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Entry version 100 (07 Apr 2021)
Sequence version 1 (13 Aug 1987)
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Protein

Protein M2-1

Gene

M2-1

Organism
Human respiratory syncytial virus A (strain A2)
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

Acts as a tetrameric transcription processivity factor that binds in a competitive manner to RNA and the phosphoprotein (P) to prevent premature termination during transcription (PubMed:19386701, PubMed:22675274). Transcription anti-terminator that enhances readthrough of intergenic junctions during viral transcription (PubMed:10364337, PubMed:27194388, PubMed:8552680, PubMed:9420254). Preferentially binds to poly(A)-rich sequences (PubMed:24434552). Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding (PubMed:18579594). Also, can activate host NF-kappa-B through association with host RELA (PubMed:15629770).9 Publications

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>Sitei8Involved in RNA-binding1 Publication1
Sitei9Involved in RNA-binding1 Publication1
Sitei23Involved in RNA-binding1 Publication1
Sitei92Involved in RNA-binding1 Publication1
Sitei151Involved in RNA-binding1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1 – 28C3H1-typePROSITE-ProRule annotation2 PublicationsAdd BLAST28

<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 processActivation of host NF-kappa-B by virus, Host-virus interaction, Transcription, Transcription antitermination, Transcription regulation, Viral transcription
LigandMetal-binding, Zinc

<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:
Protein M2-1
Alternative name(s):
Envelope-associated 22 kDa protein
Transcription antitermination factor M2-11 Publication
Vp241 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:M2-1
<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>OrganismiHuman respiratory syncytial virus A (strain A2)
<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 identifieri11259 [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 lineageiVirusesRiboviriaOrthornaviraeNegarnaviricotaHaploviricotinaMonjiviricetesMononegaviralesPneumoviridaeOrthopneumovirus
<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 hostiHomo sapiens (Human) [TaxID: 9606]
<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
  • UP000181559 <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
  • UP000181262 Componenti: Genome
  • UP000181145 Componenti: Genome
  • UP000007678 Componenti: Genome
  • UP000134464 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, Host nucleus, 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>Mutagenesisi7C → G: More than 95% loss of processivity function. 1 Publication1
Mutagenesisi7C → S: Complete loss of binding to N protein. Loss of phosphorylation. 1 Publication1
Mutagenesisi10E → G: Complete loss of binding to N protein. 1 Publication1
Mutagenesisi15C → G: About 80% loss of processivity function. 1 Publication1
Mutagenesisi15C → S: Complete loss of binding to N protein. 1 Publication1
Mutagenesisi16 – 17LN → SR: 99% loss of processivity function. 1 Publication2
Mutagenesisi16L → S: 97% loss of processivity function. 1 Publication1
Mutagenesisi17N → R: 94% loss of processivity function. 1 Publication1
Mutagenesisi21C → G: About 80% loss of processivity function. 1 Publication1
Mutagenesisi58S → A: Complete loss of phosphorylation. 1 Publication1
Mutagenesisi61S → A: About 50% loss of phosphorylation. 1 Publication1
Mutagenesisi91T → D: Slight loss of RNA-binding. 1 Publication1
Mutagenesisi92K → A: Loss of RNA-binding. 1 Publication1
Mutagenesisi92K → D: Loss of RNA-binding. No effect on M2-1 association with inclusion bodies. 1 Publication1
Mutagenesisi126R → D: Loss of M2-1 association with inclusion bodies. No effect on RNA-binding. 1 Publication1
Mutagenesisi130T → D: Loss of M2-1 association with inclusion bodies. No effect on RNA-binding. 1 Publication1
Mutagenesisi148L → A: Loss of M2-1 association with inclusion bodies. No effect on of RNA-binding. 1 Publication1
Mutagenesisi150K → A: Almost no loss of RNA-binding. 1 Publication1
Mutagenesisi150K → D: Loss of RNA-binding. No effect on M2-1 association with inclusion bodies. 1 Publication1
Mutagenesisi151R → D: Loss of RNA-binding in Ref.20, but not in Ref.31. No effect on M2-1 association with inclusion bodies. 2 Publications1
Mutagenesisi151R → K: Confers virus resistance to cyclopamine in vitro. 1 Publication1
Mutagenesisi160T → D: Loss of M2-1 association with inclusion bodies. No effect on RNA-binding. 1 Publication1
Mutagenesisi163N → D: Loss of M2-1 association with inclusion bodies. No effect on RNA-binding. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4105717

<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_00001428401 – 194Protein M2-1Add BLAST194

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 residuei58Phosphoserine; by host1 Publication1
Modified residuei61Phosphoserine; by host1 Publication1

<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 in infected cells (PubMed:11711610, PubMed:3339328, PubMed:10846068, PubMed:29489893). Only dephosphorylated M2-1 is competent for viral mRNA binding (PubMed:29489893). Cyclic turnover of phosphorylation-dephosphorylation of M2-1 is required for efficient viral transcription (PubMed:29489893).4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P04545

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P04545

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated by cyclopamine (PubMed:27194388). Expressed early in the viral replication cycle (PubMed:10846068).2 Publications

<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

Homotetramer (PubMed:19386701, PubMed:29372904, PubMed:32697936). The homotetramer interacts with RNA (PubMed:32697936, PubMed:22675274).

