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Protein

Envelope glycoprotein B

Gene

gB

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moities of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.UniRule annotation

GO - Biological processi

Keywordsi

Biological processHost-virus interaction, Viral attachment to host cell, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein BUniRule annotation
Short name:
gBUniRule annotation
Gene namesi
Name:gBUniRule annotation
ORF Names:BALF4
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000153037 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 732Virion surfaceUniRule annotationAdd BLAST711
Transmembranei733 – 753HelicalUniRule annotationAdd BLAST21
Topological domaini754 – 857IntravirionUniRule annotationAdd BLAST104

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host endosome, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112 – 113WY → HR: Loss of fusion with epithelial cells. 1 Publication2
Mutagenesisi193 – 196WLIW → RVEA: Loss of fusion with epithelial cells. 1 Publication4
Mutagenesisi428 – 432RRRRR → DDDDK: Complete loss of proteolytic cleavage. 1 Publication5

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21UniRule annotationAdd BLAST21
ChainiPRO_000003819022 – 857Envelope glycoprotein BUniRule annotationAdd BLAST836

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 528UniRule annotationCombined sources1 Publication
Disulfide bondi68 ↔ 484UniRule annotationCombined sources1 Publication
Glycosylationi76N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi141 ↔ 206UniRule annotationCombined sources1 Publication
Glycosylationi163N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Glycosylationi290N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Disulfide bondi295 ↔ 342UniRule annotationCombined sources1 Publication
Glycosylationi329N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi348N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi395N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi436N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi551 ↔ 588UniRule annotation
Glycosylationi563N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi629N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1

Post-translational modificationi

A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei432 – 433Cleavage; by host furinSequence analysis2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP03188

PTM databases

iPTMnetiP03188

Interactioni

Subunit structurei

Homotrimer; disulfide-linked. Binds to heparan sulfate proteoglycans. Interacts with gH/gL heterodimer.UniRule annotation

Protein-protein interaction databases

DIPiDIP-47669N
IntActiP03188, 10 interactors
MINTiP03188

Structurei

Secondary structure

1857
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP03188
SMRiP03188
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03188

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni108 – 114Involved in fusion and/or binding to host membraneUniRule annotation7
Regioni192 – 200Involved in fusion and/or binding to host membraneUniRule annotation9
Regioni561 – 620OligomerizationAdd BLAST60
Regioni678 – 730Hydrophobic membrane proximal regionUniRule annotationAdd BLAST53
Regioni709 – 729Hydrophobic membrane proximal regionAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi428 – 432Poly-Arg5
Compositional biasi836 – 839Poly-Arg4

Sequence similaritiesi

Belongs to the herpesviridae glycoprotein B family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19255
OrthoDBiVOG0900002K

Family and domain databases

Gene3Di2.30.29.100, 1 hit
HAMAPiMF_04032 HSV_GB, 1 hit
InterProiView protein in InterPro
IPR035377 Glycoprot_B_PH1
IPR035381 Glycoprot_B_PH2
IPR038631 Glycoprot_B_PH2_sf
IPR000234 Herpes_Glycoprot_B
PfamiView protein in Pfam
PF17416 Glycoprot_B_PH1, 1 hit
PF17417 Glycoprot_B_PH2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P03188-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTRRRVLSVV VLLAALACRL GAQTPEQPAP PATTVQPTAT RQQTSFPFRV
60 70 80 90 100
CELSSHGDLF RFSSDIQCPS FGTRENHTEG LLMVFKDNII PYSFKVRSYT
110 120 130 140 150
KIVTNILIYN GWYADSVTNR HEEKFSVDSY ETDQMDTIYQ CYNAVKMTKD
160 170 180 190 200
GLTRVYVDRD GVNITVNLKP TGGLANGVRR YASQTELYDA PGWLIWTYRT
210 220 230 240 250
RTTVNCLITD MMAKSNSPFD FFVTTTGQTV EMSPFYDGKN KETFHERADS
260 270 280 290 300
FHVRTNYKIV DYDNRGTNPQ GERRAFLDKG TYTLSWKLEN RTAYCPLQHW
310 320 330 340 350
QTFDSTIATE TGKSIHFVTD EGTSSFVTNT TVGIELPDAF KCIEEQVNKT
360 370 380 390 400
MHEKYEAVQD RYTKGQEAIT YFITSGGLLL AWLPLTPRSL ATVKNLTELT
410 420 430 440 450
TPTSSPPSSP SPPAPSAARG STPAAVLRRR RRDAGNATTP VPPTAPGKSL
460 470 480 490 500
GTLNNPATVQ IQFAYDSLRR QINRMLGDLA RAWCLEQKRQ NMVLRELTKI
510 520 530 540 550
NPTTVMSSIY GKAVAAKRLG DVISVSQCVP VNQATVTLRK SMRVPGSETM
560 570 580 590 600
CYSRPLVSFS FINDTKTYEG QLGTDNEIFL TKKMTEVCQA TSQYYFQSGN
610 620 630 640 650
EIHVYNDYHH FKTIELDGIA TLQTFISLNT SLIENIDFAS LELYSRDEQR
660 670 680 690 700
ASNVFDLEGI FREYNFQAQN IAGLRKDLDN AVSNGRNQFV DGLGELMDSL
710 720 730 740 750
GSVGQSITNL VSTVGGLFSS LVSGFISFFK NPFGGMLILV LVAGVVILVI
760 770 780 790 800
SLTRRTRQMS QQPVQMLYPG IDELAQQHAS GEGPGINPIS KTELQAIMLA
810 820 830 840 850
LHEQNQEQKR AAQRAAGPSV ASRALQAARD RFPGLRRRRY HDPETAAALL

GEAETEF
Length:857
Mass (Da):95,639
Last modified:July 21, 1986 - v1
Checksum:iD9BCE9487D8A1411
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA Translation: CAA24806.1
AJ507799 Genomic DNA Translation: CAD53463.1
PIRiA03749 QQBE1L
RefSeqiYP_401713.1, NC_007605.1

Genome annotation databases

GeneIDi3783680
KEGGivg:3783680

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA Translation: CAA24806.1
AJ507799 Genomic DNA Translation: CAD53463.1
PIRiA03749 QQBE1L
RefSeqiYP_401713.1, NC_007605.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FVCX-ray3.20A23-685[»]
ProteinModelPortaliP03188
SMRiP03188
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47669N
IntActiP03188, 10 interactors
MINTiP03188

PTM databases

iPTMnetiP03188

Proteomic databases

PRIDEiP03188

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783680
KEGGivg:3783680

Phylogenomic databases

KOiK19255
OrthoDBiVOG0900002K

Miscellaneous databases

EvolutionaryTraceiP03188

Family and domain databases

Gene3Di2.30.29.100, 1 hit
HAMAPiMF_04032 HSV_GB, 1 hit
InterProiView protein in InterPro
IPR035377 Glycoprot_B_PH1
IPR035381 Glycoprot_B_PH2
IPR038631 Glycoprot_B_PH2_sf
IPR000234 Herpes_Glycoprot_B
PfamiView protein in Pfam
PF17416 Glycoprot_B_PH1, 1 hit
PF17417 Glycoprot_B_PH2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGB_EBVB9
AccessioniPrimary (citable) accession number: P03188
Secondary accession number(s): Q777B0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 10, 2018
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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