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P08563

- POLS_RUBVM

UniProt

P08563 - POLS_RUBVM

Protein

Structural polyprotein

Gene
N/A
Organism
Rubella virus (strain M33) (RUBV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    Capsid protein interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells.
    E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein.
    E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion By similarity. E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei300 – 3012Cleavage; by host signal peptidaseSequence Analysis
    Sitei582 – 5832Cleavage; by host signal peptidaseSequence Analysis

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    3. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Structural polyprotein
    Alternative name(s):
    p110
    Cleaved into the following 3 chains:
    Alternative name(s):
    Coat protein
    Short name:
    C
    Alternative name(s):
    Spike glycoprotein E2
    Alternative name(s):
    Spike glycoprotein E1
    OrganismiRubella virus (strain M33) (RUBV)
    Taxonomic identifieri11043 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageTogaviridaeRubivirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007143: Genome

    Subcellular locationi

    Chain Capsid protein : Virion. Host cytoplasm. Host mitochondrion
    Note: The capsid protein is concentrated around Golgi region.
    Chain E1 envelope glycoprotein : Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein
    Note: E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex.
    Chain E2 envelope glycoprotein : Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein
    Note: E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex.

    GO - Cellular componenti

    1. host cell Golgi membrane Source: UniProtKB-SubCell
    2. host cell mitochondrion Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. T=4 icosahedral viral capsid Source: UniProtKB-KW
    5. viral envelope Source: UniProtKB-KW
    6. viral nucleocapsid Source: InterPro
    7. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host Golgi apparatus, Host membrane, Host mitochondrion, Membrane, T=4 icosahedral capsid protein, Viral envelope protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi35 – 439RRPRPPRQR → AAPAPPAQA: Complete loss of human C1QBP/SF2P32-binding. 90% loss of virus production from infected cell. 1 Publication
    Mutagenesisi60 – 689RRRRGNRGR → AAAAGNAGA: Complete loss of human C1QBP/SF2P32-binding. 90% loss of virus production from infected cell. 1 Publication
    Mutagenesisi153 – 1531C → S: Complete loss of Capsid dimerization. No effect on particle budding. 2 Publications
    Mutagenesisi658 – 6581N → I: Complete loss of infectivity. 2 Publications
    Mutagenesisi664 – 6641C → S: Prevents E1-E2 heterodimer formation, and subsequent transport of to the plasma membrane. Complete loss of fusion activity in vitro. 2 Publications
    Mutagenesisi675 – 6751G → D: Complete loss of fusion activity in vitro. 90% loss of infectivity in vivo. No effect on virus assembly. 3 Publications
    Mutagenesisi686 – 6861P → G: 99.9% loss of infectivity. No effect on virus assembly. No effect on fusion activity in vitro. 3 Publications
    Mutagenesisi759 – 7591N → I: No effect on infectivity. 2 Publications
    Mutagenesisi791 – 7911N → I: Complete loss of infectivity. 2 Publications
    Mutagenesisi1046 – 10461L → A: No effect on virus production from infected cell. 2 Publications
    Mutagenesisi1048 – 10481C → A: No effect on virus production from infected cell. 2 Publications
    Mutagenesisi1049 – 10491C → A: No effect on virus production from infected cell. 2 Publications
    Mutagenesisi1052 – 10521C → A: No effect on virus production from infected cell. 3 Publications
    Mutagenesisi1053 – 10531L → A: 90% loss of virus production from infected cell. 3 Publications
    Mutagenesisi1054 – 10541Y → A: Complete loss of virus production from infected cell. 2 Publications
    Mutagenesisi1055 – 10551Y → S: Complete loss of virus production from infected cell. 2 Publications
    Mutagenesisi1056 – 10561L → A: 90% loss of virus production from infected cell. 2 Publications
    Mutagenesisi1057 – 10571R → S: 98% loss of virus production from infected cell. 2 Publications
    Mutagenesisi1058 – 10581G → C: 98% loss of virus production from infected cell. 2 Publications
    Mutagenesisi1059 – 10591A → S: 90% loss of virus production from infected cell. 2 Publications
    Mutagenesisi1060 – 10601I → V: No effect on virus production from infected cell. 2 Publications
    Mutagenesisi1061 – 10611A → S: 90% loss of virus production from infected cell. 2 Publications
    Mutagenesisi1062 – 10621P → S: 90% loss of virus production from infected cell. 2 Publications
    Mutagenesisi1063 – 10631R → S: 98% loss of virus production from infected cell. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 300300Capsid proteinPRO_0000041302Add
    BLAST
    Signal peptidei278 – 30023Not cleavedSequence AnalysisAdd
    BLAST
    Chaini301 – 582282E2 envelope glycoproteinPRO_0000041303Add
    BLAST
    Signal peptidei563 – 58220Not cleavedSequence AnalysisAdd
    BLAST
    Chaini583 – 1063481E1 envelope glycoproteinPRO_0000041304Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461Phosphoserine; by host1 Publication
    Disulfide bondi590 ↔ 595By similarity
    Disulfide bondi619 ↔ 824By similarity
    Disulfide bondi641 ↔ 653By similarity
    Glycosylationi658 – 6581N-linked (GlcNAc...); by host2 Publications
    Disulfide bondi699 ↔ 712By similarity
    Disulfide bondi758 ↔ 767By similarity
    Glycosylationi759 – 7591N-linked (GlcNAc...); by host2 Publications
    Glycosylationi791 – 7911N-linked (GlcNAc...); by host2 Publications
    Disulfide bondi807 ↔ 817By similarity
    Disulfide bondi931 ↔ 934By similarity
    Disulfide bondi950 ↔ 983By similarity

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins. An internal signal peptide at the capsid C-terminus directs E2-E1 sequences of the polyprotein precursor to the endoplasmic reticulum. Signal peptidase cleaves the precursor between Capsid and E2, releasing the capsid in the cytoplasm and the E2 N-terminus in ER. Another signal peptide at E2 C-terminus directs E1 to the ER, with a similar mechanism.
    Capsid is phosphorylated on Ser-46 by host. This phosphorylation negatively regulates capsid protein RNA-binding activity. Dephosphorylated by human PP1A By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Interactioni

    Subunit structurei

    Capsid protein homooligomerizes. Forms a dimer shortly after synthesis, this dimer become disulfide-linked in the virion. Interacts with human C1QBP. E1 and E2 envelope glycoproteins heterodimerize.1 Publication

    Structurei

    Secondary structure

    1
    1063
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi151 – 16010
    Beta strandi162 – 1643
    Beta strandi167 – 17610
    Helixi190 – 1934
    Helixi203 – 2097
    Beta strandi216 – 2216
    Beta strandi227 – 2348
    Beta strandi237 – 2448
    Beta strandi585 – 5895
    Beta strandi599 – 6013
    Beta strandi603 – 62119
    Beta strandi625 – 63410
    Turni641 – 6477
    Helixi650 – 6578
    Beta strandi659 – 67012
    Beta strandi672 – 6743
    Beta strandi676 – 6783
    Helixi681 – 6833
    Helixi689 – 6946
    Beta strandi698 – 7036
    Beta strandi716 – 7183
    Beta strandi721 – 7299
    Helixi733 – 7353
    Beta strandi737 – 75317
    Beta strandi756 – 7605
    Beta strandi766 – 7683
    Beta strandi770 – 7778
    Beta strandi785 – 7906
    Beta strandi797 – 8048
    Turni807 – 8137
    Helixi815 – 8173
    Beta strandi818 – 8214
    Beta strandi824 – 8263
    Beta strandi836 – 8394
    Helixi845 – 8484
    Beta strandi855 – 8628
    Beta strandi869 – 8757
    Helixi878 – 8803
    Beta strandi881 – 8833
    Helixi885 – 8928
    Beta strandi894 – 8963
    Beta strandi904 – 9107
    Beta strandi924 – 93613
    Beta strandi938 – 9447
    Beta strandi946 – 9483
    Beta strandi950 – 9545
    Beta strandi957 – 9626
    Beta strandi964 – 9718
    Beta strandi980 – 98910
    Beta strandi991 – 9955
    Helixi997 – 10015
    Turni1002 – 10043
    Beta strandi1005 – 10084
    Beta strandi1010 – 10145

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4ADGX-ray2.18A/B/C583-1018[»]
    4ADIX-ray1.80A/B/C583-1018[»]
    4ADJX-ray1.94A/B/C583-1018[»]
    4B3VX-ray1.98A/B/C583-1018[»]
    4HARX-ray2.66A/B/C/D/E/F127-277[»]
    4HBEX-ray2.30A/B127-277[»]
    4HBOX-ray3.24A/B/C/D/E147-277[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini301 – 534234ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini556 – 58227CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini583 – 1028446ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1050 – 106314CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei535 – 55521Helical; Note=Golgi retention signalSequence AnalysisAdd
    BLAST
    Transmembranei1029 – 104921Helical; Note=Endoplasmic reticulum retention signalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 6940Human C1QBP/SF2P32-bindingAdd
    BLAST

    Domaini

    The signal peptide at the C-terminus remains bound to the mature capsid protein. It may have a role as an anchor peptide, localizing the capsid assembly at the Golgi complex, where budding occurs.

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    InterProiIPR008819. Rubella_Capsid.
    IPR008820. Rubella_E1.
    IPR008821. Rubella_E2.
    [Graphical view]
    PfamiPF05750. Rubella_Capsid. 1 hit.
    PF05748. Rubella_E1. 1 hit.
    PF05749. Rubella_E2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08563-1 [UniParc]FASTAAdd to Basket

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    MASTTPITME DLQKALEAQS RALRAGLAAG ASQSRRPRPP RQRDSSTSGD     50
    DSGRDSGGPR RRRGNRGRGQ RKDWSRAPPP PEERQESRSQ TPAPKPSRAP 100
    PQQPQPPRMQ TGRGGSAPRP ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT 150
    EACVTSWLWS EGEGAVFYRV DLHFTNLGTP PLDEDGRWDP ALMYNPCGPE 200
    PPAHVVRAYN QPAGDVRGVW GKGERTYAEQ DFRVGGTRWH RLLRMPVRGL 250
    DGDTAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL AAVAVGTARA 300
    GLQPRADMAA PPMPPQPPRA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH 350
    HRNASDVLPG HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA 400
    TPTSLTTAAN STTAATPATA PPPCHAGLND SCGGFLSGCG PMRLRHGADT 450
    RCGRLICGLS TTAQYPPTRF GCAMRWGLPP WELVVLTARP EDGWTCRGVP 500
    AHPGTRCPEL VSPMGRATCS PASALWLATA NALSLDHAFA AFVLLVPWVL 550
    IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQTP 600
    VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPT 650
    APCARIWNGT QRACTFWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACE 700
    VEPAFGHSDA ACWGFPTDTV MSVFALASYV QHPHKTVRVK FHTETRTVWQ 750
    LSVAGVSCNV TTEHPFCNTP HGQLEVQVPP DPGDLVEYIM NYTGNQQSRW 800
    GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV DADDPLLRTA 850
    PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP 900
    PGPLGLKFKT VRPVALPRAL APPRNVRVTG CYQCGTPALV EGLAPGGGNC 950
    HLTVNGEDVG AFPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ 1000
    SFTGVVYGTH TTAVSETRQT WAEWAAAHWW QLTLGAICAL LLAGLLACCA 1050
    KCLYYLRGAI APR 1063
    Length:1,063
    Mass (Da):114,736
    Last modified:May 30, 2006 - v2
    Checksum:iB546067276483ECB
    GO

    Sequence cautioni

    The sequence CAA28880.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 6928QRDSS…NRGRG → HARLQHLPEMTPAVTPEGPA PPRTGAW in CAA28880. (PubMed:3562245)CuratedAdd
    BLAST
    Sequence conflicti175 – 1751T → I in CAA28880. (PubMed:3562245)Curated
    Sequence conflicti445 – 47127RHGAD…PTRFG → PTALTPGAVGDLRAVHHRPV PAYPVC in CAA28880. (PubMed:3562245)CuratedAdd
    BLAST
    Sequence conflicti485 – 4851V → I in CAA28880. (PubMed:3562245)Curated
    Sequence conflicti562 – 57716RGAAA…LQGYN → PAPPPPSPQSSCRGTT in CAA28880. (PubMed:3562245)CuratedAdd
    BLAST
    Sequence conflicti993 – 9942RV → GH in CAA28880. (PubMed:3562245)Curated
    Sequence conflicti995 – 106369Missing in CAA28880. (PubMed:3562245)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti272 – 2721H → R in strain: Isolate HPV77 vaccine.
    Natural varianti411 – 4111S → Y in strain: Isolate HPV77 vaccine.
    Natural varianti412 – 4121T → I in strain: Isolate HPV77 vaccine.
    Natural varianti413 – 4131T → A in strain: Isolate HPV77 vaccine.
    Natural varianti609 – 6091R → G in strain: Isolate HPV77 vaccine.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05259 mRNA. Translation: CAA28880.1. Sequence problems.
    M30776 Genomic RNA. Translation: AAA47421.1. Sequence problems.
    PIRiA27505. GNWVR3.
    JQ0087. GNWV77.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05259 mRNA. Translation: CAA28880.1 . Sequence problems.
    M30776 Genomic RNA. Translation: AAA47421.1 . Sequence problems.
    PIRi A27505. GNWVR3.
    JQ0087. GNWV77.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4ADG X-ray 2.18 A/B/C 583-1018 [» ]
    4ADI X-ray 1.80 A/B/C 583-1018 [» ]
    4ADJ X-ray 1.94 A/B/C 583-1018 [» ]
    4B3V X-ray 1.98 A/B/C 583-1018 [» ]
    4HAR X-ray 2.66 A/B/C/D/E/F 127-277 [» ]
    4HBE X-ray 2.30 A/B 127-277 [» ]
    4HBO X-ray 3.24 A/B/C/D/E 147-277 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR008819. Rubella_Capsid.
    IPR008820. Rubella_E1.
    IPR008821. Rubella_E2.
    [Graphical view ]
    Pfami PF05750. Rubella_Capsid. 1 hit.
    PF05748. Rubella_E1. 1 hit.
    PF05749. Rubella_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and in vitro expression of rubella virus 24S subgenomic messenger RNA encoding the structural proteins E1, E2 and C."
      Clarke D.M., Loo T.W., Hui I., Chong P., Gillam S.
      Nucleic Acids Res. 15:3041-3057(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Expression of rubella virus cDNA coding for the structural proteins."
      Clarke D.M., Loo T.W., McDonald H., Gillam S.
      Gene 65:23-30(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Nucleotide sequence of the 24S subgenomic messenger RNA of a vaccine strain (HPV77) of rubella virus: comparison with a wild-type strain (M33)."
      Zheng D., Dickens L., Liu T.Y., Nakhasi H.L.
      Gene 82:343-349(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate HPV77 vaccine.
    4. "Analysis of rubella virus E1 glycosylation mutants expressed in COS cells."
      Hobman T.C., Qiu Z., Chaye H., Gillam S.
      Virology 181:768-772(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION OF E1 ENVELOPE GLYCOPROTEIN.
    5. "The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex."
      Hobman T.C., Woodward L., Farquhar M.G.
      J. Cell Biol. 121:269-281(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION OF E1 AND E2 ENVELOPE GLYCOPROTEINS.
    6. "Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal."
      Hobman T.C., Woodward L., Farquhar M.G.
      Mol. Biol. Cell 6:7-20(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Dimerization of rubella virus capsid protein is not required for virus particle formation."
      Lee J.Y., Hwang D., Gillam S.
      Virology 216:223-227(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-153.
    8. "Characterization of an endoplasmic reticulum retention signal in the rubella virus E1 glycoprotein."
      Hobman T.C., Lemon H.F., Jewell K.
      J. Virol. 71:7670-7680(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Effects of mutations in the rubella virus E1 glycoprotein on E1-E2 interaction and membrane fusion activity."
      Yang D., Hwang D., Qiu Z., Gillam S.
      J. Virol. 72:8747-8755(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-664; GLY-675 AND PRO-686.
    10. "Mutational analysis, using a full-length rubella virus cDNA clone, of rubella virus E1 transmembrane and cytoplasmic domains required for virus release."
      Yao J., Gillam S.
      J. Virol. 73:4622-4630(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-1046; CYS-1048; CYS-1049; CYS-1052 AND LEU-1053.
    11. "Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria."
      Beatch M.D., Hobman T.C.
      J. Virol. 74:5569-5576(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN C1QBP.
    12. "A single-amino-acid substitution of a tyrosine residue in the rubella virus E1 cytoplasmic domain blocks virus release."
      Yao J., Gillam S.
      J. Virol. 74:3029-3036(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-1052; LEU-1053; TYR-1054; TYR-1055; LEU-1056; ARG-1057; GLY-1058; ALA-1059; ILE-1060; ALA-1061; PRO-1062 AND ARG-1063.
    13. "Mutations in the E1 hydrophobic domain of rubella virus impair virus infectivity but not virus assembly."
      Qiu Z., Yao J., Cao H., Gillam S.
      J. Virol. 74:6637-6642(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-675 AND PRO-686.
    14. "Rubella virus capsid protein induces apoptosis in transfected RK13 cells."
      Duncan R., Esmaili A., Law L.M., Bertholet S., Hough C., Hobman T.C., Nakhasi H.L.
      Virology 275:20-29(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF CAPSID PROTEIN.
    15. "Rubella virus E2 signal peptide is required for perinuclear localization of capsid protein and virus assembly."
      Law L.M., Duncan R., Esmaili A., Nakhasi H.L., Hobman T.C.
      J. Virol. 75:1978-1983(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF CAPSID PROTEIN.
    16. "Effect of site-directed asparagine to isoleucine substitutions at the N-linked E1 glycosylation sites on rubella virus viability."
      Ramanujam M., Hofmann J., Nakhasi H.L., Atreya C.D.
      Virus Res. 81:151-156(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-658; ASN-759 AND ASN-791, MUTAGENESIS OF ASN-658; ASN-759 AND ASN-791.
    17. "Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication."
      Law L.M., Everitt J.C., Beatch M.D., Holmes C.F., Hobman T.C.
      J. Virol. 77:1764-1771(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-46, RNA-BINDING.
    18. "Interactions between rubella virus capsid and host protein p32 are important for virus replication."
      Beatch M.D., Everitt J.C., Law L.J., Hobman T.C.
      J. Virol. 79:10807-10820(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 35-ARG--ARG-43 AND 60-ARG--ARG-68.

    Entry informationi

    Entry nameiPOLS_RUBVM
    AccessioniPrimary (citable) accession number: P08563
    Secondary accession number(s): P21480
    , Q86373, Q86374, Q86375
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Structural polyprotein is translated from a subgenomic RNA synthesized during togaviruses replication.

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

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

    External Data

    Dasty 3