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Protein

Structural polyprotein

Gene
N/A
Organism
Rubella virus (strain Therien) (RUBV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Capsid protein: Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. 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. 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.By similarity
Spike glycoprotein E2: 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. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement.By similarity
Spike glycoprotein E1: Class II viral fusion protein (By similarity). 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 (PubMed:15557740). This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1 modulates virus release. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (By similarity).By similarity1 Publication

Miscellaneous

Structural polyprotein: Translated from a subgenomic RNA synthesized during togaviruses replication.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi670CalciumBy similarity1
Metal bindingi671Calcium; via carbonyl oxygenBy similarity1
Metal bindingi718CalciumBy similarity1
Metal bindingi719Calcium; via carbonyl oxygenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding
Biological processClathrin-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
LigandCalcium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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):
E2 envelope glycoprotein
Alternative name(s):
E1 envelope glycoprotein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRubella virus (strain Therien) (RUBV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri11045 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeRubivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000571 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Capsid protein :
Spike glycoprotein E2 :
Spike glycoprotein E1 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini301 – 534ExtracellularSequence analysisAdd BLAST234
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei535 – 555Helical; Note=Golgi retention signalBy similarityAdd BLAST21
Topological domaini556 – 582CytoplasmicSequence analysisAdd BLAST27
Topological domaini583 – 1028ExtracellularSequence analysisAdd BLAST446
Transmembranei1029 – 1049Helical; Note=Endoplasmic reticulum retention signalBy similarityAdd BLAST21
Topological domaini1050 – 1063ExtracellularSequence analysisAdd BLAST14

GO - Cellular componenti

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000413081 – 300Capsid proteinAdd BLAST300
ChainiPRO_0000041309301 – 582Spike glycoprotein E2Add BLAST282
ChainiPRO_0000041310583 – 1063Spike glycoprotein E1Add BLAST481

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei46Phosphoserine; by hostBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi153 ↔ 197By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi353N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi371N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi410N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi429N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi590 ↔ 5951 Publication
Disulfide bondi619 ↔ 8241 Publication
Disulfide bondi641 ↔ 6531 Publication
Glycosylationi658N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi699 ↔ 7121 Publication
Disulfide bondi758 ↔ 7671 Publication
Glycosylationi759N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi791N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi807 ↔ 8171 Publication
Disulfide bondi931 ↔ 9341 Publication
Disulfide bondi950 ↔ 9831 Publication
Glycosylationi1011O-linked (GalNAc...) threonine; by hostBy similarity1
Glycosylationi1012O-linked (GalNAc...) threonine; by hostBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Two signal peptidase-mediated cleavages within the polyprotein produce the structural proteins capsid, E2, and E1. The E2 signal peptide remains attached to the C-terminus of the capsid protein after cleavage by the signal peptidase. Another signal peptide at E2 C-terminus directs E1 to the ER, with a similar mechanism.By similarity
Spike glycoprotein E1: Contains three N-linked oligosaccharides.By similarity
Capsid is phosphorylated on Ser-46 by host. This phosphorylation negatively regulates capsid protein RNA-binding activity (By similarity). Dephosphorylated by human PP1A (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei300 – 301Cleavage; by host signal peptidaseSequence analysis2
Sitei582 – 583Cleavage; by host signal peptidaseSequence analysis2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Capsid protein: Homodimer; further assembles into homooligomer. Capsid protein: Interacts with human C1QBP. Capsid protein: Interacts (via N-terminus) with protease/methyltransferase p150. Spike glycoprotein E1: Heterodimer with spike glycoprotein E2. Spike glycoprotein E2: Heterodimer with spike glycoprotein E1.By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P07566, 2 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P07566

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 69Human C1QBP/SF2P32-bindingBy similarityAdd BLAST40
Regioni279 – 300Functions as E2 signal peptideBy similarityAdd BLAST22
Regioni563 – 582Functions as E1 signal peptideBy similarityAdd BLAST20

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Structural polyprotein: Contains two internal signal peptides that are necessary for directing translocation of the glycoproteins into the lumen of the endoplasmic reticulum.By similarity
Capsid protein: The capsid protein is probably attached to the viral membrane through the E2 signal peptide. This domain is also required for the localization of the capsid protein to the juxtanuclear region and subsequent virus assembly at the Golgi complex.By similarity

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
VOG0900007P

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008819 Rubella_Capsid
IPR008820 Rubella_E1
IPR008821 Rubella_E2

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05750 Rubella_Capsid, 1 hit
PF05748 Rubella_E1, 1 hit
PF05749 Rubella_E2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P07566-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASTTPITME DLQKALEAQS RALRAELAAG ASQSRRPRPP RQRDSSTSGD
60 70 80 90 100
DSGRDSGGPR RRRGNRGRGQ RRDWSRAPPP PEERQETRSQ 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
DGDSAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL ATVAVGTARA
310 320 330 340 350
GLQPRADMAA PPTLPQPPCA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH
360 370 380 390 400
YRNASDVLPG HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA
410 420 430 440 450
TPTPLTTAAN STTAATPATA PAPCHAGLND SCGGFLSGCG PMRLRHGADT
460 470 480 490 500
RCGRLICGLS TTAQYPPTRF GCAMRWGLPP WELVVLTARP EDGWTCRGVP
510 520 530 540 550
AHPGARCPEL VSPMGRATCS PASALWLATA NALSLDHALA AFVLLVPWVL
560 570 580 590 600
IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQAP
610 620 630 640 650
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPA
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 VRPVALPRTL APPRNVRVTG CYQCGTPALV EGLAPGGGNC
960 970 980 990 1000
HLTVNGEDLG AVPPGKFVTA ALLNTPPPYQ VSCGGESDRA TARVIDPAAQ
1010 1020 1030 1040 1050
SFTGVVYGTH TTAVSETRQT WAEWAAAHWW QLTLGAICAL PLAGLLACCA
1060
KCLYYLRGAI APR
Length:1,063
Mass (Da):114,679
Last modified:August 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF39B475ACA15C7D1
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti87T → S. 1
Natural varianti163E → Q. 1
Natural varianti319C → R. 1
Natural varianti395D → A. 1
Natural varianti545L → S. 1
Natural varianti613K → R. 1
Natural varianti825S → A. 1
Natural varianti959L → V. 1
Natural varianti991T → S. 1
Natural varianti1037I → T. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M15240 Genomic RNA Translation: AAA88529.1
D00242 Genomic RNA Translation: BAA00172.1
D00156 Genomic RNA Translation: BAA28178.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A24309
A29822 GNWVR4

NCBI Reference Sequences

More...
RefSeqi
NP_062884.1, NC_001545.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1502162

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:1502162

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15240 Genomic RNA Translation: AAA88529.1
D00242 Genomic RNA Translation: BAA00172.1
D00156 Genomic RNA Translation: BAA28178.1
PIRiA24309
A29822 GNWVR4
RefSeqiNP_062884.1, NC_001545.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KHEelectron microscopy35.00A/B9-277[»]
5KHFelectron microscopy35.00A/B9-277[»]
SMRiP07566
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07566, 2 interactors

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1502162
KEGGivg:1502162

Phylogenomic databases

OrthoDBiVOG0900007P

Family and domain databases

InterProiView protein in InterPro
IPR008819 Rubella_Capsid
IPR008820 Rubella_E1
IPR008821 Rubella_E2
PfamiView protein in Pfam
PF05750 Rubella_Capsid, 1 hit
PF05748 Rubella_E1, 1 hit
PF05749 Rubella_E2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLS_RUBVT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07566
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: August 1, 1988
Last modified: November 7, 2018
This is version 102 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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