfamily with unique GTPase activity. J. Interferon Cytokine Res. 25: 435-443, 2005. [PubMed: 16108726, related citations] [Full Text]


Ada Hamosh - updated : 08/16/2011
Paul J. Converse - updated : 12/11/2008
Creation Date:
Victor A. McKusick : 2/14/1995
alopez : 08/16/2011
mgross : 12/11/2008
mgross : 12/11/2008
terry : 12/11/2008
wwang : 9/26/2007
carol : 2/14/1995

* 600412

GUANYLATE-BINDING PROTEIN 2, INTERFERON-INDUCIBLE; GBP2


Alternative titles; symbols

GUANYLATE-BINDING PROTEIN 1, MOUSE, HOMOLOG OF; GBP1


HGNC Approved Gene Symbol: GBP2

Cytogenetic location: 1p22.2     Genomic coordinates (GRCh38): 1:89,106,132-89,126,114 (from NCBI)


TEXT

Description

Guanylate-binding proteins, such as GBP2, are induced by interferon and hydrolyze GTP to both GDP and GMP (Vestal, 2005).


Cloning and Expression

Cheng et al. (1991) cloned cDNAs for GBP1 (600411) and GBP2.

Vestal (2005) reported that the 592-amino acid GBP2 protein shares 76% and 64% identity with GBP1 (600411) and GBP5 (611467), respectively. Like GBP1 and GBP5, GBP2 has a C-terminal CaaX isoprenylation motif.

Olszewski et al. (2006) found that GBP2 shares 76% amino acid identity with GBP3 (600413), but only 54% and 57% identity with GBP6 (612467) and GBP7 (612468), respectively. All GBPs, including GBP2, have a conserved N-terminal globular GTP-binding domain containing 2 consensus sequences and a third T(L/V)RD sequence not found in other GTPases. EST database analysis indicated wide expression of GBP2 in human tissues.


Gene Function

Using RT-PCR, Tripal et al. (2007) detected high expression of GBP1, GBP2, and GBP3 in endothelial cells after stimulation with IFNG (147570), TNF (191160), or IL1B (147720). Immunofluorescence analysis demonstrated cytoplasmic expression of GBP2. In the presence of aluminum fluoride, IFNG induced translocation of GBP2 to the Golgi apparatus.

Kim et al. (2011) examined a complete mouse 65-kD guanylate-binding protein (Gbp) gene family as part of a 43-member interferon-gamma-inducible guanosine triphosphatase superfamily in mouse and human genomes. Family-wide loss of function analysis found that at least 4 Gbps--Gbp1, Gbp6, Gbp7 (612468), and Gbp10--conferred cell-autonomous immunity to listerial or mycobacterial infection within macrophages and gene-deficient animals. These Gbps solicited host defense proteins, including the phagocyte oxidase, antimicrobial peptides, and autophagy effectors, to kill intracellular bacteria. Thus, Kim et al. (2011) concluded that specific 65-kD Gbps coordinate a potent oxidative and vesicular trafficking program to protect the host from infection.


Gene Structure

Olszewski et al. (2006) determined that, like other GBPs, the GBP2 gene contains 11 exons and begins translation in exon 2.


Mapping

By genomic sequence analysis, Olszewski et al. (2006) mapped the GBP2 gene to the GBP gene cluster on chromosome 1p22.2. It is located telomeric to GBP7 and centromeric to GBP1.


REFERENCES

  1. Cheng, Y.-S. E., Patterson, C. E., Staeheli, P. Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP. Molec. Cell. Biol. 11: 4717-4725, 1991. [PubMed: 1715024] [Full Text: https://doi.org/10.1128/mcb.11.9.4717-4725.1991]

  2. Kim, B.-H., Shenoy, A. R., Kumar, P., Das, R., Tiwari, S., MacMicking, J. D. A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection. Science 332: 717-721, 2011. [PubMed: 21551061] [Full Text: https://doi.org/10.1126/science.1201711]

  3. Olszewski, M. A., Gray, J., Vestal, D. J. In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters. J. Interferon Cytokine Res. 26: 328-352, 2006. [PubMed: 16689661] [Full Text: https://doi.org/10.1089/jir.2006.26.328]

  4. Tripal, P., Bauer, M., Naschberger, E., Mortinger, T., Hohenadl, C., Cornali, E., Thurau, M., Sturzl, M. Unique features of different members of the human guanylate-binding protein family. J. Interferon Cytokine Res. 27: 44-52, 2007. [PubMed: 17266443] [Full Text: https://doi.org/10.1089/jir.2007.0086]

  5. Vestal, D. J. The guanylate-binding proteins (GBPs): proinflammatory cytokine-induced members of the dynamin superfamily with unique GTPase activity. J. Interferon Cytokine Res. 25: 435-443, 2005. [PubMed: 16108726] [Full Text: https://doi.org/10.1089/jir.2005.25.435]


Contributors:
Ada Hamosh - updated : 08/16/2011
Paul J. Converse - updated : 12/11/2008

Creation Date:
Victor A. McKusick : 2/14/1995

Edit History:
alopez : 08/16/2011
mgross : 12/11/2008
mgross : 12/11/2008
terry : 12/11/2008
wwang : 9/26/2007
carol : 2/14/1995