Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q05127 (VP35_EBOZM)

Entry version 98 (02 Jun 2021)
Sequence version 1 (01 Feb 1994)
Previous versions | rss
Add a publicationFeedback
Protein

Polymerase cofactor VP35

Gene

VP35

Organism
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
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

Plays an essential role in viral RNA synthesis and also a role in suppressing innate immune signaling (PubMed:11027311).

Acts as a polymerase cofactor in the RNA polymerase transcription and replication complexes (PubMed:9971816, PubMed:16495261, PubMed:24495995).

Serves as nucleoprotein/NP monomer chaperone prior to the formation of the large oligomeric RNA-bound complexes (By similarity).

Regulates RNA synthesis by modulating NP-RNA interactions and interacting with DYNLL1 (PubMed:25741013).

VP35-NP interaction controls the switch between RNA-bound NP and free NP and thus the switch between genome replication and genome packaging into the nucleocapsid (PubMed:25865894).

Prevents establishment of cellular antiviral state, thereby suppressing host DC maturation (PubMed:26962215).

Acts by inhibiting host DDX58/RIG-I activation both by shielding dsRNA from detection and by preventing PRKRA binding to DDX58 (PubMed:23870315).

Blocks virus-induced phosphorylation and activation of interferon regulatory factor 3/IRF3, a transcription factor critical for the induction of interferons alpha and beta (PubMed:12829834).

This blockage is produced through the interaction with and inhibition of host IKBKE and TBK1, producing a strong inhibition of the phosphorylation and activation of IRF3 (PubMed:12829834).

Also inhibits the antiviral effect mediated by the host interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR (PubMed:17065211).

Increases PIAS1-mediated SUMOylation of IRF7, thereby repressing interferon transcription (PubMed:19557165).

Also acts as a suppressor of RNA silencing by interacting with host DICER1, TARBP2/TRBP and PRKRA/PACT (By similarity).

As a dimer, binds and sequesters dsRNA contributing to the inhibition of interferon production (By similarity).

By similarity11 Publications

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Suppressor of RNA silencing
Biological processHost-virus interaction, Inhibition of host IKBKE by virus, Inhibition of host innate immune response by virus, Inhibition of host IRF7 by virus, Inhibition of host RLR pathway by virus, Inhibition of host TBK1 by virus, Inhibition of host TLR pathway by virus, Interferon antiviral system evasion, Transcription, Viral immunoevasion, Viral RNA replication

<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%5Fand%5Ftaxonomy%5Fsection">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:
Polymerase cofactor VP35
Alternative name(s):
Ebola VP351 Publication
Short name:
eVP351 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:VP35
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiZaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri128952 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiViruses › Riboviria › Orthornavirae › Negarnaviricota › Haploviricotina › Monjiviricetes › Mononegavirales › Filoviridae › Ebolavirus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 hostiEpomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]
Homo sapiens (Human) [TaxID: 9606]
Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000007209 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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
  • UP000109874 Componenti: Genome
  • UP000149419 Componenti: Genome
  • UP000150973 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

Keywords - Cellular componenti

Host cytoplasm, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi90 – 93LASL → AASA: Complete loss of homotrimerization; when associated with A-107. 1 Publication4
Mutagenesisi107L → A: Complete loss of homotrimerization; when associated with 90-AASA-93. 1 Publication1
Mutagenesisi187S → A: Impaired viral replication. 1 Publication1
Mutagenesisi187S → D: No effect on viral replication. 1 Publication1
Mutagenesisi210T → A: Loss of viral transcription and reduced binding to the nucleoprotein. 1 Publication1
Mutagenesisi210T → D: No effect on viral transcription and binding to the nucleoprotein. 1 Publication1
Mutagenesisi239F → A: Complete loss of interaction with host PRKRA and subsequent immune response inhibition. 1 Publication1
Mutagenesisi305R → A: No effect on IRF3 promoter inhibition. 1 Publication1
Mutagenesisi309K → A: Partial loss of IRF3 promoter inhibition. Complete loss of dsRNA-binding. 2 Publications1
Mutagenesisi312R → A: Complete loss of IRF3 promoter inhibition; dsRNA-binding and interaction with host PRKRA. 3 Publications1
Mutagenesisi317S → A: Impaired viral replication. 1 Publication1
Mutagenesisi317S → D: No effect on viral replication. 1 Publication1
Mutagenesisi319K → A: Complete loss of dsRNA binding activity; when associated with A-322. 1 Publication1
Mutagenesisi322R → A: Complete loss of dsRNA binding activity; when associated with A-319. 1 Publication1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002221611 – 340Polymerase cofactor VP35Add BLAST340

