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Protein

Guanylate-binding protein 3

Gene

GBP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits antiviral activity against influenza virus.1 Publication

Catalytic activityi

GTP + H2O = GDP + phosphate.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 528GTPBy similarity
Nucleotide bindingi67 – 693GTPBy similarity
Nucleotide bindingi97 – 1015GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-877300. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate-binding protein 3 (EC:3.6.5.-By similarity)
Alternative name(s):
GTP-binding protein 3
Short name:
GBP-3
Guanine nucleotide-binding protein 3
Gene namesi
Name:GBP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4184. GBP3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28598.

Polymorphism and mutation databases

BioMutaiGBP3.
DMDMi221222526.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595Guanylate-binding protein 3PRO_0000261159Add
BLAST

Proteomic databases

EPDiQ9H0R5.
MaxQBiQ9H0R5.
PaxDbiQ9H0R5.
PRIDEiQ9H0R5.

PTM databases

iPTMnetiQ9H0R5.
PhosphoSiteiQ9H0R5.

Expressioni

Gene expression databases

BgeeiQ9H0R5.
ExpressionAtlasiQ9H0R5. baseline and differential.
GenevisibleiQ9H0R5. HS.

Organism-specific databases

HPAiHPA045657.

Interactioni

Subunit structurei

Heterodimer with other family members, including GBP1, GBP2 and GBP5 (PubMed:21151871). Dimerization regulates subcellular location.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAP4K4O958194EBI-2798916,EBI-2511133

Protein-protein interaction databases

BioGridi108905. 3 interactions.
IntActiQ9H0R5. 2 interactions.
MINTiMINT-4716557.
STRINGi9606.ENSP00000359512.

Structurei

3D structure databases

ProteinModelPortaliQ9H0R5.
SMRiQ9H0R5. Positions 5-581.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 276242GB1/RHD3-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 309309GTPase domain (Globular)By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili482 – 595114Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00550000074475.
HOVERGENiHBG001979.
InParanoidiQ9H0R5.
OMAiDEYLDNS.
OrthoDBiEOG7BW0J3.
PhylomeDBiQ9H0R5.
TreeFamiTF331602.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030386. G_GB1_RHD3_dom.
IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H0R5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPEIHMTGP MCLIENTNGE LVANPEALKI LSAITQPVVV VAIVGLYRTG
60 70 80 90 100
KSYLMNKLAG KNKGFSLGST VKSHTKGIWM WCVPHPKKPE HTLVLLDTEG
110 120 130 140 150
LGDVKKGDNQ NDSWIFTLAV LLSSTLVYNS MGTINQQAMD QLYYVTELTH
160 170 180 190 200
RIRSKSSPDE NENEDSADFV SFFPDFVWTL RDFSLDLEAD GQPLTPDEYL
210 220 230 240 250
EYSLKLTQGT SQKDKNFNLP RLCIRKFFPK KKCFVFDLPI HRRKLAQLEK
260 270 280 290 300
LQDEELDPEF VQQVADFCSY IFSNSKTKTL SGGIKVNGPR LESLVLTYIN
310 320 330 340 350
AISRGDLPCM ENAVLALAQI ENSAAVQKAI AHYDQQMGQK VQLPAETLQE
360 370 380 390 400
LLDLHRVSER EATEVYMKNS FKDVDHLFQK KLAAQLDKKR DDFCKQNQEA
410 420 430 440 450
SSDRCSALLQ VIFSPLEEEV KAGIYSKPGG YCLFIQKLQD LEKKYYEEPR
460 470 480 490 500
KGIQAEEILQ TYLKSKESVT DAILQTDQIL TEKEKEIEVE CVKAESAQAS
510 520 530 540 550
AKMVEEMQIK YQQMMEEKEK SYQEHVKQLT EKMERERAQL LEEQEKTLTS
560 570 580 590
KLQEQARVLK ERCQGESTQL QNEIQKLQKT LKKKTKRYMS HKLKI
Length:595
Mass (Da):68,114
Last modified:January 20, 2009 - v3
Checksum:i410A9BED9ABD2DDF
GO
Isoform 2 (identifier: Q9H0R5-4) [UniParc]FASTAAdd to basket

Also known as: GBP-3DeltaC

The sequence of this isoform differs from the canonical sequence as follows:
     357-383: Missing.
     554-595: EQARVLKERCQGESTQLQNEIQKLQKTLKKKTKRYMSHKLKI → VSKCITLWFVFLFSLCSS

Note: Shows the most prominent antiviral activity in epithelial cells.
Show »
Length:544
Mass (Da):61,928
Checksum:iA5CA2D8AD3440548
GO

Sequence cautioni

The sequence AAH17992.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence CAB66615.1 differs from that shown.Unlikely isoform. Aberrant splice sites.Curated
The sequence CAI21697.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI22970.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW73151.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711I → T in AAH17992 (PubMed:15489334).Curated
Sequence conflicti290 – 2901R → C in CAB66615 (PubMed:22106366).Curated
Sequence conflicti290 – 2901R → C in AAI40838 (Ref. 4) Curated
Sequence conflicti334 – 3341D → G in AAH17992 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211R → Q.1 Publication
Corresponds to variant rs4656078 [ dbSNP | Ensembl ].
VAR_054136
Natural varianti225 – 2251R → W.2 Publications
Corresponds to variant rs4656077 [ dbSNP | Ensembl ].
VAR_054137
Natural varianti347 – 3471T → S.
Corresponds to variant rs3188433 [ dbSNP | Ensembl ].
VAR_054138
Natural varianti469 – 4691V → M.
Corresponds to variant rs10493821 [ dbSNP | Ensembl ].
VAR_029082
Natural varianti491 – 4911C → R.
Corresponds to variant rs17433780 [ dbSNP | Ensembl ].
VAR_029083
Natural varianti558 – 5581V → A.
Corresponds to variant rs11808228 [ dbSNP | Ensembl ].
VAR_029084