Interacts with the phosphoprotein (P); this interaction is required for protein M2-1 function, localization in host inclusion bodies (PubMed:12970453, PubMed:17098979, PubMed:19386701, PubMed:22675274, PubMed:29489893, PubMed:22978633). Formation of a complex host PP1/M2-1/P allows P to target host PP1 phosphatase to the M2-1 substrate (PubMed:29489893).

Interacts with the nucleoprotein (N) (PubMed:10846068, PubMed:22675274).

Interacts with the matrix protein (M); this interaction directs M localization to cytoplasmic inclusions comprising viral proteins L, N, P, and M2-1 and mediates M association with the nucleocapsid (PubMed:18579594).

Interacts with host RELA (PubMed:15629770).

Interacts with host PABPC1 (via C-terminus) (PubMed:31649314).

12 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

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P04545, 2 interactors

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P04545

<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

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P04545

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

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SMRi
P04545

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Regioni32 – 49Oligomerization1 PublicationAdd BLAST18
Regioni76 – 171Globular core1 PublicationAdd BLAST96
Regioni126 – 163Binding to the phosphoprotein1 PublicationAdd BLAST38
Regioni172 – 194Disordered1 PublicationAdd BLAST23

<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

Contains a zinc-finger domain on its N-terminus essential for its anti-termination function (PubMed:24434552). Contains an oligomerization domain (PubMed:22675274). The central globular core is responsible for binding to RNA and phosphoprotein (PubMed:22675274).2 Publications

<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 pneumoviridae M2-1 protein family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1 – 28C3H1-typePROSITE-ProRule annotation2 PublicationsAdd BLAST28

Keywords - Domaini

Zinc-finger

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009452, Pneumovirus_M2-1
IPR000571, Znf_CCCH
IPR036855, Znf_CCCH_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06436, Pneumovirus_M2, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF003913, Matrix_glycop-M2_paramyxo, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00356, ZnF_C3H1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF90229, SSF90229, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50103, ZF_C3H1, 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.

P04545-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRRNPCKFE IRGHCLNGKR CHFSHNYFEW PPHALLVRQN FMLNRILKSM
60 70 80 90 100
DKSIDTLSEI SGAAELDRTE EYALGVVGVL ESYIGSINNI TKQSACVAMS
110 120 130 140 150
KLLTELNSDD IKKLRDNEEL NSPKIRVYNT VISYIESNRK NNKQTIHLLK
160 170 180 190
RLPADVLKKT IKNTLDIHKS ITINNPKEST VSDTNDHAKN NDTT
Length:194
Mass (Da):22,154
Last modified:August 13, 1987 - 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:iCA5B397FE2707EF9
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M11486 Genomic RNA Translation: AAB59860.1
U50362 Genomic RNA Translation: AAB86665.1
U50363 Genomic RNA Translation: AAB86677.1
U63644 Genomic RNA Translation: AAC55971.1
AF035006 Genomic RNA Translation: AAC14903.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B93010, WMNZ22

<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
M11486 Genomic RNA Translation: AAB59860.1
U50362 Genomic RNA Translation: AAB86665.1
U50363 Genomic RNA Translation: AAB86677.1
U63644 Genomic RNA Translation: AAC55971.1
AF035006 Genomic RNA Translation: AAC14903.1
PIRiB93010, WMNZ22

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
2L9JNMR-A58-177[»]
4C3BX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-194[»]
4C3DX-ray2.52A/B1-194[»]
4C3EX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-194[»]
5NOHX-ray1.80A/B73-175[»]
6G0YX-ray2.42A/C/E/F1-194[»]
6PZQX-ray2.70A/B/C/D1-194[»]
BMRBiP04545
SMRiP04545
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP04545, 2 interactors

Chemistry databases

BindingDBiP04545
ChEMBLiCHEMBL4105717

PTM databases

iPTMnetiP04545

Proteomic databases

PRIDEiP04545

Family and domain databases

InterProiView protein in InterPro
IPR009452, Pneumovirus_M2-1
IPR000571, Znf_CCCH
IPR036855, Znf_CCCH_sf
PfamiView protein in Pfam
PF06436, Pneumovirus_M2, 1 hit
PIRSFiPIRSF003913, Matrix_glycop-M2_paramyxo, 1 hit
SMARTiView protein in SMART
SM00356, ZnF_C3H1, 1 hit
SUPFAMiSSF90229, SSF90229, 1 hit
PROSITEiView protein in PROSITE
PS50103, ZF_C3H1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiM21_HRSVA
<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: P04545
Secondary accession number(s): Q77YA8
<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: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 7, 2021
This is version 100 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
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