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 residuei187Phosphoserine; by host2 Publications1
Modified residuei205Phosphoserine; by host2 Publications1
Modified residuei206Phosphothreonine; by host2 Publications1
Modified residuei207Phosphothreonine; by host1 Publication1
Modified residuei208Phosphoserine; by host2 Publications1
Modified residuei210Phosphothreonine; by host1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki309Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei310Phosphoserine; by host1 Publication1
Modified residuei317Phosphoserine; by host2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylated by host IKBKE (PubMed:19153231). Phosphorylation contributes to efficient viral replication and transcription (PubMed:31694758, PubMed:31562565).3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q05127

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity). Homooligomer; via the coiled coil domain (PubMed:16095644).

Interacts with nucleoprotein NP and polymerase L; VP35 bridges L and NP and allows the formation of the polymerase complex (PubMed:25865894) (Probable).

Also interacts with VP30; this interaction is regulated by VP30 phosphorylation (PubMed:23493393).

Interacts with host IKBKE and TBK1; the interactions lead to inhibition of cellular antiviral response by blocking necessary interactions of IKBKE and TBK1 with their substrate IRF3.

Interacts with host DYNLL1; this interaction stabilizes VP35 N-terminal oligomerization domain, enhances viral RNA synthesis but does not participate in suppressing the host innate immune response (PubMed:19403681, PubMed:25741013).

Interacts with host PRKRA; this interaction inhibits the interaction between DDX58 and PRKRA.

Interacts with dsRNA (PubMed:19122151, PubMed:20071589, PubMed:23870315).

Interacts with host TRIM6; this interaction plays an important role in promoting efficient viral replication (PubMed:28679761).

Interacts with host STAU1 (PubMed:30301857).

Interacts with host IRF7, PIAS1 and UBE2I/UBC9; these interactions mediate the sumoylation of IRF7 and contribute to the inhibition of IFN-type I production (PubMed:19557165).

Interacts with host DICER1; this interaction prevents TARBP2/TRBP binding to DICER1 and thus allows the virus to counteract host RNA silencing (By similarity).

Interacts with host TARBP2/TRBP and PRKRA/PACT; these interactions prevent TARBP2 and PRKRA binding to DICER1 and thus allows the virus to counteract host RNA silencing (By similarity).

By similarity1 Publication11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-48771N

Protein interaction database and analysis system

More...IntActi		Q05127, 62 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

Secondary structure

1340
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		Q05127

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q05127

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini215 – 340VP35 IIDPROSITE-ProRule annotationAdd BLAST126

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>Regioni1 – 49Chaperones the nucleoproteinBy similarityAdd BLAST49
Regioni1 – 24DisorderedSequence analysisAdd BLAST24
Regioni33 – 48Disordered1 PublicationAdd BLAST16
Regioni33 – 48NP binding region1 PublicationAdd BLAST16
Regioni83 – 145HomooligomerizationBy similarityAdd BLAST63

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili96 – 116Sequence analysisAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi71 – 75Required for host DYNLL1 interaction1 Publication5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 21Polar residuesSequence analysisAdd BLAST21

<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

The interferon inhibitory domain (IID) binds dsRNA.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the filoviridae polymerase cofactor VP35 family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Family and domain databases

Database of protein disorder

More...DisProti		DP00998

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.8.950, 1 hit
2.10.10.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002953, Filo_VP35
IPR031163, VP35_IID
IPR043061, VP35_IID_b-sht
IPR043060, VP35_IID_hlx

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02097, Filo_VP35, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF018326, VP35_FiloV, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01240, FILOVP35

