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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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 774744Virion surfaceUniRule annotationAdd
BLAST
Transmembranei775 – 79521HelicalUniRule annotationAdd
BLAST
Topological domaini796 – 904109IntravirionUniRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi174 – 1741W → R: 90% loss of fusion with host cell. 1 Publication
Mutagenesisi179 – 1791Y → S: Complete loss of fusion with host cell. 1 Publication
Mutagenesisi263 – 2631H → A: 50% loss of fusion with host cell. 1 Publication
Mutagenesisi264 – 2641R → A: 70% loss of fusion with host cell. 1 Publication
Mutagenesisi887 – 8871T → A: Defects in nuclear egress. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030UniRule annotationAdd
BLAST
Chaini31 – 904874Envelope glycoprotein BUniRule annotationPRO_0000038162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi87 – 871N-linked (GlcNAc...); by hostUniRule annotation
Disulfide bondi116 ↔ 573UniRule annotationCombined sources1 Publication
Disulfide bondi133 ↔ 529UniRule annotationCombined sources1 Publication
Glycosylationi141 – 1411N-linked (GlcNAc...); by hostUniRule annotation
Disulfide bondi207 ↔ 271UniRule annotationCombined sources1 Publication
Disulfide bondi364 ↔ 412UniRule annotationCombined sources1 Publication
Glycosylationi398 – 3981N-linked (GlcNAc...); by hostUniRule annotation
Glycosylationi430 – 4301N-linked (GlcNAc...); by hostUniRule annotation
Glycosylationi489 – 4891N-linked (GlcNAc...); by hostUniRule annotation
Disulfide bondi596 ↔ 633UniRule annotationCombined sources1 Publication
Glycosylationi674 – 6741N-linked (GlcNAc...); by hostUniRule annotation
Modified residuei887 – 8871Phosphothreonine; by host2 Publications

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

1
904
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi113 – 1153Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi157 – 17519Combined sources
Beta strandi180 – 19112Combined sources
Helixi194 – 1985Combined sources
Turni199 – 2046Combined sources
Beta strandi205 – 22319Combined sources
Helixi224 – 2263Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi246 – 2494Combined sources
Beta strandi262 – 28019Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi303 – 3064Combined sources
Helixi307 – 3093Combined sources
Beta strandi312 – 3143Combined sources
Helixi316 – 3183Combined sources
Beta strandi319 – 3257Combined sources
Turni330 – 3323Combined sources
Beta strandi340 – 3467Combined sources
Beta strandi351 – 3555Combined sources
Turni360 – 3623Combined sources
Beta strandi365 – 3739Combined sources
Beta strandi375 – 3806Combined sources
Beta strandi383 – 3886Combined sources
Turni389 – 3924Combined sources
Beta strandi393 – 4008Combined sources
Helixi404 – 4063Combined sources
Beta strandi407 – 4093Combined sources
Helixi412 – 42817Combined sources
Turni429 – 4324Combined sources
Beta strandi433 – 4353Combined sources
Beta strandi440 – 4445Combined sources
Turni445 – 4473Combined sources
Beta strandi448 – 4547Combined sources
Helixi458 – 4636Combined sources
Helixi464 – 4707Combined sources
Helixi502 – 54544Combined sources
Helixi547 – 5559Combined sources
Beta strandi559 – 5635Combined sources
Beta strandi565 – 5728Combined sources
Beta strandi574 – 5763Combined sources
Helixi578 – 5803Combined sources
Beta strandi581 – 5833Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi595 – 5995Combined sources
Beta strandi601 – 6044Combined sources
Beta strandi606 – 6105Combined sources
Beta strandi613 – 6175Combined sources
Helixi619 – 6213Combined sources
Beta strandi622 – 6254Combined sources
Beta strandi630 – 6323Combined sources
Beta strandi638 – 6436Combined sources
Beta strandi646 – 6516Combined sources
Beta strandi654 – 6607Combined sources
Helixi661 – 6633Combined sources
Beta strandi664 – 6674Combined sources
Helixi691 – 6977Combined sources
Beta strandi698 – 7003Combined sources
Helixi702 – 7098Combined sources
Helixi712 – 7165Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 109-724.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06437.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 1797Involved in fusion and/or binding to host membraneUniRule annotation
Regioni258 – 2658Involved in fusion and/or binding to host membraneUniRule annotation
Regioni719 – 77254Hydrophobic membrane proximal regionUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi849 – 8524Golgi targetingUniRule annotation
Motifi889 – 8924Internalization motifUniRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi51 – 8333Pro-richAdd
BLAST
Compositional biasi476 – 4849Poly-Pro

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
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. Positions 109-724.
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: September 7, 2016
This is version 95 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.