Gbp2b guanylate binding protein 2b [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Gbp2bprovided by MGI
Official Full Name: guanylate binding protein 2bprovided by MGI
Primary source: MGI:MGI:95666
See related: Ensembl:ENSMUSG00000040264 AllianceGenome:MGI:95666
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Gbp1; Mpa1; Gbp-1; LIMIT; Mag-1; Mpa-1
Summary: Enables GMP binding activity. Acts upstream of or within adhesion of symbiont to host; cellular response to interferon-beta; and defense response to other organism. Located in cytoplasmic vesicle and symbiont-containing vacuole membrane. Orthologous to human GBP2 (guanylate binding protein 2). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in large intestine adult (RPKM 1.6), bladder adult (RPKM 0.7) and 12 other tissues See more
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Genomic context

Location:: 3 H1; 3 66.69 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	3	NC_000069.7 (142300577..142324940)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	3	NC_000069.6 (142594816..142619179)

Chromosome 3 - NC_000069.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Mouse guanylate-binding protein 1 does not mediate antiviral activity against influenza virus in vitro or in vivo.
Title: Mouse guanylate-binding protein 1 does not mediate antiviral activity against influenza virus in vitro or in vivo.
GBP1 Facilitates Indoleamine 2,3-Dioxygenase Extracellular Secretion to Promote the Malignant Progression of Lung Cancer.
Title: GBP1 Facilitates Indoleamine 2,3-Dioxygenase Extracellular Secretion to Promote the Malignant Progression of Lung Cancer.
Our results represent the presently most comprehensive information about expression of Gbps in leishmaniasis in vivo. We found that expression of Gbp2b/Gbp1 and Gbp5 is under strong genetic control involving in some strains also trans-regulation both in uninfected and L. major-infected mice.
Title: Genetic Regulation of Guanylate-Binding Proteins 2b and 5 during Leishmaniasis in Mice.
These observations suggest that Gbp1 may play an important role in protecting against mitochondrial dysfunction and preserving immune function of macrophages during inflammatory stress and aging.
Title: Down-regulation of guanylate binding protein 1 causes mitochondrial dysfunction and cellular senescence in macrophages.
GBP1 GBP2 enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages.
Title: Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages.
These findings demonstrate that Gbp1 plays an important role in the IFN-gamma-dependent, cell-autonomous control of toxoplasmosis and predict a broader role for this protein in host defense.
Title: Guanylate-binding protein 1 (Gbp1) contributes to cell-autonomous immunity against Toxoplasma gondii.
ROP16, ROP18, and GRA15 are parasitic virulence factors that determine strain-specific accumulation of mGBP1 on the parasitophorous vacuole
Title: Determinants of GBP recruitment to Toxoplasma gondii vacuoles and the parasitic factors that control it.
findings show that at least 4 IFN-gamma-inducible Gbps--Gbp1, Gbp6, Gbp7, and Gbp10--conferred cell-autonomous immunity to listerial or mycobacterial infection within macrophages and gene-deficient animals
Title: A family of IFN-γ-inducible 65-kD GTPases protects against bacterial infection.
These findings identify a role for IFN-alphaA-mediated GBP-1 expression in the prevention of intestinal epithelial apoptosis by commensal bacteria.
Title: Commensal Escherichia coli reduces epithelial apoptosis through IFN-alphaA-mediated induction of guanylate binding protein-1 in human and murine models of developing intestine.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (1) 1 citation
Endonuclease-mediated (4) 1 citation

