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P32455

- GBP1_HUMAN

UniProt

P32455 - GBP1_HUMAN

Protein

Interferon-induced guanylate-binding protein 1

Gene

GBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Regions

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

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: ProtInc
    3. identical protein binding Source: IntAct

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. defense response to virus Source: UniProtKB-KW
    3. interferon-gamma-mediated signaling pathway Source: Reactome

    Keywords - Biological processi

    Antiviral defense, Immunity

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_25078. Interferon gamma signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:GBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4182. GBP1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular region Source: UniProtKB-SubCell
    3. Golgi membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28596.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 589589Interferon-induced guanylate-binding protein 1PRO_0000190963Add
    BLAST
    Propeptidei590 – 5923Removed in mature formPRO_0000396777

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei589 – 5891Cysteine methyl esterBy similarity
    Lipidationi589 – 5891S-farnesyl cysteine1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP32455.
    PaxDbiP32455.
    PRIDEiP32455.

    PTM databases

    PhosphoSiteiP32455.

    Expressioni

    Inductioni

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

    Gene expression databases

    BgeeiP32455.
    CleanExiHS_GBP1.
    GenevestigatoriP32455.

    Organism-specific databases

    HPAiCAB015450.

    Interactioni

    Subunit structurei

    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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-2869161,EBI-2869161

    Protein-protein interaction databases

    BioGridi108903. 11 interactions.
    DIPiDIP-60423N.
    IntActiP32455. 1 interaction.
    MINTiMINT-4718320.
    STRINGi9606.ENSP00000359504.

    Structurei

    Secondary structure

    1
    592
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 177
    Beta strandi20 – 234
    Helixi25 – 328
    Beta strandi36 – 4611
    Helixi47 – 493
    Helixi51 – 588
    Beta strandi62 – 654
    Beta strandi70 – 723
    Beta strandi77 – 848
    Beta strandi86 – 883
    Beta strandi92 – 987
    Turni101 – 1033
    Helixi104 – 1063
    Helixi112 – 12211
    Beta strandi124 – 1329
    Helixi136 – 1405
    Helixi143 – 1464
    Helixi148 – 1514
    Beta strandi156 – 1583
    Helixi167 – 1704
    Helixi171 – 1744
    Beta strandi177 – 1837
    Beta strandi192 – 1943
    Helixi198 – 2058
    Helixi214 – 22916
    Beta strandi233 – 2375
    Helixi244 – 2529
    Helixi255 – 2573
    Helixi260 – 27617
    Turni283 – 2853
    Helixi290 – 30617
    Helixi312 – 34231
    Helixi350 – 37122
    Helixi376 – 3783
    Helixi379 – 42345
    Turni424 – 4274
    Helixi432 – 44918
    Helixi457 – 46711
    Helixi469 – 47810
    Beta strandi480 – 4823
    Helixi484 – 56380
    Helixi566 – 58217

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00313.
    ProteinModelPortaliP32455.
    SMRiP32455. Positions 7-583.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32455.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 278244GB1/RHD3-type GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 311311GTPase domain (Globular)Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG288755.
    HOGENOMiHOG000266974.
    HOVERGENiHBG001979.
    InParanoidiP32455.
    OMAiGFQKESR.
    OrthoDBiEOG7BW0J3.
    PhylomeDBiP32455.
    TreeFamiTF331602.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003191. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P32455-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG    50
    KSYLMNKLAG KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG 100
    LGDVEKGDNQ NDSWIFALAV LLSSTFVYNS IGTINQQAMD QLYYVTELTH 150
    RIRSKSSPDE NENEVEDSAD FVSFFPDFVW TLRDFSLDLE ADGQPLTPDE 200
    YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR PVHRRKLAQL 250
    EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY 300
    VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTETL 350
    QELLDLHRDS EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ 400
    EASSDRCSAL LQVIFSPLEE EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE 450
    PRKGIQAEEI LQTYLKSKES MTDAILQTDQ TLTEKEKEIE VERVKAESAQ 500
    ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV QLLKEQERTL 550
    ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKACT IS 592
    Length:592
    Mass (Da):67,931
    Last modified:November 2, 2010 - v2
    Checksum:i3A06741218360732
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti78 – 781I → V.
    Corresponds to variant rs1048401 [ dbSNP | Ensembl ].
    VAR_033950
    Natural varianti166 – 1661E → D.
    Corresponds to variant rs17130717 [ dbSNP | Ensembl ].
    VAR_033951
    Natural varianti349 – 3491T → S.3 Publications
    Corresponds to variant rs1048425 [ dbSNP | Ensembl ].
    VAR_014849
    Natural varianti409 – 4091A → G.3 Publications
    Corresponds to variant rs1048443 [ dbSNP | Ensembl ].
    VAR_046550

