HUMAN:GBP1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	GBP1
Protein Name(s)	Interferon-induced guanylate-binding protein 1 GTP-binding protein 1 GBP-1 HuGBP-1 Guanine nucleotide-binding protein 1
External Links
UniProt	P32455
EMBL	M55542 BT006847 AK291783 AL160008 CH471097 CH471097 BC002666
CCDS	CCDS718.1
PIR	A41268
RefSeq	NP_002044.2
UniGene	Hs.62661
PDB	1DG3 1F5N 2B8W 2B92 2BC9 2D4H
PDBsum	1DG3 1F5N 2B8W 2B92 2BC9 2D4H
DisProt	DP00313
ProteinModelPortal	P32455
SMR	P32455
BioGrid	108903
DIP	DIP-60423N
IntAct	P32455
MINT	MINT-4718320
STRING	9606.ENSP00000359504
PhosphoSite	P32455
DMDM	311033383
MaxQB	P32455
PaxDb	P32455
PRIDE	P32455
DNASU	2633
Ensembl	ENST00000370473
GeneID	2633
KEGG	hsa:2633
UCSC	uc001dmx.2
CTD	2633
GeneCards	GC01M089517
H-InvDB	HIX0018119 HIX0200036
HGNC	HGNC:4182
HPA	CAB015450
MIM	600411
neXtProt	NX_P32455
PharmGKB	PA28596
eggNOG	NOG288755
GeneTree	ENSGT00550000074475
HOGENOM	HOG000266974
HOVERGEN	HBG001979
InParanoid	P32455
OMA	GFQKESR
OrthoDB	EOG7BW0J3
PhylomeDB	P32455
TreeFam	TF331602
Reactome	REACT_25078
ChiTaRS	GBP1
EvolutionaryTrace	P32455
GeneWiki	GBP1
GenomeRNAi	2633
NextBio	10380
PRO	PR:P32455
Proteomes	UP000005640
Bgee	P32455
CleanEx	HS_GBP1
Genevestigator	P32455
GO	GO:0005829 GO:0005576 GO:0000139 GO:0005525 GO:0003924 GO:0042802 GO:0019221 GO:0051607 GO:0060333
Gene3D	3.40.50.300
InterPro	IPR030386 IPR003191 IPR015894 IPR027417
Pfam	PF02263 PF02841
SUPFAM	SSF48340 SSF52540
PROSITE	PS51715