General gene information

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Markers

M63961 (e-PCR)
- UniSTS:124971

Gbp1 (e-PCR), detects polymorphism
- UniSTS:143181

Gbp1 (e-PCR), detects polymorphism
- UniSTS:527356

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables G protein activity	ISO Inferred from Sequence Orthology more info
enables GDP binding	ISO Inferred from Sequence Orthology more info
enables GDP phosphatase activity	ISO Inferred from Sequence Orthology more info
enables GMP binding	IDA Inferred from Direct Assay more info	PubMed
enables GTP binding	IBA Inferred from Biological aspect of Ancestor more info
enables GTP binding	ISO Inferred from Sequence Orthology more info
enables GTPase activity	IBA Inferred from Biological aspect of Ancestor more info
enables GTPase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables GTPase activity	ISO Inferred from Sequence Orthology more info
enables Hsp90 protein binding	ISO Inferred from Sequence Orthology more info
enables actin binding	ISO Inferred from Sequence Orthology more info
enables cytokine binding	ISO Inferred from Sequence Orthology more info
enables endopeptidase inhibitor activity	ISO Inferred from Sequence Orthology more info
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables lipopolysaccharide binding	ISO Inferred from Sequence Orthology more info
enables molecular function inhibitor activity	ISO Inferred from Sequence Orthology more info
enables nucleotide binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables spectrin binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in activation of innate immune response	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within adhesion of symbiont to host	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within cellular response to interferon-beta	IDA Inferred from Direct Assay more info	PubMed
involved_in cellular response to lipopolysaccharide	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to type II interferon	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within cellular response to type II interferon	IDA Inferred from Direct Assay more info	PubMed
involved_in cytolysis in another organism	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in defense response to Gram-positive bacterium	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within defense response to Gram-positive bacterium	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within defense response to Gram-positive bacterium	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in defense response to bacterium	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in defense response to protozoan	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within defense response to protozoan	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within defense response to virus	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within immune system process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within innate immune response	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of pyroptosis	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in Golgi apparatus	ISO Inferred from Sequence Orthology more info
located_in Golgi apparatus	ISO Inferred from Sequence Orthology more info
is_active_in Golgi membrane	ISO Inferred from Sequence Orthology more info
located_in actin cytoskeleton	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
is_active_in cytoplasmic vesicle	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasmic vesicle	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasmic vesicle	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in perinuclear region of cytoplasm	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
is_active_in symbiont cell surface	ISO Inferred from Sequence Orthology more info
located_in symbiont-containing vacuole membrane	IDA Inferred from Direct Assay more info	PubMed
is_active_in vesicle membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: guanylate-binding protein 1

Names: GTP-binding protein 1; guanylate nucleotide binding protein 1; interferon-gamma-inducible protein MAG-1; interferon-induced guanylate-binding protein 1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_010259.2 → NP_034389.2 guanylate-binding protein 1

See identical proteins and their annotated locations for NP_034389.2

Status: VALIDATED

Source sequence(s)

AC102108, AK077796

Consensus CDS

CCDS38658.1

UniProtKB/Swiss-Prot

Q01514, Q32MT4

UniProtKB/TrEMBL

A4UUI2

Related

ENSMUSP00000029936.5, ENSMUST00000029936.5

Conserved Domains (2) summary

pfam02263
Location:19 → 280

GBP; Guanylate-binding protein, N-terminal domain

pfam02841
Location:282 → 578

GBP_C; Guanylate-binding protein, C-terminal domain

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000069.7 Reference GRCm39 C57BL/6J

Range

142300577..142324940

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_011240014.1 → XP_011238316.1 guanylate-binding protein 1 isoform X2

UniProtKB/Swiss-Prot

Q01514, Q32MT4

Conserved Domains (2) summary

pfam02263
Location:19 → 280

GBP; Guanylate-binding protein, N-terminal domain

pfam02841
Location:282 → 553

GBP_C; Guanylate-binding protein, C-terminal domain
XM_030252421.2 → XP_030108281.1 guanylate-binding protein 1 isoform X1

UniProtKB/Swiss-Prot

Q01514, Q32MT4

UniProtKB/TrEMBL

A4UUI2

Conserved Domains (2) summary

pfam02263
Location:19 → 280

GBP; Guanylate-binding protein, N-terminal domain

pfam02841
Location:282 → 578

GBP_C; Guanylate-binding protein, C-terminal domain