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51735, VP35_IID, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q05127-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTRTKGRGH TAATTQNDRM PGPELSGWIS EQLMTGRIPV SDIFCDIENN 
        60         70         80         90        100
PGLCYASQMQ QTKPNPKTRN SQTQTDPICN HSFEEVVQTL ASLATVVQQQ 
       110        120        130        140        150
TIASESLEQR ITSLENGLKP VYDMAKTISS LNRVCAEMVA KYDLLVMTTG 
       160        170        180        190        200
RATATAAATE AYWAEHGQPP PGPSLYEESA IRGKIESRDE TVPQSVREAF 
       210        220        230        240        250
NNLNSTTSLT EENFGKPDIS AKDLRNIMYD HLPGFGTAFH QLVQVICKLG 
       260        270        280        290        300
KDSNSLDIIH AEFQASLAEG DSPQCALIQI TKRVPIFQDA APPVIHIRSR 
       310        320        330        340
GDIPRACQKS LRPVPPSPKI DRGWVCVFQL QDGKTLGLKI
Length:340
Mass (Da):37,362
Last modified:February 1, 1994 - 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:iB171C7FDBB5B1FBD
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 varianti12A → V in strain: Isolate mouse-adapted. 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
X61274 Genomic RNA Translation: CAA43578.1
L11365 Genomic RNA Translation: AAB81002.1
AF086833 Genomic RNA Translation: AAD14582.1
AF272001 Genomic RNA Translation: AAG40165.1
AY142960 Genomic RNA Translation: AAN37505.1
AF499101 Genomic RNA Translation: AAM76032.1

NCBI Reference Sequences

More...RefSeqi		NP_066244.1, NC_002549.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		911827

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:911827

<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
X61274 Genomic RNA Translation: CAA43578.1
L11365 Genomic RNA Translation: AAB81002.1
AF086833 Genomic RNA Translation: AAD14582.1
AF272001 Genomic RNA Translation: AAG40165.1
AY142960 Genomic RNA Translation: AAN37505.1
AF499101 Genomic RNA Translation: AAM76032.1
RefSeqiNP_066244.1, NC_002549.1

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
3FKEX-ray1.40A/B215-340[»]
3L25X-ray2.00A/B/D/E215-340[»]
3L26X-ray2.40A/B215-340[»]
3L27X-ray1.95A/B/C/D215-340[»]
3L28X-ray2.40A/B/C/D/E/F215-338[»]
3L29X-ray1.70A/B215-340[»]
4IBBX-ray1.75A/B215-340[»]
4IBCX-ray1.74A/B215-340[»]
4IBDX-ray1.84A/B215-340[»]
4IBEX-ray1.95A/B215-340[»]
4IBFX-ray2.29A/B215-340[»]
4IBGX-ray1.41A/B215-340[»]
4IBIX-ray1.47A/B215-340[»]
4IBJX-ray1.54A/B215-340[»]
4IBKX-ray1.85A/B215-340[»]
4IJEX-ray1.90A/B/C/D218-340[»]
4IJFX-ray2.51A218-340[»]
4YPIX-ray3.71E/F/G/H20-47[»]
4ZTAX-ray2.40A15-59[»]
4ZTGX-ray2.80A15-59[»]
4ZTIX-ray2.40A/B15-59[»]
6GBOX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L82-145[»]
6GBPX-ray3.49A/B/C/D/E/F/G/H/I/J/K/L82-145[»]
SMRiQ05127
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-48771N
IntActiQ05127, 62 interactors

PTM databases

iPTMnetiQ05127

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		Q05127, 5 sequenced antibodies

The DNASU plasmid repository

More...DNASUi		911827

Genome annotation databases

GeneIDi911827
KEGGivg:911827

Miscellaneous databases

EvolutionaryTraceiQ05127

Family and domain databases

DisProtiDP00998
Gene3Di1.10.8.950, 1 hit
2.10.10.70, 1 hit
InterProiView protein in InterPro
IPR002953, Filo_VP35
IPR031163, VP35_IID
IPR043061, VP35_IID_b-sht
IPR043060, VP35_IID_hlx
PfamiView protein in Pfam
PF02097, Filo_VP35, 1 hit
PIRSFiPIRSF018326, VP35_FiloV, 1 hit
PRINTSiPR01240, FILOVP35
PROSITEiView protein in PROSITE
PS51735, VP35_IID, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiVP35_EBOZM
<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: Q05127
Secondary accession number(s): Q77LU7, Q8JS63
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 2, 2021
This is version 98 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again