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P32455 (GBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-induced guanylate-binding protein 1
Alternative name(s):
GTP-binding protein 1
Short name=GBP-1
Short name=HuGBP-1
Guanine nucleotide-binding protein 1
Gene names
Name:GBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Subunit structure

Homodimerizes upon GTP-binding, dimerization is required for the second hydrolysis step from GDP to GMP. Can also heterodimerize with other members of the family. Ref.12 Ref.16

Subcellular location

Cytoplasm. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Secreted. Note: Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of interferon-gamma induction. Golgi membrane localization requires isoprenylation and the presence of another IFN-gamma-induced factor. Ref.8 Ref.9 Ref.10 Ref.12

Induction

By IFNG/IFN-gamma during macrophage activation, and by TNF-alpha and IL-1beta. Ref.10

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3-type GTPase family. GB1 subfamily.

Contains 1 GB1/RHD3-type G (guanine nucleotide-binding) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself7EBI-2869161,EBI-2869161

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 589589Interferon-induced guanylate-binding protein 1
PRO_0000190963
Propeptide590 – 5923Removed in mature form
PRO_0000396777

Regions

Domain35 – 278244GB1/RHD3-type G
Nucleotide binding45 – 528GTP
Nucleotide binding67 – 693GTP
Nucleotide binding97 – 1015GTP
Region1 – 311311GTPase domain (Globular)

Amino acid modifications

Modified residue5891Cysteine methyl ester By similarity
Lipidation5891S-farnesyl cysteine Ref.7

Natural variations

Natural variant781I → V.
Corresponds to variant rs1048401 [ dbSNP | Ensembl ].
VAR_033950
Natural variant1661E → D.
Corresponds to variant rs17130717 [ dbSNP | Ensembl ].
VAR_033951
Natural variant3491T → S. Ref.1 Ref.2 Ref.6
Corresponds to variant rs1048425 [ dbSNP | Ensembl ].
VAR_014849
Natural variant4091A → G. Ref.1 Ref.2 Ref.6
Corresponds to variant rs1048443 [ dbSNP | Ensembl ].
VAR_046550

Secondary structure

................................................................................ 592
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32455 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: 3A06741218360732

FASTA59267,931
        10         20         30         40         50         60 
MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG KSYLMNKLAG 

        70         80         90        100        110        120 
KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG LGDVEKGDNQ NDSWIFALAV 

       130        140        150        160        170        180 
LLSSTFVYNS IGTINQQAMD QLYYVTELTH RIRSKSSPDE NENEVEDSAD FVSFFPDFVW 

       190        200        210        220        230        240 
TLRDFSLDLE ADGQPLTPDE YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR 

       250        260        270        280        290        300 
PVHRRKLAQL EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY 

       310        320        330        340        350        360 
VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTETL QELLDLHRDS 

       370        380        390        400        410        420 
EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ EASSDRCSAL LQVIFSPLEE 

       430        440        450        460        470        480 
EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE PRKGIQAEEI LQTYLKSKES MTDAILQTDQ 

       490        500        510        520        530        540 
TLTEKEKEIE VERVKAESAQ ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV 

       550        560        570        580        590 
QLLKEQERTL ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKACT IS 

