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Protein

Envelope glycoprotein B

Gene

gB

Organism
Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-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

  • Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host endosome membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host Golgi apparatus membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation

  • Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN).UniRule annotation

Topology

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

GO - Cellular componenti

Complete GO annotation...

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...); by hostUniRule annotation1
Disulfide bondi116 ↔ 573UniRule annotationCombined sources1 Publication
Disulfide bondi133 ↔ 529UniRule annotationCombined sources1 Publication
Glycosylationi141N-linked (GlcNAc...); by hostUniRule annotation1
Disulfide bondi207 ↔ 271UniRule annotationCombined sources1 Publication
Disulfide bondi364 ↔ 412UniRule annotationCombined sources1 Publication
Glycosylationi398N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi430N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi489N-linked (GlcNAc...); by hostUniRule annotation1
Disulfide bondi596 ↔ 633UniRule annotationCombined sources1 Publication
Glycosylationi674N-linked (GlcNAc...); 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

Protein-protein interaction databases

DIPiDIP-60474N.

Structurei

Secondary structure

1904
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi113 – 115Combined sources3
Beta strandi123 – 127Combined sources5
Beta strandi145 – 152Combined sources8
Beta strandi157 – 175Combined sources19
Beta strandi180 – 191Combined sources12
Helixi194 – 198Combined sources5
Turni199 – 204Combined sources6
Beta strandi205 – 223Combined sources19
Helixi224 – 226Combined sources3
Beta strandi231 – 233Combined sources3
Beta strandi246 – 249Combined sources4
Beta strandi262 – 280Combined sources19
Beta strandi287 – 289Combined sources3
Beta strandi290 – 292Combined sources3
Beta strandi303 – 306Combined sources4
Helixi307 – 309Combined sources3
Beta strandi312 – 314Combined sources3
Helixi316 – 318Combined sources3
Beta strandi319 – 325Combined sources7
Turni330 – 332Combined sources3
Beta strandi340 – 346Combined sources7
Beta strandi351 – 355Combined sources5
Turni360 – 362Combined sources3
Beta strandi365 – 373Combined sources9
Beta strandi375 – 380Combined sources6
Beta strandi383 – 388Combined sources6
Turni389 – 392Combined sources4
Beta strandi393 – 400Combined sources8
Helixi404 – 406Combined sources3
Beta strandi407 – 409Combined sources3
Helixi412 – 428Combined sources17
Turni429 – 432Combined sources4
Beta strandi433 – 435Combined sources3
Beta strandi440 – 444Combined sources5
Turni445 – 447Combined sources3
Beta strandi448 – 454Combined sources7
Helixi458 – 463Combined sources6
Helixi464 – 470Combined sources7
Helixi502 – 545Combined sources44
Helixi547 – 555Combined sources9
Beta strandi559 – 563Combined sources5
Beta strandi565 – 572Combined sources8
Beta strandi574 – 576Combined sources3
Helixi578 – 580Combined sources3
Beta strandi581 – 583Combined sources3
Beta strandi590 – 592Combined sources3
Beta strandi595 – 599Combined sources5
Beta strandi601 – 604Combined sources4
Beta strandi606 – 610Combined sources5
Beta strandi613 – 617Combined sources5
Helixi619 – 621Combined sources3
Beta strandi622 – 625Combined sources4
Beta strandi630 – 632Combined sources3
Beta strandi638 – 643Combined sources6
Beta strandi646 – 651Combined sources6
Beta strandi654 – 660Combined sources7
Helixi661 – 663Combined sources3
Beta strandi664 – 667Combined sources4
Helixi691 – 697Combined sources7
Beta strandi698 – 700Combined sources3
Helixi702 – 709Combined sources8
Helixi712 – 716Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GUMX-ray2.10A/B/C103-730[»]
3NW8X-ray2.76A/B/C/D30-730[»]
3NWAX-ray2.26A/B/C/D30-730[»]
3NWDX-ray2.88A/B/C/D30-730[»]
3NWFX-ray3.00A/B/C/D30-730[»]
3WV0X-ray2.30X/Y50-56[»]
4BOMelectron microscopy27.00A/B/C103-724[»]
4HSIX-ray3.10A/B/C/D61-730[»]
4L1RX-ray3.03A/B30-730[»]
5FZ2electron microscopy23.00A/B/C1-904[»]
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

HAMAPiMF_04032. HSV_GB. 1 hit.
InterProiIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamiPF00606. Glycoprotein_B. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GUMX-ray2.10A/B/C103-730[»]
3NW8X-ray2.76A/B/C/D30-730[»]
3NWAX-ray2.26A/B/C/D30-730[»]
3NWDX-ray2.88A/B/C/D30-730[»]
3NWFX-ray3.00A/B/C/D30-730[»]
3WV0X-ray2.30X/Y50-56[»]
4BOMelectron microscopy27.00A/B/C103-724[»]
4HSIX-ray3.10A/B/C/D61-730[»]
4L1RX-ray3.03A/B30-730[»]
5FZ2electron microscopy23.00A/B/C1-904[»]
ProteinModelPortaliP06437.
SMRiP06437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60474N.

PTM databases

iPTMnetiP06437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP06437.

Family and domain databases

HAMAPiMF_04032. HSV_GB. 1 hit.
InterProiIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamiPF00606. Glycoprotein_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGB_HHV1K
AccessioniPrimary (citable) accession number: P06437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.