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei357 – 38327Missing in isoform 2. 1 PublicationVSP_044360Add
BLAST
Alternative sequencei554 – 59542EQARV…HKLKI → VSKCITLWFVFLFSLCSS in isoform 2. 1 PublicationVSP_044361Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JF927951 mRNA. Translation: AEI54565.1.
AL136680 mRNA. Translation: CAB66615.1. Sequence problems.
AL139416, AL160008 Genomic DNA. Translation: CAI21697.1. Sequence problems.
AL160008, AL139416 Genomic DNA. Translation: CAI22970.1. Sequence problems.
AL139416, AL160008 Genomic DNA. Translation: CAM28262.1.
AL160008, AL139416 Genomic DNA. Translation: CAM28327.1.
CH471097 Genomic DNA. Translation: EAW73151.1. Sequence problems.
BC017992 mRNA. Translation: AAH17992.1. Sequence problems.
BC140837 mRNA. Translation: AAI40838.1.
CCDSiCCDS717.2. [Q9H0R5-1]
RefSeqiNP_001306110.1. NM_001319181.1. [Q9H0R5-4]
NP_060754.2. NM_018284.2. [Q9H0R5-1]
UniGeneiHs.720167.

Genome annotation databases

EnsembliENST00000370481; ENSP00000359512; ENSG00000117226. [Q9H0R5-1]
GeneIDi2635.
KEGGihsa:2635.
UCSCiuc001dmt.4. human. [Q9H0R5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JF927951 mRNA. Translation: AEI54565.1.
AL136680 mRNA. Translation: CAB66615.1. Sequence problems.
AL139416, AL160008 Genomic DNA. Translation: CAI21697.1. Sequence problems.
AL160008, AL139416 Genomic DNA. Translation: CAI22970.1. Sequence problems.
AL139416, AL160008 Genomic DNA. Translation: CAM28262.1.
AL160008, AL139416 Genomic DNA. Translation: CAM28327.1.
CH471097 Genomic DNA. Translation: EAW73151.1. Sequence problems.
BC017992 mRNA. Translation: AAH17992.1. Sequence problems.
BC140837 mRNA. Translation: AAI40838.1.
CCDSiCCDS717.2. [Q9H0R5-1]
RefSeqiNP_001306110.1. NM_001319181.1. [Q9H0R5-4]
NP_060754.2. NM_018284.2. [Q9H0R5-1]
UniGeneiHs.720167.

3D structure databases

ProteinModelPortaliQ9H0R5.
SMRiQ9H0R5. Positions 5-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108905. 3 interactions.
IntActiQ9H0R5. 2 interactions.
MINTiMINT-4716557.
STRINGi9606.ENSP00000359512.

PTM databases

iPTMnetiQ9H0R5.
PhosphoSiteiQ9H0R5.

Polymorphism and mutation databases

BioMutaiGBP3.
DMDMi221222526.

Proteomic databases

EPDiQ9H0R5.
MaxQBiQ9H0R5.
PaxDbiQ9H0R5.
PRIDEiQ9H0R5.

Protocols and materials databases

DNASUi2635.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370481; ENSP00000359512; ENSG00000117226. [Q9H0R5-1]
GeneIDi2635.
KEGGihsa:2635.
UCSCiuc001dmt.4. human. [Q9H0R5-1]

Organism-specific databases

CTDi2635.
GeneCardsiGBP3.
HGNCiHGNC:4184. GBP3.
HPAiHPA045657.
MIMi600413. gene.
neXtProtiNX_Q9H0R5.
PharmGKBiPA28598.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00550000074475.
HOVERGENiHBG001979.
InParanoidiQ9H0R5.
OMAiDEYLDNS.
OrthoDBiEOG7BW0J3.
PhylomeDBiQ9H0R5.
TreeFamiTF331602.

Enzyme and pathway databases

ReactomeiR-HSA-877300. Interferon gamma signaling.

Miscellaneous databases

ChiTaRSiGBP3. human.
GenomeRNAii2635.
NextBioi10388.
PROiQ9H0R5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H0R5.
ExpressionAtlasiQ9H0R5. baseline and differential.
GenevisibleiQ9H0R5. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030386. G_GB1_RHD3_dom.
IPR003191. Guanylate-bd_C.
IPR015894. Guanylate-bd_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF02263. GBP. 1 hit.
PF02841. GBP_C. 1 hit.
[Graphical view]
SUPFAMiSSF48340. SSF48340. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51715. G_GB1_RHD3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, VARIANT TRP-225, ALTERNATIVE SPLICING.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "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.
    , 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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), VARIANTS GLN-221 AND TRP-225.
    Tissue: Prostate.
  6. "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.
  7. "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, DIMERIZATION.

Entry informationi

Entry nameiGBP3_HUMAN
AccessioniPrimary (citable) accession number: Q9H0R5
Secondary accession number(s): A2A317
, A6NF86, B2RTW0, F8UW81, Q05D54, Q5T8L8, Q5T8L9, Q6P3V3, Q9NV33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: January 20, 2009
Last modified: May 11, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.