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P06437

- GB_HHV1K

UniProt

P06437 - GB_HHV1K

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
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

    1. host cell endosome membrane Source: UniProtKB-SubCell
    2. host cell Golgi membrane Source: UniProtKB-SubCell
    3. host cell plasma membrane Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. viral envelope Source: UniProtKB-KW
    6. virion membrane Source: UniProtKB-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei775 – 79521HelicalSequence AnalysisAdd
    BLAST

    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

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    MHQGAPSWGR RWFVVWALLG LTLGVLVASA APTSPGTPGV AAATQAANGG    50
    PATPAPPPLG AAPTGDPKPK KNKKPKNPTP PRPAGDNATV AAGHATLREH 100
    LRDIKAENTD ANFYVCPPPT GATVVQFEQP RRCPTRPEGQ NYTEGIAVVF 150
    KENIAPYKFK ATMYYKDVTV SQVWFGHRYS QFMGIFEDRA PVPFEEVIDK 200
    INAKGVCRST AKYVRNNLET TAFHRDDHET DMELKPANAA TRTSRGWHTT 250
    DLKYNPSRVE AFHRYGTTVN CIVEEVDARS VYPYDEFVLA TGDFVYMSPF 300
    YGYREGSHTE HTTYAADRFK QVDGFYARDL TTKARATAPT TRNLLTTPKF 350
    TVAWDWVPKR PSVCTMTKWQ EVDEMLRSEY GGSFRFSSDA ISTTFTTNLT 400
    EYPLSRVDLG DCIGKDARDA MDRIFARRYN ATHIKVGQPQ YYQANGGFLI 450
    AYQPLLSNTL AELYVREHLR EQSRKPPNPT PPPPGASANA SVERIKTTSS 500
    IEFARLQFTY NHIQRHVNDM LGRVAIAWCE LQNHELTLWN EARKLNPNAI 550
    ASVTVGRRVS ARMLGDVMAV STCVPVAADN VIVQNSMRIS SRPGACYSRP 600
    LVSFRYEDQG PLVEGQLGEN NELRLTRDAI EPCTVGHRRY FTFGGGYVYF 650
    EEYAYSHQLS RADITTVSTF IDLNITMLED HEFVPLEVYT RHEIKDSGLL 700
    DYTEVQRRNQ LHDLRFADID TVIHADANAA MFAGLGAFFE GMGDLGRAVG 750
    KVVMGIVGGV VSAVSGVSSF MSNPFGALAV GLLVLAGLAA AFFAFRYVMR 800
    LQSNPMKALY PLTTKELKNP TNPDASGEGE EGGDFDEAKL AEAREMIRYM 850
    ALVSAMERTE HKAKKKGTSA LLSAKVTDMV MRKRRNTNYT QVPNKDGDAD 900
    EDDL 904
    Length:904
    Mass (Da):100,368
    Last modified:February 1, 1996 - v2
    Checksum:iB97B7F8DE5FBA299
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01760 Genomic DNA. Translation: AAA45774.1.
    PIRiA03751. VGBEK1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01760 Genomic DNA. Translation: AAA45774.1 .
    PIRi A03751. VGBEK1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 85 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