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Protein

Guanylate-binding protein 4

Gene

Gbp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation.1 Publication

Catalytic activityi

GTP + H2O = GDP + phosphate.By similarity

Kineticsi

  1. KM=77.0 µM for GTP1 Publication
  1. Vmax=21 pmol/min/µg enzyme1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 468GTPBy similarity
Nucleotide bindingi61 – 633GTPBy similarity
Nucleotide bindingi91 – 955GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: MGI
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • adhesion of symbiont to host Source: MGI
  • cellular response to interferon-beta Source: MGI
  • cellular response to interferon-gamma Source: MGI
  • defense response to Gram-positive bacterium Source: MGI
  • defense response to protozoan Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate-binding protein 4 (EC:3.6.5.-By similarity)
Alternative name(s):
GTP-binding protein 3
Short name:
GBP-3
GTP-binding protein 4
Short name:
GBP-4
Guanine nucleotide-binding protein 4
Guanylate-binding protein 3
Gene namesi
Name:Gbp4
Synonyms:Gbp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1926263. Gbp3.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cytoplasmperinuclear region By similarity
  • Golgi apparatus membrane By similarity

  • Note: Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP-5, at the Golgi aparatus.By similarity

GO - Cellular componenti

  • cytoplasmic vesicle Source: MGI
  • cytosol Source: MGI
  • Golgi membrane Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • symbiont-containing vacuole membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Guanylate-binding protein 4PRO_0000261160Add
BLAST

Proteomic databases

EPDiQ61107.
MaxQBiQ61107.
PaxDbiQ61107.
PeptideAtlasiQ61107.
PRIDEiQ61107.

PTM databases

iPTMnetiQ61107.
PhosphoSiteiQ61107.

Expressioni

Tissue specificityi

Brain, lung, heart, spleen, kidney, liver and intestine.1 Publication

Inductioni

By IFNG during macrophage activation.1 Publication

Gene expression databases

BgeeiENSMUSG00000028268.
CleanExiMM_GBP3.
ExpressionAtlasiQ61107. baseline and differential.
GenevisibleiQ61107. MM.

Interactioni

Subunit structurei

Heterodimer with other family members, including GBP1, GBP2 and GBP5. Dimerization regulates subcellular location.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029935.

Structurei

3D structure databases

ProteinModelPortaliQ61107.
SMRiQ61107. Positions 1-576.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 271243GB1/RHD3-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 304304GTPase domain (Globular)By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili375 – 41137Sequence analysisAdd
BLAST
Coiled coili477 – 582106Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00550000074475.
HOGENOMiHOG000266974.
HOVERGENiHBG001979.
InParanoidiQ61107.
OMAiPRIENSN.
OrthoDBiEOG091G03P3.
PhylomeDBiQ61107.
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]

Sequencei

Sequence statusi: Complete.