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS718.1.
    PIRiA41268.
    RefSeqiNP_002044.2. NM_002053.2.
    UniGeneiHs.62661.

    Genome annotation databases

    EnsembliENST00000370473; ENSP00000359504; ENSG00000117228.
    GeneIDi2633.
    KEGGihsa:2633.
    UCSCiuc001dmx.2. human.

    Polymorphism databases

    DMDMi311033383.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS718.1.
    PIRi A41268.
    RefSeqi NP_002044.2. NM_002053.2.
    UniGenei Hs.62661.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DG3 X-ray 1.80 A 1-592 [» ]
    1F5N X-ray 1.70 A 1-592 [» ]
    2B8W X-ray 2.22 A/B 1-317 [» ]
    2B92 X-ray 3.20 A/B 1-317 [» ]
    2BC9 X-ray 2.80 A 1-317 [» ]
    2D4H X-ray 2.90 A/B 1-317 [» ]
    DisProti DP00313.
    ProteinModelPortali P32455.
    SMRi P32455. Positions 7-583.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108903. 11 interactions.
    DIPi DIP-60423N.
    IntActi P32455. 1 interaction.
    MINTi MINT-4718320.
    STRINGi 9606.ENSP00000359504.

    PTM databases

    PhosphoSitei P32455.

    Polymorphism databases

    DMDMi 311033383.

    Proteomic databases

    MaxQBi P32455.
    PaxDbi P32455.
    PRIDEi P32455.

    Protocols and materials databases

    DNASUi 2633.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370473 ; ENSP00000359504 ; ENSG00000117228 .
    GeneIDi 2633.
    KEGGi hsa:2633.
    UCSCi uc001dmx.2. human.

    Organism-specific databases

    CTDi 2633.
    GeneCardsi GC01M089517.
    H-InvDB HIX0018119.
    HIX0200036.
    HGNCi HGNC:4182. GBP1.
    HPAi CAB015450.
    MIMi 600411. gene.
    neXtProti NX_P32455.
    PharmGKBi PA28596.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG288755.
    HOGENOMi HOG000266974.
    HOVERGENi HBG001979.
    InParanoidi P32455.
    OMAi GFQKESR.
    OrthoDBi EOG7BW0J3.
    PhylomeDBi P32455.
    TreeFami TF331602.

    Enzyme and pathway databases

    Reactomei REACT_25078. Interferon gamma signaling.

    Miscellaneous databases

    EvolutionaryTracei P32455.
    GeneWikii GBP1.
    GenomeRNAii 2633.
    NextBioi 10380.
    PROi P32455.
    SOURCEi Search...

    Gene expression databases

    Bgeei P32455.
    CleanExi HS_GBP1.
    Genevestigatori P32455.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003191. Guanylate-bd_C.
    IPR015894. Guanylate-bd_N.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF02263. GBP. 1 hit.
    PF02841. GBP_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48340. SSF48340. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS51715. G_GB1_RHD3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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.

    Entry informationi

    Entry nameiGBP1_HUMAN
    AccessioniPrimary (citable) accession number: P32455
    Secondary accession number(s): D3DT26, Q5T8M1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3