Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Envelope glycoprotein B

Gene

gB

Organism
Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
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. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation).UniRule annotation1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct

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:UL27
OrganismiHuman herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10306 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 774Virion surfaceUniRule annotationAdd BLAST744
Transmembranei775 – 795HelicalUniRule annotationAdd BLAST21
Topological domaini796 – 904IntravirionUniRule annotationAdd BLAST109

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
Mutagenesisi174W → R: 90% loss of fusion with host cell. 1 Publication1
Mutagenesisi179Y → S: Complete loss of fusion with host cell. 1 Publication1
Mutagenesisi263H → A: 50% loss of fusion with host cell. 1 Publication1
Mutagenesisi264R → A: 70% loss of fusion with host cell. 1 Publication1
Mutagenesisi887T → A: Defects in nuclear egress. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30UniRule annotationAdd BLAST30
ChainiPRO_000003816231 – 904Envelope glycoprotein BUniRule annotationAdd BLAST874

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi87N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi116 ↔ 573UniRule annotationCombined sources1 Publication
Disulfide bondi133 ↔ 529UniRule annotationCombined sources1 Publication
Glycosylationi141N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi207 ↔ 271UniRule annotationCombined sources1 Publication
Disulfide bondi364 ↔ 412UniRule annotationCombined sources1 Publication
Glycosylationi398N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi430N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi489N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi596 ↔ 633UniRule annotationCombined sources1 Publication
Glycosylationi674N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Modified residuei887Phosphothreonine; by host2 Publications1

Post-translational modificationi

The cytoplasmic tail is phosphorylated by the viral kinase US3. Phosphorylation may be linked to a down-regulation of gB expression on cell surface.2 Publications
ubiquitinated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

PTM databases

iPTMnetiP06437

Interactioni

Subunit structurei

Homotrimer; disulfide-linked. Binds to heparan sulfate proteoglycans. Interacts with gH/gL heterodimer (By similarity). Interacts with the host coreceptor PILRA.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-16064668,EBI-16064668

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-60474N

Structurei

Secondary structure

1904
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP06437
SMRiP06437
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06437

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni173 – 179Involved in fusion and/or binding to host membraneUniRule annotation7
Regioni258 – 265Involved in fusion and/or binding to host membraneUniRule annotation8
Regioni719 – 772Hydrophobic membrane proximal regionUniRule annotationAdd BLAST54

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi849 – 852Golgi targetingUniRule annotation4
Motifi889 – 892Internalization motifUniRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi51 – 83Pro-richAdd BLAST33
Compositional biasi476 – 484Poly-Pro9

Sequence similaritiesi

Belongs to the herpesviridae glycoprotein B family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

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.

P06437-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHQGAPSWGR RWFVVWALLG LTLGVLVASA APTSPGTPGV AAATQAANGG
60 70 80 90 100
PATPAPPPLG AAPTGDPKPK KNKKPKNPTP PRPAGDNATV AAGHATLREH
110 120 130 140 150
LRDIKAENTD ANFYVCPPPT GATVVQFEQP RRCPTRPEGQ NYTEGIAVVF
160 170 180 190 200
KENIAPYKFK ATMYYKDVTV SQVWFGHRYS QFMGIFEDRA PVPFEEVIDK
210 220 230 240 250
INAKGVCRST AKYVRNNLET TAFHRDDHET DMELKPANAA TRTSRGWHTT
260 270 280 290 300
DLKYNPSRVE AFHRYGTTVN CIVEEVDARS VYPYDEFVLA TGDFVYMSPF
310 320 330 340 350
YGYREGSHTE HTTYAADRFK QVDGFYARDL TTKARATAPT TRNLLTTPKF
360 370 380 390 400
TVAWDWVPKR PSVCTMTKWQ EVDEMLRSEY GGSFRFSSDA ISTTFTTNLT
410 420 430 440 450
EYPLSRVDLG DCIGKDARDA MDRIFARRYN ATHIKVGQPQ YYQANGGFLI
460 470 480 490 500
AYQPLLSNTL AELYVREHLR EQSRKPPNPT PPPPGASANA SVERIKTTSS
510 520 530 540 550
IEFARLQFTY NHIQRHVNDM LGRVAIAWCE LQNHELTLWN EARKLNPNAI
560 570 580 590 600
ASVTVGRRVS ARMLGDVMAV STCVPVAADN VIVQNSMRIS SRPGACYSRP
610 620 630 640 650
LVSFRYEDQG PLVEGQLGEN NELRLTRDAI EPCTVGHRRY FTFGGGYVYF
660 670 680 690 700
EEYAYSHQLS RADITTVSTF IDLNITMLED HEFVPLEVYT RHEIKDSGLL
710 720 730 740 750
DYTEVQRRNQ LHDLRFADID TVIHADANAA MFAGLGAFFE GMGDLGRAVG
760 770 780 790 800
KVVMGIVGGV VSAVSGVSSF MSNPFGALAV GLLVLAGLAA AFFAFRYVMR
810 820 830 840 850
LQSNPMKALY PLTTKELKNP TNPDASGEGE EGGDFDEAKL AEAREMIRYM
860 870 880 890 900
ALVSAMERTE HKAKKKGTSA LLSAKVTDMV MRKRRNTNYT QVPNKDGDAD

EDDL
Length:904
Mass (Da):100,368
Last modified:February 1, 1996 - v2
Checksum:iB97B7F8DE5FBA299
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01760 Genomic DNA Translation: AAA45774.1
PIRiA03751 VGBEK1

Similar proteinsi

Entry informationi

Entry nameiGB_HHV1K
AccessioniPrimary (citable) accession number: P06437
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1996
Last modified: March 28, 2018
This is version 103 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again