Q61107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAPICLVEN WKNQLTVNLE AIRILEQIAQ PLVVVAIVGL YRTGKSYLMN
60 70 80 90 100
RLAGRNHGFS LGSTVQSETK GIWMWCVPHP TKPTHTLVLL DTEGLGDVEK
110 120 130 140 150
GDPKNDSWIF ALAVLLSSTF VYNSMSTINQ QALEQLHFVT ELTQLIRAKS
160 170 180 190 200
SPREDKVKDS SEFVGFFPDF IWAVRDFALE LKLNGRPITE DEYLENALKL
210 220 230 240 250
IQGDNLKVQQ SNMTRECIRY FFPVRKCFVF DRPTSDKRLL LQIENVPENQ
260 270 280 290 300
LERNFQVESE KFCSYIFTNG KTKTLRGGVI VTGNRLGTLV QTYVNAINSG
310 320 330 340 350
TVPCLENAVT TLAQRENSIA VQKAADHYSE QMAQRMRLPT DTLQELLTVH
360 370 380 390 400
AACEKEAIAV FMEHSFKDDE QEFQKKLVVT IEERKEEFIR QNEAASIRHC
410 420 430 440 450
QAELERLSES LRKSISCGAF SVPGGHSLYL EARKKIELGY QQVLRKGVKA
460 470 480 490 500
KEVLKSFLQS QAIMEDSILQ SDKALTDGER AIAAERTKKE VAEKELELLR
510 520 530 540 550
QRQKEQEQVM EAQERSFREN IAKLQEKMES EKEMLLREQE KMLEHKLKVQ
560 570 580 590 600
EELLIEGFRE KSDMLKNEIS HLREEMERTR RKPSLFGQIL DTIGNAFIMI
610 620
LPGAGKLFGV GLKFLGSLSS
Length:620
Mass (Da):70,801
Last modified:November 1, 1996 - v1
Checksum:i62C73E7FD71D8885
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841N → K in AAH19195 (PubMed:15489334).Curated
Sequence conflicti199 – 1991K → R in AAH19195 (PubMed:15489334).Curated
Sequence conflicti202 – 2021Q → P in AAH19195 (PubMed:15489334).Curated
Sequence conflicti206 – 2061L → P in AAH19195 (PubMed:15489334).Curated
Sequence conflicti336 – 3361M → V in AAH19195 (PubMed:15489334).Curated
Sequence conflicti389 – 3891I → M in AAH19195 (PubMed:15489334).Curated
Sequence conflicti444 – 4441L → P in AAH19195 (PubMed:15489334).Curated
Sequence conflicti463 – 4631I → V in AAH19195 (PubMed:15489334).Curated
Sequence conflicti555 – 5551I → T in AAH19195 (PubMed:15489334).Curated
Sequence conflicti593 – 5931I → V in AAH19195 (PubMed:15489334).Curated
Sequence conflicti620 – 6201S → N in AAH19195 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44731 mRNA. Translation: AAA86645.1.
BC019195 mRNA. Translation: AAH19195.1.
CCDSiCCDS17879.1.
RefSeqiNP_001276421.1. NM_001289492.1.
NP_001276422.1. NM_001289493.1.
NP_061204.3. NM_018734.3.
XP_006501784.1. XM_006501721.1.
XP_006501787.1. XM_006501724.2.
UniGeneiMm.439718.

Genome annotation databases

EnsembliENSMUST00000029935; ENSMUSP00000029935; ENSMUSG00000028268.
ENSMUST00000106221; ENSMUSP00000101828; ENSMUSG00000028268.
ENSMUST00000106222; ENSMUSP00000101829; ENSMUSG00000028268.
GeneIDi55932.
KEGGimmu:55932.
UCSCiuc008rou.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44731 mRNA. Translation: AAA86645.1.
BC019195 mRNA. Translation: AAH19195.1.
CCDSiCCDS17879.1.
RefSeqiNP_001276421.1. NM_001289492.1.
NP_001276422.1. NM_001289493.1.
NP_061204.3. NM_018734.3.
XP_006501784.1. XM_006501721.1.
XP_006501787.1. XM_006501724.2.
UniGeneiMm.439718.

3D structure databases

ProteinModelPortaliQ61107.
SMRiQ61107. Positions 1-576.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029935.

PTM databases

iPTMnetiQ61107.
PhosphoSiteiQ61107.

Proteomic databases

EPDiQ61107.
MaxQBiQ61107.
PaxDbiQ61107.
PeptideAtlasiQ61107.
PRIDEiQ61107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029935; ENSMUSP00000029935; ENSMUSG00000028268.
ENSMUST00000106221; ENSMUSP00000101828; ENSMUSG00000028268.
ENSMUST00000106222; ENSMUSP00000101829; ENSMUSG00000028268.
GeneIDi55932.
KEGGimmu:55932.
UCSCiuc008rou.2. mouse.

Organism-specific databases

CTDi2635.
MGIiMGI:1926263. Gbp3.

Phylogenomic databases

eggNOGiKOG2037. Eukaryota.
ENOG410XR6Z. LUCA.
GeneTreeiENSGT00550000074475.
HOGENOMiHOG000266974.
HOVERGENiHBG001979.
InParanoidiQ61107.
OMAiPRIENSN.
OrthoDBiEOG091G03P3.
PhylomeDBiQ61107.
TreeFamiTF331602.

Miscellaneous databases

ChiTaRSiGbp4. mouse.
PROiQ61107.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028268.
CleanExiMM_GBP3.
ExpressionAtlasiQ61107. baseline and differential.
GenevisibleiQ61107. MM.

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...

Entry informationi

Entry nameiGBP4_MOUSE
AccessioniPrimary (citable) accession number: Q61107
Secondary accession number(s): Q8VEC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.