« Hide

References

« Hide 'large scale' references
[1]"Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP."
Cheng Y.-S.E., Patterson C.E., Staeheli P.
Mol. Cell. Biol. 11:4717-4725(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-349 AND GLY-409.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-349 AND GLY-409.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-349 AND GLY-409.
Tissue: Uterus.
[7]"Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1."
Nantais D.E., Schwemmle M., Stickney J.T., Vestal D.J., Buss J.E.
J. Leukoc. Biol. 60:423-431(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-589.
[8]"Golgi targeting of human guanylate-binding protein-1 requires nucleotide binding, isoprenylation, and an IFN-gamma-inducible cofactor."
Modiano N., Lu Y.E., Cresswell P.
Proc. Natl. Acad. Sci. U.S.A. 102:8680-8685(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Human guanylate binding protein-1 is a secreted GTPase present in increased concentrations in the cerebrospinal fluid of patients with bacterial meningitis."
Naschberger E., Lubeseder-Martellato C., Meyer N., Gessner R., Kremmer E., Gessner A., Sturzl M.
Am. J. Pathol. 169:1088-1099(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Unique features of different members of the human guanylate-binding protein family."
Tripal P., Bauer M., Naschberger E., Mortinger T., Hohenadl C., Cornali E., Thurau M., Sturzl M.
J. Interferon Cytokine Res. 27:44-52(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner."
Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A., Reipschlager S., Naschberger E., Herrmann C., Sturzl M.
PLoS ONE 5:E14246-E14246(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[13]"A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication."
Nordmann A., Wixler L., Boergeling Y., Wixler V., Ludwig S.
FASEB J. 26:1290-1300(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins."
Prakash B., Praefcke G.J.K., Renault L., Wittinghofer A., Herrmann C.
Nature 403:567-571(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[15]"Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism."
Prakash B., Renault L., Praefcke G.J., Herrmann C., Wittinghofer A.
EMBO J. 19:4555-4564(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GTP ANALOG.
[16]"How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP."
Ghosh A., Praefcke G.J., Renault L., Wittinghofer A., Herrmann C.
Nature 440:101-104(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-317, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55542 mRNA. Translation: AAA35871.1.
BT006847 mRNA. Translation: AAP35493.1.
AK291783 mRNA. Translation: BAF84472.1.
AL160008 Genomic DNA. Translation: CAI22972.1.
CH471097 Genomic DNA. Translation: EAW73148.1.
CH471097 Genomic DNA. Translation: EAW73150.1.
BC002666 mRNA. Translation: AAH02666.1.
CCDSCCDS718.1.
PIRA41268.
RefSeqNP_002044.2. NM_002053.2.
UniGeneHs.62661.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DG3X-ray1.80A1-592[»]
1F5NX-ray1.70A1-592[»]
2B8WX-ray2.22A/B1-317[»]
2B92X-ray3.20A/B1-317[»]
2BC9X-ray2.80A1-317[»]
2D4HX-ray2.90A/B1-317[»]
DisProtDP00313.
ProteinModelPortalP32455.
SMRP32455. Positions 7-583.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108903. 10 interactions.
DIPDIP-60423N.
IntActP32455. 1 interaction.
MINTMINT-4718320.
STRING9606.ENSP00000359504.

PTM databases

PhosphoSiteP32455.

Polymorphism databases

DMDM311033383.

Proteomic databases

MaxQBP32455.
PaxDbP32455.
PRIDEP32455.

Protocols and materials databases

DNASU2633.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370473; ENSP00000359504; ENSG00000117228.
GeneID2633.
KEGGhsa:2633.
UCSCuc001dmx.2. human.

Organism-specific databases

CTD2633.
GeneCardsGC01M089517.
H-InvDBHIX0018119.
HIX0200036.
HGNCHGNC:4182. GBP1.
HPACAB015450.
MIM600411. gene.
neXtProtNX_P32455.
PharmGKBPA28596.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288755.
HOGENOMHOG000266974.
HOVERGENHBG001979.
InParanoidP32455.
OMAGFQKESR.
OrthoDBEOG7BW0J3.
PhylomeDBP32455.
TreeFamTF331602.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeP32455.
CleanExHS_GBP1.
GenevestigatorP32455.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF02263. GBP. 1 hit.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32455.
GeneWikiGBP1.
GenomeRNAi2633.
NextBio10380.
PROP32455.
SOURCESearch...

Entry information

Entry nameGBP1_HUMAN
AccessionPrimary (citable) accession number: P32455
Secondary accession number(s): D3DT26, Q5T8M1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM