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P08563

- POLS_RUBVM

UniProt

P08563 - POLS_RUBVM

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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

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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini301 – 534234ExtracellularSequence AnalysisAdd
BLAST
Transmembranei535 – 55521Helical; Note=Golgi retention signalSequence AnalysisAdd
BLAST
Topological domaini556 – 58227CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini583 – 1028446ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1029 – 104921Helical; Note=Endoplasmic reticulum retention signalSequence AnalysisAdd
BLAST
Topological domaini1050 – 106314CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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. 1 Publication
Mutagenesisi658 – 6581N → I: Complete loss of infectivity. 1 Publication
Mutagenesisi664 – 6641C → S: Prevents E1-E2 heterodimer formation, and subsequent transport of to the plasma membrane. Complete loss of fusion activity in vitro. 1 Publication
Mutagenesisi675 – 6751G → D: Complete loss of fusion activity in vitro. 90% loss of infectivity in vivo. No effect on virus assembly. 2 Publications
Mutagenesisi686 – 6861P → G: 99.9% loss of infectivity. No effect on virus assembly. No effect on fusion activity in vitro. 2 Publications
Mutagenesisi759 – 7591N → I: No effect on infectivity. 1 Publication
Mutagenesisi791 – 7911N → I: Complete loss of infectivity. 1 Publication
Mutagenesisi1046 – 10461L → A: No effect on virus production from infected cell. 1 Publication
Mutagenesisi1048 – 10481C → A: No effect on virus production from infected cell. 1 Publication
Mutagenesisi1049 – 10491C → A: No effect on virus production from infected cell. 1 Publication
Mutagenesisi1052 – 10521C → A: No effect on virus production from infected cell. 2 Publications
Mutagenesisi1053 – 10531L → A: 90% loss of virus production from infected cell. 2 Publications
Mutagenesisi1054 – 10541Y → A: Complete loss of virus production from infected cell. 1 Publication
Mutagenesisi1055 – 10551Y → S: Complete loss of virus production from infected cell. 1 Publication
Mutagenesisi1056 – 10561L → A: 90% loss of virus production from infected cell. 1 Publication
Mutagenesisi1057 – 10571R → S: 98% loss of virus production from infected cell. 1 Publication
Mutagenesisi1058 – 10581G → C: 98% loss of virus production from infected cell. 1 Publication
Mutagenesisi1059 – 10591A → S: 90% loss of virus production from infected cell. 1 Publication
Mutagenesisi1060 – 10601I → V: No effect on virus production from infected cell. 1 Publication
Mutagenesisi1061 – 10611A → S: 90% loss of virus production from infected cell. 1 Publication
Mutagenesisi1062 – 10621P → S: 90% loss of virus production from infected cell. 1 Publication
Mutagenesisi1063 – 10631R → S: 98% loss of virus production from infected cell. 1 Publication

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 host1 Publication
Disulfide bondi699 ↔ 712By similarity
Disulfide bondi758 ↔ 767By similarity
Glycosylationi759 – 7591N-linked (GlcNAc...); by host1 Publication
Glycosylationi791 – 7911N-linked (GlcNAc...); by host1 Publication
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 – 16010Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi167 – 17610Combined sources
Helixi190 – 1934Combined sources
Helixi203 – 2097Combined sources
Beta strandi216 – 2216Combined sources
Beta strandi227 – 2348Combined sources
Beta strandi237 – 2448Combined sources
Beta strandi585 – 5895Combined sources
Beta strandi599 – 6013Combined sources
Beta strandi603 – 62119Combined sources
Beta strandi625 – 63410Combined sources
Turni641 – 6477Combined sources
Helixi650 – 6578Combined sources
Beta strandi659 – 67012Combined sources
Beta strandi672 – 6743Combined sources
Beta strandi676 – 6783Combined sources
Helixi681 – 6833Combined sources
Helixi689 – 6946Combined sources
Beta strandi698 – 7036Combined sources
Beta strandi716 – 7183Combined sources
Beta strandi721 – 7299Combined sources
Helixi733 – 7353Combined sources
Beta strandi737 – 75317Combined sources
Beta strandi756 – 7605Combined sources
Beta strandi766 – 7683Combined sources
Beta strandi770 – 7778Combined sources
Beta strandi785 – 7906Combined sources
Beta strandi797 – 8048Combined sources
Turni807 – 8137Combined sources
Helixi815 – 8173Combined sources
Beta strandi818 – 8214Combined sources
Beta strandi824 – 8263Combined sources
Beta strandi836 – 8394Combined sources
Helixi845 – 8484Combined sources
Beta strandi855 – 8628Combined sources
Beta strandi869 – 8757Combined sources
Helixi878 – 8803Combined sources
Beta strandi881 – 8833Combined sources
Helixi885 – 8928Combined sources
Beta strandi894 – 8963Combined sources
Beta strandi904 – 9107Combined sources
Beta strandi924 – 93613Combined sources
Beta strandi938 – 9447Combined sources
Beta strandi946 – 9483Combined sources
Beta strandi950 – 9545Combined sources
Beta strandi957 – 9626Combined sources
Beta strandi964 – 9718Combined sources
Beta strandi980 – 98910Combined sources
Beta strandi991 – 9955Combined sources
Helixi997 – 10015Combined sources
Turni1002 – 10043Combined sources
Beta strandi1005 – 10084Combined sources
Beta strandi1010 – 10145Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

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

« Hide

        10         20         30         40         50
MASTTPITME DLQKALEAQS RALRAGLAAG ASQSRRPRPP RQRDSSTSGD
60 70 80 90 100
DSGRDSGGPR RRRGNRGRGQ RKDWSRAPPP PEERQESRSQ TPAPKPSRAP
110 120 130 140 150
PQQPQPPRMQ TGRGGSAPRP ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT
160 170 180 190 200
EACVTSWLWS EGEGAVFYRV DLHFTNLGTP PLDEDGRWDP ALMYNPCGPE
210 220 230 240 250
PPAHVVRAYN QPAGDVRGVW GKGERTYAEQ DFRVGGTRWH RLLRMPVRGL
260 270 280 290 300
DGDTAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL AAVAVGTARA
310 320 330 340 350
GLQPRADMAA PPMPPQPPRA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH
360 370 380 390 400
HRNASDVLPG HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA
410 420 430 440 450
TPTSLTTAAN STTAATPATA PPPCHAGLND SCGGFLSGCG PMRLRHGADT
460 470 480 490 500
RCGRLICGLS TTAQYPPTRF GCAMRWGLPP WELVVLTARP EDGWTCRGVP
510 520 530 540 550
AHPGTRCPEL VSPMGRATCS PASALWLATA NALSLDHAFA AFVLLVPWVL
560 570 580 590 600
IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQTP
610 620 630 640 650
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPT
660 670 680 690 700
APCARIWNGT QRACTFWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACE
710 720 730 740 750
VEPAFGHSDA ACWGFPTDTV MSVFALASYV QHPHKTVRVK FHTETRTVWQ
760 770 780 790 800
LSVAGVSCNV TTEHPFCNTP HGQLEVQVPP DPGDLVEYIM NYTGNQQSRW
810 820 830 840 850
GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV DADDPLLRTA
860 870 880 890 900
PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP
910 920 930 940 950
PGPLGLKFKT VRPVALPRAL APPRNVRVTG CYQCGTPALV EGLAPGGGNC
960 970 980 990 1000
HLTVNGEDVG AFPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ
1010 1020 1030 1040 1050
SFTGVVYGTH TTAVSETRQT WAEWAAAHWW QLTLGAICAL LLAGLLACCA
1060
KCLYYLRGAI APR
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 86 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