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P32455

- GBP1_HUMAN

UniProt

P32455 - GBP1_HUMAN

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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

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
Complete GO annotation...

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-KW
  3. Golgi apparatus Source: UniProtKB-KW
  4. membrane Source: UniProtKB-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074475.
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

        10         20         30         40         50
MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG
60 70 80 90 100
KSYLMNKLAG KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG
110 120 130 140 150
LGDVEKGDNQ NDSWIFALAV LLSSTFVYNS IGTINQQAMD QLYYVTELTH
160 170 180 190 200
RIRSKSSPDE NENEVEDSAD FVSFFPDFVW TLRDFSLDLE ADGQPLTPDE
210 220 230 240 250
YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR PVHRRKLAQL
260 270 280 290 300
EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY
310 320 330 340 350
VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTETL
360 370 380 390 400
QELLDLHRDS EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ
410 420 430 440 450
EASSDRCSAL LQVIFSPLEE EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE
460 470 480 490 500
PRKGIQAEEI LQTYLKSKES MTDAILQTDQ TLTEKEKEIE VERVKAESAQ
510 520 530 540 550
ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV QLLKEQERTL
560 570 580 590
ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKACT IS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00550000074475.
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

ChiTaRSi GBP1. human.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 137 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