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P06437

- GB_HHV1K

UniProt

P06437 - GB_HHV1K

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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: 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 of gD to one of its receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May also 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).1 Publication

GO - Biological processi

  1. viral entry into host cell Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
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 B
Short name:
gB
Alternative name(s):
gB-1
gB1
Gene namesi
Name:gB
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 By similarity; Single-pass type I membrane protein By similarity. Host cell membrane By similarity; Single-pass type I membrane protein By similarity. Host endosome membrane By similarity; Single-pass type I membrane protein By similarity. Host Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity
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) (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 774744Virion surfaceSequence AnalysisAdd
BLAST
Transmembranei775 – 79521HelicalSequence AnalysisAdd
BLAST
Topological domaini796 – 904109IntravirionSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell endosome Source: UniProtKB-KW
  2. host cell Golgi apparatus Source: UniProtKB-KW
  3. host cell plasma membrane Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
  5. viral envelope Source: UniProtKB-KW
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 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 904874Envelope glycoprotein BPRO_0000038162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi87 – 871N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi116 ↔ 573
Disulfide bondi133 ↔ 529
Glycosylationi141 – 1411N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi207 ↔ 271
Disulfide bondi364 ↔ 412
Glycosylationi398 – 3981N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi430 – 4301N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi489 – 4891N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi596 ↔ 633
Glycosylationi674 – 6741N-linked (GlcNAc...); by hostSequence Analysis
Modified residuei887 – 8871Phosphothreonine2 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

Interactioni

Subunit structurei

Homotrimer; disulfide-linked. Interacts with the host coreceptor PILRA. Binds to heparan sulfate proteoglycans. Interacts with gD. Interacts with gH/gL heterodimer. Associates with the gB-gH/gL-gD complex (By similarity).By similarity

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[»]
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 membraneSequence Analysis
Regioni258 – 2658Involved in fusion and/or binding to host membraneSequence Analysis
Regioni719 – 77254Hydrophobic membrane proximal regionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi849 – 8524Internalization motifSequence Analysis

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

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 .
PIRi A03751. VGBEK1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GUM X-ray 2.10 A/B/C 103-730 [» ]
3NW8 X-ray 2.76 A/B/C/D 30-730 [» ]
3NWA X-ray 2.26 A/B/C/D 30-730 [» ]
3NWD X-ray 2.88 A/B/C/D 30-730 [» ]
3NWF X-ray 3.00 A/B/C/D 30-730 [» ]
3WV0 X-ray 2.30 X/Y 50-56 [» ]
4BOM electron microscopy 27.00 A/B/C 103-724 [» ]
4HSI X-ray 3.10 A/B/C/D 61-730 [» ]
4L1R X-ray 3.03 A/B 30-730 [» ]
ProteinModelPortali P06437.
SMRi P06437. Positions 109-724.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60474N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P06437.

Family and domain databases

InterProi IPR000234. Herpes_Glycoprot_B.
[Graphical view ]
Pfami PF00606. Glycoprotein_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence specifying the glycoprotein gene, gB, of herpes simplex virus type 1."
    Bzik D.J., Fox B.A., Deluca N.A., Person S.
    Virology 133:301-314(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of the gB glycoprotein gene of HSV-2 and comparison with the corresponding gene of HSV-1."
    Bzik D.J., Debroy C., Fox B.A., Pederson N.E., Person S.
    Virology 155:322-333(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
  3. Pederson N.E.
    Submitted (APR-1987) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B."
    Herold B.C., Visalli R.J., Susmarski N., Brandt C.R., Spear P.G.
    J. Gen. Virol. 75:1211-1222(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO HEPARAN SULFATE.
  5. "Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B."
    Subramanian R.P., Geraghty R.J.
    Proc. Natl. Acad. Sci. U.S.A. 104:2903-2908(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion."
    Atanasiu D., Whitbeck J.C., Cairns T.M., Reilly B., Cohen G.H., Eisenberg R.J.
    Proc. Natl. Acad. Sci. U.S.A. 104:18718-18723(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GH/GL HETERODIMER.
  7. "PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B."
    Satoh T., Arii J., Suenaga T., Wang J., Kogure A., Uehori J., Arase N., Shiratori I., Tanaka S., Kawaguchi Y., Spear P.G., Lanier L.L., Arase H.
    Cell 132:935-944(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE HUMAN CORECEPTOR PILRA.
  8. "Herpes simplex virus 1 protein kinase Us3 phosphorylates viral envelope glycoprotein B and regulates its expression on the cell surface."
    Kato A., Arii J., Shiratori I., Akashi H., Arase H., Kawaguchi Y.
    J. Virol. 83:250-261(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-887 BY VIRAL KINASE US3, MUTAGENESIS OF THR-887.
  9. "Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase."
    Wisner T.W., Wright C.C., Kato A., Kawaguchi Y., Mou F., Baines J.D., Roller R.J., Johnson D.C.
    J. Virol. 83:3115-3126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-887 BY VIRAL KINASE US3, MUTAGENESIS OF THR-887.
  10. "Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops."
    Hannah B.P., Cairns T.M., Bender F.C., Whitbeck J.C., Lou H., Eisenberg R.J., Cohen G.H.
    J. Virol. 83:6825-6836(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TRP-174; TYR-179; HIS-263 AND ARG-264.
  11. "Crystal structure of glycoprotein B from herpes simplex virus 1."
    Heldwein E.E., Lou H., Bender F.C., Cohen G.H., Eisenberg R.J., Harrison S.C.
    Science 313:217-220(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 103-730.

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 26, 2014
This is version 87 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

External Data

Dasty 3