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005923	tight junction	PMID:19079332^[1]	ECO:0000314			C		Figure 2B. An IF was done in human epithelial cells. GBP1 was detected in the tight junctions colocalizing with CAR.	complete
enables	GO:0042803	protein homodimerization activity	PMID:21151871^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0012506	vesicle membrane	PMID:21151871^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21151871^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071356	cellular response to tumor necrosis factor	PMID:17266443^[3]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071347	cellular response to interleukin-1	PMID:17266443^[3]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071346	cellular response to interferon-gamma	PMID:17266443^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:17266443^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0071346)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17266443^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071346	cellular response to interferon-gamma	PMID:21151871^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:21151871^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0072665	protein localization to vacuole	PMID:21151871^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:10676968^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:10676968^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019003	GDP binding	PMID:10676968^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:10676968^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:10676968^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050860	negative regulation of T cell receptor signaling pathway	PMID:24337748^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P06239) has_regulation_target:(UniProtKB:O43561)	Seeded From UniProt	complete
involved_in	GO:0050848	regulation of calcium-mediated signaling	PMID:24337748^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0050860)	Seeded From UniProt	complete
involved_in	GO:0070373	negative regulation of ERK1 and ERK2 cascade	PMID:24337748^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0050860)	Seeded From UniProt	complete
involved_in	GO:1903076	regulation of protein localization to plasma membrane	PMID:24337748^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q01082	P	has_regulation_target:(UniProtKB:P08575) occurs_in:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:1903077	negative regulation of protein localization to plasma membrane	PMID:24337748^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P08575) occurs_in:(CL:0000084)	Seeded From UniProt	complete
involved_in	GO:1900025	negative regulation of substrate adhesion-dependent cell spreading	PMID:24337748^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000084)	Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:24337748^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051879	Hsp90 protein binding	PMID:24337748^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07900	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:24337748^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07814	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:24337748^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06733	F		Seeded From UniProt	complete
enables	GO:0030507	spectrin binding	PMID:24337748^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q01082	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:24337748^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P41252	F		Seeded From UniProt	complete
enables	GO:0019955	cytokine binding	PMID:24337748^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q12904	F		Seeded From UniProt	complete
involved_in	GO:1900041	negative regulation of interleukin-2 secretion	PMID:24337748^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000542)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:24337748^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000084)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22607347^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P32455	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22059445^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P32455	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16511497^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P32455	F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003191 InterPro:IPR015894 InterPro:IPR036543 InterPro:IPR037684	F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003191 InterPro:IPR015894 InterPro:IPR030386 InterPro:IPR036543	F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:1715024^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0060333	interferon-gamma-mediated signaling pathway	Reactome:R-HSA-877300	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-1031716	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0051	P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333	C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F		Seeded From UniProt	complete
part_of	GO:0000139	Golgi membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0134	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Schnoor, M et al. (2009) Guanylate-binding protein-1 is expressed at tight junctions of intestinal epithelial cells in response to interferon-gamma and regulates barrier function through effects on apoptosis. Mucosal Immunol 2 33-42 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Britzen-Laurent, N et al. (2010) Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner. PLoS ONE 5 e14246 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Tripal, P et al. (2007) Unique features of different members of the human guanylate-binding protein family. J. Interferon Cytokine Res. 27 44-52 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Prakash, B et al. (2000) Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature 403 567-71 PubMed GONUTS page
↑ ^5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 ^5.12 ^5.13 ^5.14 Forster, F et al. (2014) Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton. J. Immunol. 192 771-81 PubMed GONUTS page
↑ Syguda, A et al. (2012) Tetramerization of human guanylate-binding protein 1 is mediated by coiled-coil formation of the C-terminal α-helices. FEBS J. 279 2544-54 PubMed GONUTS page
↑ Wehner, M et al. (2012) The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis. FEBS J. 279 203-10 PubMed GONUTS page
↑ Ghosh, A et al. (2006) How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP. Nature 440 101-4 PubMed GONUTS page
↑ Cheng, YS et al. (1991) Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP. Mol. Cell. Biol. 11 4717-25 PubMed GONUTS page

[PMID:19079332-1] Schnoor, M et al. (2009) Guanylate-binding protein-1 is expressed at tight junctions of intestinal epithelial cells in response to interferon-gamma and regulates barrier function through effects on apoptosis. Mucosal Immunol 2 33-42 PubMed GONUTS page

[PMID:21151871-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Britzen-Laurent, N et al. (2010) Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner. PLoS ONE 5 e14246 PubMed GONUTS page

[PMID:17266443-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Tripal, P et al. (2007) Unique features of different members of the human guanylate-binding protein family. J. Interferon Cytokine Res. 27 44-52 PubMed GONUTS page

[PMID:10676968-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 Prakash, B et al. (2000) Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature 403 567-71 PubMed GONUTS page

[PMID:24337748-5] 5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 ^5.12 ^5.13 ^5.14 Forster, F et al. (2014) Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton. J. Immunol. 192 771-81 PubMed GONUTS page

[PMID:22607347-6] Syguda, A et al. (2012) Tetramerization of human guanylate-binding protein 1 is mediated by coiled-coil formation of the C-terminal α-helices. FEBS J. 279 2544-54 PubMed GONUTS page

[PMID:22059445-7] Wehner, M et al. (2012) The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis. FEBS J. 279 203-10 PubMed GONUTS page

[PMID:16511497-8] Ghosh, A et al. (2006) How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP. Nature 440 101-4 PubMed GONUTS page

[PMID:1715024-9] Cheng, YS et al. (1991) Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP. Mol. Cell. Biol. 11 4717-25 PubMed GONUTS page

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HUMAN:GBP1

Contents

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References

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